GenomeNet

Database: PDB
Entry: 4L3V
LinkDB: 4L3V
Original site: 4L3V 
HEADER    LYASE                                   07-JUN-13   4L3V              
TITLE     CRYSTAL STRUCTURE OF DELTA516-525 HUMAN CYSTATHIONINE BETA-SYNTHASE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTATHIONINE BETA-SYNTHASE;                               
COMPND   3 CHAIN: B, A, C;                                                      
COMPND   4 SYNONYM: BETA-THIONASE, SERINE SULFHYDRASE;                          
COMPND   5 EC: 4.2.1.22;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CBS;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD                             
KEYWDS    CBS DOMAIN, HOMOCYTEINE, CYSTEINE BIOSYNTHESIS, HEME, PYRIDOXAL 5'-   
KEYWDS   2 PHOSPHATE, S-ADENOSYLMETHIONINE, TRANSSULFURATION PATHWAY, LYASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ERENO,T.MAJTAN,I.OYENARTE,J.P.KRAUS,L.A.MARTINEZ                    
REVDAT   4   20-SEP-23 4L3V    1       REMARK LINK                              
REVDAT   3   16-OCT-13 4L3V    1       JRNL                                     
REVDAT   2   02-OCT-13 4L3V    1       JRNL                                     
REVDAT   1   18-SEP-13 4L3V    0                                                
JRNL        AUTH   J.ERENO-ORBEA,T.MAJTAN,I.OYENARTE,J.P.KRAUS,                 
JRNL        AUTH 2 L.A.MARTINEZ-CRUZ                                            
JRNL        TITL   STRUCTURAL BASIS OF REGULATION AND OLIGOMERIZATION OF HUMAN  
JRNL        TITL 2 CYSTATHIONINE BETA-SYNTHASE, THE CENTRAL ENZYME OF           
JRNL        TITL 3 TRANSSULFURATION.                                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 E3790 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24043838                                                     
JRNL        DOI    10.1073/PNAS.1313683110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
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) : 3.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 46253                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2340                            
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 48.5203 -  9.3068    0.97     2768   157  0.1748 0.1667        
REMARK   3     2  9.3068 -  7.3955    1.00     2752   149  0.1500 0.1660        
REMARK   3     3  7.3955 -  6.4631    1.00     2687   147  0.1880 0.2311        
REMARK   3     4  6.4631 -  5.8733    1.00     2692   143  0.2002 0.2351        
REMARK   3     5  5.8733 -  5.4529    1.00     2645   173  0.2125 0.2251        
REMARK   3     6  5.4529 -  5.1318    1.00     2669   130  0.2016 0.2377        
REMARK   3     7  5.1318 -  4.8751    1.00     2662   145  0.2015 0.2261        
REMARK   3     8  4.8751 -  4.6630    0.99     2625   140  0.2157 0.2326        
REMARK   3     9  4.6630 -  4.4836    1.00     2660   138  0.2163 0.2319        
REMARK   3    10  4.4836 -  4.3290    0.99     2639   144  0.2296 0.2284        
REMARK   3    11  4.3290 -  4.1937    0.99     2613   143  0.2392 0.2939        
REMARK   3    12  4.1937 -  4.0739    0.98     2618   123  0.2511 0.2717        
REMARK   3    13  4.0739 -  3.9667    0.99     2633   122  0.2585 0.2959        
REMARK   3    14  3.9667 -  3.8700    0.99     2596   143  0.2677 0.2894        
REMARK   3    15  3.8700 -  3.7820    0.98     2628   129  0.2882 0.3054        
REMARK   3    16  3.7820 -  3.7016    0.99     2587   150  0.3153 0.3028        
REMARK   3    17  3.7016 -  3.6276    0.54     1439    64  0.4107 0.3970        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          11968                                  
REMARK   3   ANGLE     :  1.165          16268                                  
REMARK   3   CHIRALITY :  0.073           1825                                  
REMARK   3   PLANARITY :  0.009           2080                                  
REMARK   3   DIHEDRAL  : 13.002           4449                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4L3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080147.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46253                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.628                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.516                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 2.440                              
REMARK 200  R MERGE                    (I) : 0.31000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.37                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.280                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168                                     
REMARK 200 STARTING MODEL: PDB ENTRY 4LOD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V PEG550, 0.1 M SODIUM CITRATE     
REMARK 280  TRIBASIC DEHYDRATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.62650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.62650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      113.87500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      171.32750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      113.87500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      171.32750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.62650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      113.87500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      171.32750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.62650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      113.87500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      171.32750            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -455.50000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -160.87950            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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     PRO B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     HIS B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     LYS B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     GLN B   515                                                      
REMARK 465     ILE B   516                                                      
REMARK 465     GLN B   517                                                      
REMARK 465     TYR B   518                                                      
REMARK 465     HIS B   519                                                      
REMARK 465     SER B   520                                                      
REMARK 465     THR B   521                                                      
REMARK 465     GLY B   522                                                      
REMARK 465     LYS B   523                                                      
REMARK 465     SER B   524                                                      
REMARK 465     SER B   525                                                      
REMARK 465     GLN B   526                                                      
REMARK 465     LYS B   551                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     LYS A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     GLU A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     LYS A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     LYS A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     GLN A   515                                                      
REMARK 465     ILE A   516                                                      
REMARK 465     GLN A   517                                                      
REMARK 465     TYR A   518                                                      
REMARK 465     HIS A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     GLY A   522                                                      
REMARK 465     LYS A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     GLN A   526                                                      
REMARK 465     LYS A   551                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     GLU C     9                                                      
REMARK 465     VAL C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     GLY C    14                                                      
REMARK 465     CYS C    15                                                      
REMARK 465     PRO C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     ARG C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     HIS C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     LYS C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     SER C    27                                                      
REMARK 465     LEU C    28                                                      
REMARK 465     GLU C    29                                                      
REMARK 465     LYS C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     SER C    32                                                      
REMARK 465     PRO C    33                                                      
REMARK 465     GLU C    34                                                      
REMARK 465     ASP C    35                                                      
REMARK 465     LYS C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     ALA C    38                                                      
REMARK 465     LYS C    39                                                      
REMARK 465     GLU C    40                                                      
REMARK 465     ALA C    60                                                      
REMARK 465     GLN C   515                                                      
REMARK 465     ILE C   516                                                      
REMARK 465     GLN C   517                                                      
REMARK 465     TYR C   518                                                      
REMARK 465     HIS C   519                                                      
REMARK 465     SER C   520                                                      
REMARK 465     THR C   521                                                      
REMARK 465     GLY C   522                                                      
REMARK 465     LYS C   523                                                      
REMARK 465     SER C   524                                                      
REMARK 465     SER C   525                                                      
REMARK 465     GLN C   526                                                      
REMARK 465     LYS C   551                                                      
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     THR B 403    CB   OG1  CG2                                       
REMARK 470     ASP B 444    CG   OD1  OD2                                       
REMARK 470     GLU B 514    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 444    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 514    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 444    CB   CG   OD1  OD2                                  
REMARK 470     GLU C 514    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B  94      -62.35    -96.76                                   
REMARK 500    ASP B 221       71.12     53.33                                   
REMARK 500    THR B 235      -67.63   -109.64                                   
REMARK 500    GLN B 341      -60.62    -90.22                                   
REMARK 500    LYS B 384      -86.70   -105.21                                   
REMARK 500    LYS A  94      -62.95    -94.91                                   
REMARK 500    ASN A 194       -5.32     66.86                                   
REMARK 500    ASP A 221       71.95     50.39                                   
REMARK 500    THR A 235      -66.45   -109.51                                   
REMARK 500    LYS A 384      -87.47   -105.63                                   
REMARK 500    ASP A 549      -60.50   -134.11                                   
REMARK 500    LYS C  94      -62.95    -96.53                                   
REMARK 500    ASN C 194       -5.40     64.31                                   
REMARK 500    THR C 235      -68.38   -109.25                                   
REMARK 500    LYS C 384      -87.14   -105.45                                   
REMARK 500    ASP C 549      -62.01   -134.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  52   SG                                                     
REMARK 620 2 HEM B 602   NA   90.0                                              
REMARK 620 3 HEM B 602   NB   90.0  91.7                                        
REMARK 620 4 HEM B 602   NC   90.0 179.2  87.5                                  
REMARK 620 5 HEM B 602   ND   90.0  87.6 179.3  93.2                            
REMARK 620 6 HIS B  65   NE2 180.0  90.0  90.0  90.0  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 HEM A 602   NA   90.0                                              
REMARK 620 3 HEM A 602   NB   90.0  90.8                                        
REMARK 620 4 HEM A 602   NC   90.0 178.7  87.9                                  
REMARK 620 5 HEM A 602   ND   90.0  88.7 179.5  92.6                            
REMARK 620 6 HIS A  65   NE2 180.0  90.0  90.0  90.0  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  52   SG                                                     
REMARK 620 2 HEM C 602   NA   90.0                                              
REMARK 620 3 HEM C 602   NB   90.0  90.4                                        
REMARK 620 4 HEM C 602   NC   90.0 179.4  89.1                                  
REMARK 620 5 HEM C 602   ND   90.0  89.1 179.4  91.5                            
REMARK 620 6 HIS C  65   NE2 180.0  90.0  90.0  90.0  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JBQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L0D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L27   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L28   RELATED DB: PDB                                   
DBREF  4L3V B    2   551  UNP    P35520   CBS_HUMAN        2    551             
DBREF  4L3V A    2   551  UNP    P35520   CBS_HUMAN        2    551             
DBREF  4L3V C    2   551  UNP    P35520   CBS_HUMAN        2    551             
SEQRES   1 B  550  PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY          
SEQRES   2 B  550  CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER          
SEQRES   3 B  550  LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU          
SEQRES   4 B  550  PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR          
SEQRES   5 B  550  TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS          
SEQRES   6 B  550  HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP          
SEQRES   7 B  550  ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE          
SEQRES   8 B  550  ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU          
SEQRES   9 B  550  LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL          
SEQRES  10 B  550  LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU          
SEQRES  11 B  550  ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU          
SEQRES  12 B  550  PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA          
SEQRES  13 B  550  ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO          
SEQRES  14 B  550  GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA          
SEQRES  15 B  550  LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG          
SEQRES  16 B  550  PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG          
SEQRES  17 B  550  LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN          
SEQRES  18 B  550  TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR          
SEQRES  19 B  550  THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU          
SEQRES  20 B  550  ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE          
SEQRES  21 B  550  THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY          
SEQRES  22 B  550  CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU          
SEQRES  23 B  550  ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR          
SEQRES  24 B  550  TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR          
SEQRES  25 B  550  VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER          
SEQRES  26 B  550  ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE          
SEQRES  27 B  550  ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER          
SEQRES  28 B  550  THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN          
SEQRES  29 B  550  GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL          
SEQRES  30 B  550  ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET          
SEQRES  31 B  550  LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU          
SEQRES  32 B  550  LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU          
SEQRES  33 B  550  GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR          
SEQRES  34 B  550  CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE          
SEQRES  35 B  550  ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU          
SEQRES  36 B  550  GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU          
SEQRES  37 B  550  ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL          
SEQRES  38 B  550  ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR          
SEQRES  39 B  550  LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE          
SEQRES  40 B  550  ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR          
SEQRES  41 B  550  GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL          
SEQRES  42 B  550  THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU          
SEQRES  43 B  550  ARG ASP GLN LYS                                              
SEQRES   1 A  550  PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY          
SEQRES   2 A  550  CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER          
SEQRES   3 A  550  LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU          
SEQRES   4 A  550  PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR          
SEQRES   5 A  550  TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS          
SEQRES   6 A  550  HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP          
SEQRES   7 A  550  ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE          
SEQRES   8 A  550  ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU          
SEQRES   9 A  550  LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL          
SEQRES  10 A  550  LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU          
SEQRES  11 A  550  ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU          
SEQRES  12 A  550  PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA          
SEQRES  13 A  550  ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO          
SEQRES  14 A  550  GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA          
SEQRES  15 A  550  LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG          
SEQRES  16 A  550  PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG          
SEQRES  17 A  550  LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN          
SEQRES  18 A  550  TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR          
SEQRES  19 A  550  THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU          
SEQRES  20 A  550  ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE          
SEQRES  21 A  550  THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY          
SEQRES  22 A  550  CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU          
SEQRES  23 A  550  ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR          
SEQRES  24 A  550  TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR          
SEQRES  25 A  550  VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER          
SEQRES  26 A  550  ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE          
SEQRES  27 A  550  ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER          
SEQRES  28 A  550  THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN          
SEQRES  29 A  550  GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL          
SEQRES  30 A  550  ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET          
SEQRES  31 A  550  LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU          
SEQRES  32 A  550  LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU          
SEQRES  33 A  550  GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR          
SEQRES  34 A  550  CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE          
SEQRES  35 A  550  ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU          
SEQRES  36 A  550  GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU          
SEQRES  37 A  550  ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL          
SEQRES  38 A  550  ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR          
SEQRES  39 A  550  LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE          
SEQRES  40 A  550  ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR          
SEQRES  41 A  550  GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL          
SEQRES  42 A  550  THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU          
SEQRES  43 A  550  ARG ASP GLN LYS                                              
SEQRES   1 C  550  PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY          
SEQRES   2 C  550  CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER          
SEQRES   3 C  550  LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU          
SEQRES   4 C  550  PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR          
SEQRES   5 C  550  TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS          
SEQRES   6 C  550  HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP          
SEQRES   7 C  550  ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE          
SEQRES   8 C  550  ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU          
SEQRES   9 C  550  LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL          
SEQRES  10 C  550  LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU          
SEQRES  11 C  550  ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU          
SEQRES  12 C  550  PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA          
SEQRES  13 C  550  ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO          
SEQRES  14 C  550  GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA          
SEQRES  15 C  550  LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG          
SEQRES  16 C  550  PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG          
SEQRES  17 C  550  LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN          
SEQRES  18 C  550  TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR          
SEQRES  19 C  550  THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU          
SEQRES  20 C  550  ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE          
SEQRES  21 C  550  THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY          
SEQRES  22 C  550  CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU          
SEQRES  23 C  550  ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR          
SEQRES  24 C  550  TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR          
SEQRES  25 C  550  VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER          
SEQRES  26 C  550  ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE          
SEQRES  27 C  550  ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER          
SEQRES  28 C  550  THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN          
SEQRES  29 C  550  GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL          
SEQRES  30 C  550  ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET          
SEQRES  31 C  550  LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU          
SEQRES  32 C  550  LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU          
SEQRES  33 C  550  GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR          
SEQRES  34 C  550  CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE          
SEQRES  35 C  550  ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU          
SEQRES  36 C  550  GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU          
SEQRES  37 C  550  ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL          
SEQRES  38 C  550  ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR          
SEQRES  39 C  550  LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE          
SEQRES  40 C  550  ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR          
SEQRES  41 C  550  GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL          
SEQRES  42 C  550  THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU          
SEQRES  43 C  550  ARG ASP GLN LYS                                              
HET    PLP  B 601      15                                                       
HET    HEM  B 602      43                                                       
HET    PLP  A 601      15                                                       
HET    HEM  A 602      43                                                       
HET    PLP  C 601      15                                                       
HET    HEM  C 602      43                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     HEM HEME                                                             
FORMUL   4  PLP    3(C8 H10 N O6 P)                                             
FORMUL   5  HEM    3(C34 H32 FE N4 O4)                                          
HELIX    1   1 PRO B   59  SER B   63  5                                   5    
HELIX    2   2 ASP B   79  ILE B   84  5                                   6    
HELIX    3   3 LYS B   94  PHE B   99  1                                   6    
HELIX    4   4 PHE B  111  ASN B  113  5                                   3    
HELIX    5   5 VAL B  118  ASP B  133  1                                  16    
HELIX    6   6 GLY B  148  GLY B  162  1                                  15    
HELIX    7   7 SER B  174  GLY B  185  1                                  12    
HELIX    8   8 SER B  202  ILE B  214  1                                  13    
HELIX    9   9 ALA B  226  THR B  235  1                                  10    
HELIX   10  10 THR B  235  CYS B  244  1                                  10    
HELIX   11  11 GLY B  258  CYS B  272  1                                  15    
HELIX   12  12 PRO B  290  GLN B  295  5                                   6    
HELIX   13  13 ASN B  327  GLN B  341  1                                  15    
HELIX   14  14 GLY B  347  ALA B  361  1                                  15    
HELIX   15  15 GLN B  362  LEU B  364  5                                   3    
HELIX   16  16 SER B  377  MET B  382  5                                   6    
HELIX   17  17 SER B  387  LYS B  394  1                                   8    
HELIX   18  18 LYS B  398  LYS B  406  1                                   9    
HELIX   19  19 PRO B  407  HIS B  411  5                                   5    
HELIX   20  20 ARG B  413  GLY B  418  5                                   6    
HELIX   21  21 THR B  430  GLY B  442  1                                  13    
HELIX   22  22 LEU B  461  ALA B  470  1                                  10    
HELIX   23  23 GLN B  478  ILE B  483  5                                   6    
HELIX   24  24 THR B  495  GLU B  504  1                                  10    
HELIX   25  25 THR B  535  ARG B  548  1                                  14    
HELIX   26  26 PRO A   59  SER A   63  5                                   5    
HELIX   27  27 ASP A   79  ILE A   84  5                                   6    
HELIX   28  28 ASN A   93  PHE A   99  1                                   7    
HELIX   29  29 PHE A  111  ASN A  113  5                                   3    
HELIX   30  30 VAL A  118  ASP A  133  1                                  16    
HELIX   31  31 GLY A  148  GLY A  162  1                                  15    
HELIX   32  32 SER A  174  GLY A  185  1                                  12    
HELIX   33  33 SER A  202  ILE A  214  1                                  13    
HELIX   34  34 ALA A  226  THR A  235  1                                  10    
HELIX   35  35 THR A  235  CYS A  244  1                                  10    
HELIX   36  36 GLY A  258  CYS A  272  1                                  15    
HELIX   37  37 PRO A  290  GLN A  295  5                                   6    
HELIX   38  38 ASN A  327  GLY A  343  1                                  17    
HELIX   39  39 GLY A  347  ALA A  361  1                                  15    
HELIX   40  40 GLN A  362  LEU A  364  5                                   3    
HELIX   41  41 SER A  377  MET A  382  5                                   6    
HELIX   42  42 SER A  387  LYS A  394  1                                   8    
HELIX   43  43 LYS A  398  LYS A  406  1                                   9    
HELIX   44  44 PRO A  407  HIS A  411  5                                   5    
HELIX   45  45 ARG A  413  GLY A  418  5                                   6    
HELIX   46  46 THR A  430  GLY A  442  1                                  13    
HELIX   47  47 LEU A  461  ALA A  470  1                                  10    
HELIX   48  48 GLN A  478  ILE A  483  5                                   6    
HELIX   49  49 THR A  495  LEU A  503  1                                   9    
HELIX   50  50 THR A  535  ARG A  548  1                                  14    
HELIX   51  51 ASP C   79  ILE C   84  5                                   6    
HELIX   52  52 LYS C   94  PHE C   99  1                                   6    
HELIX   53  53 PHE C  111  ASN C  113  5                                   3    
HELIX   54  54 VAL C  118  ASP C  133  1                                  16    
HELIX   55  55 GLY C  148  GLY C  162  1                                  15    
HELIX   56  56 SER C  174  GLY C  185  1                                  12    
HELIX   57  57 SER C  202  ILE C  214  1                                  13    
HELIX   58  58 ALA C  226  THR C  235  1                                  10    
HELIX   59  59 THR C  235  CYS C  244  1                                  10    
HELIX   60  60 GLY C  258  CYS C  272  1                                  15    
HELIX   61  61 PRO C  290  GLN C  295  5                                   6    
HELIX   62  62 ASN C  327  GLY C  343  1                                  17    
HELIX   63  63 GLY C  347  ALA C  361  1                                  15    
HELIX   64  64 GLN C  362  LEU C  364  5                                   3    
HELIX   65  65 SER C  377  MET C  382  5                                   6    
HELIX   66  66 SER C  387  LYS C  394  1                                   8    
HELIX   67  67 LYS C  398  LYS C  406  1                                   9    
HELIX   68  68 PRO C  407  HIS C  411  5                                   5    
HELIX   69  69 ARG C  413  GLY C  418  5                                   6    
HELIX   70  70 THR C  430  GLY C  442  1                                  13    
HELIX   71  71 LEU C  461  ALA C  470  1                                  10    
HELIX   72  72 GLN C  478  ILE C  483  5                                   6    
HELIX   73  73 THR C  495  GLU C  504  1                                  10    
HELIX   74  74 THR C  535  ARG C  548  1                                  14    
SHEET    1   A 6 MET B  89  ARG B  91  0                                        
SHEET    2   A 6 GLU B 104  CYS B 109 -1  O  ALA B 107   N  VAL B  90           
SHEET    3   A 6 ARG B 369  LEU B 374  1  O  CYS B 370   N  GLU B 104           
SHEET    4   A 6 MET B 250  SER B 254  1  N  MET B 250   O  VAL B 371           
SHEET    5   A 6 ARG B 276  PRO B 282  1  O  ILE B 278   N  LEU B 251           
SHEET    6   A 6 LYS B 322  SER B 326  1  O  PHE B 324   N  ASP B 281           
SHEET    1   B 4 GLU B 187  THR B 191  0                                        
SHEET    2   B 4 ARG B 164  PRO B 170  1  N  ILE B 167   O  GLU B 187           
SHEET    3   B 4 THR B 141  PRO B 145  1  N  ILE B 142   O  ILE B 166           
SHEET    4   B 4 SER B 217  ILE B 219  1  O  HIS B 218   N  ILE B 143           
SHEET    1   C 2 GLN B 445  VAL B 449  0                                        
SHEET    2   C 2 ILE B 455  THR B 460 -1  O  VAL B 459   N  ALA B 446           
SHEET    1   D 3 LYS B 488  ILE B 490  0                                        
SHEET    2   D 3 ALA B 509  VAL B 512  1  O  LEU B 510   N  LYS B 488           
SHEET    3   D 3 VAL B 530  VAL B 534 -1  O  VAL B 534   N  ALA B 509           
SHEET    1   E 7 ILE A  76  LEU A  77  0                                        
SHEET    2   E 7 MET C  89  ARG C  91  1  O  MET C  89   N  LEU A  77           
SHEET    3   E 7 GLU C 104  CYS C 109 -1  O  ALA C 107   N  VAL C  90           
SHEET    4   E 7 ARG C 369  LEU C 374  1  O  CYS C 370   N  LEU C 106           
SHEET    5   E 7 MET C 250  SER C 254  1  N  MET C 250   O  VAL C 371           
SHEET    6   E 7 ARG C 276  PRO C 282  1  O  ARG C 276   N  LEU C 251           
SHEET    7   E 7 LYS C 322  SER C 326  1  O  PHE C 324   N  ASP C 281           
SHEET    1   F 7 LYS A 322  SER A 326  0                                        
SHEET    2   F 7 ARG A 276  PRO A 282  1  N  ASP A 281   O  PHE A 324           
SHEET    3   F 7 MET A 250  SER A 254  1  N  LEU A 251   O  ILE A 278           
SHEET    4   F 7 ARG A 369  LEU A 374  1  O  VAL A 371   N  MET A 250           
SHEET    5   F 7 GLU A 104  CYS A 109  1  N  LYS A 108   O  VAL A 372           
SHEET    6   F 7 MET A  89  ARG A  91 -1  N  VAL A  90   O  ALA A 107           
SHEET    7   F 7 ILE C  76  LEU C  77  1  O  LEU C  77   N  MET A  89           
SHEET    1   G 4 GLU A 187  THR A 191  0                                        
SHEET    2   G 4 ARG A 164  PRO A 170  1  N  ILE A 167   O  GLU A 187           
SHEET    3   G 4 THR A 141  PRO A 145  1  N  GLU A 144   O  VAL A 168           
SHEET    4   G 4 SER A 217  ILE A 219  1  O  HIS A 218   N  ILE A 143           
SHEET    1   H 2 GLN A 445  VAL A 449  0                                        
SHEET    2   H 2 ILE A 455  THR A 460 -1  O  VAL A 459   N  ALA A 446           
SHEET    1   I 3 LYS A 488  ILE A 490  0                                        
SHEET    2   I 3 ALA A 509  VAL A 512  1  O  LEU A 510   N  LYS A 488           
SHEET    3   I 3 VAL A 530  VAL A 534 -1  O  PHE A 531   N  VAL A 511           
SHEET    1   J 4 GLU C 187  THR C 191  0                                        
SHEET    2   J 4 ARG C 164  PRO C 170  1  N  CYS C 165   O  GLU C 187           
SHEET    3   J 4 THR C 141  PRO C 145  1  N  ILE C 142   O  ILE C 166           
SHEET    4   J 4 SER C 217  ILE C 219  1  O  HIS C 218   N  ILE C 143           
SHEET    1   K 2 GLN C 445  VAL C 449  0                                        
SHEET    2   K 2 ILE C 455  THR C 460 -1  O  VAL C 459   N  ALA C 446           
SHEET    1   L 3 LYS C 488  ILE C 490  0                                        
SHEET    2   L 3 ALA C 509  VAL C 512  1  O  LEU C 510   N  LYS C 488           
SHEET    3   L 3 VAL C 530  VAL C 534 -1  O  VAL C 534   N  ALA C 509           
LINK         NZ  LYS B 119                 C4A PLP B 601     1555   1555  1.36  
LINK         NZ  LYS A 119                 C4A PLP A 601     1555   1555  1.35  
LINK         NZ  LYS C 119                 C4A PLP C 601     1555   1555  1.36  
LINK         SG  CYS B  52                FE   HEM B 602     1555   1555  2.23  
LINK         NE2 HIS B  65                FE   HEM B 602     1555   1555  2.05  
LINK         SG  CYS A  52                FE   HEM A 602     1555   1555  2.27  
LINK         NE2 HIS A  65                FE   HEM A 602     1555   1555  2.06  
LINK         SG  CYS C  52                FE   HEM C 602     1555   1555  2.27  
LINK         NE2 HIS C  65                FE   HEM C 602     1555   1555  2.10  
CISPEP   1 GLU B  289    PRO B  290          0        -1.86                     
CISPEP   2 GLU A  289    PRO A  290          0        -0.75                     
CISPEP   3 GLU C  289    PRO C  290          0        -1.79                     
SITE     1 AC1 15 LYS B 119  ASN B 149  SER B 254  VAL B 255                    
SITE     2 AC1 15 GLY B 256  THR B 257  GLY B 258  GLY B 259                    
SITE     3 AC1 15 THR B 260  GLY B 305  ILE B 306  SER B 349                    
SITE     4 AC1 15 PRO B 375  ASP B 376  TYR B 381                               
SITE     1 AC2 20 THR A  53  ARG A  58  HEM A 602  SER B  50                    
SITE     2 AC2 20 ARG B  51  CYS B  52  THR B  53  TRP B  54                    
SITE     3 AC2 20 ARG B  58  PRO B  59  GLU B  62  SER B  63                    
SITE     4 AC2 20 PRO B  64  HIS B  65  ARG B 224  ALA B 226                    
SITE     5 AC2 20 PRO B 229  TYR B 233  ARG B 266  THR B 313                    
SITE     1 AC3 14 LYS A 119  ASN A 149  SER A 254  VAL A 255                    
SITE     2 AC3 14 GLY A 256  THR A 257  GLY A 258  GLY A 259                    
SITE     3 AC3 14 THR A 260  GLY A 305  ILE A 306  SER A 349                    
SITE     4 AC3 14 PRO A 375  ASP A 376                                          
SITE     1 AC4 20 SER A  50  ARG A  51  CYS A  52  THR A  53                    
SITE     2 AC4 20 TRP A  54  ARG A  58  PRO A  59  GLU A  62                    
SITE     3 AC4 20 SER A  63  PRO A  64  HIS A  65  ALA A 226                    
SITE     4 AC4 20 LEU A 230  TYR A 233  GLY A 263  ARG A 266                    
SITE     5 AC4 20 VAL A 314  THR B  53  ARG B  58  HEM B 602                    
SITE     1 AC5 15 LYS C 119  ASN C 149  SER C 254  VAL C 255                    
SITE     2 AC5 15 GLY C 256  THR C 257  GLY C 258  GLY C 259                    
SITE     3 AC5 15 THR C 260  GLY C 305  ILE C 306  SER C 349                    
SITE     4 AC5 15 PRO C 375  ASP C 376  TYR C 381                               
SITE     1 AC6 16 PRO C  49  ARG C  51  CYS C  52  THR C  53                    
SITE     2 AC6 16 TRP C  54  PRO C  59  GLU C  62  SER C  63                    
SITE     3 AC6 16 PRO C  64  HIS C  65  ARG C 224  ALA C 226                    
SITE     4 AC6 16 LEU C 230  GLY C 263  ARG C 266  VAL C 314                    
CRYST1  227.750  342.655  107.253  90.00  90.00  90.00 C 2 2 21     24          
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      0.004391  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002918  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009324        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system