GenomeNet

Database: PDB
Entry: 5UC9
LinkDB: 5UC9
Original site: 5UC9 
HEADER    OXIDOREDUCTASE                          22-DEC-16   5UC9              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-2 IN COMPLEX WITH MYRISTATE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEME OXYGENASE 2;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 1-213;                                            
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, MYRISTIC ACID, OXIDOREDUCTASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LUO,L.TONG                                                          
REVDAT   3   22-NOV-17 5UC9    1       REMARK                                   
REVDAT   2   22-FEB-17 5UC9    1       JRNL                                     
REVDAT   1   15-FEB-17 5UC9    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 68033                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4978                            
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 25.0077 -  5.8895    0.95     2220   180  0.1535 0.1829        
REMARK   3     2  5.8895 -  4.6847    0.98     2197   173  0.1726 0.2379        
REMARK   3     3  4.6847 -  4.0954    0.99     2183   169  0.1471 0.1774        
REMARK   3     4  4.0954 -  3.7223    0.99     2192   170  0.1678 0.2479        
REMARK   3     5  3.7223 -  3.4563    1.00     2182   171  0.1793 0.2230        
REMARK   3     6  3.4563 -  3.2529    1.00     2180   175  0.1957 0.2428        
REMARK   3     7  3.2529 -  3.0903    1.00     2151   179  0.2056 0.2761        
REMARK   3     8  3.0903 -  2.9560    1.00     2190   166  0.2058 0.2595        
REMARK   3     9  2.9560 -  2.8424    1.00     2147   175  0.2069 0.2527        
REMARK   3    10  2.8424 -  2.7444    1.00     2162   175  0.2012 0.2793        
REMARK   3    11  2.7444 -  2.6587    1.00     2137   161  0.1985 0.2598        
REMARK   3    12  2.6587 -  2.5828    1.00     2143   169  0.2057 0.2679        
REMARK   3    13  2.5828 -  2.5149    1.00     2163   161  0.1967 0.2678        
REMARK   3    14  2.5149 -  2.4536    1.00     2157   184  0.1997 0.2536        
REMARK   3    15  2.4536 -  2.3978    0.99     2142   165  0.1990 0.2513        
REMARK   3    16  2.3978 -  2.3468    1.00     2127   167  0.1968 0.2658        
REMARK   3    17  2.3468 -  2.2999    1.00     2149   173  0.2003 0.2386        
REMARK   3    18  2.2999 -  2.2566    0.99     2117   163  0.2002 0.2339        
REMARK   3    19  2.2566 -  2.2163    0.98     2085   185  0.2130 0.3154        
REMARK   3    20  2.2163 -  2.1787    0.98     2138   146  0.2131 0.2600        
REMARK   3    21  2.1787 -  2.1436    0.97     2055   167  0.1989 0.2734        
REMARK   3    22  2.1436 -  2.1107    0.97     2073   169  0.2103 0.2719        
REMARK   3    23  2.1107 -  2.0796    0.96     2045   161  0.2110 0.2888        
REMARK   3    24  2.0796 -  2.0503    0.95     1999   173  0.2147 0.2540        
REMARK   3    25  2.0503 -  2.0227    0.94     2013   142  0.2082 0.2468        
REMARK   3    26  2.0227 -  1.9964    0.94     2013   161  0.2143 0.2775        
REMARK   3    27  1.9964 -  1.9715    0.93     1980   164  0.2216 0.2891        
REMARK   3    28  1.9715 -  1.9477    0.93     1999   145  0.2415 0.3667        
REMARK   3    29  1.9477 -  1.9251    0.91     1948   147  0.2479 0.3259        
REMARK   3    30  1.9251 -  1.9034    0.83     1768   142  0.2656 0.3135        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.39                          
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      :  0.008           7127                                  
REMARK   3   ANGLE     :  0.856           9559                                  
REMARK   3   CHIRALITY :  0.049            984                                  
REMARK   3   PLANARITY :  0.005           1256                                  
REMARK   3   DIHEDRAL  : 17.016           4351                                  
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 5UC9 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_1000225647.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-15                          
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   : 68092                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53400                            
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   (%): 41.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS (PH 6.5) AND 24% (W/V)    
REMARK 280  PEG 2,000 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       38.87550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.52550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.52550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.87550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.45000            
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     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   OH   TYR C   154     NH1  ARG C   203              2.05            
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       39.46    -93.47                                   
REMARK 500    PHE A  94      -28.13   -141.08                                   
REMARK 500    ASN A 120       36.61    -92.03                                   
REMARK 500    ASN B 120       34.27    -96.19                                   
REMARK 500    ASN C  61       50.77    -98.82                                   
REMARK 500    PHE D  94      -32.37   -135.38                                   
REMARK 500    ASN D 120       33.16    -88.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 586        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH D 587        DISTANCE =  6.75 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR D 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UC8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UCA   RELATED DB: PDB                                   
DBREF  5UC9 A   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UC9 B   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UC9 C   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
DBREF  5UC9 D   30   242  UNP    P30519   HMOX2_HUMAN      1    213             
SEQADV 5UC9 MET A   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UC9 GLY A   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER A   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER A   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS A   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER A   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER A   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 GLY A   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 MET B   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UC9 GLY B   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER B   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER B   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS B   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER B   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER B   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 GLY B   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 MET C   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UC9 GLY C   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER C   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER C   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS C   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER C   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER C   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 GLY C   29  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 MET D   17  UNP  P30519              INITIATING METHIONINE          
SEQADV 5UC9 GLY D   18  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER D   19  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER D   20  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   21  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   22  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   23  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   24  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   25  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 HIS D   26  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER D   27  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 SER D   28  UNP  P30519              EXPRESSION TAG                 
SEQADV 5UC9 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    MYR  A 301      16                                                       
HET    MYR  B 301      16                                                       
HET    MYR  C 301      16                                                       
HET    MYR  D 301      16                                                       
HETNAM     MYR MYRISTIC ACID                                                    
FORMUL   5  MYR    4(C14 H28 O2)                                                
FORMUL   9  HOH   *584(H2 O)                                                    
HELIX    1 AA1 ASP A   32  ASN A   50  1                                  19    
HELIX    2 AA2 THR A   51  LYS A   59  1                                   9    
HELIX    3 AA3 LYS A   63  ASN A   88  1                                  26    
HELIX    4 AA4 PHE A   94  TYR A   98  5                                   5    
HELIX    5 AA5 PHE A   99  HIS A  104  1                                   6    
HELIX    6 AA6 ARG A  105  GLY A  118  1                                  14    
HELIX    7 AA7 ASN A  120  VAL A  125  1                                   6    
HELIX    8 AA8 PRO A  128  GLU A  145  1                                  18    
HELIX    9 AA9 LEU A  148  LYS A  176  1                                  29    
HELIX   10 AB1 THR A  184  LEU A  188  5                                   5    
HELIX   11 AB2 ASN A  194  ALA A  208  1                                  15    
HELIX   12 AB3 ASN A  212  GLN A  239  1                                  28    
HELIX   13 AB4 ASP B   32  THR B   41  1                                  10    
HELIX   14 AB5 THR B   41  ASN B   50  1                                  10    
HELIX   15 AB6 THR B   51  LYS B   59  1                                   9    
HELIX   16 AB7 LYS B   63  ASN B   88  1                                  26    
HELIX   17 AB8 PHE B   94  TYR B   98  5                                   5    
HELIX   18 AB9 PHE B   99  HIS B  104  1                                   6    
HELIX   19 AC1 ARG B  105  GLY B  118  1                                  14    
HELIX   20 AC2 ASN B  120  VAL B  125  5                                   6    
HELIX   21 AC3 PRO B  128  GLU B  145  1                                  18    
HELIX   22 AC4 LEU B  148  LYS B  176  1                                  29    
HELIX   23 AC5 THR B  184  LEU B  188  5                                   5    
HELIX   24 AC6 ASN B  194  ALA B  208  1                                  15    
HELIX   25 AC7 ASN B  212  ALA B  240  1                                  29    
HELIX   26 AC8 ASP C   32  THR C   41  1                                  10    
HELIX   27 AC9 THR C   41  ASN C   50  1                                  10    
HELIX   28 AD1 THR C   51  LYS C   59  1                                   9    
HELIX   29 AD2 LYS C   63  ASN C   88  1                                  26    
HELIX   30 AD3 PHE C   94  TYR C   98  5                                   5    
HELIX   31 AD4 PHE C   99  HIS C  104  1                                   6    
HELIX   32 AD5 ARG C  105  GLY C  118  1                                  14    
HELIX   33 AD6 ASN C  120  GLN C  124  5                                   5    
HELIX   34 AD7 PRO C  128  GLU C  145  1                                  18    
HELIX   35 AD8 LEU C  148  LYS C  176  1                                  29    
HELIX   36 AD9 THR C  184  LEU C  188  5                                   5    
HELIX   37 AE1 ASN C  194  LEU C  209  1                                  16    
HELIX   38 AE2 ASN C  212  ALA C  240  1                                  29    
HELIX   39 AE3 ASP D   32  THR D   41  1                                  10    
HELIX   40 AE4 THR D   41  ASN D   50  1                                  10    
HELIX   41 AE5 THR D   51  LYS D   59  1                                   9    
HELIX   42 AE6 LYS D   63  ASN D   88  1                                  26    
HELIX   43 AE7 PHE D   94  TYR D   98  5                                   5    
HELIX   44 AE8 PHE D   99  HIS D  104  1                                   6    
HELIX   45 AE9 ARG D  105  GLY D  118  1                                  14    
HELIX   46 AF1 ASN D  120  VAL D  125  1                                   6    
HELIX   47 AF2 PRO D  128  GLU D  145  1                                  18    
HELIX   48 AF3 LEU D  148  LYS D  176  1                                  29    
HELIX   49 AF4 THR D  184  LEU D  188  5                                   5    
HELIX   50 AF5 ASN D  194  LEU D  209  1                                  16    
HELIX   51 AF6 ASN D  212  GLN D  239  1                                  28    
SITE     1 AC1  7 PHE A  53  TYR A 134  ARG A 156  LEU A 167                    
SITE     2 AC1  7 ALA A 226  ASN A 230  PHE A 234                               
SITE     1 AC2  7 GLU B  49  PHE B  53  LEU B  74  ARG B 156                    
SITE     2 AC2  7 LEU B 167  ASN B 230  PHE B 234                               
SITE     1 AC3  7 PHE C  53  TYR C 134  ARG C 156  ALA C 226                    
SITE     2 AC3  7 ASN C 230  ILE C 233  PHE C 234                               
SITE     1 AC4  6 PHE D  53  LEU D  74  ARG D 156  ASN D 230                    
SITE     2 AC4  6 PHE D 234  HOH D 441                                          
CRYST1   77.751   82.900  137.051  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      0.012862  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012063  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system