GenomeNet

Database: PDB
Entry: 1WO2
LinkDB: 1WO2
Original site: 1WO2 
HEADER    HYDROLASE                               11-AUG-04   1WO2              
TITLE     CRYSTAL STRUCTURE OF THE PIG PANCREATIC ALPHA-AMYLASE                 
TITLE    2 COMPLEXED WITH MALTO-OLIGOSAACHARIDES UNDER THE EFFECT OF            
TITLE    3 THE CHLORIDE ION                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                        
COMPND   5 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 TISSUE: PANCREAS                                                     
KEYWDS    BETA-ALPHA-BARRELS, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.QIAN,F.PAYAN,V.NAHOUM                                               
REVDAT   3   04-AUG-09 1WO2    1       HETATM HETNAM                            
REVDAT   2   24-FEB-09 1WO2    1       VERSN                                    
REVDAT   1   15-MAR-05 1WO2    0                                                
JRNL        AUTH   M.QIAN,E.H.AJANDOUZ,F.PAYAN,V.NAHOUM                         
JRNL        TITL   MOLECULAR BASIS OF THE EFFECTS OF CHLORIDE ION ON            
JRNL        TITL 2 THE ACID-BASE CATALYST IN THE MECHANISM OF                   
JRNL        TITL 3 PANCREATIC ALPHA-AMYLASE                                     
JRNL        REF    BIOCHEMISTRY                  V.  44  3194 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15736930                                                     
JRNL        DOI    10.1021/BI048201T                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.QIAN,V.NAHOUM,J.BONICEL,H.BISCHOFF,B.HENRISSAT,            
REMARK   1  AUTH 2 F.PAYAN                                                      
REMARK   1  TITL   ENZYME-CATALYZED CONDENSATION REACTION IN A                  
REMARK   1  TITL 2 MAMMALIAN ALPHA-AMYLASE. HIGH-RESOLUTION STRUCTURAL          
REMARK   1  TITL 3 ANALYSIS OF AN ENZYME-INHIBITOR COMPLEX                      
REMARK   1  REF    BIOCHEMISTRY                  V.  40  7700 2001              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   11412124                                                     
REMARK   1  DOI    10.1021/BI0102050                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.PAYAN,M.QIAN                                               
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE PIG PANCREATIC                      
REMARK   1  TITL 2 ALPHA-AMYLASE COMPLEXED WITH MALTO-OLIGOSACCHARIDES          
REMARK   1  REF    J.PROTEIN CHEM.               V.  22   275 2003              
REMARK   1  REFN                   ISSN 0277-8033                               
REMARK   1  PMID   12962327                                                     
REMARK   1  DOI    10.1023/A:1025072520607                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 61363                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2479                            
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            : 3956                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 117                                     
REMARK   3   SOLVENT ATOMS            : 749                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.30                          
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.38                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.25                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 1WO2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-AUG-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023800.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61363                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, CALCIUM CHLORIDE, SODIUM           
REMARK 280  CHLORIDE, PH 8, EVAPORATION, TEMPERATURE 277K                       
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       35.04500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.61050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.64900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.61050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.04500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.64900            
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 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    TYR A  31      -60.94   -140.14                                   
REMARK 500    MET A 102     -143.59   -110.85                                   
REMARK 500    ASP A 317       55.47   -118.13                                   
REMARK 500    SER A 414     -104.79   -133.69                                   
REMARK 500    ASP A 433       35.16    -88.92                                   
REMARK 500    PRO A 486       42.84    -73.96                                   
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 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: (11X,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     TRP A  59        25.0      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 A1199        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1409        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A1433        DISTANCE =  6.24 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 ARG A 158   O   151.9                                              
REMARK 620 3 ASP A 167   OD1  84.0 121.3                                        
REMARK 620 4 ASP A 167   OD2 128.8  79.3  51.8                                  
REMARK 620 5 HIS A 201   O    71.1  81.1 138.8 159.6                            
REMARK 620 6 HOH A 520   O    71.1 123.8  75.4  73.3 123.2                      
REMARK 620 7 HOH A 539   O    97.7  73.2 135.6  98.1  81.4  63.7                
REMARK 620 8 HOH A 527   O   100.9  78.5  71.7  89.6  81.1 146.8 148.7          
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 GLC A 1990                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1991                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1992                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1994                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1995                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1996                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1998                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1999                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2000                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2001                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2002                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2005                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HX0   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH THE "TRUNCATE" ACARBOSE              
REMARK 900 MOLECULE (PSEUDOTRISACCHARIDE)                                       
REMARK 900 RELATED ID: 1UA3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MALTO-OLIGOSACCHARIDES               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THESE CONFLICTS ARE EXPLAINED IN REFERENCE AS FOLLOWING,             
REMARK 999 M.QIAN,R.HASER,F.PAYAN                                               
REMARK 999 STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG                      
REMARK 999 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION                         
REMARK 999 (J.MOL.BIOL. V. 231 785 1993)                                        
DBREF  1WO2 A    1   496  UNP    P00690   AMYP_PIG        16    511             
SEQADV 1WO2 PCA A    1  UNP  P00690    GLN    16 ENGINEERED                     
SEQADV 1WO2 LYS A  243  UNP  P00690    GLN   258 SEE REMARK 999                 
SEQADV 1WO2 SER A  310  UNP  P00690    ALA   325 SEE REMARK 999                 
SEQADV 1WO2 ILE A  323  UNP  P00690    VAL   338 SEE REMARK 999                 
SEQADV 1WO2 GLU A  352  UNP  P00690    GLN   367 SEE REMARK 999                 
SEQADV 1WO2 GLU A  390  UNP  P00690    GLN   405 SEE REMARK 999                 
SEQADV 1WO2 ASP A  411  UNP  P00690    ALA   426 SEE REMARK 999                 
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 ILE 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 ASN 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 LYS 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 SER SER ILE          
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE 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                                                      
MODRES 1WO2 PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    GLC  A1990      11                                                       
HET    GLC  A1991      11                                                       
HET    BGC  A1992      12                                                       
HET    GLC  A1994      11                                                       
HET    GLC  A1995      11                                                       
HET    BGC  A1996      12                                                       
HET    GLC  A1998      11                                                       
HET    BGC  A1999      12                                                       
HET     CL  A 498       1                                                       
HET     CA  A 500       1                                                       
HET    EDO  A2000       4                                                       
HET    EDO  A2001       4                                                       
HET    EDO  A2002       4                                                       
HET    EDO  A2003       4                                                       
HET    EDO  A2004       4                                                       
HET    EDO  A2005       4                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  GLC    5(C6 H12 O6)                                                 
FORMUL   2  BGC    3(C6 H12 O6)                                                 
FORMUL   5   CL    CL 1-                                                        
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  EDO    6(C2 H6 O2)                                                  
FORMUL  13  HOH   *749(H2 O)                                                    
HELIX    1   1 ARG A   20  TYR A   31  1                                  12    
HELIX    2   2 PRO A   57  GLN A   63  5                                   7    
HELIX    3   3 ASN A   75  VAL A   89  1                                  15    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   5 SER A  132  PHE A  136  5                                   5    
HELIX    6   6 ASP A  153  CYS A  160  1                                   8    
HELIX    7   7 LYS A  172  GLY A  190  1                                  19    
HELIX    8   8 ALA A  198  MET A  202  5                                   5    
HELIX    9   9 TRP A  203  ASP A  212  1                                  10    
HELIX   10  10 LYS A  243  PHE A  248  5                                   6    
HELIX   11  11 PHE A  256  ARG A  267  1                                  12    
HELIX   12  12 LYS A  273  TRP A  280  5                                   8    
HELIX   13  13 GLY A  281  GLY A  285  5                                   5    
HELIX   14  14 PRO A  288  ASP A  290  5                                   3    
HELIX   15  15 ASP A  300  GLY A  304  5                                   5    
HELIX   16  16 GLY A  308  ILE A  312  5                                   5    
HELIX   17  17 THR A  314  TRP A  316  5                                   3    
HELIX   18  18 ASP A  317  HIS A  331  1                                  15    
HELIX   19  19 CYS A  384  ARG A  387  5                                   4    
HELIX   20  20 TRP A  388  VAL A  401  1                                  14    
HELIX   21  21 GLU A  493  LYS A  495  5                                   3    
SHEET    1   A 9 SER A  12  LEU A  16  0                                        
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLN A  41   N  VAL A  14           
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40           
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  ARG A 195   N  ALA A  97           
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 229   N  PHE A 194           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  GLN A 232           
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  LEU A 293   N  VAL A 253           
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294           
SHEET    9   A 9 SER A  12  LEU A  16  1  N  ILE A  13   O  VAL A 338           
SHEET    1   B 2 HIS A 101  GLY A 104  0                                        
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  CYS A 103           
SHEET    1   C 2 PHE A 348  VAL A 349  0                                        
SHEET    2   C 2 GLU A 352  ASP A 353 -1  O  GLU A 352   N  VAL A 349           
SHEET    1   D 2 ASN A 362  ASN A 363  0                                        
SHEET    2   D 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363           
SHEET    1   E 4 PHE A 406  ASP A 411  0                                        
SHEET    2   E 4 GLN A 416  ARG A 421 -1  O  GLY A 420   N  ALA A 407           
SHEET    3   E 4 GLY A 425  ASN A 430 -1  O  PHE A 429   N  VAL A 417           
SHEET    4   E 4 PHE A 487  HIS A 491 -1  O  ILE A 488   N  VAL A 428           
SHEET    1   F 2 LEU A 436  GLN A 441  0                                        
SHEET    2   F 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440           
SHEET    1   G 2 GLY A 447  CYS A 450  0                                        
SHEET    2   G 2 LYS A 466  VAL A 469 -1  O  VAL A 469   N  GLY A 447           
SHEET    1   H 2 LYS A 457  VAL A 458  0                                        
SHEET    2   H 2 SER A 461  CYS A 462 -1  O  SER A 461   N  VAL A 458           
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  2.04  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.03  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.34  
LINK         OD1 ASN A 100                CA    CA A 500     1555   1555  2.43  
LINK         O   ARG A 158                CA    CA A 500     1555   1555  2.37  
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.53  
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.49  
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.39  
LINK         C1  GLC A1990                 O4  GLC A1991     1555   1555  1.40  
LINK         C1  GLC A1991                 O4  BGC A1992     1555   1555  1.41  
LINK         C1  GLC A1994                 O4  GLC A1995     1555   1555  1.40  
LINK         C1  GLC A1995                 O4  BGC A1996     1555   1555  1.40  
LINK         C1  GLC A1998                 O4  BGC A1999     1555   1555  1.41  
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.61  
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.59  
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.45  
CISPEP   1 ASN A   53    PRO A   54          0        -0.08                     
CISPEP   2 VAL A  129    PRO A  130          0        -0.66                     
SITE     1 AC1  6 GLN A  63  VAL A 163  HOH A1207  HOH A1218                    
SITE     2 AC1  6 GLC A1991  EDO A2002                                          
SITE     1 AC2  9 TRP A  58  TRP A  59  TYR A  62  GLN A  63                    
SITE     2 AC2  9 ASP A 300  HOH A1159  HOH A1160  GLC A1990                    
SITE     3 AC2  9 BGC A1992                                                     
SITE     1 AC3 12 TRP A  58  TYR A  62  HIS A 101  ARG A 195                    
SITE     2 AC3 12 ASP A 197  ALA A 198  GLU A 233  HIS A 299                    
SITE     3 AC3 12 ASP A 300  HOH A1163  HOH A1267  GLC A1991                    
SITE     1 AC4  7 THR A  52  ASN A  53  LYS A 261  GLY A 283                    
SITE     2 AC4  7 TRP A 284  HOH A 743  GLC A1995                               
SITE     1 AC5  7 THR A  52  GLU A 272  TYR A 276  ASN A 279                    
SITE     2 AC5  7 HOH A1170  GLC A1994  BGC A1996                               
SITE     1 AC6  9 ALA A 108  TYR A 276  HOH A 879  HOH A1040                    
SITE     2 AC6  9 HOH A1051  HOH A1170  HOH A1213  HOH A1216                    
SITE     3 AC6  9 GLC A1995                                                     
SITE     1 AC7 10 ASP A 375  THR A 376  ARG A 387  TRP A 388                    
SITE     2 AC7 10 ARG A 389  GLU A 390  ARG A 392  HOH A 950                    
SITE     3 AC7 10 HOH A1138  BGC A1999                                          
SITE     1 AC8  8 ALA A 318  LYS A 322  TRP A 388  GLU A 390                    
SITE     2 AC8  8 HOH A 661  HOH A1430  HOH A1509  GLC A1998                    
SITE     1 AC9  5 ARG A 195  GLU A 233  ASN A 298  ARG A 337                    
SITE     2 AC9  5 HOH A 525                                                     
SITE     1 BC1  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 BC1  7 HOH A 520  HOH A 527  HOH A 539                               
SITE     1 BC2  8 LYS A 213  LEU A 214  HIS A 215  LYS A 466                    
SITE     2 BC2  8 VAL A 467  TYR A 468  HOH A 717  EDO A2001                    
SITE     1 BC3  6 VAL A 467  GLN A 476  PHE A 477  SER A 478                    
SITE     2 BC3  6 HOH A1146  EDO A2000                                          
SITE     1 BC4  5 TRP A  59  GLN A  63  HOH A 877  HOH A1208                    
SITE     2 BC4  5 GLC A1990                                                     
SITE     1 BC5  6 ARG A  30  ILE A 372  THR A 376  ARG A 387                    
SITE     2 BC5  6 HOH A 872  HOH A1007                                          
SITE     1 BC6  6 PCA A   1  LEU A 211  ARG A 227  PRO A 228                    
SITE     2 BC6  6 ILE A 230  HOH A 939                                          
SITE     1 BC7  5 ARG A  56  THR A 114  HOH A 654  HOH A1225                    
SITE     2 BC7  5 HOH A1230                                                     
CRYST1   70.090  113.298  117.221  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      0.014267  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008826  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008531        0.00000                         
HETATM    1  N   PCA A   1      41.308  12.289  33.973  1.00 21.28           N  
HETATM    2  CA  PCA A   1      40.384  12.678  35.037  1.00 19.66           C  
HETATM    3  CB  PCA A   1      40.976  11.870  36.129  1.00 20.61           C  
HETATM    4  CG  PCA A   1      41.403  10.656  35.233  1.00 29.11           C  
HETATM    5  CD  PCA A   1      41.998  11.155  33.854  1.00 21.10           C  
HETATM    6  OE  PCA A   1      42.795  10.472  33.215  1.00 25.24           O  
HETATM    7  C   PCA A   1      40.416  14.201  35.058  1.00 15.31           C  
HETATM    8  O   PCA A   1      39.738  14.845  35.856  1.00 12.41           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system