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Database: PDB
Entry: 1ND6
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Original site: 1ND6 
HEADER    HYDROLASE                               07-DEC-02   1ND6              
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     1ND6    NAG E 2 HAS WRONG CHIRALITY AT ATOM C1 MAN E 4 HAS WRONG     
CAVEAT   2 1ND6    CHIRALITY AT ATOM C1 NAG F 2 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 1ND6    NAG G 1 HAS WRONG CHIRALITY AT ATOM C1 MAN G 4 HAS WRONG     
CAVEAT   4 1ND6    CHIRALITY AT ATOM C1 MAN G 5 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   5 1ND6    NAG H 1 HAS WRONG CHIRALITY AT ATOM C1 NAG H 2 HAS WRONG     
CAVEAT   6 1ND6    CHIRALITY AT ATOM C1 MAN H 3 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   7 1ND6    NAG I 1 HAS WRONG CHIRALITY AT ATOM C1 NAG B 5006 HAS WRONG  
CAVEAT   8 1ND6    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    PROSTATIC ACID PHOSPHATASE, PAP, PROSTATE, PHOSPHATE, INHIBITOR,      
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ORTLUND,M.W.LACOUNT,L.LEBIODA                                       
REVDAT   5   29-JUL-20 1ND6    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   13-JUL-11 1ND6    1       VERSN                                    
REVDAT   3   24-FEB-09 1ND6    1       VERSN                                    
REVDAT   2   06-MAY-03 1ND6    1       JRNL   REMARK                            
REVDAT   1   20-DEC-02 1ND6    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 347002.320                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 62141                          
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) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6320                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7916                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 883                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11207                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 377                                     
REMARK   3   SOLVENT ATOMS            : 464                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.00000                                             
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 2.39000                                              
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) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
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        : 0.34                                                 
REMARK   3   BSOL        : 34.32                                                
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  : ION.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   : ION.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 1ND6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017776.                                   
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                         : NULL                               
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   : 89003                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
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       59.94500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.44500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      101.66000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.44500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.94500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      101.66000            
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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, 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: 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: 6670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASN B  1343                                                      
REMARK 465     SER B  1344                                                      
REMARK 465     HIS B  1345                                                      
REMARK 465     GLN B  1346                                                      
REMARK 465     GLY B  1347                                                      
REMARK 465     THR B  1348                                                      
REMARK 465     GLU B  1349                                                      
REMARK 465     ASP B  1350                                                      
REMARK 465     SER B  1351                                                      
REMARK 465     THR B  1352                                                      
REMARK 465     ASP B  1353                                                      
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              0.25            
REMARK 500   O4   NAG I     1     O1   NAG I     2              0.27            
REMARK 500   ND2  ASN A   301     O1   NAG F     1              0.30            
REMARK 500   O6   MAN I     4     O1   MAN I     5              0.31            
REMARK 500   ND2  ASN A   188     O1   NAG E     1              0.32            
REMARK 500   ND2  ASN D  3187     O1   NAG D  5015              0.36            
REMARK 500   C4   NAG G     1     O1   NAG G     2              1.66            
REMARK 500   C4   NAG I     1     O1   NAG I     2              1.69            
REMARK 500   C6   MAN I     4     O1   MAN I     5              1.73            
REMARK 500   OE2  GLU D  3301     O1   NAG I     1              2.14            
REMARK 500   CB   HIS B  1304     OXT  GLY B  9000              2.18            
REMARK 500   O4   NAG H     1     O1   NAG H     2              2.18            
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    LEU A  61       59.69   -109.45                                   
REMARK 500    ASN A  62       40.64    -82.69                                   
REMARK 500    SER A  64       88.78    -42.86                                   
REMARK 500    TYR A  65      111.65     53.88                                   
REMARK 500    LEU A 121      -50.17   -134.87                                   
REMARK 500    VAL A 177      -58.67   -128.86                                   
REMARK 500    ILE A 217      -52.98     73.08                                   
REMARK 500    GLN A 227     -109.08   -126.98                                   
REMARK 500    SER A 247       42.60    -81.48                                   
REMARK 500    ALA A 256     -144.13   -144.66                                   
REMARK 500    ALA A 279       16.00     56.97                                   
REMARK 500    CYS A 315     -155.73   -128.59                                   
REMARK 500    PRO A 330      -18.27    -49.59                                   
REMARK 500    ASP A 335       79.08   -152.16                                   
REMARK 500    LEU B1060       58.84   -102.77                                   
REMARK 500    TYR B1064      129.59     11.92                                   
REMARK 500    LEU B1120      -54.60   -143.14                                   
REMARK 500    ASN B1127       44.07    -95.79                                   
REMARK 500    HIS B1149      -52.62    -27.66                                   
REMARK 500    LEU B1158       -3.11    -57.22                                   
REMARK 500    GLN B1167       21.63    -75.74                                   
REMARK 500    VAL B1176      -53.20   -127.72                                   
REMARK 500    ALA B1194       75.01    -63.43                                   
REMARK 500    ILE B1216      -46.87     74.20                                   
REMARK 500    GLN B1226     -101.70   -125.68                                   
REMARK 500    ALA B1255     -139.84   -141.45                                   
REMARK 500    VAL B1269       16.23   -141.21                                   
REMARK 500    ALA B1278       16.49     57.88                                   
REMARK 500    GLU B1288      -82.01   -133.31                                   
REMARK 500    LYS B1289       59.47   -106.67                                   
REMARK 500    GLU B1301      126.41   -173.15                                   
REMARK 500    ASP B1334       77.25   -152.54                                   
REMARK 500    GLU B1338       -7.03    -59.57                                   
REMARK 500    THR B1341     -113.58    -88.09                                   
REMARK 500    LEU C2060       41.14    -95.88                                   
REMARK 500    PHE C2091       66.76   -119.39                                   
REMARK 500    GLN C2119       42.24   -103.20                                   
REMARK 500    LEU C2120      -55.38   -159.56                                   
REMARK 500    ASN C2127       51.35    -95.88                                   
REMARK 500    GLN C2167       48.50    -70.49                                   
REMARK 500    VAL C2176      -56.34   -128.67                                   
REMARK 500    HIS C2186       44.27    -92.41                                   
REMARK 500    ASN C2187       45.93     35.74                                   
REMARK 500    ILE C2216      -61.03     71.11                                   
REMARK 500    GLN C2226      -99.82   -127.77                                   
REMARK 500    ALA C2255     -148.81   -139.35                                   
REMARK 500    PRO C2275      108.59    -58.43                                   
REMARK 500    ALA C2278        5.64     57.78                                   
REMARK 500    LYS C2289       56.43    155.63                                   
REMARK 500    CYS C2314     -165.78   -129.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 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: 1ND5   RELATED DB: PDB                                   
DBREF  1ND6 A    1   354  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND6 B 1000  1353  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND6 C 2000  2353  UNP    P15309   PPAP_HUMAN      33    386             
DBREF  1ND6 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 1ND6 ASN A  188  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN A  301  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN B 1187  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN B 1300  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN C 2300  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN D 3187  ASN  GLYCOSYLATION SITE                                 
MODRES 1ND6 ASN D 3300  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      15                                                       
HET    NAG  E   2      15                                                       
HET    MAN  E   3      12                                                       
HET    MAN  E   4      12                                                       
HET    NAG  F   1      15                                                       
HET    NAG  F   2      15                                                       
HET    NAG  G   1      15                                                       
HET    NAG  G   2      15                                                       
HET    MAN  G   3      12                                                       
HET    MAN  G   4      12                                                       
HET    MAN  G   5      12                                                       
HET    NAG  H   1      15                                                       
HET    NAG  H   2      15                                                       
HET    MAN  H   3      12                                                       
HET    NAG  I   1      15                                                       
HET    NAG  I   2      15                                                       
HET    MAN  I   3      12                                                       
HET    MAN  I   4      12                                                       
HET    MAN  I   5      12                                                       
HET    PO4  A8000       5                                                       
HET    1PE  A6000      16                                                       
HET    NAG  B5006      15                                                       
HET    PO4  B8001       5                                                       
HET    GLY  B9000       5                                                       
HET    1PE  B7000      16                                                       
HET    PO4  C8002       5                                                       
HET    1PE  C7001      16                                                       
HET    NAG  D5015      15                                                       
HET    PO4  D8003       5                                                       
HET    1PE  D7002      16                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     GLY GLYCINE                                                          
HETSYN     1PE PEG400                                                           
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL   5  MAN    9(C6 H12 O6)                                                 
FORMUL  10  PO4    4(O4 P 3-)                                                   
FORMUL  11  1PE    4(C10 H22 O6)                                                
FORMUL  14  GLY    C2 H5 N O2                                                   
FORMUL  21  HOH   *464(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 LYS A   66  GLU A   68  5                                   3    
HELIX    4   4 VAL A   77  PHE A   92  1                                  16    
HELIX    5   5 GLU A   95  ILE A   99  5                                   5    
HELIX    6   6 PRO A  115  ASP A  119  5                                   5    
HELIX    7   7 CYS A  129  SER A  142  1                                  14    
HELIX    8   8 SER A  142  HIS A  150  1                                   9    
HELIX    9   9 TYR A  152  GLY A  164  1                                  13    
HELIX   10  10 ASP A  169  VAL A  177  1                                   9    
HELIX   11  11 VAL A  177  HIS A  187  1                                  11    
HELIX   12  12 THR A  196  GLY A  216  1                                  21    
HELIX   13  13 LYS A  219  GLN A  227  1                                   9    
HELIX   14  14 GLY A  228  ILE A  245  1                                  18    
HELIX   15  15 HIS A  257  LEU A  268  1                                  12    
HELIX   16  16 LEU A  321  GLY A  329  1                                   9    
HELIX   17  17 PRO A  330  ILE A  332  5                                   3    
HELIX   18  18 ASP A  335  CYS A  340  1                                   6    
HELIX   19  19 LYS B 1026  TRP B 1030  5                                   5    
HELIX   20  20 THR B 1038  TYR B 1056  1                                  19    
HELIX   21  21 VAL B 1076  PHE B 1091  1                                  16    
HELIX   22  22 GLU B 1094  ILE B 1098  5                                   5    
HELIX   23  23 PRO B 1114  ASP B 1118  5                                   5    
HELIX   24  24 CYS B 1128  SER B 1141  1                                  14    
HELIX   25  25 SER B 1141  HIS B 1149  1                                   9    
HELIX   26  26 TYR B 1151  GLY B 1163  1                                  13    
HELIX   27  27 ASP B 1168  VAL B 1176  1                                   9    
HELIX   28  28 VAL B 1176  HIS B 1186  1                                  11    
HELIX   29  29 THR B 1195  GLY B 1215  1                                  21    
HELIX   30  30 LYS B 1218  GLN B 1226  1                                   9    
HELIX   31  31 GLN B 1226  THR B 1242  1                                  17    
HELIX   32  32 HIS B 1256  LEU B 1267  1                                  12    
HELIX   33  33 LEU B 1320  GLY B 1328  1                                   9    
HELIX   34  34 PRO B 1329  ILE B 1331  5                                   3    
HELIX   35  35 ASP B 1334  CYS B 1339  1                                   6    
HELIX   36  36 LYS C 2026  TRP C 2030  5                                   5    
HELIX   37  37 THR C 2038  TYR C 2056  1                                  19    
HELIX   38  38 VAL C 2076  PHE C 2091  1                                  16    
HELIX   39  39 GLU C 2094  ILE C 2098  5                                   5    
HELIX   40  40 PRO C 2114  ASP C 2118  5                                   5    
HELIX   41  41 CYS C 2128  SER C 2141  1                                  14    
HELIX   42  42 SER C 2141  HIS C 2149  1                                   9    
HELIX   43  43 TYR C 2151  ALA C 2156  1                                   6    
HELIX   44  44 THR C 2157  GLY C 2163  1                                   7    
HELIX   45  45 ASP C 2168  VAL C 2176  1                                   9    
HELIX   46  46 VAL C 2176  HIS C 2186  1                                  11    
HELIX   47  47 THR C 2195  GLY C 2215  1                                  21    
HELIX   48  48 LYS C 2218  GLN C 2226  1                                   9    
HELIX   49  49 GLY C 2227  ILE C 2244  1                                  18    
HELIX   50  50 HIS C 2256  ASP C 2268  1                                  13    
HELIX   51  51 LEU C 2320  GLY C 2328  1                                   9    
HELIX   52  52 PRO C 2329  ILE C 2331  5                                   3    
HELIX   53  53 ASP C 2334  CYS C 2339  1                                   6    
HELIX   54  54 LYS D 3026  TRP D 3030  5                                   5    
HELIX   55  55 THR D 3038  TYR D 3056  1                                  19    
HELIX   56  56 VAL D 3076  PHE D 3091  1                                  16    
HELIX   57  57 GLU D 3094  ILE D 3098  5                                   5    
HELIX   58  58 PRO D 3114  ASP D 3118  5                                   5    
HELIX   59  59 CYS D 3128  SER D 3141  1                                  14    
HELIX   60  60 SER D 3141  HIS D 3149  1                                   9    
HELIX   61  61 TYR D 3151  GLY D 3163  1                                  13    
HELIX   62  62 ASP D 3168  VAL D 3176  1                                   9    
HELIX   63  63 VAL D 3176  HIS D 3186  1                                  11    
HELIX   64  64 THR D 3195  GLY D 3215  1                                  21    
HELIX   65  65 LYS D 3218  GLN D 3226  1                                   9    
HELIX   66  66 GLN D 3226  ILE D 3244  1                                  19    
HELIX   67  67 HIS D 3256  LEU D 3267  1                                  12    
HELIX   68  68 LEU D 3320  GLY D 3328  1                                   9    
HELIX   69  69 PRO D 3329  ILE D 3331  5                                   3    
HELIX   70  70 ASP D 3334  CYS D 3339  1                                   6    
SHEET    1   A 7 HIS A 112  VAL A 114  0                                        
SHEET    2   A 7 VAL A  70  THR A  75  1  N  SER A  74   O  HIS A 112           
SHEET    3   A 7 LEU A 251  ALA A 256  1  O  MET A 253   N  ARG A  73           
SHEET    4   A 7 GLU A   2  ARG A  11  1  N  PHE A  10   O  ALA A 256           
SHEET    5   A 7 CYS A 281  GLU A 289 -1  O  HIS A 282   N  VAL A   9           
SHEET    6   A 7 GLU A 292  ARG A 300 -1  O  GLU A 296   N  GLU A 285           
SHEET    7   A 7 TYR A 308  PRO A 309 -1  O  TYR A 308   N  TYR A 299           
SHEET    1   B 7 HIS A 112  VAL A 114  0                                        
SHEET    2   B 7 VAL A  70  THR A  75  1  N  SER A  74   O  HIS A 112           
SHEET    3   B 7 LEU A 251  ALA A 256  1  O  MET A 253   N  ARG A  73           
SHEET    4   B 7 GLU A   2  ARG A  11  1  N  PHE A  10   O  ALA A 256           
SHEET    5   B 7 CYS A 281  GLU A 289 -1  O  HIS A 282   N  VAL A   9           
SHEET    6   B 7 GLU A 292  ARG A 300 -1  O  GLU A 296   N  GLU A 285           
SHEET    7   B 7 SER A 318  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 B1250  ALA B1255  1  O  MET B1252   N  ARG B1072           
SHEET    4   C 7 GLU B1001  ARG B1010  1  N  PHE B1009   O  ALA B1255           
SHEET    5   C 7 CYS B1280  PHE B1287 -1  O  LEU B1285   N  PHE B1004           
SHEET    6   C 7 TYR B1292  ARG B1299 -1  O  GLU B1295   N  GLU B1284           
SHEET    7   C 7 TYR B1307  LEU B1309 -1  O  TYR B1307   N  TYR B1298           
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 B1250  ALA B1255  1  O  MET B1252   N  ARG B1072           
SHEET    4   D 7 GLU B1001  ARG B1010  1  N  PHE B1009   O  ALA B1255           
SHEET    5   D 7 CYS B1280  PHE B1287 -1  O  LEU B1285   N  PHE B1004           
SHEET    6   D 7 TYR B1292  ARG B1299 -1  O  GLU B1295   N  GLU B1284           
SHEET    7   D 7 CYS B1318  PRO B1319 -1  O  CYS B1318   N  VAL B1294           
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  LEU C2007   O  TYR C2253           
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  LEU C2309   N  MET C2296           
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  LEU C2007   O  TYR C2253           
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  PHE D3009   O  ALA D3255           
SHEET    5   G 7 CYS D3280  PHE D3287 -1  O  HIS D3281   N  VAL D3008           
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  TYR D3307   N  TYR D3298           
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  PHE D3009   O  ALA D3255           
SHEET    5   H 7 CYS D3280  PHE D3287 -1  O  HIS D3281   N  VAL D3008           
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  2.03  
SSBOND   2 CYS A  315    CYS A  319                          1555   1555  2.04  
SSBOND   3 CYS B 1128    CYS B 1339                          1555   1555  2.03  
SSBOND   4 CYS B 1314    CYS B 1318                          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  2.04  
SSBOND   7 CYS D 3128    CYS D 3339                          1555   1555  2.04  
SSBOND   8 CYS D 3314    CYS D 3318                          1555   1555  2.04  
LINK         ND2 ASN A 188                 C1  NAG E   1     1555   1555  1.46  
LINK         CG  ASN A 188                 O1  NAG E   1     1555   1555  1.61  
LINK         ND2 ASN A 301                 C1  NAG F   1     1555   1555  1.45  
LINK         CG  ASN A 301                 O1  NAG F   1     1555   1555  1.61  
LINK         ND2 ASN B1187                 C1  NAG B5006     1555   1555  1.45  
LINK         ND2 ASN B1300                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN C2300                 C1  NAG H   1     1555   1555  1.45  
LINK         ND2 ASN D3187                 C1  NAG D5015     1555   1555  1.45  
LINK         CG  ASN D3187                 O1  NAG D5015     1555   1555  1.67  
LINK         ND2 ASN D3300                 C1  NAG I   1     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.39  
LINK         O4  NAG E   2                 C1  MAN E   3     1555   1555  1.39  
LINK         O6  MAN E   3                 C1  MAN E   4     1555   1555  1.41  
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 G   2                 C1  MAN G   3     1555   1555  1.39  
LINK         O3  MAN G   3                 C1  MAN G   4     1555   1555  1.40  
LINK         O6  MAN G   3                 C1  MAN G   5     1555   1555  1.40  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.39  
LINK         O4  NAG H   2                 C1  MAN H   3     1555   1555  1.40  
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  
LINK         O6  MAN I   3                 C1  MAN I   4     1555   1555  1.40  
LINK         O6  MAN I   4                 C1  MAN I   5     1555   1555  1.40  
CISPEP   1 LEU A  124    PRO A  125          0         0.10                     
CISPEP   2 LEU B 1123    PRO B 1124          0        -0.04                     
CISPEP   3 LEU C 2123    PRO C 2124          0        -0.36                     
CISPEP   4 LEU D 3123    PRO D 3124          0         0.04                     
CRYST1  119.890  203.320   70.890  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      0.008341  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004918  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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