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Database: PDB
Entry: 5YM3
LinkDB: 5YM3
Original site: 5YM3 
HEADER    OXIDOREDUCTASE                          20-OCT-17   5YM3              
TITLE     CYP76AH1-4PI FROM SALVIA MILTIORRHIZA                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERRUGINOL SYNTHASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOCHROME P450 76AH1;                                      
COMPND   5 EC: 1.14.13.190;                                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALVIA MILTIORRHIZA;                            
SOURCE   3 ORGANISM_COMMON: CHINESE SAGE;                                       
SOURCE   4 ORGANISM_TAXID: 226208;                                              
SOURCE   5 GENE: CYP76AH1;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-THERMUS THERMOPHILUS SHUTTLE     
SOURCE   7 VECTOR PTRH1T;                                                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1085940                                     
KEYWDS    P450, INHIBITOR, BIOSYNTHETIC PROTEIN, OXIDOREDUCTASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHANG                                                               
REVDAT   2   13-JAN-21 5YM3    1       JRNL                                     
REVDAT   1   24-OCT-18 5YM3    0                                                
JRNL        AUTH   M.GU,M.WANG,J.GUO,C.SHI,J.DENG,L.HUANG,L.HUANG,Z.CHANG       
JRNL        TITL   CRYSTAL STRUCTURE OF CYP76AH1 IN 4-PI-BOUND STATE FROM       
JRNL        TITL 2 SALVIA MILTIORRHIZA.                                         
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 511   813 2019              
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   30837155                                                     
JRNL        DOI    10.1016/J.BBRC.2019.02.103                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22391                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1144                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.1375 -  5.1985    0.98     2795   140  0.1421 0.1744        
REMARK   3     2  5.1985 -  4.1273    0.99     2731   139  0.1383 0.1562        
REMARK   3     3  4.1273 -  3.6059    0.99     2624   166  0.1608 0.2173        
REMARK   3     4  3.6059 -  3.2763    0.99     2670   151  0.1885 0.2621        
REMARK   3     5  3.2763 -  3.0415    1.00     2654   151  0.2150 0.2633        
REMARK   3     6  3.0415 -  2.8623    0.99     2626   142  0.2691 0.3441        
REMARK   3     7  2.8623 -  2.7189    1.00     2706   119  0.2535 0.2880        
REMARK   3     8  2.7189 -  2.6006    0.92     2441   136  0.3616 0.4301        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.150           
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      :  0.006           3839                                  
REMARK   3   ANGLE     :  0.929           5213                                  
REMARK   3   CHIRALITY :  0.035            567                                  
REMARK   3   PLANARITY :  0.004            675                                  
REMARK   3   DIHEDRAL  : 13.595           1443                                  
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 5YM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005527.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97979                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22668                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, JEFFAMINE M-600 REAGENT,          
REMARK 280  MANGANESE CHLORIDE, VAPOR DIFFUSION, TEMPERATURE 289K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.23633            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.47267            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.47267            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.23633            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
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 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     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     PHE A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     LYS A   494                                                      
REMARK 465     SER A   495                                                      
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 A   740     O    HOH A   745              2.11            
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    ILE A  37      -66.07     65.25                                   
REMARK 500    HIS A  86      -75.05   -105.60                                   
REMARK 500    ASP A 192       59.20    -97.68                                   
REMARK 500    ASP A 266       57.48   -107.42                                   
REMARK 500    SER A 300      -72.43    -82.53                                   
REMARK 500    LEU A 366     -138.66     46.54                                   
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                              MN A 503  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 102   ND1                                                    
REMARK 620 2 HOH A 608   O    73.7                                              
REMARK 620 N                    1                                               
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 CYS A 437   SG                                                     
REMARK 620 2 HEM A 501   NA   91.4                                              
REMARK 620 3 HEM A 501   NB   85.2  90.1                                        
REMARK 620 4 HEM A 501   NC   87.5 175.8  85.8                                  
REMARK 620 5 HEM A 501   ND   92.5  87.6 176.7  96.5                            
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 PIM A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 503                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5YLW   RELATED DB: PDB                                   
REMARK 900 5YLW CONTAINS THE SAME PROTEIN                                       
DBREF  5YM3 A    1   495  UNP    S4UX02   CYPH1_SALMI      1    495             
SEQRES   1 A  495  MET ASP SER PHE PRO LEU LEU ALA ALA LEU PHE PHE ILE          
SEQRES   2 A  495  ALA ALA THR ILE THR PHE LEU SER PHE ARG ARG ARG ARG          
SEQRES   3 A  495  ASN LEU PRO PRO GLY PRO PHE PRO TYR PRO ILE VAL GLY          
SEQRES   4 A  495  ASN MET LEU GLN LEU GLY ALA ASN PRO HIS GLN VAL PHE          
SEQRES   5 A  495  ALA LYS LEU SER LYS ARG TYR GLY PRO LEU MET SER ILE          
SEQRES   6 A  495  HIS LEU GLY SER LEU TYR THR VAL ILE VAL SER SER PRO          
SEQRES   7 A  495  GLU MET ALA LYS GLU ILE LEU HIS ARG HIS GLY GLN VAL          
SEQRES   8 A  495  PHE SER GLY ARG THR ILE ALA GLN ALA VAL HIS ALA CYS          
SEQRES   9 A  495  ASP HIS ASP LYS ILE SER MET GLY PHE LEU PRO VAL ALA          
SEQRES  10 A  495  SER GLU TRP ARG ASP MET ARG LYS ILE CYS LYS GLU GLN          
SEQRES  11 A  495  MET PHE SER ASN GLN SER MET GLU ALA SER GLN GLY LEU          
SEQRES  12 A  495  ARG ARG GLN LYS LEU GLN GLN LEU LEU ASP HIS VAL GLN          
SEQRES  13 A  495  LYS CYS SER ASP SER GLY ARG ALA VAL ASP ILE ARG GLU          
SEQRES  14 A  495  ALA ALA PHE ILE THR THR LEU ASN LEU MET SER ALA THR          
SEQRES  15 A  495  LEU PHE SER SER GLN ALA THR GLU PHE ASP SER LYS ALA          
SEQRES  16 A  495  THR MET GLU PHE LYS GLU ILE ILE GLU GLY VAL ALA THR          
SEQRES  17 A  495  ILE VAL GLY VAL PRO ASN PHE ALA ASP TYR PHE PRO ILE          
SEQRES  18 A  495  LEU ARG PRO PHE ASP PRO GLN GLY VAL LYS ARG ARG ALA          
SEQRES  19 A  495  ASP VAL PHE PHE GLY LYS LEU LEU ALA LYS ILE GLU GLY          
SEQRES  20 A  495  TYR LEU ASN GLU ARG LEU GLU SER LYS ARG ALA ASN PRO          
SEQRES  21 A  495  ASN ALA PRO LYS LYS ASP ASP PHE LEU GLU ILE VAL VAL          
SEQRES  22 A  495  ASP ILE ILE GLN ALA ASN GLU PHE LYS LEU LYS THR HIS          
SEQRES  23 A  495  HIS PHE THR HIS LEU MET LEU ASP LEU PHE VAL GLY GLY          
SEQRES  24 A  495  SER ASP THR ASN THR THR SER ILE GLU TRP ALA MET SER          
SEQRES  25 A  495  GLU LEU VAL MET ASN PRO ASP LYS MET ALA ARG LEU LYS          
SEQRES  26 A  495  ALA GLU LEU LYS SER VAL ALA GLY ASP GLU LYS ILE VAL          
SEQRES  27 A  495  ASP GLU SER ALA MET PRO LYS LEU PRO TYR LEU GLN ALA          
SEQRES  28 A  495  VAL ILE LYS GLU VAL MET ARG ILE HIS PRO PRO GLY PRO          
SEQRES  29 A  495  LEU LEU LEU PRO ARG LYS ALA GLU SER ASP GLN GLU VAL          
SEQRES  30 A  495  ASN GLY TYR LEU ILE PRO LYS GLY THR GLN ILE LEU ILE          
SEQRES  31 A  495  ASN ALA TYR ALA ILE GLY ARG ASP PRO SER ILE TRP THR          
SEQRES  32 A  495  ASP PRO GLU THR PHE ASP PRO GLU ARG PHE LEU ASP ASN          
SEQRES  33 A  495  LYS ILE ASP PHE LYS GLY GLN ASP TYR GLU LEU LEU PRO          
SEQRES  34 A  495  PHE GLY SER GLY ARG ARG VAL CYS PRO GLY MET PRO LEU          
SEQRES  35 A  495  ALA THR ARG ILE LEU HIS MET ALA THR ALA THR LEU VAL          
SEQRES  36 A  495  HIS ASN PHE ASP TRP LYS LEU GLU ASP ASP SER THR ALA          
SEQRES  37 A  495  ALA ALA ASP HIS ALA GLY GLU LEU PHE GLY VAL ALA VAL          
SEQRES  38 A  495  ARG ARG ALA VAL PRO LEU ARG ILE ILE PRO ILE VAL LYS          
SEQRES  39 A  495  SER                                                          
HET    HEM  A 501      43                                                       
HET    PIM  A 502      11                                                       
HET     MN  A 503       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     PIM 4-PHENYL-1H-IMIDAZOLE                                            
HETNAM      MN MANGANESE (II) ION                                               
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  PIM    C9 H8 N2                                                     
FORMUL   4   MN    MN 2+                                                        
FORMUL   5  HOH   *149(H2 O)                                                    
HELIX    1 AA1 ASN A   40  LEU A   44  5                                   5    
HELIX    2 AA2 ASN A   47  GLY A   60  1                                  14    
HELIX    3 AA3 SER A   77  HIS A   86  1                                  10    
HELIX    4 AA4 GLN A   99  CYS A  104  5                                   6    
HELIX    5 AA5 ASP A  105  SER A  110  1                                   6    
HELIX    6 AA6 ALA A  117  GLN A  130  1                                  14    
HELIX    7 AA7 SER A  133  SER A  140  1                                   8    
HELIX    8 AA8 SER A  140  GLY A  162  1                                  23    
HELIX    9 AA9 ILE A  167  SER A  185  1                                  19    
HELIX   10 AB1 SER A  193  GLY A  211  1                                  19    
HELIX   11 AB2 ASN A  214  TYR A  218  5                                   5    
HELIX   12 AB3 PHE A  219  ARG A  223  5                                   5    
HELIX   13 AB4 GLY A  229  ASN A  259  1                                  31    
HELIX   14 AB5 ASP A  267  ASN A  279  1                                  13    
HELIX   15 AB6 LYS A  284  GLY A  299  1                                  16    
HELIX   16 AB7 GLY A  299  ASN A  317  1                                  19    
HELIX   17 AB8 ASN A  317  GLY A  333  1                                  17    
HELIX   18 AB9 ASP A  339  LYS A  345  5                                   7    
HELIX   19 AC1 LEU A  346  HIS A  360  1                                  15    
HELIX   20 AC2 ASN A  391  ARG A  397  1                                   7    
HELIX   21 AC3 ASP A  409  LEU A  414  5                                   6    
HELIX   22 AC4 GLY A  439  PHE A  458  1                                  20    
HELIX   23 AC5 THR A  467  GLY A  474  1                                   8    
SHEET    1 AA1 4 LEU A  62  LEU A  67  0                                        
SHEET    2 AA1 4 LEU A  70  VAL A  75 -1  O  THR A  72   N  ILE A  65           
SHEET    3 AA1 4 GLN A 387  ILE A 390  1  O  GLN A 387   N  VAL A  73           
SHEET    4 AA1 4 ARG A 369  LYS A 370 -1  N  ARG A 369   O  ILE A 388           
SHEET    1 AA2 3 VAL A 165  ASP A 166  0                                        
SHEET    2 AA2 3 ARG A 488  ILE A 492 -1  O  ILE A 489   N  VAL A 165           
SHEET    3 AA2 3 ASP A 459  LEU A 462 -1  N  LYS A 461   O  ILE A 490           
SHEET    1 AA3 2 GLN A 375  VAL A 377  0                                        
SHEET    2 AA3 2 TYR A 380  ILE A 382 -1  O  TYR A 380   N  VAL A 377           
SHEET    1 AA4 2 GLU A 475  LEU A 476  0                                        
SHEET    2 AA4 2 ARG A 482  ARG A 483 -1  O  ARG A 482   N  LEU A 476           
LINK         ND1 HIS A 102                MN    MN A 503     1555   1555  2.43  
LINK         SG  CYS A 437                FE   HEM A 501     1555   1555  2.57  
LINK        MN    MN A 503                 O   HOH A 608     1555   1555  2.40  
SITE     1 AC1 25 ARG A  95  MET A 111  GLY A 112  TRP A 120                    
SITE     2 AC1 25 ARG A 124  PHE A 132  MET A 179  LEU A 295                    
SITE     3 AC1 25 GLY A 298  GLY A 299  THR A 302  ASN A 303                    
SITE     4 AC1 25 PRO A 362  LEU A 366  ARG A 369  PRO A 429                    
SITE     5 AC1 25 PHE A 430  GLY A 431  SER A 432  ARG A 435                    
SITE     6 AC1 25 VAL A 436  CYS A 437  PRO A 438  GLY A 439                    
SITE     7 AC1 25 ALA A 443                                                     
SITE     1 AC2  3 ASP A 294  GLY A 298  HOH A 676                               
SITE     1 AC3  2 HIS A 102  HOH A 608                                          
CRYST1  109.103  109.103  105.709  90.00  90.00 120.00 P 31 2 1      6          
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      0.009166  0.005292  0.000000        0.00000                         
SCALE2      0.000000  0.010584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009460        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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