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Database: PDB
Entry: 2HPA
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HEADER    HYDROLASE                               11-SEP-98   2HPA              
TITLE     STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID
TITLE    2 PHOSPHATASE                                                          
CAVEAT     2HPA    NAG A 1371 HAS WRONG CHIRALITY AT ATOM C1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (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 OTHER_DETAILS: ISOLATED FROM HUMAN SEMINAL FLUID                     
KEYWDS    ACID PHOSPHATASE, N-PROPYLTARTRAMATE, HYDROLASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.W.LACOUNT,G.HANDY,L.LEBIODA                                         
REVDAT   6   29-JUL-20 2HPA    1       CAVEAT COMPND REMARK HET                 
REVDAT   6 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   6 3                   1       ATOM                                     
REVDAT   5   13-JUL-11 2HPA    1       VERSN                                    
REVDAT   4   24-FEB-09 2HPA    1       VERSN                                    
REVDAT   3   01-APR-03 2HPA    1       JRNL                                     
REVDAT   2   14-JAN-00 2HPA    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   16-SEP-98 2HPA    0                                                
JRNL        AUTH   M.W.LACOUNT,G.HANDY,L.LEBIODA                                
JRNL        TITL   STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN      
JRNL        TITL 2 PROSTATIC ACID PHOSPHATASE.                                  
JRNL        REF    J.BIOL.CHEM.                  V. 273 30406 1998              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9804805                                                      
JRNL        DOI    10.1074/JBC.273.46.30406                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.LINDQVIST,G.SCHNEIDER,P.VIHKO                              
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN       
REMARK   1  TITL 2 COMPLEX WITH L(+)-TARTRATE                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 268 20744 1993              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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) : 2.90                           
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)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 32862                          
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) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1644                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4290                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 216                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
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          : 212                                     
REMARK   3   SOLVENT ATOMS            : 350                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.034                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.490                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAIN                                                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM11.WAT                                    
REMARK   3  PARAMETER FILE  3  : TAR.PAR                                        
REMARK   3  PARAMETER FILE  4  : OLIGOSAC.PAR                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH11.WAT                                     
REMARK   3  TOPOLOGY FILE  3   : TAR.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : OLIGOSAC.TOP                                   
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE DEPOSITION ID IS D_1000008412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 123                                
REMARK 200  PH                             : 10                                 
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                  : NI FILTER                          
REMARK 200  OPTICS                         : 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   : 39548                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.13800                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 10                                    
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       59.93000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.55500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.34000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.55500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.93000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.34000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G                               
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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G                               
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 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      179.79000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      202.68000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -35.55500            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O2   BMA E     2     O    HOH A  5291              2.08            
REMARK 500   O    HOH B  5432     O    HOH B  5433              2.14            
REMARK 500   ND2  ASN C  3062     O5   NAG C  3361              2.15            
REMARK 500   N    LEU A  1038     O    HOH A  5252              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A1208   CD    GLU A1208   OE2     0.077                       
REMARK 500    GLU B2184   CG    GLU B2184   CD     -0.106                       
REMARK 500    TYR D4308   CB    TYR D4308   CG     -0.136                       
REMARK 500    TYR D4308   CE2   TYR D4308   CD2    -0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A1208   OE1 -  CD  -  OE2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    PRO B2032   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    LEU B2283   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    LEU C3283   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    PRO D4032   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    LEU D4283   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    TYR D4308   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    TYR D4308   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 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    ASN A1062       40.31   -100.12                                   
REMARK 500    SER A1064       85.75    -57.58                                   
REMARK 500    TYR A1065      127.74     64.80                                   
REMARK 500    GLN A1120       45.62   -109.40                                   
REMARK 500    LEU A1121      -63.33   -154.81                                   
REMARK 500    LYS A1153      -48.87    -28.46                                   
REMARK 500    GLN A1168        2.26    -59.42                                   
REMARK 500    VAL A1177      -43.65   -139.05                                   
REMARK 500    HIS A1218      112.00    171.31                                   
REMARK 500    GLN A1227     -111.74   -132.26                                   
REMARK 500    ALA A1256     -149.57   -155.29                                   
REMARK 500    PRO A1276      105.26    -53.55                                   
REMARK 500    LEU A1312      107.93    -58.97                                   
REMARK 500    SER A1318       78.92   -103.79                                   
REMARK 500    PRO A1330        2.69    -66.18                                   
REMARK 500    ASP A1335       78.85   -171.32                                   
REMARK 500    ASN B2062       43.98    -98.61                                   
REMARK 500    GLU B2063      118.72   -161.20                                   
REMARK 500    SER B2064       75.63    -57.33                                   
REMARK 500    TYR B2065      121.70     75.11                                   
REMARK 500    PHE B2092       73.45   -116.13                                   
REMARK 500    GLN B2120       55.04   -116.54                                   
REMARK 500    LEU B2121      -56.88   -163.38                                   
REMARK 500    GLN B2168        1.42    -62.35                                   
REMARK 500    VAL B2177      -55.08   -138.30                                   
REMARK 500    ILE B2217       17.21     46.78                                   
REMARK 500    HIS B2218      110.83    175.01                                   
REMARK 500    GLN B2227     -109.41   -119.14                                   
REMARK 500    ALA B2256     -147.53   -148.72                                   
REMARK 500    PRO B2276      109.98    -53.17                                   
REMARK 500    SER B2318       72.70   -102.88                                   
REMARK 500    PRO B2330        5.77    -65.69                                   
REMARK 500    ASP B2335       83.36   -161.52                                   
REMARK 500    ASN C3062       54.67   -107.88                                   
REMARK 500    GLU C3063      119.19   -161.85                                   
REMARK 500    SER C3064       78.37    -61.49                                   
REMARK 500    TYR C3065      124.02     71.59                                   
REMARK 500    PHE C3092       66.37   -111.97                                   
REMARK 500    SER C3117      -17.49    -48.10                                   
REMARK 500    LEU C3121      -60.56   -169.29                                   
REMARK 500    ASN C3128       32.58    -94.81                                   
REMARK 500    PRO C3151      -19.87    -49.75                                   
REMARK 500    GLN C3168        6.94    -61.05                                   
REMARK 500    VAL C3177      -50.88   -136.15                                   
REMARK 500    HIS C3187       32.12    -97.70                                   
REMARK 500    ILE C3217       26.63     48.14                                   
REMARK 500    HIS C3218      114.25    163.31                                   
REMARK 500    GLN C3227      -94.54   -126.65                                   
REMARK 500    ALA C3256     -152.27   -146.36                                   
REMARK 500    PRO C3276      107.06    -51.72                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A1215         0.10    SIDE CHAIN                              
REMARK 500    TYR B2308         0.06    SIDE CHAIN                              
REMARK 500    TYR C3182         0.06    SIDE CHAIN                              
REMARK 500    TYR D4065         0.07    SIDE CHAIN                              
REMARK 500    TYR D4308         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG E    1                                                       
DBREF  2HPA A 1001  1342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  2HPA B 2001  2342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  2HPA C 3001  3342  UNP    P15309   PPAP_HUMAN      33    374             
DBREF  2HPA 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 2HPA ASN A 1188  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN A 1301  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN B 2301  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN C 3062  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN C 3188  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN C 3301  ASN  GLYCOSYLATION SITE                                 
MODRES 2HPA ASN D 4301  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    BMA  E   2      11                                                       
HET    MAN  E   3      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    NAG  A1371      14                                                       
HET    PT3  A1345      13                                                       
HET    NAG  B2381      14                                                       
HET    PT3  B2345      13                                                       
HET    NAG  C3361      14                                                       
HET    NAG  C3371      14                                                       
HET    NAG  C3381      14                                                       
HET    PT3  D4345      13                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     PT3 N-PROPYL-TARTRAMIC ACID                                          
FORMUL   5  NAG    10(C8 H15 N O6)                                              
FORMUL   5  BMA    2(C6 H12 O6)                                                 
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   9  PT3    3(C7 H13 N O5)                                               
FORMUL  16  HOH   *350(H2 O)                                                    
HELIX    1   1 GLU A 1028  SER A 1030  5                                   3    
HELIX    2   2 GLN A 1040  ARG A 1056  1                                  17    
HELIX    3   3 ASP A 1078  LEU A 1091  1                                  14    
HELIX    4   4 GLY A 1096  SER A 1098  5                                   3    
HELIX    5   5 LEU A 1116  GLU A 1118  5                                   3    
HELIX    6   6 PRO A 1130  LYS A 1141  1                                  12    
HELIX    7   7 GLU A 1143  SER A 1163  1                                  21    
HELIX    8   8 LEU A 1170  LYS A 1176  1                                   7    
HELIX    9   9 TYR A 1178  VAL A 1186  1                                   9    
HELIX   10  10 GLU A 1197  TYR A 1215  1                                  19    
HELIX   11  11 GLN A 1220  LEU A 1226  1                                   7    
HELIX   12  12 GLY A 1228  GLN A 1244  5                                  17    
HELIX   13  13 ASP A 1258  LEU A 1268  1                                  11    
HELIX   14  14 LEU A 1321  VAL A 1331  1                                  11    
HELIX   15  15 TRP A 1336  CYS A 1340  1                                   5    
HELIX   16  16 GLU B 2028  SER B 2030  5                                   3    
HELIX   17  17 GLN B 2040  TYR B 2057  1                                  18    
HELIX   18  18 ASP B 2078  LEU B 2091  1                                  14    
HELIX   19  19 GLY B 2096  SER B 2098  5                                   3    
HELIX   20  20 LEU B 2116  GLU B 2118  5                                   3    
HELIX   21  21 PRO B 2130  LYS B 2141  1                                  12    
HELIX   22  22 GLU B 2143  SER B 2163  1                                  21    
HELIX   23  23 LEU B 2170  LYS B 2176  1                                   7    
HELIX   24  24 TYR B 2178  VAL B 2186  1                                   9    
HELIX   25  25 GLU B 2197  TYR B 2215  1                                  19    
HELIX   26  26 GLN B 2220  LEU B 2226  1                                   7    
HELIX   27  27 GLY B 2228  GLN B 2244  1                                  17    
HELIX   28  28 ASP B 2258  LEU B 2268  1                                  11    
HELIX   29  29 LEU B 2321  LEU B 2327  1                                   7    
HELIX   30  30 GLY B 2329  VAL B 2331  5                                   3    
HELIX   31  31 TRP B 2336  CYS B 2340  1                                   5    
HELIX   32  32 GLU C 3028  SER C 3030  5                                   3    
HELIX   33  33 GLN C 3040  ARG C 3056  1                                  17    
HELIX   34  34 ASP C 3078  LEU C 3091  1                                  14    
HELIX   35  35 GLY C 3096  SER C 3098  5                                   3    
HELIX   36  36 LEU C 3116  GLU C 3118  5                                   3    
HELIX   37  37 PRO C 3130  LYS C 3141  1                                  12    
HELIX   38  38 GLU C 3143  SER C 3163  1                                  21    
HELIX   39  39 LEU C 3170  LYS C 3176  1                                   7    
HELIX   40  40 TYR C 3178  HIS C 3187  1                                  10    
HELIX   41  41 GLU C 3197  TYR C 3215  1                                  19    
HELIX   42  42 GLN C 3220  LEU C 3226  1                                   7    
HELIX   43  43 GLY C 3228  GLN C 3244  1                                  17    
HELIX   44  44 ASP C 3258  LEU C 3268  1                                  11    
HELIX   45  45 LEU C 3321  VAL C 3331  1                                  11    
HELIX   46  46 TRP C 3336  CYS C 3340  1                                   5    
HELIX   47  47 GLU D 4028  SER D 4030  5                                   3    
HELIX   48  48 GLN D 4040  ARG D 4056  1                                  17    
HELIX   49  49 ASP D 4078  LEU D 4091  1                                  14    
HELIX   50  50 GLY D 4096  SER D 4098  5                                   3    
HELIX   51  51 LEU D 4116  GLU D 4118  5                                   3    
HELIX   52  52 PRO D 4130  LYS D 4141  1                                  12    
HELIX   53  53 GLU D 4143  SER D 4163  1                                  21    
HELIX   54  54 LEU D 4170  LYS D 4176  1                                   7    
HELIX   55  55 TYR D 4178  VAL D 4186  1                                   9    
HELIX   56  56 GLU D 4197  TYR D 4215  1                                  19    
HELIX   57  57 GLN D 4220  LEU D 4226  1                                   7    
HELIX   58  58 GLY D 4228  GLN D 4244  1                                  17    
HELIX   59  59 ASP D 4258  LEU D 4268  1                                  11    
HELIX   60  60 LEU D 4321  LEU D 4327  1                                   7    
HELIX   61  61 GLY D 4329  VAL D 4331  5                                   3    
HELIX   62  62 TRP D 4336  CYS D 4340  1                                   5    
SHEET    1   A 6 VAL A1070  SER A1074  0                                        
SHEET    2   A 6 LEU A1251  ALA A1256  1  N  LEU A1251   O  TYR A1071           
SHEET    3   A 6 LEU A1003  ARG A1011  1  N  VAL A1006   O  ILE A1252           
SHEET    4   A 6 CYS A1281  GLU A1289 -1  N  LEU A1286   O  LYS A1004           
SHEET    5   A 6 GLU A1292  ARG A1300 -1  N  ARG A1300   O  CYS A1281           
SHEET    6   A 6 SER A1318  PRO A1320 -1  N  CYS A1319   O  VAL A1295           
SHEET    1   B 6 VAL B2070  SER B2074  0                                        
SHEET    2   B 6 LEU B2251  ALA B2256  1  N  LEU B2251   O  TYR B2071           
SHEET    3   B 6 GLU B2002  ARG B2011  1  N  VAL B2006   O  ILE B2252           
SHEET    4   B 6 CYS B2281  GLU B2289 -1  N  PHE B2288   O  GLU B2002           
SHEET    5   B 6 GLU B2292  ARG B2300 -1  N  ARG B2300   O  CYS B2281           
SHEET    6   B 6 SER B2318  PRO B2320 -1  N  CYS B2319   O  VAL B2295           
SHEET    1   C 2 MET B2297  TYR B2299  0                                        
SHEET    2   C 2 TYR B2308  LEU B2310 -1  N  LEU B2310   O  MET B2297           
SHEET    1   D 7 VAL C3111  VAL C3114  0                                        
SHEET    2   D 7 VAL C3070  THR C3075  1  N  ILE C3072   O  HIS C3112           
SHEET    3   D 7 LEU C3251  ALA C3256  1  N  LEU C3251   O  TYR C3071           
SHEET    4   D 7 LEU C3003  ARG C3011  1  N  VAL C3006   O  ILE C3252           
SHEET    5   D 7 CYS C3281  GLU C3289 -1  N  LEU C3286   O  LYS C3004           
SHEET    6   D 7 GLU C3292  ARG C3300 -1  N  ARG C3300   O  CYS C3281           
SHEET    7   D 7 SER C3318  PRO C3320 -1  N  CYS C3319   O  VAL C3295           
SHEET    1   E 2 MET C3297  TYR C3299  0                                        
SHEET    2   E 2 TYR C3308  LEU C3310 -1  N  LEU C3310   O  MET C3297           
SHEET    1   F 6 VAL D4070  SER D4074  0                                        
SHEET    2   F 6 LEU D4251  ALA D4256  1  N  LEU D4251   O  TYR D4071           
SHEET    3   F 6 LEU D4003  ARG D4011  1  N  VAL D4006   O  ILE D4252           
SHEET    4   F 6 CYS D4281  GLU D4289 -1  N  LEU D4286   O  LYS D4004           
SHEET    5   F 6 GLU D4292  ARG D4300 -1  N  ARG D4300   O  CYS D4281           
SHEET    6   F 6 SER D4318  PRO D4320 -1  N  CYS D4319   O  VAL D4295           
SHEET    1   G 2 MET D4297  TYR D4299  0                                        
SHEET    2   G 2 TYR D4308  LEU D4310 -1  N  LEU D4310   O  MET D4297           
SSBOND   1 CYS A 1129    CYS A 1340                          1555   1555  2.05  
SSBOND   2 CYS A 1315    CYS A 1319                          1555   1555  2.04  
SSBOND   3 CYS B 2129    CYS B 2340                          1555   1555  2.05  
SSBOND   4 CYS B 2315    CYS B 2319                          1555   1555  2.02  
SSBOND   5 CYS C 3129    CYS C 3340                          1555   1555  2.06  
SSBOND   6 CYS C 3315    CYS C 3319                          1555   1555  2.04  
SSBOND   7 CYS D 4129    CYS D 4340                          1555   1555  2.03  
SSBOND   8 CYS D 4315    CYS D 4319                          1555   1555  2.05  
LINK         ND2 ASN A1188                 C1  NAG A1371     1555   1555  1.52  
LINK         ND2 ASN A1188                 O5  NAG A1371     1555   1555  1.87  
LINK         ND2 ASN A1301                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN B2301                 C1  NAG B2381     1555   1555  1.46  
LINK         ND2 ASN C3062                 C1  NAG C3361     1555   1555  1.38  
LINK         ND2 ASN C3188                 C1  NAG C3371     1555   1555  1.44  
LINK         ND2 ASN C3301                 C1  NAG C3381     1555   1555  1.45  
LINK         ND2 ASN D4301                 C1  NAG G   1     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  BMA E   2     1555   1555  1.38  
LINK         O6  BMA E   2                 C1  MAN E   3     1555   1555  1.40  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.40  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.38  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.38  
CISPEP   1 LEU A 1124    PRO A 1125          0        -0.17                     
CISPEP   2 LEU B 2124    PRO B 2125          0         0.27                     
CISPEP   3 LEU C 3124    PRO C 3125          0         3.13                     
CISPEP   4 LEU D 4124    PRO D 4125          0        -0.91                     
CRYST1  119.860  202.680   71.110  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      0.008343  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004934  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014063        0.00000                         
MTRIX1   1 -0.792218  0.090391 -0.603507      110.03060    1                    
MTRIX2   1  0.019346 -0.984751 -0.172888      163.15530    1                    
MTRIX3   1 -0.609932 -0.148641  0.778389       52.18480    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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