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Database: PDB
Entry: 1CVI
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Original site: 1CVI 
HEADER    HYDROLASE                               23-AUG-99   1CVI              
TITLE     CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTATIC ACID PHOSPHATASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.3.2                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 SECRETION: SEMINAL FLUID                                             
KEYWDS    ACID PHOSPHATASE, INHIBITION, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.G.JAKOB,K.LEWINSKI,R.KUCIEL,W.OSTROWSKI,L.LEBIODA                   
REVDAT   8   29-JUL-20 1CVI    1       COMPND REMARK HETNAM LINK                
REVDAT   8 2                   1       SITE   ATOM                              
REVDAT   7   24-JAN-18 1CVI    1       JRNL                                     
REVDAT   6   04-OCT-17 1CVI    1       REMARK                                   
REVDAT   5   13-JUL-11 1CVI    1       VERSN                                    
REVDAT   4   24-FEB-09 1CVI    1       VERSN                                    
REVDAT   3   01-APR-03 1CVI    1       JRNL                                     
REVDAT   2   07-APR-00 1CVI    1       JRNL                                     
REVDAT   1   31-AUG-99 1CVI    0                                                
JRNL        AUTH   C.G.JAKOB,K.LEWINSKI,R.KUCIEL,W.OSTROWSKI,L.LEBIODA          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE .      
JRNL        REF    PROSTATE                      V.  42   211 2000              
JRNL        REFN                   ISSN 0270-4137                               
JRNL        PMID   10639192                                                     
JRNL        DOI    10.1002/(SICI)1097-0045(20000215)42:3<211::AID-PROS7>3.0.CO; 
JRNL        DOI  2 2-U                                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.W.LACOUNT,G.HANDY,L.LEBIODA                                
REMARK   1  TITL   STRUCTURAL ORIGINS OF L(+)-TARTARATE INHIBITION OF HUMAN     
REMARK   1  TITL 2 PROSTATIC ACID PHOSPHATASE                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 273 30406 1998              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  DOI    10.1074/JBC.273.46.30406                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   L.LOVELACE,K.LEWINSKI,C.G.JAKOB,R.KUCIEL,W.OSTROWSKI,        
REMARK   1  AUTH 2 L.LEBIODA                                                    
REMARK   1  TITL   PROSTATIC ACID PHOSPHATASE: STRUCTURAL ASPECTS OF INHIBITION 
REMARK   1  TITL 2 BY L-(+)-TARTARATE IONS                                      
REMARK   1  REF    ACTA BIOCHIM.POL.             V.  44   673 1997              
REMARK   1  REFN                   ISSN 0001-527X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27778                          
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) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1805                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3787                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2140                       
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 265                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11204                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 539                                     
REMARK   3   SOLVENT ATOMS            : 633                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.62                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.570                           
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) : 5.480 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 8.540 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.750 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 11.350; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009564.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-93                          
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 10.0                               
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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.160                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.16                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MERLOT                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1450, POTASSIUM CHLORIDE, GLYCINE,   
REMARK 280  PH 10.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       63.16500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.51000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      103.98000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.51000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       63.16500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      103.98000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 57.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G, H, I                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, K, L, M                      
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: 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    TYR A1057       36.26   -100.00                                   
REMARK 500    LEU A1061       64.84   -105.95                                   
REMARK 500    TYR A1065      102.33      6.86                                   
REMARK 500    HIS A1067      -26.83    -38.18                                   
REMARK 500    ILE A1099       91.69    -58.84                                   
REMARK 500    ASP A1119       90.77    -64.67                                   
REMARK 500    GLN A1120       36.70    -97.77                                   
REMARK 500    LEU A1121      -42.28   -147.00                                   
REMARK 500    ASN A1128       47.41    -96.98                                   
REMARK 500    GLN A1168      -11.30    -45.09                                   
REMARK 500    ASP A1169      106.29    -47.13                                   
REMARK 500    TYR A1182      -70.47    -63.30                                   
REMARK 500    ILE A1217      -11.41     64.28                                   
REMARK 500    HIS A1218     -113.33   -121.22                                   
REMARK 500    GLN A1220      -81.47      0.32                                   
REMARK 500    VAL A1270       15.33   -140.01                                   
REMARK 500    GLN A1304       44.69    -79.60                                   
REMARK 500    HIS A1305      140.24    164.12                                   
REMARK 500    TRP A1336      -52.75    -25.27                                   
REMARK 500    SER B2029      -18.67    -44.09                                   
REMARK 500    TYR B2057       33.68    -98.22                                   
REMARK 500    LEU B2061       65.03   -107.72                                   
REMARK 500    TYR B2065      101.26      7.51                                   
REMARK 500    ILE B2099       91.72    -59.48                                   
REMARK 500    ASP B2119       91.83    -64.75                                   
REMARK 500    GLN B2120       37.72    -98.09                                   
REMARK 500    LEU B2121      -41.17   -148.37                                   
REMARK 500    ASN B2128       47.53    -96.35                                   
REMARK 500    GLN B2168      -11.21    -45.97                                   
REMARK 500    ASP B2169      105.73    -47.35                                   
REMARK 500    TYR B2182      -70.48    -61.94                                   
REMARK 500    ILE B2217      -12.68     63.53                                   
REMARK 500    HIS B2218     -111.45   -120.39                                   
REMARK 500    GLN B2220      -82.58      1.43                                   
REMARK 500    GLU B2302      133.11   -170.15                                   
REMARK 500    GLN B2304       42.71    -79.26                                   
REMARK 500    HIS B2305      138.20    165.93                                   
REMARK 500    TRP B2336      -51.16    -25.01                                   
REMARK 500    SER C3029      -19.85    -43.90                                   
REMARK 500    TYR C3057       33.21    -98.93                                   
REMARK 500    LEU C3061       65.43   -105.60                                   
REMARK 500    TYR C3065      102.40      7.84                                   
REMARK 500    ILE C3099       92.67    -57.01                                   
REMARK 500    ASP C3119       91.16    -63.64                                   
REMARK 500    GLN C3120       36.54    -97.51                                   
REMARK 500    LEU C3121      -44.54   -146.78                                   
REMARK 500    ASN C3128       47.22    -94.61                                   
REMARK 500    GLN C3168      -10.48    -46.04                                   
REMARK 500    ASP C3169      106.26    -47.86                                   
REMARK 500    TYR C3182      -70.39    -60.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HPA   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC    
REMARK 900 ACID PHOSPHATASE                                                     
DBREF  1CVI A 1001  1342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  1CVI B 2001  2342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  1CVI C 3001  3342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  1CVI D 4001  4342  UNP    P15309   PPAP_HUMAN      33    374             
SEQRES   1 A  342  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 A  342  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 A  342  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 A  342  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 A  342  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 A  342  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 A  342  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 A  342  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 A  342  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 A  342  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 A  342  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 A  342  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 A  342  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 A  342  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 A  342  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 A  342  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 A  342  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 A  342  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 A  342  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 A  342  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 A  342  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 A  342  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 A  342  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 A  342  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 A  342  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 A  342  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 A  342  GLU CYS MET THR                                              
SEQRES   1 B  342  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 B  342  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 B  342  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 B  342  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 B  342  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 B  342  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 B  342  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 B  342  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 B  342  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 B  342  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 B  342  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 B  342  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 B  342  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 B  342  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 B  342  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 B  342  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 B  342  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 B  342  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 B  342  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 B  342  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 B  342  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 B  342  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 B  342  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 B  342  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 B  342  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 B  342  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 B  342  GLU CYS MET THR                                              
SEQRES   1 C  342  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 C  342  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 C  342  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 C  342  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 C  342  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 C  342  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 C  342  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 C  342  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 C  342  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 C  342  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 C  342  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 C  342  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 C  342  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 C  342  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 C  342  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 C  342  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 C  342  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 C  342  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 C  342  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 C  342  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 C  342  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 C  342  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 C  342  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 C  342  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 C  342  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 C  342  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 C  342  GLU CYS MET THR                                              
SEQRES   1 D  342  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 D  342  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 D  342  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 D  342  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 D  342  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 D  342  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 D  342  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 D  342  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 D  342  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 D  342  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 D  342  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 D  342  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 D  342  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 D  342  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 D  342  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 D  342  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 D  342  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 D  342  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 D  342  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 D  342  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 D  342  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 D  342  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 D  342  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 D  342  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 D  342  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 D  342  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 D  342  GLU CYS MET THR                                              
MODRES 1CVI ASN A 1062  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN A 1188  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN A 1301  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN B 2062  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN B 2188  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN B 2301  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN C 3062  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN C 3188  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN C 3301  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN D 4062  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN D 4188  ASN  GLYCOSYLATION SITE                                 
MODRES 1CVI ASN D 4301  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    NAG  E   5      14                                                       
HET    MAN  E   6      11                                                       
HET    NAG  E   7      14                                                       
HET    FUC  E   8      10                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    BMA  H   3      11                                                       
HET    MAN  H   4      11                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    BMA  I   3      11                                                       
HET    MAN  I   4      11                                                       
HET    MAN  I   5      11                                                       
HET    MAN  I   6      11                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    BMA  J   3      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    BMA  K   3      11                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    BMA  L   3      11                                                       
HET    MAN  L   4      11                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    BMA  M   3      11                                                       
HET    NAG  A1361      14                                                       
HET    GLY  A1350       5                                                       
HET    GLY  B2350       5                                                       
HET    NAG  C3361      14                                                       
HET    GLY  C3350       5                                                       
HET    NAG  D4371      14                                                       
HET    GLY  D4350       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GLY GLYCINE                                                          
FORMUL   5  NAG    23(C8 H15 N O6)                                              
FORMUL   5  BMA    9(C6 H12 O6)                                                 
FORMUL   5  MAN    8(C6 H12 O6)                                                 
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL  15  GLY    4(C2 H5 N O2)                                                
FORMUL  21  HOH   *633(H2 O)                                                    
HELIX    1   1 LYS A 1027  TRP A 1031  5                                   5    
HELIX    2   2 THR A 1039  TYR A 1057  1                                  19    
HELIX    3   3 VAL A 1077  PHE A 1092  1                                  16    
HELIX    4   4 GLU A 1095  ILE A 1099  5                                   5    
HELIX    5   5 PRO A 1115  ASP A 1119  5                                   5    
HELIX    6   6 CYS A 1129  SER A 1142  1                                  14    
HELIX    7   7 SER A 1142  HIS A 1150  1                                   9    
HELIX    8   8 TYR A 1152  GLY A 1164  1                                  13    
HELIX    9   9 ASP A 1169  VAL A 1177  1                                   9    
HELIX   10  10 VAL A 1177  HIS A 1187  1                                  11    
HELIX   11  11 THR A 1196  GLY A 1216  1                                  21    
HELIX   12  12 LYS A 1219  ARG A 1225  1                                   7    
HELIX   13  13 GLY A 1228  ILE A 1245  1                                  18    
HELIX   14  14 HIS A 1257  LEU A 1268  1                                  12    
HELIX   15  15 LEU A 1321  GLY A 1329  1                                   9    
HELIX   16  16 PRO A 1330  ILE A 1332  5                                   3    
HELIX   17  17 ASP A 1335  MET A 1341  1                                   7    
HELIX   18  18 LYS B 2027  TRP B 2031  5                                   5    
HELIX   19  19 THR B 2039  TYR B 2057  1                                  19    
HELIX   20  20 VAL B 2077  PHE B 2092  1                                  16    
HELIX   21  21 GLU B 2095  ILE B 2099  5                                   5    
HELIX   22  22 PRO B 2115  ASP B 2119  5                                   5    
HELIX   23  23 CYS B 2129  SER B 2142  1                                  14    
HELIX   24  24 SER B 2142  HIS B 2150  1                                   9    
HELIX   25  25 TYR B 2152  GLY B 2164  1                                  13    
HELIX   26  26 ASP B 2169  VAL B 2177  1                                   9    
HELIX   27  27 VAL B 2177  HIS B 2187  1                                  11    
HELIX   28  28 THR B 2196  GLY B 2216  1                                  21    
HELIX   29  29 LYS B 2219  ARG B 2225  1                                   7    
HELIX   30  30 GLY B 2228  ILE B 2245  1                                  18    
HELIX   31  31 HIS B 2257  ASP B 2269  1                                  13    
HELIX   32  32 LEU B 2321  GLY B 2329  1                                   9    
HELIX   33  33 ASP B 2335  MET B 2341  1                                   7    
HELIX   34  34 LYS C 3027  TRP C 3031  5                                   5    
HELIX   35  35 THR C 3039  TYR C 3057  1                                  19    
HELIX   36  36 VAL C 3077  PHE C 3092  1                                  16    
HELIX   37  37 GLU C 3095  ILE C 3099  5                                   5    
HELIX   38  38 PRO C 3115  ASP C 3119  5                                   5    
HELIX   39  39 CYS C 3129  SER C 3142  1                                  14    
HELIX   40  40 SER C 3142  HIS C 3150  1                                   9    
HELIX   41  41 TYR C 3152  GLY C 3164  1                                  13    
HELIX   42  42 ASP C 3169  VAL C 3177  1                                   9    
HELIX   43  43 VAL C 3177  HIS C 3187  1                                  11    
HELIX   44  44 THR C 3196  GLY C 3216  1                                  21    
HELIX   45  45 LYS C 3219  ARG C 3225  1                                   7    
HELIX   46  46 GLY C 3228  ILE C 3245  1                                  18    
HELIX   47  47 HIS C 3257  LEU C 3268  1                                  12    
HELIX   48  48 LEU C 3321  GLY C 3329  1                                   9    
HELIX   49  49 ASP C 3335  MET C 3341  1                                   7    
HELIX   50  50 LYS D 4027  TRP D 4031  5                                   5    
HELIX   51  51 THR D 4039  TYR D 4057  1                                  19    
HELIX   52  52 VAL D 4077  PHE D 4092  1                                  16    
HELIX   53  53 GLU D 4095  ILE D 4099  5                                   5    
HELIX   54  54 CYS D 4129  SER D 4142  1                                  14    
HELIX   55  55 SER D 4142  HIS D 4150  1                                   9    
HELIX   56  56 TYR D 4152  GLY D 4164  1                                  13    
HELIX   57  57 ASP D 4169  VAL D 4177  1                                   9    
HELIX   58  58 VAL D 4177  HIS D 4187  1                                  11    
HELIX   59  59 THR D 4196  GLY D 4216  1                                  21    
HELIX   60  60 LYS D 4219  ARG D 4225  1                                   7    
HELIX   61  61 GLY D 4228  ILE D 4245  1                                  18    
HELIX   62  62 HIS D 4257  LEU D 4268  1                                  12    
HELIX   63  63 LEU D 4321  GLY D 4329  1                                   9    
HELIX   64  64 PRO D 4330  ILE D 4332  5                                   3    
HELIX   65  65 ASP D 4335  MET D 4341  1                                   7    
SHEET    1   A 7 HIS A1112  VAL A1114  0                                        
SHEET    2   A 7 VAL A1070  THR A1075  1  O  ILE A1072   N  HIS A1112           
SHEET    3   A 7 LEU A1251  ALA A1256  1  O  LEU A1251   N  TYR A1071           
SHEET    4   A 7 GLU A1002  ARG A1011  1  O  VAL A1006   N  ILE A1252           
SHEET    5   A 7 CYS A1281  GLU A1289 -1  N  HIS A1282   O  VAL A1009           
SHEET    6   A 7 GLU A1292  ARG A1300 -1  O  GLU A1292   N  GLU A1289           
SHEET    7   A 7 TYR A1308  PRO A1309 -1  N  TYR A1308   O  TYR A1299           
SHEET    1  A1 7 HIS A1112  VAL A1114  0                                        
SHEET    2  A1 7 VAL A1070  THR A1075  1  O  ILE A1072   N  HIS A1112           
SHEET    3  A1 7 LEU A1251  ALA A1256  1  O  LEU A1251   N  TYR A1071           
SHEET    4  A1 7 GLU A1002  ARG A1011  1  O  VAL A1006   N  ILE A1252           
SHEET    5  A1 7 CYS A1281  GLU A1289 -1  N  HIS A1282   O  VAL A1009           
SHEET    6  A1 7 GLU A1292  ARG A1300 -1  O  GLU A1292   N  GLU A1289           
SHEET    7  A1 7 SER A1318  PRO A1320 -1  O  CYS A1319   N  VAL A1295           
SHEET    1   B 7 HIS B2112  VAL B2114  0                                        
SHEET    2   B 7 VAL B2070  THR B2075  1  O  ILE B2072   N  HIS B2112           
SHEET    3   B 7 LEU B2251  ALA B2256  1  O  LEU B2251   N  TYR B2071           
SHEET    4   B 7 GLU B2002  ARG B2011  1  O  VAL B2006   N  ILE B2252           
SHEET    5   B 7 CYS B2281  GLU B2289 -1  N  HIS B2282   O  VAL B2009           
SHEET    6   B 7 GLU B2292  ARG B2300 -1  O  GLU B2292   N  GLU B2289           
SHEET    7   B 7 TYR B2308  PRO B2309 -1  N  TYR B2308   O  TYR B2299           
SHEET    1  B1 7 HIS B2112  VAL B2114  0                                        
SHEET    2  B1 7 VAL B2070  THR B2075  1  O  ILE B2072   N  HIS B2112           
SHEET    3  B1 7 LEU B2251  ALA B2256  1  O  LEU B2251   N  TYR B2071           
SHEET    4  B1 7 GLU B2002  ARG B2011  1  O  VAL B2006   N  ILE B2252           
SHEET    5  B1 7 CYS B2281  GLU B2289 -1  N  HIS B2282   O  VAL B2009           
SHEET    6  B1 7 GLU B2292  ARG B2300 -1  O  GLU B2292   N  GLU B2289           
SHEET    7  B1 7 SER B2318  PRO B2320 -1  O  CYS B2319   N  VAL B2295           
SHEET    1   C 7 HIS C3112  VAL C3114  0                                        
SHEET    2   C 7 VAL C3070  THR C3075  1  O  ILE C3072   N  HIS C3112           
SHEET    3   C 7 LEU C3251  ALA C3256  1  O  LEU C3251   N  TYR C3071           
SHEET    4   C 7 GLU C3002  ARG C3011  1  O  VAL C3006   N  ILE C3252           
SHEET    5   C 7 CYS C3281  GLU C3289 -1  N  HIS C3282   O  VAL C3009           
SHEET    6   C 7 GLU C3292  ARG C3300 -1  O  GLU C3292   N  GLU C3289           
SHEET    7   C 7 TYR C3308  PRO C3309 -1  N  TYR C3308   O  TYR C3299           
SHEET    1  C1 7 HIS C3112  VAL C3114  0                                        
SHEET    2  C1 7 VAL C3070  THR C3075  1  O  ILE C3072   N  HIS C3112           
SHEET    3  C1 7 LEU C3251  ALA C3256  1  O  LEU C3251   N  TYR C3071           
SHEET    4  C1 7 GLU C3002  ARG C3011  1  O  VAL C3006   N  ILE C3252           
SHEET    5  C1 7 CYS C3281  GLU C3289 -1  N  HIS C3282   O  VAL C3009           
SHEET    6  C1 7 GLU C3292  ARG C3300 -1  O  GLU C3292   N  GLU C3289           
SHEET    7  C1 7 SER C3318  PRO C3320 -1  O  CYS C3319   N  VAL C3295           
SHEET    1   D 7 HIS D4112  VAL D4114  0                                        
SHEET    2   D 7 VAL D4070  THR D4075  1  O  ILE D4072   N  HIS D4112           
SHEET    3   D 7 LEU D4251  ALA D4256  1  O  LEU D4251   N  TYR D4071           
SHEET    4   D 7 GLU D4002  ARG D4011  1  O  VAL D4006   N  ILE D4252           
SHEET    5   D 7 CYS D4281  GLU D4289 -1  N  HIS D4282   O  VAL D4009           
SHEET    6   D 7 GLU D4292  ARG D4300 -1  O  GLU D4292   N  GLU D4289           
SHEET    7   D 7 TYR D4308  PRO D4309 -1  N  TYR D4308   O  TYR D4299           
SHEET    1  D1 7 HIS D4112  VAL D4114  0                                        
SHEET    2  D1 7 VAL D4070  THR D4075  1  O  ILE D4072   N  HIS D4112           
SHEET    3  D1 7 LEU D4251  ALA D4256  1  O  LEU D4251   N  TYR D4071           
SHEET    4  D1 7 GLU D4002  ARG D4011  1  O  VAL D4006   N  ILE D4252           
SHEET    5  D1 7 CYS D4281  GLU D4289 -1  N  HIS D4282   O  VAL D4009           
SHEET    6  D1 7 GLU D4292  ARG D4300 -1  O  GLU D4292   N  GLU D4289           
SHEET    7  D1 7 SER D4318  PRO D4320 -1  O  CYS D4319   N  VAL D4295           
SSBOND   1 CYS A 1129    CYS A 1340                          1555   1555  2.03  
SSBOND   2 CYS A 1315    CYS A 1319                          1555   1555  2.03  
SSBOND   3 CYS B 2129    CYS B 2340                          1555   1555  2.03  
SSBOND   4 CYS B 2315    CYS B 2319                          1555   1555  2.03  
SSBOND   5 CYS C 3129    CYS C 3340                          1555   1555  2.02  
SSBOND   6 CYS C 3315    CYS C 3319                          1555   1555  2.03  
SSBOND   7 CYS D 4129    CYS D 4340                          1555   1555  2.03  
SSBOND   8 CYS D 4315    CYS D 4319                          1555   1555  2.02  
LINK         ND2 ASN A1062                 C1  NAG A1361     1555   1555  1.45  
LINK         ND2 ASN A1188                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN A1301                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN B2062                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN B2188                 C1  NAG H   1     1555   1555  1.45  
LINK         ND2 ASN B2301                 C1  NAG I   1     1555   1555  1.45  
LINK         ND2 ASN C3062                 C1  NAG C3361     1555   1555  1.45  
LINK         ND2 ASN C3188                 C1  NAG J   1     1555   1555  1.45  
LINK         ND2 ASN C3301                 C1  NAG K   1     1555   1555  1.45  
LINK         ND2 ASN D4062                 C1  NAG L   1     1555   1555  1.46  
LINK         ND2 ASN D4188                 C1  NAG D4371     1555   1555  1.45  
LINK         ND2 ASN D4301                 C1  NAG M   1     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.39  
LINK         O6  NAG E   1                 C1  FUC E   8     1555   1555  1.41  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.40  
LINK         O3  BMA E   3                 C1  MAN E   4     1555   1555  1.40  
LINK         O6  BMA E   3                 C1  MAN E   6     1555   1555  1.41  
LINK         O2  MAN E   4                 C1  NAG E   5     1555   1555  1.39  
LINK         O2  MAN E   6                 C1  NAG E   7     1555   1555  1.39  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.40  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.39  
LINK         O3  BMA F   3                 C1  MAN F   4     1555   1555  1.41  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.39  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.39  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.40  
LINK         O4  NAG H   2                 C1  BMA H   3     1555   1555  1.39  
LINK         O6  BMA H   3                 C1  MAN H   4     1555   1555  1.41  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.39  
LINK         O4  NAG I   2                 C1  BMA I   3     1555   1555  1.40  
LINK         O6  BMA I   3                 C1  MAN I   4     1555   1555  1.41  
LINK         O3  BMA I   3                 C1  MAN I   6     1555   1555  1.41  
LINK         O6  MAN I   4                 C1  MAN I   5     1555   1555  1.40  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.39  
LINK         O4  NAG J   2                 C1  BMA J   3     1555   1555  1.39  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.40  
LINK         O4  NAG K   2                 C1  BMA K   3     1555   1555  1.40  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.39  
LINK         O4  NAG L   2                 C1  BMA L   3     1555   1555  1.39  
LINK         O6  BMA L   3                 C1  MAN L   4     1555   1555  1.41  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.39  
LINK         O4  NAG M   2                 C1  BMA M   3     1555   1555  1.39  
CISPEP   1 LEU A 1124    PRO A 1125          0         0.04                     
CISPEP   2 LEU B 2124    PRO B 2125          0         0.14                     
CISPEP   3 LEU C 3124    PRO C 3125          0         0.21                     
CISPEP   4 LEU D 4124    PRO D 4125          0         0.32                     
CRYST1  126.330  207.960   73.020  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007916  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system