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Database: PDB
Entry: 2TAA
LinkDB: 2TAA
Original site: 2TAA 
HEADER    HYDROLASE (O-GLYCOSYL)                  18-OCT-82   2TAA              
TITLE     STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TAKA-AMYLASE A;                                            
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.2.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062                                                 
KEYWDS    HYDROLASE (O-GLYCOSYL)                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KUSUNOKI,Y.MATSUURA,N.TANAKA,M.KAKUDO                               
REVDAT   9   22-OCT-14 2TAA    1       LINK                                     
REVDAT   8   13-JUL-11 2TAA    1       VERSN                                    
REVDAT   7   24-FEB-09 2TAA    1       VERSN                                    
REVDAT   6   15-OCT-89 2TAA    3       MTRIX                                    
REVDAT   5   22-OCT-84 2TAA    1       SEQRES SHEET                             
REVDAT   4   17-JUL-84 2TAA    2       REMARK SSBOND CONECT                     
REVDAT   3   31-JAN-84 2TAA    1       REMARK                                   
REVDAT   2   30-SEP-83 2TAA    1       REVDAT                                   
REVDAT   1   21-OCT-82 2TAA    0                                                
SPRSDE     21-OCT-82 2TAA      1TAA                                             
JRNL        AUTH   Y.MATSUURA,M.KUSUNOKI,W.HARADA,M.KAKUDO                      
JRNL        TITL   STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A  
JRNL        REF    J.BIOCHEM.(TOKYO)             V.  95   697 1984              
JRNL        REFN                   ISSN 0021-924X                               
JRNL        PMID   6609921                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.MATSUURA,M.KUSUNOKI,W.HARADA,N.TANAKA,Y.IGA,N.YASUOKA,     
REMARK   1  AUTH 2 H.TODA,K.NARITA,M.KAKUDO                                     
REMARK   1  TITL   MOLECULAR STRUCTURE OF TAKA-AMYLASE A. I. BACKBONE CHAIN     
REMARK   1  TITL 2 FOLDING AT 3 ANGSTROMS RESOLUTION                            
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V.  87  1555 1980              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.MATSUURA,M.KUSUNOKI,W.DATE,S.HARADA,S.BANDO,N.TANAKA,      
REMARK   1  AUTH 2 M.KAKUDO                                                     
REMARK   1  TITL   LOW RESOLUTION CRYSTAL STRUCTURES OF TAKA-AMYLASE A AND ITS  
REMARK   1  TITL 2 COMPLEXES WITH INHIBITORS                                    
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V.  86  1773 1979              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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             : NULL                           
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) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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            : 11070                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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 2TAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 285                                                                      
REMARK 285 THE ENTRY COORDINATES                                                
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       66.66667            
REMARK 290   SMTRY3   2  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 CRYSTALLOGRAPHIC ASYMMETRIC UNIT FOR THIS ENTRY          
REMARK 300 CONTAINS THREE AMYLASE MOLECULES.  THEY CAN BE GENERATED             
REMARK 300 FROM CHAIN A OF THIS ENTRY BY APPLYING THE                           
REMARK 300 NON-CRYSTALLOGRAPHIC THREE-FOLD SCREW AXIS GIVEN BY THE              
REMARK 300 MTRIX RECORDS BELOW.                                                 
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 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 479  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD2                                                    
REMARK 620 2 ASN A 121   OD1  92.1                                              
REMARK 620 3 ASP A 175   OD1  43.0  81.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 479  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 121   OD1                                                    
REMARK 620 2 ASP B 175   OD1  81.5                                              
REMARK 620 3 ASP B 175   OD2  92.1  43.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 479  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 121   OD1                                                    
REMARK 620 2 ASP C 175   OD1  81.5                                              
REMARK 620 3 ASP C 175   OD2  92.1  43.0                                        
REMARK 620 N                    1     2                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE NINE-STRANDED SHEET BS1 DESCRIBED BELOW IS ACTUALLY              
REMARK 700 AN EIGHT-STRANDED BETA BARREL.  THIS IS DENOTED BY THE               
REMARK 700 FIRST STRAND RECURRING AS THE LAST STRAND.                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 479                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 479                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 479                  
DBREF  2TAA A    1   478  UNP    P10529   AMYA_ASPOR      22    499             
DBREF  2TAA B    1   478  UNP    P10529   AMYA_ASPOR      22    499             
DBREF  2TAA C    1   478  UNP    P10529   AMYA_ASPOR      22    499             
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN ASP CYS ALA TYR GLY ASP ALA          
SEQRES   7 A  478  TYR THR GLY TYR TRP GLN THR ASP ILE TYR SER LEU ASN          
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY LEU PRO          
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN PRO TYR ILE LYS ASP ASP          
SEQRES  31 A  478  THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER GLN          
SEQRES  32 A  478  ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY ASP          
SEQRES  33 A  478  SER TYR THR LEU SER LEU SER GLY ALA SER TYR THR ALA          
SEQRES  34 A  478  GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR VAL          
SEQRES  35 A  478  THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET ALA          
SEQRES  36 A  478  GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS LEU          
SEQRES  37 A  478  ALA GLY SER LYS ILE CYS SER ASP SER SER                      
SEQRES   1 B  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 B  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 B  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 B  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 B  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 B  478  THR ALA GLN LEU PRO GLN ASP CYS ALA TYR GLY ASP ALA          
SEQRES   7 B  478  TYR THR GLY TYR TRP GLN THR ASP ILE TYR SER LEU ASN          
SEQRES   8 B  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 B  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 B  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 B  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 B  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 B  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 B  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 B  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 B  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 B  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 B  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 B  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 B  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 B  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 B  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 B  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 B  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 B  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY LEU PRO          
SEQRES  26 B  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 B  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 B  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 B  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 B  478  GLY PHE VAL THR TYR LYS ASN PRO TYR ILE LYS ASP ASP          
SEQRES  31 B  478  THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER GLN          
SEQRES  32 B  478  ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY ASP          
SEQRES  33 B  478  SER TYR THR LEU SER LEU SER GLY ALA SER TYR THR ALA          
SEQRES  34 B  478  GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR VAL          
SEQRES  35 B  478  THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET ALA          
SEQRES  36 B  478  GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS LEU          
SEQRES  37 B  478  ALA GLY SER LYS ILE CYS SER ASP SER SER                      
SEQRES   1 C  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 C  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 C  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 C  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 C  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 C  478  THR ALA GLN LEU PRO GLN ASP CYS ALA TYR GLY ASP ALA          
SEQRES   7 C  478  TYR THR GLY TYR TRP GLN THR ASP ILE TYR SER LEU ASN          
SEQRES   8 C  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 C  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 C  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 C  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 C  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 C  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 C  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 C  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 C  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 C  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 C  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 C  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 C  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 C  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 C  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 C  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 C  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 C  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY LEU PRO          
SEQRES  26 C  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 C  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 C  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 C  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 C  478  GLY PHE VAL THR TYR LYS ASN PRO TYR ILE LYS ASP ASP          
SEQRES  31 C  478  THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER GLN          
SEQRES  32 C  478  ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY ASP          
SEQRES  33 C  478  SER TYR THR LEU SER LEU SER GLY ALA SER TYR THR ALA          
SEQRES  34 C  478  GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR VAL          
SEQRES  35 C  478  THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET ALA          
SEQRES  36 C  478  GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS LEU          
SEQRES  37 C  478  ALA GLY SER LYS ILE CYS SER ASP SER SER                      
HET     CA  A 479       1                                                       
HET     CA  B 479       1                                                       
HET     CA  C 479       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   CA    3(CA 2+)                                                     
HELIX    1  H1 GLY A   44  GLN A   53  1HELIX IS BENT AT 49 TO 50         10    
HELIX    2  H2 ASP A   99  ARG A  110  1                                  12    
HELIX    3  H3 VAL A  182  VAL A  195  1                                  14    
HELIX    4  H4 PHE A  215  ALA A  222  1                                   8    
HELIX    5  H5 ALA A  237  TYR A  242  1                                   6    
HELIX    6  H6 PRO A  253  ALA A  261  1                                   9    
HELIX    7  H7 ASP A  270  LYS A  280  1                                  11    
HELIX    8  H8 ILE A  308  LEU A  320  1                                  13    
HELIX    9  H9 GLU A  357  SER A  374  1                                  18    
HELIX   10 H11 GLY B   44  GLN B   53  1HELIX IS BENT AT 49 TO 50         10    
HELIX   11 H12 ASP B   99  ARG B  110  1                                  12    
HELIX   12 H13 VAL B  182  VAL B  195  1                                  14    
HELIX   13 H14 PHE B  215  ALA B  222  1                                   8    
HELIX   14 H15 ALA B  237  TYR B  242  1                                   6    
HELIX   15 H16 PRO B  253  ALA B  261  1                                   9    
HELIX   16 H17 ASP B  270  LYS B  280  1                                  11    
HELIX   17 H18 ILE B  308  LEU B  320  1                                  13    
HELIX   18 H19 GLU B  357  SER B  374  1                                  18    
HELIX   19 H21 GLY C   44  GLN C   53  1HELIX IS BENT AT 49 TO 50         10    
HELIX   20 H22 ASP C   99  ARG C  110  1                                  12    
HELIX   21 H23 VAL C  182  VAL C  195  1                                  14    
HELIX   22 H24 PHE C  215  ALA C  222  1                                   8    
HELIX   23 H25 ALA C  237  TYR C  242  1                                   6    
HELIX   24 H26 PRO C  253  ALA C  261  1                                   9    
HELIX   25 H27 ASP C  270  LYS C  280  1                                  11    
HELIX   26 H28 ILE C  308  LEU C  320  1                                  13    
HELIX   27 H29 GLU C  357  SER C  374  1                                  18    
SHEET    1 BS1 9 SER A  10  LEU A  15  0                                        
SHEET    2 BS1 9 THR A  58  PRO A  64  1                                        
SHEET    3 BS1 9 MET A 112  VAL A 118  1                                        
SHEET    4 BS1 9 GLY A 202  ASP A 206  1                                        
SHEET    5 BS1 9 TYR A 226  VAL A 231  1                                        
SHEET    6 BS1 9 GLY A 248  TYR A 252  1                                        
SHEET    7 BS1 9 LEU A 289  VAL A 293  1                                        
SHEET    8 BS1 9 GLY A 323  ALA A 329  1                                        
SHEET    9 BS1 9 SER A  10  LEU A  15  1                                        
SHEET    1 BS2 3 HIS A 122  GLY A 127  0                                        
SHEET    2 BS2 3 THR A 170  ASP A 175 -1                                        
SHEET    3 BS2 3 TRP A 165  ASN A 169 -1                                        
SHEET    1 BS3 8 ASN A 384  ASP A 390  0                                        
SHEET    2 BS3 8 THR A 392  GLY A 398 -1                                        
SHEET    3 BS3 8 ILE A 404  ASN A 410 -1                                        
SHEET    4 BS3 8 SER A 417  GLY A 424 -1                                        
SHEET    5 BS3 8 GLY A 430  VAL A 436 -1                                        
SHEET    6 BS3 8 THR A 440  GLY A 445 -1                                        
SHEET    7 BS3 8 VAL A 450  GLY A 456 -1                                        
SHEET    8 BS3 8 LEU A 458  THR A 465 -1                                        
SHEET    1 BS4 9 SER B  10  LEU B  15  0                                        
SHEET    2 BS4 9 THR B  58  PRO B  64  1                                        
SHEET    3 BS4 9 MET B 112  VAL B 118  1                                        
SHEET    4 BS4 9 GLY B 202  ASP B 206  1                                        
SHEET    5 BS4 9 TYR B 226  VAL B 231  1                                        
SHEET    6 BS4 9 GLY B 248  TYR B 252  1                                        
SHEET    7 BS4 9 LEU B 289  VAL B 293  1                                        
SHEET    8 BS4 9 GLY B 323  ALA B 329  1                                        
SHEET    9 BS4 9 SER B  10  LEU B  15  1                                        
SHEET    1 BS5 3 HIS B 122  GLY B 127  0                                        
SHEET    2 BS5 3 THR B 170  ASP B 175 -1                                        
SHEET    3 BS5 3 TRP B 165  ASN B 169 -1                                        
SHEET    1 BS6 8 ASN B 384  ASP B 390  0                                        
SHEET    2 BS6 8 THR B 392  GLY B 398 -1                                        
SHEET    3 BS6 8 ILE B 404  ASN B 410 -1                                        
SHEET    4 BS6 8 SER B 417  GLY B 424 -1                                        
SHEET    5 BS6 8 GLY B 430  VAL B 436 -1                                        
SHEET    6 BS6 8 THR B 440  GLY B 445 -1                                        
SHEET    7 BS6 8 VAL B 450  GLY B 456 -1                                        
SHEET    8 BS6 8 LEU B 458  THR B 465 -1                                        
SHEET    1 BS7 9 SER C  10  LEU C  15  0                                        
SHEET    2 BS7 9 THR C  58  PRO C  64  1                                        
SHEET    3 BS7 9 MET C 112  VAL C 118  1                                        
SHEET    4 BS7 9 GLY C 202  ASP C 206  1                                        
SHEET    5 BS7 9 TYR C 226  VAL C 231  1                                        
SHEET    6 BS7 9 GLY C 248  TYR C 252  1                                        
SHEET    7 BS7 9 LEU C 289  VAL C 293  1                                        
SHEET    8 BS7 9 GLY C 323  ALA C 329  1                                        
SHEET    9 BS7 9 SER C  10  LEU C  15  1                                        
SHEET    1 BS8 3 HIS C 122  GLY C 127  0                                        
SHEET    2 BS8 3 THR C 170  ASP C 175 -1                                        
SHEET    3 BS8 3 TRP C 165  ASN C 169 -1                                        
SHEET    1 BS9 8 ASN C 384  ASP C 390  0                                        
SHEET    2 BS9 8 THR C 392  GLY C 398 -1                                        
SHEET    3 BS9 8 ILE C 404  ASN C 410 -1                                        
SHEET    4 BS9 8 SER C 417  GLY C 424 -1                                        
SHEET    5 BS9 8 GLY C 430  VAL C 436 -1                                        
SHEET    6 BS9 8 THR C 440  GLY C 445 -1                                        
SHEET    7 BS9 8 VAL C 450  GLY C 456 -1                                        
SHEET    8 BS9 8 LEU C 458  THR C 465 -1                                        
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  1.79  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  1.88  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.06  
SSBOND   4 CYS A  439    CYS A  474                          1555   1555  2.23  
SSBOND   5 CYS B   30    CYS B   38                          1555   1555  1.79  
SSBOND   6 CYS B  150    CYS B  164                          1555   1555  1.88  
SSBOND   7 CYS B  240    CYS B  283                          1555   1555  2.06  
SSBOND   8 CYS B  439    CYS B  474                          1555   1555  2.23  
SSBOND   9 CYS C   30    CYS C   38                          1555   1555  1.79  
SSBOND  10 CYS C  150    CYS C  164                          1555   1555  1.88  
SSBOND  11 CYS C  240    CYS C  283                          1555   1555  2.06  
SSBOND  12 CYS C  439    CYS C  474                          1555   1555  2.23  
LINK        CA    CA A 479                 OD2 ASP A 175     1555   1555  3.03  
LINK        CA    CA A 479                 OD1 ASN A 121     1555   1555  2.11  
LINK        CA    CA A 479                 OD1 ASP A 175     1555   1555  3.07  
LINK        CA    CA B 479                 OD1 ASN B 121     1555   1555  2.11  
LINK        CA    CA B 479                 OD1 ASP B 175     1555   1555  3.07  
LINK        CA    CA B 479                 OD2 ASP B 175     1555   1555  3.03  
LINK        CA    CA C 479                 OD1 ASN C 121     1555   1555  2.11  
LINK        CA    CA C 479                 OD1 ASP C 175     1555   1555  3.07  
LINK        CA    CA C 479                 OD2 ASP C 175     1555   1555  3.03  
SITE     1 AC1  3 ASN A 121  GLU A 162  ASP A 175                               
SITE     1 AC2  3 ASN B 121  GLU B 162  ASP B 175                               
SITE     1 AC3  3 ASN C 121  GLU C 162  ASP C 175                               
CRYST1   91.900  133.300   94.300  90.00 102.70  90.00 P 1 21 1      6          
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      0.007110  0.000000  0.008600        0.31300                         
SCALE2      0.000000  0.007500  0.000000        0.13700                         
SCALE3     -0.006650  0.000000  0.008600        0.41400                         
MTRIX1   1 -0.537662  0.842761  0.003491      -13.11357    1                    
MTRIX2   1 -0.843195 -0.537874 -0.015704       15.05393    1                    
MTRIX3   1 -0.011223 -0.011613  0.999697       37.58095    1                    
MTRIX1   2  0.494189  0.868623  0.024926      -18.69613    1                    
MTRIX2   2  0.869382 -0.494682  0.002191       40.90763    1                    
MTRIX3   2  0.014088  0.020356 -0.999516        4.56432    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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