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Database: PDB
Entry: 1PIG
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Original site: 1PIG 
HEADER    GLYCOSYLTRANSFERASE                     15-JUN-96   1PIG              
TITLE     PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE                       
TITLE    2 OLIGOSACCHARIDE V-1532                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-1,4-GLUCAN-4-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 ORGAN: PANCREAS                                                      
KEYWDS    ALPHA-AMYLASE ALPHA-1, 4-GLUCAN-4-GLUCANOHYDROLASE                    
KEYWDS   2 GLYCOSYLTRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MACHIUS,L.VERTESY,R.HUBER,G.WIEGAND                                 
REVDAT   4   08-SEP-09 1PIG    1       HETATM HETNAM                            
REVDAT   3   24-FEB-09 1PIG    1       VERSN                                    
REVDAT   2   01-APR-03 1PIG    1       JRNL                                     
REVDAT   1   07-DEC-96 1PIG    0                                                
JRNL        AUTH   M.MACHIUS,L.VERTESY,R.HUBER,G.WIEGAND                        
JRNL        TITL   CARBOHYDRATE AND PROTEIN-BASED INHIBITORS OF                 
JRNL        TITL 2 PORCINE PANCREATIC ALPHA-AMYLASE: STRUCTURE                  
JRNL        TITL 3 ANALYSIS AND COMPARISON OF THEIR BINDING                     
JRNL        TITL 4 CHARACTERISTICS.                                             
JRNL        REF    J.MOL.BIOL.                   V. 260   409 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8757803                                                      
JRNL        DOI    10.1006/JMBI.1996.0410                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.WIEGAND,O.EPP,R.HUBER                                      
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF PORCINE PANCREATIC                  
REMARK   1  TITL 2 ALPHA-AMYLASE IN COMPLEX WITH THE MICROBIAL                  
REMARK   1  TITL 3 INHIBITOR TENDAMISTAT                                        
REMARK   1  REF    J.MOL.BIOL.                   V. 247    99 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   CARBOHYDRATE BINDING SITES IN A PANCREATIC                   
REMARK   1  TITL 2 ALPHA-AMYLASE-SUBSTRATE COMPLEX, DERIVED FROM X-RAY          
REMARK   1  TITL 3 STRUCTURE ANALYSIS AT 2.1 ANGSTROM RESOLUTION                
REMARK   1  REF    PROTEIN SCI.                  V.   4   747 1995              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   S.B.LARSON,A.GREENWOOD,D.CASCIO,J.DAY,A.MCPHERSON            
REMARK   1  TITL   REFINED MOLECULAR STRUCTURE OF PIG PANCREATIC                
REMARK   1  TITL 2 ALPHA-AMYLASE AT 2.1 A RESOLUTION                            
REMARK   1  REF    J.MOL.BIOL.                   V. 235  1560 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN                      
REMARK   1  TITL   THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE.              
REMARK   1  TITL 2 STRUCTURE OF THE COMPLEX OF A PANCREATIC                     
REMARK   1  TITL 3 ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED          
REMARK   1  TITL 4 TO 2.2-A RESOLUTION                                          
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG              
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION                 
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 44944                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4366                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60                        
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            : 3904                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 125                                     
REMARK   3   SOLVENT ATOMS            : 228                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 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) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20                            
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  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
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 1PIG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 275                                
REMARK 200  PH                             : 6.0-10.0                           
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47260                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.12300                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: 1PIF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION; 10 MICROLITER OF        
REMARK 280  PROTEIN (15 MG/ML IN 0.1 M AMMONIUM CACODYLATE, PH 10.0 0.001       
REMARK 280  M V-1532) WERE STEPWISE CONCENTRATED OVER 0.1, 0.15, AND 0.25       
REMARK 280  M AMMONIUM CACODYLATE, PH 6.0., VAPOR DIFFUSION                     
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       35.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.35000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.35000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.40000            
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TRP A  134   CD1   CD2   NE1   CE2   CE3   CZ2   CZ3             
REMARK 480     TRP A  134   CH2                                                 
REMARK 480     ASN A  350   CB    CG    OD1   ND2                               
REMARK 480     GLU A  352   CD    OE1   OE2                                     
REMARK 480     ASN A  460   CB    CG    OD1   ND2                               
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      -59.22   -138.02                                   
REMARK 500    MET A 102     -150.75   -108.07                                   
REMARK 500    ALA A 133      -39.87    -39.74                                   
REMARK 500    THR A 219       -7.90    -59.95                                   
REMARK 500    ASP A 317       57.91   -111.84                                   
REMARK 500    ASP A 402      119.39    -39.72                                   
REMARK 500    SER A 414     -102.08   -136.01                                   
REMARK 500    ASP A 433       31.29    -95.30                                   
REMARK 500    SER A 437       87.91   -150.97                                   
REMARK 500    PRO A 486       39.22    -73.84                                   
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    TYR A 468         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 TRESTATIN LIKE COMPOUNDS HAVE BEEN ISOLATED FROM                     
REMARK 600 STREPTOMYCES GALBUS CULTURE MEDIUM AND TREATED WITH                  
REMARK 600 ALPHA-AMYLASE FROM BACILLUS SUBTILIS.  FROM THAT MIXTURE,            
REMARK 600 A SUBSTANCE WITH MOLECULAR WEIGHT 1272.5 CONTAINING TWO              
REMARK 600 NITROGEN ATOMS COULD BE ISOLATED.  THE PRELIMINARY                   
REMARK 600 STRUCTURE OF THIS COMPOUND HAS BEEN DETERMINED USING MASS            
REMARK 600 SPECTROMETRY AND FOUND TO COMPRISE 2 CYC, 2 GLA, AND 4 GLC           
REMARK 600 RESIDUES.  THE MOLECULE SEEN IN THE ELECTRON DENSITY HAS             
REMARK 600 THE SEQUENCE GLA-GLC-CYC-GLA-GLC-GLC AND RESULTS FROM                
REMARK 600 PROCESSING OF THE ORIGINAL COMPOUND BY ALPHA-AMYLASE, A              
REMARK 600 PHENOMENON WHICH WAS ALREADY OBSERVED WITH ACARBOSE (SEE             
REMARK 600 REFERENCE 3 FOR DETAILS).                                            
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 ARG A 158   O                                                      
REMARK 620 2 ASN A 100   OD1 154.2                                              
REMARK 620 3 ASP A 167   CG   95.8 106.6                                        
REMARK 620 4 ASP A 167   OD1 111.4  86.1  25.4                                  
REMARK 620 5 ASP A 167   OD2  77.2 127.9  25.4  50.7                            
REMARK 620 6 HIS A 201   O    85.3  69.5 162.6 139.4 162.5                      
REMARK 620 7 HOH A2095   O   130.8  68.2  77.2  82.5  77.5 115.1                
REMARK 620 8 HOH A2094   O    75.9 104.6 115.5 137.2  93.9  81.7  64.6          
REMARK 620 9 HOH A2102   O    71.2 101.1  77.5  66.3  87.7  86.5 148.0 145.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AS                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE RESIDUES.                     
REMARK 800 SITE_IDENTIFIER: CA                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.                              
REMARK 800 SITE_IDENTIFIER: CL                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CHLORIDE BINDING SITE.                             
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGL A 701                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 702                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMC A 703                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGL A 704                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 705                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 706                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 801                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 802                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 901                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 902                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1002                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 600                  
DBREF  1PIG A    2   496  UNP    P00690   AMYP_PIG         2    496             
SEQADV 1PIG VAL A   49  UNP  P00690    ILE    49 CONFLICT                       
SEQADV 1PIG SER A  243  UNP  P00690    GLN   243 CONFLICT                       
SEQADV 1PIG SER A  310  UNP  P00690    ALA   310 CONFLICT                       
SEQADV 1PIG GLN A  404  UNP  P00690    GLU   404 CONFLICT                       
SEQADV 1PIG ASN A  451  UNP  P00690    ASP   451 CONFLICT                       
SEQADV 1PIG GLN A  484  UNP  P00690    GLU   484 CONFLICT                       
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL VAL VAL THR          
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 A  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE SER 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 VAL ALA VAL          
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASN 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 GLN ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 A  496  LYS LEU                                                      
MODRES 1PIG PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    AGL  A 701      10                                                       
HET    GLC  A 702      11                                                       
HET    HMC  A 703      11                                                       
HET    AGL  A 704      10                                                       
HET    GLC  A 705      11                                                       
HET    BGC  A 706      12                                                       
HET    GLC  A 801      11                                                       
HET    GLC  A 802      12                                                       
HET    BGC  A 901      11                                                       
HET    GLC  A 902      12                                                       
HET    BGC  A1002      12                                                       
HET     CA  A 500       1                                                       
HET     CL  A 600       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     AGL 4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE                              
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     HMC 5-HYDROXYMETHYL-CHONDURITOL                                      
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  AGL    2(C6 H13 N O4)                                               
FORMUL   2  GLC    5(C6 H12 O6)                                                 
FORMUL   3  HMC    C7 H12 O5                                                    
FORMUL   4  BGC    3(C6 H12 O6)                                                 
FORMUL   8   CA    CA 2+                                                        
FORMUL   9   CL    CL 1-                                                        
FORMUL  10  HOH   *228(H2 O)                                                    
HELIX    1   1 TRP A   21  ARG A   30  1                                  10    
HELIX    2   2 TRP A   58  TYR A   62  5                                   5    
HELIX    3   3 GLU A   76  VAL A   89  1                                  14    
HELIX    4   4 PRO A  121  SER A  123  5                                   3    
HELIX    5   5 ALA A  133  ASP A  135  5                                   3    
HELIX    6   6 PRO A  154  ASP A  159  1                                   6    
HELIX    7   7 ASP A  173  ILE A  189  1                                  17    
HELIX    8   8 SER A  199  HIS A  201  5                                   3    
HELIX    9   9 PRO A  204  LYS A  213  1                                  10    
HELIX   10  10 SER A  244  TYR A  247  5                                   4    
HELIX   11  11 PHE A  256  ARG A  267  1                                  12    
HELIX   12  12 MET A  274  ASN A  279  5                                   6    
HELIX   13  13 GLU A  282  TRP A  284  5                                   3    
HELIX   14  14 SER A  289  ARG A  291  5                                   3    
HELIX   15  15 ASN A  301  ARG A  303  5                                   3    
HELIX   16  16 GLY A  309  SER A  311  5                                   3    
HELIX   17  17 PHE A  315  ALA A  330  5                                  16    
HELIX   18  18 GLU A  385  ARG A  387  5                                   3    
HELIX   19  19 ARG A  389  VAL A  401  1                                  13    
HELIX   20  20 ALA A  492  SER A  494  5                                   3    
SHEET    1   A 6 THR A 336  SER A 340  0                                        
SHEET    2   A 6 SER A  12  LEU A  16  1  N  ILE A  13   O  THR A 336           
SHEET    3   A 6 GLY A  39  VAL A  42  1  N  GLY A  39   O  VAL A  14           
SHEET    4   A 6 ARG A  92  ALA A  97  1  N  ARG A  92   O  VAL A  40           
SHEET    5   A 6 GLY A 193  ILE A 196  1  N  GLY A 193   O  VAL A  95           
SHEET    6   A 6 PHE A 229  GLN A 232  1  N  PHE A 229   O  PHE A 194           
SHEET    1   B 3 GLN A 416  ARG A 421  0                                        
SHEET    2   B 3 GLY A 425  ASN A 430 -1  N  PHE A 429   O  VAL A 417           
SHEET    3   B 3 PHE A 487  HIS A 491 -1  N  ILE A 490   O  PHE A 426           
SHEET    1   C 2 LEU A 436  GLN A 441  0                                        
SHEET    2   C 2 THR A 474  ILE A 479 -1  N  ILE A 479   O  LEU A 436           
SHEET    1   D 2 GLY A 447  CYS A 450  0                                        
SHEET    2   D 2 LYS A 466  VAL A 469 -1  N  VAL A 469   O  GLY A 447           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.03  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33  
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  2.36  
LINK         C1  AGL A 701                 O4  GLC A 702     1555   1555  1.41  
LINK         C1  GLC A 702                 O4  HMC A 703     1555   1555  1.41  
LINK         C1  HMC A 703                 N4  AGL A 704     1555   1555  1.47  
LINK         C1  AGL A 704                 O4  GLC A 705     1555   1555  1.40  
LINK         C1  GLC A 801                 O4  GLC A 802     1555   1555  1.40  
LINK         C1  BGC A 901                 O4  GLC A 902     1555   1555  1.39  
LINK         OD1 ASN A 100                CA    CA A 500     1555   1555  2.45  
LINK         CG  ASP A 167                CA    CA A 500     1555   1555  2.89  
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.51  
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.58  
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.41  
LINK        CA    CA A 500                 O   HOH A2095     1555   1555  2.43  
LINK        CA    CA A 500                 O   HOH A2094     1555   1555  2.50  
LINK        CA    CA A 500                 O   HOH A2102     1555   1555  2.58  
LINK         C1  GLC A 705                 O4  BGC A 706     1555   1555  1.40  
CISPEP   1 ASN A   53    PRO A   54          0        -0.30                     
CISPEP   2 VAL A  129    PRO A  130          0         0.04                     
SITE     1  AS  3 ASP A 197  GLU A 233  ASP A 300                               
SITE     1  CA  4 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     1  CL  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC1  6 TRP A  59  GLN A  63  VAL A 163  GLC A 702                    
SITE     2 AC1  6 HOH A2205  HOH A2208                                          
SITE     1 AC2  8 TRP A  58  TRP A  59  TYR A  62  GLN A  63                    
SITE     2 AC2  8 HIS A 305  AGL A 701  HMC A 703  AGL A 704                    
SITE     1 AC3  9 TRP A  58  TYR A  62  HIS A 101  ASP A 197                    
SITE     2 AC3  9 GLU A 233  HIS A 299  ASP A 300  GLC A 702                    
SITE     3 AC3  9 AGL A 704                                                     
SITE     1 AC4  8 ALA A 198  HIS A 201  GLU A 233  ASP A 300                    
SITE     2 AC4  8 GLC A 702  HMC A 703  GLC A 705  HOH A2087                    
SITE     1 AC5  6 TYR A 151  LYS A 200  ILE A 235  GLU A 240                    
SITE     2 AC5  6 AGL A 704  BGC A 706                                          
SITE     1 AC6  8 LEU A 237  GLU A 240  GLY A 306  ASN A 362                    
SITE     2 AC6  8 ASN A 363  ASN A 364  GLC A 705  HOH A2183                    
SITE     1 AC7  6 THR A 376  ARG A 387  TRP A 388  ARG A 389                    
SITE     2 AC7  6 GLU A 390  GLC A 802                                          
SITE     1 AC8  6 ALA A 318  LYS A 322  TRP A 388  GLU A 390                    
SITE     2 AC8  6 GLC A 801  HOH A2165                                          
SITE     1 AC9  7 THR A  52  ASN A  53  LYS A 261  GLY A 283                    
SITE     2 AC9  7 TRP A 284  GLC A 902  HOH A4003                               
SITE     1 BC1  9 THR A  52  GLU A 272  ASN A 279  TRP A 284                    
SITE     2 BC1  9 BGC A 901  HOH A2218  HOH A4004  HOH A4005                    
SITE     3 BC1  9 HOH A4006                                                     
SITE     1 BC2 11 ASP A 181  ASN A 184  LYS A 185  ASP A 188                    
SITE     2 BC2 11 HIS A 215  THR A 439  TYR A 468  SER A 470                    
SITE     3 BC2 11 THR A 474  ALA A 475  HOH A2121                               
SITE     1 BC3  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 BC3  7 HOH A2094  HOH A2095  HOH A2102                               
SITE     1 BC4  3 ARG A 195  ASN A 298  ARG A 337                               
CRYST1   70.500  114.800  118.700  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      0.014184  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008711  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008425        0.00000                         
HETATM    1  N   PCA A   1      40.881  12.650  34.096  1.00 39.67           N  
HETATM    2  CA  PCA A   1      40.558  13.344  35.344  1.00 35.81           C  
HETATM    3  CB  PCA A   1      41.321  12.588  36.432  1.00 36.73           C  
HETATM    4  CG  PCA A   1      42.510  12.105  35.629  1.00 39.27           C  
HETATM    5  CD  PCA A   1      41.992  11.931  34.217  1.00 44.13           C  
HETATM    6  OE  PCA A   1      42.181  11.388  33.124  1.00 50.73           O  
HETATM    7  C   PCA A   1      40.787  14.838  35.457  1.00 33.67           C  
HETATM    8  O   PCA A   1      40.277  15.448  36.392  1.00 33.98           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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