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Database: PDB
Entry: 3KP1
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Original site: 3KP1 
HEADER    METAL BINDING PROTEIN                   14-NOV-09   3KP1              
TITLE     CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE (RESTING STATE)        
CAVEAT     3KP1    B12 A 1801 HAS WRONG CHIRALITY AT ATOM C19 5AD A 767 HAS     
CAVEAT   2 3KP1    WRONG CHIRALITY AT ATOM C1' B12 B 1801 HAS WRONG CHIRALITY   
CAVEAT   3 3KP1    AT ATOM C19 5AD B 767 HAS WRONG CHIRALITY AT ATOM C1' B12 D  
CAVEAT   4 3KP1    1801 HAS WRONG CHIRALITY AT ATOM C19 5AD D 767 HAS WRONG     
CAVEAT   5 3KP1    CHIRALITY AT ATOM C1' 5AD C 767 HAS WRONG CHIRALITY AT ATOM  
CAVEAT   6 3KP1    C1'                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ORNITHINE AMINOMUTASE E COMPONENT;                       
COMPND   3 CHAIN: A, B, D, C;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: D-ORNITHINE AMINOMUTASE S COMPONENT;                       
COMPND   7 CHAIN: E, F, H, G;                                                   
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), METAL BINDING PROTEIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.WOLTHERS,C.W.LEVY,N.S.SCRUTTON,D.LEYS                             
REVDAT   5   30-OCT-19 3KP1    1       CAVEAT REMARK SEQADV                     
REVDAT   4   17-JUL-19 3KP1    1       REMARK LINK                              
REVDAT   3   24-OCT-12 3KP1    1       FORMUL VERSN                             
REVDAT   2   12-MAY-10 3KP1    1       JRNL                                     
REVDAT   1   26-JAN-10 3KP1    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.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 243030                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12199                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.7473 -  6.2399    0.98     7707   406  0.1497 0.1705        
REMARK   3     2  6.2399 -  4.9550    1.00     7730   466  0.1567 0.1998        
REMARK   3     3  4.9550 -  4.3293    1.00     7786   376  0.1312 0.1874        
REMARK   3     4  4.3293 -  3.9338    1.00     7707   418  0.1342 0.1732        
REMARK   3     5  3.9338 -  3.6520    1.00     7703   437  0.1416 0.1913        
REMARK   3     6  3.6520 -  3.4367    1.00     7792   376  0.1507 0.1743        
REMARK   3     7  3.4367 -  3.2647    1.00     7718   398  0.1584 0.2034        
REMARK   3     8  3.2647 -  3.1226    1.00     7716   423  0.1664 0.2147        
REMARK   3     9  3.1226 -  3.0024    1.00     7717   419  0.1715 0.2372        
REMARK   3    10  3.0024 -  2.8989    1.00     7657   442  0.1682 0.2223        
REMARK   3    11  2.8989 -  2.8082    1.00     7712   433  0.1738 0.2462        
REMARK   3    12  2.8082 -  2.7280    1.00     7769   411  0.1708 0.2283        
REMARK   3    13  2.7280 -  2.6562    1.00     7658   390  0.1734 0.2470        
REMARK   3    14  2.6562 -  2.5914    1.00     7802   387  0.1677 0.2333        
REMARK   3    15  2.5914 -  2.5325    1.00     7725   380  0.1645 0.2176        
REMARK   3    16  2.5325 -  2.4786    1.00     7731   420  0.1665 0.2390        
REMARK   3    17  2.4786 -  2.4290    1.00     7769   388  0.1689 0.2290        
REMARK   3    18  2.4290 -  2.3832    1.00     7699   373  0.1722 0.2398        
REMARK   3    19  2.3832 -  2.3406    1.00     7752   407  0.1729 0.2470        
REMARK   3    20  2.3406 -  2.3009    1.00     7667   401  0.1731 0.2492        
REMARK   3    21  2.3009 -  2.2638    1.00     7716   431  0.1743 0.2474        
REMARK   3    22  2.2638 -  2.2290    1.00     7643   441  0.1763 0.2377        
REMARK   3    23  2.2290 -  2.1962    1.00     7701   423  0.1727 0.2464        
REMARK   3    24  2.1962 -  2.1653    1.00     7752   385  0.1792 0.2294        
REMARK   3    25  2.1653 -  2.1360    1.00     7680   396  0.1831 0.2410        
REMARK   3    26  2.1360 -  2.1083    0.99     7714   403  0.1845 0.2497        
REMARK   3    27  2.1083 -  2.0819    0.99     7644   402  0.1927 0.2444        
REMARK   3    28  2.0819 -  2.0568    0.99     7753   405  0.1961 0.2578        
REMARK   3    29  2.0568 -  2.0329    0.99     7672   414  0.2144 0.2792        
REMARK   3    30  2.0329 -  2.0100    0.92     7039   348  0.2223 0.2895        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 46.38                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.32000                                             
REMARK   3    B22 (A**2) : 1.59000                                              
REMARK   3    B33 (A**2) : -1.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.85000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          27016                                  
REMARK   3   ANGLE     :  1.281          36647                                  
REMARK   3   CHIRALITY :  0.122           4097                                  
REMARK   3   PLANARITY :  0.005           4734                                  
REMARK   3   DIHEDRAL  : 19.229          10125                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KP1 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_1000056267.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 121.200                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
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 RED LIGHT AT ROOM               
REMARK 280  TEMPERATURE, 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      117.25500            
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: 30920 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.0 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: 31060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 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     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
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     LEU B     5                                                      
REMARK 465     GLN B     6                                                      
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 D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     LEU D     5                                                      
REMARK 465     GLN D     6                                                      
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 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     GLN C     6                                                      
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 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     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 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     GLU C 738    CG   CD   OE1  OE2                                  
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 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   O    HOH D  1019     O    HOH D  1719              2.09            
REMARK 500   O    HOH A  3058     O    HOH A  3163              2.18            
REMARK 500   O    HOH F   836     O    HOH F  3146              2.18            
REMARK 500   O    HOH D  1069     O    HOH H   122              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH F  3045     O    HOH D   834     1656     1.99            
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    ALA A  83       89.67   -163.34                                   
REMARK 500    SER A 159     -155.38   -146.74                                   
REMARK 500    TYR A 304       68.12   -106.36                                   
REMARK 500    GLU A 306     -153.37   -130.69                                   
REMARK 500    THR A 326      -97.72   -123.23                                   
REMARK 500    PRO A 447       46.30    -87.40                                   
REMARK 500    ASP A 493       79.78   -109.08                                   
REMARK 500    GLU A 516      -36.32   -143.66                                   
REMARK 500    PRO A 586      155.33    -47.67                                   
REMARK 500    HIS A 630       44.93   -106.10                                   
REMARK 500    ALA B  83       86.62   -162.67                                   
REMARK 500    SER B 159     -155.91   -147.62                                   
REMARK 500    TYR B 304       70.82   -105.63                                   
REMARK 500    GLU B 306     -150.87   -128.26                                   
REMARK 500    THR B 326     -100.30   -129.93                                   
REMARK 500    ASP B 461      101.87   -167.89                                   
REMARK 500    GLU B 516      -31.70   -149.95                                   
REMARK 500    GLU B 738       -2.53    -54.98                                   
REMARK 500    ALA D  83       88.16   -162.90                                   
REMARK 500    SER D 159     -155.97   -146.16                                   
REMARK 500    TYR D 304       67.44   -105.40                                   
REMARK 500    GLU D 306     -153.98   -130.11                                   
REMARK 500    THR D 326      -98.50   -124.66                                   
REMARK 500    ASP D 461      103.74   -163.09                                   
REMARK 500    GLU D 516      -37.22   -146.56                                   
REMARK 500    ALA C  83       93.35   -167.78                                   
REMARK 500    SER C 159     -153.75   -149.01                                   
REMARK 500    TYR C 304       67.25   -103.78                                   
REMARK 500    GLU C 306     -148.39   -130.57                                   
REMARK 500    THR C 326      -98.64   -124.68                                   
REMARK 500    PRO C 447       48.15    -79.34                                   
REMARK 500    ASP C 461      111.49   -176.66                                   
REMARK 500    ASP C 487      -76.86    -78.30                                   
REMARK 500    ASP C 493       79.87   -101.05                                   
REMARK 500    GLU C 516      -36.68   -148.30                                   
REMARK 500    PRO C 586      160.57    -49.16                                   
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 A2006        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH E2679        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH B1996        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B2684        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH B3088        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH B3104        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH F1017        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH F3214        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH D2224        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH D3223        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH D3225        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C 895        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C2676        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH C2830        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH C3098        DISTANCE =  6.18 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 5AD A 767   C5'                                                    
REMARK 620 2 B12 C1801   N21  98.9                                              
REMARK 620 3 B12 C1801   N22  99.9  87.7                                        
REMARK 620 4 B12 C1801   N23  83.1 174.5  97.1                                  
REMARK 620 5 B12 C1801   N24  93.1  83.3 165.1  91.5                            
REMARK 620 6 HIS C 618   NE2 177.5  80.5  82.5  97.3  84.4                      
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 5AD C 767   C5'                                                    
REMARK 620 2 B12 A1801   N21 100.7                                              
REMARK 620 3 B12 A1801   N22 102.6  86.5                                        
REMARK 620 4 B12 A1801   N23  81.0 175.7  97.1                                  
REMARK 620 5 B12 A1801   N24  95.6  84.0 160.7  91.9                            
REMARK 620 6 HIS A 618   NE2 172.9  82.7  83.8  95.2  78.4                      
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 5AD D 767   C5'                                                    
REMARK 620 2 B12 B1801   N21  99.6                                              
REMARK 620 3 B12 B1801   N22 101.4  87.3                                        
REMARK 620 4 B12 B1801   N23  83.3 175.2  95.8                                  
REMARK 620 5 B12 B1801   N24  92.7  82.8 164.0  93.3                            
REMARK 620 6 HIS B 618   NE2 174.9  83.1  83.0  93.7  83.3                      
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 5AD B 767   C5'                                                    
REMARK 620 2 B12 D1801   N21  97.2                                              
REMARK 620 3 B12 D1801   N22 101.4  86.2                                        
REMARK 620 4 B12 D1801   N23  85.0 175.3  97.5                                  
REMARK 620 5 B12 D1801   N24  95.2  83.7 161.5  92.0                            
REMARK 620 6 HIS D 618   NE2 175.4  79.3  75.6  98.7  87.3                      
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 PLP A 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD A 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1802                
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 5AD B 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 D 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD D 767                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B12 C 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD C 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: 3KOX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORNITHINE 4,5 AMINOMUTASE IN COMPLEX WITH 2,4-  
REMARK 900 DIAMINOBUTYRATE (ANAEROBIC)                                          
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 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  3KP1 A    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KP1 E    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KP1 B    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KP1 F    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KP1 D    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KP1 H    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
DBREF  3KP1 C    1   743  UNP    Q8VPJ5   Q8VPJ5_CLOST     1    743             
DBREF  3KP1 G    1   121  UNP    Q8VPJ6   Q8VPJ6_CLOST     1    121             
SEQADV 3KP1     A       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KP1     A       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KP1     A       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KP1 SER A  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU A  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP A  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 PRO A  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASN A  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER A  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER A  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER A  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 VAL A  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP A  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LYS A  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU A  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA A  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA A  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA A  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU A  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU A  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS A  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1     B       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KP1     B       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KP1     B       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KP1 SER B  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU B  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP B  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 PRO B  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASN B  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER B  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER B  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER B  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 VAL B  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP B  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LYS B  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU B  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA B  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA B  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA B  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU B  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU B  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS B  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1     D       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KP1     D       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KP1     D       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KP1 SER D  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU D  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP D  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 PRO D  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASN D  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER D  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER D  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER D  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 VAL D  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP D  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LYS D  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU D  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA D  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA D  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA D  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU D  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU D  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS D  766  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1     C       UNP  Q8VPJ5    ILE   218 SEE REMARK 999                 
SEQADV 3KP1     C       UNP  Q8VPJ5    ASP   219 SEE REMARK 999                 
SEQADV 3KP1     C       UNP  Q8VPJ5    GLY   220 SEE REMARK 999                 
SEQADV 3KP1 SER C  744  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU C  745  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP C  746  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 PRO C  747  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASN C  748  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER C  749  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER C  750  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 SER C  751  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 VAL C  752  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ASP C  753  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LYS C  754  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU C  755  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA C  756  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA C  757  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 ALA C  758  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 LEU C  759  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 GLU C  760  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  761  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  762  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  763  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  764  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  765  UNP  Q8VPJ5              EXPRESSION TAG                 
SEQADV 3KP1 HIS C  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 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                                              
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                                              
HET    PLP  A1802      15                                                       
HET    B12  A1801      91                                                       
HET    5AD  A 767      18                                                       
HET    PLP  B1802      15                                                       
HET    B12  B1801      91                                                       
HET    5AD  B 767      18                                                       
HET    PLP  D1802      15                                                       
HET    B12  D1801      91                                                       
HET    5AD  D 767      18                                                       
HET    PLP  C1802      15                                                       
HET    B12  C1801      91                                                       
HET    5AD  C 767      18                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     B12 COBALAMIN                                                        
HETNAM     5AD 5'-DEOXYADENOSINE                                                
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   9  PLP    4(C8 H10 N O6 P)                                             
FORMUL  10  B12    4(C62 H89 CO N13 O14 P 2+)                                   
FORMUL  11  5AD    4(C10 H13 N5 O3)                                             
FORMUL  21  HOH   *3137(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  VAL A  465  5                                   3    
HELIX   22  22 GLU A  467  ASP A  473  5                                   7    
HELIX   23  23 VAL A  479  ILE A  483  5                                   5    
HELIX   24  24 ASN A  494  THR A  502  1                                   9    
HELIX   25  25 LYS A  503  ARG A  506  5                                   4    
HELIX   26  26 SER A  532  MET A  547  1                                  16    
HELIX   27  27 ASN A  581  LEU A  583  5                                   3    
HELIX   28  28 SER A  593  THR A  604  1                                  12    
HELIX   29  29 SER A  619  VAL A  625  1                                   7    
HELIX   30  30 GLY A  632  GLY A  637  5                                   6    
HELIX   31  31 PRO A  648  LEU A  659  1                                  12    
HELIX   32  32 SER A  671  ASP A  673  5                                   3    
HELIX   33  33 ASP A  674  LYS A  690  1                                  17    
HELIX   34  34 THR A  706  LYS A  712  1                                   7    
HELIX   35  35 LYS A  724  ARG A  740  1                                  17    
HELIX   36  36 ASP E    6  ARG E   11  1                                   6    
HELIX   37  37 ALA E   12  ALA E   15  5                                   4    
HELIX   38  38 SER E   18  LYS E   43  1                                  26    
HELIX   39  39 THR E   46  MET E   57  1                                  12    
HELIX   40  40 SER E   60  ARG E   74  1                                  15    
HELIX   41  41 LEU E   76  LYS E   79  5                                   4    
HELIX   42  42 GLY E   80  LYS E   92  1                                  13    
HELIX   43  43 SER E   95  GLU E  105  1                                  11    
HELIX   44  44 TYR E  108  GLN E  114  1                                   7    
HELIX   45  45 ASP B   14  LEU B   19  1                                   6    
HELIX   46  46 ASP B   21  TYR B   25  5                                   5    
HELIX   47  47 LEU B   61  GLY B   68  5                                   8    
HELIX   48  48 ARG B   86  HIS B  100  1                                  15    
HELIX   49  49 GLY B  112  TYR B  116  5                                   5    
HELIX   50  50 THR B  133  GLY B  152  1                                  20    
HELIX   51  51 ALA B  165  GLU B  176  1                                  12    
HELIX   52  52 ASP B  184  TYR B  191  1                                   8    
HELIX   53  53 ASN B  195  ALA B  213  1                                  19    
HELIX   54  54 ALA B  224  ALA B  231  1                                   8    
HELIX   55  55 GLU B  233  LYS B  236  5                                   4    
HELIX   56  56 VAL B  237  GLY B  256  1                                  20    
HELIX   57  57 LYS B  258  SER B  260  5                                   3    
HELIX   58  58 PRO B  275  PHE B  291  1                                  17    
HELIX   59  59 SER B  308  THR B  326  1                                  19    
HELIX   60  60 TRP B  344  MET B  362  1                                  19    
HELIX   61  61 GLY B  364  ASP B  367  5                                   4    
HELIX   62  62 GLY B  375  ALA B  398  1                                  24    
HELIX   63  63 GLY B  400  GLN B  407  1                                   8    
HELIX   64  64 ASP B  461  VAL B  465  5                                   5    
HELIX   65  65 GLU B  467  ASP B  473  5                                   7    
HELIX   66  66 VAL B  479  ILE B  483  5                                   5    
HELIX   67  67 ASN B  494  LYS B  503  1                                  10    
HELIX   68  68 GLU B  504  ARG B  506  5                                   3    
HELIX   69  69 SER B  532  MET B  547  1                                  16    
HELIX   70  70 ASN B  581  LEU B  583  5                                   3    
HELIX   71  71 SER B  593  THR B  604  1                                  12    
HELIX   72  72 SER B  619  VAL B  625  1                                   7    
HELIX   73  73 GLY B  632  GLY B  637  5                                   6    
HELIX   74  74 PRO B  648  LEU B  659  1                                  12    
HELIX   75  75 SER B  671  ASP B  673  5                                   3    
HELIX   76  76 ASP B  674  LYS B  690  1                                  17    
HELIX   77  77 ILE B  692  ILE B  696  5                                   5    
HELIX   78  78 THR B  706  LYS B  712  1                                   7    
HELIX   79  79 LYS B  724  GLU B  738  1                                  15    
HELIX   80  80 ASP F    6  ARG F   11  1                                   6    
HELIX   81  81 ALA F   12  LEU F   14  5                                   3    
HELIX   82  82 SER F   18  LYS F   43  1                                  26    
HELIX   83  83 THR F   46  GLY F   58  1                                  13    
HELIX   84  84 SER F   60  ARG F   74  1                                  15    
HELIX   85  85 GLY F   75  LYS F   79  5                                   5    
HELIX   86  86 GLY F   80  ASN F   93  1                                  14    
HELIX   87  87 SER F   95  GLU F  105  1                                  11    
HELIX   88  88 TYR F  108  GLN F  114  1                                   7    
HELIX   89  89 ASP D   14  LEU D   19  1                                   6    
HELIX   90  90 ASP D   21  TYR D   25  5                                   5    
HELIX   91  91 LEU D   61  GLY D   68  5                                   8    
HELIX   92  92 ARG D   86  HIS D  100  1                                  15    
HELIX   93  93 GLY D  112  TYR D  116  5                                   5    
HELIX   94  94 THR D  133  GLY D  152  1                                  20    
HELIX   95  95 ALA D  165  GLU D  176  1                                  12    
HELIX   96  96 ASP D  184  ASN D  193  1                                  10    
HELIX   97  97 ASN D  195  ALA D  213  1                                  19    
HELIX   98  98 ALA D  224  ALA D  231  1                                   8    
HELIX   99  99 GLU D  233  LYS D  236  5                                   4    
HELIX  100 100 VAL D  237  GLY D  256  1                                  20    
HELIX  101 101 LYS D  258  SER D  260  5                                   3    
HELIX  102 102 PRO D  275  PHE D  291  1                                  17    
HELIX  103 103 SER D  308  THR D  326  1                                  19    
HELIX  104 104 TRP D  344  MET D  362  1                                  19    
HELIX  105 105 GLY D  364  ASP D  367  5                                   4    
HELIX  106 106 GLY D  375  ALA D  398  1                                  24    
HELIX  107 107 GLY D  400  GLN D  407  1                                   8    
HELIX  108 108 GLU D  467  ASP D  473  5                                   7    
HELIX  109 109 VAL D  479  ILE D  483  5                                   5    
HELIX  110 110 ASN D  494  THR D  502  1                                   9    
HELIX  111 111 LYS D  503  ARG D  506  5                                   4    
HELIX  112 112 SER D  532  MET D  547  1                                  16    
HELIX  113 113 ASN D  581  LEU D  583  5                                   3    
HELIX  114 114 SER D  593  THR D  604  1                                  12    
HELIX  115 115 SER D  619  VAL D  625  1                                   7    
HELIX  116 116 GLY D  632  GLY D  637  5                                   6    
HELIX  117 117 PRO D  648  LEU D  659  1                                  12    
HELIX  118 118 SER D  671  ASP D  673  5                                   3    
HELIX  119 119 ASP D  674  LYS D  690  1                                  17    
HELIX  120 120 ILE D  692  ILE D  696  5                                   5    
HELIX  121 121 THR D  706  GLN D  713  1                                   8    
HELIX  122 122 LYS D  724  ARG D  740  1                                  17    
HELIX  123 123 ASP H    6  ARG H   11  1                                   6    
HELIX  124 124 ALA H   12  ALA H   15  5                                   4    
HELIX  125 125 SER H   18  LYS H   43  1                                  26    
HELIX  126 126 THR H   46  MET H   57  1                                  12    
HELIX  127 127 SER H   60  ARG H   74  1                                  15    
HELIX  128 128 GLY H   75  LYS H   79  5                                   5    
HELIX  129 129 GLY H   80  LYS H   92  1                                  13    
HELIX  130 130 SER H   95  GLU H  105  1                                  11    
HELIX  131 131 TYR H  108  GLN H  114  1                                   7    
HELIX  132 132 ASP C   14  LEU C   19  1                                   6    
HELIX  133 133 ASP C   21  TYR C   25  5                                   5    
HELIX  134 134 LEU C   61  GLY C   68  5                                   8    
HELIX  135 135 ARG C   86  HIS C  100  1                                  15    
HELIX  136 136 GLY C  112  TYR C  116  5                                   5    
HELIX  137 137 THR C  133  GLY C  152  1                                  20    
HELIX  138 138 ALA C  165  GLY C  177  1                                  13    
HELIX  139 139 ASP C  184  ASN C  193  1                                  10    
HELIX  140 140 ASN C  195  ALA C  213  1                                  19    
HELIX  141 141 ALA C  224  ALA C  231  1                                   8    
HELIX  142 142 GLU C  233  LYS C  236  5                                   4    
HELIX  143 143 VAL C  237  GLY C  256  1                                  20    
HELIX  144 144 LYS C  258  SER C  260  5                                   3    
HELIX  145 145 PRO C  275  PHE C  291  1                                  17    
HELIX  146 146 SER C  308  THR C  326  1                                  19    
HELIX  147 147 TRP C  344  MET C  362  1                                  19    
HELIX  148 148 GLY C  364  ASP C  367  5                                   4    
HELIX  149 149 GLY C  375  ALA C  398  1                                  24    
HELIX  150 150 GLY C  400  GLN C  407  1                                   8    
HELIX  151 151 ASP C  461  ASP C  473  5                                  13    
HELIX  152 152 VAL C  479  ILE C  483  5                                   5    
HELIX  153 153 ASN C  494  LYS C  503  1                                  10    
HELIX  154 154 GLU C  504  ARG C  506  5                                   3    
HELIX  155 155 SER C  532  MET C  547  1                                  16    
HELIX  156 156 ASN C  581  LEU C  583  5                                   3    
HELIX  157 157 SER C  593  THR C  604  1                                  12    
HELIX  158 158 SER C  619  VAL C  625  1                                   7    
HELIX  159 159 GLY C  632  GLY C  637  5                                   6    
HELIX  160 160 PRO C  648  LEU C  659  1                                  12    
HELIX  161 161 SER C  671  ASP C  673  5                                   3    
HELIX  162 162 ASP C  674  LYS C  690  1                                  17    
HELIX  163 163 ILE C  692  ILE C  696  5                                   5    
HELIX  164 164 THR C  706  GLN C  713  1                                   8    
HELIX  165 165 LYS C  724  ARG C  740  1                                  17    
HELIX  166 166 ASP G    6  ARG G   11  1                                   6    
HELIX  167 167 ALA G   12  ALA G   15  5                                   4    
HELIX  168 168 SER G   18  LYS G   43  1                                  26    
HELIX  169 169 THR G   46  MET G   57  1                                  12    
HELIX  170 170 SER G   60  ARG G   74  1                                  15    
HELIX  171 171 LEU G   76  LYS G   79  5                                   4    
HELIX  172 172 GLY G   80  LYS G   92  1                                  13    
HELIX  173 173 SER G   95  GLU G  105  1                                  11    
HELIX  174 174 TYR G  108  GLN G  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  MET A 106   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  HIS A 182   N  SER A 159           
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 297   N  LEU A 264           
SHEET    8   C 9 ILE A 330  GLN A 331  1  O  ILE A 330   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 567   N  GLU A 558           
SHEET    3   G 6 THR A 522  LEU A 529 -1  N  MET A 527   O  ILE A 568           
SHEET    4   G 6 THR C 522  LEU C 529 -1  O  THR C 526   N  LEU A 524           
SHEET    5   G 6 GLY C 565  ARG C 573 -1  O  LEU C 570   N  LEU C 525           
SHEET    6   G 6 GLU C 550  GLN C 561 -1  N  GLU C 550   O  ARG C 573           
SHEET    1   H 5 GLU A 639  TYR A 642  0                                        
SHEET    2   H 5 LYS A 607  THR A 612  1  N  ILE A 608   O  HIS A 641           
SHEET    3   H 5 ALA A 663  SER A 667  1  O  LEU A 665   N  VAL A 609           
SHEET    4   H 5 MET A 697  GLY A 701  1  O  MET A 697   N  ILE A 664           
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  HIS B 182   N  SER B 159           
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 297   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 567   N  GLU B 558           
SHEET    3   O 6 THR B 522  LEU B 529 -1  N  MET B 527   O  ILE B 568           
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  GLU D 558   O  ARG D 567           
SHEET    1   P 5 GLU B 639  TYR B 642  0                                        
SHEET    2   P 5 LYS B 607  THR B 612  1  N  ILE B 608   O  GLU B 639           
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  ALA B 717   N  CYS B 700           
SHEET    1   Q 2 LEU D  41  MET D  43  0                                        
SHEET    2   Q 2 PHE D  46  TYR D  48 -1  O  TYR D  48   N  LEU D  41           
SHEET    1   R 2 ALA D  51  SER D  52  0                                        
SHEET    2   R 2 GLN D  73  PRO D  74 -1  O  GLN D  73   N  SER D  52           
SHEET    1   S 9 VAL D  77  GLU D  81  0                                        
SHEET    2   S 9 HIS D 104  MET D 106  1  O  MET D 106   N  THR D  80           
SHEET    3   S 9 ASN D 156  TYR D 160  1  O  ASN D 156   N  ILE D 105           
SHEET    4   S 9 GLY D 180  HIS D 182  1  O  HIS D 182   N  SER D 159           
SHEET    5   S 9 ALA D 216  ILE D 218  1  O  ALA D 216   N  ALA D 181           
SHEET    6   S 9 ILE D 262  THR D 266  1  O  CYS D 263   N  GLN D 217           
SHEET    7   S 9 ARG D 295  ALA D 298  1  O  ARG D 297   N  LEU D 264           
SHEET    8   S 9 ILE D 330  SER D 332  1  O  SER D 332   N  ALA D 298           
SHEET    9   S 9 VAL D  77  GLU D  81  1  N  VAL D  77   O  GLN D 331           
SHEET    1   T 2 PHE D 438  GLU D 439  0                                        
SHEET    2   T 2 ASN H  44  THR H  45 -1  O  THR H  45   N  PHE D 438           
SHEET    1   U 2 MET D 510  ILE D 511  0                                        
SHEET    2   U 2 ILE D 578  ASP D 579 -1  O  ILE D 578   N  ILE D 511           
SHEET    1   V 5 GLU D 639  TYR D 642  0                                        
SHEET    2   V 5 LYS D 607  THR D 612  1  N  ILE D 608   O  GLU D 639           
SHEET    3   V 5 ALA D 663  SER D 667  1  O  LEU D 665   N  VAL D 609           
SHEET    4   V 5 MET D 697  GLY D 701  1  O  GLY D 699   N  ILE D 664           
SHEET    5   V 5 ALA D 717  PHE D 719  1  O  ALA D 717   N  CYS D 700           
SHEET    1   W 2 LEU C  41  MET C  43  0                                        
SHEET    2   W 2 PHE C  46  TYR C  48 -1  O  TYR C  48   N  LEU C  41           
SHEET    1   X 2 ALA C  51  SER C  52  0                                        
SHEET    2   X 2 GLN C  73  PRO C  74 -1  O  GLN C  73   N  SER C  52           
SHEET    1   Y 9 VAL C  77  GLU C  81  0                                        
SHEET    2   Y 9 HIS C 104  MET C 106  1  O  MET C 106   N  THR C  80           
SHEET    3   Y 9 ASN C 156  TYR C 160  1  O  ASN C 156   N  ILE C 105           
SHEET    4   Y 9 GLY C 180  HIS C 182  1  O  HIS C 182   N  SER C 159           
SHEET    5   Y 9 ALA C 216  ILE C 218  1  O  ALA C 216   N  ALA C 181           
SHEET    6   Y 9 ILE C 262  THR C 266  1  O  CYS C 263   N  GLN C 217           
SHEET    7   Y 9 ARG C 295  ALA C 298  1  O  ARG C 297   N  LEU C 264           
SHEET    8   Y 9 ILE C 330  GLN C 331  1  O  ILE C 330   N  ALA C 298           
SHEET    9   Y 9 VAL C  77  GLU C  81  1  N  VAL C  77   O  GLN C 331           
SHEET    1   Z 2 PHE C 438  GLU C 439  0                                        
SHEET    2   Z 2 ASN G  44  THR G  45 -1  O  THR G  45   N  PHE C 438           
SHEET    1  AA 2 MET C 510  ILE C 511  0                                        
SHEET    2  AA 2 ILE C 578  ASP C 579 -1  O  ILE C 578   N  ILE C 511           
SHEET    1  AB 5 GLU C 639  TYR C 642  0                                        
SHEET    2  AB 5 LYS C 607  THR C 612  1  N  ILE C 608   O  HIS C 641           
SHEET    3  AB 5 ALA C 663  SER C 667  1  O  LEU C 665   N  VAL C 609           
SHEET    4  AB 5 MET C 697  GLY C 701  1  O  MET C 697   N  ILE C 664           
SHEET    5  AB 5 ALA C 717  PHE C 719  1  O  ALA C 717   N  CYS C 700           
LINK         C5' 5AD A 767                CO   B12 C1801     1555   1555  1.96  
LINK        CO   B12 A1801                 C5' 5AD C 767     1555   1555  1.98  
LINK        CO   B12 B1801                 C5' 5AD D 767     1555   1555  2.06  
LINK         NE2 HIS B 618                CO   B12 B1801     1555   1555  2.10  
LINK         NE2 HIS A 618                CO   B12 A1801     1555   1555  2.13  
LINK         C5' 5AD B 767                CO   B12 D1801     1555   1555  2.14  
LINK         NE2 HIS D 618                CO   B12 D1801     1555   1555  2.19  
LINK         NE2 HIS C 618                CO   B12 C1801     1555   1555  2.25  
LINK         NZ  LYS A 629                 C4A PLP A1802     1555   1555  1.45  
LINK         NZ  LYS B 629                 C4A PLP B1802     1555   1555  1.43  
LINK         NZ  LYS C 629                 C4A PLP C1802     1555   1555  1.42  
LINK         NZ  LYS D 629                 C4A PLP D1802     1555   1555  1.44  
CISPEP   1 PRO A  272    PRO A  273          0         6.47                     
CISPEP   2 TYR A  416    PRO A  417          0        10.89                     
CISPEP   3 PRO B  272    PRO B  273          0         7.36                     
CISPEP   4 TYR B  416    PRO B  417          0        12.85                     
CISPEP   5 PRO D  272    PRO D  273          0        12.99                     
CISPEP   6 TYR D  416    PRO D  417          0         8.45                     
CISPEP   7 PRO C  272    PRO C  273          0         9.91                     
CISPEP   8 TYR C  416    PRO C  417          0        11.66                     
SITE     1 AC1 13 LYS A 629  HOH A1661  ARG C 109  GLY C 112                    
SITE     2 AC1 13 GLN C 113  SER C 114  TYR C 160  SER C 162                    
SITE     3 AC1 13 TYR C 187  ARG C 192  HIS C 225  ASN C 226                    
SITE     4 AC1 13 HOH C 908                                                     
SITE     1 AC2 30 GLU A 617  HIS A 618  SER A 619  VAL A 620                    
SITE     2 AC2 30 GLY A 621  VAL A 625  ALA A 666  SER A 667                    
SITE     3 AC2 30 ILE A 669  ILE A 670  SER A 671  HIS A 672                    
SITE     4 AC2 30 GLY A 701  GLY A 702  THR A 703  PHE A 719                    
SITE     5 AC2 30 GLY A 720  SER A 723  VAL A 728  HOH A 912                    
SITE     6 AC2 30 HOH A 950  HOH A1297  HOH A2153  HOH A2982                    
SITE     7 AC2 30 HIS C 115  TYR C 116  ILE C 127  5AD C 767                    
SITE     8 AC2 30 HOH C1285  HOH C2766                                          
SITE     1 AC3  5 LEU A 489  HOH A 861  HOH A 923  HOH A1074                    
SITE     2 AC3  5 B12 C1801                                                     
SITE     1 AC4 14 LYS B 629  HIS B 630  HOH B 774  HOH B 967                    
SITE     2 AC4 14 ARG D 109  GLY D 112  GLN D 113  SER D 114                    
SITE     3 AC4 14 TYR D 160  SER D 162  TYR D 187  ARG D 192                    
SITE     4 AC4 14 HIS D 225  ASN D 226                                          
SITE     1 AC5 40 GLU B 615  GLU B 617  HIS B 618  SER B 619                    
SITE     2 AC5 40 VAL B 620  GLY B 621  VAL B 625  ALA B 666                    
SITE     3 AC5 40 SER B 667  ILE B 669  ILE B 670  SER B 671                    
SITE     4 AC5 40 HIS B 672  GLY B 701  GLY B 702  THR B 703                    
SITE     5 AC5 40 PHE B 719  GLY B 720  SER B 723  VAL B 728                    
SITE     6 AC5 40 HOH B 807  HOH B 850  HOH B 858  HOH B 943                    
SITE     7 AC5 40 HOH B 956  HOH B1004  HOH B1232  HOH B1883                    
SITE     8 AC5 40 HOH B1978  HOH B2337  HOH B2813  HOH B2819                    
SITE     9 AC5 40 HOH B3190  HIS D 115  TYR D 116  ASP D 490                    
SITE    10 AC5 40 5AD D 767  HOH D 856  HOH D 936  HOH D1594                    
SITE     1 AC6  5 LEU B 489  HOH B 781  HOH B 983  HOH B1019                    
SITE     2 AC6  5 B12 D1801                                                     
SITE     1 AC7 13 ARG B 109  GLY B 112  GLN B 113  SER B 114                    
SITE     2 AC7 13 TYR B 160  SER B 162  TYR B 187  ARG B 192                    
SITE     3 AC7 13 HIS B 225  ASN B 226  LYS D 629  HOH D 823                    
SITE     4 AC7 13 HOH D 844                                                     
SITE     1 AC8 34 TYR B 116  ILE B 127  5AD B 767  HOH B 781                    
SITE     2 AC8 34 HOH B 860  HOH B1534  HOH B3091  GLU D 615                    
SITE     3 AC8 34 GLU D 617  HIS D 618  SER D 619  VAL D 620                    
SITE     4 AC8 34 GLY D 621  GLU D 624  VAL D 625  ALA D 666                    
SITE     5 AC8 34 SER D 667  ILE D 669  ILE D 670  SER D 671                    
SITE     6 AC8 34 HIS D 672  GLY D 701  GLY D 702  THR D 703                    
SITE     7 AC8 34 PHE D 719  GLY D 720  SER D 723  VAL D 728                    
SITE     8 AC8 34 HOH D 875  HOH D 886  HOH D 975  HOH D1504                    
SITE     9 AC8 34 HOH D1759  HOH D1921                                          
SITE     1 AC9  7 B12 B1801  LEU D 489  HOH D 785  HOH D 915                    
SITE     2 AC9  7 HOH D 990  HOH D1020  HOH D2785                               
SITE     1 BC1 14 ARG A 109  GLY A 112  GLN A 113  SER A 114                    
SITE     2 BC1 14 TYR A 160  SER A 162  TYR A 187  ARG A 192                    
SITE     3 BC1 14 HIS A 225  ASN A 226  HOH A1618  LYS C 629                    
SITE     4 BC1 14 HOH C 854  HOH C 874                                          
SITE     1 BC2 39 TYR A 116  ILE A 127  5AD A 767  HOH A 923                    
SITE     2 BC2 39 HOH A1045  GLU C 615  GLU C 617  HIS C 618                    
SITE     3 BC2 39 SER C 619  VAL C 620  GLY C 621  GLU C 624                    
SITE     4 BC2 39 VAL C 625  ALA C 666  SER C 667  ILE C 669                    
SITE     5 BC2 39 ILE C 670  SER C 671  HIS C 672  GLY C 701                    
SITE     6 BC2 39 GLY C 702  THR C 703  PHE C 719  GLY C 720                    
SITE     7 BC2 39 SER C 723  VAL C 728  HOH C 782  HOH C 787                    
SITE     8 BC2 39 HOH C 843  HOH C 946  HOH C 952  HOH C 984                    
SITE     9 BC2 39 HOH C 989  HOH C1036  HOH C1251  HOH C1362                    
SITE    10 BC2 39 HOH C1706  HOH C1779  HOH C2998                               
SITE     1 BC3  6 B12 A1801  LEU C 489  HOH C 936  HOH C1063                    
SITE     2 BC3  6 HOH C1699  HOH C2858                                          
CRYST1   66.430  234.510  124.560  90.00 103.51  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      0.015053  0.000000  0.003617        0.00000                         
SCALE2      0.000000  0.004264  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008257        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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