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Database: PDB
Entry: 1DHK
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HEADER    COMPLEX (HYDROLASE/INHIBITOR)           14-OCT-96   1DHK              
TITLE     STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PORCINE PANCREATIC ALPHA-AMYLASE;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PPA;                                                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BEAN LECTIN-LIKE INHIBITOR;                                
COMPND   8 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: PHASEOLUS VULGARIS;                             
SOURCE   8 ORGANISM_TAXID: 3885;                                                
SOURCE   9 ORGAN: SEED                                                          
KEYWDS    PANCREATIC ALPHA-AMYLASE, PORCINE, LECTIN-LIKE INHIBITOR, COMPLEX     
KEYWDS   2 (HYDROLASE-INHIBITOR), COMPLEX (HYDROLASE-INHIBITOR) COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BOMPARD-GILLES,F.PAYAN                                              
REVDAT   3   13-JUL-11 1DHK    1       VERSN                                    
REVDAT   2   24-FEB-09 1DHK    1       VERSN                                    
REVDAT   1   24-DEC-97 1DHK    0                                                
JRNL        AUTH   C.BOMPARD-GILLES,P.ROUSSEAU,P.ROUGE,F.PAYAN                  
JRNL        TITL   SUBSTRATE MIMICRY IN THE ACTIVE CENTER OF A MAMMALIAN        
JRNL        TITL 2 ALPHA-AMYLASE: STRUCTURAL ANALYSIS OF AN ENZYME-INHIBITOR    
JRNL        TITL 3 COMPLEX.                                                     
JRNL        REF    STRUCTURE                     V.   4  1441 1996              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   8994970                                                      
JRNL        DOI    10.1016/S0969-2126(96)00151-7                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.GILLES,P.ROUSSEAU,P.ROUGE,F.PAYAN                          
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF PIG        
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH A BEAN LECTIN-LIKE  
REMARK   1  TITL 3 INHIBITOR                                                    
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52   581 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN                      
REMARK   1  TITL   THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. STRUCTURE OF 
REMARK   1  TITL 2 THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A             
REMARK   1  TITL 3 CARBOHYDRATE INHIBITOR REFINED TO 2.2-A RESOLUTION           
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG PANCREATIC   
REMARK   1  TITL 2 ALPHA-AMYLASE AT 2.1 A RESOLUTION                            
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 66557                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5429                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 322                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.48                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : 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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DHK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.928                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66769                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PPA NATIVE AND LECTIN FROM SEEDS OF LATHYRUS OCHRUS  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       75.80000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       75.80000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: ALPHA-AI IS A DIMERIC MOLECULE (I2) CONSISTING OF TWO        
REMARK 300 IDENTICAL SUBUNITS.  IT BINDS TWO AMYLASE MOLECULES (2E)             
REMARK 300 TO FORM A DIMERIC COMPLEX E2I2.  HOWEVER, THE                        
REMARK 300 CRYSTALLOGRAPHIC ASYMMETRIC UNIT CORRESPONDS TO HALF THE             
REMARK 300 COMPLEX MOLECULE (EI).  IN THIS ENTRY, COORDINATES FOR ALL           
REMARK 300 ATOMS ARE PROVIDED FOR ONE CHAIN OF AMYLASE AND ONE CHAIN            
REMARK 300 OF ALPHA-AI.                                                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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   BIOMT1   2 -1.000000  0.000000  0.000000      151.60000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLN B    75                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     ASN B    77                                                      
REMARK 465     GLN B    90                                                      
REMARK 465     PRO B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     LYS B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     ILE B   205                                                      
REMARK 465     ASN B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     LYS B   208                                                      
REMARK 465     ASP B   209                                                      
REMARK 465     GLN B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     GLU B   213                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     ASN B   216                                                      
REMARK 465     ILE B   217                                                      
REMARK 465     VAL B   218                                                      
REMARK 465     LEU B   219                                                      
REMARK 465     ASN B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     ILE B   222                                                      
REMARK 465     LEU B   223                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B  74    CG   CD   NE   CZ   NH1  NH2                        
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   H    ARG A   319     H1   HOH A   619              0.96            
REMARK 500   HH   TYR A    67     HH   TYR A   131              0.99            
REMARK 500   H    VAL B   177     H2   HOH B   538              1.04            
REMARK 500   H    SER A   478     H2   HOH A   603              1.05            
REMARK 500   HG1  THR A    11    HD22  ASN A   399              1.09            
REMARK 500  HD22  ASN A   431     H2   HOH A   554              1.11            
REMARK 500   H    SER A    43     H1   HOH A   501              1.11            
REMARK 500   H    GLY A   446     H2   HOH A   649              1.12            
REMARK 500   H    ASN B    12     H2   HOH B   516              1.13            
REMARK 500   CD1  PHE B    84     O    HOH B   513              1.13            
REMARK 500   H    ILE A   372     H2   HOH A   650              1.13            
REMARK 500   HE2  HIS A   491     H1   HOH A   680              1.14            
REMARK 500   H    LEU B    18     H1   HOH B   524              1.16            
REMARK 500   HG   SER B    41     H1   HOH B   532              1.17            
REMARK 500  HH12  ARG A    61     HG   SER A    73              1.18            
REMARK 500  HH12  ARG B    71     H1   HOH B   563              1.19            
REMARK 500   H    GLN A     7     H2   HOH A   539              1.20            
REMARK 500   H    ILE A    93     H2   HOH A   507              1.20            
REMARK 500   H    HIS A   305     H1   HOH A   647              1.21            
REMARK 500  HH12  ARG A   421     H1   HOH A   565              1.21            
REMARK 500   HG   SER A   145     H    GLY A   147              1.22            
REMARK 500   H    GLN A     5     H2   HOH A   634              1.23            
REMARK 500   HH   TYR A   182     H1   HOH A   530              1.24            
REMARK 500  HH11  ARG A    56     H2   HOH A   643              1.24            
REMARK 500   H    TYR B   186     H2   HOH B   519              1.24            
REMARK 500  HD22  ASN A   373     HG1  THR A   377              1.25            
REMARK 500   HG   SER B   176     H2   HOH B   539              1.26            
REMARK 500   H    TYR A   468     H1   HOH A   642              1.27            
REMARK 500  HE22  GLN A   441     H2   HOH A   640              1.27            
REMARK 500  CA     CA B   497     H1   HOH B   545              1.28            
REMARK 500  HE21  GLN A    41    HH11  ARG A   337              1.29            
REMARK 500  HD21  ASN A   298     HH   TYR B    37              1.29            
REMARK 500   HG   SER A    12     H2   HOH A   536              1.31            
REMARK 500  HD22  ASN A    88     H1   HOH A   572              1.31            
REMARK 500   H2   HOH A   688     H1   HOH A   689              1.33            
REMARK 500  HE22  GLN A   302    HH12  ARG A   303              1.33            
REMARK 500  CA     CA A   500     H1   HOH A   518              1.34            
REMARK 500   HE   ARG A   392     H2   HOH A   599              1.35            
REMARK 500   H    LYS A   200     H1   HOH A   586              1.36            
REMARK 500   H1   HOH A   570     H2   HOH A   726              1.36            
REMARK 500   HD1  HIS A   331     H    TYR A   333              1.37            
REMARK 500   H    ALA A   307     H1   HOH A   670              1.38            
REMARK 500   H1   HOH A   559     H2   HOH B   536              1.38            
REMARK 500   HG   SER A   275     H1   HOH A   691              1.38            
REMARK 500   HH   TYR A   468     H2   HOH A   735              1.39            
REMARK 500   H    LEU A    69     H1   HOH A   550              1.41            
REMARK 500   H1   HOH A   537     H1   HOH A   549              1.41            
REMARK 500   HD1  HIS A   491     H    GLU A   493              1.43            
REMARK 500   HG1  THR A    71     H2   HOH A   522              1.43            
REMARK 500   HE2  HIS A   299     H2   HOH A   574              1.43            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      97 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   H2   ALA B     1     H1   HOH B   527     2655     1.13            
REMARK 500   HZ1  LYS A   495     H2   HOH A   751     4655     1.14            
REMARK 500  HD22  ASN B    15     H2   HOH B   521     2655     1.41            
REMARK 500   H    THR A   448     H1   HOH A   751     4655     1.48            
REMARK 500   H2   HOH A   687     H2   HOH A   687     2656     1.55            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN A 216   CA    ASN A 216   CB     -0.182                       
REMARK 500    ARG A 424   CD    ARG A 424   NE     -0.136                       
REMARK 500    ASP B  96   CA    ASP B  96   CB     -0.275                       
REMARK 500    ARG B 108   CD    ARG B 108   NE     -0.153                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A   8   CA  -  C   -  O   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    GLY A   9   CA  -  C   -  O   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    SER A   8   CA  -  C   -  N   ANGL. DEV. =  13.5 DEGREES          
REMARK 500    LEU A 162   CB  -  CG  -  CD1 ANGL. DEV. = -19.3 DEGREES          
REMARK 500    LEU A 162   CB  -  CG  -  CD2 ANGL. DEV. =  21.1 DEGREES          
REMARK 500    LEU A 165   CB  -  CG  -  CD2 ANGL. DEV. =  27.3 DEGREES          
REMARK 500    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    ARG A 176   NE  -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 424   CD  -  NE  -  CZ  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    VAL A 469   CA  -  CB  -  CG1 ANGL. DEV. =  19.6 DEGREES          
REMARK 500    VAL B  59   CA  -  CB  -  CG2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    THR B  67   CA  -  CB  -  CG2 ANGL. DEV. =  21.4 DEGREES          
REMARK 500    ARG B  71   CG  -  CD  -  NE  ANGL. DEV. = -19.4 DEGREES          
REMARK 500    ASP B  96   CB  -  CA  -  C   ANGL. DEV. =  25.8 DEGREES          
REMARK 500    ASP B  96   CA  -  CB  -  CG  ANGL. DEV. =  43.7 DEGREES          
REMARK 500    VAL B  98   CA  -  CB  -  CG1 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG B 108   CD  -  NE  -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG B 108   NE  -  CZ  -  NH1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG B 108   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   8       97.45     -4.71                                   
REMARK 500    TYR A  31      -61.37   -145.70                                   
REMARK 500    MET A 102     -146.98   -110.91                                   
REMARK 500    ASP A 317       62.38   -115.66                                   
REMARK 500    SER A 414     -111.76   -131.03                                   
REMARK 500    ASP A 433       34.92    -84.75                                   
REMARK 500    PRO A 486       42.40    -72.70                                   
REMARK 500    PHE B 102       79.20   -110.34                                   
REMARK 500    ASN B 115       -0.01     71.93                                   
REMARK 500    TYR B 186     -120.03     52.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 424         0.20    SIDE CHAIN                              
REMARK 500    ARG B 108         0.16    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A   8        18.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP B  96        21.0      L          L   OUTSIDE RANGE           
REMARK 500    TYR B 190        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 698        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B 570        DISTANCE =  5.10 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 100   OD1                                                    
REMARK 620 2 ASP A 167   OD1 115.7                                              
REMARK 620 3 ARG A 158   O   132.3 106.7                                        
REMARK 620 4 HIS A 201   O    71.7 145.8  60.9                                  
REMARK 620 5 ASN A 100   ND2  42.9  74.6 146.3  98.5                            
REMARK 620 6 ASP A 167   OD2 164.7  54.7  62.4 123.2 129.3                      
REMARK 620 7 HOH A 518   O    90.7  96.8 105.4 116.9 107.9  79.6                
REMARK 620 8 HOH A 525   O   111.1  75.2  59.4  71.3  89.7  79.3 158.3          
REMARK 620 9 HOH A 537   O   102.4 136.5  53.3  64.6 145.2  83.3  61.2 110.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 499  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  36   O                                                      
REMARK 620 2 SER B 189   O   115.0                                              
REMARK 620 3 HOH B 555   O   129.0 116.0                                        
REMARK 620 4 HOH B 556   O    85.9  80.9 101.6                                  
REMARK 620 5 HOH B 554   O    90.1  89.5  90.6 166.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 497  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 545   O                                                      
REMARK 620 2 HOH B 540   O   112.8                                              
REMARK 620 3 ASP B 112   OD2  80.6 146.3                                        
REMARK 620 4 ASP B 117   OD1  99.4  76.2  71.0                                  
REMARK 620 5 GLU B 101   OE1 161.1  82.2  80.6  72.1                            
REMARK 620 6 ASP B 117   OD2  69.9  61.5  98.3  44.4 110.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 497                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 499                  
DBREF  1DHK A    2   496  UNP    P00690   AMYP_PIG         2    496             
DBREF  1DHK B    1   223  UNP    P02873   LEA1_PHAVU      24    246             
SEQADV 1DHK VAL A   49  UNP  P00690    ILE    49 CONFLICT                       
SEQADV 1DHK GLN A  404  UNP  P00690    GLU   404 CONFLICT                       
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL VAL VAL THR          
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 A  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE GLN SER SER GLU TYR          
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE          
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS VAL ALA VAL          
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 A  496  LYS LEU                                                      
SEQRES   1 B  223  ALA THR GLU THR SER PHE ILE ILE ASP ALA PHE ASN LYS          
SEQRES   2 B  223  THR ASN LEU ILE LEU GLN GLY ASP ALA THR VAL SER SER          
SEQRES   3 B  223  ASN GLY ASN LEU GLN LEU SER TYR ASN SER TYR ASP SER          
SEQRES   4 B  223  MET SER ARG ALA PHE TYR SER ALA PRO ILE GLN ILE ARG          
SEQRES   5 B  223  ASP SER THR THR GLY ASN VAL ALA SER PHE ASP THR ASN          
SEQRES   6 B  223  PHE THR MET ASN ILE ARG THR HIS ARG GLN ALA ASN SER          
SEQRES   7 B  223  ALA VAL GLY LEU ASP PHE VAL LEU VAL PRO VAL GLN PRO          
SEQRES   8 B  223  GLU SER LYS GLY ASP THR VAL THR VAL GLU PHE ASP THR          
SEQRES   9 B  223  PHE LEU SER ARG ILE SER ILE ASP VAL ASN ASN ASN ASP          
SEQRES  10 B  223  ILE LYS SER VAL PRO TRP ASP VAL HIS ASP TYR ASP GLY          
SEQRES  11 B  223  GLN ASN ALA GLU VAL ARG ILE THR TYR ASN SER SER THR          
SEQRES  12 B  223  LYS VAL PHE SER VAL SER LEU SER ASN PRO SER THR GLY          
SEQRES  13 B  223  LYS SER ASN ASN VAL SER THR THR VAL GLU LEU GLU LYS          
SEQRES  14 B  223  GLU VAL TYR ASP TRP VAL SER VAL GLY PHE SER ALA THR          
SEQRES  15 B  223  SER GLY ALA TYR GLN TRP SER TYR GLU THR HIS ASP VAL          
SEQRES  16 B  223  LEU SER TRP SER PHE SER SER LYS PHE ILE ASN LEU LYS          
SEQRES  17 B  223  ASP GLN LYS SER GLU ARG SER ASN ILE VAL LEU ASN LYS          
SEQRES  18 B  223  ILE LEU                                                      
MODRES 1DHK ASN B   12  ASN  GLYCOSYLATION SITE                                 
MODRES 1DHK ASN B   65  ASN  GLYCOSYLATION SITE                                 
MODRES 1DHK ASN B  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1DHK PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    NAG  B 510      18                                                       
HET    NAG  B 511      17                                                       
HET    NAG  B 508      18                                                       
HET    NAG  B 509      17                                                       
HET    NAG  B 512      18                                                       
HET     CA  A 500       1                                                       
HET     CL  A 498       1                                                       
HET     CA  B 497       1                                                       
HET     CA  B 499       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   3  NAG    5(C8 H15 N O6)                                               
FORMUL   6   CA    3(CA 2+)                                                     
FORMUL   7   CL    CL 1-                                                        
FORMUL  10  HOH   *322(H2 O)                                                    
HELIX    1   1 TRP A   21  ARG A   30  1                                  10    
HELIX    2   2 TRP A   58  TYR A   62  5                                   5    
HELIX    3   3 GLU A   76  VAL A   89  1                                  14    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   6 PRO A  154  ASP A  159  1                                   6    
HELIX    6   7 ASP A  173  ILE A  189  1                                  17    
HELIX    7   9 PRO A  204  LYS A  213  1                                  10    
HELIX    8  10 SER A  244  TYR A  247  5                                   4    
HELIX    9  11 PHE A  256  ARG A  267  1                                  12    
HELIX   10  12 MET A  274  ASN A  279  5                                   6    
HELIX   11  13 GLY A  281  GLY A  285  5                                   5    
HELIX   12  14 PRO A  288  ALA A  292  5                                   5    
HELIX   13  15 PHE A  315  ALA A  330  5                                  16    
HELIX   14  16 CYS A  384  TRP A  388  5                                   5    
HELIX   15  17 ARG A  389  VAL A  400  1                                  12    
SHEET    1   A 8 SER A  12  LEU A  16  0                                        
SHEET    2   A 8 GLY A  38  VAL A  42  1  N  GLY A  38   O  SER A  12           
SHEET    3   A 8 ARG A  92  ALA A  97  1  N  ARG A  92   O  GLY A  38           
SHEET    4   A 8 ALA A 192  ASP A 197  1  N  ALA A 192   O  ILE A  93           
SHEET    5   A 8 PHE A 229  GLU A 233  1  N  PHE A 229   O  ALA A 192           
SHEET    6   A 8 ARG A 252  GLU A 255  1  N  ARG A 252   O  ILE A 230           
SHEET    7   A 8 ARG A 291  VAL A 294  1  O  ARG A 291   N  VAL A 253           
SHEET    8   A 8 PHE A 335  SER A 340  1  N  PHE A 335   O  ALA A 292           
SHEET    1   B 4 SER A  73  GLU A  76  0                                        
SHEET    2   B 4 LEU A  69  THR A  71 -1  O  CYS A  70   N  SER A  73           
SHEET    3   B 4 PRO A  45  VAL A  50  1  O  PRO A  45   N  CYS A  70           
SHEET    4   B 4 GLY A 110  THR A 114 -1  N  THR A 114   O  ASN A  48           
SHEET    1   C 2 ASN A 347  VAL A 349  0                                        
SHEET    2   C 2 GLU A 352  VAL A 354 -1  N  VAL A 354   O  ASN A 347           
SHEET    1   D 2 THR A 371  ASN A 373  0                                        
SHEET    2   D 2 THR A 376  GLY A 379 -1  N  GLY A 379   O  THR A 371           
SHEET    1   E 4 GLY A 110  THR A 114  0                                        
SHEET    2   E 4 CYS A 119  PRO A 121 -1  O  CYS A 119   N  GLY A 110           
SHEET    3   E 4 ARG A 124  PRO A 127 -1  N  ARG A 124   O  PRO A 121           
SHEET    4   E 4 TYR A 131  ALA A 133 -1  N  ALA A 133   O  ARG A 124           
SHEET    1   F 3 ASN A 100  SER A 105  0                                        
SHEET    2   F 3 GLY A 164  ALA A 169 -1  N  LEU A 168   O  ASN A 100           
SHEET    3   F 3 ASP A 135  ASN A 137 -1  O  ASP A 135   N  ALA A 169           
SHEET    1   G 3 GLY A 146  ILE A 148  0                                        
SHEET    2   G 3 GLN A 161  LEU A 162  1  N  GLN A 161   O  GLY A 146           
SHEET    3   G 3 GLY A 164  ALA A 169  1  N  LEU A 165   O  LEU A 162           
SHEET    1   H 4 PRO A 405  ASN A 412  0                                        
SHEET    2   H 4 ASN A 415  GLY A 422 -1  O  GLN A 416   N  ASN A 412           
SHEET    3   H 4 ARG A 424  ASN A 431 -1  N  ASN A 431   O  ASN A 415           
SHEET    4   H 4 PRO A 486  ALA A 492 -1  O  PRO A 486   N  ASN A 430           
SHEET    1   I 4 LEU A 436  THR A 442  0                                        
SHEET    2   I 4 GLY A 473  ILE A 479 -1  O  GLY A 473   N  THR A 442           
SHEET    3   I 4 ILE A 465  SER A 470 -1  O  SER A 470   N  GLY A 473           
SHEET    4   I 4 GLY A 447  ASP A 451 -1  N  GLY A 447   O  VAL A 469           
SHEET    1   J 2 ASP A 456  VAL A 458  0                                        
SHEET    2   J 2 SER A 461  THR A 463 -1  N  THR A 463   O  ASP A 456           
SHEET    1   K 6 SER B   5  ILE B   8  0                                        
SHEET    2   K 6 THR B 192  LYS B 203 -1  N  PHE B 200   O  PHE B   6           
SHEET    3   K 6 SER B  61  ARG B  71 -1  N  ARG B  71   O  THR B 192           
SHEET    4   K 6 ALA B 133  ASN B 140 -1  N  TYR B 139   O  PHE B  62           
SHEET    5   K 6 VAL B 145  ASN B 152 -1  N  SER B 151   O  GLU B 134           
SHEET    6   K 6 LYS B 157  THR B 164 -1  N  THR B 163   O  PHE B 146           
SHEET    1   L 7 LEU B  16  GLN B  19  0                                        
SHEET    2   L 7 SER B  39  TYR B  45 -1  N  PHE B  44   O  ILE B  17           
SHEET    3   L 7 VAL B 175  SER B 183 -1  N  SER B 183   O  SER B  39           
SHEET    4   L 7 GLY B  81  PRO B  88 -1  N  VAL B  87   O  SER B 176           
SHEET    5   L 7 VAL B  98  ASP B 103 -1  N  PHE B 102   O  LEU B  82           
SHEET    6   L 7 ARG B 108  VAL B 113 -1  N  ASP B 112   O  THR B  99           
SHEET    7   L 7 ASN B 116  PRO B 122 -1  N  VAL B 121   O  ILE B 109           
SHEET    1   M 3 ALA B  22  VAL B  24  0                                        
SHEET    2   M 3 LEU B  30  LEU B  32 -1  N  GLN B  31   O  THR B  23           
SHEET    3   M 3 HIS B 193  VAL B 195 -1  N  VAL B 195   O  LEU B  30           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.02  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.02  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33  
LINK        CA    CA A 500                 OD1 ASN A 100     1555   1555  1.74  
LINK        CA    CA A 500                 OD1 ASP A 167     1555   1555  1.96  
LINK         C1  NAG B 510                 O4  NAG B 511     1555   1555  1.44  
LINK         C1  NAG B 511                 ND2 ASN B  12     1555   1555  1.46  
LINK         C1  NAG B 508                 O4  NAG B 509     1555   1555  1.43  
LINK         C1  NAG B 509                 ND2 ASN B  65     1555   1555  1.46  
LINK         C1  NAG B 512                 ND2 ASN B 140     1555   1555  1.46  
LINK        CA    CA B 499                 O   SER B  36     1555   1555  2.05  
LINK        CA    CA B 499                 O   SER B 189     1555   1555  2.24  
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  3.14  
LINK        CA    CA A 500                 O   HIS A 201     1555   1555  2.85  
LINK        CA    CA A 500                 ND2 ASN A 100     1555   1555  3.17  
LINK        CA    CA A 500                 OD2 ASP A 167     1555   1555  2.61  
LINK        CA    CA A 500                 O   HOH A 518     1555   1555  2.02  
LINK        CA    CA A 500                 O   HOH A 525     1555   1555  2.53  
LINK        CA    CA A 500                 O   HOH A 537     1555   1555  2.98  
LINK        CA    CA B 497                 O   HOH B 545     1555   1555  1.73  
LINK        CA    CA B 497                 O   HOH B 540     1555   1555  2.17  
LINK        CA    CA B 497                 OD2 ASP B 112     1555   1555  2.47  
LINK        CA    CA B 497                 OD1 ASP B 117     1555   1555  2.63  
LINK        CA    CA B 497                 OE1 GLU B 101     1555   1555  2.73  
LINK        CA    CA B 497                 OD2 ASP B 117     1555   1555  3.08  
LINK        CA    CA B 499                 O   HOH B 555     1555   1555  2.05  
LINK        CA    CA B 499                 O   HOH B 556     1555   1555  2.20  
LINK        CA    CA B 499                 O   HOH B 554     1555   1555  2.45  
CISPEP   1 ASN A   53    PRO A   54          0        -0.02                     
CISPEP   2 VAL A  129    PRO A  130          0         0.01                     
SITE     1 AC1  3 SER B  54  GLU B 170  NAG B 511                               
SITE     1 AC2  8 PHE B  11  ASN B  12  SER B  25  ASP B 173                    
SITE     2 AC2  8 TRP B 174  NAG B 510  HOH B 520  HOH B 541                    
SITE     1 AC3  2 ARG B 136  NAG B 509                                          
SITE     1 AC4  5 ASP B  63  ASN B  65  ARG B 136  SER B 199                    
SITE     2 AC4  5 NAG B 508                                                     
SITE     1 AC5  2 ASN B 140  THR B 143                                          
SITE     1 AC6  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC6  7 HOH A 518  HOH A 525  HOH A 537                               
SITE     1 AC7  4 ARG A 195  ASN A 298  ARG A 337  HOH A 523                    
SITE     1 AC8  6 GLU A 149  GLU B 101  ASP B 112  ASP B 117                    
SITE     2 AC8  6 HOH B 540  HOH B 545                                          
SITE     1 AC9  6 SER B  33  SER B  36  SER B 189  HOH B 554                    
SITE     2 AC9  6 HOH B 555  HOH B 556                                          
CRYST1  151.600   79.400   68.000  90.00  91.54  90.00 C 1 2 1       4          
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      0.006596  0.000000  0.000177        0.00000                         
SCALE2      0.000000  0.012594  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014711        0.00000                         
HETATM    1  N   PCA A   1      89.631  53.022  21.568  1.00 29.23           N  
HETATM    2  CA  PCA A   1      90.068  51.638  21.733  1.00 27.26           C  
HETATM    3  CB  PCA A   1      88.744  50.997  21.886  1.00 28.59           C  
HETATM    4  CG  PCA A   1      88.144  52.155  22.751  1.00 34.62           C  
HETATM    5  CD  PCA A   1      88.531  53.542  22.113  1.00 31.49           C  
HETATM    6  OE  PCA A   1      87.822  54.539  22.262  1.00 43.11           O  
HETATM    7  C   PCA A   1      90.758  50.986  20.550  1.00 22.51           C  
HETATM    8  O   PCA A   1      91.480  50.005  20.695  1.00 18.82           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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