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Database: PDB
Entry: 2QPP
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Original site: 2QPP 
HEADER    OXIDOREDUCTASE                          24-JUL-07   2QPP              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-2 C127A (HO-2) WITH BOUND   
TITLE    2 HEME                                                                 
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: 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, ENDOPLASMIC    
KEYWDS   4 RETICULUM, IRON, METAL-BINDING, MICROSOME, 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   25-OCT-17 2QPP    1       REMARK                                   
REVDAT   4   13-JUL-11 2QPP    1       VERSN                                    
REVDAT   3   24-FEB-09 2QPP    1       VERSN                                    
REVDAT   2   22-JAN-08 2QPP    1       JRNL                                     
REVDAT   1   07-AUG-07 2QPP    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.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19515                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
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) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1290                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.4130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3552                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 83                                      
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) : 65.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34000                                             
REMARK   3    B22 (A**2) : -1.21600                                             
REMARK   3    B33 (A**2) : 1.55500                                              
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): 0.549         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.228         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.685        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3734 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5049 ; 0.951 ; 2.029       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   433 ; 4.470 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   200 ;37.971 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   676 ;15.542 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;19.242 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   507 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2895 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1653 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2569 ; 0.290 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   132 ; 0.127 ; 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):    23 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.266 ; 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):  2238 ; 0.732 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3448 ; 1.234 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1735 ; 0.859 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1597 ; 1.167 ; 4.000       
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 : NULL                              
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 : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    29        A    86                          
REMARK   3    RESIDUE RANGE :   A    87        A   128                          
REMARK   3    RESIDUE RANGE :   A   129        A   202                          
REMARK   3    RESIDUE RANGE :   A   203        A   218                          
REMARK   3    RESIDUE RANGE :   A   219        A   242                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3659  21.7848   6.6330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1276 T22:  -0.1631                                     
REMARK   3      T33:  -0.0645 T12:   0.0463                                     
REMARK   3      T13:  -0.0738 T23:  -0.0739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7934 L22:   2.6104                                     
REMARK   3      L33:   2.5292 L12:   0.8189                                     
REMARK   3      L13:   0.1946 L23:  -0.1534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:   0.2683 S13:  -0.2849                       
REMARK   3      S21:  -0.0017 S22:   0.0709 S23:  -0.0175                       
REMARK   3      S31:   0.1109 S32:  -0.1057 S33:  -0.0664                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 6                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    31        B    64                          
REMARK   3    RESIDUE RANGE :   B    65        B   114                          
REMARK   3    RESIDUE RANGE :   B   115        B   134                          
REMARK   3    RESIDUE RANGE :   B   135        B   163                          
REMARK   3    RESIDUE RANGE :   B   164        B   178                          
REMARK   3    RESIDUE RANGE :   B   179        B   248                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.5264  16.1659  29.0624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1132 T22:  -0.0877                                     
REMARK   3      T33:  -0.1371 T12:  -0.0111                                     
REMARK   3      T13:  -0.0587 T23:   0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7116 L22:   5.5164                                     
REMARK   3      L33:   3.0735 L12:   1.3460                                     
REMARK   3      L13:   0.4004 L23:  -0.9646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1187 S12:   0.0261 S13:   0.2258                       
REMARK   3      S21:   0.0858 S22:  -0.0307 S23:  -0.5656                       
REMARK   3      S31:  -0.3091 S32:   0.6285 S33:   0.1495                       
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 2QPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000043899.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : ADJUSTABLE FOCUS K-B PAIR SI       
REMARK 200                                   PLUS PT, RH COATINGS               
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   : 24030                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.413                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.6                               
REMARK 200  DATA REDUNDANCY                : 11.60                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2680                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 27.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.776                              
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 2Q32                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (5 MG/ML PROTEIN, 1:1   
REMARK 280  RATIO HEME, 2% DMSO, 0.050 M POTASSIUM CHLORIDE, 0.050 M TRIS-      
REMARK 280  HCL PH 7.5) MIXED IN A 1.5:1 RATIO WITH THE WELL SOLUTION (33%      
REMARK 280  PEG DME 500, 0.020 M MAGNESIUM CHLORIDE, 0.10 M HEPES PH 7.5).      
REMARK 280  CRYOPROTECTED WITH WELL SOLUTION, VAPOR DIFFUSION, HANGING DROP,    
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       37.48850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.92300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.54700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.92300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.48850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.54700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3                                                       
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     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     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     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: 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    PHE A  94      -30.46   -136.19                                   
REMARK 500    ASN A 120       49.59    -96.63                                   
REMARK 500    ASN B  61       70.42   -102.14                                   
REMARK 500    ASN B 120       41.47    -99.58                                   
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 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  45   NE2                                                    
REMARK 620 2 HEM A 300   NA   99.7                                              
REMARK 620 3 HEM A 300   NB  101.3  89.0                                        
REMARK 620 4 HEM A 300   NC   89.6 170.6  87.7                                  
REMARK 620 5 HEM A 300   ND   87.4  89.9 171.2  92.0                            
REMARK 620 6 HOH A 319   O   165.6  94.2  74.9  76.4  96.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  45   NE2                                                    
REMARK 620 2 HEM B 300   NA   91.8                                              
REMARK 620 3 HEM B 300   NB  106.0  89.2                                        
REMARK 620 4 HEM B 300   NC   90.5 177.7  90.2                                  
REMARK 620 5 HEM B 300   ND   76.2  89.8 177.5  90.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: GO.91265   RELATED DB: TARGETDB                          
REMARK 900 RELATED ID: 2Q32   RELATED DB: PDB                                   
REMARK 900 HUMAN HEME OXYGENASE-2 C127A (HO-2) WITHOUT BOUND HEME               
DBREF  2QPP A    1   264  UNP    P30519   HMOX2_HUMAN      1    264             
DBREF  2QPP B    1   264  UNP    P30519   HMOX2_HUMAN      1    264             
SEQADV 2QPP ALA A  127  UNP  P30519    CYS   127 ENGINEERED                     
SEQADV 2QPP 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    HEM  A 300      43                                                       
HET    HEM  B 300      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5  HOH   *83(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  GLY A   60  1                                  10    
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 ARG A  105  GLY A  118  1                                  14    
HELIX    7   7 TRP A  121  VAL A  125  5                                   5    
HELIX    8   8 PRO A  128  GLU A  145  1                                  18    
HELIX    9   9 LEU A  148  LYS A  176  1                                  29    
HELIX   10  10 THR A  184  LEU A  188  5                                   5    
HELIX   11  11 ASN A  194  LEU A  209  1                                  16    
HELIX   12  12 ASN A  212  SER A  242  1                                  31    
HELIX   13  13 ASP B   32  THR B   41  1                                  10    
HELIX   14  14 THR B   41  ASN B   50  1                                  10    
HELIX   15  15 THR B   51  LYS B   59  1                                   9    
HELIX   16  16 LYS B   63  ASN B   88  1                                  26    
HELIX   17  17 PHE B   94  TYR B   98  5                                   5    
HELIX   18  18 PHE B   99  HIS B  104  1                                   6    
HELIX   19  19 ARG B  105  GLY B  118  1                                  14    
HELIX   20  20 ASN B  120  VAL B  125  1                                   6    
HELIX   21  21 PRO B  128  GLU B  145  1                                  18    
HELIX   22  22 LEU B  148  LYS B  176  1                                  29    
HELIX   23  23 THR B  184  LEU B  188  5                                   5    
HELIX   24  24 ASN B  194  ALA B  208  1                                  15    
HELIX   25  25 ASN B  212  THR B  248  1                                  37    
LINK         NE2 HIS A  45                FE   HEM A 300     1555   1555  2.06  
LINK         NE2 HIS B  45                FE   HEM B 300     1555   1555  2.44  
LINK        FE   HEM A 300                 O   HOH A 319     1555   1555  2.43  
SITE     1 AC1 13 HIS A  45  VAL A  54  LEU A  58  TYR A 154                    
SITE     2 AC1 13 THR A 155  ARG A 156  GLY A 159  SER A 162                    
SITE     3 AC1 13 LYS A 199  ARG A 203  PHE A 227  PHE A 234                    
SITE     4 AC1 13 HOH A 319                                                     
SITE     1 AC2 13 HIS B  45  VAL B  54  LEU B  58  TYR B 154                    
SITE     2 AC2 13 THR B 155  ARG B 156  GLY B 159  SER B 162                    
SITE     3 AC2 13 LYS B 199  ARG B 203  PHE B 227  ASN B 230                    
SITE     4 AC2 13 PHE B 234                                                     
CRYST1   74.977   85.094   97.846  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      0.013337  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011752  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010220        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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