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Database: PDB
Entry: 1WAR
LinkDB: 1WAR
Original site: 1WAR 
HEADER    HYDROLASE                               28-OCT-04   1WAR              
TITLE     RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN PURPLE ACID PHOSPHATASE;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACP5 PROTEIN, TARTRATE-RESISTANT ACID ATPASE, TRATPASE, TR- 
COMPND   5 AP;                                                                  
COMPND   6 EC: 3.1.3.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: A SIX AMINO ACID CLONING ARTIFACT IS ATTACHED TO THE  
COMPND   9 N-TERMINUS                                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PPICZALPHAA                                
KEYWDS    GLYCOPROTEIN, HYDROLASE, IRON, IRON TRANSPORT, METALLOENZYME, PURPLE  
KEYWDS   2 ACID PHOSPHATASE, TARTRATE RESISTANT ACID PHOSPHATASE, UTEROFERRIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.DUFF,D.B.LANGLEY,R.HAN,B.A.AVERILL,H.C.FREEMAN,J.M.GUSS           
REVDAT   5   03-APR-19 1WAR    1       REMARK LINK                              
REVDAT   4   13-JUL-11 1WAR    1       VERSN                                    
REVDAT   3   24-FEB-09 1WAR    1       VERSN                                    
REVDAT   2   20-JUL-05 1WAR    1       JRNL                                     
REVDAT   1   06-JUL-05 1WAR    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.    2.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 15167                          
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) : 0.141                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 767                             
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) : 2.22                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1051                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2477                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 36.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.78000                                             
REMARK   3    B22 (A**2) : -0.78000                                             
REMARK   3    B33 (A**2) : 1.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.230         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.187         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.020         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2570 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2274 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3489 ; 1.373 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5267 ; 0.862 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   309 ; 6.366 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   370 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2874 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   570 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   440 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2413 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1522 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    88 ; 0.149 ; 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):     3 ; 0.059 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.254 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.157 ; 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):  1543 ; 2.645 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2482 ; 4.614 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 6.455 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1007 ;10.013 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -6        A    -1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.8890 -15.1500  53.8630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0623 T22:   0.0619                                     
REMARK   3      T33:   0.0627 T12:   0.0000                                     
REMARK   3      T13:  -0.0005 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.2512 L22:   3.8686                                     
REMARK   3      L33:  26.5322 L12:   7.3242                                     
REMARK   3      L13:  18.6134 L23:  -0.9271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1232 S12:   0.3995 S13:   0.0051                       
REMARK   3      S21:  -0.9740 S22:  -0.1938 S23:  -0.0765                       
REMARK   3      S31:  -0.0278 S32:   0.6788 S33:   0.0707                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.5160  21.0960  46.1960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0840 T22:   0.0504                                     
REMARK   3      T33:   0.0280 T12:   0.0089                                     
REMARK   3      T13:   0.0109 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1878 L22:   1.6019                                     
REMARK   3      L33:   0.8215 L12:   0.3340                                     
REMARK   3      L13:   0.0198 L23:  -0.2285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.0934 S13:   0.0094                       
REMARK   3      S21:   0.0423 S22:  -0.0308 S23:  -0.0114                       
REMARK   3      S31:  -0.0054 S32:  -0.0306 S33:   0.0022                       
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   : 1.40                                          
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 1WAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290021442.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 300.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.490                              
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   (%): 57.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN (10 MG/ML) IN 50 MM MES AT   
REMARK 280  PH 6, WAS PASSED THROUGH AN ULTRAFREE-MC 0.22 MM SPIN FILTER        
REMARK 280  UNIT (MILLIPORE) AND ALLOWED TO STAND AT 4 DEGREES C. PURPLE        
REMARK 280  CRYSTALS GREW SPONTANEOUSLY OVERNIGHT AND REACHED SIZES UP TO       
REMARK 280  0.5 MM IN SEVERAL WEEKS., TEMPERATURE 277K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.99900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.26900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.26900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.99850            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.26900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.26900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.99950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.26900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.26900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.99850            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.26900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.26900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       24.99950            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.99900            
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: 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 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 A  75   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP A 135   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 145   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 156   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 177   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 220   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 244   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    PHE A  69      -68.88   -109.63                                   
REMARK 500    PHE A 111       73.29   -152.26                                   
REMARK 500    SER A 189      142.38   -170.89                                   
REMARK 500    ALA A 191     -146.30    -98.82                                   
REMARK 500    HIS A 219      -48.29     73.88                                   
REMARK 500    ASN A 241      -34.75   -148.30                                   
REMARK 500    THR A 264      130.12    -36.51                                   
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                              FE A 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  12   OD1                                                    
REMARK 620 2 HOH A2008   O    82.5                                              
REMARK 620 3 ASP A  50   OD2  90.7  71.1                                        
REMARK 620 4 TYR A  53   OH   99.2 168.3  97.2                                  
REMARK 620 5 HIS A 221   NE2  93.4 102.3 171.8  89.2                            
REMARK 620 6 PO4 A 411   O4  167.2  84.6  84.8  93.3  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 184   NE2                                                    
REMARK 620 2 HIS A 219   ND1  88.0                                              
REMARK 620 3 PO4 A 411   O3  171.2  96.1                                        
REMARK 620 4 HOH A2008   O   107.6  88.0  80.4                                  
REMARK 620 5 ASP A  50   OD2  86.9 164.5  91.0  79.6                            
REMARK 620 6 ASN A  89   OD1  82.3  88.3  89.9 169.2 105.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1095                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 411                 
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                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 20 RESIDUES OF Q6IAS6 ARE NOT PART OF THE MATURE           
REMARK 999 ENZYME.  THE MATURE PROTEIN COMPRISES RESIDUES 21-325 AS             
REMARK 999 NUMBERED IN Q6IAS6.  A SIX AMINO ACID CLONING ARTIFACT IS            
REMARK 999 ATTACHED TO THE N-TERMINUS OF THE MATURE PROTEIN.                    
DBREF  1WAR A   -6    -1  PDB    1WAR     1WAR            -6     -1             
DBREF  1WAR A    1   304  UNP    Q6IAS6   Q6IAS6          22    325             
SEQADV 1WAR VAL A  127  UNP  Q6IAS6    MET   148 CONFLICT                       
SEQADV 1WAR VAL A  179  UNP  Q6IAS6    MET   200 CONFLICT                       
SEQRES   1 A  310  GLU ALA GLU ALA GLU PHE ALA THR PRO ALA LEU ARG PHE          
SEQRES   2 A  310  VAL ALA VAL GLY ASP TRP GLY GLY VAL PRO ASN ALA PRO          
SEQRES   3 A  310  PHE HIS THR ALA ARG GLU MET ALA ASN ALA LYS GLU ILE          
SEQRES   4 A  310  ALA ARG THR VAL GLN ILE LEU GLY ALA ASP PHE ILE LEU          
SEQRES   5 A  310  SER LEU GLY ASP ASN PHE TYR PHE THR GLY VAL GLN ASP          
SEQRES   6 A  310  ILE ASN ASP LYS ARG PHE GLN GLU THR PHE GLU ASP VAL          
SEQRES   7 A  310  PHE SER ASP ARG SER LEU ARG LYS VAL PRO TRP TYR VAL          
SEQRES   8 A  310  LEU ALA GLY ASN HIS ASP HIS LEU GLY ASN VAL SER ALA          
SEQRES   9 A  310  GLN ILE ALA TYR SER LYS ILE SER LYS ARG TRP ASN PHE          
SEQRES  10 A  310  PRO SER PRO PHE TYR ARG LEU HIS PHE LYS ILE PRO GLN          
SEQRES  11 A  310  THR ASN VAL SER VAL ALA ILE PHE MET LEU ASP THR VAL          
SEQRES  12 A  310  THR LEU CYS GLY ASN SER ASP ASP PHE LEU SER GLN GLN          
SEQRES  13 A  310  PRO GLU ARG PRO ARG ASP VAL LYS LEU ALA ARG THR GLN          
SEQRES  14 A  310  LEU SER TRP LEU LYS LYS GLN LEU ALA ALA ALA ARG GLU          
SEQRES  15 A  310  ASP TYR VAL LEU VAL ALA GLY HIS TYR PRO VAL TRP SER          
SEQRES  16 A  310  ILE ALA GLU HIS GLY PRO THR HIS CYS LEU VAL LYS GLN          
SEQRES  17 A  310  LEU ARG PRO LEU LEU ALA THR TYR GLY VAL THR ALA TYR          
SEQRES  18 A  310  LEU CYS GLY HIS ASP HIS ASN LEU GLN TYR LEU GLN ASP          
SEQRES  19 A  310  GLU ASN GLY VAL GLY TYR VAL LEU SER GLY ALA GLY ASN          
SEQRES  20 A  310  PHE MET ASP PRO SER LYS ARG HIS GLN ARG LYS VAL PRO          
SEQRES  21 A  310  ASN GLY TYR LEU ARG PHE HIS TYR GLY THR GLU ASP SER          
SEQRES  22 A  310  LEU GLY GLY PHE ALA TYR VAL GLU ILE SER SER LYS GLU          
SEQRES  23 A  310  MET THR VAL THR TYR ILE GLU ALA SER GLY LYS SER LEU          
SEQRES  24 A  310  PHE LYS THR ARG LEU PRO ARG ARG ALA ARG PRO                  
MODRES 1WAR ASN A   95  ASN  GLYCOSYLATION SITE                                 
HET     FE  A 401       1                                                       
HET     FE  A 402       1                                                       
HET    PO4  A 411       5                                                       
HET    NAG  A1095      25                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2   FE    2(FE 3+)                                                     
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   5  NAG    C8 H15 N O6                                                  
FORMUL   6  HOH   *61(H2 O)                                                     
HELIX    1   1 THR A   23  LEU A   40  1                                  18    
HELIX    2   2 LYS A   63  PHE A   69  1                                   7    
HELIX    3   3 HIS A   90  GLY A   94  5                                   5    
HELIX    4   4 ASN A   95  TYR A  102  1                                   8    
HELIX    5   5 SER A  103  ILE A  105  5                                   3    
HELIX    6   6 ASP A  135  GLY A  141  1                                   7    
HELIX    7   7 ASN A  142  PHE A  146  5                                   5    
HELIX    8   8 ASP A  156  ALA A  174  1                                  19    
HELIX    9   9 THR A  196  LEU A  203  1                                   8    
HELIX   10  10 LEU A  203  TYR A  210  1                                   8    
HELIX   11  11 HIS A  249  VAL A  253  5                                   5    
SHEET    1  AA 7 TRP A 109  ASN A 110  0                                        
SHEET    2  AA 7 TRP A  83  VAL A  85  1  O  TRP A  83   N  ASN A 110           
SHEET    3  AA 7 PHE A  44  SER A  47  1  O  ILE A  45   N  TYR A  84           
SHEET    4  AA 7 LEU A   5  VAL A  10  1  O  VAL A   8   N  LEU A  46           
SHEET    5  AA 7 GLY A 270  ILE A 276 -1  O  ALA A 272   N  ALA A   9           
SHEET    6  AA 7 GLU A 280  GLU A 287 -1  O  THR A 282   N  GLU A 275           
SHEET    7  AA 7 SER A 292  PRO A 299 -1  N  LEU A 293   O  TYR A 285           
SHEET    1  AB 7 TYR A 116  LYS A 121  0                                        
SHEET    2  AB 7 SER A 128  MET A 133 -1  O  VAL A 129   N  PHE A 120           
SHEET    3  AB 7 TYR A 178  ALA A 182  1  O  TYR A 178   N  ALA A 130           
SHEET    4  AB 7 ALA A 214  CYS A 217  1  O  ALA A 214   N  VAL A 181           
SHEET    5  AB 7 GLY A 233  SER A 237  1  O  GLY A 233   N  TYR A 215           
SHEET    6  AB 7 LEU A 223  GLN A 227 -1  O  GLN A 224   N  LEU A 236           
SHEET    7  AB 7 LEU A 258  TYR A 262 -1  N  ARG A 259   O  TYR A 225           
SSBOND   1 CYS A  140    CYS A  198                          1555   1555  2.04  
LINK         ND2 ASN A  95                 C1  NAG A1095     1555   1555  1.45  
LINK        FE    FE A 401                 OD1 ASP A  12     1555   1555  2.05  
LINK        FE    FE A 401                 O   HOH A2008     1555   1555  2.08  
LINK        FE    FE A 401                 OD2 ASP A  50     1555   1555  2.24  
LINK        FE    FE A 401                 OH  TYR A  53     1555   1555  1.95  
LINK        FE    FE A 401                 NE2 HIS A 221     1555   1555  2.22  
LINK        FE    FE A 401                 O4  PO4 A 411     1555   1555  2.12  
LINK        FE    FE A 402                 NE2 HIS A 184     1555   1555  2.18  
LINK        FE    FE A 402                 ND1 HIS A 219     1555   1555  2.22  
LINK        FE    FE A 402                 O3  PO4 A 411     1555   1555  2.15  
LINK        FE    FE A 402                 O   HOH A2008     1555   1555  1.74  
LINK        FE    FE A 402                 OD2 ASP A  50     1555   1555  2.17  
LINK        FE    FE A 402                 OD1 ASN A  89     1555   1555  2.06  
CISPEP   1 ALA A   19    PRO A   20          0         4.65                     
CISPEP   2 TYR A   53    PHE A   54          0         6.87                     
SITE     1 AC1  6 PHE A  -1  ASP A  59  ILE A  60  ASN A  95                    
SITE     2 AC1  6 ALA A  98  HOH A2011                                          
SITE     1 AC2  7 ASP A  12  ASP A  50  TYR A  53  HIS A 221                    
SITE     2 AC2  7  FE A 402  PO4 A 411  HOH A2008                               
SITE     1 AC3  7 ASP A  50  ASN A  89  HIS A 184  HIS A 219                    
SITE     2 AC3  7  FE A 401  PO4 A 411  HOH A2008                               
SITE     1 AC4 11 ASP A  50  TYR A  53  ASN A  89  HIS A  90                    
SITE     2 AC4 11 HIS A 193  HIS A 219  HIS A 221   FE A 401                    
SITE     3 AC4 11  FE A 402  HOH A2008  HOH A2061                               
CRYST1   80.538   80.538   99.998  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012416  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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