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Database: PDB
Entry: 7TAA
LinkDB: 7TAA
Original site: 7TAA 
HEADER    HYDROLASE                               06-OCT-97   7TAA              
TITLE     FAMILY 13 ALPHA AMYLASE IN COMPLEX WITH ACARBOSE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TAKA AMYLASE;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062                                                 
KEYWDS    HYDROLASE, GLYCOSYL HYDROLASE, TAKA, AMYLASE, ACARBOSE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.DAVIES,A.M.BRZOZOWSKI                                             
REVDAT   2   24-FEB-09 7TAA    1       VERSN                                    
REVDAT   1   25-NOV-98 7TAA    0                                                
JRNL        AUTH   A.M.BRZOZOWSKI,G.J.DAVIES                                    
JRNL        TITL   STRUCTURE OF THE ASPERGILLUS ORYZAE ALPHA-AMYLASE            
JRNL        TITL 2 COMPLEXED WITH THE INHIBITOR ACARBOSE AT 2.0 A               
JRNL        TITL 3 RESOLUTION.                                                  
JRNL        REF    BIOCHEMISTRY                  V.  36 10837 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9283074                                                      
JRNL        DOI    10.1021/BI970539I                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 31015                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1553                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3688                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 465                                     
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.014 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.033 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.037 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.136 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.176 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.184 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.173 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.300 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 18.300; 20.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.266 ; 4.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.941 ; 6.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.183 ; 6.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.423 ; 8.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7TAA 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        : 1995                               
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : LONG MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63935                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NATIVE STRUCTURE             
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   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% MM PEG 5000, 5MM CALCIUM             
REMARK 280  CHLORIDE, 0.1M HEPES BUFFER, PH 7.5. METHOD: HANGING DROP           
REMARK 280  VAPOUR DIFFUSION. THE NATIVE CRYSTALS WERE SOAKED FOR 6 HOURS       
REMARK 280  IN STABILIZING SOLUTION CONTAINING 15 MM OF ACARBOSE., VAPOR        
REMARK 280  DIFFUSION - HANGING DROP                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.52000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.78000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.59150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.78000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.52000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.59150            
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 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 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     SER A   477                                                      
REMARK 465     SER A   478                                                      
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   O    HOH A   554     O    HOH A   592              1.98            
REMARK 500   O    HOH A   554     O    HOH A   684              2.05            
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   O    HOH A   570     O    HOH A   762     3655     2.09            
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    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TYR A  94   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A  94   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    GLU A 109   OE1 -  CD  -  OE2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    CYS A 283   CA  -  CB  -  SG  ANGL. DEV. =  10.4 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    PHE A  19      -60.68    -92.75                                   
REMARK 500    CYS A  30       84.39   -150.65                                   
REMARK 500    ALA A  78       48.53    -86.23                                   
REMARK 500    TRP A  83       67.45   -115.12                                   
REMARK 500    SER A 141       20.75    -71.72                                   
REMARK 500    ASP A 168     -159.49   -153.23                                   
REMARK 500    THR A 207       44.27     39.79                                   
REMARK 500    ASP A 340      124.91    -37.20                                   
REMARK 500    ALA A 456      149.62   -176.89                                   
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 831        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A 909        DISTANCE =  5.62 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 480  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 210   O                                                      
REMARK 620 2 GLU A 162   O    80.3                                              
REMARK 620 3 ASP A 175   OD2 163.3  83.2                                        
REMARK 620 4 HOH A 505   O    80.7  70.4  91.2                                  
REMARK 620 5 ASN A 121   OD1  77.2 154.9 119.5 116.2                            
REMARK 620 6 ASP A 175   OD1 139.4 116.0  52.4 139.0  76.1                      
REMARK 620 7 HOH A 492   O   116.4 128.3  72.4  65.5  72.7  83.7                
REMARK 620 8 HOH A 507   O    78.2  76.6 100.6 143.2  88.0  70.8 151.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABC A 479                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 480                  
DBREF  7TAA A    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 THR THR ALA TYR GLY ASP ALA          
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN 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 ILE 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 TRP PRO ILE TYR LYS ASP          
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER          
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY          
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR          
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR          
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET          
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS          
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER                      
HET    ABC  A 479      64                                                       
HET     CA  A 480       1                                                       
HETNAM     ABC MODIFIED ACARBOSE HEXASACCHARIDE                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  ABC    C37 H63 N O26                                                
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *465(H2 O)                                                    
HELIX    1   1 PRO A    3  SER A    8  1                                   6    
HELIX    2   2 THR A   16  PHE A   19  1                                   4    
HELIX    3   3 THR A   32  ASP A   34  5                                   3    
HELIX    4   4 TRP A   42  MET A   55  1                                  14    
HELIX    5   5 ALA A   97  ARG A  110  1                                  14    
HELIX    6   6 GLY A  129  SER A  131  5                                   3    
HELIX    7   7 TYR A  134  VAL A  136  5                                   3    
HELIX    8   8 GLN A  143  TYR A  145  5                                   3    
HELIX    9   9 GLN A  158  ASP A  163  1                                   6    
HELIX   10  10 ASP A  181  TYR A  198  1                                  18    
HELIX   11  11 VAL A  208  HIS A  210  5                                   3    
HELIX   12  12 LYS A  213  ALA A  223  1                                  11    
HELIX   13  13 PRO A  236  ASN A  244  1                                   9    
HELIX   14  14 TYR A  252  LYS A  263  1                                  12    
HELIX   15  15 MET A  269  ASP A  282  1                                  14    
HELIX   16  16 SER A  286  LEU A  288  5                                   3    
HELIX   17  17 PHE A  301  TYR A  304  1                                   4    
HELIX   18  18 ILE A  308  LEU A  320  1                                  13    
HELIX   19  19 GLN A  331  GLN A  333  5                                   3    
HELIX   20  20 THR A  347  SER A  350  5                                   4    
HELIX   21  21 GLU A  357  LYS A  375  1                                  19    
HELIX   22  22 GLU A  467  LEU A  469  5                                   3    
SHEET    1   A 6 PRO A 325  TYR A 328  0                                        
SHEET    2   A 6 SER A  10  LEU A  14  1  N  ILE A  11   O  PRO A 325           
SHEET    3   A 6 ALA A  59  ILE A  62  1  N  ALA A  59   O  TYR A  12           
SHEET    4   A 6 TYR A 113  VAL A 118  1  N  TYR A 113   O  ILE A  60           
SHEET    5   A 6 GLY A 202  ILE A 205  1  N  GLY A 202   O  VAL A 116           
SHEET    6   A 6 TYR A 226  GLY A 229  1  N  TYR A 226   O  LEU A 203           
SHEET    1   B 6 THR A 441  THR A 444  0                                        
SHEET    2   B 6 GLN A 433  GLU A 436 -1  N  GLU A 436   O  THR A 441           
SHEET    3   B 6 ARG A 461  PRO A 465 -1  N  TYR A 464   O  THR A 435           
SHEET    4   B 6 ILE A 405  SER A 410 -1  N  ILE A 408   O  ARG A 461           
SHEET    5   B 6 THR A 393  LYS A 398 -1  N  LYS A 398   O  ILE A 405           
SHEET    6   B 6 TRP A 385  ASP A 390 -1  N  ASP A 390   O  THR A 393           
SHEET    1   C 2 TYR A 419  LEU A 423  0                                        
SHEET    2   C 2 VAL A 451  MET A 455 -1  N  MET A 455   O  TYR A 419           
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.05  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.07  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  1.93  
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  1.98  
LINK        CA    CA A 480                 O   HIS A 210     1555   1555  2.54  
LINK        CA    CA A 480                 O   GLU A 162     1555   1555  2.51  
LINK        CA    CA A 480                 OD2 ASP A 175     1555   1555  2.54  
LINK        CA    CA A 480                 O   HOH A 505     1555   1555  2.76  
LINK        CA    CA A 480                 OD1 ASN A 121     1555   1555  2.52  
LINK        CA    CA A 480                 OD1 ASP A 175     1555   1555  2.54  
LINK        CA    CA A 480                 O   HOH A 492     1555   1555  2.41  
LINK        CA    CA A 480                 O   HOH A 507     1555   1555  2.46  
CISPEP   1 LYS A  138    PRO A  139          0         8.63                     
CISPEP   2 ASP A  340    PRO A  341          0         7.94                     
SITE     1 AC1 26 GLN A  35  TYR A  82  TRP A  83  HIS A 122                    
SITE     2 AC1 26 TYR A 155  ARG A 204  ASP A 206  THR A 207                    
SITE     3 AC1 26 LYS A 209  HIS A 210  GLU A 230  LEU A 232                    
SITE     4 AC1 26 ASP A 233  GLY A 234  TYR A 256  HIS A 296                    
SITE     5 AC1 26 ASP A 297  ASP A 340  ARG A 344  HOH A 513                    
SITE     6 AC1 26 HOH A 537  HOH A 563  HOH A 653  HOH A 693                    
SITE     7 AC1 26 HOH A 722  HOH A 751                                          
SITE     1 AC2  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210                    
SITE     2 AC2  7 HOH A 492  HOH A 505  HOH A 507                               
CRYST1   51.040   67.183  133.560  90.00  90.00  90.00 P 21 21 21    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      0.019592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007487        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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