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Database: PDB
Entry: 3KOX
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Original site: 3KOX 
HEADER    METAL BINDING PROTEIN                   14-NOV-09   3KOX              
TITLE     CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH 2,4-   
TITLE    2 DIAMINOBUTYRATE (ANAEROBIC)                                          
CAVEAT     3KOX    B12 A 1801 HAS WRONG CHIRALITY AT ATOM C19 5AD A 1500 HAS    
CAVEAT   2 3KOX    WRONG CHIRALITY AT ATOM C2' B12 B 1801 HAS WRONG CHIRALITY   
CAVEAT   3 3KOX    AT ATOM C19 B12 C 1801 HAS WRONG CHIRALITY AT ATOM C19 5AD   
CAVEAT   4 3KOX    D 1500 HAS WRONG CHIRALITY AT ATOM C2'                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ORNITHINE AMINOMUTASE E COMPONENT;                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: D-ORNITHINE AMINOMUTASE S COMPONENT;                       
COMPND   7 CHAIN: E, F, G, H;                                                   
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM STICKLANDII;                        
SOURCE   3 ORGANISM_TAXID: 1511;                                                
SOURCE   4 GENE: ORAE;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE STRATAGENE;                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET23D;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: CLOSTRIDIUM STICKLANDII;                        
SOURCE  12 ORGANISM_TAXID: 1511;                                                
SOURCE  13 GENE: ORAS;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE STRATAGENE;                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET23D                                    
KEYWDS    D-ORNITHINE 4, 5 AMINOMUTASE (OAM), 2, 4-DIAMINOBUTYRATE (DAB)        
KEYWDS   2 COMPLEX, ANAEROBIC, METAL BINDING PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.WOLTHERS,C.W.LEVY,N.S.SCRUTTON,D.LEYS                             
REVDAT   4   29-JAN-20 3KOX    1       CAVEAT REMARK SEQADV                     
REVDAT   3   24-OCT-12 3KOX    1       FORMUL VERSN                             
REVDAT   2   12-MAY-10 3KOX    1       JRNL                                     
REVDAT   1   26-JAN-10 3KOX    0                                                
JRNL        AUTH   K.R.WOLTHERS,C.LEVY,N.S.SCRUTTON,D.LEYS                      
JRNL        TITL   LARGE-SCALE DOMAIN DYNAMICS AND ADENOSYLCOBALAMIN            
JRNL        TITL 2 REORIENTATION ORCHESTRATE RADICAL CATALYSIS IN ORNITHINE     
JRNL        TITL 3 4,5-AMINOMUTASE.                                             
JRNL        REF    J.BIOL.CHEM.                  V. 285 13942 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20106986                                                     
JRNL        DOI    10.1074/JBC.M109.068908                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 133606                         
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 + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7055                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9888                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 519                          
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 26064                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 528                                     
REMARK   3   SOLVENT ATOMS            : 787                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.25000                                              
REMARK   3    B33 (A**2) : -0.37000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.24000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.498         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.285         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.212         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.088         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 27124 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 18386 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 36800 ; 1.795 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44788 ; 0.988 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3332 ; 6.746 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1203 ;38.835 ;24.298       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4722 ;17.637 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   191 ;17.906 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4121 ; 0.185 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 29991 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5292 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 16656 ; 0.666 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6804 ; 0.137 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 26807 ; 1.245 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 10468 ; 2.030 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9993 ; 3.281 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056263.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133606                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: A PROTEIN SOLUTION (8 MG/ML 4,5-OAM, 5   
REMARK 280  MM 2-MERCAPTOETHANOL, 10 MM TRIS HCL PH 8.0, 2 MM PLP, AND 2 MM     
REMARK 280  ADOCBL) WAS MIXED IN A 1:1 RATIO WITH PRECIPITANT SOLUTION [(0.1    
REMARK 280  M TRIS HCL, PH 8.0, 0.2 M MGCL2, 25% (WT/VOL) POLYETHYLENE          
REMARK 280  GLYCOL 2000 MONO-METHYLETHER] UNDER REDLIGHT AT ROOM TEMPERATURE,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      115.84500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 29700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, C, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 29980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, D, H                            
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 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     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     GLU A   588                                                      
REMARK 465     PRO A   589                                                      
REMARK 465     GLU A   590                                                      
REMARK 465     GLU A   741                                                      
REMARK 465     GLY A   742                                                      
REMARK 465     LYS A   743                                                      
REMARK 465     SER A   744                                                      
REMARK 465     GLU A   745                                                      
REMARK 465     ASP A   746                                                      
REMARK 465     PRO A   747                                                      
REMARK 465     ASN A   748                                                      
REMARK 465     SER A   749                                                      
REMARK 465     SER A   750                                                      
REMARK 465     SER A   751                                                      
REMARK 465     VAL A   752                                                      
REMARK 465     ASP A   753                                                      
REMARK 465     LYS A   754                                                      
REMARK 465     LEU A   755                                                      
REMARK 465     ALA A   756                                                      
REMARK 465     ALA A   757                                                      
REMARK 465     ALA A   758                                                      
REMARK 465     LEU A   759                                                      
REMARK 465     GLU A   760                                                      
REMARK 465     HIS A   761                                                      
REMARK 465     HIS A   762                                                      
REMARK 465     HIS A   763                                                      
REMARK 465     HIS A   764                                                      
REMARK 465     HIS A   765                                                      
REMARK 465     HIS A   766                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ASP E     5                                                      
REMARK 465     ILE E   115                                                      
REMARK 465     PHE E   116                                                      
REMARK 465     LYS E   117                                                      
REMARK 465     GLY E   118                                                      
REMARK 465     GLY E   119                                                      
REMARK 465     VAL E   120                                                      
REMARK 465     LYS E   121                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     GLU B   588                                                      
REMARK 465     PRO B   589                                                      
REMARK 465     GLU B   590                                                      
REMARK 465     GLU B   741                                                      
REMARK 465     GLY B   742                                                      
REMARK 465     LYS B   743                                                      
REMARK 465     SER B   744                                                      
REMARK 465     GLU B   745                                                      
REMARK 465     ASP B   746                                                      
REMARK 465     PRO B   747                                                      
REMARK 465     ASN B   748                                                      
REMARK 465     SER B   749                                                      
REMARK 465     SER B   750                                                      
REMARK 465     SER B   751                                                      
REMARK 465     VAL B   752                                                      
REMARK 465     ASP B   753                                                      
REMARK 465     LYS B   754                                                      
REMARK 465     LEU B   755                                                      
REMARK 465     ALA B   756                                                      
REMARK 465     ALA B   757                                                      
REMARK 465     ALA B   758                                                      
REMARK 465     LEU B   759                                                      
REMARK 465     GLU B   760                                                      
REMARK 465     HIS B   761                                                      
REMARK 465     HIS B   762                                                      
REMARK 465     HIS B   763                                                      
REMARK 465     HIS B   764                                                      
REMARK 465     HIS B   765                                                      
REMARK 465     HIS B   766                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     ASP F     5                                                      
REMARK 465     ILE F   115                                                      
REMARK 465     PHE F   116                                                      
REMARK 465     LYS F   117                                                      
REMARK 465     GLY F   118                                                      
REMARK 465     GLY F   119                                                      
REMARK 465     VAL F   120                                                      
REMARK 465     LYS F   121                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     HIS C   507                                                      
REMARK 465     SER C   508                                                      
REMARK 465     GLU C   588                                                      
REMARK 465     PRO C   589                                                      
REMARK 465     GLU C   590                                                      
REMARK 465     GLU C   741                                                      
REMARK 465     GLY C   742                                                      
REMARK 465     LYS C   743                                                      
REMARK 465     SER C   744                                                      
REMARK 465     GLU C   745                                                      
REMARK 465     ASP C   746                                                      
REMARK 465     PRO C   747                                                      
REMARK 465     ASN C   748                                                      
REMARK 465     SER C   749                                                      
REMARK 465     SER C   750                                                      
REMARK 465     SER C   751                                                      
REMARK 465     VAL C   752                                                      
REMARK 465     ASP C   753                                                      
REMARK 465     LYS C   754                                                      
REMARK 465     LEU C   755                                                      
REMARK 465     ALA C   756                                                      
REMARK 465     ALA C   757                                                      
REMARK 465     ALA C   758                                                      
REMARK 465     LEU C   759                                                      
REMARK 465     GLU C   760                                                      
REMARK 465     HIS C   761                                                      
REMARK 465     HIS C   762                                                      
REMARK 465     HIS C   763                                                      
REMARK 465     HIS C   764                                                      
REMARK 465     HIS C   765                                                      
REMARK 465     HIS C   766                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LYS G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     ALA G     4                                                      
REMARK 465     ASP G     5                                                      
REMARK 465     ILE G   115                                                      
REMARK 465     PHE G   116                                                      
REMARK 465     LYS G   117                                                      
REMARK 465     GLY G   118                                                      
REMARK 465     GLY G   119                                                      
REMARK 465     VAL G   120                                                      
REMARK 465     LYS G   121                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     HIS D   507                                                      
REMARK 465     SER D   508                                                      
REMARK 465     GLU D   588                                                      
REMARK 465     PRO D   589                                                      
REMARK 465     GLU D   590                                                      
REMARK 465     GLU D   741                                                      
REMARK 465     GLY D   742                                                      
REMARK 465     LYS D   743                                                      
REMARK 465     SER D   744                                                      
REMARK 465     GLU D   745                                                      
REMARK 465     ASP D   746                                                      
REMARK 465     PRO D   747                                                      
REMARK 465     ASN D   748                                                      
REMARK 465     SER D   749                                                      
REMARK 465     SER D   750                                                      
REMARK 465     SER D   751                                                      
REMARK 465     VAL D   752                                                      
REMARK 465     ASP D   753                                                      
REMARK 465     LYS D   754                                                      
REMARK 465     LEU D   755                                                      
REMARK 465     ALA D   756                                                      
REMARK 465     ALA D   757                                                      
REMARK 465     ALA D   758                                                      
REMARK 465     LEU D   759                                                      
REMARK 465     GLU D   760                                                      
REMARK 465     HIS D   761                                                      
REMARK 465     HIS D   762                                                      
REMARK 465     HIS D   763                                                      
REMARK 465     HIS D   764                                                      
REMARK 465     HIS D   765                                                      
REMARK 465     HIS D   766                                                      
REMARK 465     MET H     1                                                      
REMARK 465     LYS H     2                                                      
REMARK 465     ARG H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     ASP H     5                                                      
REMARK 465     ILE H   115                                                      
REMARK 465     PHE H   116                                                      
REMARK 465     LYS H   117                                                      
REMARK 465     GLY H   118                                                      
REMARK 465     GLY H   119                                                      
REMARK 465     VAL H   120                                                      
REMARK 465     LYS H   121                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  39    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  75    CG   CD1  CD2                                       
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 503    CG   CD   CE   NZ                                   
REMARK 470     GLU A 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 594    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 596    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 599    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 603    CG   CD   CE   NZ                                   
REMARK 470     GLU A 658    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 659    CG   CD1  CD2                                       
REMARK 470     LYS A 660    CG   CD   CE   NZ                                   
REMARK 470     ILE A 692    CG1  CG2  CD1                                       
REMARK 470     LYS A 695    CG   CD   CE   NZ                                   
REMARK 470     ARG A 740    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  87    CG   CD   CE   NZ                                   
REMARK 470     ASP E 110    CG   OD1  OD2                                       
REMARK 470     GLU B 374    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 462    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 491    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 503    CG   CD   CE   NZ                                   
REMARK 470     GLU B 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 594    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 596    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 599    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 740    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F  87    CG   CD   CE   NZ                                   
REMARK 470     GLU C 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 292    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 374    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 442    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 491    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 501    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 503    CG   CD   CE   NZ                                   
REMARK 470     GLU C 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 594    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 596    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 599    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 682    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 740    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  87    CG   CD   CE   NZ                                   
REMARK 470     ASP G 110    CG   OD1  OD2                                       
REMARK 470     LYS D 503    CG   CD   CE   NZ                                   
REMARK 470     GLU D 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 550    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 551    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 594    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 596    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 599    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 602    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 658    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 738    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 740    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H  87    CG   CD   CE   NZ                                   
REMARK 470     ASP H 110    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU C   240     NE2  GLN C   244              2.07            
REMARK 500   O    THR B   123     NH2  ARG B   498              2.12            
REMARK 500   NZ   LYS B   629     C4A  Z98 D   767              2.14            
REMARK 500   O    SER C   723     O8R  B12 C  1801              2.16            
REMARK 500   OE1  GLU D   233     NZ   LYS D   236              2.16            
REMARK 500   OG1  THR D   449     OE2  GLU D   478              2.16            
REMARK 500   OD2  ASP C   202     OG   SER G    48              2.16            
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 B  92   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 498   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 498   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG C 382   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 498   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 498   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG D 498   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG D 498   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 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    GLN A   6     -143.12    129.05                                   
REMARK 500    LEU A   7      109.69     67.60                                   
REMARK 500    ASN A  40       60.89     39.72                                   
REMARK 500    ALA A  83       90.63   -175.27                                   
REMARK 500    ASP A 117       49.69    -75.92                                   
REMARK 500    SER A 159     -149.19   -141.57                                   
REMARK 500    TYR A 304       73.64   -108.03                                   
REMARK 500    THR A 326      -98.25   -120.41                                   
REMARK 500    ARG A 327      137.41   -170.12                                   
REMARK 500    PRO A 447       57.51    -94.58                                   
REMARK 500    ASP A 461       83.08   -159.22                                   
REMARK 500    GLU A 462      -55.84    -10.76                                   
REMARK 500    VAL A 479       78.54   -117.74                                   
REMARK 500    ASP A 487      -86.52    -71.67                                   
REMARK 500    ASP A 493       79.75   -104.13                                   
REMARK 500    GLU A 516      -40.16   -139.04                                   
REMARK 500    PRO A 530       58.37    -69.05                                   
REMARK 500    PRO A 575       31.02    -87.29                                   
REMARK 500    HIS A 618       99.99    -64.58                                   
REMARK 500    LYS A 660       75.10     70.60                                   
REMARK 500    GLU A 689      -36.65    -38.06                                   
REMARK 500    MET A 739      -77.64    -78.41                                   
REMARK 500    ASN E  93       37.45     31.69                                   
REMARK 500    TYR E 108        5.69     84.48                                   
REMARK 500    GLN B   6     -144.78     82.78                                   
REMARK 500    LEU B   7      108.51     46.28                                   
REMARK 500    ASP B  69       38.90     34.07                                   
REMARK 500    ASP B  71       59.88   -142.44                                   
REMARK 500    ALA B  83       88.19   -169.56                                   
REMARK 500    ASP B 117       49.13    -84.44                                   
REMARK 500    SER B 159     -157.00   -142.48                                   
REMARK 500    ASP B 184      110.16   -160.26                                   
REMARK 500    THR B 326      -98.56   -131.83                                   
REMARK 500    PRO B 447       57.46    -97.06                                   
REMARK 500    ASP B 461      115.42   -170.20                                   
REMARK 500    GLU B 467       52.13   -141.12                                   
REMARK 500    LEU B 471      -36.70    -36.31                                   
REMARK 500    GLU B 516      -33.40   -135.13                                   
REMARK 500    PRO B 586     -171.19    -69.88                                   
REMARK 500    THR B 668       85.97   -155.81                                   
REMARK 500    ASP B 673       16.70     82.40                                   
REMARK 500    GLU B 689       27.05    -61.76                                   
REMARK 500    LYS B 712        2.04    -69.34                                   
REMARK 500    ARG B 721      137.10    -35.88                                   
REMARK 500    GLU B 738       67.57    -69.29                                   
REMARK 500    MET B 739      -32.67    176.46                                   
REMARK 500    ALA F  15      -45.69    -28.57                                   
REMARK 500    GLN C   6     -102.10    174.57                                   
REMARK 500    LEU C   7      111.42     66.73                                   
REMARK 500    ALA C  83       81.54   -172.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      84 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN B    6     LEU B    7                 -140.61                    
REMARK 500 GLN D    6     LEU D    7                 -131.20                    
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 B 803        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH F 984        DISTANCE =  7.26 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                             B12 C1801  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 618   NE2                                                    
REMARK 620 2 B12 C1801   N21  89.9                                              
REMARK 620 3 B12 C1801   N22  88.3  90.4                                        
REMARK 620 4 B12 C1801   N23  88.0 177.9  89.7                                  
REMARK 620 5 B12 C1801   N24  90.1  88.1 177.8  91.6                            
REMARK 620 6 5AD A1500   C5' 173.6  95.9  88.9  86.2  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 B1801  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 618   NE2                                                    
REMARK 620 2 B12 B1801   N21  90.3                                              
REMARK 620 3 B12 B1801   N22  82.5  90.6                                        
REMARK 620 4 B12 B1801   N23  87.6 177.8  89.7                                  
REMARK 620 5 B12 B1801   N24  95.7  88.0 177.6  91.7                            
REMARK 620 6 5AD D1500   C5' 170.9  91.7  88.7  90.5  93.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 A1801  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 618   NE2                                                    
REMARK 620 2 B12 A1801   N21  84.9                                              
REMARK 620 3 B12 A1801   N22  94.1  90.0                                        
REMARK 620 4 B12 A1801   N23  96.3 177.8  91.8                                  
REMARK 620 5 B12 A1801   N24  84.7  87.9 177.6  90.4                            
REMARK 620 6 5AD C1500   C5' 172.6  93.5  78.7  85.6 102.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 D1801  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 618   NE2                                                    
REMARK 620 2 B12 D1801   N21  79.5                                              
REMARK 620 3 B12 D1801   N22  78.2  89.6                                        
REMARK 620 4 B12 D1801   N23  99.4 178.5  91.1                                  
REMARK 620 5 B12 D1801   N24 100.2  89.3 178.2  90.0                            
REMARK 620 6 5AD B1500   C5' 168.1  91.6  94.0  89.6  87.4                      
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 B12 A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD A 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z98 A 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD B 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 B 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z98 B 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD C 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 C 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z98 C 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 D 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD D 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z98 D 767                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KOW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE BACKSOAKED COMPLEX    
REMARK 900 RELATED ID: 3KOY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH       
REMARK 900 ORNITHINE (AEROBIC)                                                  
REMARK 900 RELATED ID: 3KOZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH       
REMARK 900 ORNITHINE (ANAEROBIC)                                                
REMARK 900 RELATED ID: 3KP0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH 2,4-  
REMARK 900 DIAMINOBUTYRATE (DAB) (AEROBIC)                                      
REMARK 900 RELATED ID: 3KP1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE (RESTING STATE)       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE STRUCTURE DOES NOT CONTAIN RESIDUES GLY220 TO ASP222 OF ORAE     
REMARK 999 PRESENT IN THE UNP SEQUENCE. WE DO NOT FIND ANY EVIDENCE FOR THESE   
REMARK 999 RESIDUES FROM CLOSTRIDIUM STICKLANDII GENOMIC DNA SEQUENCING OR BY   
REMARK 999 ALIGNMENT BETWEEN THE ORAE PROTEIN SEQUENCES FROM CLOSTRIDIUM        
REMARK 999 STICKLANDII AND CLOSTRIDIUM DIFFICILE (ACCESSION NUMBER ZP_05349629; 
REMARK 999 79% SEQUENCE IDENTITY) WHICH ALSO SHOWS THAT THE CORRESPONDING       
REMARK 999 ORAE CODING SEQUENCE FROM THE LATTER ORGANISM ALSO DOES NOT CONTAIN  
REMARK 999 THE THREE AMINO ACID GID INSERT (A SIMILAR CONCLUSION CAN BE         
REMARK 999 REACHED BY ALIGNMENT WITH VARIOUS THERMOANAEROBACTER SP)             
DBREF  3KOX A    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KOX E    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KOX B    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KOX F    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KOX C    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KOX G    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KOX D    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KOX H    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
SEQADV 3KOX     A       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KOX     A       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KOX     A       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KOX SER A  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU A  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP A  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX PRO A  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASN A  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER A  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER A  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER A  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX VAL A  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP A  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LYS A  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU A  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA A  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA A  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA A  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU A  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU A  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS A  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX     B       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KOX     B       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KOX     B       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KOX SER B  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU B  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP B  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX PRO B  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASN B  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER B  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER B  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER B  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX VAL B  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP B  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LYS B  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU B  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA B  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA B  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA B  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU B  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU B  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS B  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX     C       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KOX     C       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KOX     C       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KOX SER C  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU C  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP C  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX PRO C  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASN C  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER C  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER C  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER C  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX VAL C  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP C  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LYS C  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU C  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA C  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA C  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA C  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU C  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU C  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS C  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX     D       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KOX     D       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KOX     D       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KOX SER D  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU D  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP D  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX PRO D  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASN D  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER D  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER D  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX SER D  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX VAL D  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ASP D  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LYS D  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU D  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA D  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA D  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX ALA D  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX LEU D  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX GLU D  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KOX HIS D  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQRES   1 A  763  MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU          
SEQRES   2 A  763  ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR          
SEQRES   3 A  763  PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU          
SEQRES   4 A  763  ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER          
SEQRES   5 A  763  THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS          
SEQRES   6 A  763  TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE          
SEQRES   7 A  763  THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE          
SEQRES   8 A  763  ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS          
SEQRES   9 A  763  ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP          
SEQRES  10 A  763  GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL          
SEQRES  11 A  763  PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA          
SEQRES  12 A  763  LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN          
SEQRES  13 A  763  TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE          
SEQRES  14 A  763  ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS          
SEQRES  15 A  763  GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN          
SEQRES  16 A  763  MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR          
SEQRES  17 A  763  ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA          
SEQRES  18 A  763  HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL          
SEQRES  19 A  763  MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE          
SEQRES  20 A  763  PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS          
SEQRES  21 A  763  LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER          
SEQRES  22 A  763  MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU          
SEQRES  23 A  763  MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR          
SEQRES  24 A  763  LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR          
SEQRES  25 A  763  HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA          
SEQRES  26 A  763  ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN          
SEQRES  27 A  763  VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR          
SEQRES  28 A  763  ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP          
SEQRES  29 A  763  MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR          
SEQRES  30 A  763  VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU          
SEQRES  31 A  763  GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU          
SEQRES  32 A  763  GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG          
SEQRES  33 A  763  ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE          
SEQRES  34 A  763  GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET          
SEQRES  35 A  763  ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS          
SEQRES  36 A  763  GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU          
SEQRES  37 A  763  ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL          
SEQRES  38 A  763  TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL          
SEQRES  39 A  763  ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET          
SEQRES  40 A  763  ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL          
SEQRES  41 A  763  LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA          
SEQRES  42 A  763  GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU          
SEQRES  43 A  763  GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU          
SEQRES  44 A  763  ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO          
SEQRES  45 A  763  PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU          
SEQRES  46 A  763  PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE          
SEQRES  47 A  763  GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY          
SEQRES  48 A  763  GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP          
SEQRES  49 A  763  ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL          
SEQRES  50 A  763  HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL          
SEQRES  51 A  763  ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA          
SEQRES  52 A  763  SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN          
SEQRES  53 A  763  MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE          
SEQRES  54 A  763  ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL          
SEQRES  55 A  763  THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY          
SEQRES  56 A  763  PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE          
SEQRES  57 A  763  LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER          
SEQRES  58 A  763  GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA          
SEQRES  59 A  763  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 E  121  MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS          
SEQRES   2 E  121  LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE          
SEQRES   3 E  121  TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP          
SEQRES   4 E  121  LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER          
SEQRES   5 E  121  VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS          
SEQRES   6 E  121  ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY          
SEQRES   7 E  121  LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU          
SEQRES   8 E  121  LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER          
SEQRES   9 E  121  GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS          
SEQRES  10 E  121  GLY GLY VAL LYS                                              
SEQRES   1 B  763  MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU          
SEQRES   2 B  763  ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR          
SEQRES   3 B  763  PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU          
SEQRES   4 B  763  ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER          
SEQRES   5 B  763  THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS          
SEQRES   6 B  763  TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE          
SEQRES   7 B  763  THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE          
SEQRES   8 B  763  ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS          
SEQRES   9 B  763  ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP          
SEQRES  10 B  763  GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL          
SEQRES  11 B  763  PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA          
SEQRES  12 B  763  LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN          
SEQRES  13 B  763  TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE          
SEQRES  14 B  763  ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS          
SEQRES  15 B  763  GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN          
SEQRES  16 B  763  MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR          
SEQRES  17 B  763  ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA          
SEQRES  18 B  763  HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL          
SEQRES  19 B  763  MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE          
SEQRES  20 B  763  PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS          
SEQRES  21 B  763  LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER          
SEQRES  22 B  763  MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU          
SEQRES  23 B  763  MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR          
SEQRES  24 B  763  LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR          
SEQRES  25 B  763  HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA          
SEQRES  26 B  763  ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN          
SEQRES  27 B  763  VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR          
SEQRES  28 B  763  ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP          
SEQRES  29 B  763  MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR          
SEQRES  30 B  763  VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU          
SEQRES  31 B  763  GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU          
SEQRES  32 B  763  GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG          
SEQRES  33 B  763  ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE          
SEQRES  34 B  763  GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET          
SEQRES  35 B  763  ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS          
SEQRES  36 B  763  GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU          
SEQRES  37 B  763  ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL          
SEQRES  38 B  763  TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL          
SEQRES  39 B  763  ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET          
SEQRES  40 B  763  ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL          
SEQRES  41 B  763  LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA          
SEQRES  42 B  763  GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU          
SEQRES  43 B  763  GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU          
SEQRES  44 B  763  ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO          
SEQRES  45 B  763  PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU          
SEQRES  46 B  763  PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE          
SEQRES  47 B  763  GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY          
SEQRES  48 B  763  GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP          
SEQRES  49 B  763  ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL          
SEQRES  50 B  763  HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL          
SEQRES  51 B  763  ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA          
SEQRES  52 B  763  SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN          
SEQRES  53 B  763  MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE          
SEQRES  54 B  763  ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL          
SEQRES  55 B  763  THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY          
SEQRES  56 B  763  PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE          
SEQRES  57 B  763  LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER          
SEQRES  58 B  763  GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA          
SEQRES  59 B  763  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 F  121  MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS          
SEQRES   2 F  121  LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE          
SEQRES   3 F  121  TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP          
SEQRES   4 F  121  LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER          
SEQRES   5 F  121  VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS          
SEQRES   6 F  121  ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY          
SEQRES   7 F  121  LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU          
SEQRES   8 F  121  LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER          
SEQRES   9 F  121  GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS          
SEQRES  10 F  121  GLY GLY VAL LYS                                              
SEQRES   1 C  763  MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU          
SEQRES   2 C  763  ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR          
SEQRES   3 C  763  PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU          
SEQRES   4 C  763  ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER          
SEQRES   5 C  763  THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS          
SEQRES   6 C  763  TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE          
SEQRES   7 C  763  THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE          
SEQRES   8 C  763  ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS          
SEQRES   9 C  763  ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP          
SEQRES  10 C  763  GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL          
SEQRES  11 C  763  PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA          
SEQRES  12 C  763  LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN          
SEQRES  13 C  763  TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE          
SEQRES  14 C  763  ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS          
SEQRES  15 C  763  GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN          
SEQRES  16 C  763  MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR          
SEQRES  17 C  763  ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA          
SEQRES  18 C  763  HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL          
SEQRES  19 C  763  MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE          
SEQRES  20 C  763  PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS          
SEQRES  21 C  763  LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER          
SEQRES  22 C  763  MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU          
SEQRES  23 C  763  MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR          
SEQRES  24 C  763  LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR          
SEQRES  25 C  763  HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA          
SEQRES  26 C  763  ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN          
SEQRES  27 C  763  VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR          
SEQRES  28 C  763  ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP          
SEQRES  29 C  763  MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR          
SEQRES  30 C  763  VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU          
SEQRES  31 C  763  GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU          
SEQRES  32 C  763  GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG          
SEQRES  33 C  763  ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE          
SEQRES  34 C  763  GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET          
SEQRES  35 C  763  ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS          
SEQRES  36 C  763  GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU          
SEQRES  37 C  763  ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL          
SEQRES  38 C  763  TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL          
SEQRES  39 C  763  ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET          
SEQRES  40 C  763  ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL          
SEQRES  41 C  763  LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA          
SEQRES  42 C  763  GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU          
SEQRES  43 C  763  GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU          
SEQRES  44 C  763  ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO          
SEQRES  45 C  763  PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU          
SEQRES  46 C  763  PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE          
SEQRES  47 C  763  GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY          
SEQRES  48 C  763  GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP          
SEQRES  49 C  763  ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL          
SEQRES  50 C  763  HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL          
SEQRES  51 C  763  ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA          
SEQRES  52 C  763  SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN          
SEQRES  53 C  763  MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE          
SEQRES  54 C  763  ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL          
SEQRES  55 C  763  THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY          
SEQRES  56 C  763  PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE          
SEQRES  57 C  763  LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER          
SEQRES  58 C  763  GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA          
SEQRES  59 C  763  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 G  121  MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS          
SEQRES   2 G  121  LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE          
SEQRES   3 G  121  TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP          
SEQRES   4 G  121  LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER          
SEQRES   5 G  121  VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS          
SEQRES   6 G  121  ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY          
SEQRES   7 G  121  LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU          
SEQRES   8 G  121  LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER          
SEQRES   9 G  121  GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS          
SEQRES  10 G  121  GLY GLY VAL LYS                                              
SEQRES   1 D  763  MET GLU LYS ASP LEU GLN LEU ARG VAL ASN GLU LYS LEU          
SEQRES   2 D  763  ASP VAL GLU ASN ILE LEU LYS ASP LEU ASP LYS TYR THR          
SEQRES   3 D  763  PRO LYS ARG ARG GLY TRP THR TRP ARG GLN PRO ALA GLU          
SEQRES   4 D  763  ASN LEU GLN MET GLY PRO PHE ILE TYR LYS ASP ALA SER          
SEQRES   5 D  763  THR PRO LEU GLU ASN SER VAL ALA LEU PRO SER ALA LYS          
SEQRES   6 D  763  TYR PHE GLY ASP ILE ASP PRO GLN PRO LEU PRO VAL ILE          
SEQRES   7 D  763  THR THR GLU ILE ALA SER GLY ARG PHE GLU ASP ASP ILE          
SEQRES   8 D  763  ARG ARG MET ARG MET ALA ALA TRP HIS GLY ALA ASP HIS          
SEQRES   9 D  763  ILE MET VAL ILE ARG THR ALA GLY GLN SER HIS TYR ASP          
SEQRES  10 D  763  GLY LEU ILE GLU GLY THR PRO GLN GLY ILE GLY GLY VAL          
SEQRES  11 D  763  PRO ILE THR ARG LYS GLN VAL ARG ALA GLN ARG LYS ALA          
SEQRES  12 D  763  LEU ASP LEU ILE GLU GLU GLU VAL GLY ARG PRO ILE ASN          
SEQRES  13 D  763  TYR HIS SER TYR VAL SER GLY VAL ALA GLY PRO ASP ILE          
SEQRES  14 D  763  ALA VAL MET PHE ALA GLU GLU GLY VAL ASN GLY ALA HIS          
SEQRES  15 D  763  GLN ASP PRO GLN TYR ASN VAL LEU TYR ARG ASN ILE ASN          
SEQRES  16 D  763  MET ILE ARG SER PHE ILE ASP ALA CYS GLU SER LYS THR          
SEQRES  17 D  763  ILE MET ALA TRP ALA ASP MET ALA GLN ILE ASP GLY ALA          
SEQRES  18 D  763  HIS ASN ALA ASN ALA THR ALA ARG GLU ALA TRP LYS VAL          
SEQRES  19 D  763  MET PRO GLU LEU MET VAL GLN HIS ALA LEU ASN SER ILE          
SEQRES  20 D  763  PHE SER LEU LYS VAL GLY MET LYS LYS SER ASN ILE CYS          
SEQRES  21 D  763  LEU SER THR VAL PRO PRO THR ALA PRO PRO ALA PRO SER          
SEQRES  22 D  763  MET TYR LEU ASP LEU PRO TYR ALA VAL ALA LEU ARG GLU          
SEQRES  23 D  763  MET PHE GLU GLY TYR ARG MET ARG ALA GLN MET ASN THR          
SEQRES  24 D  763  LYS TYR MET GLU ALA SER THR ARG GLU ALA THR VAL THR          
SEQRES  25 D  763  HIS VAL LEU ASN LEU LEU ILE SER LYS LEU THR ARG ALA          
SEQRES  26 D  763  ASP ILE GLN SER THR ILE THR PRO ASP GLU GLY ARG ASN          
SEQRES  27 D  763  VAL PRO TRP HIS ILE TYR ASN ILE GLU ALA CYS ASP THR          
SEQRES  28 D  763  ALA LYS GLN ALA LEU ILE GLY MET ASP GLY LEU MET ASP          
SEQRES  29 D  763  MET VAL GLN LEU LYS ARG GLU GLY VAL LEU GLY ASP THR          
SEQRES  30 D  763  VAL ARG GLU LEU LYS GLU ARG ALA VAL LEU PHE MET GLU          
SEQRES  31 D  763  GLU ILE ILE GLU ALA GLY GLY TYR PHE ASN ALA VAL GLU          
SEQRES  32 D  763  GLN GLY PHE PHE VAL ASP SER GLY TYR TYR PRO GLU ARG          
SEQRES  33 D  763  ASN GLY ASP GLY ILE ALA ARG GLN ILE ASN GLY GLY ILE          
SEQRES  34 D  763  GLY ALA GLY THR VAL PHE GLU ARG ASP GLU ASP TYR MET          
SEQRES  35 D  763  ALA PRO VAL THR ALA HIS PHE GLY TYR ASN ASN VAL LYS          
SEQRES  36 D  763  GLN TYR ASP GLU ALA LEU VAL SER GLU PRO SER LYS LEU          
SEQRES  37 D  763  ILE ASP GLY CYS THR LEU GLU VAL PRO GLU LYS ILE VAL          
SEQRES  38 D  763  TYR ILE ASP GLU LEU ASP GLU ASN ASP ASN VAL ASN VAL          
SEQRES  39 D  763  ARG MET GLU GLU THR LYS GLU PHE ARG HIS SER SER MET          
SEQRES  40 D  763  ILE LYS PRO GLU VAL GLU TRP GLN ALA ASP GLY THR VAL          
SEQRES  41 D  763  LEU LEU THR MET PHE LEU PRO THR SER LYS ARG VAL ALA          
SEQRES  42 D  763  GLU PHE ALA ALA ILE GLU PHE ALA LYS LYS MET ASN LEU          
SEQRES  43 D  763  GLU GLU VAL GLU VAL ILE ASN ARG GLU VAL MET GLN GLU          
SEQRES  44 D  763  ALA GLU GLY THR ARG ILE GLU LEU LYS GLY ARG VAL PRO          
SEQRES  45 D  763  PHE SER ILE ASP ILE ASN SER LEU VAL ILE PRO PRO GLU          
SEQRES  46 D  763  PRO GLU ILE LEU SER GLU ASP GLU ILE ARG GLU ASP ILE          
SEQRES  47 D  763  GLU LYS THR PRO LEU LYS ILE VAL ALA ALA THR VAL GLY          
SEQRES  48 D  763  GLU ASP GLU HIS SER VAL GLY LEU ARG GLU VAL ILE ASP          
SEQRES  49 D  763  ILE LYS HIS GLY GLY ILE GLU LYS TYR GLY VAL GLU VAL          
SEQRES  50 D  763  HIS TYR LEU GLY THR SER VAL PRO VAL GLU LYS LEU VAL          
SEQRES  51 D  763  ASP ALA ALA ILE GLU LEU LYS ALA ASP ALA ILE LEU ALA          
SEQRES  52 D  763  SER THR ILE ILE SER HIS ASP ASP ILE HIS TYR LYS ASN          
SEQRES  53 D  763  MET LYS ARG ILE HIS GLU LEU ALA VAL GLU LYS GLY ILE          
SEQRES  54 D  763  ARG ASP LYS ILE MET ILE GLY CYS GLY GLY THR GLN VAL          
SEQRES  55 D  763  THR PRO GLU VAL ALA VAL LYS GLN GLY VAL ASP ALA GLY          
SEQRES  56 D  763  PHE GLY ARG GLY SER LYS GLY ILE HIS VAL ALA THR PHE          
SEQRES  57 D  763  LEU VAL LYS LYS ARG ARG GLU MET ARG GLU GLY LYS SER          
SEQRES  58 D  763  GLU ASP PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA          
SEQRES  59 D  763  ALA LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 H  121  MET LYS ARG ALA ASP ASP PHE GLN GLN ARG ARG ALA HIS          
SEQRES   2 H  121  LEU ALA ASN LEU SER ASP GLU GLU LEU GLN THR ARG PHE          
SEQRES   3 H  121  TRP GLU MET ALA GLU LYS ILE VAL ASP PRO LEU LEU ASP          
SEQRES   4 H  121  LEU GLY LYS LYS ASN THR THR PRO SER ILE GLU ARG SER          
SEQRES   5 H  121  VAL LEU LEU ARG MET GLY PHE SER SER LEU GLU ALA LYS          
SEQRES   6 H  121  ALA ILE VAL ASP LYS THR MET ASP ARG GLY LEU MET GLY          
SEQRES   7 H  121  LYS GLY ALA GLY HIS ILE VAL TYR LYS ILE ALA LYS GLU          
SEQRES   8 H  121  LYS ASN ILE SER VAL ARG GLU ALA GLY LEU ALA LEU SER          
SEQRES   9 H  121  GLU GLY LYS TYR TRP ASP ASP ALA ILE GLN ILE PHE LYS          
SEQRES  10 H  121  GLY GLY VAL LYS                                              
HET    B12  A1801      91                                                       
HET    5AD  A1500      18                                                       
HET    Z98  A 767      23                                                       
HET    5AD  B1500      18                                                       
HET    B12  B1801      91                                                       
HET    Z98  B 767      23                                                       
HET    5AD  C1500      18                                                       
HET    B12  C1801      91                                                       
HET    Z98  C 767      23                                                       
HET    B12  D1801      91                                                       
HET    5AD  D1500      18                                                       
HET    Z98  D 767      23                                                       
HETNAM     B12 COBALAMIN                                                        
HETNAM     5AD 5'-DEOXYADENOSINE                                                
HETNAM     Z98 (2S)-2-AMINO-4-{[(1Z)-{3-HYDROXY-2-METHYL-5-                     
HETNAM   2 Z98  [(PHOSPHONOOXY)METHYL]PYRIDIN-4-                                
HETNAM   3 Z98  YL}METHYLIDENE]AMINO}BUTANOIC ACID                              
FORMUL   9  B12    4(C62 H89 CO N13 O14 P 2+)                                   
FORMUL  10  5AD    4(C10 H13 N5 O3)                                             
FORMUL  11  Z98    4(C12 H18 N3 O7 P)                                           
FORMUL  21  HOH   *787(H2 O)                                                    
HELIX    1   1 ASP A   14  LEU A   19  1                                   6    
HELIX    2   2 ASP A   21  TYR A   25  5                                   5    
HELIX    3   3 LEU A   61  GLY A   68  5                                   8    
HELIX    4   4 ARG A   86  HIS A  100  1                                  15    
HELIX    5   5 GLY A  112  TYR A  116  5                                   5    
HELIX    6   6 THR A  133  GLY A  152  1                                  20    
HELIX    7   7 ALA A  165  GLY A  177  1                                  13    
HELIX    8   8 ASP A  184  ASN A  193  1                                  10    
HELIX    9   9 ASN A  195  ALA A  213  1                                  19    
HELIX   10  10 ALA A  224  ALA A  231  1                                   8    
HELIX   11  11 GLU A  233  LYS A  236  5                                   4    
HELIX   12  12 VAL A  237  GLY A  256  1                                  20    
HELIX   13  13 LYS A  258  SER A  260  5                                   3    
HELIX   14  14 PRO A  275  PHE A  291  1                                  17    
HELIX   15  15 SER A  308  THR A  326  1                                  19    
HELIX   16  16 TRP A  344  MET A  362  1                                  19    
HELIX   17  17 GLY A  364  ASP A  367  5                                   4    
HELIX   18  18 GLY A  375  ALA A  398  1                                  24    
HELIX   19  19 GLY A  400  GLN A  407  1                                   8    
HELIX   20  20 VAL A  457  GLU A  462  1                                   6    
HELIX   21  21 ALA A  463  ASP A  473  5                                  11    
HELIX   22  22 VAL A  479  ILE A  483  5                                   5    
HELIX   23  23 ASN A  494  GLU A  501  1                                   8    
HELIX   24  24 SER A  532  MET A  547  1                                  16    
HELIX   25  25 ASN A  581  LEU A  583  5                                   3    
HELIX   26  26 SER A  593  THR A  604  1                                  12    
HELIX   27  27 SER A  619  VAL A  625  1                                   7    
HELIX   28  28 ASP A  627  GLY A  631  5                                   5    
HELIX   29  29 GLY A  632  GLY A  637  5                                   6    
HELIX   30  30 PRO A  648  LYS A  660  1                                  13    
HELIX   31  31 SER A  671  ASP A  673  5                                   3    
HELIX   32  32 ASP A  674  LYS A  690  1                                  17    
HELIX   33  33 THR A  706  GLN A  713  1                                   8    
HELIX   34  34 LYS A  724  ARG A  740  1                                  17    
HELIX   35  35 ASP E    6  ALA E   12  1                                   7    
HELIX   36  36 HIS E   13  LEU E   17  5                                   5    
HELIX   37  37 SER E   18  LYS E   43  1                                  26    
HELIX   38  38 THR E   46  MET E   57  1                                  12    
HELIX   39  39 SER E   60  ARG E   74  1                                  15    
HELIX   40  40 LEU E   76  LYS E   79  5                                   4    
HELIX   41  41 GLY E   80  GLU E   91  1                                  12    
HELIX   42  42 SER E   95  SER E  104  1                                  10    
HELIX   43  43 TYR E  108  GLN E  114  1                                   7    
HELIX   44  44 ASP B   14  LEU B   19  1                                   6    
HELIX   45  45 ASP B   21  TYR B   25  5                                   5    
HELIX   46  46 LEU B   61  GLY B   68  5                                   8    
HELIX   47  47 ARG B   86  HIS B  100  1                                  15    
HELIX   48  48 GLY B  112  TYR B  116  5                                   5    
HELIX   49  49 THR B  133  GLY B  152  1                                  20    
HELIX   50  50 ALA B  165  GLU B  176  1                                  12    
HELIX   51  51 ASP B  184  TYR B  191  1                                   8    
HELIX   52  52 ASN B  195  ALA B  213  1                                  19    
HELIX   53  53 ALA B  224  ALA B  231  1                                   8    
HELIX   54  54 GLU B  233  LYS B  236  5                                   4    
HELIX   55  55 VAL B  237  GLY B  256  1                                  20    
HELIX   56  56 LYS B  258  SER B  260  5                                   3    
HELIX   57  57 PRO B  275  PHE B  291  1                                  17    
HELIX   58  58 SER B  308  THR B  326  1                                  19    
HELIX   59  59 TRP B  344  MET B  362  1                                  19    
HELIX   60  60 GLY B  364  MET B  368  1                                   5    
HELIX   61  61 GLY B  375  ALA B  398  1                                  24    
HELIX   62  62 GLY B  400  GLN B  407  1                                   8    
HELIX   63  63 ASP B  461  VAL B  465  5                                   5    
HELIX   64  64 SER B  469  ASP B  473  5                                   5    
HELIX   65  65 VAL B  479  ILE B  483  5                                   5    
HELIX   66  66 ASN B  494  GLU B  501  1                                   8    
HELIX   67  67 THR B  502  ARG B  506  5                                   5    
HELIX   68  68 SER B  532  MET B  547  1                                  16    
HELIX   69  69 SER B  593  THR B  604  1                                  12    
HELIX   70  70 SER B  619  VAL B  625  1                                   7    
HELIX   71  71 ASP B  627  GLY B  631  5                                   5    
HELIX   72  72 GLY B  632  GLY B  637  5                                   6    
HELIX   73  73 PRO B  648  LYS B  660  1                                  13    
HELIX   74  74 SER B  671  ASP B  673  5                                   3    
HELIX   75  75 ASP B  674  GLU B  689  1                                  16    
HELIX   76  76 LYS B  690  ILE B  696  5                                   7    
HELIX   77  77 THR B  706  LYS B  712  1                                   7    
HELIX   78  78 LYS B  724  GLU B  738  1                                  15    
HELIX   79  79 ASP F    6  ARG F   11  1                                   6    
HELIX   80  80 ALA F   12  LEU F   14  5                                   3    
HELIX   81  81 SER F   18  LYS F   43  1                                  26    
HELIX   82  82 THR F   46  GLY F   58  1                                  13    
HELIX   83  83 SER F   60  ARG F   74  1                                  15    
HELIX   84  84 GLY F   75  LYS F   79  5                                   5    
HELIX   85  85 GLY F   80  LYS F   92  1                                  13    
HELIX   86  86 SER F   95  GLU F  105  1                                  11    
HELIX   87  87 TYR F  108  GLN F  114  1                                   7    
HELIX   88  88 ASP C   14  LYS C   20  1                                   7    
HELIX   89  89 ASP C   21  TYR C   25  5                                   5    
HELIX   90  90 LEU C   61  GLY C   68  5                                   8    
HELIX   91  91 ARG C   86  HIS C  100  1                                  15    
HELIX   92  92 GLY C  112  TYR C  116  5                                   5    
HELIX   93  93 THR C  133  GLY C  152  1                                  20    
HELIX   94  94 ALA C  165  GLU C  176  1                                  12    
HELIX   95  95 ASP C  184  ASN C  193  1                                  10    
HELIX   96  96 ASN C  195  ALA C  213  1                                  19    
HELIX   97  97 ALA C  224  THR C  230  1                                   7    
HELIX   98  98 GLU C  233  LYS C  236  5                                   4    
HELIX   99  99 VAL C  237  GLY C  256  1                                  20    
HELIX  100 100 LYS C  258  SER C  260  5                                   3    
HELIX  101 101 PRO C  275  PHE C  291  1                                  17    
HELIX  102 102 SER C  308  THR C  326  1                                  19    
HELIX  103 103 TRP C  344  MET C  362  1                                  19    
HELIX  104 104 ASP C  363  ASP C  367  5                                   5    
HELIX  105 105 GLY C  375  ALA C  398  1                                  24    
HELIX  106 106 GLY C  400  GLN C  407  1                                   8    
HELIX  107 107 ASP C  461  VAL C  465  5                                   5    
HELIX  108 108 GLU C  467  ASP C  473  5                                   7    
HELIX  109 109 VAL C  479  ILE C  483  5                                   5    
HELIX  110 110 ASN C  494  THR C  502  1                                   9    
HELIX  111 111 SER C  532  LYS C  546  1                                  15    
HELIX  112 112 SER C  593  THR C  604  1                                  12    
HELIX  113 113 SER C  619  VAL C  625  1                                   7    
HELIX  114 114 GLY C  632  GLY C  637  5                                   6    
HELIX  115 115 PRO C  648  LYS C  660  1                                  13    
HELIX  116 116 SER C  671  ASP C  673  5                                   3    
HELIX  117 117 ASP C  674  GLY C  691  1                                  18    
HELIX  118 118 THR C  706  LYS C  712  1                                   7    
HELIX  119 119 LYS C  724  ARG C  740  1                                  17    
HELIX  120 120 ASP G    6  ARG G   11  1                                   6    
HELIX  121 121 ARG G   11  ASN G   16  1                                   6    
HELIX  122 122 SER G   18  LYS G   43  1                                  26    
HELIX  123 123 THR G   46  ARG G   56  1                                  11    
HELIX  124 124 SER G   60  ARG G   74  1                                  15    
HELIX  125 125 LEU G   76  LYS G   79  5                                   4    
HELIX  126 126 GLY G   80  ASN G   93  1                                  14    
HELIX  127 127 SER G   95  SER G  104  1                                  10    
HELIX  128 128 TYR G  108  GLN G  114  1                                   7    
HELIX  129 129 ASP D   14  LEU D   19  1                                   6    
HELIX  130 130 ASP D   21  TYR D   25  5                                   5    
HELIX  131 131 LEU D   61  GLY D   68  5                                   8    
HELIX  132 132 ARG D   86  HIS D  100  1                                  15    
HELIX  133 133 GLY D  112  TYR D  116  5                                   5    
HELIX  134 134 THR D  133  GLY D  152  1                                  20    
HELIX  135 135 ALA D  165  GLY D  177  1                                  13    
HELIX  136 136 ASP D  184  TYR D  191  1                                   8    
HELIX  137 137 ASN D  195  ALA D  213  1                                  19    
HELIX  138 138 ALA D  224  ALA D  231  1                                   8    
HELIX  139 139 GLU D  233  LYS D  236  5                                   4    
HELIX  140 140 VAL D  237  GLY D  256  1                                  20    
HELIX  141 141 LYS D  258  SER D  260  5                                   3    
HELIX  142 142 PRO D  275  PHE D  291  1                                  17    
HELIX  143 143 SER D  308  THR D  326  1                                  19    
HELIX  144 144 TRP D  344  MET D  362  1                                  19    
HELIX  145 145 GLY D  364  ASP D  367  5                                   4    
HELIX  146 146 GLY D  375  ALA D  398  1                                  24    
HELIX  147 147 GLY D  400  GLN D  407  1                                   8    
HELIX  148 148 ASP D  461  ASP D  473  5                                  13    
HELIX  149 149 VAL D  479  ILE D  483  5                                   5    
HELIX  150 150 ASN D  494  THR D  502  1                                   9    
HELIX  151 151 LYS D  503  ARG D  506  5                                   4    
HELIX  152 152 SER D  532  MET D  547  1                                  16    
HELIX  153 153 ASN D  581  LEU D  583  5                                   3    
HELIX  154 154 SER D  593  THR D  604  1                                  12    
HELIX  155 155 SER D  619  VAL D  625  1                                   7    
HELIX  156 156 ILE D  626  GLY D  631  5                                   6    
HELIX  157 157 GLY D  632  GLY D  637  5                                   6    
HELIX  158 158 PRO D  648  LEU D  659  1                                  12    
HELIX  159 159 SER D  671  ASP D  673  5                                   3    
HELIX  160 160 ASP D  674  LYS D  690  1                                  17    
HELIX  161 161 ILE D  692  ILE D  696  5                                   5    
HELIX  162 162 THR D  706  VAL D  711  1                                   6    
HELIX  163 163 LYS D  724  ARG D  740  1                                  17    
HELIX  164 164 ASP H    6  ARG H   11  1                                   6    
HELIX  165 165 ALA H   12  ALA H   15  5                                   4    
HELIX  166 166 SER H   18  LYS H   43  1                                  26    
HELIX  167 167 THR H   46  GLY H   58  1                                  13    
HELIX  168 168 SER H   60  ARG H   74  1                                  15    
HELIX  169 169 LEU H   76  LYS H   79  5                                   4    
HELIX  170 170 GLY H   80  LYS H   92  1                                  13    
HELIX  171 171 SER H   95  GLU H  105  1                                  11    
HELIX  172 172 TYR H  108  GLN H  114  1                                   7    
SHEET    1   A 2 LEU A  41  MET A  43  0                                        
SHEET    2   A 2 PHE A  46  TYR A  48 -1  O  PHE A  46   N  MET A  43           
SHEET    1   B 2 ALA A  51  SER A  52  0                                        
SHEET    2   B 2 GLN A  73  PRO A  74 -1  O  GLN A  73   N  SER A  52           
SHEET    1   C 9 VAL A  77  GLU A  81  0                                        
SHEET    2   C 9 HIS A 104  MET A 106  1  O  HIS A 104   N  THR A  80           
SHEET    3   C 9 ASN A 156  TYR A 160  1  O  ASN A 156   N  ILE A 105           
SHEET    4   C 9 GLY A 180  HIS A 182  1  O  GLY A 180   N  TYR A 157           
SHEET    5   C 9 ALA A 216  ILE A 218  1  O  ALA A 216   N  ALA A 181           
SHEET    6   C 9 ILE A 262  THR A 266  1  O  CYS A 263   N  GLN A 217           
SHEET    7   C 9 ARG A 295  ALA A 298  1  O  ARG A 295   N  LEU A 264           
SHEET    8   C 9 ILE A 330  SER A 332  1  O  SER A 332   N  ALA A 298           
SHEET    9   C 9 VAL A  77  GLU A  81  1  N  VAL A  77   O  GLN A 331           
SHEET    1   D 2 VAL A 369  LEU A 371  0                                        
SHEET    2   D 2 VAL C 369  LEU C 371 -1  O  GLN C 370   N  GLN A 370           
SHEET    1   E 2 PHE A 438  GLU A 439  0                                        
SHEET    2   E 2 ASN E  44  THR E  45 -1  O  THR E  45   N  PHE A 438           
SHEET    1   F 2 MET A 510  ILE A 511  0                                        
SHEET    2   F 2 ILE A 578  ASP A 579 -1  O  ILE A 578   N  ILE A 511           
SHEET    1   G 6 GLU A 550  GLN A 561  0                                        
SHEET    2   G 6 GLY A 565  ARG A 573 -1  O  ARG A 573   N  GLU A 550           
SHEET    3   G 6 THR A 522  LEU A 529 -1  N  LEU A 525   O  LEU A 570           
SHEET    4   G 6 THR C 522  LEU C 529 -1  O  LEU C 524   N  THR A 526           
SHEET    5   G 6 GLY C 565  ARG C 573 -1  O  ILE C 568   N  MET C 527           
SHEET    6   G 6 GLU C 550  GLN C 561 -1  N  GLU C 558   O  ARG C 567           
SHEET    1   H 5 GLU A 639  VAL A 647  0                                        
SHEET    2   H 5 LYS A 607  VAL A 613  1  N  ILE A 608   O  GLU A 639           
SHEET    3   H 5 ALA A 663  THR A 668  1  O  ALA A 663   N  VAL A 609           
SHEET    4   H 5 MET A 697  GLY A 702  1  O  GLY A 701   N  ALA A 666           
SHEET    5   H 5 ALA A 717  PHE A 719  1  O  ALA A 717   N  CYS A 700           
SHEET    1   I 2 LEU B  41  MET B  43  0                                        
SHEET    2   I 2 PHE B  46  TYR B  48 -1  O  PHE B  46   N  MET B  43           
SHEET    1   J 2 ALA B  51  SER B  52  0                                        
SHEET    2   J 2 GLN B  73  PRO B  74 -1  O  GLN B  73   N  SER B  52           
SHEET    1   K 9 VAL B  77  GLU B  81  0                                        
SHEET    2   K 9 HIS B 104  MET B 106  1  O  MET B 106   N  THR B  80           
SHEET    3   K 9 ASN B 156  TYR B 160  1  O  ASN B 156   N  ILE B 105           
SHEET    4   K 9 GLY B 180  HIS B 182  1  O  GLY B 180   N  TYR B 157           
SHEET    5   K 9 ALA B 216  ILE B 218  1  O  ALA B 216   N  ALA B 181           
SHEET    6   K 9 ILE B 262  THR B 266  1  O  CYS B 263   N  GLN B 217           
SHEET    7   K 9 ARG B 295  ALA B 298  1  O  ARG B 295   N  LEU B 264           
SHEET    8   K 9 ILE B 330  GLN B 331  1  O  ILE B 330   N  ALA B 298           
SHEET    9   K 9 VAL B  77  GLU B  81  1  N  VAL B  77   O  GLN B 331           
SHEET    1   L 2 VAL B 369  LEU B 371  0                                        
SHEET    2   L 2 VAL D 369  LEU D 371 -1  O  GLN D 370   N  GLN B 370           
SHEET    1   M 2 PHE B 438  GLU B 439  0                                        
SHEET    2   M 2 ASN F  44  THR F  45 -1  O  THR F  45   N  PHE B 438           
SHEET    1   N 2 MET B 510  ILE B 511  0                                        
SHEET    2   N 2 ILE B 578  ASP B 579 -1  O  ILE B 578   N  ILE B 511           
SHEET    1   O 6 GLU B 550  GLN B 561  0                                        
SHEET    2   O 6 GLY B 565  ARG B 573 -1  O  ARG B 573   N  GLU B 550           
SHEET    3   O 6 THR B 522  LEU B 529 -1  N  LEU B 525   O  LEU B 570           
SHEET    4   O 6 THR D 522  LEU D 529 -1  O  THR D 526   N  LEU B 524           
SHEET    5   O 6 GLY D 565  ARG D 573 -1  O  LEU D 570   N  LEU D 525           
SHEET    6   O 6 GLU D 550  GLN D 561 -1  N  ASN D 556   O  GLU D 569           
SHEET    1   P 5 GLU B 639  VAL B 647  0                                        
SHEET    2   P 5 LYS B 607  VAL B 613  1  N  ALA B 610   O  LEU B 643           
SHEET    3   P 5 ALA B 663  SER B 667  1  O  LEU B 665   N  VAL B 609           
SHEET    4   P 5 MET B 697  GLY B 701  1  O  GLY B 699   N  ILE B 664           
SHEET    5   P 5 ALA B 717  PHE B 719  1  O  PHE B 719   N  CYS B 700           
SHEET    1   Q 2 LEU C  41  MET C  43  0                                        
SHEET    2   Q 2 PHE C  46  TYR C  48 -1  O  TYR C  48   N  LEU C  41           
SHEET    1   R 2 ALA C  51  SER C  52  0                                        
SHEET    2   R 2 GLN C  73  PRO C  74 -1  O  GLN C  73   N  SER C  52           
SHEET    1   S 9 VAL C  77  GLU C  81  0                                        
SHEET    2   S 9 HIS C 104  MET C 106  1  O  MET C 106   N  THR C  80           
SHEET    3   S 9 ASN C 156  TYR C 160  1  O  ASN C 156   N  ILE C 105           
SHEET    4   S 9 GLY C 180  HIS C 182  1  O  GLY C 180   N  TYR C 157           
SHEET    5   S 9 ALA C 216  ILE C 218  1  O  ALA C 216   N  ALA C 181           
SHEET    6   S 9 ILE C 262  THR C 266  1  O  CYS C 263   N  GLN C 217           
SHEET    7   S 9 ARG C 295  ALA C 298  1  O  ARG C 295   N  LEU C 264           
SHEET    8   S 9 ILE C 330  GLN C 331  1  O  ILE C 330   N  ALA C 298           
SHEET    9   S 9 VAL C  77  GLU C  81  1  N  VAL C  77   O  GLN C 331           
SHEET    1   T 2 PHE C 438  GLU C 439  0                                        
SHEET    2   T 2 ASN G  44  THR G  45 -1  O  THR G  45   N  PHE C 438           
SHEET    1   U 2 MET C 510  ILE C 511  0                                        
SHEET    2   U 2 ILE C 578  ASP C 579 -1  O  ILE C 578   N  ILE C 511           
SHEET    1   V 5 GLU C 639  TYR C 642  0                                        
SHEET    2   V 5 LYS C 607  THR C 612  1  N  ILE C 608   O  HIS C 641           
SHEET    3   V 5 ALA C 663  SER C 667  1  O  SER C 667   N  ALA C 611           
SHEET    4   V 5 MET C 697  GLY C 701  1  O  GLY C 699   N  ILE C 664           
SHEET    5   V 5 ALA C 717  PHE C 719  1  O  ALA C 717   N  CYS C 700           
SHEET    1   W 2 LEU D  41  MET D  43  0                                        
SHEET    2   W 2 PHE D  46  TYR D  48 -1  O  PHE D  46   N  MET D  43           
SHEET    1   X 2 ALA D  51  SER D  52  0                                        
SHEET    2   X 2 GLN D  73  PRO D  74 -1  O  GLN D  73   N  SER D  52           
SHEET    1   Y 9 VAL D  77  GLU D  81  0                                        
SHEET    2   Y 9 HIS D 104  MET D 106  1  O  MET D 106   N  THR D  80           
SHEET    3   Y 9 ASN D 156  TYR D 160  1  O  ASN D 156   N  ILE D 105           
SHEET    4   Y 9 GLY D 180  HIS D 182  1  O  GLY D 180   N  TYR D 157           
SHEET    5   Y 9 ALA D 216  ILE D 218  1  O  ALA D 216   N  ALA D 181           
SHEET    6   Y 9 ILE D 262  THR D 266  1  O  CYS D 263   N  GLN D 217           
SHEET    7   Y 9 ARG D 295  ALA D 298  1  O  ARG D 297   N  LEU D 264           
SHEET    8   Y 9 ILE D 330  GLN D 331  1  O  ILE D 330   N  ALA D 298           
SHEET    9   Y 9 VAL D  77  GLU D  81  1  N  VAL D  77   O  GLN D 331           
SHEET    1   Z 2 PHE D 438  GLU D 439  0                                        
SHEET    2   Z 2 ASN H  44  THR H  45 -1  O  THR H  45   N  PHE D 438           
SHEET    1  AA 2 MET D 510  ILE D 511  0                                        
SHEET    2  AA 2 ILE D 578  ASP D 579 -1  O  ILE D 578   N  ILE D 511           
SHEET    1  AB 5 GLU D 639  VAL D 647  0                                        
SHEET    2  AB 5 LYS D 607  VAL D 613  1  N  ALA D 610   O  LEU D 643           
SHEET    3  AB 5 ALA D 663  SER D 667  1  O  LEU D 665   N  VAL D 609           
SHEET    4  AB 5 MET D 697  GLY D 701  1  O  GLY D 699   N  ILE D 664           
SHEET    5  AB 5 ALA D 717  PHE D 719  1  O  PHE D 719   N  CYS D 700           
LINK         NE2 HIS C 618                CO   B12 C1801     1555   1555  2.01  
LINK         NE2 HIS B 618                CO   B12 B1801     1555   1555  2.18  
LINK         NE2 HIS A 618                CO   B12 A1801     1555   1555  2.18  
LINK         NE2 HIS D 618                CO   B12 D1801     1555   1555  2.41  
LINK        CO   B12 A1801                 C5' 5AD C1500     1555   1555  2.79  
LINK        CO   B12 B1801                 C5' 5AD D1500     1555   1555  2.39  
LINK        CO   B12 C1801                 C5' 5AD A1500     1555   1555  2.35  
LINK        CO   B12 D1801                 C5' 5AD B1500     1555   1555  2.17  
CISPEP   1 PRO A  272    PRO A  273          0         7.90                     
CISPEP   2 TYR A  416    PRO A  417          0         8.81                     
CISPEP   3 PRO B  272    PRO B  273          0         9.08                     
CISPEP   4 TYR B  416    PRO B  417          0         0.94                     
CISPEP   5 PRO C  272    PRO C  273          0         9.47                     
CISPEP   6 TYR C  416    PRO C  417          0         9.43                     
CISPEP   7 PRO D  272    PRO D  273          0         9.88                     
CISPEP   8 TYR D  416    PRO D  417          0         9.22                     
SITE     1 AC1 24 ASP A 616  GLU A 617  HIS A 618  SER A 619                    
SITE     2 AC1 24 VAL A 620  GLY A 621  ALA A 666  SER A 667                    
SITE     3 AC1 24 ILE A 669  ILE A 670  SER A 671  GLY A 701                    
SITE     4 AC1 24 GLY A 702  THR A 703  PHE A 719  GLY A 720                    
SITE     5 AC1 24 GLY A 722  SER A 723  VAL A 728  HOH A 852                    
SITE     6 AC1 24 TYR C 116  ASP C 490  ASP C 493  5AD C1500                    
SITE     1 AC2  5 LEU A 489  ASP A 490  HOH A 846  HOH A 921                    
SITE     2 AC2  5 B12 C1801                                                     
SITE     1 AC3 17 GLU A  81  ARG A 109  GLY A 112  GLN A 113                    
SITE     2 AC3 17 SER A 114  TYR A 160  SER A 162  HIS A 182                    
SITE     3 AC3 17 TYR A 187  ARG A 192  HIS A 225  ASN A 226                    
SITE     4 AC3 17 ARG A 297  GLN A 299  HOH A 886  HOH A 919                    
SITE     5 AC3 17 LYS C 629                                                     
SITE     1 AC4  3 LEU B 489  HOH B 786  B12 D1801                               
SITE     1 AC5 25 GLU B 615  GLU B 617  HIS B 618  SER B 619                    
SITE     2 AC5 25 VAL B 620  GLY B 621  LEU B 622  LEU B 665                    
SITE     3 AC5 25 ALA B 666  SER B 667  ILE B 670  SER B 671                    
SITE     4 AC5 25 HIS B 672  GLY B 701  GLY B 702  THR B 703                    
SITE     5 AC5 25 PHE B 719  GLY B 720  SER B 723  VAL B 728                    
SITE     6 AC5 25 HOH B 846  HOH B 945  TYR D 116  ASP D 490                    
SITE     7 AC5 25 5AD D1500                                                     
SITE     1 AC6 18 GLU B  81  ARG B 109  GLY B 112  GLN B 113                    
SITE     2 AC6 18 SER B 114  TYR B 160  SER B 162  HIS B 182                    
SITE     3 AC6 18 TYR B 187  ARG B 192  HIS B 225  ASN B 226                    
SITE     4 AC6 18 ARG B 297  GLN B 299  HOH B 776  HOH B 784                    
SITE     5 AC6 18 LYS D 629  HOH D 838                                          
SITE     1 AC7  2 B12 A1801  LEU C 489                                          
SITE     1 AC8 28 TYR A 116  ASP A 490  HOH A 877  5AD A1500                    
SITE     2 AC8 28 ASP C 616  GLU C 617  HIS C 618  SER C 619                    
SITE     3 AC8 28 VAL C 620  GLY C 621  VAL C 625  LEU C 665                    
SITE     4 AC8 28 ALA C 666  SER C 667  ILE C 669  ILE C 670                    
SITE     5 AC8 28 SER C 671  HIS C 672  GLY C 701  GLY C 702                    
SITE     6 AC8 28 THR C 703  PHE C 719  GLY C 720  SER C 723                    
SITE     7 AC8 28 VAL C 728  HOH C 768  HOH C 830  HOH C 888                    
SITE     1 AC9 16 LYS A 629  GLU C  81  ARG C 109  GLY C 112                    
SITE     2 AC9 16 GLN C 113  SER C 114  TYR C 160  SER C 162                    
SITE     3 AC9 16 HIS C 182  TYR C 187  ARG C 192  HIS C 225                    
SITE     4 AC9 16 ASN C 226  ARG C 297  GLN C 299  HOH C 899                    
SITE     1 BC1 27 HIS B 115  TYR B 116  ASP B 490  HOH B 912                    
SITE     2 BC1 27 5AD B1500  GLU D 615  ASP D 616  GLU D 617                    
SITE     3 BC1 27 HIS D 618  SER D 619  VAL D 620  GLY D 621                    
SITE     4 BC1 27 VAL D 625  ALA D 666  SER D 667  ILE D 669                    
SITE     5 BC1 27 ILE D 670  SER D 671  HIS D 672  GLY D 701                    
SITE     6 BC1 27 GLY D 702  THR D 703  PHE D 719  GLY D 720                    
SITE     7 BC1 27 SER D 723  VAL D 728  HOH D 787                               
SITE     1 BC2  4 B12 B1801  LEU D 489  HOH D 860  HOH D 865                    
SITE     1 BC3 17 LYS B 629  GLU D  81  ARG D 109  GLY D 112                    
SITE     2 BC3 17 GLN D 113  SER D 114  TYR D 160  SER D 162                    
SITE     3 BC3 17 HIS D 182  TYR D 187  ARG D 192  HIS D 225                    
SITE     4 BC3 17 ASN D 226  ARG D 297  GLN D 299  HOH D 785                    
SITE     5 BC3 17 HOH D 920                                                     
CRYST1   65.960  231.690  123.890  90.00 103.16  90.00 P 1 21 1      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      0.015161  0.000000  0.003545        0.00000                         
SCALE2      0.000000  0.004316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008289        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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