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Database: PDB
Entry: 1ND5
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HEADER    HYDROLASE                               07-DEC-02   1ND5              
TITLE     CRYSTAL STRUCTURES OF HUMAN PROSTATIC ACID PHOSPHATASE IN COMPLEX WITH
TITLE    2 A PHOSPHATE ION AND ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID UPDATE THE
TITLE    3 MECHANISTIC PICTURE AND OFFER NEW INSIGHTS INTO INHIBITOR DESIGN     
CAVEAT     1ND5    NAG E 2 HAS WRONG CHIRALITY AT ATOM C1 NAG F 1 HAS WRONG     
CAVEAT   2 1ND5    CHIRALITY AT ATOM C1 NAG G 1 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 1ND5    NAG H 1 HAS WRONG CHIRALITY AT ATOM C1 NAG H 2 HAS WRONG     
CAVEAT   4 1ND5    CHIRALITY AT ATOM C1 NAG I 1 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   5 1ND5    NAG D 5009 HAS WRONG CHIRALITY AT ATOM C1                    
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 TISSUE: SEMEN                                                        
KEYWDS    ACID PHOSPHATASE, PAP, PROSTATE, PHOSPHATE, INHIBITOR, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ORTLUND,M.W.LACOUNT,L.LEBIODA                                       
REVDAT   5   29-JUL-20 1ND5    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   13-JUL-11 1ND5    1       VERSN                                    
REVDAT   3   24-FEB-09 1ND5    1       VERSN                                    
REVDAT   2   06-MAY-03 1ND5    1       JRNL   REMARK                            
REVDAT   1   20-DEC-02 1ND5    0                                                
JRNL        AUTH   E.ORTLUND,M.W.LACOUNT,L.LEBIODA                              
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN PROSTATIC ACID PHOSPHATASE IN    
JRNL        TITL 2 COMPLEX WITH A PHOSPHATE ION AND                             
JRNL        TITL 3 ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID UPDATE THE            
JRNL        TITL 4 MECHANISTIC PICTURE AND OFFER NEW INSIGHTS INTO INHIBITOR    
JRNL        TITL 5 DESIGN                                                       
JRNL        REF    BIOCHEMISTRY                  V.  42   383 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12525165                                                     
JRNL        DOI    10.1021/BI0265067                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 245501.330                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31444                          
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) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1557                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3773                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 219                          
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            : 11196                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 396                                     
REMARK   3   SOLVENT ATOMS            : 135                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.95000                                             
REMARK   3    B22 (A**2) : -2.52000                                             
REMARK   3    B33 (A**2) : 4.47000                                              
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.870                           
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 34.25                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DRUGS.PARAM                                    
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : PGE_PAR.TXT                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DRUGS.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  5   : PGE_TOP.TXT                                    
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ND5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017775.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
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                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06300                            
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) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.7                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2HPA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, KCL, GLYCINE, PH 10.0, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       60.05000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.61000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.43000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.61000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.05000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.43000            
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                                                    
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 300 REMARK: THE BIOLOGICAL ASSEMBLEY IS A DIMER. THE ASYMMETRIC UNIT     
REMARK 300 CONTAINS TWO SUCH DIMERS.                                            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H                   
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: 7510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLN A   347                                                      
REMARK 465     GLY A   348                                                      
REMARK 465     THR A   349                                                      
REMARK 465     GLU A   350                                                      
REMARK 465     ASP A   351                                                      
REMARK 465     SER A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     PHE B  1130A                                                     
REMARK 465     ASN B  1342                                                      
REMARK 465     SER B  1343                                                      
REMARK 465     HIS B  1344                                                      
REMARK 465     GLN B  1345                                                      
REMARK 465     GLY B  1346                                                      
REMARK 465     THR B  1347                                                      
REMARK 465     GLU B  1348                                                      
REMARK 465     ASP B  1349                                                      
REMARK 465     SER B  1350                                                      
REMARK 465     THR B  1351                                                      
REMARK 465     ASP B  1352                                                      
REMARK 465     THR C  2342                                                      
REMARK 465     ASN C  2343                                                      
REMARK 465     SER C  2344                                                      
REMARK 465     HIS C  2345                                                      
REMARK 465     GLN C  2346                                                      
REMARK 465     GLY C  2347                                                      
REMARK 465     THR C  2348                                                      
REMARK 465     GLU C  2349                                                      
REMARK 465     ASP C  2350                                                      
REMARK 465     SER C  2351                                                      
REMARK 465     THR C  2352                                                      
REMARK 465     ASP C  2353                                                      
REMARK 465     THR D  3342                                                      
REMARK 465     ASN D  3343                                                      
REMARK 465     SER D  3344                                                      
REMARK 465     HIS D  3345                                                      
REMARK 465     GLN D  3346                                                      
REMARK 465     GLY D  3347                                                      
REMARK 465     THR D  3348                                                      
REMARK 465     GLU D  3349                                                      
REMARK 465     ASP D  3350                                                      
REMARK 465     SER D  3351                                                      
REMARK 465     THR D  3352                                                      
REMARK 465     ASP D  3353                                                      
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   O4   NAG G     1     O1   NAG G     2              0.26            
REMARK 500   O4   NAG F     1     O1   NAG F     2              0.29            
REMARK 500   O4   NAG I     1     O1   NAG I     2              0.29            
REMARK 500   ND2  ASN A   188     O1   NAG E     1              0.30            
REMARK 500   C4   NAG G     1     O1   NAG G     2              1.68            
REMARK 500   C4   NAG F     1     O1   NAG F     2              1.70            
REMARK 500   C4   NAG I     1     O1   NAG I     2              1.71            
REMARK 500   O    LEU D  3169     O    HOH D  4122              2.06            
REMARK 500   O    GLY D  3166     N    ASP D  3168              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  19     -174.88   -174.74                                   
REMARK 500    PRO A  32      -43.09    -29.03                                   
REMARK 500    ASN A  62      -13.50    -18.76                                   
REMARK 500    SER A  64      105.45    -39.82                                   
REMARK 500    TYR A  65      108.19     37.30                                   
REMARK 500    SER A 117       -2.90    -51.95                                   
REMARK 500    LEU A 121      -56.39   -147.62                                   
REMARK 500    TYR A 123       82.99    -59.79                                   
REMARK 500    PRO A 151        7.62    -53.33                                   
REMARK 500    TYR A 152      -32.00   -130.58                                   
REMARK 500    LYS A 153      -40.72    -26.75                                   
REMARK 500    VAL A 177      -59.91   -129.04                                   
REMARK 500    HIS A 187       34.40    -84.18                                   
REMARK 500    ASN A 188       57.95     34.20                                   
REMARK 500    ILE A 217      -70.31     69.50                                   
REMARK 500    GLN A 227     -121.05   -116.88                                   
REMARK 500    PRO A 246      -75.33    -58.21                                   
REMARK 500    ALA A 256     -147.78   -146.85                                   
REMARK 500    ASP A 269       49.58     77.59                                   
REMARK 500    ALA A 279       19.53     57.30                                   
REMARK 500    PRO A 330      -16.53    -41.69                                   
REMARK 500    ASP A 335       75.83   -177.72                                   
REMARK 500    HIS B1011      170.21    -52.66                                   
REMARK 500    ASP B1013      126.31    -35.27                                   
REMARK 500    ASP B1018     -175.20   -175.01                                   
REMARK 500    GLU B1027      -61.05    -19.63                                   
REMARK 500    GLN B1032       44.66   -107.29                                   
REMARK 500    ARG B1057      -31.47    -39.79                                   
REMARK 500    LEU B1060       45.28   -100.34                                   
REMARK 500    ASN B1061       24.20    -66.76                                   
REMARK 500    SER B1063      101.47    -54.13                                   
REMARK 500    TYR B1064      149.35     43.18                                   
REMARK 500    LYS B1065      114.12   -175.99                                   
REMARK 500    HIS B1066      -17.99    -48.46                                   
REMARK 500    PHE B1091       73.59   -111.22                                   
REMARK 500    SER B1097       56.39   -101.77                                   
REMARK 500    LEU B1120      -48.74   -143.53                                   
REMARK 500    ASN B1127       45.55    -98.56                                   
REMARK 500    LYS B1139      -76.81    -69.13                                   
REMARK 500    SER B1140      116.35    -10.56                                   
REMARK 500    HIS B1148      -59.42    -15.27                                   
REMARK 500    HIS B1164       55.54   -105.86                                   
REMARK 500    GLN B1166       20.92    -78.51                                   
REMARK 500    VAL B1175      -61.82   -129.21                                   
REMARK 500    HIS B1185       20.14    -77.85                                   
REMARK 500    ILE B1215      -76.97     76.14                                   
REMARK 500    GLN B1225     -103.62   -124.51                                   
REMARK 500    SER B1245       47.10     16.87                                   
REMARK 500    ALA B1254     -147.59   -129.59                                   
REMARK 500    ASP B1267       39.29     72.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     123 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HPA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1CVI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ND6   RELATED DB: PDB                                   
DBREF  1ND5 A    1   354  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND5 B 1000  1352  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND5 C 2000  2353  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND5 D 3000  3353  UNP    P15309   PPAP_HUMAN      33    386             
SEQRES   1 A  354  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 A  354  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 A  354  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 A  354  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 A  354  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 A  354  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 A  354  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 A  354  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 A  354  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 A  354  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 A  354  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 A  354  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 A  354  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 A  354  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 A  354  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 A  354  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 A  354  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 A  354  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 A  354  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 A  354  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 A  354  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 A  354  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 A  354  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 A  354  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 A  354  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 A  354  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 A  354  GLU CYS MET THR THR ASN SER HIS GLN GLY THR GLU ASP          
SEQRES  28 A  354  SER THR ASP                                                  
SEQRES   1 B  354  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 B  354  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 B  354  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 B  354  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 B  354  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 B  354  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 B  354  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 B  354  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 B  354  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 B  354  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 B  354  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 B  354  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 B  354  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 B  354  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 B  354  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 B  354  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 B  354  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 B  354  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 B  354  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 B  354  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 B  354  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 B  354  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 B  354  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 B  354  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 B  354  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 B  354  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 B  354  GLU CYS MET THR THR ASN SER HIS GLN GLY THR GLU ASP          
SEQRES  28 B  354  SER THR ASP                                                  
SEQRES   1 C  354  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 C  354  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 C  354  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 C  354  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 C  354  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 C  354  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 C  354  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 C  354  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 C  354  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 C  354  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 C  354  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 C  354  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 C  354  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 C  354  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 C  354  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 C  354  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 C  354  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 C  354  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 C  354  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 C  354  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 C  354  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 C  354  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 C  354  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 C  354  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 C  354  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 C  354  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 C  354  GLU CYS MET THR THR ASN SER HIS GLN GLY THR GLU ASP          
SEQRES  28 C  354  SER THR ASP                                                  
SEQRES   1 D  354  LYS GLU LEU LYS PHE VAL THR LEU VAL PHE ARG HIS GLY          
SEQRES   2 D  354  ASP ARG SER PRO ILE ASP THR PHE PRO THR ASP PRO ILE          
SEQRES   3 D  354  LYS GLU SER SER TRP PRO GLN GLY PHE GLY GLN LEU THR          
SEQRES   4 D  354  GLN LEU GLY MET GLU GLN HIS TYR GLU LEU GLY GLU TYR          
SEQRES   5 D  354  ILE ARG LYS ARG TYR ARG LYS PHE LEU ASN GLU SER TYR          
SEQRES   6 D  354  LYS HIS GLU GLN VAL TYR ILE ARG SER THR ASP VAL ASP          
SEQRES   7 D  354  ARG THR LEU MET SER ALA MET THR ASN LEU ALA ALA LEU          
SEQRES   8 D  354  PHE PRO PRO GLU GLY VAL SER ILE TRP ASN PRO ILE LEU          
SEQRES   9 D  354  LEU TRP GLN PRO ILE PRO VAL HIS THR VAL PRO LEU SER          
SEQRES  10 D  354  GLU ASP GLN LEU LEU TYR LEU PRO PHE ARG ASN CYS PRO          
SEQRES  11 D  354  ARG PHE GLN GLU LEU GLU SER GLU THR LEU LYS SER GLU          
SEQRES  12 D  354  GLU PHE GLN LYS ARG LEU HIS PRO TYR LYS ASP PHE ILE          
SEQRES  13 D  354  ALA THR LEU GLY LYS LEU SER GLY LEU HIS GLY GLN ASP          
SEQRES  14 D  354  LEU PHE GLY ILE TRP SER LYS VAL TYR ASP PRO LEU TYR          
SEQRES  15 D  354  CYS GLU SER VAL HIS ASN PHE THR LEU PRO SER TRP ALA          
SEQRES  16 D  354  THR GLU ASP THR MET THR LYS LEU ARG GLU LEU SER GLU          
SEQRES  17 D  354  LEU SER LEU LEU SER LEU TYR GLY ILE HIS LYS GLN LYS          
SEQRES  18 D  354  GLU LYS SER ARG LEU GLN GLY GLY VAL LEU VAL ASN GLU          
SEQRES  19 D  354  ILE LEU ASN HIS MET LYS ARG ALA THR GLN ILE PRO SER          
SEQRES  20 D  354  TYR LYS LYS LEU ILE MET TYR SER ALA HIS ASP THR THR          
SEQRES  21 D  354  VAL SER GLY LEU GLN MET ALA LEU ASP VAL TYR ASN GLY          
SEQRES  22 D  354  LEU LEU PRO PRO TYR ALA SER CYS HIS LEU THR GLU LEU          
SEQRES  23 D  354  TYR PHE GLU LYS GLY GLU TYR PHE VAL GLU MET TYR TYR          
SEQRES  24 D  354  ARG ASN GLU THR GLN HIS GLU PRO TYR PRO LEU MET LEU          
SEQRES  25 D  354  PRO GLY CYS SER PRO SER CYS PRO LEU GLU ARG PHE ALA          
SEQRES  26 D  354  GLU LEU VAL GLY PRO VAL ILE PRO GLN ASP TRP SER THR          
SEQRES  27 D  354  GLU CYS MET THR THR ASN SER HIS GLN GLY THR GLU ASP          
SEQRES  28 D  354  SER THR ASP                                                  
MODRES 1ND5 ASN A  188  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND5 ASN A  301  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND5 ASN C 2300  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND5 ASN D 3187  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND5 ASN D 3300  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      15                                                       
HET    NAG  E   2      15                                                       
HET    NAG  F   1      15                                                       
HET    NAG  F   2      15                                                       
HET    NAG  G   1      15                                                       
HET    NAG  G   2      15                                                       
HET    NAG  H   1      15                                                       
HET    NAG  H   2      15                                                       
HET    NAG  I   1      15                                                       
HET    NAG  I   2      15                                                       
HET    MAN  I   3      12                                                       
HET    2BF  A6000      19                                                       
HET    1PE  A7000      16                                                       
HET    1PE  A7004      16                                                       
HET    1PE  A7007      16                                                       
HET    NDG  B5004      15                                                       
HET    2BF  B6001      19                                                       
HET    1PE  B7001      16                                                       
HET    1PE  B7005      16                                                       
HET    2BF  C6002      19                                                       
HET    1PE  C7002      16                                                       
HET    1PE  C7006      16                                                       
HET    NAG  D5009      15                                                       
HET    2BF  D6003      19                                                       
HET    1PE  D7003      16                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     2BF ALPHA-BENZYL-AMINOBENZYL-PHOSPHONIC ACID                         
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETSYN     1PE PEG400                                                           
FORMUL   5  NAG    11(C8 H15 N O6)                                              
FORMUL   9  MAN    C6 H12 O6                                                    
FORMUL  10  2BF    4(C14 H16 N O3 P)                                            
FORMUL  11  1PE    8(C10 H22 O6)                                                
FORMUL  14  NDG    C8 H15 N O6                                                  
FORMUL  24  HOH   *135(H2 O)                                                    
HELIX    1   1 LYS A   27  TRP A   31  5                                   5    
HELIX    2   2 THR A   39  TYR A   57  1                                  19    
HELIX    3   3 VAL A   77  PHE A   92  1                                  16    
HELIX    4   4 GLU A   95  ILE A   99  5                                   5    
HELIX    5   5 PRO A  115  ASP A  119  5                                   5    
HELIX    6   6 CYS A  129  SER A  142  1                                  14    
HELIX    7   7 SER A  142  GLY A  164  1                                  23    
HELIX    8   8 ASP A  169  VAL A  177  1                                   9    
HELIX    9   9 VAL A  177  HIS A  187  1                                  11    
HELIX   10  10 THR A  196  GLY A  216  1                                  21    
HELIX   11  11 LYS A  219  GLN A  227  1                                   9    
HELIX   12  12 GLY A  228  ILE A  245  1                                  18    
HELIX   13  13 HIS A  257  ASP A  269  1                                  13    
HELIX   14  14 LEU A  321  GLY A  329  1                                   9    
HELIX   15  15 PRO A  330  ILE A  332  5                                   3    
HELIX   16  16 ASP A  335  MET A  341  1                                   7    
HELIX   17  17 LYS B 1026  TRP B 1030  5                                   5    
HELIX   18  18 THR B 1038  TYR B 1056  1                                  19    
HELIX   19  19 VAL B 1076  PHE B 1091  1                                  16    
HELIX   20  20 PRO B 1114  ASP B 1118  5                                   5    
HELIX   21  21 GLN B 1131  SER B 1140  1                                  10    
HELIX   22  22 SER B 1140  HIS B 1148  1                                   9    
HELIX   23  23 TYR B 1150  GLY B 1162  1                                  13    
HELIX   24  24 ASP B 1167  VAL B 1175  1                                   9    
HELIX   25  25 VAL B 1175  HIS B 1185  1                                  11    
HELIX   26  26 THR B 1194  GLY B 1214  1                                  21    
HELIX   27  27 LYS B 1217  GLN B 1225  1                                   9    
HELIX   28  28 GLN B 1225  ILE B 1243  1                                  19    
HELIX   29  29 HIS B 1255  LEU B 1266  1                                  12    
HELIX   30  30 LEU B 1319  GLY B 1327  1                                   9    
HELIX   31  31 PRO B 1328  ILE B 1330  5                                   3    
HELIX   32  32 ASP B 1333  CYS B 1338  1                                   6    
HELIX   33  33 LYS C 2026  TRP C 2030  5                                   5    
HELIX   34  34 THR C 2038  TYR C 2056  1                                  19    
HELIX   35  35 VAL C 2076  PHE C 2091  1                                  16    
HELIX   36  36 PRO C 2114  ASP C 2118  5                                   5    
HELIX   37  37 CYS C 2128  LYS C 2140  1                                  13    
HELIX   38  38 SER C 2141  HIS C 2149  1                                   9    
HELIX   39  39 TYR C 2151  GLY C 2163  1                                  13    
HELIX   40  40 ASP C 2168  LYS C 2175  1                                   8    
HELIX   41  41 VAL C 2176  HIS C 2186  1                                  11    
HELIX   42  42 THR C 2195  GLY C 2215  1                                  21    
HELIX   43  43 LYS C 2218  LEU C 2225  1                                   8    
HELIX   44  44 GLN C 2226  ILE C 2244  1                                  19    
HELIX   45  45 HIS C 2256  ASP C 2268  1                                  13    
HELIX   46  46 LEU C 2320  GLY C 2328  1                                   9    
HELIX   47  47 PRO C 2329  ILE C 2331  5                                   3    
HELIX   48  48 ASP C 2334  CYS C 2339  1                                   6    
HELIX   49  49 LYS D 3026  TRP D 3030  5                                   5    
HELIX   50  50 THR D 3038  TYR D 3056  1                                  19    
HELIX   51  51 VAL D 3076  PHE D 3091  1                                  16    
HELIX   52  52 GLU D 3094  ILE D 3098  5                                   5    
HELIX   53  53 PRO D 3114  ASP D 3118  5                                   5    
HELIX   54  54 CYS D 3128  LYS D 3140  1                                  13    
HELIX   55  55 SER D 3141  HIS D 3149  1                                   9    
HELIX   56  56 LYS D 3152  GLY D 3163  1                                  12    
HELIX   57  57 ASP D 3168  VAL D 3176  1                                   9    
HELIX   58  58 VAL D 3176  HIS D 3186  1                                  11    
HELIX   59  59 THR D 3195  GLY D 3215  1                                  21    
HELIX   60  60 LYS D 3218  GLN D 3226  1                                   9    
HELIX   61  61 GLN D 3226  GLN D 3243  1                                  18    
HELIX   62  62 HIS D 3256  ASP D 3268  1                                  13    
HELIX   63  63 LEU D 3320  GLY D 3328  1                                   9    
HELIX   64  64 PRO D 3329  ILE D 3331  5                                   3    
HELIX   65  65 ASP D 3334  MET D 3340  1                                   7    
SHEET    1   A 6 VAL A  70  SER A  74  0                                        
SHEET    2   A 6 LEU A 251  ALA A 256  1  O  MET A 253   N  TYR A  71           
SHEET    3   A 6 GLU A   2  ARG A  11  1  N  PHE A  10   O  ALA A 256           
SHEET    4   A 6 CYS A 281  PHE A 288 -1  O  HIS A 282   N  VAL A   9           
SHEET    5   A 6 TYR A 293  ARG A 300 -1  O  PHE A 294   N  TYR A 287           
SHEET    6   A 6 TYR A 308  LEU A 310 -1  O  LEU A 310   N  MET A 297           
SHEET    1   B 6 VAL A  70  SER A  74  0                                        
SHEET    2   B 6 LEU A 251  ALA A 256  1  O  MET A 253   N  TYR A  71           
SHEET    3   B 6 GLU A   2  ARG A  11  1  N  PHE A  10   O  ALA A 256           
SHEET    4   B 6 CYS A 281  PHE A 288 -1  O  HIS A 282   N  VAL A   9           
SHEET    5   B 6 TYR A 293  ARG A 300 -1  O  PHE A 294   N  TYR A 287           
SHEET    6   B 6 CYS A 319  PRO A 320 -1  O  CYS A 319   N  VAL A 295           
SHEET    1   C 7 HIS B1111  VAL B1113  0                                        
SHEET    2   C 7 VAL B1069  THR B1074  1  N  SER B1073   O  HIS B1111           
SHEET    3   C 7 LEU B1249  ALA B1254  1  O  SER B1253   N  ARG B1072           
SHEET    4   C 7 GLU B1001  ARG B1010  1  N  LEU B1007   O  TYR B1252           
SHEET    5   C 7 CYS B1279  PHE B1286 -1  O  PHE B1286   N  GLU B1001           
SHEET    6   C 7 TYR B1291  ARG B1298 -1  O  PHE B1292   N  TYR B1285           
SHEET    7   C 7 TYR B1306  LEU B1308 -1  O  TYR B1306   N  TYR B1297           
SHEET    1   D 7 HIS B1111  VAL B1113  0                                        
SHEET    2   D 7 VAL B1069  THR B1074  1  N  SER B1073   O  HIS B1111           
SHEET    3   D 7 LEU B1249  ALA B1254  1  O  SER B1253   N  ARG B1072           
SHEET    4   D 7 GLU B1001  ARG B1010  1  N  LEU B1007   O  TYR B1252           
SHEET    5   D 7 CYS B1279  PHE B1286 -1  O  PHE B1286   N  GLU B1001           
SHEET    6   D 7 TYR B1291  ARG B1298 -1  O  PHE B1292   N  TYR B1285           
SHEET    7   D 7 SER B1316  PRO B1318 -1  O  CYS B1317   N  VAL B1293           
SHEET    1   E 7 HIS C2111  VAL C2113  0                                        
SHEET    2   E 7 VAL C2069  THR C2074  1  N  SER C2073   O  HIS C2111           
SHEET    3   E 7 LEU C2250  ALA C2255  1  O  MET C2252   N  ARG C2072           
SHEET    4   E 7 GLU C2001  ARG C2010  1  N  PHE C2009   O  ALA C2255           
SHEET    5   E 7 CYS C2280  PHE C2287 -1  O  PHE C2287   N  GLU C2001           
SHEET    6   E 7 TYR C2292  ARG C2299 -1  O  GLU C2295   N  GLU C2284           
SHEET    7   E 7 TYR C2307  LEU C2309 -1  O  TYR C2307   N  TYR C2298           
SHEET    1   F 7 HIS C2111  VAL C2113  0                                        
SHEET    2   F 7 VAL C2069  THR C2074  1  N  SER C2073   O  HIS C2111           
SHEET    3   F 7 LEU C2250  ALA C2255  1  O  MET C2252   N  ARG C2072           
SHEET    4   F 7 GLU C2001  ARG C2010  1  N  PHE C2009   O  ALA C2255           
SHEET    5   F 7 CYS C2280  PHE C2287 -1  O  PHE C2287   N  GLU C2001           
SHEET    6   F 7 TYR C2292  ARG C2299 -1  O  GLU C2295   N  GLU C2284           
SHEET    7   F 7 CYS C2318  PRO C2319 -1  O  CYS C2318   N  VAL C2294           
SHEET    1   G 7 HIS D3111  VAL D3113  0                                        
SHEET    2   G 7 VAL D3069  THR D3074  1  N  SER D3073   O  HIS D3111           
SHEET    3   G 7 LEU D3250  ALA D3255  1  O  MET D3252   N  ARG D3072           
SHEET    4   G 7 GLU D3001  ARG D3010  1  N  LEU D3007   O  ILE D3251           
SHEET    5   G 7 CYS D3280  PHE D3287 -1  O  LEU D3285   N  PHE D3004           
SHEET    6   G 7 TYR D3292  ARG D3299 -1  O  PHE D3293   N  TYR D3286           
SHEET    7   G 7 TYR D3307  LEU D3309 -1  O  LEU D3309   N  MET D3296           
SHEET    1   H 7 HIS D3111  VAL D3113  0                                        
SHEET    2   H 7 VAL D3069  THR D3074  1  N  SER D3073   O  HIS D3111           
SHEET    3   H 7 LEU D3250  ALA D3255  1  O  MET D3252   N  ARG D3072           
SHEET    4   H 7 GLU D3001  ARG D3010  1  N  LEU D3007   O  ILE D3251           
SHEET    5   H 7 CYS D3280  PHE D3287 -1  O  LEU D3285   N  PHE D3004           
SHEET    6   H 7 TYR D3292  ARG D3299 -1  O  PHE D3293   N  TYR D3286           
SHEET    7   H 7 CYS D3318  PRO D3319 -1  O  CYS D3318   N  VAL D3294           
SSBOND   1 CYS A  129    CYS A  340                          1555   1555  2.04  
SSBOND   2 CYS A  315    CYS A  319                          1555   1555  2.04  
SSBOND   3 CYS B 1128    CYS B 1338                          1555   1555  2.04  
SSBOND   4 CYS B 1313    CYS B 1317                          1555   1555  2.03  
SSBOND   5 CYS C 2128    CYS C 2339                          1555   1555  2.04  
SSBOND   6 CYS C 2314    CYS C 2318                          1555   1555  2.03  
SSBOND   7 CYS D 3128    CYS D 3339                          1555   1555  2.03  
SSBOND   8 CYS D 3314    CYS D 3318                          1555   1555  2.03  
LINK         ND2 ASN A 188                 C1  NAG E   1     1555   1555  1.45  
LINK         CG  ASN A 188                 O1  NAG E   1     1555   1555  1.59  
LINK         ND2 ASN A 301                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN C2300                 C1  NAG H   1     1555   1555  1.45  
LINK         ND2 ASN D3187                 C1  NAG D5009     1555   1555  1.45  
LINK         ND2 ASN D3300                 C1  NAG I   1     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.39  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.39  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.39  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.39  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.39  
LINK         O4  NAG I   2                 C1  MAN I   3     1555   1555  1.39  
CISPEP   1 LEU A  124    PRO A  125          0        -0.19                     
CISPEP   2 LEU B 1123    PRO B 1124          0        -0.03                     
CISPEP   3 LEU C 2123    PRO C 2124          0         0.13                     
CISPEP   4 LEU D 3123    PRO D 3124          0        -0.01                     
CRYST1  120.100  204.860   71.220  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      0.008326  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014041        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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