HEADER    METAL BINDING PROTEIN                   20-AUG-22   7YVZ              
TITLE     STRUCTURE OF CAENORHABDITIS ELEGANS CISD-1/MITONEET                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CDGSH IRON-SULFUR DOMAIN-CONTAINING PROTEIN 1 (CISD-       
COMPND   3 1/MITONEET);                                                         
COMPND   4 CHAIN: A;                                                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CAENORHABDITIS ELEGANS, MITOCHONDRIAL OUTER MEMBRANE PROTEIN, CDGSH   
KEYWDS   2 IRON SULFUR CONTAINING PROTEIN, REGULATING MITOCHONDRIAL FUNCTION    
KEYWDS   3 AND MORPHOLOGY, METAL BINDING PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HASEGAWA,E.HAGIUDA,A.T.TAGUCHI,W.GELDENHUYS,T.IWASAKI,T.KUMASAKA    
REVDAT   3   08-MAY-24 7YVZ    1       JRNL                                     
REVDAT   2   03-APR-24 7YVZ    1       REMARK                                   
REVDAT   1   19-OCT-22 7YVZ    0                                                
JRNL        AUTH   J.R.BOOS,H.N.JANDRAIN,E.HAGIUDA,A.T.TAGUCHI,K.HASEGAWA,      
JRNL        AUTH 2 B.L.FEDUN,S.J.TAYLOR,S.M.ELAD,S.E.FABER,T.KUMASAKA,          
JRNL        AUTH 3 T.IWASAKI,W.J.GELDENHUYS                                     
JRNL        TITL   STRUCTURE AND BIOLOGICAL EVALUATION OF CAENORHABDITIS        
JRNL        TITL 2 ELEGANS CISD-1/MITONEET, A KLP-17 TAIL DOMAIN HOMOLOGUE,     
JRNL        TITL 3 SUPPORTS ATTENUATION OF PARAQUAT-INDUCED OXIDATIVE STRESS    
JRNL        TITL 4 THROUGH A P38 MAPK-MEDIATED ANTIOXIDANT DEFENSE RESPONSE.    
JRNL        REF    ADV REDOX RES                 V.   6       2022              
JRNL        REFN                   ISSN 2667-1379                               
JRNL        PMID   36533211                                                     
JRNL        DOI    10.1016/J.ARRES.2022.100048                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.1192.2_4158                                 
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 7076                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 708                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.3500 -  2.9000    0.99     1356   151  0.1618 0.1756        
REMARK   3     2  2.9000 -  2.3100    1.00     1282   142  0.1895 0.2075        
REMARK   3     3  2.3000 -  2.0100    1.00     1247   139  0.1593 0.1975        
REMARK   3     4  2.0100 -  1.8300    1.00     1247   139  0.1601 0.2085        
REMARK   3     5  1.8300 -  1.7000    1.00     1236   137  0.1727 0.2113        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.139            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.279           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.03                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.015            502                                  
REMARK   3   ANGLE     :  1.461            678                                  
REMARK   3   CHIRALITY :  0.085             72                                  
REMARK   3   PLANARITY :  0.012             87                                  
REMARK   3   DIHEDRAL  :  5.944             72                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 38 THROUGH 100)                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5915   8.2381   2.0055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2491 T22:   0.2434                                     
REMARK   3      T33:   0.2307 T12:   0.0040                                     
REMARK   3      T13:  -0.0115 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6211 L22:   1.6223                                     
REMARK   3      L33:   1.3954 L12:  -0.6778                                     
REMARK   3      L13:   0.4198 L23:  -0.2936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.1387 S13:   0.1564                       
REMARK   3      S21:   0.1085 S22:   0.0293 S23:   0.0561                       
REMARK   3      S31:  -0.1147 S32:  -0.2457 S33:   0.0001                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7YVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300031698.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7076                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.04914                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: RAT MITONEET                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 19.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM CHES-NAOH, PH 9.5, AND 30%(W/V)   
REMARK 280  PEG 3000 TO WHICH 5%(V/V) OF 1 M BICINE, PH8.5, WAS ADDED, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       41.13000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       18.89900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       18.89900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.56500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       18.89900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       18.89900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.69500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       18.89900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       18.89900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.56500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       18.89900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       18.89900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.69500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       41.13000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6350 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     LYS A    28                                                      
REMARK 465     PHE A    29                                                      
REMARK 465     TYR A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     PHE A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     LYS A   102                                                      
REMARK 465     LYS A   103                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  58    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  84    CG   CD   CE   NZ                                   
REMARK 470     LYS A  87    CG   CD   CE   NZ                                   
REMARK 470     GLU A  88    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  43      -42.74   -132.44                                   
REMARK 500    GLN A  45       61.52     39.09                                   
REMARK 500    LYS A  50      119.52   -167.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A 401  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  67   SG                                                     
REMARK 620 2 FES A 401   S1  116.1                                              
REMARK 620 3 FES A 401   S2  111.7 107.8                                        
REMARK 620 4 CYS A  69   SG   98.5 114.7 107.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A 401  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  78   SG                                                     
REMARK 620 2 FES A 401   S1  124.0                                              
REMARK 620 3 FES A 401   S2  108.9 105.4                                        
REMARK 620 4 HIS A  82   ND1  93.3 109.5 116.0                                  
REMARK 620 N                    1     2     3                                   
DBREF  7YVZ A   32   103  UNP    A7LPG5   A7LPG5_CAEEL    63    134             
SEQADV 7YVZ GLY A   19  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ SER A   20  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ HIS A   21  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ MET A   22  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ ALA A   23  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ SER A   24  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ SER A   25  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ GLY A   26  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ LYS A   27  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ LYS A   28  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ PHE A   29  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ TYR A   30  UNP  A7LPG5              EXPRESSION TAG                 
SEQADV 7YVZ ALA A   31  UNP  A7LPG5              EXPRESSION TAG                 
SEQRES   1 A   85  GLY SER HIS MET ALA SER SER GLY LYS LYS PHE TYR ALA          
SEQRES   2 A   85  LYS PHE GLY GLN ARG SER ALA ARG CYS ASN TYR LYS ILE          
SEQRES   3 A   85  GLN LEU ASP SER ASN LYS ILE VAL ASP THR VAL ASP ILE          
SEQRES   4 A   85  GLU ASP ILE GLY GLU LYS LYS ALA PHE CYS ARG CYS TRP          
SEQRES   5 A   85  LYS SER GLU LYS TRP PRO TYR CYS ASP GLY SER HIS GLY          
SEQRES   6 A   85  LYS HIS ASN LYS GLU THR GLY ASP ASN VAL GLY PRO LEU          
SEQRES   7 A   85  ILE VAL LYS SER GLU LYS LYS                                  
HET    FES  A 401       4                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
FORMUL   2  FES    FE2 S2                                                       
FORMUL   3  HOH   *19(H2 O)                                                     
HELIX    1 AA1 ASP A   56  ILE A   60  5                                   5    
HELIX    2 AA2 SER A   81  GLY A   90  1                                  10    
SHEET    1 AA1 2 LYS A  63  PHE A  66  0                                        
SHEET    2 AA1 2 LEU A  96  LYS A  99 -1  O  VAL A  98   N  LYS A  64           
SSBOND   1 CYS A   40    CYS A   40                          1555   7555  2.74  
LINK         SG  CYS A  67                FE1  FES A 401     1555   1555  2.33  
LINK         SG  CYS A  69                FE1  FES A 401     1555   1555  2.31  
LINK         SG  CYS A  78                FE2  FES A 401     1555   1555  2.45  
LINK         ND1 HIS A  82                FE2  FES A 401     1555   1555  2.13  
CISPEP   1 TRP A   75    PRO A   76          0         6.74                     
CRYST1   37.798   37.798   82.260  90.00  90.00  90.00 P 41 21 2     8          
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      0.026456  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.026456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012157        0.00000                         
ATOM      1  N   ALA A  38      19.935  13.535   3.087  1.00 61.37           N  
ATOM      2  CA  ALA A  38      18.644  13.955   2.547  1.00 51.34           C  
ATOM      3  C   ALA A  38      17.453  13.027   2.950  1.00 47.71           C  
ATOM      4  O   ALA A  38      17.078  12.108   2.226  1.00 53.15           O  
ATOM      5  CB  ALA A  38      18.744  14.064   1.031  1.00 63.35           C  
ATOM      6  N   ARG A  39      16.855  13.307   4.109  1.00 49.92           N  
ATOM      7  CA  ARG A  39      15.662  12.592   4.555  1.00 46.51           C  
ATOM      8  C   ARG A  39      14.477  12.904   3.635  1.00 41.79           C  
ATOM      9  O   ARG A  39      14.439  13.932   2.952  1.00 42.65           O  
ATOM     10  CB  ARG A  39      15.324  12.961   6.006  1.00 43.97           C  
ATOM     11  CG  ARG A  39      14.840  14.404   6.236  1.00 43.84           C  
ATOM     12  CD  ARG A  39      14.697  14.609   7.740  1.00 41.43           C  
ATOM     13  NE  ARG A  39      13.590  13.793   8.199  1.00 39.15           N  
ATOM     14  CZ  ARG A  39      13.578  13.172   9.360  1.00 37.48           C  
ATOM     15  NH1 ARG A  39      14.643  13.174  10.150  1.00 36.96           N  
ATOM     16  NH2 ARG A  39      12.523  12.434   9.685  1.00 33.92           N  
ATOM     17  N  ACYS A  40      13.497  11.990   3.635  0.50 32.14           N  
ATOM     18  N  BCYS A  40      13.502  11.997   3.616  0.50 32.15           N  
ATOM     19  CA ACYS A  40      12.291  12.047   2.806  0.50 35.15           C  
ATOM     20  CA BCYS A  40      12.288  12.210   2.834  0.50 35.13           C  
ATOM     21  C  ACYS A  40      11.069  12.573   3.555  0.50 36.25           C  
ATOM     22  C  BCYS A  40      11.188  12.838   3.684  0.50 36.37           C  
ATOM     23  O  ACYS A  40      10.231  13.262   2.958  0.50 31.14           O  
ATOM     24  O  BCYS A  40      10.578  13.845   3.305  0.50 32.09           O  
ATOM     25  CB ACYS A  40      11.958  10.650   2.245  0.50 37.40           C  
ATOM     26  CB BCYS A  40      11.803  10.878   2.239  0.50 37.30           C  
ATOM     27  SG ACYS A  40      12.585  10.236   0.566  0.50 49.82           S  
ATOM     28  SG BCYS A  40      10.268  10.955   1.280  0.50 48.62           S  
ATOM     29  N   ASN A  41      10.947  12.265   4.848  1.00 31.65           N  
ATOM     30  CA  ASN A  41       9.774  12.586   5.653  1.00 29.16           C  
ATOM     31  C   ASN A  41      10.037  13.793   6.530  1.00 31.37           C  
ATOM     32  O   ASN A  41      10.811  13.704   7.505  1.00 32.81           O  
ATOM     33  CB  ASN A  41       9.442  11.409   6.562  1.00 26.18           C  
ATOM     34  CG  ASN A  41       8.217  11.659   7.392  1.00 26.96           C  
ATOM     35  OD1 ASN A  41       7.357  12.515   7.037  1.00 26.47           O  
ATOM     36  ND2 ASN A  41       8.203  11.061   8.597  1.00 25.03           N  
ATOM     37  N   TYR A  42       9.336  14.899   6.254  1.00 28.46           N  
ATOM     38  CA  TYR A  42       9.406  16.072   7.121  1.00 26.57           C  
ATOM     39  C   TYR A  42       8.111  16.299   7.887  1.00 33.15           C  
ATOM     40  O   TYR A  42       7.952  17.346   8.501  1.00 34.97           O  
ATOM     41  CB  TYR A  42       9.749  17.317   6.289  1.00 29.81           C  
ATOM     42  CG  TYR A  42      11.195  17.364   5.856  1.00 33.52           C  
ATOM     43  CD1 TYR A  42      12.156  17.968   6.656  1.00 41.66           C  
ATOM     44  CD2 TYR A  42      11.614  16.757   4.681  1.00 36.62           C  
ATOM     45  CE1 TYR A  42      13.513  18.002   6.274  1.00 45.39           C  
ATOM     46  CE2 TYR A  42      12.948  16.798   4.285  1.00 42.37           C  
ATOM     47  CZ  TYR A  42      13.896  17.412   5.093  1.00 46.10           C  
ATOM     48  OH  TYR A  42      15.222  17.438   4.709  1.00 50.06           O  
ATOM     49  N   LYS A  43       7.177  15.371   7.838  1.00 27.10           N  
ATOM     50  CA  LYS A  43       5.852  15.669   8.377  1.00 29.22           C  
ATOM     51  C   LYS A  43       5.267  14.608   9.298  1.00 30.71           C  
ATOM     52  O   LYS A  43       4.661  14.958  10.323  1.00 30.25           O  
ATOM     53  CB  LYS A  43       4.880  15.843   7.185  1.00 28.34           C  
ATOM     54  CG  LYS A  43       3.464  16.208   7.590  1.00 32.28           C  
ATOM     55  CD  LYS A  43       2.641  16.368   6.344  1.00 33.48           C  
ATOM     56  CE  LYS A  43       1.263  16.783   6.702  1.00 39.50           C  
ATOM     57  NZ  LYS A  43       1.415  18.174   7.216  1.00 43.58           N  
ATOM     58  N   ILE A  44       5.396  13.329   8.951  1.00 24.90           N  
ATOM     59  CA  ILE A  44       4.613  12.269   9.586  1.00 27.79           C  
ATOM     60  C   ILE A  44       5.340  11.788  10.836  1.00 27.63           C  
ATOM     61  O   ILE A  44       6.502  11.360  10.761  1.00 26.84           O  
ATOM     62  CB  ILE A  44       4.394  11.094   8.619  1.00 24.69           C  
ATOM     63  CG1 ILE A  44       3.857  11.580   7.260  1.00 26.12           C  
ATOM     64  CG2 ILE A  44       3.440  10.150   9.243  1.00 26.15           C  
ATOM     65  CD1 ILE A  44       2.517  12.346   7.365  1.00 29.74           C  
ATOM     66  N   GLN A  45       4.674  11.889  11.998  1.00 27.44           N  
ATOM     67  CA  GLN A  45       5.120  11.276  13.278  1.00 30.06           C  
ATOM     68  C   GLN A  45       6.636  11.383  13.446  1.00 26.92           C  
ATOM     69  O   GLN A  45       7.354  10.381  13.471  1.00 28.45           O  
ATOM     70  CB  GLN A  45       4.728   9.808  13.366  1.00 29.63           C  
ATOM     71  CG  GLN A  45       3.244   9.623  12.987  1.00 30.85           C  
ATOM     72  CD  GLN A  45       2.805   8.160  12.935  1.00 40.93           C  
ATOM     73  OE1 GLN A  45       3.457   7.276  13.465  1.00 43.60           O  
ATOM     74  NE2 GLN A  45       1.818   7.905  12.077  1.00 37.05           N  
ATOM     75  N   LEU A  46       7.129  12.635  13.492  1.00 27.07           N  
ATOM     76  CA  LEU A  46       8.574  12.794  13.552  1.00 26.81           C  
ATOM     77  C   LEU A  46       9.172  12.299  14.857  1.00 31.75           C  
ATOM     78  O   LEU A  46      10.397  12.122  14.911  1.00 34.00           O  
ATOM     79  CB  LEU A  46       8.953  14.269  13.348  1.00 26.85           C  
ATOM     80  CG  LEU A  46       8.666  14.701  11.902  1.00 26.89           C  
ATOM     81  CD1 LEU A  46       8.935  16.154  11.711  1.00 28.26           C  
ATOM     82  CD2 LEU A  46       9.546  13.886  10.907  1.00 28.68           C  
ATOM     83  N   ASP A  47       8.347  12.060  15.898  1.00 36.03           N  
ATOM     84  CA  ASP A  47       8.806  11.403  17.125  1.00 38.69           C  
ATOM     85  C   ASP A  47       9.105   9.923  16.950  1.00 38.62           C  
ATOM     86  O   ASP A  47       9.878   9.344  17.738  1.00 39.95           O  
ATOM     87  CB  ASP A  47       7.786  11.553  18.264  1.00 38.05           C  
ATOM     88  CG  ASP A  47       6.355  11.158  17.882  1.00 42.03           C  
ATOM     89  OD1 ASP A  47       5.944  11.148  16.700  1.00 42.86           O  
ATOM     90  OD2 ASP A  47       5.630  10.749  18.819  1.00 52.48           O  
ATOM     91  N   SER A  48       8.481   9.281  15.985  1.00 32.32           N  
ATOM     92  CA  SER A  48       8.661   7.850  15.808  1.00 31.21           C  
ATOM     93  C   SER A  48      10.002   7.507  15.171  1.00 31.31           C  
ATOM     94  O   SER A  48      10.515   8.215  14.303  1.00 31.35           O  
ATOM     95  CB  SER A  48       7.533   7.298  14.952  1.00 33.08           C  
ATOM     96  OG  SER A  48       7.779   5.931  14.628  1.00 34.89           O  
ATOM     97  N   ASN A  49      10.553   6.372  15.590  1.00 33.19           N  
ATOM     98  CA  ASN A  49      11.815   5.896  15.040  1.00 34.91           C  
ATOM     99  C   ASN A  49      11.620   5.236  13.669  1.00 32.58           C  
ATOM    100  O   ASN A  49      12.552   5.169  12.854  1.00 32.70           O  
ATOM    101  CB  ASN A  49      12.407   4.950  16.085  1.00 43.00           C  
ATOM    102  CG  ASN A  49      13.905   4.880  16.025  1.00 56.21           C  
ATOM    103  OD1 ASN A  49      14.560   4.555  17.019  1.00 74.47           O  
ATOM    104  ND2 ASN A  49      14.463   5.131  14.859  1.00 60.41           N  
ATOM    105  N   LYS A  50      10.404   4.786  13.386  1.00 26.88           N  
ATOM    106  CA  LYS A  50      10.160   3.982  12.189  1.00 25.70           C  
ATOM    107  C   LYS A  50       8.671   3.866  11.956  1.00 26.83           C  
ATOM    108  O   LYS A  50       7.931   3.366  12.822  1.00 33.34           O  
ATOM    109  CB  LYS A  50      10.808   2.608  12.427  1.00 36.05           C  
ATOM    110  CG  LYS A  50      10.656   1.609  11.395  1.00 35.77           C  
ATOM    111  CD  LYS A  50      11.224   2.124  10.091  1.00 28.57           C  
ATOM    112  CE  LYS A  50      11.214   0.949   9.161  1.00 32.21           C  
ATOM    113  NZ  LYS A  50      12.266   0.096   9.823  1.00 34.23           N  
ATOM    114  N   ILE A  51       8.216   4.347  10.816  1.00 24.57           N  
ATOM    115  CA  ILE A  51       6.796   4.423  10.549  1.00 23.52           C  
ATOM    116  C   ILE A  51       6.428   3.271   9.620  1.00 25.12           C  
ATOM    117  O   ILE A  51       6.718   3.270   8.409  1.00 24.92           O  
ATOM    118  CB  ILE A  51       6.419   5.792   9.975  1.00 22.68           C  
ATOM    119  CG1 ILE A  51       6.791   6.846  11.027  1.00 29.36           C  
ATOM    120  CG2 ILE A  51       4.952   5.784   9.676  1.00 25.13           C  
ATOM    121  CD1 ILE A  51       6.653   8.264  10.499  1.00 30.86           C  
ATOM    122  N   VAL A  52       5.779   2.284  10.208  1.00 24.76           N  
ATOM    123  CA  VAL A  52       5.256   1.123   9.485  1.00 25.09           C  
ATOM    124  C   VAL A  52       3.755   1.116   9.728  1.00 25.80           C  
ATOM    125  O   VAL A  52       3.318   1.099  10.882  1.00 29.64           O  
ATOM    126  CB  VAL A  52       5.882  -0.186  10.008  1.00 28.37           C  
ATOM    127  CG1 VAL A  52       5.290  -1.368   9.296  1.00 26.34           C  
ATOM    128  CG2 VAL A  52       7.439  -0.177   9.875  1.00 31.20           C  
ATOM    129  N   ASP A  53       2.970   1.101   8.655  1.00 24.07           N  
ATOM    130  CA  ASP A  53       1.521   1.069   8.775  1.00 24.52           C  
ATOM    131  C   ASP A  53       1.025  -0.284   8.294  1.00 27.57           C  
ATOM    132  O   ASP A  53       1.561  -0.821   7.338  1.00 29.16           O  
ATOM    133  CB  ASP A  53       0.954   2.172   7.928  1.00 28.79           C  
ATOM    134  CG  ASP A  53       1.208   3.512   8.539  1.00 30.85           C  
ATOM    135  OD1 ASP A  53       0.767   3.715   9.701  1.00 32.06           O  
ATOM    136  OD2 ASP A  53       2.067   4.258   7.986  1.00 25.90           O  
ATOM    137  N   THR A  54      -0.023  -0.808   8.937  1.00 31.31           N  
ATOM    138  CA  THR A  54      -0.630  -2.087   8.549  1.00 33.22           C  
ATOM    139  C   THR A  54      -2.113  -1.896   8.248  1.00 33.38           C  
ATOM    140  O   THR A  54      -2.829  -1.228   9.006  1.00 38.18           O  
ATOM    141  CB  THR A  54      -0.433  -3.123   9.666  1.00 38.26           C  
ATOM    142  OG1 THR A  54       0.967  -3.247   9.950  1.00 33.79           O  
ATOM    143  CG2 THR A  54      -0.991  -4.486   9.270  1.00 38.52           C  
ATOM    144  N   VAL A  55      -2.581  -2.440   7.137  1.00 31.41           N  
ATOM    145  CA  VAL A  55      -4.010  -2.400   6.828  1.00 33.29           C  
ATOM    146  C   VAL A  55      -4.446  -3.794   6.429  1.00 38.55           C  
ATOM    147  O   VAL A  55      -3.674  -4.549   5.838  1.00 35.08           O  
ATOM    148  CB  VAL A  55      -4.336  -1.396   5.711  1.00 33.40           C  
ATOM    149  CG1 VAL A  55      -3.949  -0.020   6.159  1.00 42.41           C  
ATOM    150  CG2 VAL A  55      -3.536  -1.748   4.484  1.00 33.02           C  
ATOM    151  N   ASP A  56      -5.687  -4.135   6.755  1.00 35.25           N  
ATOM    152  CA  ASP A  56      -6.243  -5.414   6.382  1.00 38.80           C  
ATOM    153  C   ASP A  56      -7.070  -5.209   5.118  1.00 42.83           C  
ATOM    154  O   ASP A  56      -7.754  -4.189   4.966  1.00 40.28           O  
ATOM    155  CB  ASP A  56      -7.069  -5.980   7.541  1.00 43.32           C  
ATOM    156  CG  ASP A  56      -7.483  -7.445   7.337  1.00 59.67           C  
ATOM    157  OD1 ASP A  56      -7.365  -8.010   6.222  1.00 56.01           O  
ATOM    158  OD2 ASP A  56      -7.865  -8.076   8.350  1.00 72.43           O  
ATOM    159  N   ILE A  57      -6.961  -6.171   4.190  1.00 42.88           N  
ATOM    160  CA  ILE A  57      -7.684  -6.069   2.921  1.00 51.93           C  
ATOM    161  C   ILE A  57      -9.174  -5.868   3.181  1.00 53.08           C  
ATOM    162  O   ILE A  57      -9.863  -5.185   2.415  1.00 47.31           O  
ATOM    163  CB  ILE A  57      -7.433  -7.310   2.023  1.00 53.82           C  
ATOM    164  CG1 ILE A  57      -7.945  -8.584   2.709  1.00 57.59           C  
ATOM    165  CG2 ILE A  57      -5.945  -7.409   1.590  1.00 52.65           C  
ATOM    166  CD1 ILE A  57      -7.941  -9.828   1.824  1.00 62.91           C  
ATOM    167  N   GLU A  58      -9.677  -6.406   4.280  1.00 55.13           N  
ATOM    168  CA  GLU A  58     -11.090  -6.234   4.598  1.00 58.76           C  
ATOM    169  C   GLU A  58     -11.428  -4.802   5.031  1.00 56.96           C  
ATOM    170  O   GLU A  58     -12.542  -4.590   5.523  1.00 68.81           O  
ATOM    171  CB  GLU A  58     -11.502  -7.240   5.678  1.00 62.49           C  
ATOM    172  N   ASP A  59     -10.506  -3.850   4.882  1.00 55.94           N  
ATOM    173  CA  ASP A  59     -10.777  -2.432   5.097  1.00 59.09           C  
ATOM    174  C   ASP A  59     -10.546  -1.605   3.840  1.00 58.83           C  
ATOM    175  O   ASP A  59     -10.570  -0.372   3.906  1.00 60.48           O  
ATOM    176  CB  ASP A  59      -9.909  -1.897   6.228  1.00 59.34           C  
ATOM    177  CG  ASP A  59     -10.253  -2.537   7.549  1.00 67.87           C  
ATOM    178  OD1 ASP A  59     -11.430  -2.941   7.723  1.00 71.44           O  
ATOM    179  OD2 ASP A  59      -9.347  -2.667   8.397  1.00 71.06           O  
ATOM    180  N   ILE A  60     -10.314  -2.254   2.701  1.00 59.02           N  
ATOM    181  CA  ILE A  60     -10.053  -1.546   1.451  1.00 54.52           C  
ATOM    182  C   ILE A  60     -11.356  -1.109   0.794  1.00 50.49           C  
ATOM    183  O   ILE A  60     -11.432  -0.028   0.200  1.00 46.98           O  
ATOM    184  CB  ILE A  60      -9.211  -2.444   0.518  1.00 51.00           C  
ATOM    185  CG1 ILE A  60      -7.866  -2.763   1.155  1.00 51.73           C  
ATOM    186  CG2 ILE A  60      -9.029  -1.837  -0.869  1.00 46.61           C  
ATOM    187  CD1 ILE A  60      -7.005  -1.543   1.432  1.00 48.70           C  
ATOM    188  N   GLY A  61     -12.396  -1.936   0.863  1.00 50.61           N  
ATOM    189  CA  GLY A  61     -13.606  -1.610   0.103  1.00 45.74           C  
ATOM    190  C   GLY A  61     -13.360  -1.723  -1.399  1.00 49.46           C  
ATOM    191  O   GLY A  61     -12.616  -2.599  -1.860  1.00 53.49           O  
ATOM    192  N   GLU A  62     -13.985  -0.834  -2.182  1.00 45.73           N  
ATOM    193  CA  GLU A  62     -13.741  -0.847  -3.623  1.00 47.19           C  
ATOM    194  C   GLU A  62     -12.256  -0.641  -3.911  1.00 41.16           C  
ATOM    195  O   GLU A  62     -11.638  -1.416  -4.649  1.00 41.73           O  
ATOM    196  CB  GLU A  62     -14.573   0.233  -4.321  1.00 48.69           C  
ATOM    197  N   LYS A  63     -11.659   0.379  -3.293  1.00 38.90           N  
ATOM    198  CA  LYS A  63     -10.246   0.683  -3.459  1.00 32.02           C  
ATOM    199  C   LYS A  63      -9.856   1.742  -2.441  1.00 32.54           C  
ATOM    200  O   LYS A  63     -10.722   2.439  -1.894  1.00 35.50           O  
ATOM    201  CB  LYS A  63      -9.893   1.190  -4.869  1.00 38.65           C  
ATOM    202  CG  LYS A  63     -10.654   2.442  -5.283  1.00 44.06           C  
ATOM    203  CD  LYS A  63     -10.150   2.934  -6.619  1.00 38.62           C  
ATOM    204  CE  LYS A  63     -10.982   4.082  -7.165  1.00 41.96           C  
ATOM    205  NZ  LYS A  63     -12.260   3.570  -7.713  1.00 40.31           N  
ATOM    206  N   LYS A  64      -8.549   1.784  -2.127  1.00 30.38           N  
ATOM    207  CA  LYS A  64      -7.969   2.855  -1.322  1.00 28.70           C  
ATOM    208  C   LYS A  64      -6.637   3.269  -1.916  1.00 27.73           C  
ATOM    209  O   LYS A  64      -5.903   2.458  -2.490  1.00 29.80           O  
ATOM    210  CB  LYS A  64      -7.728   2.516   0.158  1.00 34.74           C  
ATOM    211  CG  LYS A  64      -8.975   2.479   0.985  1.00 41.45           C  
ATOM    212  CD  LYS A  64      -9.576   3.883   1.025  1.00 50.77           C  
ATOM    213  CE  LYS A  64     -10.890   3.908   1.784  1.00 61.73           C  
ATOM    214  NZ  LYS A  64     -11.526   5.242   1.624  1.00 61.66           N  
ATOM    215  N   ALA A  65      -6.323   4.548  -1.750  1.00 26.81           N  
ATOM    216  CA  ALA A  65      -5.044   5.088  -2.221  1.00 21.68           C  
ATOM    217  C   ALA A  65      -4.195   5.454  -1.022  1.00 23.58           C  
ATOM    218  O   ALA A  65      -4.652   6.181  -0.116  1.00 25.90           O  
ATOM    219  CB  ALA A  65      -5.269   6.332  -3.086  1.00 22.66           C  
ATOM    220  N   PHE A  66      -2.970   4.926  -1.006  1.00 21.21           N  
ATOM    221  CA  PHE A  66      -2.065   5.103   0.117  1.00 21.84           C  
ATOM    222  C   PHE A  66      -0.935   6.027  -0.286  1.00 24.24           C  
ATOM    223  O   PHE A  66      -0.329   5.879  -1.369  1.00 22.64           O  
ATOM    224  CB  PHE A  66      -1.507   3.748   0.546  1.00 22.69           C  
ATOM    225  CG  PHE A  66      -2.567   2.841   1.135  1.00 22.91           C  
ATOM    226  CD1 PHE A  66      -2.880   2.985   2.483  1.00 25.33           C  
ATOM    227  CD2 PHE A  66      -3.297   1.929   0.350  1.00 24.64           C  
ATOM    228  CE1 PHE A  66      -3.850   2.149   3.088  1.00 29.69           C  
ATOM    229  CE2 PHE A  66      -4.314   1.114   0.951  1.00 30.71           C  
ATOM    230  CZ  PHE A  66      -4.571   1.239   2.325  1.00 30.16           C  
ATOM    231  N   CYS A  67      -0.574   6.934   0.643  1.00 24.07           N  
ATOM    232  CA  CYS A  67       0.428   7.959   0.386  1.00 21.12           C  
ATOM    233  C   CYS A  67       1.838   7.348   0.392  1.00 19.82           C  
ATOM    234  O   CYS A  67       2.167   6.525   1.242  1.00 22.15           O  
ATOM    235  CB  CYS A  67       0.296   9.060   1.472  1.00 21.88           C  
ATOM    236  SG  CYS A  67       1.529  10.410   1.270  1.00 21.06           S  
ATOM    237  N   ARG A  68       2.613   7.685  -0.632  1.00 20.13           N  
ATOM    238  CA  ARG A  68       4.032   7.377  -0.663  1.00 19.44           C  
ATOM    239  C   ARG A  68       4.894   8.607  -0.748  1.00 23.09           C  
ATOM    240  O   ARG A  68       6.113   8.472  -0.978  1.00 23.41           O  
ATOM    241  CB  ARG A  68       4.328   6.458  -1.867  1.00 19.64           C  
ATOM    242  CG  ARG A  68       3.499   5.232  -1.763  1.00 17.76           C  
ATOM    243  CD  ARG A  68       3.801   4.101  -2.788  1.00 20.13           C  
ATOM    244  NE  ARG A  68       3.589   4.586  -4.146  1.00 20.34           N  
ATOM    245  CZ  ARG A  68       3.671   3.828  -5.234  1.00 20.70           C  
ATOM    246  NH1 ARG A  68       3.919   2.534  -5.139  1.00 20.64           N  
ATOM    247  NH2 ARG A  68       3.411   4.366  -6.436  1.00 23.79           N  
ATOM    248  N   CYS A  69       4.343   9.805  -0.525  1.00 20.24           N  
ATOM    249  CA  CYS A  69       5.124  11.042  -0.594  1.00 20.78           C  
ATOM    250  C   CYS A  69       5.371  11.688   0.758  1.00 23.60           C  
ATOM    251  O   CYS A  69       6.189  12.629   0.818  1.00 25.59           O  
ATOM    252  CB  CYS A  69       4.456  12.104  -1.497  1.00 19.89           C  
ATOM    253  SG  CYS A  69       2.931  12.867  -0.809  1.00 23.39           S  
ATOM    254  N   TRP A  70       4.718  11.189   1.834  1.00 19.41           N  
ATOM    255  CA  TRP A  70       4.979  11.646   3.211  1.00 21.79           C  
ATOM    256  C   TRP A  70       4.485  13.060   3.442  1.00 23.07           C  
ATOM    257  O   TRP A  70       4.906  13.738   4.413  1.00 23.57           O  
ATOM    258  CB  TRP A  70       6.497  11.499   3.610  1.00 23.39           C  
ATOM    259  CG  TRP A  70       6.831  10.007   3.538  1.00 24.06           C  
ATOM    260  CD1 TRP A  70       7.249   9.327   2.404  1.00 23.24           C  
ATOM    261  CD2 TRP A  70       6.697   9.036   4.578  1.00 20.99           C  
ATOM    262  NE1 TRP A  70       7.380   7.988   2.700  1.00 23.01           N  
ATOM    263  CE2 TRP A  70       7.097   7.776   4.032  1.00 20.61           C  
ATOM    264  CE3 TRP A  70       6.367   9.108   5.946  1.00 23.42           C  
ATOM    265  CZ2 TRP A  70       7.041   6.576   4.778  1.00 20.72           C  
ATOM    266  CZ3 TRP A  70       6.317   7.930   6.705  1.00 23.56           C  
ATOM    267  CH2 TRP A  70       6.676   6.667   6.137  1.00 22.50           C  
ATOM    268  N   LYS A  71       3.574  13.549   2.601  1.00 25.29           N  
ATOM    269  CA  LYS A  71       2.992  14.887   2.785  1.00 23.28           C  
ATOM    270  C   LYS A  71       1.489  14.869   3.079  1.00 28.94           C  
ATOM    271  O   LYS A  71       0.934  15.932   3.357  1.00 29.23           O  
ATOM    272  CB  LYS A  71       3.273  15.770   1.550  1.00 26.38           C  
ATOM    273  CG  LYS A  71       4.804  16.043   1.465  1.00 36.19           C  
ATOM    274  CD  LYS A  71       5.176  17.087   0.454  1.00 41.97           C  
ATOM    275  CE  LYS A  71       6.658  17.442   0.494  1.00 46.08           C  
ATOM    276  NZ  LYS A  71       6.844  18.586  -0.511  1.00 46.20           N  
ATOM    277  N   SER A  72       0.802  13.721   3.000  1.00 24.72           N  
ATOM    278  CA  SER A  72      -0.653  13.692   3.190  1.00 25.33           C  
ATOM    279  C   SER A  72      -1.074  14.133   4.584  1.00 30.14           C  
ATOM    280  O   SER A  72      -0.470  13.766   5.594  1.00 29.44           O  
ATOM    281  CB  SER A  72      -1.194  12.293   2.944  1.00 24.53           C  
ATOM    282  OG  SER A  72      -2.608  12.220   3.206  1.00 25.23           O  
ATOM    283  N   GLU A  73      -2.167  14.888   4.640  1.00 31.77           N  
ATOM    284  CA  GLU A  73      -2.759  15.204   5.924  1.00 31.40           C  
ATOM    285  C   GLU A  73      -3.682  14.108   6.422  1.00 33.70           C  
ATOM    286  O   GLU A  73      -4.204  14.227   7.541  1.00 37.98           O  
ATOM    287  CB  GLU A  73      -3.569  16.502   5.790  1.00 35.92           C  
ATOM    288  CG  GLU A  73      -2.789  17.725   5.327  1.00 39.14           C  
ATOM    289  CD  GLU A  73      -1.875  18.321   6.386  1.00 57.09           C  
ATOM    290  OE1 GLU A  73      -2.180  18.147   7.589  1.00 63.62           O  
ATOM    291  OE2 GLU A  73      -0.908  19.041   6.019  1.00 63.87           O  
ATOM    292  N   LYS A  74      -3.929  13.083   5.617  1.00 27.13           N  
ATOM    293  CA  LYS A  74      -4.751  11.939   5.982  1.00 32.79           C  
ATOM    294  C   LYS A  74      -3.925  10.661   6.050  1.00 29.32           C  
ATOM    295  O   LYS A  74      -4.425   9.573   5.794  1.00 29.25           O  
ATOM    296  CB  LYS A  74      -5.899  11.767   4.986  1.00 33.44           C  
ATOM    297  CG  LYS A  74      -6.779  13.016   4.824  1.00 39.29           C  
ATOM    298  CD  LYS A  74      -8.124  12.613   4.204  1.00 52.70           C  
ATOM    299  CE  LYS A  74      -8.176  12.565   2.671  1.00 57.34           C  
ATOM    300  NZ  LYS A  74      -7.566  11.311   2.042  1.00 44.89           N  
ATOM    301  N   TRP A  75      -2.648  10.779   6.397  1.00 29.86           N  
ATOM    302  CA  TRP A  75      -1.768   9.615   6.524  1.00 27.23           C  
ATOM    303  C   TRP A  75      -2.450   8.457   7.255  1.00 29.48           C  
ATOM    304  O   TRP A  75      -3.105   8.703   8.291  1.00 31.45           O  
ATOM    305  CB  TRP A  75      -0.541  10.046   7.329  1.00 26.78           C  
ATOM    306  CG  TRP A  75       0.482   8.929   7.348  1.00 23.85           C  
ATOM    307  CD1 TRP A  75       0.667   7.982   8.313  1.00 23.75           C  
ATOM    308  CD2 TRP A  75       1.420   8.663   6.313  1.00 25.32           C  
ATOM    309  NE1 TRP A  75       1.681   7.105   7.917  1.00 24.66           N  
ATOM    310  CE2 TRP A  75       2.152   7.529   6.701  1.00 24.38           C  
ATOM    311  CE3 TRP A  75       1.724   9.293   5.081  1.00 25.05           C  
ATOM    312  CZ2 TRP A  75       3.159   7.007   5.930  1.00 22.02           C  
ATOM    313  CZ3 TRP A  75       2.769   8.767   4.292  1.00 24.60           C  
ATOM    314  CH2 TRP A  75       3.463   7.603   4.740  1.00 23.36           C  
ATOM    315  N   PRO A  76      -2.351   7.191   6.782  1.00 26.89           N  
ATOM    316  CA  PRO A  76      -1.490   6.808   5.648  1.00 24.08           C  
ATOM    317  C   PRO A  76      -2.142   6.869   4.292  1.00 24.59           C  
ATOM    318  O   PRO A  76      -1.564   6.343   3.339  1.00 23.98           O  
ATOM    319  CB  PRO A  76      -1.144   5.344   5.949  1.00 23.77           C  
ATOM    320  CG  PRO A  76      -2.446   4.803   6.648  1.00 28.62           C  
ATOM    321  CD  PRO A  76      -2.923   6.009   7.469  1.00 30.42           C  
ATOM    322  N   TYR A  77      -3.318   7.495   4.196  1.00 27.12           N  
ATOM    323  CA  TYR A  77      -3.982   7.597   2.906  1.00 25.51           C  
ATOM    324  C   TYR A  77      -3.518   8.813   2.128  1.00 25.94           C  
ATOM    325  O   TYR A  77      -3.134   9.829   2.693  1.00 27.22           O  
ATOM    326  CB  TYR A  77      -5.496   7.677   3.140  1.00 24.73           C  
ATOM    327  CG  TYR A  77      -5.983   6.470   3.876  1.00 29.99           C  
ATOM    328  CD1 TYR A  77      -6.114   5.258   3.241  1.00 34.55           C  
ATOM    329  CD2 TYR A  77      -6.313   6.559   5.209  1.00 35.69           C  
ATOM    330  CE1 TYR A  77      -6.551   4.132   3.952  1.00 38.86           C  
ATOM    331  CE2 TYR A  77      -6.759   5.465   5.918  1.00 45.74           C  
ATOM    332  CZ  TYR A  77      -6.874   4.250   5.286  1.00 48.40           C  
ATOM    333  OH  TYR A  77      -7.323   3.157   6.016  1.00 58.28           O  
ATOM    334  N   CYS A  78      -3.572   8.699   0.798  1.00 24.27           N  
ATOM    335  CA  CYS A  78      -3.297   9.790  -0.108  1.00 24.90           C  
ATOM    336  C   CYS A  78      -4.408  10.828   0.037  1.00 27.89           C  
ATOM    337  O   CYS A  78      -5.595  10.463   0.195  1.00 27.65           O  
ATOM    338  CB  CYS A  78      -3.242   9.224  -1.541  1.00 27.52           C  
ATOM    339  SG  CYS A  78      -3.011  10.373  -2.895  1.00 26.56           S  
ATOM    340  N   ASP A  79      -4.020  12.126   0.045  1.00 24.20           N  
ATOM    341  CA  ASP A  79      -5.016  13.210  -0.009  1.00 28.57           C  
ATOM    342  C   ASP A  79      -4.739  14.175  -1.158  1.00 31.74           C  
ATOM    343  O   ASP A  79      -5.185  15.354  -1.113  1.00 31.39           O  
ATOM    344  CB  ASP A  79      -5.106  14.006   1.315  1.00 29.50           C  
ATOM    345  CG  ASP A  79      -3.867  14.838   1.599  1.00 30.55           C  
ATOM    346  OD1 ASP A  79      -2.902  14.768   0.840  1.00 27.41           O  
ATOM    347  OD2 ASP A  79      -3.866  15.622   2.600  1.00 28.80           O  
ATOM    348  N   GLY A  80      -3.971  13.728  -2.170  1.00 28.66           N  
ATOM    349  CA  GLY A  80      -3.593  14.556  -3.283  1.00 26.31           C  
ATOM    350  C   GLY A  80      -2.424  15.504  -3.066  1.00 27.90           C  
ATOM    351  O   GLY A  80      -2.085  16.257  -3.989  1.00 30.30           O  
ATOM    352  N   SER A  81      -1.828  15.546  -1.873  1.00 27.27           N  
ATOM    353  CA  SER A  81      -0.726  16.483  -1.617  1.00 26.80           C  
ATOM    354  C   SER A  81       0.495  16.193  -2.511  1.00 26.57           C  
ATOM    355  O   SER A  81       1.326  17.086  -2.719  1.00 27.37           O  
ATOM    356  CB  SER A  81      -0.315  16.380  -0.118  1.00 29.34           C  
ATOM    357  OG  SER A  81      -1.349  16.854   0.758  1.00 31.39           O  
ATOM    358  N   HIS A  82       0.563  14.990  -3.104  1.00 23.65           N  
ATOM    359  CA  HIS A  82       1.668  14.649  -3.991  1.00 25.42           C  
ATOM    360  C   HIS A  82       1.744  15.592  -5.183  1.00 29.52           C  
ATOM    361  O   HIS A  82       2.833  15.855  -5.702  1.00 29.29           O  
ATOM    362  CB  HIS A  82       1.544  13.184  -4.475  1.00 24.32           C  
ATOM    363  CG  HIS A  82       0.249  12.877  -5.166  1.00 26.80           C  
ATOM    364  ND1 HIS A  82      -0.815  12.294  -4.513  1.00 24.64           N  
ATOM    365  CD2 HIS A  82      -0.195  13.166  -6.420  1.00 31.90           C  
ATOM    366  CE1 HIS A  82      -1.831  12.162  -5.354  1.00 26.29           C  
ATOM    367  NE2 HIS A  82      -1.486  12.708  -6.508  1.00 31.07           N  
ATOM    368  N   GLY A  83       0.609  16.181  -5.586  1.00 30.87           N  
ATOM    369  CA  GLY A  83       0.619  16.942  -6.821  1.00 32.73           C  
ATOM    370  C   GLY A  83       1.413  18.227  -6.687  1.00 33.83           C  
ATOM    371  O   GLY A  83       2.286  18.521  -7.514  1.00 32.47           O  
ATOM    372  N   LYS A  84       1.147  18.987  -5.610  1.00 34.69           N  
ATOM    373  CA  LYS A  84       1.924  20.190  -5.308  1.00 33.03           C  
ATOM    374  C   LYS A  84       3.401  19.879  -5.105  1.00 38.99           C  
ATOM    375  O   LYS A  84       4.271  20.648  -5.550  1.00 40.68           O  
ATOM    376  CB  LYS A  84       1.353  20.875  -4.069  1.00 39.58           C  
ATOM    377  N   HIS A  85       3.709  18.797  -4.382  1.00 35.85           N  
ATOM    378  CA  HIS A  85       5.099  18.362  -4.226  1.00 30.91           C  
ATOM    379  C   HIS A  85       5.780  18.133  -5.573  1.00 35.81           C  
ATOM    380  O   HIS A  85       6.889  18.629  -5.826  1.00 34.51           O  
ATOM    381  CB  HIS A  85       5.135  17.094  -3.399  1.00 33.11           C  
ATOM    382  CG  HIS A  85       6.469  16.435  -3.411  1.00 33.93           C  
ATOM    383  ND1 HIS A  85       7.553  16.942  -2.737  1.00 35.88           N  
ATOM    384  CD2 HIS A  85       6.905  15.333  -4.065  1.00 31.25           C  
ATOM    385  CE1 HIS A  85       8.603  16.169  -2.964  1.00 37.65           C  
ATOM    386  NE2 HIS A  85       8.232  15.174  -3.751  1.00 32.92           N  
ATOM    387  N   ASN A  86       5.138  17.383  -6.461  1.00 31.27           N  
ATOM    388  CA  ASN A  86       5.789  17.093  -7.742  1.00 29.14           C  
ATOM    389  C   ASN A  86       5.959  18.363  -8.580  1.00 29.53           C  
ATOM    390  O   ASN A  86       6.987  18.539  -9.252  1.00 35.43           O  
ATOM    391  CB  ASN A  86       4.991  16.054  -8.520  1.00 31.18           C  
ATOM    392  CG  ASN A  86       5.035  14.696  -7.878  1.00 27.40           C  
ATOM    393  OD1 ASN A  86       6.001  14.365  -7.170  1.00 25.80           O  
ATOM    394  ND2 ASN A  86       4.064  13.851  -8.215  1.00 26.42           N  
ATOM    395  N   LYS A  87       4.949  19.250  -8.580  1.00 30.76           N  
ATOM    396  CA  LYS A  87       5.048  20.497  -9.335  1.00 35.39           C  
ATOM    397  C   LYS A  87       6.218  21.330  -8.842  1.00 41.36           C  
ATOM    398  O   LYS A  87       7.004  21.846  -9.646  1.00 41.74           O  
ATOM    399  CB  LYS A  87       3.735  21.283  -9.220  1.00 34.45           C  
ATOM    400  N   GLU A  88       6.370  21.451  -7.520  1.00 36.03           N  
ATOM    401  CA  GLU A  88       7.411  22.314  -6.961  1.00 41.43           C  
ATOM    402  C   GLU A  88       8.806  21.758  -7.241  1.00 41.10           C  
ATOM    403  O   GLU A  88       9.715  22.505  -7.617  1.00 46.53           O  
ATOM    404  CB  GLU A  88       7.199  22.481  -5.443  1.00 42.47           C  
ATOM    405  N   THR A  89       8.990  20.446  -7.091  1.00 38.69           N  
ATOM    406  CA  THR A  89      10.315  19.838  -7.048  1.00 39.09           C  
ATOM    407  C   THR A  89      10.721  19.151  -8.337  1.00 42.63           C  
ATOM    408  O   THR A  89      11.903  18.800  -8.491  1.00 41.34           O  
ATOM    409  CB  THR A  89      10.383  18.814  -5.936  1.00 40.70           C  
ATOM    410  OG1 THR A  89       9.420  17.790  -6.213  1.00 35.11           O  
ATOM    411  CG2 THR A  89      10.043  19.454  -4.568  1.00 39.80           C  
ATOM    412  N   GLY A  90       9.800  18.957  -9.268  1.00 36.67           N  
ATOM    413  CA  GLY A  90      10.104  18.113 -10.414  1.00 37.15           C  
ATOM    414  C   GLY A  90      10.017  16.635 -10.144  1.00 36.64           C  
ATOM    415  O   GLY A  90      10.387  15.833 -11.025  1.00 36.33           O  
ATOM    416  N   ASP A  91       9.580  16.240  -8.953  1.00 32.46           N  
ATOM    417  CA  ASP A  91       9.530  14.833  -8.559  1.00 29.86           C  
ATOM    418  C   ASP A  91       8.379  14.155  -9.333  1.00 28.08           C  
ATOM    419  O   ASP A  91       7.621  14.808 -10.056  1.00 29.87           O  
ATOM    420  CB  ASP A  91       9.317  14.769  -7.024  1.00 33.62           C  
ATOM    421  CG  ASP A  91       9.849  13.496  -6.362  1.00 33.16           C  
ATOM    422  OD1 ASP A  91      10.396  12.636  -7.091  1.00 30.66           O  
ATOM    423  OD2 ASP A  91       9.795  13.364  -5.084  1.00 32.80           O  
ATOM    424  N   ASN A  92       8.264  12.829  -9.178  1.00 28.31           N  
ATOM    425  CA  ASN A  92       7.247  12.064  -9.889  1.00 26.64           C  
ATOM    426  C   ASN A  92       6.577  11.045  -8.978  1.00 25.47           C  
ATOM    427  O   ASN A  92       6.110   9.999  -9.453  1.00 25.90           O  
ATOM    428  CB  ASN A  92       7.822  11.349 -11.126  1.00 28.43           C  
ATOM    429  CG  ASN A  92       8.973  10.415 -10.779  1.00 28.13           C  
ATOM    430  OD1 ASN A  92       9.365  10.275  -9.614  1.00 29.13           O  
ATOM    431  ND2 ASN A  92       9.430   9.673 -11.766  1.00 25.83           N  
ATOM    432  N   VAL A  93       6.474  11.344  -7.680  1.00 23.50           N  
ATOM    433  CA  VAL A  93       5.956  10.328  -6.777  1.00 20.07           C  
ATOM    434  C   VAL A  93       4.425  10.355  -6.786  1.00 22.20           C  
ATOM    435  O   VAL A  93       3.789  11.384  -7.018  1.00 24.49           O  
ATOM    436  CB  VAL A  93       6.509  10.486  -5.341  1.00 22.33           C  
ATOM    437  CG1 VAL A  93       8.015  10.160  -5.322  1.00 23.36           C  
ATOM    438  CG2 VAL A  93       6.283  11.891  -4.851  1.00 24.11           C  
ATOM    439  N   GLY A  94       3.852   9.235  -6.388  1.00 21.61           N  
ATOM    440  CA  GLY A  94       2.425   9.065  -6.398  1.00 23.48           C  
ATOM    441  C   GLY A  94       2.026   7.893  -5.534  1.00 21.01           C  
ATOM    442  O   GLY A  94       2.849   7.154  -5.002  1.00 21.63           O  
ATOM    443  N   PRO A  95       0.729   7.724  -5.357  1.00 19.73           N  
ATOM    444  CA  PRO A  95       0.216   6.748  -4.375  1.00 20.53           C  
ATOM    445  C   PRO A  95       0.202   5.300  -4.893  1.00 21.81           C  
ATOM    446  O   PRO A  95       0.316   5.024  -6.089  1.00 23.63           O  
ATOM    447  CB  PRO A  95      -1.237   7.229  -4.157  1.00 19.42           C  
ATOM    448  CG  PRO A  95      -1.594   7.931  -5.403  1.00 23.84           C  
ATOM    449  CD  PRO A  95      -0.322   8.612  -5.883  1.00 24.55           C  
ATOM    450  N   LEU A  96       0.048   4.373  -3.942  1.00 20.39           N  
ATOM    451  CA  LEU A  96      -0.276   2.975  -4.224  1.00 21.30           C  
ATOM    452  C   LEU A  96      -1.773   2.807  -4.159  1.00 24.67           C  
ATOM    453  O   LEU A  96      -2.360   3.131  -3.123  1.00 24.60           O  
ATOM    454  CB  LEU A  96       0.326   2.082  -3.136  1.00 20.99           C  
ATOM    455  CG  LEU A  96      -0.041   0.603  -3.218  1.00 22.47           C  
ATOM    456  CD1 LEU A  96       0.593  -0.044  -4.496  1.00 27.73           C  
ATOM    457  CD2 LEU A  96       0.393  -0.088  -1.962  1.00 24.69           C  
ATOM    458  N   ILE A  97      -2.398   2.272  -5.230  1.00 23.29           N  
ATOM    459  CA  ILE A  97      -3.847   2.043  -5.232  1.00 26.53           C  
ATOM    460  C   ILE A  97      -4.047   0.567  -4.925  1.00 30.36           C  
ATOM    461  O   ILE A  97      -3.489  -0.278  -5.626  1.00 30.43           O  
ATOM    462  CB  ILE A  97      -4.474   2.358  -6.603  1.00 28.65           C  
ATOM    463  CG1 ILE A  97      -4.109   3.734  -7.118  1.00 34.27           C  
ATOM    464  CG2 ILE A  97      -5.980   2.085  -6.563  1.00 31.04           C  
ATOM    465  CD1 ILE A  97      -4.419   4.844  -6.152  1.00 34.20           C  
ATOM    466  N   VAL A  98      -4.806   0.232  -3.886  1.00 23.36           N  
ATOM    467  CA  VAL A  98      -5.088  -1.173  -3.593  1.00 26.93           C  
ATOM    468  C   VAL A  98      -6.563  -1.358  -3.942  1.00 32.85           C  
ATOM    469  O   VAL A  98      -7.417  -0.645  -3.399  1.00 33.26           O  
ATOM    470  CB  VAL A  98      -4.765  -1.530  -2.130  1.00 25.76           C  
ATOM    471  CG1 VAL A  98      -5.174  -3.009  -1.859  1.00 32.85           C  
ATOM    472  CG2 VAL A  98      -3.237  -1.280  -1.784  1.00 28.64           C  
ATOM    473  N   LYS A  99      -6.877  -2.278  -4.869  1.00 31.49           N  
ATOM    474  CA  LYS A  99      -8.243  -2.419  -5.361  1.00 37.53           C  
ATOM    475  C   LYS A  99      -8.801  -3.812  -5.077  1.00 42.17           C  
ATOM    476  O   LYS A  99      -8.073  -4.733  -4.701  1.00 40.92           O  
ATOM    477  CB  LYS A  99      -8.322  -2.117  -6.862  1.00 40.49           C  
ATOM    478  CG  LYS A  99      -7.635  -3.100  -7.753  1.00 42.95           C  
ATOM    479  CD  LYS A  99      -7.767  -2.676  -9.205  1.00 41.09           C  
ATOM    480  CE  LYS A  99      -7.094  -3.654 -10.147  1.00 50.66           C  
ATOM    481  NZ  LYS A  99      -7.810  -4.960 -10.171  1.00 48.67           N  
ATOM    482  N   SER A 100     -10.120  -3.959  -5.276  1.00 50.90           N  
ATOM    483  CA  SER A 100     -10.830  -5.252  -5.101  1.00 52.88           C  
ATOM    484  C   SER A 100     -11.629  -5.671  -6.342  1.00 56.20           C  
ATOM    485  O   SER A 100     -11.524  -5.054  -7.398  1.00 55.59           O  
ATOM    486  CB  SER A 100     -11.795  -5.208  -3.906  1.00 54.81           C  
ATOM    487  OG  SER A 100     -11.107  -5.079  -2.673  1.00 64.50           O  
TER     488      SER A 100                                                      
HETATM  489 FE1  FES A 401       1.156  11.395  -0.804  1.00 22.37          FE  
HETATM  490 FE2  FES A 401      -0.753  11.280  -2.639  1.00 24.16          FE  
HETATM  491  S1  FES A 401       1.092  10.026  -2.531  1.00 21.39           S  
HETATM  492  S2  FES A 401      -0.695  12.581  -0.820  1.00 22.35           S  
HETATM  493  O   HOH A 501      12.289  10.397  14.477  1.00 32.46           O  
HETATM  494  O   HOH A 502       3.342  11.583  16.457  1.00 44.30           O  
HETATM  495  O   HOH A 503       2.053  17.832 -10.075  1.00 38.50           O  
HETATM  496  O   HOH A 504      -1.429  18.863  -4.208  1.00 34.86           O  
HETATM  497  O   HOH A 505       7.207  15.165   4.341  1.00 28.62           O  
HETATM  498  O   HOH A 506      -0.939  13.302   8.244  1.00 34.91           O  
HETATM  499  O   HOH A 507      -6.342  16.396   3.501  1.00 42.47           O  
HETATM  500  O   HOH A 508       0.877   4.858   3.012  1.00 22.45           O  
HETATM  501  O   HOH A 509       8.561   2.380  15.344  1.00 38.37           O  
HETATM  502  O   HOH A 510       2.138  -1.275  11.818  1.00 39.90           O  
HETATM  503  O   HOH A 511       2.417  19.095  -1.055  1.00 36.30           O  
HETATM  504  O   HOH A 512      10.703  13.164 -11.902  1.00 34.59           O  
HETATM  505  O   HOH A 513       5.301  14.848  13.085  1.00 32.31           O  
HETATM  506  O   HOH A 514       8.044  14.595   1.682  1.00 36.51           O  
HETATM  507  O   HOH A 515      -0.683   0.242  11.497  1.00 37.40           O  
HETATM  508  O   HOH A 516       1.933  12.789  12.147  1.00 37.59           O  
HETATM  509  O   HOH A 517      14.811   1.589   9.894  1.00 42.90           O  
HETATM  510  O   HOH A 518       4.967   2.807  13.203  1.00 37.64           O  
HETATM  511  O   HOH A 519       9.244   4.756  17.810  1.00 42.97           O  
CONECT  236  489                                                                
CONECT  253  489                                                                
CONECT  339  490                                                                
CONECT  364  490                                                                
CONECT  489  236  253  491  492                                                 
CONECT  490  339  364  491  492                                                 
CONECT  491  489  490                                                           
CONECT  492  489  490                                                           
MASTER      313    0    1    2    2    0    0    6  504    1    8    7          
END                                                                             
