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Database: PDB
Entry: 2BQ8
LinkDB: 2BQ8
Original site: 2BQ8 
HEADER    HYDROLASE                               27-APR-05   2BQ8              
TITLE     CRYSTAL STRUCTURE OF HUMAN PURPLE ACID PHOSPHATASE WITH AN INHIBITORY 
TITLE    2 CONFORMATION OF THE REPRESSION LOOP                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5;                
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: PURPLE ACID PHOSPHATASE, TR-AP, TRATPASE, TARTRATE-RESISTANT
COMPND   5 ACID ATPASE;                                                         
COMPND   6 EC: 3.1.3.2;                                                         
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METALLOPHOSPHATASE, DINUCLEAR METAL SITE, TRAP, HYDROLASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.STRAETER,B.JASPER,B.KREBS                                           
REVDAT   3   24-JUL-19 2BQ8    1       REMARK                                   
REVDAT   2   24-FEB-09 2BQ8    1       VERSN                                    
REVDAT   1   24-OCT-05 2BQ8    0                                                
JRNL        AUTH   N.STRATER,B.JASPER,M.SCHOLTE,B.KREBS,A.P.DUFF,D.B.LANGLEY,   
JRNL        AUTH 2 R.HAN,B.A.AVERILL,H.C.FREEMAN,J.M.GUSS                       
JRNL        TITL   CRYSTAL STRUCTURES OF RECOMBINANT HUMAN PURPLE ACID          
JRNL        TITL 2 PHOSPHATASE WITH AND WITHOUT AN INHIBITORY CONFORMATION OF   
JRNL        TITL 3 THE REPRESSION LOOP.                                         
JRNL        REF    J.MOL.BIOL.                   V. 351   233 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15993892                                                     
JRNL        DOI    10.1016/J.JMB.2005.04.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18826                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1014                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1360                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.1990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2429                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.19000                                             
REMARK   3    B22 (A**2) : -1.19000                                             
REMARK   3    B33 (A**2) : 1.78000                                              
REMARK   3    B12 (A**2) : -0.59000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.224         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.698         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2501 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3396 ; 1.383 ; 1.926       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   303 ; 6.745 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   122 ;36.432 ;22.869       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   398 ;13.902 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;19.776 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   360 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1943 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1115 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1685 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   171 ; 0.205 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.209 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.211 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1558 ; 0.859 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2436 ; 1.393 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1090 ; 2.161 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   960 ; 3.374 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2BQ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290023804.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8122                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1988                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 19.40                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.7000                            
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) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1UTE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M HEPES PH6.0, 2 M AMMONIUM         
REMARK 280  SULFATE, 10% PEG400, 0.05M ZINC SULFATE, PH 6.00                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.00233            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.00467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       72.00350            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      120.00583            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       24.00117            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.00233            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       96.00467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      120.00583            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       72.00350            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       24.00117            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH X2014  LIES ON A SPECIAL POSITION.                          
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   O    HOH X  2089     O    HOH X  2092              1.95            
REMARK 500   NE2  HIS X   249     O    HOH X  2123              2.08            
REMARK 500   O    HOH X  2013     O    HOH X  2042              2.12            
REMARK 500   O    HOH X  2047     O    HOH X  2106              2.16            
REMARK 500   O    HOH X  2087     O    HOH X  2089              2.16            
REMARK 500   OE1  GLU X   265     O    HOH X  2131              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP X  62   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP X 135   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP X 177   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP X 220   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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 X  50       60.26     60.13                                   
REMARK 500    ASP X  59     -179.69   -175.12                                   
REMARK 500    PHE X  69      -68.54   -104.97                                   
REMARK 500    PHE X  73       59.23    -93.78                                   
REMARK 500    SER X 148       62.16   -103.12                                   
REMARK 500    GLU X 152      -73.74    -57.88                                   
REMARK 500    ALA X 191     -148.00    -98.99                                   
REMARK 500    HIS X 219      -48.68     73.32                                   
REMARK 500    ASN X 241      -39.06   -150.94                                   
REMARK 500    PHE X 294      141.28   -170.51                                   
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                             FE2 X1305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP X  12   OD1                                                    
REMARK 620 2 ASP X  50   OD2  94.0                                              
REMARK 620 3 TYR X  53   OH   97.5 100.8                                        
REMARK 620 4 ASP X 145   OD2 158.6  77.3 103.3                                  
REMARK 620 5 HOH X2080   O    80.8  78.8 178.2  78.4                            
REMARK 620 6 HIS X 221   NE2  94.8 166.2  88.6  90.8  92.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 X1306  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH X2110   O                                                      
REMARK 620 2 HIS X 184   NE2  92.2                                              
REMARK 620 3 HOH X2080   O   166.7 100.9                                        
REMARK 620 4 HIS X 219   ND1  88.1  87.7  90.7                                  
REMARK 620 5 ASP X 145   OD1  89.8 176.8  77.1  94.9                            
REMARK 620 6 ASP X  50   OD2 104.4  87.8  78.1 166.9  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN X1307  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU X  67   OE2                                                    
REMARK 620 2 ASP X  71   OD2 102.1                                              
REMARK 620 3 HIS X  22   NE2 126.5 100.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 X1305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 X1306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN X1307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X1308                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BQ8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PURPLE ACID PHOSPHATASE WITH AN           
REMARK 900 INHIBITORY CONFORMATION OF THE REPRESSION LOOP                       
DBREF  2BQ8 X    1   304  UNP    P13686   PPA5_HUMAN      22    325             
SEQRES   1 X  304  ALA THR PRO ALA LEU ARG PHE VAL ALA VAL GLY ASP TRP          
SEQRES   2 X  304  GLY GLY VAL PRO ASN ALA PRO PHE HIS THR ALA ARG GLU          
SEQRES   3 X  304  MET ALA ASN ALA LYS GLU ILE ALA ARG THR VAL GLN ILE          
SEQRES   4 X  304  LEU GLY ALA ASP PHE ILE LEU SER LEU GLY ASP ASN PHE          
SEQRES   5 X  304  TYR PHE THR GLY VAL GLN ASP ILE ASN ASP LYS ARG PHE          
SEQRES   6 X  304  GLN GLU THR PHE GLU ASP VAL PHE SER ASP ARG SER LEU          
SEQRES   7 X  304  ARG LYS VAL PRO TRP TYR VAL LEU ALA GLY ASN HIS ASP          
SEQRES   8 X  304  HIS LEU GLY ASN VAL SER ALA GLN ILE ALA TYR SER LYS          
SEQRES   9 X  304  ILE SER LYS ARG TRP ASN PHE PRO SER PRO PHE TYR ARG          
SEQRES  10 X  304  LEU HIS PHE LYS ILE PRO GLN THR ASN VAL SER VAL ALA          
SEQRES  11 X  304  ILE PHE MET LEU ASP THR VAL THR LEU CYS GLY ASN SER          
SEQRES  12 X  304  ASP ASP PHE LEU SER GLN GLN PRO GLU ARG PRO ARG ASP          
SEQRES  13 X  304  VAL LYS LEU ALA ARG THR GLN LEU SER TRP LEU LYS LYS          
SEQRES  14 X  304  GLN LEU ALA ALA ALA ARG GLU ASP TYR VAL LEU VAL ALA          
SEQRES  15 X  304  GLY HIS TYR PRO VAL TRP SER ILE ALA GLU HIS GLY PRO          
SEQRES  16 X  304  THR HIS CYS LEU VAL LYS GLN LEU ARG PRO LEU LEU ALA          
SEQRES  17 X  304  THR TYR GLY VAL THR ALA TYR LEU CYS GLY HIS ASP HIS          
SEQRES  18 X  304  ASN LEU GLN TYR LEU GLN ASP GLU ASN GLY VAL GLY TYR          
SEQRES  19 X  304  VAL LEU SER GLY ALA GLY ASN PHE MET ASP PRO SER LYS          
SEQRES  20 X  304  ARG HIS GLN ARG LYS VAL PRO ASN GLY TYR LEU ARG PHE          
SEQRES  21 X  304  HIS TYR GLY THR GLU ASP SER LEU GLY GLY PHE ALA TYR          
SEQRES  22 X  304  VAL GLU ILE SER SER LYS GLU MET THR VAL THR TYR ILE          
SEQRES  23 X  304  GLU ALA SER GLY LYS SER LEU PHE LYS THR ARG LEU PRO          
SEQRES  24 X  304  ARG ARG ALA ARG PRO                                          
HET    FE2  X1305       1                                                       
HET    FE2  X1306       1                                                       
HET     ZN  X1307       1                                                       
HET    SO4  X1308       5                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  FE2    2(FE 2+)                                                     
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *147(H2 O)                                                    
HELIX    1   1 THR X   23  GLY X   41  1                                  19    
HELIX    2   2 LYS X   63  PHE X   69  1                                   7    
HELIX    3   3 ASP X   75  LYS X   80  1                                   6    
HELIX    4   4 GLY X   88  LEU X   93  1                                   6    
HELIX    5   5 ASN X   95  TYR X  102  1                                   8    
HELIX    6   6 SER X  103  ILE X  105  5                                   3    
HELIX    7   7 ASP X  135  GLY X  141  1                                   7    
HELIX    8   8 ASP X  156  ALA X  174  1                                  19    
HELIX    9   9 THR X  196  LEU X  203  1                                   8    
HELIX   10  10 LEU X  203  TYR X  210  1                                   8    
HELIX   11  11 HIS X  249  VAL X  253  5                                   5    
SHEET    1  XA 7 TRP X 109  ASN X 110  0                                        
SHEET    2  XA 7 TRP X  83  VAL X  85  1  O  TRP X  83   N  ASN X 110           
SHEET    3  XA 7 PHE X  44  SER X  47  1  O  ILE X  45   N  TYR X  84           
SHEET    4  XA 7 LEU X   5  VAL X  10  1  O  VAL X   8   N  LEU X  46           
SHEET    5  XA 7 GLY X 270  ILE X 276 -1  O  ALA X 272   N  ALA X   9           
SHEET    6  XA 7 GLU X 280  GLU X 287 -1  O  THR X 282   N  GLU X 275           
SHEET    7  XA 7 SER X 292  PRO X 299 -1  N  LEU X 293   O  TYR X 285           
SHEET    1  XB 7 TYR X 116  LYS X 121  0                                        
SHEET    2  XB 7 SER X 128  MET X 133 -1  O  VAL X 129   N  PHE X 120           
SHEET    3  XB 7 TYR X 178  ALA X 182  1  O  TYR X 178   N  ALA X 130           
SHEET    4  XB 7 ALA X 214  CYS X 217  1  O  ALA X 214   N  VAL X 181           
SHEET    5  XB 7 GLY X 233  SER X 237  1  O  GLY X 233   N  TYR X 215           
SHEET    6  XB 7 LEU X 223  GLN X 227 -1  O  GLN X 224   N  LEU X 236           
SHEET    7  XB 7 LEU X 258  TYR X 262 -1  N  ARG X 259   O  TYR X 225           
SSBOND   1 CYS X  140    CYS X  198                          1555   1555  2.06  
LINK        FE   FE2 X1305                 OD1 ASP X  12     1555   1555  2.12  
LINK        FE   FE2 X1305                 OD2 ASP X  50     1555   1555  2.26  
LINK        FE   FE2 X1305                 OH  TYR X  53     1555   1555  1.83  
LINK        FE   FE2 X1305                 OD2 ASP X 145     1555   1555  2.03  
LINK        FE   FE2 X1305                 O   HOH X2080     1555   1555  1.99  
LINK        FE   FE2 X1305                 NE2 HIS X 221     1555   1555  2.21  
LINK        FE   FE2 X1306                 O   HOH X2110     1555   1555  2.03  
LINK        FE   FE2 X1306                 NE2 HIS X 184     1555   1555  2.14  
LINK        FE   FE2 X1306                 O   HOH X2080     1555   1555  2.03  
LINK        FE   FE2 X1306                 ND1 HIS X 219     1555   1555  2.15  
LINK        FE   FE2 X1306                 OD1 ASP X 145     1555   1555  2.10  
LINK        FE   FE2 X1306                 OD2 ASP X  50     1555   1555  2.26  
LINK        ZN    ZN X1307                 OE2 GLU X  67     1555   1555  2.02  
LINK        ZN    ZN X1307                 OD2 ASP X  71     1555   1555  1.82  
LINK        ZN    ZN X1307                 NE2 HIS X  22     1555  10665  2.04  
CISPEP   1 ALA X   19    PRO X   20          0        10.91                     
CISPEP   2 TYR X   53    PHE X   54          0        -0.92                     
SITE     1 AC1  7 ASP X  12  ASP X  50  TYR X  53  ASP X 145                    
SITE     2 AC1  7 HIS X 221  FE2 X1306  HOH X2080                               
SITE     1 AC2  7 ASP X  50  ASP X 145  HIS X 184  HIS X 219                    
SITE     2 AC2  7 FE2 X1305  HOH X2080  HOH X2110                               
SITE     1 AC3  3 HIS X  22  GLU X  67  ASP X  71                               
SITE     1 AC4  5 ARG X  79  SER X 106  LYS X 107  ARG X 108                    
SITE     2 AC4  5 HOH X2147                                                     
CRYST1   94.756   94.756  144.007  90.00  90.00 120.00 P 61 2 2     12          
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      0.010553  0.006093  0.000000        0.00000                         
SCALE2      0.000000  0.012186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006944        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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