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Database: PDB
Entry: 1E6V
LinkDB: 1E6V
Original site: 1E6V 
HEADER    OXIDOREDUCTASE                          23-AUG-00   1E6V              
TITLE     METHYL-COENZYME M REDUCTASE FROM METHANOPYRUS KANDLERI                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYL-COENZYME M REDUCTASE I ALPHA SUBUNIT;               
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: METHYL-COENZYME M REDUCTASE I BETA SUBUNIT;                
COMPND   6 CHAIN: B, E;                                                         
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: METHYL-COENZYME M REDUCTASE I GAMMA SUBUNIT;               
COMPND   9 CHAIN: C, F                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOPYRUS KANDLERI;                          
SOURCE   3 ORGANISM_TAXID: 2320;                                                
SOURCE   4 CELLULAR_LOCATION: CYTOPLASMA;                                       
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: METHANOPYRUS KANDLERI;                          
SOURCE   7 ORGANISM_TAXID: 2320;                                                
SOURCE   8 CELLULAR_LOCATION: CYTOPLASMA;                                       
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: METHANOPYRUS KANDLERI;                          
SOURCE  11 ORGANISM_TAXID: 2320;                                                
SOURCE  12 CELLULAR_LOCATION: CYTOPLASMA                                        
KEYWDS    BIOLOGICAL METHANOGENESIS, NI-ENZYME, OXIDOREDUCTASE, NI ENZYME       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.GRABARSE,U.ERMLER                                                   
REVDAT   7   29-MAR-17 1E6V    1       FORMUL                                   
REVDAT   6   20-MAY-15 1E6V    1       KEYWDS JRNL   REMARK VERSN               
REVDAT   6 2                   1       HETNAM HETSYN FORMUL HELIX               
REVDAT   6 3                   1       SHEET  LINK   MASTER                     
REVDAT   5   16-JUN-09 1E6V    1       REMARK                                   
REVDAT   4   02-JUN-09 1E6V    1       REVDAT REMARK                            
REVDAT   3   24-FEB-09 1E6V    1       VERSN                                    
REVDAT   2   04-DEC-00 1E6V    1       DBREF  SEQRES ATOM   REMARK              
REVDAT   1   18-OCT-00 1E6V    0                                                
JRNL        AUTH   W.GRABARSE,F.MAHLERT,S.SHIMA,R.K.THAUER,U.ERMLER             
JRNL        TITL   COMPARISON OF THREE METHYL-COENZYME M REDUCTASES FROM        
JRNL        TITL 2 PHYLOGENETICALLY DISTANT ORGANISMS: UNUSUAL AMINO ACID       
JRNL        TITL 3 MODIFICATION, CONSERVATION AND ADAPTATION                    
JRNL        REF    J.MOL.BIOL.                   V. 303   329 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11023796                                                     
JRNL        DOI    10.1006/JMBI.2000.4136                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 274750.550                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 62.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43932                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2196                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 61.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6655                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 350                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19222                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.30000                                             
REMARK   3    B22 (A**2) : -2.84000                                             
REMARK   3    B33 (A**2) : 12.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.46                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.550                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED, REFINEMENT WAS   
REMARK   3  CARRIED WITH NCS RESTRAINTS AND THE PDB GENERATED THE ATOMS FOR     
REMARK   3  CHAINS D, E, F. MCR FROM M. KANDLERI MIGHT CONTAIN MODIFIED         
REMARK   3  AMINO ACIDS ANALOGOUS TO MCR FROM M. THERMOAUTOTROPHICUM AND M.     
REMARK   3  BARKERI. THE DATA SET IS OF UNUSUALLY LOW COMPLETENESS              
REMARK   3  CORRESPONDING TO ABOUT 3.2 A EFFECTIVE RESOLUTION.                  
REMARK   4                                                                      
REMARK   4 1E6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5309.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.84                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 326507                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 0.3                                               
REMARK 200 STARTING MODEL: 1MRO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.00                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.25950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      134.25500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.87000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      134.25500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.25950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.87000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 53570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -280.9 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE HEXAMER OF TWO ALPHA, TWO BETA, AND TWO GAMMA CHAINS             
REMARK 400  CATALYZES THE FINAL STEP IN METHANOGENESIS, WHICH IS THE            
REMARK 400  TERMINAL STEP OF ANAEROBIC DEGRADATION OF BIOMASS                   
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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     GLU A   553                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ARG B   443                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     ALA C   255                                                      
REMARK 465     GLU C   256                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     LYS C   258                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     GLU D   553                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     GLU E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     LYS E     6                                                      
REMARK 465     ARG E   443                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     GLN F     6                                                      
REMARK 465     ALA F   255                                                      
REMARK 465     GLU F   256                                                      
REMARK 465     GLY F   257                                                      
REMARK 465     LYS F   258                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   14   CE   NZ                                             
REMARK 480     GLU A   15   CD                                                  
REMARK 480     GLU A   18   CG   CD   OE1  OE2                                  
REMARK 480     LYS A   24   CD   CE   NZ                                        
REMARK 480     ARG A  121   CG   CD                                             
REMARK 480     LYS A  189   CD   CE   NZ                                        
REMARK 480     GLU A  355   CD   OE1  OE2                                       
REMARK 480     ARG B   15   NE   CZ   NH1  NH2                                  
REMARK 480     ASP B   99   CB   CG   OD1  OD2                                  
REMARK 480     LYS B  262   CD   CE   NZ                                        
REMARK 480     GLU B  279   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  284   CD                                                  
REMARK 480     GLU B  439   CD   OE1  OE2                                       
REMARK 480     ASP C   14   CG                                                  
REMARK 480     GLU C   61   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS C  136   CE   NZ                                             
REMARK 480     GLU C  168   CD   OE1  OE2                                       
REMARK 480     GLU C  184   CB   CG                                             
REMARK 480     GLU C  198   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  201   C    CD   OE1  OE2                                  
REMARK 480     GLU C  211   CB   CG   CD   OE1  OE2                             
REMARK 480     ASP C  212   CB   CG                                             
REMARK 480     GLU C  216   CG   CD   OE1  OE2                                  
REMARK 480     LYS D   14   CE   NZ                                             
REMARK 480     GLU D   15   CD                                                  
REMARK 480     GLU D   18   CG   CD   OE1  OE2                                  
REMARK 480     LYS D   24   CD   CE   NZ                                        
REMARK 480     ARG D  121   CG   CD                                             
REMARK 480     LYS D  189   CD   CE   NZ                                        
REMARK 480     GLU D  355   CD   OE1  OE2                                       
REMARK 480     ARG E   15   NE   CZ   NH1  NH2                                  
REMARK 480     ASP E   99   CB   CG   OD1  OD2                                  
REMARK 480     LYS E  262   CD   CE   NZ                                        
REMARK 480     GLU E  279   CG   CD   OE1  OE2                                  
REMARK 480     GLU E  284   CD                                                  
REMARK 480     GLU E  439   CD   OE1  OE2                                       
REMARK 480     ASP F   14   CG                                                  
REMARK 480     GLU F   61   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS F  136   CE   NZ                                             
REMARK 480     GLU F  168   CD   OE1  OE2                                       
REMARK 480     GLU F  184   CB   CG                                             
REMARK 480     GLU F  198   CG   CD   OE1  OE2                                  
REMARK 480     GLU F  201   C    CD   OE1  OE2                                  
REMARK 480     GLU F  211   CB   CG   CD   OE1  OE2                             
REMARK 480     ASP F  212   CB   CG                                             
REMARK 480     GLU F  216   CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   181     OE1  GLU D   174     1455     1.74            
REMARK 500   CE   LYS E    92     NZ   LYS E   262     3655     1.83            
REMARK 500   CE   LYS E    92     CE   LYS E   262     3655     2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 228   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG B 121   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG C  20   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG D 228   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG E 121   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG F  20   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  31       -7.89   -143.60                                   
REMARK 500    ARG A  54      -71.42    -94.18                                   
REMARK 500    HIS A  58     -134.26   -126.73                                   
REMARK 500    TRP A 162        0.18    -58.69                                   
REMARK 500    ASP A 177       52.15    -99.08                                   
REMARK 500    ASN A 205       44.02    -80.46                                   
REMARK 500    CYS A 221     -128.20   -112.98                                   
REMARK 500    HIS A 260      -56.23   -142.03                                   
REMARK 500    ARG A 274       50.95   -111.01                                   
REMARK 500    SER A 325      -66.56   -144.06                                   
REMARK 500    SER A 328      -84.58   -147.18                                   
REMARK 500    TYR A 341      -19.98   -141.87                                   
REMARK 500    ASN A 344       27.98     49.35                                   
REMARK 500    LEU A 444      -67.84   -136.59                                   
REMARK 500    PHE A 446     -177.19    -68.37                                   
REMARK 500    SER A 465      -91.09    -14.86                                   
REMARK 500    ASP A 466       42.12   -100.51                                   
REMARK 500    LEU A 469      130.38    174.66                                   
REMARK 500    HIS A 487      -53.74   -142.13                                   
REMARK 500    VAL A 508      -25.52   -156.77                                   
REMARK 500    GLU B  21     -124.93    -77.47                                   
REMARK 500    MET B  75      108.20   -164.44                                   
REMARK 500    ASP B  99       41.26   -107.36                                   
REMARK 500    VAL B 122      -80.76    -60.03                                   
REMARK 500    LYS B 123      -48.65      5.15                                   
REMARK 500    SER B 130      -34.97    -37.32                                   
REMARK 500    ASP B 170     -168.16   -118.29                                   
REMARK 500    TYR B 171       58.02    -90.35                                   
REMARK 500    VAL B 182      131.24     39.48                                   
REMARK 500    ASP B 250       12.25     55.18                                   
REMARK 500    THR B 265     -169.69   -127.09                                   
REMARK 500    PRO B 290       63.32    -58.75                                   
REMARK 500    SER B 291      -23.90    134.12                                   
REMARK 500    GLN B 326      -83.85     30.22                                   
REMARK 500    HIS B 365       26.46   -147.94                                   
REMARK 500    GLU B 428       59.37   -141.23                                   
REMARK 500    TYR C   8      -61.65     80.55                                   
REMARK 500    GLU C  62       35.73   -143.09                                   
REMARK 500    GLU C  67       93.27    -62.06                                   
REMARK 500    ALA C 207       75.90     61.14                                   
REMARK 500    GLU C 253      138.15    166.83                                   
REMARK 500    PHE D  31       -7.82   -143.65                                   
REMARK 500    ARG D  54      -71.37    -94.22                                   
REMARK 500    HIS D  58     -134.21   -126.72                                   
REMARK 500    TRP D 162        0.15    -58.69                                   
REMARK 500    ASP D 177       52.18    -99.11                                   
REMARK 500    ASN D 205       43.97    -80.45                                   
REMARK 500    CYS D 221     -128.20   -112.92                                   
REMARK 500    HIS D 260      -56.22   -142.06                                   
REMARK 500    ARG D 274       50.97   -111.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  54         0.12    SIDE CHAIN                              
REMARK 500    ARG A 212         0.08    SIDE CHAIN                              
REMARK 500    ARG A 228         0.17    SIDE CHAIN                              
REMARK 500    ARG A 274         0.07    SIDE CHAIN                              
REMARK 500    TYR A 447         0.07    SIDE CHAIN                              
REMARK 500    ARG B 121         0.20    SIDE CHAIN                              
REMARK 500    TYR B 129         0.13    SIDE CHAIN                              
REMARK 500    TYR B 334         0.08    SIDE CHAIN                              
REMARK 500    ARG C  19         0.10    SIDE CHAIN                              
REMARK 500    ARG C  20         0.13    SIDE CHAIN                              
REMARK 500    ARG D  54         0.12    SIDE CHAIN                              
REMARK 500    ARG D 212         0.08    SIDE CHAIN                              
REMARK 500    ARG D 228         0.17    SIDE CHAIN                              
REMARK 500    ARG D 274         0.07    SIDE CHAIN                              
REMARK 500    TYR D 447         0.07    SIDE CHAIN                              
REMARK 500    ARG E 121         0.20    SIDE CHAIN                              
REMARK 500    TYR E 129         0.13    SIDE CHAIN                              
REMARK 500    TYR E 334         0.08    SIDE CHAIN                              
REMARK 500    ARG F  19         0.10    SIDE CHAIN                              
REMARK 500    ARG F  20         0.13    SIDE CHAIN                              
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                             F43 A1553  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 150   OE1                                                    
REMARK 620 2 F43 A1553   NA   80.8                                              
REMARK 620 3 F43 A1553   NB   81.0  86.3                                        
REMARK 620 4 F43 A1553   NC   92.7 173.4  93.9                                  
REMARK 620 5 F43 A1553   ND   87.9  94.3 168.7  84.2                            
REMARK 620 6 COM A1555   S1  164.8  85.3  92.2 101.3  99.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F43 D1553  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D 150   OE1                                                    
REMARK 620 2 F43 D1553   NA   80.8                                              
REMARK 620 3 F43 D1553   NB   81.0  86.3                                        
REMARK 620 4 F43 D1553   NC   92.7 173.4  93.9                                  
REMARK 620 5 F43 D1553   ND   87.9  94.3 168.7  84.2                            
REMARK 620 6 COM D1555   S1  164.8  85.3  92.2 101.3  99.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F43 A 1553                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP7 A 1554                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM A 1555                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F43 D 1553                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP7 D 1554                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM D 1555                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E6Y   RELATED DB: PDB                                   
REMARK 900 METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI              
REMARK 900 RELATED ID: 1MRO   RELATED DB: PDB                                   
REMARK 900 METHYL-COENZYME M REDUCTASE                                          
DBREF  1E6V A    1   553  UNP    Q49605   MCRA_METKA       1    553             
DBREF  1E6V B    1   443  UNP    Q49601   Q49601           1    443             
DBREF  1E6V C    1   258  UNP    Q49604   Q49604           1    258             
DBREF  1E6V D    1   553  UNP    Q49605   MCRA_METKA       1    553             
DBREF  1E6V E    1   443  UNP    Q49601   Q49601           1    443             
DBREF  1E6V F    1   258  UNP    Q49604   Q49604           1    258             
SEQADV 1E6V VAL B   49  UNP  Q49601    ILE    49 CLONING ARTIFACT               
SEQADV 1E6V GLN B   98  UNP  Q49601    GLU    98 CLONING ARTIFACT               
SEQADV 1E6V GLN B  220  UNP  Q49601    GLU   220 CLONING ARTIFACT               
SEQADV 1E6V VAL E   49  UNP  Q49601    ILE    49 CLONING ARTIFACT               
SEQADV 1E6V GLN E   98  UNP  Q49601    GLU    98 CLONING ARTIFACT               
SEQADV 1E6V GLN E  220  UNP  Q49601    GLU   220 CLONING ARTIFACT               
SEQRES   1 A  553  MET SER SER ALA GLU GLU LYS LEU PHE MET LYS ALA LEU          
SEQRES   2 A  553  LYS GLU LYS PHE GLU GLU SER PRO GLU GLU LYS TYR THR          
SEQRES   3 A  553  LYS PHE TYR ILE PHE GLY GLY TRP LYS GLN SER GLU ARG          
SEQRES   4 A  553  LYS LYS GLU PHE LYS GLU TRP ALA ASP LYS ILE VAL GLU          
SEQRES   5 A  553  GLU ARG GLY VAL PRO HIS TYR ASN PRO ASP ILE GLY VAL          
SEQRES   6 A  553  PRO LEU GLY GLN ARG LYS LEU MET SER TYR GLN VAL SER          
SEQRES   7 A  553  GLY THR ASP VAL PHE VAL GLU GLY ASP ASP LEU THR PHE          
SEQRES   8 A  553  VAL ASN ASN ALA ALA MET GLN GLN MET TRP ASP ASP ILE          
SEQRES   9 A  553  ARG ARG THR VAL ILE VAL GLY MET ASP THR ALA HIS ARG          
SEQRES  10 A  553  VAL LEU GLU ARG ARG LEU GLY LYS GLU VAL THR PRO GLU          
SEQRES  11 A  553  THR ILE ASN GLU TYR MET GLU THR LEU ASN HIS ALA LEU          
SEQRES  12 A  553  PRO GLY GLY ALA VAL VAL GLN GLU HIS MET VAL GLU ILE          
SEQRES  13 A  553  HIS PRO GLY LEU THR TRP ASP CYS TYR ALA LYS ILE ILE          
SEQRES  14 A  553  THR GLY ASP LEU GLU LEU ALA ASP GLU ILE ASP ASP LYS          
SEQRES  15 A  553  PHE LEU ILE ASP ILE GLU LYS LEU PHE PRO GLU GLU GLN          
SEQRES  16 A  553  ALA GLU GLN LEU ILE LYS ALA ILE GLY ASN ARG THR TYR          
SEQRES  17 A  553  GLN VAL CYS ARG MET PRO THR ILE VAL GLY HIS VAL CYS          
SEQRES  18 A  553  ASP GLY ALA THR MET TYR ARG TRP ALA ALA MET GLN ILE          
SEQRES  19 A  553  ALA MET SER PHE ILE CYS ALA TYR LYS ILE ALA ALA GLY          
SEQRES  20 A  553  GLU ALA ALA VAL SER ASP PHE ALA PHE ALA SER LYS HIS          
SEQRES  21 A  553  ALA GLU VAL ILE ASN MET GLY GLU MET LEU PRO ALA ARG          
SEQRES  22 A  553  ARG ALA ARG GLY GLU ASN GLU PRO GLY GLY VAL PRO PHE          
SEQRES  23 A  553  GLY VAL LEU ALA ASP CYS VAL GLN THR MET ARG LYS TYR          
SEQRES  24 A  553  PRO ASP ASP PRO ALA LYS VAL ALA LEU GLU VAL ILE ALA          
SEQRES  25 A  553  ALA GLY ALA MET LEU TYR ASP GLN ILE TRP LEU GLY SER          
SEQRES  26 A  553  TYR MET SER GLY GLY VAL GLY PHE THR GLN TYR ALA THR          
SEQRES  27 A  553  ALA VAL TYR PRO ASP ASN ILE LEU ASP ASP TYR VAL TYR          
SEQRES  28 A  553  TYR GLY LEU GLU TYR VAL GLU ASP LYS TYR GLY ILE ALA          
SEQRES  29 A  553  GLU ALA GLU PRO SER MET ASP VAL VAL LYS ASP VAL ALA          
SEQRES  30 A  553  THR GLU VAL THR LEU TYR GLY LEU GLU GLN TYR GLU ARG          
SEQRES  31 A  553  TYR PRO ALA ALA MET GLU THR HIS PHE GLY GLY SER GLN          
SEQRES  32 A  553  ARG ALA ALA VAL CYS ALA ALA ALA ALA GLY CYS SER THR          
SEQRES  33 A  553  ALA PHE ALA THR GLY HIS ALA GLN ALA GLY LEU ASN GLY          
SEQRES  34 A  553  TRP TYR LEU SER GLN ILE LEU HIS LYS GLU GLY GLN GLY          
SEQRES  35 A  553  ARG LEU GLY PHE TYR GLY TYR ALA LEU GLN ASP GLN CYS          
SEQRES  36 A  553  GLY ALA ALA ASN SER LEU SER VAL ARG SER ASP GLU GLY          
SEQRES  37 A  553  LEU PRO LEU GLU LEU ARG GLY PRO ASN TYR PRO ASN TYR          
SEQRES  38 A  553  ALA MET ASN VAL GLY HIS LEU GLY GLU TYR ALA GLY ILE          
SEQRES  39 A  553  VAL GLN ALA ALA HIS ALA ALA ARG GLY ASP ALA PHE CYS          
SEQRES  40 A  553  VAL HIS PRO VAL ILE LYS VAL ALA PHE ALA ASP GLU ASN          
SEQRES  41 A  553  LEU VAL PHE ASP PHE THR GLU PRO ARG LYS GLU PHE ALA          
SEQRES  42 A  553  LYS GLY ALA LEU ARG GLU PHE GLU PRO ALA GLY GLU ARG          
SEQRES  43 A  553  ASP LEU ILE VAL PRO ALA GLU                                  
SEQRES   1 B  443  MET ALA ARG GLU ALA LYS ASP THR VAL ASP LEU TYR ASP          
SEQRES   2 B  443  ASP ARG GLY ASN CYS VAL ALA GLU GLU VAL PRO ILE GLU          
SEQRES   3 B  443  VAL LEU SER PRO MET ARG ASN GLU ALA ILE GLN SER ILE          
SEQRES   4 B  443  VAL ASN ASP ILE LYS ARG THR VAL ALA VAL ASP LEU GLU          
SEQRES   5 B  443  GLY ILE GLU ASN ALA LEU GLN ASN ALA THR VAL GLY GLY          
SEQRES   6 B  443  LYS GLY MET LYS ILE PRO GLY ARG GLU MET ASP VAL ASP          
SEQRES   7 B  443  ILE VAL ASP ASN ALA GLU ALA ILE ALA ASP GLU ILE GLU          
SEQRES   8 B  443  LYS MET ILE ARG VAL TYR GLN ASP ASP ASP THR ASN VAL          
SEQRES   9 B  443  GLU PRO MET TYR ASP GLY LYS ARG LEU LEU VAL GLN LEU          
SEQRES  10 B  443  PRO SER GLU ARG VAL LYS VAL MET ALA ASP PRO TYR SER          
SEQRES  11 B  443  GLY THR LEU GLN ALA GLY MET ALA VAL VAL HIS ALA ILE          
SEQRES  12 B  443  ILE ASP VAL CYS GLU VAL ASP MET TRP ASP ALA ASN MET          
SEQRES  13 B  443  VAL LYS ALA ALA VAL PHE GLY ARG TYR PRO GLN THR ILE          
SEQRES  14 B  443  ASP TYR PHE GLY GLY ASN VAL ALA SER MET LEU ASP VAL          
SEQRES  15 B  443  PRO MET LYS GLN GLU GLY VAL GLY TYR ALA LEU ARG ASN          
SEQRES  16 B  443  ILE MET VAL ASN HIS ILE VAL ALA ALA THR ARG LYS ASN          
SEQRES  17 B  443  THR MET GLN ALA VAL CYS LEU ALA ALA THR LEU GLN GLN          
SEQRES  18 B  443  THR ALA MET PHE GLU MET GLY ASP ALA LEU GLY PRO PHE          
SEQRES  19 B  443  GLU ARG LEU HIS LEU LEU GLY TYR ALA TYR GLN GLY LEU          
SEQRES  20 B  443  ASN ALA ASP ASN MET VAL TYR ASP ILE VAL LYS LYS HIS          
SEQRES  21 B  443  GLY LYS GLU GLY THR VAL GLY THR VAL VAL ARG GLU VAL          
SEQRES  22 B  443  VAL GLU ARG ALA LEU GLU ASP GLY VAL ILE GLU VAL LYS          
SEQRES  23 B  443  GLU GLU LEU PRO SER PHE LYS VAL TYR LYS ALA ASN ASP          
SEQRES  24 B  443  MET ASP LEU TRP ASN ALA TYR ALA ALA ALA GLY LEU VAL          
SEQRES  25 B  443  ALA ALA VAL MET VAL ASN GLN GLY ALA ALA ARG ALA ALA          
SEQRES  26 B  443  GLN GLY VAL SER ALA THR ILE LEU TYR TYR ASN ASP LEU          
SEQRES  27 B  443  LEU GLU TYR GLU THR GLY LEU PRO GLY VAL ASP PHE GLY          
SEQRES  28 B  443  ARG ALA GLU GLY THR ALA VAL GLY PHE SER PHE PHE SER          
SEQRES  29 B  443  HIS SER ILE TYR GLY GLY GLY GLY PRO GLY ILE PHE HIS          
SEQRES  30 B  443  GLY ASN HIS ILE VAL THR ARG HIS SER LYS GLY PHE ALA          
SEQRES  31 B  443  ILE PRO PRO VAL ALA ALA ALA MET ALA LEU ASP ALA GLY          
SEQRES  32 B  443  THR GLN MET PHE SER PRO GLU VAL THR SER LYS LEU ILE          
SEQRES  33 B  443  GLY ASP VAL PHE GLY GLU ILE ASP GLU PHE ARG GLU PRO          
SEQRES  34 B  443  MET LYS TYR ILE THR GLU ALA ALA ALA GLU GLU ALA LYS          
SEQRES  35 B  443  ARG                                                          
SEQRES   1 C  258  MET ALA GLU LYS ALA GLN PHE TYR TYR PRO GLY GLU THR          
SEQRES   2 C  258  ASP VAL ALA GLU ASN ARG ARG LYS TYR MET ASN PRO ASN          
SEQRES   3 C  258  TYR GLU LEU LYS LYS LEU ARG GLU ILE PRO ASP GLU ASP          
SEQRES   4 C  258  ILE VAL ARG LEU MET GLY HIS ARG GLU PRO GLY GLU GLU          
SEQRES   5 C  258  TYR PRO SER VAL HIS PRO PRO LEU GLU GLU MET GLU GLU          
SEQRES   6 C  258  PRO GLU CYS PRO ILE ARG GLU LEU VAL GLU PRO THR GLU          
SEQRES   7 C  258  GLY ALA LYS ALA GLY ASP ARG ILE ARG TYR ILE GLN PHE          
SEQRES   8 C  258  THR ASP SER VAL TYR PHE ALA PRO ILE HIS PRO TYR ILE          
SEQRES   9 C  258  ARG ALA ARG MET TYR MET TRP ARG TYR ARG GLY VAL ASP          
SEQRES  10 C  258  THR GLY SER LEU SER GLY ARG GLN ILE ILE GLU VAL ARG          
SEQRES  11 C  258  GLU ARG ASP LEU GLU LYS ILE ALA LYS GLU LEU LEU GLU          
SEQRES  12 C  258  THR GLU ILE PHE ASP PRO ALA ARG SER GLY VAL ARG GLY          
SEQRES  13 C  258  ALA THR VAL HIS GLY HIS ALA LEU ARG LEU ASP GLU ASN          
SEQRES  14 C  258  GLY LEU MET LEU HIS ALA LEU ARG ARG TYR ARG LEU ASN          
SEQRES  15 C  258  GLU GLU THR GLY GLU VAL GLU TYR VAL LYS ASP GLN VAL          
SEQRES  16 C  258  GLY ILE GLU LEU ASP GLU PRO ILE PRO VAL GLY ALA PRO          
SEQRES  17 C  258  ALA ASP GLU ASP ASP LEU LYS GLU ARG THR THR ILE TYR          
SEQRES  18 C  258  ARG ILE ASP GLY THR PRO TYR ARG GLU ASP GLU GLU LEU          
SEQRES  19 C  258  LEU GLN VAL VAL GLN ARG ILE HIS GLU LEU ARG THR LEU          
SEQRES  20 C  258  ALA GLY TYR ARG PRO GLU GLU ALA GLU GLY LYS                  
SEQRES   1 D  553  MET SER SER ALA GLU GLU LYS LEU PHE MET LYS ALA LEU          
SEQRES   2 D  553  LYS GLU LYS PHE GLU GLU SER PRO GLU GLU LYS TYR THR          
SEQRES   3 D  553  LYS PHE TYR ILE PHE GLY GLY TRP LYS GLN SER GLU ARG          
SEQRES   4 D  553  LYS LYS GLU PHE LYS GLU TRP ALA ASP LYS ILE VAL GLU          
SEQRES   5 D  553  GLU ARG GLY VAL PRO HIS TYR ASN PRO ASP ILE GLY VAL          
SEQRES   6 D  553  PRO LEU GLY GLN ARG LYS LEU MET SER TYR GLN VAL SER          
SEQRES   7 D  553  GLY THR ASP VAL PHE VAL GLU GLY ASP ASP LEU THR PHE          
SEQRES   8 D  553  VAL ASN ASN ALA ALA MET GLN GLN MET TRP ASP ASP ILE          
SEQRES   9 D  553  ARG ARG THR VAL ILE VAL GLY MET ASP THR ALA HIS ARG          
SEQRES  10 D  553  VAL LEU GLU ARG ARG LEU GLY LYS GLU VAL THR PRO GLU          
SEQRES  11 D  553  THR ILE ASN GLU TYR MET GLU THR LEU ASN HIS ALA LEU          
SEQRES  12 D  553  PRO GLY GLY ALA VAL VAL GLN GLU HIS MET VAL GLU ILE          
SEQRES  13 D  553  HIS PRO GLY LEU THR TRP ASP CYS TYR ALA LYS ILE ILE          
SEQRES  14 D  553  THR GLY ASP LEU GLU LEU ALA ASP GLU ILE ASP ASP LYS          
SEQRES  15 D  553  PHE LEU ILE ASP ILE GLU LYS LEU PHE PRO GLU GLU GLN          
SEQRES  16 D  553  ALA GLU GLN LEU ILE LYS ALA ILE GLY ASN ARG THR TYR          
SEQRES  17 D  553  GLN VAL CYS ARG MET PRO THR ILE VAL GLY HIS VAL CYS          
SEQRES  18 D  553  ASP GLY ALA THR MET TYR ARG TRP ALA ALA MET GLN ILE          
SEQRES  19 D  553  ALA MET SER PHE ILE CYS ALA TYR LYS ILE ALA ALA GLY          
SEQRES  20 D  553  GLU ALA ALA VAL SER ASP PHE ALA PHE ALA SER LYS HIS          
SEQRES  21 D  553  ALA GLU VAL ILE ASN MET GLY GLU MET LEU PRO ALA ARG          
SEQRES  22 D  553  ARG ALA ARG GLY GLU ASN GLU PRO GLY GLY VAL PRO PHE          
SEQRES  23 D  553  GLY VAL LEU ALA ASP CYS VAL GLN THR MET ARG LYS TYR          
SEQRES  24 D  553  PRO ASP ASP PRO ALA LYS VAL ALA LEU GLU VAL ILE ALA          
SEQRES  25 D  553  ALA GLY ALA MET LEU TYR ASP GLN ILE TRP LEU GLY SER          
SEQRES  26 D  553  TYR MET SER GLY GLY VAL GLY PHE THR GLN TYR ALA THR          
SEQRES  27 D  553  ALA VAL TYR PRO ASP ASN ILE LEU ASP ASP TYR VAL TYR          
SEQRES  28 D  553  TYR GLY LEU GLU TYR VAL GLU ASP LYS TYR GLY ILE ALA          
SEQRES  29 D  553  GLU ALA GLU PRO SER MET ASP VAL VAL LYS ASP VAL ALA          
SEQRES  30 D  553  THR GLU VAL THR LEU TYR GLY LEU GLU GLN TYR GLU ARG          
SEQRES  31 D  553  TYR PRO ALA ALA MET GLU THR HIS PHE GLY GLY SER GLN          
SEQRES  32 D  553  ARG ALA ALA VAL CYS ALA ALA ALA ALA GLY CYS SER THR          
SEQRES  33 D  553  ALA PHE ALA THR GLY HIS ALA GLN ALA GLY LEU ASN GLY          
SEQRES  34 D  553  TRP TYR LEU SER GLN ILE LEU HIS LYS GLU GLY GLN GLY          
SEQRES  35 D  553  ARG LEU GLY PHE TYR GLY TYR ALA LEU GLN ASP GLN CYS          
SEQRES  36 D  553  GLY ALA ALA ASN SER LEU SER VAL ARG SER ASP GLU GLY          
SEQRES  37 D  553  LEU PRO LEU GLU LEU ARG GLY PRO ASN TYR PRO ASN TYR          
SEQRES  38 D  553  ALA MET ASN VAL GLY HIS LEU GLY GLU TYR ALA GLY ILE          
SEQRES  39 D  553  VAL GLN ALA ALA HIS ALA ALA ARG GLY ASP ALA PHE CYS          
SEQRES  40 D  553  VAL HIS PRO VAL ILE LYS VAL ALA PHE ALA ASP GLU ASN          
SEQRES  41 D  553  LEU VAL PHE ASP PHE THR GLU PRO ARG LYS GLU PHE ALA          
SEQRES  42 D  553  LYS GLY ALA LEU ARG GLU PHE GLU PRO ALA GLY GLU ARG          
SEQRES  43 D  553  ASP LEU ILE VAL PRO ALA GLU                                  
SEQRES   1 E  443  MET ALA ARG GLU ALA LYS ASP THR VAL ASP LEU TYR ASP          
SEQRES   2 E  443  ASP ARG GLY ASN CYS VAL ALA GLU GLU VAL PRO ILE GLU          
SEQRES   3 E  443  VAL LEU SER PRO MET ARG ASN GLU ALA ILE GLN SER ILE          
SEQRES   4 E  443  VAL ASN ASP ILE LYS ARG THR VAL ALA VAL ASP LEU GLU          
SEQRES   5 E  443  GLY ILE GLU ASN ALA LEU GLN ASN ALA THR VAL GLY GLY          
SEQRES   6 E  443  LYS GLY MET LYS ILE PRO GLY ARG GLU MET ASP VAL ASP          
SEQRES   7 E  443  ILE VAL ASP ASN ALA GLU ALA ILE ALA ASP GLU ILE GLU          
SEQRES   8 E  443  LYS MET ILE ARG VAL TYR GLN ASP ASP ASP THR ASN VAL          
SEQRES   9 E  443  GLU PRO MET TYR ASP GLY LYS ARG LEU LEU VAL GLN LEU          
SEQRES  10 E  443  PRO SER GLU ARG VAL LYS VAL MET ALA ASP PRO TYR SER          
SEQRES  11 E  443  GLY THR LEU GLN ALA GLY MET ALA VAL VAL HIS ALA ILE          
SEQRES  12 E  443  ILE ASP VAL CYS GLU VAL ASP MET TRP ASP ALA ASN MET          
SEQRES  13 E  443  VAL LYS ALA ALA VAL PHE GLY ARG TYR PRO GLN THR ILE          
SEQRES  14 E  443  ASP TYR PHE GLY GLY ASN VAL ALA SER MET LEU ASP VAL          
SEQRES  15 E  443  PRO MET LYS GLN GLU GLY VAL GLY TYR ALA LEU ARG ASN          
SEQRES  16 E  443  ILE MET VAL ASN HIS ILE VAL ALA ALA THR ARG LYS ASN          
SEQRES  17 E  443  THR MET GLN ALA VAL CYS LEU ALA ALA THR LEU GLN GLN          
SEQRES  18 E  443  THR ALA MET PHE GLU MET GLY ASP ALA LEU GLY PRO PHE          
SEQRES  19 E  443  GLU ARG LEU HIS LEU LEU GLY TYR ALA TYR GLN GLY LEU          
SEQRES  20 E  443  ASN ALA ASP ASN MET VAL TYR ASP ILE VAL LYS LYS HIS          
SEQRES  21 E  443  GLY LYS GLU GLY THR VAL GLY THR VAL VAL ARG GLU VAL          
SEQRES  22 E  443  VAL GLU ARG ALA LEU GLU ASP GLY VAL ILE GLU VAL LYS          
SEQRES  23 E  443  GLU GLU LEU PRO SER PHE LYS VAL TYR LYS ALA ASN ASP          
SEQRES  24 E  443  MET ASP LEU TRP ASN ALA TYR ALA ALA ALA GLY LEU VAL          
SEQRES  25 E  443  ALA ALA VAL MET VAL ASN GLN GLY ALA ALA ARG ALA ALA          
SEQRES  26 E  443  GLN GLY VAL SER ALA THR ILE LEU TYR TYR ASN ASP LEU          
SEQRES  27 E  443  LEU GLU TYR GLU THR GLY LEU PRO GLY VAL ASP PHE GLY          
SEQRES  28 E  443  ARG ALA GLU GLY THR ALA VAL GLY PHE SER PHE PHE SER          
SEQRES  29 E  443  HIS SER ILE TYR GLY GLY GLY GLY PRO GLY ILE PHE HIS          
SEQRES  30 E  443  GLY ASN HIS ILE VAL THR ARG HIS SER LYS GLY PHE ALA          
SEQRES  31 E  443  ILE PRO PRO VAL ALA ALA ALA MET ALA LEU ASP ALA GLY          
SEQRES  32 E  443  THR GLN MET PHE SER PRO GLU VAL THR SER LYS LEU ILE          
SEQRES  33 E  443  GLY ASP VAL PHE GLY GLU ILE ASP GLU PHE ARG GLU PRO          
SEQRES  34 E  443  MET LYS TYR ILE THR GLU ALA ALA ALA GLU GLU ALA LYS          
SEQRES  35 E  443  ARG                                                          
SEQRES   1 F  258  MET ALA GLU LYS ALA GLN PHE TYR TYR PRO GLY GLU THR          
SEQRES   2 F  258  ASP VAL ALA GLU ASN ARG ARG LYS TYR MET ASN PRO ASN          
SEQRES   3 F  258  TYR GLU LEU LYS LYS LEU ARG GLU ILE PRO ASP GLU ASP          
SEQRES   4 F  258  ILE VAL ARG LEU MET GLY HIS ARG GLU PRO GLY GLU GLU          
SEQRES   5 F  258  TYR PRO SER VAL HIS PRO PRO LEU GLU GLU MET GLU GLU          
SEQRES   6 F  258  PRO GLU CYS PRO ILE ARG GLU LEU VAL GLU PRO THR GLU          
SEQRES   7 F  258  GLY ALA LYS ALA GLY ASP ARG ILE ARG TYR ILE GLN PHE          
SEQRES   8 F  258  THR ASP SER VAL TYR PHE ALA PRO ILE HIS PRO TYR ILE          
SEQRES   9 F  258  ARG ALA ARG MET TYR MET TRP ARG TYR ARG GLY VAL ASP          
SEQRES  10 F  258  THR GLY SER LEU SER GLY ARG GLN ILE ILE GLU VAL ARG          
SEQRES  11 F  258  GLU ARG ASP LEU GLU LYS ILE ALA LYS GLU LEU LEU GLU          
SEQRES  12 F  258  THR GLU ILE PHE ASP PRO ALA ARG SER GLY VAL ARG GLY          
SEQRES  13 F  258  ALA THR VAL HIS GLY HIS ALA LEU ARG LEU ASP GLU ASN          
SEQRES  14 F  258  GLY LEU MET LEU HIS ALA LEU ARG ARG TYR ARG LEU ASN          
SEQRES  15 F  258  GLU GLU THR GLY GLU VAL GLU TYR VAL LYS ASP GLN VAL          
SEQRES  16 F  258  GLY ILE GLU LEU ASP GLU PRO ILE PRO VAL GLY ALA PRO          
SEQRES  17 F  258  ALA ASP GLU ASP ASP LEU LYS GLU ARG THR THR ILE TYR          
SEQRES  18 F  258  ARG ILE ASP GLY THR PRO TYR ARG GLU ASP GLU GLU LEU          
SEQRES  19 F  258  LEU GLN VAL VAL GLN ARG ILE HIS GLU LEU ARG THR LEU          
SEQRES  20 F  258  ALA GLY TYR ARG PRO GLU GLU ALA GLU GLY LYS                  
HET    F43  A1553      62                                                       
HET    TP7  A1554      21                                                       
HET    COM  A1555       7                                                       
HET    F43  D1553      62                                                       
HET    TP7  D1554      21                                                       
HET    COM  D1555       7                                                       
HETNAM     F43 FACTOR 430                                                       
HETNAM     TP7 COENZYME B                                                       
HETNAM     COM 1-THIOETHANESULFONIC ACID                                        
HETSYN     TP7 7-MERCAPTOHEPTANOYLTHREONINEPHOSPHATE                            
FORMUL   7  F43    2(C42 H51 N6 NI O13 1+)                                      
FORMUL   8  TP7    2(C11 H22 N O7 P S)                                          
FORMUL   9  COM    2(C2 H6 O3 S2)                                               
HELIX    1   1 PHE A    9  PHE A   17  1                                   9    
HELIX    2   2 GLY A   32  GLN A   36  5                                   5    
HELIX    3   3 SER A   37  GLY A   55  1                                  19    
HELIX    4   4 ASP A   87  LEU A   89  5                                   3    
HELIX    5   5 THR A   90  ASN A   93  5                                   4    
HELIX    6   6 ASN A   94  ARG A  106  1                                  13    
HELIX    7   7 MET A  112  ARG A  122  1                                  11    
HELIX    8   8 THR A  128  LEU A  143  1                                  16    
HELIX    9   9 ASP A  172  ASP A  177  1                                   6    
HELIX   10  10 ASP A  180  PHE A  183  5                                   4    
HELIX   11  11 ASP A  186  PHE A  191  1                                   6    
HELIX   12  12 PRO A  192  GLY A  204  1                                  13    
HELIX   13  13 PRO A  214  CYS A  221  1                                   8    
HELIX   14  14 ASP A  222  LYS A  243  1                                  22    
HELIX   15  15 ALA A  250  HIS A  260  1                                  11    
HELIX   16  16 PRO A  271  ALA A  275  5                                   5    
HELIX   17  17 GLU A  280  VAL A  284  5                                   5    
HELIX   18  18 PRO A  285  VAL A  293  1                                   9    
HELIX   19  19 GLN A  294  TYR A  299  1                                   6    
HELIX   20  20 ASP A  302  GLN A  320  1                                  19    
HELIX   21  21 ILE A  321  MET A  327  1                                   7    
HELIX   22  22 PHE A  333  ALA A  339  1                                   7    
HELIX   23  23 ASN A  344  TYR A  361  1                                  18    
HELIX   24  24 SER A  369  TYR A  391  1                                  23    
HELIX   25  25 TYR A  391  HIS A  398  1                                   8    
HELIX   26  26 GLY A  400  GLY A  421  1                                  22    
HELIX   27  27 HIS A  422  GLY A  442  1                                  21    
HELIX   28  28 ALA A  450  SER A  462  1                                  13    
HELIX   29  29 PRO A  470  ARG A  474  5                                   5    
HELIX   30  30 TYR A  478  ALA A  482  5                                   5    
HELIX   31  31 HIS A  487  GLY A  503  1                                  17    
HELIX   32  32 HIS A  509  PHE A  516  1                                   8    
HELIX   33  33 GLU A  527  LEU A  537  1                                  11    
HELIX   34  34 ARG A  546  VAL A  550  5                                   5    
HELIX   35  35 GLU B   26  SER B   29  5                                   4    
HELIX   36  36 ASN B   33  ARG B   45  1                                  13    
HELIX   37  37 LEU B   51  ALA B   61  1                                  11    
HELIX   38  38 ILE B   79  ASP B   81  5                                   3    
HELIX   39  39 ASN B   82  ARG B   95  1                                  14    
HELIX   40  40 TYR B  108  GLY B  110  5                                   3    
HELIX   41  41 PRO B  118  LYS B  123  1                                   6    
HELIX   42  42 SER B  130  ASP B  145  1                                  16    
HELIX   43  43 ASP B  150  ASP B  153  5                                   4    
HELIX   44  44 ALA B  154  GLY B  163  1                                  10    
HELIX   45  45 VAL B  182  GLN B  186  5                                   5    
HELIX   46  46 TYR B  191  ASN B  195  5                                   5    
HELIX   47  47 MET B  197  THR B  205  1                                   9    
HELIX   48  48 ASN B  208  MET B  227  1                                  20    
HELIX   49  49 LEU B  231  PRO B  233  5                                   3    
HELIX   50  50 PHE B  234  LEU B  247  1                                  14    
HELIX   51  51 ASN B  251  GLY B  261  1                                  11    
HELIX   52  52 THR B  265  ASP B  280  1                                  16    
HELIX   53  53 ASP B  299  ARG B  323  1                                  25    
HELIX   54  54 GLY B  327  GLU B  342  1                                  16    
HELIX   55  55 GLY B  347  PHE B  350  5                                   4    
HELIX   56  56 GLY B  351  PHE B  363  1                                  13    
HELIX   57  57 GLY B  372  PHE B  376  5                                   5    
HELIX   58  58 ALA B  390  LEU B  400  1                                  11    
HELIX   59  59 SER B  413  PHE B  420  1                                   8    
HELIX   60  60 ILE B  423  GLU B  428  1                                   6    
HELIX   61  61 GLU B  428  ALA B  441  1                                  14    
HELIX   62  62 THR C   13  TYR C   22  1                                  10    
HELIX   63  63 PRO C   36  MET C   44  1                                   9    
HELIX   64  64 PRO C   59  MET C   63  5                                   5    
HELIX   65  65 THR C   77  GLY C   83  1                                   7    
HELIX   66  66 HIS C  101  TYR C  113  1                                  13    
HELIX   67  67 GLU C  131  THR C  144  1                                  14    
HELIX   68  68 ASP C  210  GLU C  216  1                                   7    
HELIX   69  69 PRO C  227  GLU C  230  5                                   4    
HELIX   70  70 ASP C  231  ARG C  251  1                                  21    
HELIX   71  71 PHE D    9  PHE D   17  1                                   9    
HELIX   72  72 GLY D   32  GLN D   36  5                                   5    
HELIX   73  73 SER D   37  GLY D   55  1                                  19    
HELIX   74  74 ASP D   87  LEU D   89  5                                   3    
HELIX   75  75 THR D   90  ASN D   93  5                                   4    
HELIX   76  76 ASN D   94  ARG D  106  1                                  13    
HELIX   77  77 MET D  112  ARG D  122  1                                  11    
HELIX   78  78 THR D  128  LEU D  143  1                                  16    
HELIX   79  79 ASP D  172  ASP D  177  1                                   6    
HELIX   80  80 ASP D  180  PHE D  183  5                                   4    
HELIX   81  81 ASP D  186  PHE D  191  1                                   6    
HELIX   82  82 PRO D  192  GLY D  204  1                                  13    
HELIX   83  83 PRO D  214  CYS D  221  1                                   8    
HELIX   84  84 ASP D  222  LYS D  243  1                                  22    
HELIX   85  85 ALA D  250  HIS D  260  1                                  11    
HELIX   86  86 PRO D  271  ALA D  275  5                                   5    
HELIX   87  87 GLU D  280  VAL D  284  5                                   5    
HELIX   88  88 PRO D  285  VAL D  293  1                                   9    
HELIX   89  89 GLN D  294  TYR D  299  1                                   6    
HELIX   90  90 ASP D  302  GLN D  320  1                                  19    
HELIX   91  91 ILE D  321  MET D  327  1                                   7    
HELIX   92  92 PHE D  333  ALA D  339  1                                   7    
HELIX   93  93 ASN D  344  TYR D  361  1                                  18    
HELIX   94  94 SER D  369  TYR D  391  1                                  23    
HELIX   95  95 TYR D  391  HIS D  398  1                                   8    
HELIX   96  96 GLY D  400  GLY D  421  1                                  22    
HELIX   97  97 HIS D  422  GLY D  442  1                                  21    
HELIX   98  98 ALA D  450  SER D  462  1                                  13    
HELIX   99  99 PRO D  470  ARG D  474  5                                   5    
HELIX  100 100 TYR D  478  ALA D  482  5                                   5    
HELIX  101 101 HIS D  487  GLY D  503  1                                  17    
HELIX  102 102 HIS D  509  PHE D  516  1                                   8    
HELIX  103 103 GLU D  527  LEU D  537  1                                  11    
HELIX  104 104 ARG D  546  VAL D  550  5                                   5    
HELIX  105 105 GLU E   26  SER E   29  5                                   4    
HELIX  106 106 ASN E   33  ARG E   45  1                                  13    
HELIX  107 107 LEU E   51  ALA E   61  1                                  11    
HELIX  108 108 ILE E   79  ASP E   81  5                                   3    
HELIX  109 109 ASN E   82  ARG E   95  1                                  14    
HELIX  110 110 TYR E  108  GLY E  110  5                                   3    
HELIX  111 111 PRO E  118  LYS E  123  1                                   6    
HELIX  112 112 SER E  130  ASP E  145  1                                  16    
HELIX  113 113 ASP E  150  ASP E  153  5                                   4    
HELIX  114 114 ALA E  154  GLY E  163  1                                  10    
HELIX  115 115 VAL E  182  GLN E  186  5                                   5    
HELIX  116 116 TYR E  191  ASN E  195  5                                   5    
HELIX  117 117 MET E  197  THR E  205  1                                   9    
HELIX  118 118 ASN E  208  MET E  227  1                                  20    
HELIX  119 119 LEU E  231  PRO E  233  5                                   3    
HELIX  120 120 PHE E  234  LEU E  247  1                                  14    
HELIX  121 121 ASN E  251  GLY E  261  1                                  11    
HELIX  122 122 THR E  265  ASP E  280  1                                  16    
HELIX  123 123 ASP E  299  ARG E  323  1                                  25    
HELIX  124 124 GLY E  327  GLU E  342  1                                  16    
HELIX  125 125 GLY E  347  PHE E  350  5                                   4    
HELIX  126 126 GLY E  351  PHE E  363  1                                  13    
HELIX  127 127 GLY E  372  PHE E  376  5                                   5    
HELIX  128 128 ALA E  390  LEU E  400  1                                  11    
HELIX  129 129 SER E  413  PHE E  420  1                                   8    
HELIX  130 130 ILE E  423  GLU E  428  1                                   6    
HELIX  131 131 GLU E  428  ALA E  441  1                                  14    
HELIX  132 132 THR F   13  TYR F   22  1                                  10    
HELIX  133 133 PRO F   36  MET F   44  1                                   9    
HELIX  134 134 PRO F   59  MET F   63  5                                   5    
HELIX  135 135 THR F   77  GLY F   83  1                                   7    
HELIX  136 136 HIS F  101  TYR F  113  1                                  13    
HELIX  137 137 GLU F  131  THR F  144  1                                  14    
HELIX  138 138 ASP F  210  GLU F  216  1                                   7    
HELIX  139 139 PRO F  227  GLU F  230  5                                   4    
HELIX  140 140 ASP F  231  ARG F  251  1                                  21    
SHEET    1  AA 2 SER A  74  GLN A  76  0                                        
SHEET    2  AA 2 PHE A  83  GLU A  85 -1  O  VAL A  84   N  TYR A  75           
SHEET    1  AB 4 TYR A 165  THR A 170  0                                        
SHEET    2  AB 4 THR A 207  ARG A 212 -1  O  TYR A 208   N  ILE A 169           
SHEET    3  AB 4 THR A 107  GLY A 111 -1  O  VAL A 108   N  CYS A 211           
SHEET    4  AB 4 VAL A 263  ASN A 265 -1  O  ILE A 264   N  ILE A 109           
SHEET    1  BA 2 THR B   8  TYR B  12  0                                        
SHEET    2  BA 2 CYS B  18  PRO B  24 -1  N  VAL B  19   O  LEU B  11           
SHEET    1  BB 4 ASN B 103  MET B 107  0                                        
SHEET    2  BB 4 ARG B 112  GLN B 116 -1  O  ARG B 112   N  MET B 107           
SHEET    3  BB 4 THR B  46  ASP B  50 -1  O  VAL B  47   N  VAL B 115           
SHEET    4  BB 4 VAL B 176  ALA B 177 -1  O  ALA B 177   N  ALA B  48           
SHEET    1  BC 2 ILE B 283  GLU B 288  0                                        
SHEET    2  BC 2 LYS B 293  ALA B 297 -1  O  VAL B 294   N  LYS B 286           
SHEET    1  CA 4 ASP C 117  SER C 120  0                                        
SHEET    2  CA 4 GLN C 125  ARG C 130 -1  O  ILE C 126   N  GLY C 119           
SHEET    3  CA 4 ILE C  86  ASP C  93 -1  O  ARG C  87   N  VAL C 129           
SHEET    4  CA 4 SER C 152  VAL C 154 -1  O  GLY C 153   N  THR C  92           
SHEET    1  CB 3 TYR C 179  ASN C 182  0                                        
SHEET    2  CB 3 GLU C 187  LYS C 192 -1  O  GLU C 187   N  ASN C 182           
SHEET    3  CB 3 GLU C 198  PRO C 204 -1  N  LEU C 199   O  VAL C 191           
SHEET    1  DA 2 SER D  74  GLN D  76  0                                        
SHEET    2  DA 2 PHE D  83  GLU D  85 -1  O  VAL D  84   N  TYR D  75           
SHEET    1  DB 4 TYR D 165  THR D 170  0                                        
SHEET    2  DB 4 THR D 207  ARG D 212 -1  O  TYR D 208   N  ILE D 169           
SHEET    3  DB 4 THR D 107  GLY D 111 -1  O  VAL D 108   N  CYS D 211           
SHEET    4  DB 4 VAL D 263  ASN D 265 -1  O  ILE D 264   N  ILE D 109           
SHEET    1  EA 2 THR E   8  TYR E  12  0                                        
SHEET    2  EA 2 CYS E  18  PRO E  24 -1  N  VAL E  19   O  LEU E  11           
SHEET    1  EB 4 ASN E 103  MET E 107  0                                        
SHEET    2  EB 4 ARG E 112  GLN E 116 -1  O  ARG E 112   N  MET E 107           
SHEET    3  EB 4 THR E  46  ASP E  50 -1  O  VAL E  47   N  VAL E 115           
SHEET    4  EB 4 VAL E 176  ALA E 177 -1  O  ALA E 177   N  ALA E  48           
SHEET    1  EC 2 ILE E 283  GLU E 288  0                                        
SHEET    2  EC 2 LYS E 293  ALA E 297 -1  O  VAL E 294   N  LYS E 286           
SHEET    1  FA 4 ASP F 117  SER F 120  0                                        
SHEET    2  FA 4 GLN F 125  ARG F 130 -1  O  ILE F 126   N  GLY F 119           
SHEET    3  FA 4 ILE F  86  ASP F  93 -1  O  ARG F  87   N  VAL F 129           
SHEET    4  FA 4 SER F 152  VAL F 154 -1  O  GLY F 153   N  THR F  92           
SHEET    1  FB 3 TYR F 179  ASN F 182  0                                        
SHEET    2  FB 3 GLU F 187  LYS F 192 -1  O  GLU F 187   N  ASN F 182           
SHEET    3  FB 3 GLU F 198  PRO F 204 -1  N  LEU F 199   O  VAL F 191           
LINK         OE1 GLN A 150                NI   F43 A1553     1555   1555  2.08  
LINK        NI   F43 A1553                 S1  COM A1555     1555   1555  2.48  
LINK         OE1 GLN D 150                NI   F43 D1553     1555   1555  2.08  
LINK        NI   F43 D1553                 S1  COM D1555     1555   1555  2.48  
CISPEP   1 TYR B  165    PRO B  166          0        18.77                     
CISPEP   2 TYR E  165    PRO E  166          0        18.84                     
SITE     1 AC1 31 ALA A 147  VAL A 148  VAL A 149  GLN A 150                    
SITE     2 AC1 31 MET A 153  GLN A 233  MET A 236  ALA A 246                    
SITE     3 AC1 31 COM A1555  GLY D 329  GLY D 330  VAL D 331                    
SITE     4 AC1 31 GLY D 332  PHE D 333  THR D 334  GLN D 335                    
SITE     5 AC1 31 TYR D 336  PHE D 399  GLY D 400  PHE D 446                    
SITE     6 AC1 31 SER E 366  ILE E 367  TYR E 368  SER F 122                    
SITE     7 AC1 31 GLY F 123  ARG F 124  ALA F 157  THR F 158                    
SITE     8 AC1 31 VAL F 159  HIS F 160  HIS F 162                               
SITE     1 AC2 15 ARG A 273  LEU A 323  MET A 327  SER A 328                    
SITE     2 AC2 15 PHE A 446  MET A 483  ASN A 484  VAL A 485                    
SITE     3 AC2 15 TYR B 368  GLY B 370  HIS B 380  VAL B 382                    
SITE     4 AC2 15 ARG D 228  LYS D 259  HIS D 260                               
SITE     1 AC3  8 F43 A1553  TYR D 336  PHE D 446  TYR D 447                    
SITE     2 AC3  8 PHE E 362  TYR E 368  LEU F 121  ARG F 124                    
SITE     1 AC4 31 GLY A 329  GLY A 330  VAL A 331  GLY A 332                    
SITE     2 AC4 31 PHE A 333  THR A 334  GLN A 335  TYR A 336                    
SITE     3 AC4 31 PHE A 399  GLY A 400  PHE A 446  SER B 366                    
SITE     4 AC4 31 ILE B 367  TYR B 368  SER C 122  GLY C 123                    
SITE     5 AC4 31 ARG C 124  ALA C 157  THR C 158  VAL C 159                    
SITE     6 AC4 31 HIS C 160  HIS C 162  ALA D 147  VAL D 148                    
SITE     7 AC4 31 VAL D 149  GLN D 150  MET D 153  GLN D 233                    
SITE     8 AC4 31 MET D 236  ALA D 246  COM D1555                               
SITE     1 AC5 15 ARG A 228  LYS A 259  HIS A 260  ARG D 273                    
SITE     2 AC5 15 LEU D 323  MET D 327  SER D 328  PHE D 446                    
SITE     3 AC5 15 MET D 483  ASN D 484  VAL D 485  TYR E 368                    
SITE     4 AC5 15 GLY E 370  HIS E 380  VAL E 382                               
SITE     1 AC6  8 TYR A 336  PHE A 446  TYR A 447  PHE B 362                    
SITE     2 AC6  8 TYR B 368  LEU C 121  ARG C 124  F43 D1553                    
CRYST1   80.519  115.740  268.510  90.00  90.00  90.00 P 21 21 21    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      0.012419  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008640  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003724        0.00000                         
MTRIX1   1 -0.928500 -0.010300 -0.371300      147.06590    1                    
MTRIX2   1 -0.009900 -0.998600  0.052500      -34.96940    1                    
MTRIX3   1 -0.371300  0.052400  0.927000       29.28690    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system