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Database: PDB
Entry: 6E45
LinkDB: 6E45
Original site: 6E45 
HEADER    OXIDOREDUCTASE                          16-JUL-18   6E45              
TITLE     CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) FREE  
TITLE    2 ENZYME IN THE FERROUS STATE                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDOLEAMINE 2,3-DIOXYGENASE 1;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUE 15-403;                                            
COMPND   5 SYNONYM: IDO-1,INDOLEAMINE-PYRROLE 2,3-DIOXYGENASE;                  
COMPND   6 EC: 1.13.11.52;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IDO1, IDO, INDO;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    IDO1, FREE ENZYME, FERROUS STATE, OXIDOREDUCTASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LUO,L.TONG                                                          
REVDAT   1   14-NOV-18 6E45    0                                                
JRNL        AUTH   S.LUO,K.XU,S.XIANG,J.CHEN,C.CHEN,C.GUO,Y.TONG,L.TONG         
JRNL        TITL   HIGH-RESOLUTION STRUCTURES OF INHIBITOR COMPLEXES OF HUMAN   
JRNL        TITL 2 INDOLEAMINE 2,3-DIOXYGENASE 1 IN A NEW CRYSTAL FORM.         
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  74   717 2018              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   30387777                                                     
JRNL        DOI    10.1107/S2053230X18012955                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 123872                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1862                            
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 65.9133 -  4.6962    0.99     9824   148  0.1689 0.1989        
REMARK   3     2  4.6962 -  3.7276    1.00     9592   148  0.1445 0.1994        
REMARK   3     3  3.7276 -  3.2564    1.00     9518   143  0.1711 0.1872        
REMARK   3     4  3.2564 -  2.9587    1.00     9427   145  0.1983 0.2378        
REMARK   3     5  2.9587 -  2.7466    1.00     9432   144  0.1992 0.2179        
REMARK   3     6  2.7466 -  2.5847    1.00     9370   142  0.1981 0.2815        
REMARK   3     7  2.5847 -  2.4552    1.00     9423   143  0.2056 0.2231        
REMARK   3     8  2.4552 -  2.3484    1.00     9329   144  0.2126 0.2370        
REMARK   3     9  2.3484 -  2.2579    1.00     9420   142  0.2179 0.2645        
REMARK   3    10  2.2579 -  2.1800    1.00     9324   142  0.2279 0.2902        
REMARK   3    11  2.1800 -  2.1119    1.00     9302   142  0.2362 0.2723        
REMARK   3    12  2.1119 -  2.0515    1.00     9344   144  0.2596 0.2876        
REMARK   3    13  2.0515 -  1.9975    0.93     8705   135  0.2884 0.2993        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.64                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.51                          
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      :  0.010          12203                                  
REMARK   3   ANGLE     :  1.047          16567                                  
REMARK   3   CHIRALITY :  0.263           1793                                  
REMARK   3   PLANARITY :  0.006           2101                                  
REMARK   3   DIHEDRAL  : 19.762           4450                                  
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 6E45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235675.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS-II                            
REMARK 200  BEAMLINE                       : 17-ID-2                            
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 123961                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.878                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.947                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5500                            
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) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.83                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.880                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE (PH 6.2), AND 15%        
REMARK 280  (W/V) PEG3350, EVAPORATION, TEMPERATURE 298K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       39.98450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.26900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.98450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.26900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLN A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     ASN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 465     THR A   367                                                      
REMARK 465     SER A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     ASP A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     SER A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     LEU A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     LYS A   377                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLN B   361                                                      
REMARK 465     PRO B   362                                                      
REMARK 465     LYS B   363                                                      
REMARK 465     GLU B   364                                                      
REMARK 465     ASN B   365                                                      
REMARK 465     LYS B   366                                                      
REMARK 465     THR B   367                                                      
REMARK 465     SER B   368                                                      
REMARK 465     GLU B   369                                                      
REMARK 465     ASP B   370                                                      
REMARK 465     PRO B   371                                                      
REMARK 465     SER B   372                                                      
REMARK 465     LYS B   373                                                      
REMARK 465     LEU B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     GLU B   402                                                      
REMARK 465     GLY B   403                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     ALA C    13                                                      
REMARK 465     GLN C   361                                                      
REMARK 465     PRO C   362                                                      
REMARK 465     LYS C   363                                                      
REMARK 465     GLU C   364                                                      
REMARK 465     ASN C   365                                                      
REMARK 465     LYS C   366                                                      
REMARK 465     THR C   367                                                      
REMARK 465     SER C   368                                                      
REMARK 465     GLU C   369                                                      
REMARK 465     ASP C   370                                                      
REMARK 465     PRO C   371                                                      
REMARK 465     SER C   372                                                      
REMARK 465     LYS C   373                                                      
REMARK 465     LEU C   374                                                      
REMARK 465     GLU C   375                                                      
REMARK 465     ALA C   376                                                      
REMARK 465     LYS C   377                                                      
REMARK 465     GLY C   378                                                      
REMARK 465     THR C   379                                                      
REMARK 465     GLY C   403                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     GLN D   361                                                      
REMARK 465     PRO D   362                                                      
REMARK 465     LYS D   363                                                      
REMARK 465     GLU D   364                                                      
REMARK 465     ASN D   365                                                      
REMARK 465     LYS D   366                                                      
REMARK 465     THR D   367                                                      
REMARK 465     SER D   368                                                      
REMARK 465     GLU D   369                                                      
REMARK 465     ASP D   370                                                      
REMARK 465     PRO D   371                                                      
REMARK 465     SER D   372                                                      
REMARK 465     LYS D   373                                                      
REMARK 465     LEU D   374                                                      
REMARK 465     GLU D   375                                                      
REMARK 465     ALA D   376                                                      
REMARK 465     LYS D   377                                                      
REMARK 465     GLY D   378                                                      
REMARK 465     THR D   379                                                      
REMARK 465     GLU D   402                                                      
REMARK 465     GLY D   403                                                      
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 C   742     O    HOH C   829              2.07            
REMARK 500   O    ASP A   156     O    HOH A   601              2.08            
REMARK 500   OD1  ASP A    68     O    HOH A   602              2.13            
REMARK 500   O    HOH B   658     O    HOH B   856              2.14            
REMARK 500   O    HOH A   662     O    HOH A   784              2.16            
REMARK 500   O    HOH A   790     O    HOH A   794              2.16            
REMARK 500   NH2  ARG C   105     O    HOH C   601              2.17            
REMARK 500   NZ   LYS C   198     O    HOH C   602              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  55   CA  -  CB  -  CG  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    LEU B  55   CA  -  CB  -  CG  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    LEU C  55   CA  -  CB  -  CG  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    LEU C 355   CB  -  CG  -  CD1 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    MET C 385   CG  -  SD  -  CE  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    LEU D  55   CA  -  CB  -  CG  ANGL. DEV. = -16.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  33      152.09    -48.17                                   
REMARK 500    ASN A 133       54.35   -104.38                                   
REMARK 500    ILE A 354      -51.85   -126.25                                   
REMARK 500    ASN B 133       54.29   -108.36                                   
REMARK 500    GLU B 192       78.54   -112.78                                   
REMARK 500    ILE B 354      -56.05   -124.04                                   
REMARK 500    ASN C 133       55.12   -106.21                                   
REMARK 500    VAL C 229      -62.99   -121.12                                   
REMARK 500    ILE C 354      -51.57   -129.08                                   
REMARK 500    ASN D 133       54.52   -110.46                                   
REMARK 500    VAL D 229      -65.87   -122.27                                   
REMARK 500    ILE D 354      -55.52   -128.47                                   
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 A 818        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH C 854        DISTANCE =  6.16 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                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 346   NE2                                                    
REMARK 620 2 HEM A 501   NA   88.8                                              
REMARK 620 3 HEM A 501   NB  102.1  94.1                                        
REMARK 620 4 HEM A 501   NC  102.3 168.9  85.0                                  
REMARK 620 5 HEM A 501   ND   92.1  86.5 165.8  91.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 346   NE2                                                    
REMARK 620 2 HEM B 501   NA   91.3                                              
REMARK 620 3 HEM B 501   NB  101.8  93.9                                        
REMARK 620 4 HEM B 501   NC   97.5 170.8  87.1                                  
REMARK 620 5 HEM B 501   ND   91.1  86.0 167.1  90.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 346   NE2                                                    
REMARK 620 2 HEM C 501   NA   92.1                                              
REMARK 620 3 HEM C 501   NB  102.2  92.3                                        
REMARK 620 4 HEM C 501   NC   97.3 170.3  88.0                                  
REMARK 620 5 HEM C 501   ND   91.1  87.2 166.7  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 346   NE2                                                    
REMARK 620 2 HEM D 501   NA   94.3                                              
REMARK 620 3 HEM D 501   NB  101.0  91.5                                        
REMARK 620 4 HEM D 501   NC   97.1 168.5  87.6                                  
REMARK 620 5 HEM D 501   ND   93.9  87.5 165.1  90.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 506                 
DBREF  6E45 A   15   403  UNP    P14902   I23O1_HUMAN     15    403             
DBREF  6E45 B   15   403  UNP    P14902   I23O1_HUMAN     15    403             
DBREF  6E45 C   15   403  UNP    P14902   I23O1_HUMAN     15    403             
DBREF  6E45 D   15   403  UNP    P14902   I23O1_HUMAN     15    403             
SEQADV 6E45 MET A   -1  UNP  P14902              INITIATING METHIONINE          
SEQADV 6E45 GLY A    0  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER A    1  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER A    2  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    3  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    4  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    5  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    6  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    7  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS A    8  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER A    9  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER A   10  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 GLY A   11  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER A   12  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA A   13  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA A   14  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA A  116  UNP  P14902    LYS   116 ENGINEERED MUTATION            
SEQADV 6E45 ALA A  117  UNP  P14902    LYS   117 ENGINEERED MUTATION            
SEQADV 6E45 MET B   -1  UNP  P14902              INITIATING METHIONINE          
SEQADV 6E45 GLY B    0  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER B    1  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER B    2  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    3  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    4  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    5  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    6  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    7  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS B    8  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER B    9  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER B   10  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 GLY B   11  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER B   12  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA B   13  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA B   14  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA B  116  UNP  P14902    LYS   116 ENGINEERED MUTATION            
SEQADV 6E45 ALA B  117  UNP  P14902    LYS   117 ENGINEERED MUTATION            
SEQADV 6E45 MET C   -1  UNP  P14902              INITIATING METHIONINE          
SEQADV 6E45 GLY C    0  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER C    1  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER C    2  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    3  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    4  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    5  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    6  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    7  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS C    8  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER C    9  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER C   10  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 GLY C   11  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER C   12  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA C   13  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA C   14  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA C  116  UNP  P14902    LYS   116 ENGINEERED MUTATION            
SEQADV 6E45 ALA C  117  UNP  P14902    LYS   117 ENGINEERED MUTATION            
SEQADV 6E45 MET D   -1  UNP  P14902              INITIATING METHIONINE          
SEQADV 6E45 GLY D    0  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER D    1  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER D    2  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    3  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    4  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    5  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    6  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    7  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 HIS D    8  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER D    9  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER D   10  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 GLY D   11  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 SER D   12  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA D   13  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA D   14  UNP  P14902              EXPRESSION TAG                 
SEQADV 6E45 ALA D  116  UNP  P14902    LYS   116 ENGINEERED MUTATION            
SEQADV 6E45 ALA D  117  UNP  P14902    LYS   117 ENGINEERED MUTATION            
SEQRES   1 A  405  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  405  SER ALA ALA TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA          
SEQRES   3 A  405  LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN          
SEQRES   4 A  405  ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE          
SEQRES   5 A  405  GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN          
SEQRES   6 A  405  MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN          
SEQRES   7 A  405  ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA          
SEQRES   8 A  405  TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL          
SEQRES   9 A  405  LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER          
SEQRES  10 A  405  ALA ALA LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP          
SEQRES  11 A  405  CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS          
SEQRES  12 A  405  PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE          
SEQRES  13 A  405  ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER          
SEQRES  14 A  405  LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL          
SEQRES  15 A  405  ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG          
SEQRES  16 A  405  ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS          
SEQRES  17 A  405  LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP          
SEQRES  18 A  405  HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE          
SEQRES  19 A  405  TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP          
SEQRES  20 A  405  GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU          
SEQRES  21 A  405  PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN          
SEQRES  22 A  405  CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY          
SEQRES  23 A  405  GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG          
SEQRES  24 A  405  TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU          
SEQRES  25 A  405  GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS          
SEQRES  26 A  405  GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL          
SEQRES  27 A  405  LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE          
SEQRES  28 A  405  VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO          
SEQRES  29 A  405  LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU          
SEQRES  30 A  405  ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU          
SEQRES  31 A  405  LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS          
SEQRES  32 A  405  GLU GLY                                                      
SEQRES   1 B  405  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  405  SER ALA ALA TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA          
SEQRES   3 B  405  LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN          
SEQRES   4 B  405  ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE          
SEQRES   5 B  405  GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN          
SEQRES   6 B  405  MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN          
SEQRES   7 B  405  ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA          
SEQRES   8 B  405  TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL          
SEQRES   9 B  405  LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER          
SEQRES  10 B  405  ALA ALA LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP          
SEQRES  11 B  405  CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS          
SEQRES  12 B  405  PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE          
SEQRES  13 B  405  ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER          
SEQRES  14 B  405  LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL          
SEQRES  15 B  405  ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG          
SEQRES  16 B  405  ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS          
SEQRES  17 B  405  LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP          
SEQRES  18 B  405  HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE          
SEQRES  19 B  405  TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP          
SEQRES  20 B  405  GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU          
SEQRES  21 B  405  PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN          
SEQRES  22 B  405  CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY          
SEQRES  23 B  405  GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG          
SEQRES  24 B  405  TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU          
SEQRES  25 B  405  GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS          
SEQRES  26 B  405  GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL          
SEQRES  27 B  405  LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE          
SEQRES  28 B  405  VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO          
SEQRES  29 B  405  LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU          
SEQRES  30 B  405  ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU          
SEQRES  31 B  405  LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS          
SEQRES  32 B  405  GLU GLY                                                      
SEQRES   1 C  405  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  405  SER ALA ALA TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA          
SEQRES   3 C  405  LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN          
SEQRES   4 C  405  ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE          
SEQRES   5 C  405  GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN          
SEQRES   6 C  405  MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN          
SEQRES   7 C  405  ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA          
SEQRES   8 C  405  TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL          
SEQRES   9 C  405  LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER          
SEQRES  10 C  405  ALA ALA LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP          
SEQRES  11 C  405  CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS          
SEQRES  12 C  405  PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE          
SEQRES  13 C  405  ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER          
SEQRES  14 C  405  LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL          
SEQRES  15 C  405  ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG          
SEQRES  16 C  405  ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS          
SEQRES  17 C  405  LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP          
SEQRES  18 C  405  HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE          
SEQRES  19 C  405  TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP          
SEQRES  20 C  405  GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU          
SEQRES  21 C  405  PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN          
SEQRES  22 C  405  CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY          
SEQRES  23 C  405  GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG          
SEQRES  24 C  405  TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU          
SEQRES  25 C  405  GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS          
SEQRES  26 C  405  GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL          
SEQRES  27 C  405  LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE          
SEQRES  28 C  405  VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO          
SEQRES  29 C  405  LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU          
SEQRES  30 C  405  ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU          
SEQRES  31 C  405  LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS          
SEQRES  32 C  405  GLU GLY                                                      
SEQRES   1 D  405  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  405  SER ALA ALA TYR HIS ILE ASP GLU GLU VAL GLY PHE ALA          
SEQRES   3 D  405  LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR ASN          
SEQRES   4 D  405  ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU ILE          
SEQRES   5 D  405  GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU ASN          
SEQRES   6 D  405  MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER GLN          
SEQRES   7 D  405  ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET ALA          
SEQRES   8 D  405  TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS VAL          
SEQRES   9 D  405  LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU SER          
SEQRES  10 D  405  ALA ALA LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA ASP          
SEQRES  11 D  405  CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN LYS          
SEQRES  12 D  405  PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER PHE          
SEQRES  13 D  405  ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL SER          
SEQRES  14 D  405  LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS VAL          
SEQRES  15 D  405  ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU ARG          
SEQRES  16 D  405  ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER CYS          
SEQRES  17 D  405  LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS ASP          
SEQRES  18 D  405  HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG ILE          
SEQRES  19 D  405  TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER ASP          
SEQRES  20 D  405  GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS GLU          
SEQRES  21 D  405  PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL PHE GLN          
SEQRES  22 D  405  CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA GLY          
SEQRES  23 D  405  GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG ARG          
SEQRES  24 D  405  TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER LEU          
SEQRES  25 D  405  GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER LYS          
SEQRES  26 D  405  GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS VAL          
SEQRES  27 D  405  LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN ILE          
SEQRES  28 D  405  VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN PRO          
SEQRES  29 D  405  LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU GLU          
SEQRES  30 D  405  ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE LEU          
SEQRES  31 D  405  LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU LYS          
SEQRES  32 D  405  GLU GLY                                                      
HET    HEM  A 501      43                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HET    HEM  B 501      43                                                       
HET    PO4  B 502       5                                                       
HET    HEM  C 501      43                                                       
HET    HEM  D 501      43                                                       
HET    PO4  D 502       5                                                       
HET    PO4  D 503       5                                                       
HET    GOL  D 504       6                                                       
HET    GOL  D 505       6                                                       
HET    GOL  D 506       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  GOL    5(C3 H8 O3)                                                  
FORMUL   9  PO4    3(O4 P 3-)                                                   
FORMUL  17  HOH   *1047(H2 O)                                                   
HELIX    1 AA1 PRO A   33  PHE A   35  5                                   3    
HELIX    2 AA2 TYR A   36  HIS A   45  1                                  10    
HELIX    3 AA3 HIS A   45  GLY A   53  1                                   9    
HELIX    4 AA4 GLN A   54  LYS A   61  1                                   8    
HELIX    5 AA5 SER A   66  LEU A   70  5                                   5    
HELIX    6 AA6 ASP A   72  GLY A   93  1                                  22    
HELIX    7 AA7 PRO A  104  GLU A  119  1                                  16    
HELIX    8 AA8 VAL A  125  VAL A  130  1                                   6    
HELIX    9 AA9 THR A  144  GLU A  146  5                                   3    
HELIX   10 AB1 CYS A  159  LYS A  179  1                                  21    
HELIX   11 AB2 VAL A  180  MET A  190  1                                  11    
HELIX   12 AB3 GLU A  192  HIS A  215  1                                  24    
HELIX   13 AB4 HIS A  215  VAL A  221  1                                   7    
HELIX   14 AB5 ASN A  222  VAL A  229  1                                   8    
HELIX   15 AB6 VAL A  229  SER A  235  1                                   7    
HELIX   16 AB7 ASN A  240  SER A  244  5                                   5    
HELIX   17 AB8 SER A  263  SER A  267  5                                   5    
HELIX   18 AB9 SER A  268  LEU A  277  1                                  10    
HELIX   19 AC1 GLY A  286  ARG A  297  1                                  12    
HELIX   20 AC2 PRO A  300  ASN A  313  1                                  14    
HELIX   21 AC3 SER A  315  SER A  322  1                                   8    
HELIX   22 AC4 ASP A  325  ILE A  354  1                                  30    
HELIX   23 AC5 ILE A  354  GLN A  360  1                                   7    
HELIX   24 AC6 THR A  382  SER A  398  1                                  17    
HELIX   25 AC7 PRO B   33  PHE B   35  5                                   3    
HELIX   26 AC8 TYR B   36  HIS B   45  1                                  10    
HELIX   27 AC9 HIS B   45  SER B   52  1                                   8    
HELIX   28 AD1 GLN B   54  LEU B   62  1                                   9    
HELIX   29 AD2 SER B   66  LEU B   70  5                                   5    
HELIX   30 AD3 ASP B   72  GLY B   93  1                                  22    
HELIX   31 AD4 PRO B  104  GLU B  119  1                                  16    
HELIX   32 AD5 VAL B  125  VAL B  130  1                                   6    
HELIX   33 AD6 THR B  144  GLU B  146  5                                   3    
HELIX   34 AD7 CYS B  159  LYS B  179  1                                  21    
HELIX   35 AD8 VAL B  180  MET B  190  1                                  11    
HELIX   36 AD9 GLU B  192  HIS B  215  1                                  24    
HELIX   37 AE1 GLN B  216  VAL B  221  1                                   6    
HELIX   38 AE2 ASN B  222  VAL B  229  1                                   8    
HELIX   39 AE3 VAL B  229  SER B  235  1                                   7    
HELIX   40 AE4 ASN B  240  SER B  244  5                                   5    
HELIX   41 AE5 SER B  263  SER B  267  5                                   5    
HELIX   42 AE6 SER B  268  LEU B  277  1                                  10    
HELIX   43 AE7 GLY B  286  ARG B  296  1                                  11    
HELIX   44 AE8 ARG B  297  MET B  299  5                                   3    
HELIX   45 AE9 PRO B  300  ASN B  313  1                                  14    
HELIX   46 AF1 SER B  315  SER B  322  1                                   8    
HELIX   47 AF2 ASP B  325  ILE B  354  1                                  30    
HELIX   48 AF3 ILE B  354  GLN B  360  1                                   7    
HELIX   49 AF4 GLY B  378  LYS B  397  1                                  20    
HELIX   50 AF5 PRO C   33  PHE C   35  5                                   3    
HELIX   51 AF6 TYR C   36  HIS C   45  1                                  10    
HELIX   52 AF7 HIS C   45  GLY C   53  1                                   9    
HELIX   53 AF8 GLN C   54  LYS C   61  1                                   8    
HELIX   54 AF9 SER C   66  LEU C   70  5                                   5    
HELIX   55 AG1 ASP C   72  GLY C   93  1                                  22    
HELIX   56 AG2 PRO C  104  GLU C  119  1                                  16    
HELIX   57 AG3 VAL C  125  VAL C  130  1                                   6    
HELIX   58 AG4 THR C  144  GLU C  146  5                                   3    
HELIX   59 AG5 CYS C  159  LYS C  179  1                                  21    
HELIX   60 AG6 VAL C  180  MET C  190  1                                  11    
HELIX   61 AG7 GLU C  192  HIS C  215  1                                  24    
HELIX   62 AG8 HIS C  215  VAL C  221  1                                   7    
HELIX   63 AG9 ASN C  222  VAL C  229  1                                   8    
HELIX   64 AH1 VAL C  229  SER C  235  1                                   7    
HELIX   65 AH2 ASN C  240  SER C  244  5                                   5    
HELIX   66 AH3 SER C  263  SER C  267  5                                   5    
HELIX   67 AH4 SER C  268  GLY C  278  1                                  11    
HELIX   68 AH5 GLY C  286  ARG C  297  1                                  12    
HELIX   69 AH6 PRO C  300  ASN C  313  1                                  14    
HELIX   70 AH7 SER C  315  SER C  322  1                                   8    
HELIX   71 AH8 ASP C  325  ILE C  354  1                                  30    
HELIX   72 AH9 ILE C  354  GLN C  360  1                                   7    
HELIX   73 AI1 GLY C  381  SER C  398  1                                  18    
HELIX   74 AI2 PRO D   33  PHE D   35  5                                   3    
HELIX   75 AI3 TYR D   36  HIS D   45  1                                  10    
HELIX   76 AI4 HIS D   45  SER D   52  1                                   8    
HELIX   77 AI5 GLN D   54  LEU D   62  1                                   9    
HELIX   78 AI6 SER D   66  LEU D   70  5                                   5    
HELIX   79 AI7 ASP D   72  GLY D   93  1                                  22    
HELIX   80 AI8 PRO D  104  GLU D  119  1                                  16    
HELIX   81 AI9 VAL D  125  VAL D  130  1                                   6    
HELIX   82 AJ1 THR D  144  GLU D  146  5                                   3    
HELIX   83 AJ2 CYS D  159  LYS D  179  1                                  21    
HELIX   84 AJ3 VAL D  180  MET D  190  1                                  11    
HELIX   85 AJ4 GLU D  192  HIS D  215  1                                  24    
HELIX   86 AJ5 GLN D  216  VAL D  221  1                                   6    
HELIX   87 AJ6 ASN D  222  VAL D  229  1                                   8    
HELIX   88 AJ7 VAL D  229  SER D  235  1                                   7    
HELIX   89 AJ8 ASN D  240  SER D  244  5                                   5    
HELIX   90 AJ9 SER D  263  SER D  267  5                                   5    
HELIX   91 AK1 SER D  268  LEU D  277  1                                  10    
HELIX   92 AK2 GLY D  286  ARG D  297  1                                  12    
HELIX   93 AK3 PRO D  300  SER D  312  1                                  13    
HELIX   94 AK4 SER D  315  SER D  322  1                                   8    
HELIX   95 AK5 ASP D  325  ILE D  354  1                                  30    
HELIX   96 AK6 ILE D  354  GLN D  360  1                                   7    
HELIX   97 AK7 GLY D  381  LYS D  397  1                                  17    
SHEET    1 AA1 2 VAL A 102  LEU A 103  0                                        
SHEET    2 AA1 2 VAL A 248  TYR A 249  1  O  VAL A 248   N  LEU A 103           
SHEET    1 AA2 2 LYS A 135  LYS A 136  0                                        
SHEET    2 AA2 2 MET A 148  ASP A 149 -1  O  ASP A 149   N  LYS A 135           
SHEET    1 AA3 2 VAL B 102  LEU B 103  0                                        
SHEET    2 AA3 2 VAL B 248  TYR B 249  1  O  VAL B 248   N  LEU B 103           
SHEET    1 AA4 2 LYS B 135  LYS B 136  0                                        
SHEET    2 AA4 2 MET B 148  ASP B 149 -1  O  ASP B 149   N  LYS B 135           
SHEET    1 AA5 2 VAL C 102  LEU C 103  0                                        
SHEET    2 AA5 2 VAL C 248  TYR C 249  1  O  VAL C 248   N  LEU C 103           
SHEET    1 AA6 2 LYS C 135  LYS C 136  0                                        
SHEET    2 AA6 2 MET C 148  ASP C 149 -1  O  ASP C 149   N  LYS C 135           
SHEET    1 AA7 2 VAL D 102  LEU D 103  0                                        
SHEET    2 AA7 2 VAL D 248  TYR D 249  1  O  VAL D 248   N  LEU D 103           
SHEET    1 AA8 2 LYS D 135  LYS D 136  0                                        
SHEET    2 AA8 2 MET D 148  ASP D 149 -1  O  ASP D 149   N  LYS D 135           
LINK         NE2 HIS A 346                FE   HEM A 501     1555   1555  2.23  
LINK         NE2 HIS B 346                FE   HEM B 501     1555   1555  2.22  
LINK         NE2 HIS C 346                FE   HEM C 501     1555   1555  2.07  
LINK         NE2 HIS D 346                FE   HEM D 501     1555   1555  2.17  
SITE     1 AC1 19 TYR A 126  SER A 167  VAL A 170  PHE A 214                    
SITE     2 AC1 19 PHE A 226  SER A 263  ALA A 264  GLY A 265                    
SITE     3 AC1 19 PHE A 270  PHE A 291  ARG A 343  HIS A 346                    
SITE     4 AC1 19 ILE A 349  TYR A 353  ILE A 354  LEU A 384                    
SITE     5 AC1 19 VAL A 391  HOH A 633  HOH A 680                               
SITE     1 AC2  6 LEU A 234  GLY A 236  GLY A 261  GLY A 262                    
SITE     2 AC2  6 HOH A 610  HOH A 716                                          
SITE     1 AC3  6 CYS A 159  ASN A 222  GLN B 212  HIS B 215                    
SITE     2 AC3  6 ASP B 219  HOH B 652                                          
SITE     1 AC4 19 TYR B 126  SER B 167  VAL B 170  PHE B 214                    
SITE     2 AC4 19 ILE B 217  PHE B 226  SER B 263  ALA B 264                    
SITE     3 AC4 19 GLY B 265  PHE B 270  PHE B 291  ARG B 343                    
SITE     4 AC4 19 HIS B 346  ILE B 349  ILE B 354  LEU B 384                    
SITE     5 AC4 19 VAL B 391  HOH B 625  HOH B 768                               
SITE     1 AC5  7 HIS A 218  HOH A 640  HIS B 215  TYR B 345                    
SITE     2 AC5  7 GLN B 348  HOH B 716  HOH B 787                               
SITE     1 AC6 20 TYR C 126  PHE C 163  SER C 167  VAL C 170                    
SITE     2 AC6 20 PHE C 214  PHE C 226  SER C 263  ALA C 264                    
SITE     3 AC6 20 GLY C 265  PHE C 270  PHE C 291  ARG C 343                    
SITE     4 AC6 20 HIS C 346  ILE C 349  TYR C 353  ILE C 354                    
SITE     5 AC6 20 LEU C 384  VAL C 391  HOH C 615  HOH C 744                    
SITE     1 AC7 20 TYR D 126  SER D 167  VAL D 170  PHE D 214                    
SITE     2 AC7 20 ILE D 217  PHE D 226  SER D 263  ALA D 264                    
SITE     3 AC7 20 GLY D 265  PHE D 270  PHE D 291  ARG D 343                    
SITE     4 AC7 20 HIS D 346  ILE D 349  TYR D 353  ILE D 354                    
SITE     5 AC7 20 LEU D 384  VAL D 391  HOH D 610  HOH D 768                    
SITE     1 AC8  5 PRO A  33  ASP A  34  HOH A 624  GLU D  60                    
SITE     2 AC8  5 ARG D 100                                                     
SITE     1 AC9  9 HIS C 218  HOH C 646  HOH C 682  HIS D 215                    
SITE     2 AC9  9 TYR D 345  GLN D 348  HOH D 606  HOH D 672                    
SITE     3 AC9  9 HOH D 812                                                     
SITE     1 AD1  6 GLY D 236  TRP D 237  LYS D 238  ALA D 260                    
SITE     2 AD1  6 GLY D 261  HOH D 717                                          
SITE     1 AD2  7 HOH C 726  HIS D  16  GLU D 119  PRO D 301                    
SITE     2 AD2  7 ALA D 302  HOH D 689  HOH D 753                               
SITE     1 AD3  3 GLU D  60  LYS D  61  HOH D 607                               
CRYST1   79.969  196.538  116.207  90.00  90.00  90.00 P 21 21 2    16          
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      0.012505  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005088  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008605        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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