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Database: PDB
Entry: 1E6Y
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Original site: 1E6Y 
HEADER    OXIDOREDUCTASE                          23-AUG-00   1E6Y              
TITLE     METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYL-COENZYME M REDUCTASE SUBUNIT ALPHA;                 
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: COENZYME-B SULFOETHYLTHIOTRANSFERASE ALPHA, METHYL-COENZYME 
COMPND   5 M REDUCTASE I ALPHA SUBUNIT;                                         
COMPND   6 EC: 2.8.4.1;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: METHYL-COENZYME M REDUCTASE I BETA SUBUNIT;                
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 SYNONYM: METHYL-COENZYME M REDUCTASE I BETA SUBUNIT, COENZYME-B      
COMPND  11 SULFOETHYLTHIOTRANSFERASE BETA;                                      
COMPND  12 EC: 2.8.4.1;                                                         
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: METHYL-COENZYME M REDUCTASE SUBUNIT GAMMA;                 
COMPND  15 CHAIN: C, F;                                                         
COMPND  16 SYNONYM: METHYL-COENZYME M REDUCTASE I GAMMA SUBUNIT, COENZYME-B     
COMPND  17 SULFOETHYLTHIOTRANSFERASE GAMMA;                                     
COMPND  18 EC: 2.8.4.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOSARCINA BARKERI;                         
SOURCE   3 ORGANISM_TAXID: 2208;                                                
SOURCE   4 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: METHANOSARCINA BARKERI;                         
SOURCE   7 ORGANISM_TAXID: 2208;                                                
SOURCE   8 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: METHANOSARCINA BARKERI;                         
SOURCE  11 ORGANISM_TAXID: 2208;                                                
SOURCE  12 CELLULAR_LOCATION: CYTOPLASM                                         
KEYWDS    BIOLOGICAL METHANOGENESIS, NI-ENZYME, OXIDOREDUCTASE, NI ENZYME       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.GRABARSE,U.ERMLER                                                   
REVDAT   6   29-MAR-17 1E6Y    1       CAVEAT FORMUL                            
REVDAT   5   20-MAY-15 1E6Y    1       HETNAM HETSYN FORMUL                     
REVDAT   4   16-NOV-11 1E6Y    1       COMPND SOURCE KEYWDS REMARK              
REVDAT   4 2                   1       SEQADV HETSYN FORMUL HETATM              
REVDAT   4 3                   1       MASTER VERSN                             
REVDAT   3   24-FEB-09 1E6Y    1       VERSN                                    
REVDAT   2   01-DEC-00 1E6Y    1       SEQRES                                   
REVDAT   1   18-OCT-00 1E6Y    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.    1.60 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 4119399.530                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 311702                         
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) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 15708                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.001                           
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 45831                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE                    : 0.2370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2408                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.005                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18915                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 198                                     
REMARK   3   SOLVENT ATOMS            : 2195                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.97000                                              
REMARK   3    B22 (A**2) : -7.04000                                             
REMARK   3    B33 (A**2) : 3.07000                                              
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) : 0.15                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
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) : 0.17                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 3.060                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.540 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.850 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.970 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.460 ; 2.500                
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 : NULL                                                    
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  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1E6Y 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-5281.                                        
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: PDB ENTRY 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): 2.47                     
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       56.83900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.64400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.54950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.64400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.83900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.54950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 54880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -246.9 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     LYS A  1570                                                      
REMARK 465     LEU B  2434                                                      
REMARK 465     LYS D  4570                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG D4551   CG    ARG D4551   CD     -0.201                       
REMARK 500    ARG D4551   CG    ARG D4551   CD      0.244                       
REMARK 500    ARG D4551   NE    ARG D4551   CZ      0.131                       
REMARK 500    ARG D4551   CZ    ARG D4551   NH2     0.294                       
REMARK 500    ARG D4551   CZ    ARG D4551   NH2     0.365                       
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 A1081   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A1284   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    GLU A1396   OE1 -  CD  -  OE2 ANGL. DEV. = -24.5 DEGREES          
REMARK 500    GLU A1396   OE1 -  CD  -  OE2 ANGL. DEV. = -20.4 DEGREES          
REMARK 500    ARG A1547   CD  -  NE  -  CZ  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG A1563   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B2064   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B2069   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B2117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B2190   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG B2384   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG B2384   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C3018   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG C3019   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG C3068   CD  -  NE  -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG C3068   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C3102   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG C3121   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG C3121   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG C3152   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG C3152   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG C3175   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C3175   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C3235   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C3235   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG D4063   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG D4116   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG D4284   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D4421   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG D4421   NE  -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG D4460   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG D4491   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D4491   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D4551   CB  -  CG  -  CD  ANGL. DEV. =  28.5 DEGREES          
REMARK 500    ARG D4551   CB  -  CG  -  CD  ANGL. DEV. = -20.4 DEGREES          
REMARK 500    ARG D4551   CG  -  CD  -  NE  ANGL. DEV. =  40.0 DEGREES          
REMARK 500    ARG D4551   CG  -  CD  -  NE  ANGL. DEV. = -41.7 DEGREES          
REMARK 500    ARG D4551   NH1 -  CZ  -  NH2 ANGL. DEV. = -93.8 DEGREES          
REMARK 500    ARG D4551   NH1 -  CZ  -  NH2 ANGL. DEV. = 102.0 DEGREES          
REMARK 500    ARG D4551   NE  -  CZ  -  NH1 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG D4551   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG D4551   NE  -  CZ  -  NH2 ANGL. DEV. = -22.4 DEGREES          
REMARK 500    ARG D4551   NE  -  CZ  -  NH2 ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ARG E5011   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG E5028   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG E5117   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG E5190   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG E5384   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG E5384   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    VAL F6040   CG1 -  CB  -  CG2 ANGL. DEV. = -94.5 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 ANGLE DEVIATIONS.                             
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 A1067     -152.59   -143.86                                   
REMARK 500    ASN A1069      100.62   -160.92                                   
REMARK 500    VAL A1160      -55.48   -125.00                                   
REMARK 500    THR A1232     -121.67   -110.68                                   
REMARK 500    MHS A1271      -66.11   -142.61                                   
REMARK 500    TRP A1332      -73.35    -71.63                                   
REMARK 500    SER A1335      -72.03   -132.49                                   
REMARK 500    SER A1338      -97.59   -150.73                                   
REMARK 500    TYR A1351       15.81   -140.01                                   
REMARK 500    LEU A1461      -99.26   -134.87                                   
REMARK 500    LEU A1486      132.79    178.21                                   
REMARK 500    HIS A1504      -54.16   -132.30                                   
REMARK 500    VAL A1525      -20.33   -155.11                                   
REMARK 500    ASP B2123     -129.83   -140.14                                   
REMARK 500    SER B2177     -148.90   -100.34                                   
REMARK 500    HIS B2362       15.41   -149.51                                   
REMARK 500    TYR C3007      -58.95     74.41                                   
REMARK 500    HIS C3157      124.14    -38.99                                   
REMARK 500    ASN C3220      -91.18   -133.89                                   
REMARK 500    PHE D4067     -152.48   -145.18                                   
REMARK 500    ASN D4069      100.18   -160.81                                   
REMARK 500    VAL D4160      -54.12   -124.22                                   
REMARK 500    THR D4232     -121.70   -111.52                                   
REMARK 500    MHS D4271      -66.55   -143.57                                   
REMARK 500    TRP D4332      -72.14    -74.21                                   
REMARK 500    SER D4335      -72.60   -132.67                                   
REMARK 500    SER D4338      -94.93   -150.15                                   
REMARK 500    LEU D4461     -105.04   -133.63                                   
REMARK 500    LEU D4486      134.84    179.33                                   
REMARK 500    HIS D4504      -52.22   -132.61                                   
REMARK 500    VAL D4525      -22.24   -154.17                                   
REMARK 500    ASP E5096     -168.59    -79.30                                   
REMARK 500    ASP E5123     -129.63   -137.07                                   
REMARK 500    SER E5177     -145.57    -99.27                                   
REMARK 500    ASN E5246       19.80     59.85                                   
REMARK 500    ASN E5247       18.48     59.13                                   
REMARK 500    HIS E5362       15.25   -148.58                                   
REMARK 500    TYR F6007      -55.52     72.52                                   
REMARK 500    ALA F6064       33.04    -95.42                                   
REMARK 500    TYR F6093       59.72    -92.54                                   
REMARK 500    HIS F6157      125.04    -35.77                                   
REMARK 500    ASN F6220      -85.59   -135.57                                   
REMARK 500    ASP F6226       73.92   -102.77                                   
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    GLU A1396         0.16    SIDE CHAIN                              
REMARK 500    TYR B2331         0.10    SIDE CHAIN                              
REMARK 500    TYR B2347         0.07    SIDE CHAIN                              
REMARK 500    TYR C3093         0.07    SIDE CHAIN                              
REMARK 500    ARG D4551         0.23    SIDE CHAIN                              
REMARK 500    TYR E5148         0.07    SIDE CHAIN                              
REMARK 500    TYR E5331         0.10    SIDE CHAIN                              
REMARK 500    TYR E5347         0.07    SIDE CHAIN                              
REMARK 500    TYR F6093         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C2109        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH D2220        DISTANCE =  5.86 ANGSTROMS                       
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 A2570  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A1161   OE1                                                    
REMARK 620 2 F43 A2570   NA   84.2                                              
REMARK 620 3 F43 A2570   NB   80.7  86.9                                        
REMARK 620 4 F43 A2570   NC   88.6 172.6  93.4                                  
REMARK 620 5 F43 A2570   ND   87.6  93.4 168.2  84.8                            
REMARK 620 6 COM D5572   S1  170.1  87.3  94.0 100.1  97.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F43 D5570  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 COM A2572   S1                                                     
REMARK 620 2 F43 D5570   NA   87.3                                              
REMARK 620 3 F43 D5570   NB   95.1  86.7                                        
REMARK 620 4 F43 D5570   NC  100.3 172.4  93.3                                  
REMARK 620 5 F43 D5570   ND   96.9  93.4 168.0  85.0                            
REMARK 620 6 GLN D4161   OE1 172.9  87.3  80.1  85.2  88.0                      
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 2570                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP7 A 2571                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM A 2572                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F43 D 5570                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP7 D 5571                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM D 5572                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2573                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2574                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 5573                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E6V   RELATED DB: PDB                                   
REMARK 900 METHYL-COENZYME M REDUCTASE FROM METHANOPYRUS KANDLERI               
REMARK 900 RELATED ID: 1MRO   RELATED DB: PDB                                   
REMARK 900 METHYL-COENZYME M REDUCTASE                                          
DBREF  1E6Y A 1002  1570  UNP    P07962   MCRA_METBA       1    569             
DBREF  1E6Y B 2002  2434  UNP    P07955   MCRB_METBA       1    433             
DBREF  1E6Y C 3002  3248  UNP    P07964   MCRG_METBA       1    247             
DBREF  1E6Y D 4002  4570  UNP    P07962   MCRA_METBA       1    569             
DBREF  1E6Y E 5002  5434  UNP    P07955   MCRB_METBA       1    433             
DBREF  1E6Y F 6002  6248  UNP    P07964   MCRG_METBA       1    247             
SEQRES   1 A  569  ALA ALA ASP ILE PHE SER LYS PHE LYS LYS ASP MET GLU          
SEQRES   2 A  569  VAL LYS PHE ALA GLN GLU PHE GLY SER ASN LYS GLN THR          
SEQRES   3 A  569  GLY GLY ASP ILE THR ASP LYS THR ALA LYS PHE LEU ARG          
SEQRES   4 A  569  LEU GLY PRO GLU GLN ASP PRO ARG LYS VAL GLU MET ILE          
SEQRES   5 A  569  LYS ALA GLY LYS GLU ILE ALA GLU LYS ARG GLY ILE ALA          
SEQRES   6 A  569  PHE TYR ASN PRO MET MET HIS SER GLY ALA PRO LEU GLY          
SEQRES   7 A  569  GLN ARG ALA ILE THR PRO TYR THR ILE SER GLY THR ASP          
SEQRES   8 A  569  ILE VAL CYS GLU PRO ASP ASP LEU HIS TYR VAL ASN ASN          
SEQRES   9 A  569  ALA ALA MET GLN GLN MET TRP ASP ASP ILE ARG ARG THR          
SEQRES  10 A  569  CYS ILE VAL GLY LEU ASP MET ALA HIS GLU THR LEU GLU          
SEQRES  11 A  569  LYS ARG LEU GLY LYS GLU VAL THR PRO GLU THR ILE ASN          
SEQRES  12 A  569  HIS TYR LEU GLU VAL LEU ASN HIS ALA MET PRO GLY ALA          
SEQRES  13 A  569  ALA VAL VAL GLN GLU MET MET VAL GLU THR HIS PRO ALA          
SEQRES  14 A  569  LEU VAL ASP ASP CYS TYR VAL LYS VAL PHE THR GLY ASP          
SEQRES  15 A  569  ASP ALA LEU ALA ASP GLU ILE ASP LYS GLN PHE LEU ILE          
SEQRES  16 A  569  ASP ILE ASN LYS GLU PHE SER GLU GLU GLN ALA ALA GLN          
SEQRES  17 A  569  ILE LYS ALA SER ILE GLY LYS THR SER TRP GLN ALA ILE          
SEQRES  18 A  569  HIS ILE PRO THR ILE VAL SER ARG THR THR ASP GLY ALA          
SEQRES  19 A  569  GLN THR SER ARG TRP ALA ALA MET GLN ILE GLY MET SER          
SEQRES  20 A  569  PHE ILE SER ALA TYR ALA MET CYS ALA GLY GLU ALA ALA          
SEQRES  21 A  569  VAL ALA ASP LEU SER PHE ALA ALA LYS MHS ALA ALA LEU          
SEQRES  22 A  569  VAL SER MET GLY GLU MET LEU PRO ALA ARG AGM ALA ARG          
SEQRES  23 A  569  GLY PRO ASN GLU PRO GLY GLY LEU SER PHE GLY HIS LEU          
SEQRES  24 A  569  SER ASP ILE VAL GLN THR SER ARG VAL SER GLU ASP PRO          
SEQRES  25 A  569  ALA LYS ILE ALA LEU GLU VAL VAL GLY ALA GLY CYS MET          
SEQRES  26 A  569  LEU TYR ASP GLN ILE TRP LEU GLY SER TYR MET SER GLY          
SEQRES  27 A  569  GLY VAL GLY PHE THR GLN TYR ALA THR ALA ALA TYR THR          
SEQRES  28 A  569  ASP ASP ILE LEU ASP ASN ASN THR TYR TYR ASP VAL ASP          
SEQRES  29 A  569  TYR ILE ASN ASP LYS TYR ASN GLY ALA ALA THR VAL GLY          
SEQRES  30 A  569  LYS ASP ASN LYS VAL LYS ALA SER LEU GLU VAL VAL LYS          
SEQRES  31 A  569  ASP ILE ALA THR GLU SER THR LEU TYR GLY ILE GLU THR          
SEQRES  32 A  569  TYR GLU LYS PHE PRO THR ALA LEU GLU ASP HIS PHE GLY          
SEQRES  33 A  569  GLY SER GLN ARG ALA THR VAL LEU ALA ALA ALA ALA GLY          
SEQRES  34 A  569  VAL ALA CYS SER LEU ALA THR GLY ASN ALA ASN ALA GLY          
SEQRES  35 A  569  LEU SER GLY TRP TYR LEU SER MET TYR LEU HIS LYS GLU          
SEQRES  36 A  569  ALA TRP GLY ARG LEU GLY PHE PHE GL3 PHE ASP LEU GLN          
SEQRES  37 A  569  ASP GLN SMC GLY ALA THR ASN VAL LEU SER TYR GLN GLY          
SEQRES  38 A  569  ASP GLU GLY LEU PRO ASP GLU LEU ARG GLY PRO ASN TYR          
SEQRES  39 A  569  PRO ASN TYR ALA MET ASN VAL GLY HIS GLN GLY GLY TYR          
SEQRES  40 A  569  ALA GLY ILE ALA GLN ALA ALA HIS SER GLY ARG GLY ASP          
SEQRES  41 A  569  ALA PHE THR VAL ASN PRO LEU LEU LYS VAL CYS PHE ALA          
SEQRES  42 A  569  ASP ASP LEU LEU PRO PHE ASN PHE ALA GLU PRO ARG ARG          
SEQRES  43 A  569  GLU PHE GLY ARG GLY ALA ILE ARG GLU PHE VAL PRO ALA          
SEQRES  44 A  569  GLY GLU ARG SER LEU VAL ILE PRO ALA LYS                      
SEQRES   1 B  433  SER ASP THR VAL ASP ILE TYR ASP ASP ARG GLY LYS LEU          
SEQRES   2 B  433  LEU GLU SER ASN VAL ASP ILE MET SER LEU ALA PRO THR          
SEQRES   3 B  433  ARG ASN ALA ALA ILE GLN SER ILE ILE MET ASP THR LYS          
SEQRES   4 B  433  ARG SER VAL ALA VAL ASN LEU ALA GLY ILE GLN GLY ALA          
SEQRES   5 B  433  LEU ALA SER GLY LYS MET GLY GLY LYS GLY ARG GLN ILE          
SEQRES   6 B  433  LEU GLY ARG GLY LEU ASN TYR ASP ILE VAL GLY ASN ALA          
SEQRES   7 B  433  ASP ALA ILE ALA GLU ASN VAL LYS LYS LEU VAL GLN VAL          
SEQRES   8 B  433  ASP GLU GLY ASP ASP THR ASN VAL ILE LYS VAL LYS GLY          
SEQRES   9 B  433  GLY LYS SER LEU LEU ILE GLN SER PRO LYS SER ARG ILE          
SEQRES  10 B  433  ILE ALA GLY ALA ASP PHE MET SER ALA THR THR VAL GLY          
SEQRES  11 B  433  ALA ALA ALA VAL THR GLN THR ILE MET ASP MET PHE GLY          
SEQRES  12 B  433  THR ASP PRO TYR ASP ALA PRO ILE VAL LYS SER ALA VAL          
SEQRES  13 B  433  TRP GLY SER TYR PRO GLN THR MET ASP LEU MET GLY GLY          
SEQRES  14 B  433  GLN VAL GLN GLY ILE LEU SER ILE PRO GLN ASN ASN GLU          
SEQRES  15 B  433  GLY LEU GLY PHE SER LEU ARG ASN ILE MET ALA ASN HIS          
SEQRES  16 B  433  VAL ALA ALA ILE SER ASN ARG ASN ALA MET ASN ALA SER          
SEQRES  17 B  433  ALA LEU SER SER ILE TYR GLU GLN SER GLY ILE PHE GLU          
SEQRES  18 B  433  MET GLY GLY ALA VAL GLY MET PHE GLU ARG HIS GLN LEU          
SEQRES  19 B  433  LEU GLY LEU ALA TYR GLN GLY LEU ASN ALA ASN ASN LEU          
SEQRES  20 B  433  LEU TYR ASP ILE VAL LYS GLU ASN GLY LYS ASP GLY THR          
SEQRES  21 B  433  ILE GLY THR VAL ILE GLU SER VAL VAL ARG ARG ALA ILE          
SEQRES  22 B  433  GLU ALA GLY ILE ILE SER VAL ASP LYS THR ALA PRO SER          
SEQRES  23 B  433  GLY TYR ASN PHE TYR LYS ALA ASN ASP VAL PRO LYS TRP          
SEQRES  24 B  433  ASN ALA CYS ALA ALA VAL GLY THR LEU ALA ALA THR LEU          
SEQRES  25 B  433  VAL ASN CYS GLY ALA GLY ARG ALA ALA GLN ASN VAL SER          
SEQRES  26 B  433  SER THR LEU LEU TYR PHE ASN ASP ILE LEU GLU LYS GLU          
SEQRES  27 B  433  THR GLY LEU PRO GLY CYS ASP TYR GLY LYS VAL GLU GLY          
SEQRES  28 B  433  THR ALA VAL GLY PHE SER PHE PHE SER HIS SER ILE TYR          
SEQRES  29 B  433  GLY GLY GLY GLY PRO GLY VAL PHE ASN GLY ASN HIS VAL          
SEQRES  30 B  433  VAL THR ARG HIS SER ARG GLY PHE ALA ILE PRO CYS VAL          
SEQRES  31 B  433  CYS ALA ALA VAL ALA LEU ASP ALA GLY THR GLN MET PHE          
SEQRES  32 B  433  SER ILE GLU SER THR SER GLY LEU ILE GLY ASP VAL PHE          
SEQRES  33 B  433  GLY ALA ILE PRO GLU PHE ARG GLU PRO ILE LYS ALA VAL          
SEQRES  34 B  433  ALA GLY VAL LEU                                              
SEQRES   1 C  247  ALA TYR GLU ARG GLN TYR TYR PRO GLY ALA THR SER VAL          
SEQRES   2 C  247  ALA ALA ASN ARG ARG LYS HIS MET SER GLY LYS LEU GLU          
SEQRES   3 C  247  LYS LEU ARG GLU ILE SER ASP GLU ASP LEU THR ALA VAL          
SEQRES   4 C  247  LEU GLY HIS ARG ALA PRO GLY SER ASP TYR PRO SER THR          
SEQRES   5 C  247  HIS PRO PRO LEU ALA GLU MET GLY GLU PRO ALA OCS SER          
SEQRES   6 C  247  THR ARG GLU ASN VAL ALA ALA THR PRO GLY ALA ALA ALA          
SEQRES   7 C  247  GLY ASP ARG VAL ARG TYR ILE GLN PHE ALA ASP SER MET          
SEQRES   8 C  247  TYR ASN ALA PRO ALA THR PRO TYR PHE ARG SER TYR PHE          
SEQRES   9 C  247  ALA ALA ILE ASN PHE ARG GLY VAL ASP PRO GLY THR LEU          
SEQRES  10 C  247  SER GLY ARG GLN ILE VAL GLU ALA ARG GLU ARG ASP MET          
SEQRES  11 C  247  GLU GLN CYS ALA LYS VAL GLN MET GLU THR GLU ILE THR          
SEQRES  12 C  247  ASP HIS ALA LEU ALA GLY VAL ARG GLY ALA THR VAL HIS          
SEQRES  13 C  247  GLY HIS SER VAL ARG LEU GLN GLU ASP GLY VAL MET PHE          
SEQRES  14 C  247  ASP MET LEU ASP ARG ARG ARG LEU GLU ASN GLY THR ILE          
SEQRES  15 C  247  ILE MET ASP LYS ASP GLN VAL ALA ILE PRO LEU ASP ARG          
SEQRES  16 C  247  LYS VAL ASP LEU GLY LYS PRO MET SER SER GLU GLU ALA          
SEQRES  17 C  247  ALA LYS ARG THR THR ILE TYR ARG VAL ASP ASN VAL ALA          
SEQRES  18 C  247  PHE ARG ASP ASP ALA GLU VAL VAL GLU TRP VAL HIS ARG          
SEQRES  19 C  247  ILE PHE ASP GLN ARG THR LYS PHE GLY PHE GLN PRO LYS          
SEQRES   1 D  569  ALA ALA ASP ILE PHE SER LYS PHE LYS LYS ASP MET GLU          
SEQRES   2 D  569  VAL LYS PHE ALA GLN GLU PHE GLY SER ASN LYS GLN THR          
SEQRES   3 D  569  GLY GLY ASP ILE THR ASP LYS THR ALA LYS PHE LEU ARG          
SEQRES   4 D  569  LEU GLY PRO GLU GLN ASP PRO ARG LYS VAL GLU MET ILE          
SEQRES   5 D  569  LYS ALA GLY LYS GLU ILE ALA GLU LYS ARG GLY ILE ALA          
SEQRES   6 D  569  PHE TYR ASN PRO MET MET HIS SER GLY ALA PRO LEU GLY          
SEQRES   7 D  569  GLN ARG ALA ILE THR PRO TYR THR ILE SER GLY THR ASP          
SEQRES   8 D  569  ILE VAL CYS GLU PRO ASP ASP LEU HIS TYR VAL ASN ASN          
SEQRES   9 D  569  ALA ALA MET GLN GLN MET TRP ASP ASP ILE ARG ARG THR          
SEQRES  10 D  569  CYS ILE VAL GLY LEU ASP MET ALA HIS GLU THR LEU GLU          
SEQRES  11 D  569  LYS ARG LEU GLY LYS GLU VAL THR PRO GLU THR ILE ASN          
SEQRES  12 D  569  HIS TYR LEU GLU VAL LEU ASN HIS ALA MET PRO GLY ALA          
SEQRES  13 D  569  ALA VAL VAL GLN GLU MET MET VAL GLU THR HIS PRO ALA          
SEQRES  14 D  569  LEU VAL ASP ASP CYS TYR VAL LYS VAL PHE THR GLY ASP          
SEQRES  15 D  569  ASP ALA LEU ALA ASP GLU ILE ASP LYS GLN PHE LEU ILE          
SEQRES  16 D  569  ASP ILE ASN LYS GLU PHE SER GLU GLU GLN ALA ALA GLN          
SEQRES  17 D  569  ILE LYS ALA SER ILE GLY LYS THR SER TRP GLN ALA ILE          
SEQRES  18 D  569  HIS ILE PRO THR ILE VAL SER ARG THR THR ASP GLY ALA          
SEQRES  19 D  569  GLN THR SER ARG TRP ALA ALA MET GLN ILE GLY MET SER          
SEQRES  20 D  569  PHE ILE SER ALA TYR ALA MET CYS ALA GLY GLU ALA ALA          
SEQRES  21 D  569  VAL ALA ASP LEU SER PHE ALA ALA LYS MHS ALA ALA LEU          
SEQRES  22 D  569  VAL SER MET GLY GLU MET LEU PRO ALA ARG AGM ALA ARG          
SEQRES  23 D  569  GLY PRO ASN GLU PRO GLY GLY LEU SER PHE GLY HIS LEU          
SEQRES  24 D  569  SER ASP ILE VAL GLN THR SER ARG VAL SER GLU ASP PRO          
SEQRES  25 D  569  ALA LYS ILE ALA LEU GLU VAL VAL GLY ALA GLY CYS MET          
SEQRES  26 D  569  LEU TYR ASP GLN ILE TRP LEU GLY SER TYR MET SER GLY          
SEQRES  27 D  569  GLY VAL GLY PHE THR GLN TYR ALA THR ALA ALA TYR THR          
SEQRES  28 D  569  ASP ASP ILE LEU ASP ASN ASN THR TYR TYR ASP VAL ASP          
SEQRES  29 D  569  TYR ILE ASN ASP LYS TYR ASN GLY ALA ALA THR VAL GLY          
SEQRES  30 D  569  LYS ASP ASN LYS VAL LYS ALA SER LEU GLU VAL VAL LYS          
SEQRES  31 D  569  ASP ILE ALA THR GLU SER THR LEU TYR GLY ILE GLU THR          
SEQRES  32 D  569  TYR GLU LYS PHE PRO THR ALA LEU GLU ASP HIS PHE GLY          
SEQRES  33 D  569  GLY SER GLN ARG ALA THR VAL LEU ALA ALA ALA ALA GLY          
SEQRES  34 D  569  VAL ALA CYS SER LEU ALA THR GLY ASN ALA ASN ALA GLY          
SEQRES  35 D  569  LEU SER GLY TRP TYR LEU SER MET TYR LEU HIS LYS GLU          
SEQRES  36 D  569  ALA TRP GLY ARG LEU GLY PHE PHE GL3 PHE ASP LEU GLN          
SEQRES  37 D  569  ASP GLN SMC GLY ALA THR ASN VAL LEU SER TYR GLN GLY          
SEQRES  38 D  569  ASP GLU GLY LEU PRO ASP GLU LEU ARG GLY PRO ASN TYR          
SEQRES  39 D  569  PRO ASN TYR ALA MET ASN VAL GLY HIS GLN GLY GLY TYR          
SEQRES  40 D  569  ALA GLY ILE ALA GLN ALA ALA HIS SER GLY ARG GLY ASP          
SEQRES  41 D  569  ALA PHE THR VAL ASN PRO LEU LEU LYS VAL CYS PHE ALA          
SEQRES  42 D  569  ASP ASP LEU LEU PRO PHE ASN PHE ALA GLU PRO ARG ARG          
SEQRES  43 D  569  GLU PHE GLY ARG GLY ALA ILE ARG GLU PHE VAL PRO ALA          
SEQRES  44 D  569  GLY GLU ARG SER LEU VAL ILE PRO ALA LYS                      
SEQRES   1 E  433  SER ASP THR VAL ASP ILE TYR ASP ASP ARG GLY LYS LEU          
SEQRES   2 E  433  LEU GLU SER ASN VAL ASP ILE MET SER LEU ALA PRO THR          
SEQRES   3 E  433  ARG ASN ALA ALA ILE GLN SER ILE ILE MET ASP THR LYS          
SEQRES   4 E  433  ARG SER VAL ALA VAL ASN LEU ALA GLY ILE GLN GLY ALA          
SEQRES   5 E  433  LEU ALA SER GLY LYS MET GLY GLY LYS GLY ARG GLN ILE          
SEQRES   6 E  433  LEU GLY ARG GLY LEU ASN TYR ASP ILE VAL GLY ASN ALA          
SEQRES   7 E  433  ASP ALA ILE ALA GLU ASN VAL LYS LYS LEU VAL GLN VAL          
SEQRES   8 E  433  ASP GLU GLY ASP ASP THR ASN VAL ILE LYS VAL LYS GLY          
SEQRES   9 E  433  GLY LYS SER LEU LEU ILE GLN SER PRO LYS SER ARG ILE          
SEQRES  10 E  433  ILE ALA GLY ALA ASP PHE MET SER ALA THR THR VAL GLY          
SEQRES  11 E  433  ALA ALA ALA VAL THR GLN THR ILE MET ASP MET PHE GLY          
SEQRES  12 E  433  THR ASP PRO TYR ASP ALA PRO ILE VAL LYS SER ALA VAL          
SEQRES  13 E  433  TRP GLY SER TYR PRO GLN THR MET ASP LEU MET GLY GLY          
SEQRES  14 E  433  GLN VAL GLN GLY ILE LEU SER ILE PRO GLN ASN ASN GLU          
SEQRES  15 E  433  GLY LEU GLY PHE SER LEU ARG ASN ILE MET ALA ASN HIS          
SEQRES  16 E  433  VAL ALA ALA ILE SER ASN ARG ASN ALA MET ASN ALA SER          
SEQRES  17 E  433  ALA LEU SER SER ILE TYR GLU GLN SER GLY ILE PHE GLU          
SEQRES  18 E  433  MET GLY GLY ALA VAL GLY MET PHE GLU ARG HIS GLN LEU          
SEQRES  19 E  433  LEU GLY LEU ALA TYR GLN GLY LEU ASN ALA ASN ASN LEU          
SEQRES  20 E  433  LEU TYR ASP ILE VAL LYS GLU ASN GLY LYS ASP GLY THR          
SEQRES  21 E  433  ILE GLY THR VAL ILE GLU SER VAL VAL ARG ARG ALA ILE          
SEQRES  22 E  433  GLU ALA GLY ILE ILE SER VAL ASP LYS THR ALA PRO SER          
SEQRES  23 E  433  GLY TYR ASN PHE TYR LYS ALA ASN ASP VAL PRO LYS TRP          
SEQRES  24 E  433  ASN ALA CYS ALA ALA VAL GLY THR LEU ALA ALA THR LEU          
SEQRES  25 E  433  VAL ASN CYS GLY ALA GLY ARG ALA ALA GLN ASN VAL SER          
SEQRES  26 E  433  SER THR LEU LEU TYR PHE ASN ASP ILE LEU GLU LYS GLU          
SEQRES  27 E  433  THR GLY LEU PRO GLY CYS ASP TYR GLY LYS VAL GLU GLY          
SEQRES  28 E  433  THR ALA VAL GLY PHE SER PHE PHE SER HIS SER ILE TYR          
SEQRES  29 E  433  GLY GLY GLY GLY PRO GLY VAL PHE ASN GLY ASN HIS VAL          
SEQRES  30 E  433  VAL THR ARG HIS SER ARG GLY PHE ALA ILE PRO CYS VAL          
SEQRES  31 E  433  CYS ALA ALA VAL ALA LEU ASP ALA GLY THR GLN MET PHE          
SEQRES  32 E  433  SER ILE GLU SER THR SER GLY LEU ILE GLY ASP VAL PHE          
SEQRES  33 E  433  GLY ALA ILE PRO GLU PHE ARG GLU PRO ILE LYS ALA VAL          
SEQRES  34 E  433  ALA GLY VAL LEU                                              
SEQRES   1 F  247  ALA TYR GLU ARG GLN TYR TYR PRO GLY ALA THR SER VAL          
SEQRES   2 F  247  ALA ALA ASN ARG ARG LYS HIS MET SER GLY LYS LEU GLU          
SEQRES   3 F  247  LYS LEU ARG GLU ILE SER ASP GLU ASP LEU THR ALA VAL          
SEQRES   4 F  247  LEU GLY HIS ARG ALA PRO GLY SER ASP TYR PRO SER THR          
SEQRES   5 F  247  HIS PRO PRO LEU ALA GLU MET GLY GLU PRO ALA OCS SER          
SEQRES   6 F  247  THR ARG GLU ASN VAL ALA ALA THR PRO GLY ALA ALA ALA          
SEQRES   7 F  247  GLY ASP ARG VAL ARG TYR ILE GLN PHE ALA ASP SER MET          
SEQRES   8 F  247  TYR ASN ALA PRO ALA THR PRO TYR PHE ARG SER TYR PHE          
SEQRES   9 F  247  ALA ALA ILE ASN PHE ARG GLY VAL ASP PRO GLY THR LEU          
SEQRES  10 F  247  SER GLY ARG GLN ILE VAL GLU ALA ARG GLU ARG ASP MET          
SEQRES  11 F  247  GLU GLN CYS ALA LYS VAL GLN MET GLU THR GLU ILE THR          
SEQRES  12 F  247  ASP HIS ALA LEU ALA GLY VAL ARG GLY ALA THR VAL HIS          
SEQRES  13 F  247  GLY HIS SER VAL ARG LEU GLN GLU ASP GLY VAL MET PHE          
SEQRES  14 F  247  ASP MET LEU ASP ARG ARG ARG LEU GLU ASN GLY THR ILE          
SEQRES  15 F  247  ILE MET ASP LYS ASP GLN VAL ALA ILE PRO LEU ASP ARG          
SEQRES  16 F  247  LYS VAL ASP LEU GLY LYS PRO MET SER SER GLU GLU ALA          
SEQRES  17 F  247  ALA LYS ARG THR THR ILE TYR ARG VAL ASP ASN VAL ALA          
SEQRES  18 F  247  PHE ARG ASP ASP ALA GLU VAL VAL GLU TRP VAL HIS ARG          
SEQRES  19 F  247  ILE PHE ASP GLN ARG THR LYS PHE GLY PHE GLN PRO LYS          
MODRES 1E6Y MHS A 1271  HIS  N1-METHYLATED HISTIDINE                            
MODRES 1E6Y AGM A 1285  ARG  5-METHYL-ARGININE                                  
MODRES 1E6Y GL3 A 1465  GLY  THIOGLYCIN                                         
MODRES 1E6Y SMC A 1472  CYS  S-METHYLCYSTEINE                                   
MODRES 1E6Y OCS C 3065  CYS  CYSTEINESULFONIC ACID                              
MODRES 1E6Y MHS D 4271  HIS  N1-METHYLATED HISTIDINE                            
MODRES 1E6Y AGM D 4285  ARG  5-METHYL-ARGININE                                  
MODRES 1E6Y GL3 D 4465  GLY  THIOGLYCIN                                         
MODRES 1E6Y SMC D 4472  CYS  S-METHYLCYSTEINE                                   
MODRES 1E6Y OCS F 6065  CYS  CYSTEINESULFONIC ACID                              
HET    MHS  A1271      11                                                       
HET    AGM  A1285      12                                                       
HET    GL3  A1465       4                                                       
HET    SMC  A1472       7                                                       
HET    OCS  C3065       9                                                       
HET    MHS  D4271      11                                                       
HET    AGM  D4285      12                                                       
HET    GL3  D4465       4                                                       
HET    SMC  D4472       7                                                       
HET    OCS  F6065       9                                                       
HET    F43  A2570      62                                                       
HET    TP7  A2571      21                                                       
HET    COM  A2572       7                                                       
HET    GOL  A2573       6                                                       
HET    GOL  A2574       6                                                       
HET    F43  D5570      62                                                       
HET    TP7  D5571      21                                                       
HET    COM  D5572       7                                                       
HET    GOL  D5573       6                                                       
HETNAM     MHS N1-METHYLATED HISTIDINE                                          
HETNAM     AGM 5-METHYL-ARGININE                                                
HETNAM     GL3 THIOGLYCIN                                                       
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     OCS CYSTEINESULFONIC ACID                                            
HETNAM     F43 FACTOR 430                                                       
HETNAM     TP7 COENZYME B                                                       
HETNAM     COM 1-THIOETHANESULFONIC ACID                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     TP7 7-MERCAPTOHEPTANOYLTHREONINEPHOSPHATE                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MHS    2(C7 H11 N3 O2)                                              
FORMUL   1  AGM    2(C7 H17 N4 O2 1+)                                           
FORMUL   1  GL3    2(C2 H5 N O S)                                               
FORMUL   1  SMC    2(C4 H9 N O2 S)                                              
FORMUL   3  OCS    2(C3 H7 N O5 S)                                              
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)                                               
FORMUL  10  GOL    3(C3 H8 O3)                                                  
FORMUL  16  HOH   *2195(H2 O)                                                   
HELIX    1   1 ALA A 1002  ALA A 1018  1                                  17    
HELIX    2   2 GLY A 1042  GLN A 1045  5                                   4    
HELIX    3   3 ASP A 1046  GLY A 1064  1                                  19    
HELIX    4   4 ASN A 1069  HIS A 1073  5                                   5    
HELIX    5   5 GLU A 1096  HIS A 1101  5                                   6    
HELIX    6   6 HIS A 1101  ASN A 1104  5                                   4    
HELIX    7   7 ASN A 1105  ARG A 1117  1                                  13    
HELIX    8   8 LEU A 1123  GLY A 1135  1                                  13    
HELIX    9   9 THR A 1139  MET A 1154  1                                  16    
HELIX   10  10 HIS A 1168  VAL A 1172  5                                   5    
HELIX   11  11 ASP A 1183  ASP A 1188  1                                   6    
HELIX   12  12 GLU A 1189  ILE A 1190  5                                   2    
HELIX   13  13 ASP A 1191  PHE A 1194  5                                   4    
HELIX   14  14 ASP A 1197  PHE A 1202  1                                   6    
HELIX   15  15 SER A 1203  GLY A 1215  1                                  13    
HELIX   16  16 PRO A 1225  THR A 1232  1                                   8    
HELIX   17  17 ALA A 1235  TYR A 1253  1                                  19    
HELIX   18  18 GLU A 1259  LYS A 1270  1                                  12    
HELIX   19  19 GLU A 1291  LEU A 1295  5                                   5    
HELIX   20  20 SER A 1296  VAL A 1304  1                                   9    
HELIX   21  21 GLN A 1305  SER A 1310  1                                   6    
HELIX   22  22 ASP A 1312  ILE A 1331  1                                  20    
HELIX   23  23 ALA A 1002  MET A 1337  1                                 336    
HELIX   24  24 PHE A 1343  ALA A 1349  1                                   7    
HELIX   25  25 ASP A 1354  TYR A 1371  1                                  18    
HELIX   26  26 SER A 1386  PHE A 1408  1                                  23    
HELIX   27  27 PHE A 1408  HIS A 1415  1                                   8    
HELIX   28  28 GLY A 1417  GLY A 1438  1                                  22    
HELIX   29  29 ASN A 1439  GLY A 1459  1                                  21    
HELIX   30  30 GLY A 1473  LEU A 1478  1                                   6    
HELIX   31  31 TYR A 1495  ALA A 1499  5                                   5    
HELIX   32  32 HIS A 1504  GLY A 1518  1                                  15    
HELIX   33  33 ASN A 1526  PHE A 1533  1                                   8    
HELIX   34  34 GLU A 1544  ILE A 1554  1                                  11    
HELIX   35  35 ARG A 1563  ILE A 1567  5                                   5    
HELIX   36  36 MET B 2022  ALA B 2025  5                                   4    
HELIX   37  37 ASN B 2029  ARG B 2041  1                                  13    
HELIX   38  38 LEU B 2047  GLY B 2057  1                                  11    
HELIX   39  39 ILE B 2075  GLY B 2077  5                                   3    
HELIX   40  40 ASN B 2078  GLN B 2091  1                                  14    
HELIX   41  41 PRO B 2114  ALA B 2120  1                                   7    
HELIX   42  42 MET B 2125  PHE B 2143  1                                  19    
HELIX   43  43 ASP B 2146  TYR B 2148  5                                   3    
HELIX   44  44 ASP B 2149  GLY B 2159  1                                  11    
HELIX   45  45 ILE B 2178  ASN B 2182  5                                   5    
HELIX   46  46 PHE B 2187  ASN B 2191  5                                   5    
HELIX   47  47 MET B 2193  SER B 2201  1                                   9    
HELIX   48  48 ASN B 2204  MET B 2223  1                                  20    
HELIX   49  49 GLY B 2228  ASN B 2244  1                                  17    
HELIX   50  50 ASN B 2247  GLY B 2257  1                                  11    
HELIX   51  51 THR B 2261  ALA B 2276  1                                  16    
HELIX   52  52 ASP B 2296  ARG B 2320  1                                  25    
HELIX   53  53 ALA B 2321  GLN B 2323  5                                   3    
HELIX   54  54 ASN B 2324  GLY B 2341  1                                  18    
HELIX   55  55 GLY B 2344  TYR B 2347  5                                   4    
HELIX   56  56 GLY B 2348  PHE B 2360  1                                  13    
HELIX   57  57 GLY B 2369  PHE B 2373  5                                   5    
HELIX   58  58 ALA B 2387  ASP B 2398  1                                  12    
HELIX   59  59 SER B 2405  GLY B 2411  1                                   7    
HELIX   60  60 SER B 2410  GLY B 2418  1                                   9    
HELIX   61  61 ILE B 2420  GLU B 2425  1                                   6    
HELIX   62  62 GLU B 2425  GLY B 2432  1                                   8    
HELIX   63  63 THR C 3012  GLY C 3024  1                                  13    
HELIX   64  64 SER C 3033  GLY C 3042  1                                  10    
HELIX   65  65 PRO C 3056  GLY C 3061  1                                   6    
HELIX   66  66 SER C 3066  VAL C 3071  1                                   6    
HELIX   67  67 THR C 3074  GLY C 3080  1                                   7    
HELIX   68  68 THR C 3098  PHE C 3110  1                                  13    
HELIX   69  69 GLU C 3128  THR C 3141  1                                  14    
HELIX   70  70 SER C 3205  THR C 3213  1                                   9    
HELIX   71  71 ALA C 3222  ASP C 3225  5                                   4    
HELIX   72  72 ASP C 3226  GLN C 3246  1                                  21    
HELIX   73  73 ALA D 4002  ALA D 4018  1                                  17    
HELIX   74  74 GLY D 4042  GLN D 4045  5                                   4    
HELIX   75  75 ASP D 4046  GLY D 4064  1                                  19    
HELIX   76  76 ASN D 4069  HIS D 4073  5                                   5    
HELIX   77  77 GLU D 4096  HIS D 4101  5                                   6    
HELIX   78  78 HIS D 4101  ASN D 4104  5                                   4    
HELIX   79  79 ASN D 4105  ARG D 4117  1                                  13    
HELIX   80  80 LEU D 4123  GLY D 4135  1                                  13    
HELIX   81  81 THR D 4139  MET D 4154  1                                  16    
HELIX   82  82 HIS D 4168  VAL D 4172  5                                   5    
HELIX   83  83 ASP D 4183  ASP D 4188  1                                   6    
HELIX   84  84 GLU D 4189  ILE D 4190  5                                   2    
HELIX   85  85 ASP D 4191  PHE D 4194  5                                   4    
HELIX   86  86 ASP D 4197  PHE D 4202  1                                   6    
HELIX   87  87 SER D 4203  GLY D 4215  1                                  13    
HELIX   88  88 PRO D 4225  THR D 4232  1                                   8    
HELIX   89  89 ALA D 4235  TYR D 4253  1                                  19    
HELIX   90  90 GLU D 4259  LYS D 4270  1                                  12    
HELIX   91  91 GLU D 4291  LEU D 4295  5                                   5    
HELIX   92  92 SER D 4296  VAL D 4304  1                                   9    
HELIX   93  93 GLN D 4305  SER D 4310  1                                   6    
HELIX   94  94 ASP D 4312  GLN D 4330  1                                  19    
HELIX   95  95 ALA A 1002  MET D 4337  1                                 336    
HELIX   96  96 PHE D 4343  THR D 4352  1                                  10    
HELIX   97  97 ASP D 4354  TYR D 4371  1                                  18    
HELIX   98  98 SER D 4386  PHE D 4408  1                                  23    
HELIX   99  99 PHE D 4408  HIS D 4415  1                                   8    
HELIX  100 100 GLY D 4417  GLY D 4438  1                                  22    
HELIX  101 101 ASN D 4439  GLY D 4459  1                                  21    
HELIX  102 102 GLY D 4473  LEU D 4478  1                                   6    
HELIX  103 103 TYR D 4495  ALA D 4499  5                                   5    
HELIX  104 104 HIS D 4504  GLY D 4518  1                                  15    
HELIX  105 105 ASN D 4526  PHE D 4533  1                                   8    
HELIX  106 106 GLU D 4544  ILE D 4554  1                                  11    
HELIX  107 107 ARG D 4563  ILE D 4567  5                                   5    
HELIX  108 108 MET E 5022  ALA E 5025  5                                   4    
HELIX  109 109 ASN E 5029  ARG E 5041  1                                  13    
HELIX  110 110 LEU E 5047  GLY E 5057  1                                  11    
HELIX  111 111 ILE E 5075  GLY E 5077  5                                   3    
HELIX  112 112 ASN E 5078  GLN E 5091  1                                  14    
HELIX  113 113 LYS E 5104  GLY E 5106  5                                   3    
HELIX  114 114 PRO E 5114  ALA E 5120  1                                   7    
HELIX  115 115 MET E 5125  PHE E 5143  1                                  19    
HELIX  116 116 ASP E 5146  TYR E 5148  5                                   3    
HELIX  117 117 ASP E 5149  GLY E 5159  1                                  11    
HELIX  118 118 ILE E 5178  ASN E 5182  5                                   5    
HELIX  119 119 PHE E 5187  ASN E 5191  5                                   5    
HELIX  120 120 MET E 5193  SER E 5201  1                                   9    
HELIX  121 121 ASN E 5204  MET E 5223  1                                  20    
HELIX  122 122 GLY E 5228  LEU E 5243  1                                  16    
HELIX  123 123 ASN E 5247  GLY E 5257  1                                  11    
HELIX  124 124 THR E 5261  ALA E 5276  1                                  16    
HELIX  125 125 ASP E 5296  ARG E 5320  1                                  25    
HELIX  126 126 ALA E 5321  GLN E 5323  5                                   3    
HELIX  127 127 ASN E 5324  GLY E 5341  1                                  18    
HELIX  128 128 GLY E 5344  TYR E 5347  5                                   4    
HELIX  129 129 GLY E 5348  PHE E 5360  1                                  13    
HELIX  130 130 GLY E 5369  PHE E 5373  5                                   5    
HELIX  131 131 ALA E 5387  LEU E 5397  1                                  11    
HELIX  132 132 SER E 5405  GLY E 5411  1                                   7    
HELIX  133 133 SER E 5410  GLY E 5418  1                                   9    
HELIX  134 134 ILE E 5420  GLU E 5425  1                                   6    
HELIX  135 135 GLU E 5425  ALA E 5431  1                                   7    
HELIX  136 136 THR F 6012  GLY F 6024  1                                  13    
HELIX  137 137 SER F 6033  GLY F 6042  1                                  10    
HELIX  138 138 PRO F 6056  GLY F 6061  1                                   6    
HELIX  139 139 SER F 6066  VAL F 6071  1                                   6    
HELIX  140 140 THR F 6074  GLY F 6080  1                                   7    
HELIX  141 141 THR F 6098  PHE F 6110  1                                  13    
HELIX  142 142 GLU F 6128  THR F 6141  1                                  14    
HELIX  143 143 SER F 6205  THR F 6213  1                                   9    
HELIX  144 144 ALA F 6222  ASP F 6225  5                                   4    
HELIX  145 145 ASP F 6226  GLN F 6246  1                                  21    
SHEET    1   A 2 TYR A1086  THR A1087  0                                        
SHEET    2   A 2 VAL A1094  CYS A1095 -1  O  CYS A1095   N  TYR A1086           
SHEET    1   B 4 TYR A1176  THR A1181  0                                        
SHEET    2   B 4 SER A1218  HIS A1223 -1  O  TRP A1219   N  PHE A1180           
SHEET    3   B 4 THR A1118  GLY A1122 -1  O  CYS A1119   N  ILE A1222           
SHEET    4   B 4 LEU A1274  VAL A1275 -1  O  VAL A1275   N  ILE A1120           
SHEET    1   C 2 THR B2004  TYR B2008  0                                        
SHEET    2   C 2 LEU B2014  ASP B2020 -1  N  LEU B2015   O  ILE B2007           
SHEET    1   D 4 ASN B2099  VAL B2103  0                                        
SHEET    2   D 4 SER B2108  GLN B2112 -1  O  SER B2108   N  VAL B2103           
SHEET    3   D 4 SER B2042  ASN B2046 -1  O  VAL B2043   N  ILE B2111           
SHEET    4   D 4 VAL B2172  GLN B2173 -1  O  GLN B2173   N  ALA B2044           
SHEET    1   E 2 ILE B2279  THR B2284  0                                        
SHEET    2   E 2 ASN B2290  ALA B2294 -1  O  PHE B2291   N  ASP B2282           
SHEET    1   F 4 ASP C3114  THR C3117  0                                        
SHEET    2   F 4 GLN C3122  ARG C3127 -1  O  ILE C3123   N  GLY C3116           
SHEET    3   F 4 VAL C3083  ASP C3090 -1  O  ARG C3084   N  ALA C3126           
SHEET    4   F 4 ALA C3149  VAL C3151 -1  O  GLY C3150   N  ALA C3089           
SHEET    1   G 3 ARG C3176  GLU C3179  0                                        
SHEET    2   G 3 THR C3182  LYS C3187 -1  O  THR C3182   N  GLU C3179           
SHEET    3   G 3 PRO C3193  ASP C3199 -1  N  LEU C3194   O  ASP C3186           
SHEET    1   H 2 THR D4035  ALA D4036  0                                        
SHEET    2   H 2 LEU F6163  GLN F6164  1  O  LEU F6163   N  ALA D4036           
SHEET    1   I 2 TYR D4086  THR D4087  0                                        
SHEET    2   I 2 VAL D4094  CYS D4095 -1  O  CYS D4095   N  TYR D4086           
SHEET    1   J 4 TYR D4176  THR D4181  0                                        
SHEET    2   J 4 SER D4218  HIS D4223 -1  O  TRP D4219   N  PHE D4180           
SHEET    3   J 4 THR D4118  GLY D4122 -1  O  CYS D4119   N  ILE D4222           
SHEET    4   J 4 LEU D4274  VAL D4275 -1  O  VAL D4275   N  ILE D4120           
SHEET    1   K 2 THR E5004  TYR E5008  0                                        
SHEET    2   K 2 LEU E5014  ASP E5020 -1  N  LEU E5015   O  ILE E5007           
SHEET    1   L 4 ASN E5099  VAL E5103  0                                        
SHEET    2   L 4 SER E5108  GLN E5112 -1  O  SER E5108   N  VAL E5103           
SHEET    3   L 4 SER E5042  ASN E5046 -1  O  VAL E5043   N  ILE E5111           
SHEET    4   L 4 VAL E5172  GLN E5173 -1  O  GLN E5173   N  ALA E5044           
SHEET    1   M 2 ILE E5279  THR E5284  0                                        
SHEET    2   M 2 ASN E5290  ALA E5294 -1  O  PHE E5291   N  ASP E5282           
SHEET    1   N 4 ASP F6114  THR F6117  0                                        
SHEET    2   N 4 GLN F6122  ARG F6127 -1  O  ILE F6123   N  GLY F6116           
SHEET    3   N 4 VAL F6083  ASP F6090 -1  O  ARG F6084   N  ALA F6126           
SHEET    4   N 4 ALA F6149  VAL F6151 -1  O  GLY F6150   N  ALA F6089           
SHEET    1   O 3 ARG F6176  GLU F6179  0                                        
SHEET    2   O 3 THR F6182  LYS F6187 -1  O  THR F6182   N  GLU F6179           
SHEET    3   O 3 PRO F6193  ASP F6199 -1  N  LEU F6194   O  ASP F6186           
LINK         C   LYS A1270                 N   MHS A1271     1555   1555  1.33  
LINK         C   MHS A1271                 N   ALA A1272     1555   1555  1.33  
LINK         C   ARG A1284                 N   AGM A1285     1555   1555  1.33  
LINK         C   AGM A1285                 N   ALA A1286     1555   1555  1.33  
LINK         C   PHE A1464                 N   GL3 A1465     1555   1555  1.33  
LINK         C   GL3 A1465                 N   PHE A1466     1555   1555  1.33  
LINK         C   GLN A1471                 N   SMC A1472     1555   1555  1.33  
LINK         C   SMC A1472                 N   GLY A1473     1555   1555  1.33  
LINK        NI   F43 A2570                 OE1 GLN A1161     1555   1555  2.28  
LINK        NI   F43 A2570                 S1  COM D5572     1555   1555  2.54  
LINK         C   ALA C3064                 N   OCS C3065     1555   1555  1.33  
LINK         C   OCS C3065                 N   SER C3066     1555   1555  1.33  
LINK         C   LYS D4270                 N   MHS D4271     1555   1555  1.33  
LINK         C   MHS D4271                 N   ALA D4272     1555   1555  1.33  
LINK         C   ARG D4284                 N   AGM D4285     1555   1555  1.33  
LINK         C   AGM D4285                 N   ALA D4286     1555   1555  1.33  
LINK         C   PHE D4464                 N   GL3 D4465     1555   1555  1.33  
LINK         C   GL3 D4465                 N   PHE D4466     1555   1555  1.33  
LINK         C   GLN D4471                 N   SMC D4472     1555   1555  1.33  
LINK         C   SMC D4472                 N   GLY D4473     1555   1555  1.33  
LINK        NI   F43 D5570                 S1  COM A2572     1555   1555  2.51  
LINK        NI   F43 D5570                 OE1 GLN D4161     1555   1555  2.25  
LINK         C   ALA F6064                 N   OCS F6065     1555   1555  1.33  
LINK         C   OCS F6065                 N   SER F6066     1555   1555  1.33  
CISPEP   1 TYR B 2161    PRO B 2162          0        15.79                     
CISPEP   2 TYR E 5161    PRO E 5162          0        18.36                     
SITE     1 AC1 38 ALA A1158  VAL A1159  VAL A1160  GLN A1161                    
SITE     2 AC1 38 GLN A1244  MET A1247  ALA A1257  HOH A2224                    
SITE     3 AC1 38 HOH A2477  HOH A2478  HOH A2479  HOH A2480                    
SITE     4 AC1 38 HOH A2481  HOH D2427  GLY D4339  GLY D4340                    
SITE     5 AC1 38 VAL D4341  GLY D4342  PHE D4343  THR D4344                    
SITE     6 AC1 38 GLN D4345  TYR D4346  PHE D4416  GLY D4417                    
SITE     7 AC1 38 GLY D4462  PHE D4463  COM D5572  SER E5363                    
SITE     8 AC1 38 ILE E5364  TYR E5365  LEU F6118  SER F6119                    
SITE     9 AC1 38 GLY F6120  ALA F6154  THR F6155  VAL F6156                    
SITE    10 AC1 38 HIS F6157  HIS F6159                                          
SITE     1 AC2 23 ARG A1284  LEU A1333  MET A1337  SER A1338                    
SITE     2 AC2 23 PHE A1343  PHE A1463  MET A1500  ASN A1501                    
SITE     3 AC2 23 VAL A1502  HOH A2275  HOH A2482  HOH A2483                    
SITE     4 AC2 23 HOH A2484  HOH A2485  HOH A2486  PHE B2360                    
SITE     5 AC2 23 TYR B2365  GLY B2367  HIS B2377  VAL B2378                    
SITE     6 AC2 23 ARG D4239  LYS D4270  MHS D4271                               
SITE     1 AC3  9 TYR A1346  PHE A1463  PHE A1464  HOH A2487                    
SITE     2 AC3  9 PHE B2359  TYR B2365  LEU C3118  ARG C3121                    
SITE     3 AC3  9 F43 D5570                                                     
SITE     1 AC4 38 GLY A1339  GLY A1340  VAL A1341  GLY A1342                    
SITE     2 AC4 38 PHE A1343  THR A1344  GLN A1345  TYR A1346                    
SITE     3 AC4 38 PHE A1416  GLY A1417  GLY A1462  PHE A1463                    
SITE     4 AC4 38 HOH A2353  COM A2572  SER B2363  ILE B2364                    
SITE     5 AC4 38 TYR B2365  LEU C3118  SER C3119  GLY C3120                    
SITE     6 AC4 38 ALA C3154  THR C3155  VAL C3156  HIS C3157                    
SITE     7 AC4 38 HIS C3159  HOH D2285  HOH D2511  HOH D2512                    
SITE     8 AC4 38 HOH D2513  HOH D2514  HOH D2515  ALA D4158                    
SITE     9 AC4 38 VAL D4159  VAL D4160  GLN D4161  GLN D4244                    
SITE    10 AC4 38 MET D4247  ALA D4257                                          
SITE     1 AC5 22 ARG A1239  LYS A1270  MHS A1271  HOH D2366                    
SITE     2 AC5 22 HOH D2461  HOH D2517  HOH D2518  HOH D2519                    
SITE     3 AC5 22 HOH D2520  ARG D4284  LEU D4333  MET D4337                    
SITE     4 AC5 22 SER D4338  PHE D4463  MET D4500  ASN D4501                    
SITE     5 AC5 22 VAL D4502  PHE E5360  TYR E5365  GLY E5367                    
SITE     6 AC5 22 HIS E5377  VAL E5378                                          
SITE     1 AC6  9 F43 A2570  HOH D2521  TYR D4346  PHE D4463                    
SITE     2 AC6  9 PHE D4464  PHE E5359  TYR E5365  LEU F6118                    
SITE     3 AC6  9 ARG F6121                                                     
SITE     1 AC7  8 LYS A1379  LYS A1382  THR A1437  GLY A1438                    
SITE     2 AC7  8 ARG A1519  HOH A2362  HOH A2488  GLY E5068                    
SITE     1 AC8  8 MHS A1271  LEU A1274  VAL A1275  SER A1276                    
SITE     2 AC8  8 GLU A1279  HOH A2489  LYS E5062  MET E5168                    
SITE     1 AC9  8 GLY B2068  ARG B2069  HOH D2522  LYS D4379                    
SITE     2 AC9  8 LYS D4382  THR D4437  GLY D4438  ARG D4519                    
CRYST1  113.678  153.099  153.288  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      0.008797  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006532  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006524        0.00000                         
MTRIX1   1 -0.997000  0.002100 -0.077900      117.32380    1                    
MTRIX2   1  0.000000 -0.999700 -0.023900      154.28999    1                    
MTRIX3   1 -0.078000 -0.023800  0.996700        6.43030    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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