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Database: PDB
Entry: 2Q32
LinkDB: 2Q32
Original site: 2Q32 
HEADER    OXIDOREDUCTASE                          29-MAY-07   2Q32              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-2 C127A (HO-2)              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEME OXYGENASE 2;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HO-2;                                                       
COMPND   5 EC: 1.14.99.3;                                                       
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: HS.284279, HMOX2, HO2;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T-2                                 
KEYWDS    HO-2, HEME OXYGENASE, STRUCTURAL GENOMICS MEDICAL RELEVANCE,          
KEYWDS   2 STRUCTURAL GENOMICS COMMUNITY REQUEST, PROTEIN STRUCTURE INITIATIVE, 
KEYWDS   3 PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, OXIDOREDUCTASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.BIANCHETTI,C.A.BINGMAN,E.BITTO,G.E.WESENBERG,G.N.PHILLIPS JR.,    
AUTHOR   2 CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)                     
REVDAT   5   18-OCT-17 2Q32    1       REMARK                                   
REVDAT   4   13-JUL-11 2Q32    1       VERSN                                    
REVDAT   3   24-FEB-09 2Q32    1       VERSN                                    
REVDAT   2   22-JAN-08 2Q32    1       JRNL                                     
REVDAT   1   05-JUN-07 2Q32    0                                                
JRNL        AUTH   C.M.BIANCHETTI,L.YI,S.W.RAGSDALE,G.N.PHILLIPS JR.            
JRNL        TITL   COMPARISON OF APO- AND HEME-BOUND CRYSTAL STRUCTURES OF A    
JRNL        TITL 2 TRUNCATED HUMAN HEME OXYGENASE-2.                            
JRNL        REF    J.BIOL.CHEM.                  V. 282 37624 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17965015                                                     
JRNL        DOI    10.1074/JBC.M707396200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 25217                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.056                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1275                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1552                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3538                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.31500                                             
REMARK   3    B22 (A**2) : -1.04900                                             
REMARK   3    B33 (A**2) : 3.36400                                              
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): 0.331         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.022        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3770 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5072 ; 1.255 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   447 ; 5.145 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   207 ;36.670 ;25.072       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   689 ;16.946 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;22.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   517 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2899 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1825 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2601 ; 0.294 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   191 ; 0.155 ; 0.200       
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):    19 ; 0.103 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.286 ; 0.200       
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):  2272 ; 0.514 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3520 ; 0.799 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1688 ; 1.232 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1552 ; 1.966 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     30       A     240      4                      
REMARK   3           1     B     31       B     240      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1675 ; 0.470 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1675 ; 0.630 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 8                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    29        A    42                          
REMARK   3    RESIDUE RANGE :   A    43        A    62                          
REMARK   3    RESIDUE RANGE :   A    63        A   133                          
REMARK   3    RESIDUE RANGE :   A   134        A   162                          
REMARK   3    RESIDUE RANGE :   A   163        A   181                          
REMARK   3    RESIDUE RANGE :   A   182        A   203                          
REMARK   3    RESIDUE RANGE :   A   204        A   229                          
REMARK   3    RESIDUE RANGE :   A   230        A   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6580  21.8173   6.7170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2701 T22:  -0.2374                                     
REMARK   3      T33:  -0.1773 T12:   0.0546                                     
REMARK   3      T13:  -0.0441 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3867 L22:   2.1547                                     
REMARK   3      L33:   2.1897 L12:   0.9854                                     
REMARK   3      L13:  -0.1486 L23:  -0.3659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:  -0.0481 S13:  -0.1587                       
REMARK   3      S21:   0.1784 S22:  -0.0279 S23:   0.0297                       
REMARK   3      S31:  -0.0414 S32:  -0.0759 S33:   0.0278                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 9                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    31        B    43                          
REMARK   3    RESIDUE RANGE :   B    44        B    65                          
REMARK   3    RESIDUE RANGE :   B    66        B   115                          
REMARK   3    RESIDUE RANGE :   B   116        B   132                          
REMARK   3    RESIDUE RANGE :   B   133        B   154                          
REMARK   3    RESIDUE RANGE :   B   155        B   176                          
REMARK   3    RESIDUE RANGE :   B   177        B   196                          
REMARK   3    RESIDUE RANGE :   B   197        B   218                          
REMARK   3    RESIDUE RANGE :   B   219        B   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.6902  15.5956  29.4417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1437 T22:  -0.0656                                     
REMARK   3      T33:  -0.0598 T12:   0.0096                                     
REMARK   3      T13:  -0.0572 T23:   0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1248 L22:   4.5599                                     
REMARK   3      L33:   4.4445 L12:   0.7763                                     
REMARK   3      L13:   0.3817 L23:  -1.6589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0218 S12:   0.0029 S13:   0.2004                       
REMARK   3      S21:   0.1975 S22:  -0.2365 S23:  -0.7597                       
REMARK   3      S31:  -0.2125 S32:   0.8885 S33:   0.2147                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
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 2Q32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000043086.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97933                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : ADJUSTABLE FOCUSING MIRRORS IN K   
REMARK 200                                   -B GEOMETRY                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28128                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.148                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5050                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.929                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1N45                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (5 MG/ML PROTEIN,       
REMARK 280  0.050 M POTASSIUM CHLORIDE, 0.005 M TRIS-HCL PH 8.5) MIXED IN A     
REMARK 280  1.5:1 RATIO WITH THE WELL SOLUTION (40% PEG 1500, 0.20 M            
REMARK 280  POTASSIUM GLUTAMATE, 0.10 M TRIETHANOLAMINE, PH 8.5).               
REMARK 280  CRYOPROTECTED WITH WELL SOLUTION, VAPOR DIFUSSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K, VAPOR DIFFUSION, HANGING DROP                     
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       37.88450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.87650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.00850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.87650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.88450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.00850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER  (CHAINS A & B IN ASU).       
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     LYS A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     SER A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     ALA A   245                                                      
REMARK 465     ARG A   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     THR A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     GLU A   250                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     PHE A   253                                                      
REMARK 465     PRO A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     HIS A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     ASP A   261                                                      
REMARK 465     MET A   262                                                      
REMARK 465     ARG A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     ASN B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     ALA B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     GLN B    27                                                      
REMARK 465     MET B    28                                                      
REMARK 465     ARG B    29                                                      
REMARK 465     MET B    30                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     GLY B   252                                                      
REMARK 465     PHE B   253                                                      
REMARK 465     PRO B   254                                                      
REMARK 465     VAL B   255                                                      
REMARK 465     HIS B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     ASP B   261                                                      
REMARK 465     MET B   262                                                      
REMARK 465     ARG B   263                                                      
REMARK 465     LYS B   264                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 123   CG    GLU B 123   CD      0.185                       
REMARK 500    GLU B 123   CD    GLU B 123   OE2     0.166                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 156   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 156   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLU B 123   OE1 -  CD  -  OE2 ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 120       51.07   -101.01                                   
REMARK 500    ASN A 120       51.07    -99.14                                   
REMARK 500    ASN A 144      -39.41   -133.06                                   
REMARK 500    ARG A 156      -71.40    -66.71                                   
REMARK 500    PHE B  94      -31.69   -135.71                                   
REMARK 500    ASN B 144      -34.10   -133.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OXN A  301                                                       
REMARK 610     OXN B  301                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXN A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXN B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: GO.91265   RELATED DB: TARGETDB                          
DBREF  2Q32 A    1   264  UNP    P30519   HMOX2_HUMAN      1    264             
DBREF  2Q32 B    1   264  UNP    P30519   HMOX2_HUMAN      1    264             
SEQADV 2Q32 ALA A  127  UNP  P30519    CYS   127 ENGINEERED                     
SEQADV 2Q32 ALA B  127  UNP  P30519    CYS   127 ENGINEERED                     
SEQRES   1 A  264  MET SER ALA GLU VAL GLU THR SER GLU GLY VAL ASP GLU          
SEQRES   2 A  264  SER GLU LYS LYS ASN SER GLY ALA LEU GLU LYS GLU ASN          
SEQRES   3 A  264  GLN MET ARG MET ALA ASP LEU SER GLU LEU LEU LYS GLU          
SEQRES   4 A  264  GLY THR LYS GLU ALA HIS ASP ARG ALA GLU ASN THR GLN          
SEQRES   5 A  264  PHE VAL LYS ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU          
SEQRES   6 A  264  LEU PHE LYS LEU ALA THR THR ALA LEU TYR PHE THR TYR          
SEQRES   7 A  264  SER ALA LEU GLU GLU GLU MET GLU ARG ASN LYS ASP HIS          
SEQRES   8 A  264  PRO ALA PHE ALA PRO LEU TYR PHE PRO MET GLU LEU HIS          
SEQRES   9 A  264  ARG LYS GLU ALA LEU THR LYS ASP MET GLU TYR PHE PHE          
SEQRES  10 A  264  GLY GLU ASN TRP GLU GLU GLN VAL GLN ALA PRO LYS ALA          
SEQRES  11 A  264  ALA GLN LYS TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN          
SEQRES  12 A  264  ASN GLU PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG          
SEQRES  13 A  264  TYR MET GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS          
SEQRES  14 A  264  VAL ALA GLN ARG ALA LEU LYS LEU PRO SER THR GLY GLU          
SEQRES  15 A  264  GLY THR GLN PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA          
SEQRES  16 A  264  GLN GLN PHE LYS GLN LEU TYR ARG ALA ARG MET ASN ALA          
SEQRES  17 A  264  LEU ASP LEU ASN MET LYS THR LYS GLU ARG ILE VAL GLU          
SEQRES  18 A  264  GLU ALA ASN LYS ALA PHE GLU TYR ASN MET GLN ILE PHE          
SEQRES  19 A  264  ASN GLU LEU ASP GLN ALA GLY SER THR LEU ALA ARG GLU          
SEQRES  20 A  264  THR LEU GLU ASP GLY PHE PRO VAL HIS ASP GLY LYS GLY          
SEQRES  21 A  264  ASP MET ARG LYS                                              
SEQRES   1 B  264  MET SER ALA GLU VAL GLU THR SER GLU GLY VAL ASP GLU          
SEQRES   2 B  264  SER GLU LYS LYS ASN SER GLY ALA LEU GLU LYS GLU ASN          
SEQRES   3 B  264  GLN MET ARG MET ALA ASP LEU SER GLU LEU LEU LYS GLU          
SEQRES   4 B  264  GLY THR LYS GLU ALA HIS ASP ARG ALA GLU ASN THR GLN          
SEQRES   5 B  264  PHE VAL LYS ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU          
SEQRES   6 B  264  LEU PHE LYS LEU ALA THR THR ALA LEU TYR PHE THR TYR          
SEQRES   7 B  264  SER ALA LEU GLU GLU GLU MET GLU ARG ASN LYS ASP HIS          
SEQRES   8 B  264  PRO ALA PHE ALA PRO LEU TYR PHE PRO MET GLU LEU HIS          
SEQRES   9 B  264  ARG LYS GLU ALA LEU THR LYS ASP MET GLU TYR PHE PHE          
SEQRES  10 B  264  GLY GLU ASN TRP GLU GLU GLN VAL GLN ALA PRO LYS ALA          
SEQRES  11 B  264  ALA GLN LYS TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN          
SEQRES  12 B  264  ASN GLU PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG          
SEQRES  13 B  264  TYR MET GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS          
SEQRES  14 B  264  VAL ALA GLN ARG ALA LEU LYS LEU PRO SER THR GLY GLU          
SEQRES  15 B  264  GLY THR GLN PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA          
SEQRES  16 B  264  GLN GLN PHE LYS GLN LEU TYR ARG ALA ARG MET ASN ALA          
SEQRES  17 B  264  LEU ASP LEU ASN MET LYS THR LYS GLU ARG ILE VAL GLU          
SEQRES  18 B  264  GLU ALA ASN LYS ALA PHE GLU TYR ASN MET GLN ILE PHE          
SEQRES  19 B  264  ASN GLU LEU ASP GLN ALA GLY SER THR LEU ALA ARG GLU          
SEQRES  20 B  264  THR LEU GLU ASP GLY PHE PRO VAL HIS ASP GLY LYS GLY          
SEQRES  21 B  264  ASP MET ARG LYS                                              
HET    OXN  A 301      32                                                       
HET    OXN  B 301      38                                                       
HETNAM     OXN OXTOXYNOL-10                                                     
HETSYN     OXN ALPHA-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENYL]-OMEGA-                
HETSYN   2 OXN  HYDROXYPOLY(OXY-1,2-ETHANEDIYL); TRITON X-100                   
FORMUL   3  OXN    2(C34 H62 O11)                                               
FORMUL   5  HOH   *154(H2 O)                                                    
HELIX    1   1 ASP A   32  THR A   41  1                                  10    
HELIX    2   2 THR A   41  ASN A   50  1                                  10    
HELIX    3   3 THR A   51  LYS A   59  1                                   9    
HELIX    4   4 LYS A   63  ASN A   88  1                                  26    
HELIX    5   5 PHE A   94  TYR A   98  5                                   5    
HELIX    6   6 PHE A   99  HIS A  104  1                                   6    
HELIX    7   7 ARG A  105  GLY A  118  1                                  14    
HELIX    8   8 ASN A  120  VAL A  125  5                                   6    
HELIX    9   9 PRO A  128  GLU A  145  1                                  18    
HELIX   10  10 LEU A  148  LYS A  176  1                                  29    
HELIX   11  11 THR A  184  LEU A  188  5                                   5    
HELIX   12  12 ASN A  194  LEU A  209  1                                  16    
HELIX   13  13 ASN A  212  GLN A  239  1                                  28    
HELIX   14  14 ASP B   32  THR B   41  1                                  10    
HELIX   15  15 THR B   41  ASN B   50  1                                  10    
HELIX   16  16 THR B   51  GLY B   60  1                                  10    
HELIX   17  17 LYS B   63  ASN B   88  1                                  26    
HELIX   18  18 PHE B   94  TYR B   98  5                                   5    
HELIX   19  19 PHE B   99  HIS B  104  1                                   6    
HELIX   20  20 ARG B  105  GLY B  118  1                                  14    
HELIX   21  21 ASN B  120  GLN B  124  5                                   5    
HELIX   22  22 PRO B  128  GLU B  145  1                                  18    
HELIX   23  23 LEU B  148  LYS B  176  1                                  29    
HELIX   24  24 THR B  184  LEU B  188  5                                   5    
HELIX   25  25 ASN B  194  LEU B  209  1                                  16    
HELIX   26  26 ASN B  212  THR B  243  1                                  32    
SITE     1 AC1 14 GLU A  49  VAL A  54  PHE A  57  LEU A  74                    
SITE     2 AC1 14 TYR A 134  THR A 155  ARG A 156  LEU A 167                    
SITE     3 AC1 14 TYR A 187  ALA A 226  PHE A 227  ASN A 230                    
SITE     4 AC1 14 PHE A 234  HOH A 390                                          
SITE     1 AC2 14 PHE B  53  VAL B  54  TYR B 134  THR B 155                    
SITE     2 AC2 14 ARG B 156  GLY B 159  ASP B 160  GLY B 163                    
SITE     3 AC2 14 LEU B 167  ALA B 226  PHE B 227  ASN B 230                    
SITE     4 AC2 14 ILE B 233  PHE B 234                                          
CRYST1   75.769   86.017   97.753  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      0.013198  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011626  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010230        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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