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Database: PDB
Entry: 1QFC
LinkDB: 1QFC
Original site: 1QFC 
HEADER    HYDROLASE                               08-APR-99   1QFC              
TITLE     STRUCTURE OF RAT PURPLE ACID PHOSPHATASE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (PURPLE ACID PHOSPHATASE);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TARTRATE RESISTANT ACID PHOSPHATASE, TRAP;                  
COMPND   5 EC: 3.1.3.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS                                
KEYWDS    HYDROLASE, METAL PHOSPHATASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.UPPENBERG,F.LINDQVIST,C.SVENSSON,B.EK-RYLANDER,G.ANDERSSON          
REVDAT   4   29-JUL-20 1QFC    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 1QFC    1       VERSN                                    
REVDAT   2   24-FEB-09 1QFC    1       VERSN                                    
REVDAT   1   10-APR-00 1QFC    0                                                
JRNL        AUTH   J.UPPENBERG,F.LINDQVIST,C.SVENSSON,B.EK-RYLANDER,G.ANDERSSON 
JRNL        TITL   CRYSTAL STRUCTURE OF A MAMMALIAN PURPLE ACID PHOSPHATASE.    
JRNL        REF    J.MOL.BIOL.                   V. 290   201 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10388567                                                     
JRNL        DOI    10.1006/JMBI.1999.2896                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.4                                              
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
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)   (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10276                          
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) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1058                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1088                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.80                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 132                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2269                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -17.00000                                            
REMARK   3    B22 (A**2) : -17.00000                                            
REMARK   3    B33 (A**2) : 34.17000                                             
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.59                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.930                           
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) : 3.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 8.060 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 11.110; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 42.13                                                
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  : MYTOP:PROTEIN_REP.PARAM                        
REMARK   3  PARAMETER FILE  2  : MYTOP:ION_JONAS.PARAM                          
REMARK   3  PARAMETER FILE  3  : MYTOP:CARBOHYDRATE.PARAM                       
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : MYTOP:PROTEIN.TOP                              
REMARK   3  TOPOLOGY FILE  2   : MYTOP:ION_JONAS.TOP                            
REMARK   3  TOPOLOGY FILE  3   : MYTOP:CARBOHYDRATE.TOP                         
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000000815.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE, SHARP                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       58.19000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       58.19000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.63500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       58.19000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       15.81750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       58.19000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.45250            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       58.19000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.19000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       31.63500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       58.19000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       47.45250            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       58.19000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       15.81750            
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                                     
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     ASP A   146                                                      
REMARK 465     ASP A   147                                                      
REMARK 465     PHE A   148                                                      
REMARK 465     VAL A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     GLN A   151                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     MET A   155                                                      
REMARK 465     PRO A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     PRO A   306                                                      
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    TYR A  55   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    CYS A 142   CA  -  CB  -  SG  ANGL. DEV. =   6.8 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    PRO A   3       37.28    -58.99                                   
REMARK 500    SER A   5       48.30    -75.71                                   
REMARK 500    PHE A   9      147.83   -176.83                                   
REMARK 500    PRO A  19     -158.18    -68.69                                   
REMARK 500    ASN A  20     -172.16     77.24                                   
REMARK 500    PRO A  22     -144.26    -83.69                                   
REMARK 500    VAL A  59      119.24     76.83                                   
REMARK 500    HIS A  60      -87.78    -81.40                                   
REMARK 500    ASN A  63      -43.60     83.94                                   
REMARK 500    PHE A  75       54.60    -91.59                                   
REMARK 500    ASP A  77      123.19   -171.36                                   
REMARK 500    ARG A  78      -27.97    -36.98                                   
REMARK 500    ARG A  81      -15.01    -41.17                                   
REMARK 500    ASN A  82       24.95   -147.66                                   
REMARK 500    PHE A 113       76.78   -162.84                                   
REMARK 500    PRO A 125       -7.64    -53.94                                   
REMARK 500    ARG A 126       44.81    -99.61                                   
REMARK 500    SER A 127     -111.20     37.04                                   
REMARK 500    ASN A 128      -48.55    -15.98                                   
REMARK 500    CYS A 142     -131.74   -125.77                                   
REMARK 500    ALA A 162       65.83   -162.61                                   
REMARK 500    GLU A 178      170.12    -56.92                                   
REMARK 500    ILE A 189      -62.20    -93.16                                   
REMARK 500    SER A 191      134.19   -176.64                                   
REMARK 500    ALA A 193     -165.69    -65.52                                   
REMARK 500    HIS A 221      -49.12     79.04                                   
REMARK 500    HIS A 223       75.19    -65.79                                   
REMARK 500    ASN A 224     -177.70   -175.67                                   
REMARK 500    GLU A 231        7.56    -63.59                                   
REMARK 500    ASN A 243      -39.10   -134.56                                   
REMARK 500    VAL A 249       29.66   -144.08                                   
REMARK 500    PRO A 256      109.36    -52.42                                   
REMARK 500    ASN A 257      128.53    -30.17                                   
REMARK 500    LEU A 270     -150.47    -76.38                                   
REMARK 500    PHE A 296      133.74   -174.15                                   
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 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  14   OD2                                                    
REMARK 620 2 ASP A  52   OD2  72.1                                              
REMARK 620 3 TYR A  55   OH   72.8  91.1                                        
REMARK 620 4 HIS A 223   NE2  96.3 162.3  72.5                                  
REMARK 620 N                    1     2     3                                   
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  52   OD2                                                    
REMARK 620 2 ASN A  91   OD1 113.3                                              
REMARK 620 3 HIS A 186   NE2  79.9  85.9                                        
REMARK 620 4 HIS A 221   ND1 152.7  92.2  93.0                                  
REMARK 620 5 PO4 A 410   O2   95.7  73.0 154.8 101.3                            
REMARK 620 N                    1     2     3     4                             
DBREF  1QFC A    1   306  UNP    P29288   PPA5_RAT        22    327             
SEQRES   1 A  306  THR ALA PRO ALA SER THR LEU ARG PHE VAL ALA VAL GLY          
SEQRES   2 A  306  ASP TRP GLY GLY VAL PRO ASN ALA PRO PHE HIS THR ALA          
SEQRES   3 A  306  ARG GLU MET ALA ASN ALA LYS GLU ILE ALA ARG THR VAL          
SEQRES   4 A  306  GLN ILE MET GLY ALA ASP PHE ILE MET SER LEU GLY ASP          
SEQRES   5 A  306  ASN PHE TYR PHE THR GLY VAL HIS ASP ALA ASN ASP LYS          
SEQRES   6 A  306  ARG PHE GLN GLU THR PHE GLU ASP VAL PHE SER ASP ARG          
SEQRES   7 A  306  ALA LEU ARG ASN ILE PRO TRP TYR VAL LEU ALA GLY ASN          
SEQRES   8 A  306  HIS ASP HIS LEU GLY ASN VAL SER ALA GLN ILE ALA TYR          
SEQRES   9 A  306  SER LYS ILE SER LYS ARG TRP ASN PHE PRO SER PRO TYR          
SEQRES  10 A  306  TYR ARG LEU ARG PHE LYS VAL PRO ARG SER ASN ILE THR          
SEQRES  11 A  306  VAL ALA ILE PHE MET LEU ASP THR VAL MET LEU CYS GLY          
SEQRES  12 A  306  ASN SER ASP ASP PHE VAL SER GLN GLN PRO GLU MET PRO          
SEQRES  13 A  306  ARG ASP LEU GLY VAL ALA ARG THR GLN LEU SER TRP LEU          
SEQRES  14 A  306  LYS LYS GLN LEU ALA ALA ALA LYS GLU ASP TYR VAL LEU          
SEQRES  15 A  306  VAL ALA GLY HIS TYR PRO ILE TRP SER ILE ALA GLU HIS          
SEQRES  16 A  306  GLY PRO THR ARG CYS LEU VAL LYS ASN LEU ARG PRO LEU          
SEQRES  17 A  306  LEU ALA ALA TYR GLY VAL THR ALA TYR LEU CYS GLY HIS          
SEQRES  18 A  306  ASP HIS ASN LEU GLN TYR LEU GLN ASP GLU ASN GLY VAL          
SEQRES  19 A  306  GLY TYR VAL LEU SER GLY ALA GLY ASN PHE MET ASP PRO          
SEQRES  20 A  306  SER VAL ARG HIS GLN ARG LYS VAL PRO ASN GLY TYR LEU          
SEQRES  21 A  306  ARG PHE HIS TYR GLY SER GLU ASP SER LEU GLY GLY PHE          
SEQRES  22 A  306  THR TYR VAL GLU ILE GLY SER LYS GLU MET SER ILE THR          
SEQRES  23 A  306  TYR VAL GLU ALA SER GLY LYS SER LEU PHE LYS THR SER          
SEQRES  24 A  306  LEU PRO ARG ARG PRO ARG PRO                                  
MODRES 1QFC ASN A   97  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 400      14                                                       
HET     FE  A 401       1                                                       
HET     FE  A 402       1                                                       
HET    PO4  A 410       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      FE FE (III) ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  PO4    O4 P 3-                                                      
HELIX    1   1 ALA A   26  ILE A   41  1                                  16    
HELIX    2   2 ARG A   66  VAL A   74  5                                   9    
HELIX    3   3 HIS A   92  HIS A   94  5                                   3    
HELIX    4   4 VAL A   98  LYS A  106  1                                   9    
HELIX    5   5 THR A  138  LEU A  141  1                                   4    
HELIX    6   6 GLN A  165  ALA A  175  1                                  11    
HELIX    7   7 ARG A  199  ASN A  204  1                                   6    
HELIX    8   8 ARG A  206  TYR A  212  1                                   7    
SHEET    1   A 6 PRO A  84  TYR A  86  0                                        
SHEET    2   A 6 PHE A  46  SER A  49  1  N  ILE A  47   O  PRO A  84           
SHEET    3   A 6 LEU A   7  VAL A  12  1  N  VAL A  10   O  PHE A  46           
SHEET    4   A 6 GLY A 272  ILE A 278 -1  N  ILE A 278   O  LEU A   7           
SHEET    5   A 6 GLU A 282  GLU A 289 -1  N  VAL A 288   O  PHE A 273           
SHEET    6   A 6 SER A 294  PRO A 301 -1  N  LEU A 300   O  MET A 283           
SHEET    1   B 7 TYR A 118  LYS A 123  0                                        
SHEET    2   B 7 THR A 130  MET A 135 -1  N  MET A 135   O  TYR A 118           
SHEET    3   B 7 TYR A 180  ALA A 184  1  N  TYR A 180   O  ALA A 132           
SHEET    4   B 7 ALA A 216  CYS A 219  1  N  ALA A 216   O  VAL A 183           
SHEET    5   B 7 GLY A 235  SER A 239  1  N  GLY A 235   O  TYR A 217           
SHEET    6   B 7 LEU A 225  GLN A 229 -1  N  LEU A 228   O  TYR A 236           
SHEET    7   B 7 LEU A 260  TYR A 264 -1  N  TYR A 264   O  LEU A 225           
SSBOND   1 CYS A  142    CYS A  200                          1555   1555  2.03  
LINK         ND2 ASN A  97                 C1  NAG A 400     1555   1555  1.46  
LINK         OD2 ASP A  14                FE    FE A 402     1555   1555  2.15  
LINK         OD2 ASP A  52                FE    FE A 401     1555   1555  2.21  
LINK         OD2 ASP A  52                FE    FE A 402     1555   1555  2.13  
LINK         OH  TYR A  55                FE    FE A 402     1555   1555  1.96  
LINK         OD1 ASN A  91                FE    FE A 401     1555   1555  2.02  
LINK         NE2 HIS A 186                FE    FE A 401     1555   1555  2.18  
LINK         ND1 HIS A 221                FE    FE A 401     1555   1555  2.15  
LINK         NE2 HIS A 223                FE    FE A 402     1555   1555  2.09  
LINK        FE    FE A 401                 O2  PO4 A 410     1555   1555  2.47  
CISPEP   1 VAL A   18    PRO A   19          0         0.42                     
CISPEP   2 ALA A   21    PRO A   22          0        -0.58                     
CRYST1  116.380  116.380   63.270  90.00  90.00  90.00 I 41          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      0.008592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015805        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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