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Database: PDB
Entry: 5UCA
LinkDB: 5UCA
Original site: 5UCA 
HEADER    OXIDOREDUCTASE                          22-DEC-16   5UCA              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-2 IN COMPLEX WITH LAURATE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEME OXYGENASE 2;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 30-242;                                           
COMPND   5 SYNONYM: HO-2;                                                       
COMPND   6 EC: 1.14.14.18;                                                      
COMPND   7 ENGINEERED: 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HEME OXYGENASE, LAURIC ACID, OXIDOREDUCTASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LUO,L.TONG                                                          
REVDAT   3   22-NOV-17 5UCA    1       REMARK                                   
REVDAT   2   22-FEB-17 5UCA    1       JRNL                                     
REVDAT   1   15-FEB-17 5UCA    0                                                
JRNL        AUTH   Y.ZHU,S.LUO,Y.SABO,C.WANG,L.TONG,S.P.GOFF                    
JRNL        TITL   HEME OXYGENASE 2 BINDS MYRISTATE TO REGULATE RETROVIRUS      
JRNL        TITL 2 ASSEMBLY AND TLR4 SIGNALING.                                 
JRNL        REF    CELL HOST MICROBE             V.  21   220 2017              
JRNL        REFN                   ESSN 1934-6069                               
JRNL        PMID   28132836                                                     
JRNL        DOI    10.1016/J.CHOM.2017.01.002                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10_2155                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51395                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1445                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 24.6518 -  4.5522    0.96     5115   149  0.1634 0.2066        
REMARK   3     2  4.5522 -  3.6169    1.00     5114   147  0.1630 0.1979        
REMARK   3     3  3.6169 -  3.1607    1.00     5062   150  0.1969 0.2582        
REMARK   3     4  3.1607 -  2.8722    1.00     5029   144  0.2169 0.2700        
REMARK   3     5  2.8722 -  2.6666    1.00     5022   147  0.2183 0.2793        
REMARK   3     6  2.6666 -  2.5096    1.00     5010   143  0.2181 0.2898        
REMARK   3     7  2.5096 -  2.3840    1.00     5008   149  0.2144 0.3131        
REMARK   3     8  2.3840 -  2.2803    1.00     4967   132  0.2117 0.3092        
REMARK   3     9  2.2803 -  2.1926    1.00     4997   147  0.2385 0.2962        
REMARK   3    10  2.1926 -  2.1169    0.93     4626   137  0.2531 0.3331        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           7098                                  
REMARK   3   ANGLE     :  0.797           9528                                  
REMARK   3   CHIRALITY :  0.043            983                                  
REMARK   3   PLANARITY :  0.005           1254                                  
REMARK   3   DIHEDRAL  : 19.404           4327                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225646.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-16                          
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                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : LR-DESIGN DETECTOR POSITIONER      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, SCALEPACK                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51449                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 5UC8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS (PH 6.5) AND 24% (W/V)    
REMARK 280  PEG 2000 MONOMETHYL ETHER, VAPOR DIFFUSION, TEMPERATURE 293K        
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       38.68150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.14850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.96000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.14850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.68150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.96000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     HIS A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     MET A    30                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     SER A   242                                                      
REMARK 465     MET B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     HIS B    22                                                      
REMARK 465     HIS B    23                                                      
REMARK 465     HIS B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     HIS B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     MET B    30                                                      
REMARK 465     GLY B   241                                                      
REMARK 465     SER B   242                                                      
REMARK 465     MET C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     HIS C    21                                                      
REMARK 465     HIS C    22                                                      
REMARK 465     HIS C    23                                                      
REMARK 465     HIS C    24                                                      
REMARK 465     HIS C    25                                                      
REMARK 465     HIS C    26                                                      
REMARK 465     SER C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     MET C    30                                                      
REMARK 465     GLY C   241                                                      
REMARK 465     SER C   242                                                      
REMARK 465     MET D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     HIS D    21                                                      
REMARK 465     HIS D    22                                                      
REMARK 465     HIS D    23                                                      
REMARK 465     HIS D    24                                                      
REMARK 465     HIS D    25                                                      
REMARK 465     HIS D    26                                                      
REMARK 465     SER D    27                                                      
REMARK 465     SER D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     MET D    30                                                      
REMARK 465     GLY D   241                                                      
REMARK 465     SER D   242                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG D    47     OE2  GLU D   228              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   455     O    HOH D   490     4555     2.19            
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  61       58.17   -105.92                                   
REMARK 500    PHE A  94      -27.32   -141.19                                   
REMARK 500    ASN A 120       36.78    -91.10                                   
REMARK 500    ARG A 156      -63.34    -92.80                                   
REMARK 500    PHE A 189       79.15   -102.78                                   
REMARK 500    ASN B  61       48.10    -99.57                                   
REMARK 500    PHE B  94      -30.03   -130.57                                   
REMARK 500    ASN B 120       31.16    -89.51                                   
REMARK 500    ASN B 144      -26.81   -140.28                                   
REMARK 500    GLN B 239        1.32    -69.81                                   
REMARK 500    ARG C 156      -60.27    -90.17                                   
REMARK 500    ASN D  61       49.77   -102.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO D 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UC8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UC9   RELATED DB: PDB                                   
DBREF  5UCA A   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UCA B   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UCA C   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UCA D   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
SEQADV 5UCA MET A   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UCA GLY A   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER A   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER A   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS A   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER A   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER A   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA GLY A   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA MET B   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UCA GLY B   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER B   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER B   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS B   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER B   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER B   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA GLY B   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA MET C   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UCA GLY C   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER C   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER C   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS C   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER C   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER C   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA GLY C   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA MET D   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UCA GLY D   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER D   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER D   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA HIS D   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER D   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA SER D   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UCA GLY D   29  UNP  P30519              EXPRESSION TAG                 
SEQRES   1 A  226  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  226  MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS          
SEQRES   3 A  226  GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS          
SEQRES   4 A  226  ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS          
SEQRES   5 A  226  LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU          
SEQRES   6 A  226  GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE          
SEQRES   7 A  226  ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU          
SEQRES   8 A  226  ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN          
SEQRES   9 A  226  TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS          
SEQRES  10 A  226  TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO          
SEQRES  11 A  226  GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY          
SEQRES  12 A  226  ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN          
SEQRES  13 A  226  ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN          
SEQRES  14 A  226  PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE          
SEQRES  15 A  226  LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU          
SEQRES  16 A  226  ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN          
SEQRES  17 A  226  LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU          
SEQRES  18 A  226  ASP GLN ALA GLY SER                                          
SEQRES   1 B  226  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  226  MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS          
SEQRES   3 B  226  GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS          
SEQRES   4 B  226  ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS          
SEQRES   5 B  226  LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU          
SEQRES   6 B  226  GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE          
SEQRES   7 B  226  ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU          
SEQRES   8 B  226  ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN          
SEQRES   9 B  226  TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS          
SEQRES  10 B  226  TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO          
SEQRES  11 B  226  GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY          
SEQRES  12 B  226  ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN          
SEQRES  13 B  226  ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN          
SEQRES  14 B  226  PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE          
SEQRES  15 B  226  LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU          
SEQRES  16 B  226  ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN          
SEQRES  17 B  226  LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU          
SEQRES  18 B  226  ASP GLN ALA GLY SER                                          
SEQRES   1 C  226  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  226  MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS          
SEQRES   3 C  226  GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS          
SEQRES   4 C  226  ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS          
SEQRES   5 C  226  LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU          
SEQRES   6 C  226  GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE          
SEQRES   7 C  226  ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU          
SEQRES   8 C  226  ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN          
SEQRES   9 C  226  TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS          
SEQRES  10 C  226  TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO          
SEQRES  11 C  226  GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY          
SEQRES  12 C  226  ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN          
SEQRES  13 C  226  ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN          
SEQRES  14 C  226  PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE          
SEQRES  15 C  226  LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU          
SEQRES  16 C  226  ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN          
SEQRES  17 C  226  LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU          
SEQRES  18 C  226  ASP GLN ALA GLY SER                                          
SEQRES   1 D  226  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  226  MET ALA ASP LEU SER GLU LEU LEU LYS GLU GLY THR LYS          
SEQRES   3 D  226  GLU ALA HIS ASP ARG ALA GLU ASN THR GLN PHE VAL LYS          
SEQRES   4 D  226  ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU LEU PHE LYS          
SEQRES   5 D  226  LEU ALA THR THR ALA LEU TYR PHE THR TYR SER ALA LEU          
SEQRES   6 D  226  GLU GLU GLU MET GLU ARG ASN LYS ASP HIS PRO ALA PHE          
SEQRES   7 D  226  ALA PRO LEU TYR PHE PRO MET GLU LEU HIS ARG LYS GLU          
SEQRES   8 D  226  ALA LEU THR LYS ASP MET GLU TYR PHE PHE GLY GLU ASN          
SEQRES   9 D  226  TRP GLU GLU GLN VAL GLN CYS PRO LYS ALA ALA GLN LYS          
SEQRES  10 D  226  TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN ASN GLU PRO          
SEQRES  11 D  226  GLU LEU LEU VAL ALA HIS ALA TYR THR ARG TYR MET GLY          
SEQRES  12 D  226  ASP LEU SER GLY GLY GLN VAL LEU LYS LYS VAL ALA GLN          
SEQRES  13 D  226  ARG ALA LEU LYS LEU PRO SER THR GLY GLU GLY THR GLN          
SEQRES  14 D  226  PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA GLN GLN PHE          
SEQRES  15 D  226  LYS GLN LEU TYR ARG ALA ARG MET ASN ALA LEU ASP LEU          
SEQRES  16 D  226  ASN MET LYS THR LYS GLU ARG ILE VAL GLU GLU ALA ASN          
SEQRES  17 D  226  LYS ALA PHE GLU TYR ASN MET GLN ILE PHE ASN GLU LEU          
SEQRES  18 D  226  ASP GLN ALA GLY SER                                          
HET    DAO  B 301      14                                                       
HET    DAO  C 301      14                                                       
HET    DAO  D 301      14                                                       
HETNAM     DAO LAURIC ACID                                                      
FORMUL   5  DAO    3(C12 H24 O2)                                                
FORMUL   8  HOH   *414(H2 O)                                                    
HELIX    1 AA1 ASP A   32  THR A   41  1                                  10    
HELIX    2 AA2 THR A   41  ASN A   50  1                                  10    
HELIX    3 AA3 THR A   51  LYS A   59  1                                   9    
HELIX    4 AA4 LYS A   63  ASN A   88  1                                  26    
HELIX    5 AA5 PHE A   94  TYR A   98  5                                   5    
HELIX    6 AA6 PHE A   99  HIS A  104  1                                   6    
HELIX    7 AA7 ARG A  105  GLY A  118  1                                  14    
HELIX    8 AA8 ASN A  120  VAL A  125  1                                   6    
HELIX    9 AA9 PRO A  128  GLU A  145  1                                  18    
HELIX   10 AB1 LEU A  148  LEU A  175  1                                  28    
HELIX   11 AB2 THR A  184  LEU A  188  5                                   5    
HELIX   12 AB3 ASN A  194  ALA A  208  1                                  15    
HELIX   13 AB4 ASN A  212  GLN A  239  1                                  28    
HELIX   14 AB5 ASP B   32  THR B   41  1                                  10    
HELIX   15 AB6 THR B   41  ASN B   50  1                                  10    
HELIX   16 AB7 THR B   51  GLY B   60  1                                  10    
HELIX   17 AB8 LYS B   63  ASN B   88  1                                  26    
HELIX   18 AB9 PHE B   94  TYR B   98  5                                   5    
HELIX   19 AC1 PHE B   99  HIS B  104  1                                   6    
HELIX   20 AC2 ARG B  105  GLY B  118  1                                  14    
HELIX   21 AC3 ASN B  120  VAL B  125  1                                   6    
HELIX   22 AC4 PRO B  128  GLU B  145  1                                  18    
HELIX   23 AC5 LEU B  148  LYS B  176  1                                  29    
HELIX   24 AC6 THR B  184  LEU B  188  5                                   5    
HELIX   25 AC7 ASN B  194  LEU B  209  1                                  16    
HELIX   26 AC8 ASN B  212  GLN B  239  1                                  28    
HELIX   27 AC9 ASP C   32  THR C   41  1                                  10    
HELIX   28 AD1 THR C   41  ASN C   50  1                                  10    
HELIX   29 AD2 THR C   51  GLY C   60  1                                  10    
HELIX   30 AD3 LYS C   63  ASN C   88  1                                  26    
HELIX   31 AD4 PHE C   94  TYR C   98  5                                   5    
HELIX   32 AD5 PHE C   99  HIS C  104  1                                   6    
HELIX   33 AD6 ARG C  105  GLY C  118  1                                  14    
HELIX   34 AD7 ASN C  120  VAL C  125  1                                   6    
HELIX   35 AD8 PRO C  128  GLU C  145  1                                  18    
HELIX   36 AD9 LEU C  148  LYS C  176  1                                  29    
HELIX   37 AE1 THR C  184  LEU C  188  5                                   5    
HELIX   38 AE2 ASN C  194  LEU C  209  1                                  16    
HELIX   39 AE3 ASN C  212  ALA C  240  1                                  29    
HELIX   40 AE4 ASP D   32  THR D   41  1                                  10    
HELIX   41 AE5 THR D   41  ASN D   50  1                                  10    
HELIX   42 AE6 THR D   51  LYS D   59  1                                   9    
HELIX   43 AE7 LYS D   63  ASN D   88  1                                  26    
HELIX   44 AE8 PHE D   94  TYR D   98  5                                   5    
HELIX   45 AE9 PHE D   99  HIS D  104  1                                   6    
HELIX   46 AF1 ARG D  105  GLY D  118  1                                  14    
HELIX   47 AF2 ASN D  120  VAL D  125  1                                   6    
HELIX   48 AF3 PRO D  128  GLU D  145  1                                  18    
HELIX   49 AF4 LEU D  148  LEU D  175  1                                  28    
HELIX   50 AF5 THR D  184  LEU D  188  5                                   5    
HELIX   51 AF6 ASN D  194  LEU D  209  1                                  16    
HELIX   52 AF7 ASN D  212  ALA D  240  1                                  29    
SITE     1 AC1  5 GLU B  49  LEU B  74  ARG B 156  TYR B 187                    
SITE     2 AC1  5 PHE B 234                                                     
SITE     1 AC2  4 GLU C  49  VAL C  54  LEU C  74  ARG C 156                    
SITE     1 AC3  8 VAL D  54  ALA D  70  THR D  77  ARG D 156                    
SITE     2 AC3  8 TYR D 187  ASN D 230  PHE D 234  HOH D 404                    
CRYST1   77.363   83.920  138.297  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012926  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011916  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007231        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system