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Database: PDB
Entry: 1QHW
LinkDB: 1QHW
Original site: 1QHW 
HEADER    HYDROLASE                               26-MAR-99   1QHW              
TITLE     PURPLE ACID PHOSPHATASE FROM RAT BONE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (PURPLE ACID PHOSPHATASE);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TARTRATE-RESISTANT ACID PHOSPHATASE;                        
COMPND   5 EC: 3.1.3.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: GLYCOSIDIC LINK BETWEEN ASN 118 AND NAG 344 GLYCOSIDIC
COMPND   8 LINK BETWEEN NAG 344 AND NAG 345                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 TISSUE: BONE;                                                        
SOURCE   6 CELL: OSTEOCLAST;                                                    
SOURCE   7 ORGANELLE: LYSOSOME;                                                 
SOURCE   8 GENE: ACP5;                                                          
SOURCE   9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  16 EXPRESSION_SYSTEM_GENE: ACP5                                         
KEYWDS    METAL PHOSPHATASE, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LINDQVIST,E.JOHANSSON,H.KAIJA,P.VIHKO,G.SCHNEIDER                   
REVDAT   5   29-JUL-20 1QHW    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   13-JUL-11 1QHW    1       VERSN                                    
REVDAT   3   24-FEB-09 1QHW    1       VERSN                                    
REVDAT   2   10-NOV-99 1QHW    1       HELIX  SHEET  SITE                       
REVDAT   1   15-SEP-99 1QHW    0                                                
JRNL        AUTH   Y.LINDQVIST,E.JOHANSSON,H.KAIJA,P.VIHKO,G.SCHNEIDER          
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF A MAMMALIAN PURPLE ACID       
JRNL        TITL 2 PHOSPHATASE AT 2.2 A RESOLUTION WITH A MU-(HYDR)OXO BRIDGED  
JRNL        TITL 3 DI-IRON CENTER.                                              
JRNL        REF    J.MOL.BIOL.                   V. 291   135 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10438611                                                     
JRNL        DOI    10.1006/JMBI.1999.2962                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.KAIJA,J.JIA,Y.LINDQVIST,G.ANDERSSON,P.VIHKO                
REMARK   1  TITL   TARTRATE-RESISTANT BONE ACID PHOSPHATASE: LARGE-SCALE        
REMARK   1  TITL 2 PRODUCTION AND PURIFICATION OF THE RECOMBINANT ENZYME,       
REMARK   1  TITL 3 CHARACTERIZATION, AND CRYSTALLIZATION                        
REMARK   1  REF    J.BONE MINER.RES.             V.  14   424 1999              
REMARK   1  REFN                   ISSN 0884-0431                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17201                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 880                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2408                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 150                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2383                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.71000                                             
REMARK   3    B22 (A**2) : -4.48000                                             
REMARK   3    B33 (A**2) : 12.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.710                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.150 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.950 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.540 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 47.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000001136.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7816                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17244                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.12700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: BASED ON PDB ENTRY 4KBP                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
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       34.99000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.53500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.06000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.53500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.99000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.06000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     TRP A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     CYS A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ARG A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 109   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  73       60.06     63.64                                   
REMARK 500    PHE A  92      -74.31   -105.71                                   
REMARK 500    PHE A  96       58.57    -93.89                                   
REMARK 500    ASN A 103       -1.71     76.83                                   
REMARK 500    ARG A 147      -66.57     67.04                                   
REMARK 500    ALA A 195       40.66    -89.40                                   
REMARK 500    ALA A 196      -13.45   -165.72                                   
REMARK 500    ALA A 214     -152.49    -85.39                                   
REMARK 500    HIS A 242      -54.66     70.15                                   
REMARK 500    ASN A 245     -168.81   -171.51                                   
REMARK 500    ASN A 264      -28.63   -144.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 433  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  35   OD2                                                    
REMARK 620 2 ASP A  73   OD2  86.5                                              
REMARK 620 3 TYR A  76   OH  101.0  95.8                                        
REMARK 620 4 HIS A 244   NE2  96.1 166.0  97.3                                  
REMARK 620 5 HOH A 588   O    83.2  76.3 170.9  90.3                            
REMARK 620 6 HOH A 591   O   172.7 100.7  79.6  76.7  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 434  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  73   OD2                                                    
REMARK 620 2 ASN A 112   OD1 104.7                                              
REMARK 620 3 HIS A 207   NE2  88.2  89.0                                        
REMARK 620 4 HIS A 242   ND1 157.7  97.6  91.6                                  
REMARK 620 5 SO4 A 437   O3   79.1  86.3 164.9 103.2                            
REMARK 620 6 HOH A 588   O    71.2 156.6 113.5  88.6  70.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 435  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  90   OE1                                                    
REMARK 620 2 ASP A  94   OD2 122.0                                              
REMARK 620 3 HIS A 284   ND1 111.6 102.4                                        
REMARK 620 4 HOH A 536   O   103.9 114.1 101.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 436  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 216   NE2                                                    
REMARK 620 2 SO4 A 437   O4   75.9                                              
REMARK 620 3 SO4 A 437   O1  128.2  52.3                                        
REMARK 620 4 HOH A 527   O   109.4 131.9 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: 2FE                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: BINUCLEAR IRON-CENTER                              
DBREF  1QHW A    1   327  UNP    P29288   PPA5_RAT         1    327             
SEQRES   1 A  327  MET ASP THR TRP MET VAL LEU LEU GLY LEU GLN ILE LEU          
SEQRES   2 A  327  LEU LEU PRO LEU LEU ALA HIS CYS THR ALA PRO ALA SER          
SEQRES   3 A  327  THR LEU ARG PHE VAL ALA VAL GLY ASP TRP GLY GLY VAL          
SEQRES   4 A  327  PRO ASN ALA PRO PHE HIS THR ALA ARG GLU MET ALA ASN          
SEQRES   5 A  327  ALA LYS GLU ILE ALA ARG THR VAL GLN ILE MET GLY ALA          
SEQRES   6 A  327  ASP PHE ILE MET SER LEU GLY ASP ASN PHE TYR PHE THR          
SEQRES   7 A  327  GLY VAL HIS ASP ALA ASN ASP LYS ARG PHE GLN GLU THR          
SEQRES   8 A  327  PHE GLU ASP VAL PHE SER ASP ARG ALA LEU ARG ASN ILE          
SEQRES   9 A  327  PRO TRP TYR VAL LEU ALA GLY ASN HIS ASP HIS LEU GLY          
SEQRES  10 A  327  ASN VAL SER ALA GLN ILE ALA TYR SER LYS ILE SER LYS          
SEQRES  11 A  327  ARG TRP ASN PHE PRO SER PRO TYR TYR ARG LEU ARG PHE          
SEQRES  12 A  327  LYS VAL PRO ARG SER ASN ILE THR VAL ALA ILE PHE MET          
SEQRES  13 A  327  LEU ASP THR VAL MET LEU CYS GLY ASN SER ASP ASP PHE          
SEQRES  14 A  327  VAL SER GLN GLN PRO GLU MET PRO ARG ASP LEU GLY VAL          
SEQRES  15 A  327  ALA ARG THR GLN LEU SER TRP LEU LYS LYS GLN LEU ALA          
SEQRES  16 A  327  ALA ALA LYS GLU ASP TYR VAL LEU VAL ALA GLY HIS TYR          
SEQRES  17 A  327  PRO ILE TRP SER ILE ALA GLU HIS GLY PRO THR ARG CYS          
SEQRES  18 A  327  LEU VAL LYS ASN LEU ARG PRO LEU LEU ALA ALA TYR GLY          
SEQRES  19 A  327  VAL THR ALA TYR LEU CYS GLY HIS ASP HIS ASN LEU GLN          
SEQRES  20 A  327  TYR LEU GLN ASP GLU ASN GLY VAL GLY TYR VAL LEU SER          
SEQRES  21 A  327  GLY ALA GLY ASN PHE MET ASP PRO SER VAL ARG HIS GLN          
SEQRES  22 A  327  ARG LYS VAL PRO ASN GLY TYR LEU ARG PHE HIS TYR GLY          
SEQRES  23 A  327  SER GLU ASP SER LEU GLY GLY PHE THR TYR VAL GLU ILE          
SEQRES  24 A  327  GLY SER LYS GLU MET SER ILE THR TYR VAL GLU ALA SER          
SEQRES  25 A  327  GLY LYS SER LEU PHE LYS THR SER LEU PRO ARG ARG PRO          
SEQRES  26 A  327  ARG PRO                                                      
MODRES 1QHW ASN A  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET     FE  A 433       1                                                       
HET     FE  A 434       1                                                       
HET     ZN  A 435       1                                                       
HET     ZN  A 436       1                                                       
HET    SO4  A 437       5                                                       
HET    SO4  A 438       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      FE FE (III) ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   7  SO4    2(O4 S 2-)                                                   
FORMUL   9  HOH   *103(H2 O)                                                    
HELIX    1   1 ALA A   47  MET A   63  1                                  17    
HELIX    2   2 LYS A   86  GLU A   90  5                                   5    
HELIX    3   3 ARG A   99  LEU A  101  5                                   3    
HELIX    4   4 ASP A  114  LEU A  116  5                                   3    
HELIX    5   5 VAL A  119  LYS A  127  1                                   9    
HELIX    6   6 THR A  159  CYS A  163  1                                   5    
HELIX    7   7 SER A  166  ASP A  168  5                                   3    
HELIX    8   8 LEU A  180  LEU A  194  1                                  15    
HELIX    9   9 ARG A  220  ASN A  225  1                                   6    
HELIX   10  10 ARG A  227  TYR A  233  1                                   7    
HELIX   11  11 GLN A  273  LYS A  275  5                                   3    
SHEET    1   A 6 PRO A 105  TYR A 107  0                                        
SHEET    2   A 6 PHE A  67  SER A  70  1  N  ILE A  68   O  PRO A 105           
SHEET    3   A 6 LEU A  28  VAL A  33  1  N  VAL A  31   O  PHE A  67           
SHEET    4   A 6 GLY A 293  ILE A 299 -1  N  ILE A 299   O  LEU A  28           
SHEET    5   A 6 GLU A 303  GLU A 310 -1  N  VAL A 309   O  PHE A 294           
SHEET    6   A 6 SER A 315  PRO A 322 -1  N  LEU A 321   O  MET A 304           
SHEET    1   B 7 TYR A 139  LYS A 144  0                                        
SHEET    2   B 7 THR A 151  MET A 156 -1  N  MET A 156   O  TYR A 139           
SHEET    3   B 7 TYR A 201  ALA A 205  1  N  TYR A 201   O  ALA A 153           
SHEET    4   B 7 ALA A 237  CYS A 240  1  N  ALA A 237   O  VAL A 204           
SHEET    5   B 7 GLY A 256  SER A 260  1  N  GLY A 256   O  TYR A 238           
SHEET    6   B 7 LEU A 246  GLN A 250 -1  N  LEU A 249   O  TYR A 257           
SHEET    7   B 7 LEU A 281  TYR A 285 -1  N  TYR A 285   O  LEU A 246           
LINK         ND2 ASN A 118                 C1  NAG B   1     1555   1555  1.45  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.39  
LINK         OD2 ASP A  35                FE    FE A 433     1555   1555  2.05  
LINK         OD2 ASP A  73                FE    FE A 433     1555   1555  2.25  
LINK         OD2 ASP A  73                FE    FE A 434     1555   1555  2.39  
LINK         OH  TYR A  76                FE    FE A 433     1555   1555  1.97  
LINK         OE1 GLU A  90                ZN    ZN A 435     4556   1555  2.54  
LINK         OD2 ASP A  94                ZN    ZN A 435     4556   1555  2.40  
LINK         OD1 ASN A 112                FE    FE A 434     1555   1555  2.16  
LINK         NE2 HIS A 207                FE    FE A 434     1555   1555  2.01  
LINK         NE2 HIS A 216                ZN    ZN A 436     1555   1555  2.47  
LINK         ND1 HIS A 242                FE    FE A 434     1555   1555  2.30  
LINK         NE2 HIS A 244                FE    FE A 433     1555   1555  2.34  
LINK         ND1 HIS A 284                ZN    ZN A 435     1555   1555  2.42  
LINK        FE    FE A 433                 O   HOH A 588     1555   1555  2.02  
LINK        FE    FE A 433                 O   HOH A 591     1555   1555  2.11  
LINK        FE    FE A 434                 O3  SO4 A 437     1555   1555  2.59  
LINK        FE    FE A 434                 O   HOH A 588     1555   1555  2.14  
LINK        ZN    ZN A 435                 O   HOH A 536     1555   4556  2.60  
LINK        ZN    ZN A 436                 O4  SO4 A 437     1555   1555  2.77  
LINK        ZN    ZN A 436                 O1  SO4 A 437     1555   1555  2.73  
LINK        ZN    ZN A 436                 O   HOH A 527     1555   1555  2.63  
CISPEP   1 ALA A   42    PRO A   43          0         0.96                     
CISPEP   2 TYR A   76    PHE A   77          0         0.06                     
SITE     1 2FE 12 ASN A 112  HIS A 242  HIS A 207  ASP A  73                    
SITE     2 2FE 12 TYR A  76  ASP A  35  HIS A 244  SO4 A 437                    
SITE     3 2FE 12 HOH A 588  HOH A 591   FE A 433   FE A 434                    
CRYST1   69.980   88.120   57.070  90.00  90.00  90.00 P 21 21 21    4          
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      0.014290  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011348  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017522        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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