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Database: PDB
Entry: 5WMW
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HEADER    OXIDOREDUCTASE                          31-JUL-17   5WMW              
TITLE     STRUCTURAL INSIGHTS INTO SUBSTRATE AND INHIBITOR BINDING SITES IN     
TITLE    2 HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDOLEAMINE 2,3-DIOXYGENASE 1;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: IDO-1,INDOLEAMINE-PYRROLE 2,3-DIOXYGENASE;                  
COMPND   5 EC: 1.13.11.52;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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                                         
KEYWDS    DIOXYGENASE TRYPTOPHAN HEME INHIBITOR, OXIDOREDUCTASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LEWIS-BALLESTER,S.R.YEH,K.N.PHAM,D.BATABYAL,S.KARKASHON,            
AUTHOR   2 J.B.BONANNO,T.L.POULOS                                               
REVDAT   2   27-NOV-19 5WMW    1       REMARK                                   
REVDAT   1   06-DEC-17 5WMW    0                                                
JRNL        AUTH   A.LEWIS-BALLESTER,K.N.PHAM,D.BATABYAL,S.KARKASHON,           
JRNL        AUTH 2 J.B.BONANNO,T.L.POULOS,S.R.YEH                               
JRNL        TITL   STRUCTURAL INSIGHTS INTO SUBSTRATE AND INHIBITOR BINDING     
JRNL        TITL 2 SITES IN HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1.                
JRNL        REF    NAT COMMUN                    V.   8  1693 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29167421                                                     
JRNL        DOI    10.1038/S41467-017-01725-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19850                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.03                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1380                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.3950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5998                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 150                                     
REMARK   3   SOLVENT ATOMS            : 104                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.81000                                              
REMARK   3    B22 (A**2) : -4.71000                                             
REMARK   3    B33 (A**2) : 2.90000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.456         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.396         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.739        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6306 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5892 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8550 ; 1.020 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13670 ; 0.848 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   756 ; 4.997 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   275 ;32.787 ;24.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1089 ;12.908 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ; 9.329 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   923 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6942 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1292 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3050 ; 0.765 ; 7.503       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3049 ; 0.765 ; 7.501       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3796 ; 1.384 ;11.239       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3797 ; 1.384 ;11.242       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3256 ; 0.508 ; 7.533       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3256 ; 0.508 ; 7.533       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4755 ; 0.951 ;11.289       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  7103 ; 3.442 ;87.278       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  7104 ; 3.441 ;87.298       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A   503                          
REMARK   3    ORIGIN FOR THE GROUP (A): 203.1566  98.5533 143.3761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0436 T22:   0.2443                                     
REMARK   3      T33:   0.3795 T12:   0.0400                                     
REMARK   3      T13:  -0.0255 T23:   0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4521 L22:   2.6099                                     
REMARK   3      L33:   1.9672 L12:  -0.2857                                     
REMARK   3      L13:   1.0829 L23:  -0.5163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1195 S12:  -0.0721 S13:  -0.0383                       
REMARK   3      S21:   0.2421 S22:  -0.1254 S23:  -0.6873                       
REMARK   3      S31:  -0.0007 S32:   0.4891 S33:   0.2449                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    13        B   502                          
REMARK   3    ORIGIN FOR THE GROUP (A): 187.5981 127.7736 154.7252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0212 T22:   0.0990                                     
REMARK   3      T33:   0.2329 T12:  -0.0273                                     
REMARK   3      T13:  -0.0144 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7197 L22:   1.2136                                     
REMARK   3      L33:   1.8510 L12:   0.9430                                     
REMARK   3      L13:  -2.4322 L23:  -0.4486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:  -0.2715 S13:  -0.1275                       
REMARK   3      S21:   0.1179 S22:  -0.1132 S23:  -0.0498                       
REMARK   3      S31:  -0.0718 S32:   0.3285 S33:   0.0995                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 0                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2094 T22:   0.2094                                     
REMARK   3      T33:   0.2094 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5WMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229284.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10                                 
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21897                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.030                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.7.17                                         
REMARK 200 STARTING MODEL: 2D0T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM THIOSULFATE, 100 MM PH     
REMARK 280  10.0 CAPS BUFFER, AND 20% (W/V) PEG 8000, MICROBATCH,               
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       44.09600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.93150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.95350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.93150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.09600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.95350            
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                                                    
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 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    11                                                      
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     GLU A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     GLY A   405                                                      
REMARK 465     GLU A   406                                                      
REMARK 465     LEU A   407                                                      
REMARK 465     ASN A   408                                                      
REMARK 465     SER A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     LEU A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     LYS A   414                                                      
REMARK 465     PRO A   415                                                      
REMARK 465     ILE A   416                                                      
REMARK 465     PRO A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     PRO A   419                                                      
REMARK 465     LEU A   420                                                      
REMARK 465     LEU A   421                                                      
REMARK 465     GLY A   422                                                      
REMARK 465     LEU A   423                                                      
REMARK 465     ASP A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     THR A   426                                                      
REMARK 465     ARG A   427                                                      
REMARK 465     THR A   428                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     MET B    11                                                      
REMARK 465     SER B    12                                                      
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     LYS B   404                                                      
REMARK 465     GLY B   405                                                      
REMARK 465     GLU B   406                                                      
REMARK 465     LEU B   407                                                      
REMARK 465     ASN B   408                                                      
REMARK 465     SER B   409                                                      
REMARK 465     LYS B   410                                                      
REMARK 465     LEU B   411                                                      
REMARK 465     GLU B   412                                                      
REMARK 465     GLY B   413                                                      
REMARK 465     LYS B   414                                                      
REMARK 465     PRO B   415                                                      
REMARK 465     ILE B   416                                                      
REMARK 465     PRO B   417                                                      
REMARK 465     ASN B   418                                                      
REMARK 465     PRO B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     LEU B   421                                                      
REMARK 465     GLY B   422                                                      
REMARK 465     LEU B   423                                                      
REMARK 465     ASP B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     THR B   426                                                      
REMARK 465     ARG B   427                                                      
REMARK 465     THR B   428                                                      
REMARK 465     GLY B   429                                                      
REMARK 465     HIS B   430                                                      
REMARK 465     HIS B   431                                                      
REMARK 465     HIS B   432                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
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    ASN A  27       72.17     51.98                                   
REMARK 500    TYR A  36       42.98   -108.54                                   
REMARK 500    LEU A  62      107.82   -164.09                                   
REMARK 500    HIS A  69       54.45   -100.06                                   
REMARK 500    SER A 312       53.39    -90.00                                   
REMARK 500    PRO A 362     -176.50    -68.92                                   
REMARK 500    ASN B  27       75.81     59.24                                   
REMARK 500    HIS B  45       45.15   -107.91                                   
REMARK 500    ASN B 133       59.56   -108.38                                   
REMARK 500    PRO B 300      171.31    -57.24                                   
REMARK 500    ILE B 354      -57.13   -121.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 346   NE2                                                    
REMARK 620 2 HEM A 501   NA   89.5                                              
REMARK 620 3 HEM A 501   NB   90.3  89.6                                        
REMARK 620 4 HEM A 501   NC   91.6 178.5  89.4                                  
REMARK 620 5 HEM A 501   ND   90.6  90.8 179.0  90.2                            
REMARK 620 6 CYN A 502   C   173.1  83.9  87.8  94.9  91.4                      
REMARK 620 N                    1     2     3     4     5                       
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   89.5                                              
REMARK 620 3 HEM B 501   NB   91.0  89.7                                        
REMARK 620 4 HEM B 501   NC   91.8 178.4  89.4                                  
REMARK 620 5 HEM B 501   ND   89.8  90.9 179.0  90.0                            
REMARK 620 6 CYN B 502   C   178.9  91.4  88.3  87.3  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP B 504                 
DBREF  5WMW A   12   403  UNP    P14902   I23O1_HUMAN     12    403             
DBREF  5WMW B   12   403  UNP    P14902   I23O1_HUMAN     12    403             
SEQADV 5WMW MET A   11  UNP  P14902              INITIATING METHIONINE          
SEQADV 5WMW GLY A  270  UNP  P14902    PHE   270 ENGINEERED MUTATION            
SEQADV 5WMW LYS A  404  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY A  405  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLU A  406  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU A  407  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASN A  408  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW SER A  409  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LYS A  410  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU A  411  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLU A  412  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY A  413  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LYS A  414  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO A  415  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ILE A  416  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO A  417  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASN A  418  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO A  419  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU A  420  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU A  421  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY A  422  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU A  423  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASP A  424  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW SER A  425  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW THR A  426  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ARG A  427  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW THR A  428  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY A  429  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  430  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  431  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  432  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  433  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  434  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS A  435  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW MET B   11  UNP  P14902              INITIATING METHIONINE          
SEQADV 5WMW GLY B  270  UNP  P14902    PHE   270 ENGINEERED MUTATION            
SEQADV 5WMW LYS B  404  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY B  405  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLU B  406  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU B  407  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASN B  408  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW SER B  409  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LYS B  410  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU B  411  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLU B  412  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY B  413  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LYS B  414  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO B  415  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ILE B  416  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO B  417  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASN B  418  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW PRO B  419  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU B  420  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU B  421  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY B  422  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW LEU B  423  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ASP B  424  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW SER B  425  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW THR B  426  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW ARG B  427  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW THR B  428  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW GLY B  429  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  430  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  431  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  432  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  433  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  434  UNP  P14902              EXPRESSION TAG                 
SEQADV 5WMW HIS B  435  UNP  P14902              EXPRESSION TAG                 
SEQRES   1 A  425  MET SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE          
SEQRES   2 A  425  ALA LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR          
SEQRES   3 A  425  ASN ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU          
SEQRES   4 A  425  ILE GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU          
SEQRES   5 A  425  ASN MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER          
SEQRES   6 A  425  GLN ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET          
SEQRES   7 A  425  ALA TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS          
SEQRES   8 A  425  VAL LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU          
SEQRES   9 A  425  SER LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA          
SEQRES  10 A  425  ASP CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN          
SEQRES  11 A  425  LYS PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER          
SEQRES  12 A  425  PHE ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL          
SEQRES  13 A  425  SER LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS          
SEQRES  14 A  425  VAL ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU          
SEQRES  15 A  425  ARG ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER          
SEQRES  16 A  425  CYS LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS          
SEQRES  17 A  425  ASP HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG          
SEQRES  18 A  425  ILE TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER          
SEQRES  19 A  425  ASP GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS          
SEQRES  20 A  425  GLU PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL GLY          
SEQRES  21 A  425  GLN CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA          
SEQRES  22 A  425  GLY GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG          
SEQRES  23 A  425  ARG TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER          
SEQRES  24 A  425  LEU GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER          
SEQRES  25 A  425  LYS GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS          
SEQRES  26 A  425  VAL LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN          
SEQRES  27 A  425  ILE VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN          
SEQRES  28 A  425  PRO LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU          
SEQRES  29 A  425  GLU ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE          
SEQRES  30 A  425  LEU LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU          
SEQRES  31 A  425  LYS GLU GLY LYS GLY GLU LEU ASN SER LYS LEU GLU GLY          
SEQRES  32 A  425  LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR          
SEQRES  33 A  425  ARG THR GLY HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  425  MET SER LYS GLU TYR HIS ILE ASP GLU GLU VAL GLY PHE          
SEQRES   2 B  425  ALA LEU PRO ASN PRO GLN GLU ASN LEU PRO ASP PHE TYR          
SEQRES   3 B  425  ASN ASP TRP MET PHE ILE ALA LYS HIS LEU PRO ASP LEU          
SEQRES   4 B  425  ILE GLU SER GLY GLN LEU ARG GLU ARG VAL GLU LYS LEU          
SEQRES   5 B  425  ASN MET LEU SER ILE ASP HIS LEU THR ASP HIS LYS SER          
SEQRES   6 B  425  GLN ARG LEU ALA ARG LEU VAL LEU GLY CYS ILE THR MET          
SEQRES   7 B  425  ALA TYR VAL TRP GLY LYS GLY HIS GLY ASP VAL ARG LYS          
SEQRES   8 B  425  VAL LEU PRO ARG ASN ILE ALA VAL PRO TYR CYS GLN LEU          
SEQRES   9 B  425  SER LYS LYS LEU GLU LEU PRO PRO ILE LEU VAL TYR ALA          
SEQRES  10 B  425  ASP CYS VAL LEU ALA ASN TRP LYS LYS LYS ASP PRO ASN          
SEQRES  11 B  425  LYS PRO LEU THR TYR GLU ASN MET ASP VAL LEU PHE SER          
SEQRES  12 B  425  PHE ARG ASP GLY ASP CYS SER LYS GLY PHE PHE LEU VAL          
SEQRES  13 B  425  SER LEU LEU VAL GLU ILE ALA ALA ALA SER ALA ILE LYS          
SEQRES  14 B  425  VAL ILE PRO THR VAL PHE LYS ALA MET GLN MET GLN GLU          
SEQRES  15 B  425  ARG ASP THR LEU LEU LYS ALA LEU LEU GLU ILE ALA SER          
SEQRES  16 B  425  CYS LEU GLU LYS ALA LEU GLN VAL PHE HIS GLN ILE HIS          
SEQRES  17 B  425  ASP HIS VAL ASN PRO LYS ALA PHE PHE SER VAL LEU ARG          
SEQRES  18 B  425  ILE TYR LEU SER GLY TRP LYS GLY ASN PRO GLN LEU SER          
SEQRES  19 B  425  ASP GLY LEU VAL TYR GLU GLY PHE TRP GLU ASP PRO LYS          
SEQRES  20 B  425  GLU PHE ALA GLY GLY SER ALA GLY GLN SER SER VAL GLY          
SEQRES  21 B  425  GLN CYS PHE ASP VAL LEU LEU GLY ILE GLN GLN THR ALA          
SEQRES  22 B  425  GLY GLY GLY HIS ALA ALA GLN PHE LEU GLN ASP MET ARG          
SEQRES  23 B  425  ARG TYR MET PRO PRO ALA HIS ARG ASN PHE LEU CYS SER          
SEQRES  24 B  425  LEU GLU SER ASN PRO SER VAL ARG GLU PHE VAL LEU SER          
SEQRES  25 B  425  LYS GLY ASP ALA GLY LEU ARG GLU ALA TYR ASP ALA CYS          
SEQRES  26 B  425  VAL LYS ALA LEU VAL SER LEU ARG SER TYR HIS LEU GLN          
SEQRES  27 B  425  ILE VAL THR LYS TYR ILE LEU ILE PRO ALA SER GLN GLN          
SEQRES  28 B  425  PRO LYS GLU ASN LYS THR SER GLU ASP PRO SER LYS LEU          
SEQRES  29 B  425  GLU ALA LYS GLY THR GLY GLY THR ASP LEU MET ASN PHE          
SEQRES  30 B  425  LEU LYS THR VAL ARG SER THR THR GLU LYS SER LEU LEU          
SEQRES  31 B  425  LYS GLU GLY LYS GLY GLU LEU ASN SER LYS LEU GLU GLY          
SEQRES  32 B  425  LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR          
SEQRES  33 B  425  ARG THR GLY HIS HIS HIS HIS HIS HIS                          
HET    HEM  A 501      43                                                       
HET    CYN  A 502       2                                                       
HET    TRP  A 503      15                                                       
HET    TRP  A 504      15                                                       
HET    HEM  B 501      43                                                       
HET    CYN  B 502       2                                                       
HET    TRP  B 503      15                                                       
HET    TRP  B 504      15                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CYN CYANIDE ION                                                      
HETNAM     TRP TRYPTOPHAN                                                       
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  CYN    2(C N 1-)                                                    
FORMUL   5  TRP    4(C11 H12 N2 O2)                                             
FORMUL  11  HOH   *104(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 ASP A   72  GLY A   93  1                                  22    
HELIX    6 AA6 PRO A  104  GLU A  119  1                                  16    
HELIX    7 AA7 VAL A  125  VAL A  130  1                                   6    
HELIX    8 AA8 THR A  144  GLU A  146  5                                   3    
HELIX    9 AA9 CYS A  159  LYS A  179  1                                  21    
HELIX   10 AB1 VAL A  180  MET A  190  1                                  11    
HELIX   11 AB2 GLU A  192  HIS A  215  1                                  24    
HELIX   12 AB3 GLN A  216  VAL A  221  1                                   6    
HELIX   13 AB4 ASN A  222  VAL A  229  1                                   8    
HELIX   14 AB5 VAL A  229  SER A  235  1                                   7    
HELIX   15 AB6 ASN A  240  SER A  244  5                                   5    
HELIX   16 AB7 SER A  263  GLN A  266  5                                   4    
HELIX   17 AB8 SER A  267  LEU A  277  1                                  11    
HELIX   18 AB9 GLY A  286  MET A  295  1                                  10    
HELIX   19 AC1 PRO A  300  SER A  312  1                                  13    
HELIX   20 AC2 SER A  315  GLY A  324  1                                  10    
HELIX   21 AC3 ASP A  325  ILE A  354  1                                  30    
HELIX   22 AC4 ILE A  354  GLN A  361  1                                   8    
HELIX   23 AC5 ASP A  383  SER A  398  1                                  16    
HELIX   24 AC6 PRO B   33  PHE B   35  5                                   3    
HELIX   25 AC7 TYR B   36  HIS B   45  1                                  10    
HELIX   26 AC8 HIS B   45  GLY B   53  1                                   9    
HELIX   27 AC9 GLN B   54  LEU B   62  1                                   9    
HELIX   28 AD1 SER B   66  LEU B   70  5                                   5    
HELIX   29 AD2 ASP B   72  GLY B   93  1                                  22    
HELIX   30 AD3 PRO B  104  LEU B  118  1                                  15    
HELIX   31 AD4 VAL B  125  VAL B  130  1                                   6    
HELIX   32 AD5 CYS B  159  LYS B  179  1                                  21    
HELIX   33 AD6 VAL B  180  MET B  190  1                                  11    
HELIX   34 AD7 GLU B  192  HIS B  215  1                                  24    
HELIX   35 AD8 GLN B  216  VAL B  221  1                                   6    
HELIX   36 AD9 ASN B  222  VAL B  229  1                                   8    
HELIX   37 AE1 LEU B  230  SER B  235  5                                   6    
HELIX   38 AE2 SER B  267  LEU B  277  1                                  11    
HELIX   39 AE3 GLY B  286  ARG B  296  1                                  11    
HELIX   40 AE4 ARG B  297  MET B  299  5                                   3    
HELIX   41 AE5 PRO B  300  ASN B  313  1                                  14    
HELIX   42 AE6 SER B  315  GLY B  324  1                                  10    
HELIX   43 AE7 ASP B  325  ILE B  354  1                                  30    
HELIX   44 AE8 ILE B  354  GLN B  361  1                                   8    
HELIX   45 AE9 ASP B  383  SER B  398  1                                  16    
SHEET    1 AA1 3 VAL A 102  LEU A 103  0                                        
SHEET    2 AA1 3 LEU A 247  TYR A 249  1  O  VAL A 248   N  LEU A 103           
SHEET    3 AA1 3 PRO A 256  LYS A 257 -1  O  LYS A 257   N  LEU A 247           
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           
SSBOND   1 CYS A  308    CYS B  308                          1555   1555  2.03  
LINK         NE2 HIS A 346                FE   HEM A 501     1555   1555  1.88  
LINK         NE2 HIS B 346                FE   HEM B 501     1555   1555  1.89  
LINK         C   CYN A 502                FE   HEM A 501     1555   1555  1.93  
LINK         C   CYN B 502                FE   HEM B 501     1555   1555  1.94  
SITE     1 AC1 23 VAL A 170  PHE A 214  ILE A 217  PHE A 226                    
SITE     2 AC1 23 ALA A 264  GLY A 265  ARG A 343  HIS A 346                    
SITE     3 AC1 23 ILE A 349  VAL A 350  ILE A 354  GLY A 378                    
SITE     4 AC1 23 THR A 379  GLY A 380  GLY A 381  THR A 382                    
SITE     5 AC1 23 LEU A 384  PHE A 387  CYN A 502  TRP A 503                    
SITE     6 AC1 23 TRP A 504  HOH A 606  HOH A 610                               
SITE     1 AC2  4 SER A 263  ALA A 264  HEM A 501  TRP A 503                    
SITE     1 AC3 10 TYR A 126  PHE A 163  ARG A 231  GLY A 262                    
SITE     2 AC3 10 SER A 263  ILE A 354  GLY A 378  THR A 379                    
SITE     3 AC3 10 HEM A 501  CYN A 502                                          
SITE     1 AC4  9 VAL A 170  GLU A 171  ALA A 174  ALA A 210                    
SITE     2 AC4  9 VAL A 269  GLY A 270  ARG A 343  HIS A 346                    
SITE     3 AC4  9 HEM A 501                                                     
SITE     1 AC5 21 SER B 167  VAL B 170  PHE B 214  PHE B 226                    
SITE     2 AC5 21 SER B 263  ALA B 264  GLY B 265  ARG B 343                    
SITE     3 AC5 21 HIS B 346  ILE B 349  VAL B 350  TYR B 353                    
SITE     4 AC5 21 GLY B 378  THR B 379  GLY B 380  THR B 382                    
SITE     5 AC5 21 LEU B 384  PHE B 387  CYN B 502  TRP B 503                    
SITE     6 AC5 21 TRP B 504                                                     
SITE     1 AC6  4 SER B 263  ALA B 264  HEM B 501  TRP B 503                    
SITE     1 AC7 10 TYR B 126  PHE B 163  PHE B 226  ARG B 231                    
SITE     2 AC7 10 GLY B 262  SER B 263  ILE B 354  THR B 379                    
SITE     3 AC7 10 HEM B 501  CYN B 502                                          
SITE     1 AC8  8 VAL B 170  GLU B 171  ALA B 174  SER B 267                    
SITE     2 AC8  8 VAL B 269  GLY B 270  ARG B 343  HEM B 501                    
CRYST1   88.192   97.907  127.863  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011339  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007821        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system