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Database: PDB
Entry: 1UA3
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Original site: 1UA3 
HEADER    HYDROLASE                               27-FEB-03   1UA3              
TITLE     CRYSTAL STRUCTURE OF THE PIG PANCREATIC A-AMYLASE COMPLEXED           
TITLE    2 WITH MALTO-OLIGOSACCHARIDES                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 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                                                 
KEYWDS    BETA-ALPHA-BARRELS, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.PAYAN,M.QIAN                                                        
REVDAT   3   04-AUG-09 1UA3    1       FORMUL HET    HETATM HETNAM              
REVDAT   3 2                   1       SITE                                     
REVDAT   2   24-FEB-09 1UA3    1       VERSN                                    
REVDAT   1   14-OCT-03 1UA3    0                                                
JRNL        AUTH   F.PAYAN,M.QIAN                                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE PIG PANCREATIC                      
JRNL        TITL 2 ALPHA-AMYLASE COMPLEXED WITH MALTO-OLIGOSACCHARIDES          
JRNL        REF    J.PROTEIN CHEM.               V.  22   275 2003              
JRNL        REFN                   ISSN 0277-8033                               
JRNL        PMID   12962327                                                     
JRNL        DOI    10.1023/A:1025072520607                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.QIAN,S.SPINELLI,H.DRIGUEZ,F.PAYAN                          
REMARK   1  TITL   STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A           
REMARK   1  TITL 2 SUBSTRATE ANALOGUE AT 2.03 A RESOLUTION                      
REMARK   1  REF    PROTEIN SCI.                  V.   6  2285 1997              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 61298                          
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) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1849                            
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            : 3939                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 129                                     
REMARK   3   SOLVENT ATOMS            : 759                                     
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.85                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.00                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1UA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005605.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU 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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61298                              
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) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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   (%): 63.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, CALSIUM CHLORIDE,       
REMARK 280  PH 8.0, LIQUID DIFFUSION, 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       34.89050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.46200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.59150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.46200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.89050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.59150            
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   1    N                                                   
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   O2   EDO A  2000     C1   EDO A  2001              1.52            
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    GLN A   1   OE1 -  CD  -  NE2 ANGL. DEV. =  17.1 DEGREES          
REMARK 500    GLN A   1   CG  -  CD  -  NE2 ANGL. DEV. = -16.1 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    TYR A  31      -60.65   -143.73                                   
REMARK 500    CYS A  70       93.70   -161.80                                   
REMARK 500    MET A 102     -140.97   -101.14                                   
REMARK 500    VAL A 163       54.20     27.28                                   
REMARK 500    ASP A 317       60.07   -110.03                                   
REMARK 500    SER A 414     -106.23   -132.36                                   
REMARK 500    ASP A 433       35.27    -88.27                                   
REMARK 500    PRO A 486       43.38    -82.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  303     GLY A  304                  137.14                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  20         0.12    SIDE_CHAIN                              
REMARK 500    ARG A 303         0.17    SIDE_CHAIN                              
REMARK 500    ARG A 343         0.11    SIDE_CHAIN                              
REMARK 500    ARG A 392         0.10    SIDE_CHAIN                              
REMARK 500    ARG A 421         0.09    SIDE_CHAIN                              
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 706        DISTANCE = 12.36 ANGSTROMS                       
REMARK 525    HOH A 761        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH A 782        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH A 815        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH A 849        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH A1054        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1213        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH A1298        DISTANCE =  7.00 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EDO A 2001                                                       
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   153.9                                              
REMARK 620 3 ASP A 167   OD1  83.7 120.3                                        
REMARK 620 4 ASP A 167   OD2 127.0  79.0  49.2                                  
REMARK 620 5 HIS A 201   O    71.4  82.9 140.2 160.6                            
REMARK 620 6 HOH A 527   O    99.7  80.9  71.1  87.8  82.6                      
REMARK 620 7 HOH A 520   O    69.7 123.1  75.5  75.3 121.1 145.9                
REMARK 620 8 HOH A 539   O    99.9  72.0 132.6  97.4  83.3 150.8  62.3          
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 BGC A 1997                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL A 1998                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 499                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLR A 1990                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLR A 1994                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2000                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2001                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2002                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
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: 1JFH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A SUBSTRATE ANALOGUE                 
DBREF  1UA3 A    1   496  UNP    P00690   AMYP_PIG         1    496             
SEQADV 1UA3 ASN A  123  UNP  P00690    SER   123 CONFLICT                       
SEQADV 1UA3 LYS A  243  UNP  P00690    GLN   243 CONFLICT                       
SEQADV 1UA3 SER A  310  UNP  P00690    ALA   310 CONFLICT                       
SEQADV 1UA3 ILE A  323  UNP  P00690    VAL   323 CONFLICT                       
SEQADV 1UA3 GLN A  404  UNP  P00690    GLU   404 CONFLICT                       
SEQRES   1 A  496  GLN 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                                                      
HET    BGC  A1997      12                                                       
HET    MAL  A1998      23                                                       
HET     CL  A 498       1                                                       
HET     CL  A 499       1                                                       
HET     CA  A 500       1                                                       
HET    MLR  A1990      34                                                       
HET    MLR  A1994      34                                                       
HET    EDO  A2000       4                                                       
HET    EDO  A2001       3                                                       
HET    EDO  A2002       4                                                       
HET    EDO  A2003       4                                                       
HET    EDO  A2004       4                                                       
HET    EDO  A2005       4                                                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     MAL MALTOSE                                                          
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     MLR MALTOTRIOSE                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     MLR AMYLOTRIOSE                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  BGC    C6 H12 O6                                                    
FORMUL   3  MAL    C12 H22 O11                                                  
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  MLR    2(C18 H32 O16)                                               
FORMUL   9  EDO    6(C2 H6 O2)                                                  
FORMUL  15  HOH   *759(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  ASP A  402  1                                  15    
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  THR A 254   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  PHE A 477   N  SER A 438           
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         OD1 ASN A 100                CA    CA A 500     1555   1555  2.54  
LINK         O   ARG A 158                CA    CA A 500     1555   1555  2.49  
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.65  
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.64  
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.49  
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.62  
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.66  
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.70  
CISPEP   1 ASN A   53    PRO A   54          0        -3.12                     
CISPEP   2 VAL A  129    PRO A  130          0        -6.60                     
SITE     1 AC1  9 LYS A 140  TRP A 203  GLY A 205  ASP A 206                    
SITE     2 AC1  9  CL A 499  HOH A 577  HOH A1027  HOH A1082                    
SITE     3 AC1  9 HOH A1197                                                     
SITE     1 AC2 16 ALA A 318  LYS A 322  THR A 376  THR A 377                    
SITE     2 AC2 16 ARG A 387  TRP A 388  ARG A 389  GLU A 390                    
SITE     3 AC2 16 HOH A 661  HOH A 750  HOH A 967  HOH A1035                    
SITE     4 AC2 16 HOH A1080  HOH A1162  HOH A1198  HOH A1199                    
SITE     1 AC3  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC4  4 TRP A 203  PRO A 204  GLY A 205  BGC A1997                    
SITE     1 AC5  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC5  7 HOH A 520  HOH A 527  HOH A 539                               
SITE     1 AC6 16 TRP A  58  TRP A  59  TYR A  62  GLN A  63                    
SITE     2 AC6 16 HIS A 101  GLY A 104  VAL A 163  ARG A 195                    
SITE     3 AC6 16 ASP A 197  GLU A 233  HIS A 299  ASP A 300                    
SITE     4 AC6 16 HOH A 812  HOH A1092  HOH A1187  HOH A1190                    
SITE     1 AC7 15 THR A  52  ASN A  53  ALA A 108  LYS A 261                    
SITE     2 AC7 15 GLU A 272  TYR A 276  ASN A 279  GLY A 283                    
SITE     3 AC7 15 TRP A 284  HOH A1134  HOH A1146  HOH A1191                    
SITE     4 AC7 15 HOH A1193  HOH A1195  HOH A1282                               
SITE     1 AC8  4 SER A 132  ASP A 135  TYR A 174  EDO A2001                    
SITE     1 AC9  4 ASP A 135  LYS A 172  TYR A 174  EDO A2000                    
SITE     1 BC1  5 THR A 114  CYS A 115  GLY A 116  HOH A1025                    
SITE     2 BC1  5 HOH A1266                                                     
SITE     1 BC2  9 LYS A 213  LEU A 214  HIS A 215  LYS A 466                    
SITE     2 BC2  9 VAL A 467  TYR A 468  HOH A 841  HOH A1307                    
SITE     3 BC2  9 EDO A2004                                                     
SITE     1 BC3  7 LYS A 466  VAL A 467  GLN A 476  PHE A 477                    
SITE     2 BC3  7 SER A 478  HOH A1307  EDO A2003                               
SITE     1 BC4  5 ARG A  30  THR A 376  ARG A 387  HOH A1256                    
SITE     2 BC4  5 HOH A1287                                                     
CRYST1   69.781  113.183  116.924  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      0.014331  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008835  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008553        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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