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Database: PDB
Entry: 1BVN
LinkDB: 1BVN
Original site: 1BVN 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           16-SEP-98   1BVN              
TITLE     PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE                      
TITLE    2 PROTEINACEOUS INHIBITOR TENDAMISTAT                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (ALPHA-AMYLASE);                                   
COMPND   3 CHAIN: P;                                                            
COMPND   4 SYNONYM: 1,4-GLUCAN-4-GLUCANOHYDROLASE,                              
COMPND   5 GLYCOSYLTRANSFERASE;                                                 
COMPND   6 EC: 3.2.1.1;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN (TENDAMISTAT);                                     
COMPND   9 CHAIN: T                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: STREPTOMYCES TENDAE;                            
SOURCE   8 ORGANISM_TAXID: 1932;                                                
SOURCE   9 STRAIN: 4158                                                         
KEYWDS    GLYCOSYLTRANSFERASE, ALPHA-1, 4-GLUCAN-4-GLUCANOHYDROLASE,            
KEYWDS   2 ALPHA-AMYLASE, PROTEINACEOUS ALPHA-AMYLASE INHIBITOR,                
KEYWDS   3 HYDROLASE/HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MACHIUS,G.WIEGAND,O.EPP,R.HUBER                                     
REVDAT   3   24-FEB-09 1BVN    1       VERSN                                    
REVDAT   2   29-DEC-99 1BVN    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   23-SEP-98 1BVN    0                                                
JRNL        AUTH   G.WIEGAND,O.EPP,R.HUBER                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF PORCINE PANCREATIC                  
JRNL        TITL 2 ALPHA-AMYLASE IN COMPLEX WITH THE MICROBIAL                  
JRNL        TITL 3 INHIBITOR TENDAMISTAT.                                       
JRNL        REF    J.MOL.BIOL.                   V. 247    99 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7897663                                                      
JRNL        DOI    10.1006/JMBI.1994.0125                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.MACHIUS,L.VERTESY,R.HUBER,G.WIEGAND                        
REMARK   1  TITL   CARBOHYDRATE AND PROTEIN-BASED INHIBITORS OF                 
REMARK   1  TITL 2 PORCINE PANCREATIC ALPHA-AMYLASE: STRUCTURE                  
REMARK   1  TITL 3 ANALYSIS AND COMPARISON OF THEIR BINDING                     
REMARK   1  TITL 4 CHARACTERISTICS                                              
REMARK   1  REF    J.MOL.BIOL.                   V. 260   409 1996              
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                
REMARK   1  TITL 3 X-RAY 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                  
REMARK   1  TITL 4 REFINED 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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 73.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 17259                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1889                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1059                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 134                          
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            : 4443                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 161                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.60                          
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) : 0.25                            
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.49                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.51                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.71                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.500 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TIP3P.PARAMETER                                
REMARK   3  PARAMETER FILE  3  : PARAMETER.ELEMENTS                             
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TIP3P.TOPOLOGY                                 
REMARK   3  TOPOLOGY FILE  3   : TOPOLOGY.ELEMENTS                              
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FINAL RMS COORD. SHIFT 0.0 ANGSTROMS      
REMARK   4                                                                      
REMARK   4 1BVN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008332.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 275                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NI-FILTER, DOUBLE-FOCUSING         
REMARK 200                                   MIRROR SYSTEM                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : FILM                               
REMARK 200  DETECTOR MANUFACTURER          : KODAK                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : FILME                              
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19789                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.06020                            
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) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 42.4                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: PROTEIN                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 12 MG/ML IN 50 MM TRIS/         
REMARK 280  HCL, PH 8.0, MIXED 5:1 WITH 40% (W/V) PEG 1000; RESERVOIR:          
REMARK 280  0.18-0.20 M SODIUM PHOSPHATE, PH 8.0 HARVESTED IN: 3 M SODIUM       
REMARK 280  ACETATE, PH 7.5                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      239.66667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      119.83333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      179.75000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.91667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      299.58333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      239.66667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      119.83333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       59.91667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      179.75000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      299.58333            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, T                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP T   801                                                      
REMARK 465     THR T   802                                                      
REMARK 465     THR T   803                                                      
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 P  31      -60.81   -131.98                                   
REMARK 500    SER P  55       77.09     86.30                                   
REMARK 500    MET P 102     -150.52   -109.30                                   
REMARK 500    CYS P 103     -169.26    -70.69                                   
REMARK 500    THR P 111      -62.10     52.91                                   
REMARK 500    VAL P 163       38.04     35.44                                   
REMARK 500    LEU P 170        8.19    -60.57                                   
REMARK 500    SER P 270       60.39     39.80                                   
REMARK 500    TRP P 280      144.25    -23.41                                   
REMARK 500    ASP P 290        4.37    -63.97                                   
REMARK 500    ASP P 297      -91.86    -82.39                                   
REMARK 500    ASN P 298      142.75     79.33                                   
REMARK 500    HIS P 305       35.68    -83.02                                   
REMARK 500    ALA P 307       93.05    -67.35                                   
REMARK 500    ALA P 318      -48.57    -21.60                                   
REMARK 500    ARG P 319      -74.46    -56.87                                   
REMARK 500    SER P 341     -166.75   -126.05                                   
REMARK 500    ALA P 345       97.69    -69.75                                   
REMARK 500    ASN P 347       97.63   -166.32                                   
REMARK 500    VAL P 354       -3.29    -59.13                                   
REMARK 500    ASN P 364       69.82     60.56                                   
REMARK 500    THR P 376      -20.85     93.85                                   
REMARK 500    ASP P 402      107.60    -42.93                                   
REMARK 500    ASP P 411      139.78   -171.56                                   
REMARK 500    SER P 414     -102.22   -127.07                                   
REMARK 500    PHE P 419      148.78   -174.81                                   
REMARK 500    SER P 437      119.85   -170.99                                   
REMARK 500    SER P 438      166.71    179.55                                   
REMARK 500    PRO P 486       37.38    -64.71                                   
REMARK 500    ASP T 840       -3.18     87.97                                   
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 ASN P   53     PRO P   54                   32.05                    
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 P   2         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 P2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN P 100   OD1                                                    
REMARK 620 2 ARG P 158   O   146.7                                              
REMARK 620 3 ASP P 167   OD1  85.6  95.5                                        
REMARK 620 4 ASP P 167   OD2 127.2  74.7  50.2                                  
REMARK 620 5 HIS P 201   O    81.9  71.5 128.9 145.9                            
REMARK 620 6 HOH P1152   O    94.2  60.5  56.0  83.9  75.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AS                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE RESIDUES.                     
REMARK 800 SITE_IDENTIFIER: CA                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.                              
REMARK 800 SITE_IDENTIFIER: CL                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
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 CA P 2001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL P 2002                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE DISCREPANCIES ARE DESCRIBED IN THE CITED                
REMARK 999 REFERENCES                                                           
REMARK 999                                                                      
REMARK 999 GLN1: THIS RESIDUE IS REPORTED TO BE PYROGLUTAMATE IN OTHER          
REMARK 999  STRUCTURES OF PIG PANCREATIC AND SIMILAR ALPHA-AMYLASES.            
REMARK 999  ALTHOUGH AMINO ACID SEQUENCING INDICATED THAT THE                   
REMARK 999  N-TERMINUS WAS BLOCKED IN THE MATERIAL WHICH WAS USED FOR           
REMARK 999  CRYSTALLIZATION IN THE PRESENTED STUDY, THE QUALITY OF THE          
REMARK 999  ELECTRON DENSITY DID NOT ALLOW TO UNAMBIGOUSLY IDENTIFY             
REMARK 999  THE NATURE OF THIS RESIDUE.                                         
DBREF  1BVN P    1   496  UNP    P00690   AMYP_PIG         1    496             
DBREF  1BVN T  801   874  UNP    P01092   IAA_STRTE       31    104             
SEQADV 1BVN ASP P   12  UNP  P00690    SER    12 CONFLICT                       
SEQADV 1BVN VAL P   49  UNP  P00690    ILE    49 CONFLICT                       
SEQADV 1BVN LEU P  196  UNP  P00690    ILE   196 CONFLICT                       
SEQADV 1BVN SER P  243  UNP  P00690    GLN   243 CONFLICT                       
SEQADV 1BVN SER P  310  UNP  P00690    ALA   310 CONFLICT                       
SEQADV 1BVN GLN P  404  UNP  P00690    GLU   404 CONFLICT                       
SEQADV 1BVN ASN P  451  UNP  P00690    ASP   451 CONFLICT                       
SEQADV 1BVN GLN P  484  UNP  P00690    GLU   484 CONFLICT                       
SEQADV 1BVN GLU T  829  UNP  P01092    GLN    59 CONFLICT                       
SEQRES   1 P  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR ASP ILE          
SEQRES   2 P  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 P  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 P  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL VAL VAL THR          
SEQRES   5 P  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 P  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 P  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 P  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 P  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 P  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 P  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 P  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 P  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 P  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 P  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 P  496  LEU ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 P  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 P  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 P  496  ILE ASP LEU GLY GLY GLU ALA ILE SER SER SER GLU TYR          
SEQRES  20 P  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 P  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 P  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 P  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 P  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 P  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS VAL ALA VAL          
SEQRES  26 P  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 P  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 P  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 P  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 P  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 P  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 P  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 P  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 P  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 P  496  GLY LEU PRO GLY GLY THR TYR CYS ASN VAL ILE SER GLY          
SEQRES  36 P  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 P  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 P  496  SER ALA GLN ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 P  496  LYS LEU                                                      
SEQRES   1 T   74  ASP THR THR VAL SER GLU PRO ALA PRO SER CYS VAL THR          
SEQRES   2 T   74  LEU TYR GLN SER TRP ARG TYR SER GLN ALA ASP ASN GLY          
SEQRES   3 T   74  CYS ALA GLU THR VAL THR VAL LYS VAL VAL TYR GLU ASP          
SEQRES   4 T   74  ASP THR GLU GLY LEU CYS TYR ALA VAL ALA PRO GLY GLN          
SEQRES   5 T   74  ILE THR THR VAL GLY ASP GLY TYR ILE GLY SER HIS GLY          
SEQRES   6 T   74  HIS ALA ARG TYR LEU ALA ARG CYS LEU                          
HET     CA  P2001       1                                                       
HET     CL  P2002       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CA    CA 2+                                                        
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  HOH   *161(H2 O)                                                    
HELIX    1   1 TRP P   21  ARG P   30  1                                  10    
HELIX    2   2 TRP P   58  GLU P   60  5                                   3    
HELIX    3   3 GLU P   76  VAL P   89  1                                  14    
HELIX    4   4 PRO P  121  SER P  123  5                                   3    
HELIX    5   5 ALA P  133  ASP P  135  5                                   3    
HELIX    6   6 PRO P  154  ASP P  159  1                                   6    
HELIX    7   7 ASP P  173  ILE P  189  1                                  17    
HELIX    8   8 SER P  199  HIS P  201  5                                   3    
HELIX    9   9 PRO P  204  LYS P  213  1                                  10    
HELIX   10  10 SER P  244  TYR P  247  5                                   4    
HELIX   11  11 PHE P  256  VAL P  266  1                                  11    
HELIX   12  12 MET P  274  ASN P  279  5                                   6    
HELIX   13  13 GLU P  282  TRP P  284  5                                   3    
HELIX   14  14 SER P  289  ARG P  291  5                                   3    
HELIX   15  15 ASN P  301  ARG P  303  5                                   3    
HELIX   16  16 PHE P  315  ALA P  330  5                                  16    
HELIX   17  17 GLU P  385  ARG P  387  5                                   3    
HELIX   18  18 ARG P  389  VAL P  400  1                                  12    
HELIX   19  19 ALA P  492  SER P  494  5                                   3    
SHEET    1   A 6 THR P 336  SER P 340  0                                        
SHEET    2   A 6 ASP P  12  LEU P  16  1  N  ILE P  13   O  THR P 336           
SHEET    3   A 6 GLY P  39  GLN P  41  1  N  GLY P  39   O  VAL P  14           
SHEET    4   A 6 ARG P  92  ALA P  97  1  N  ARG P  92   O  VAL P  40           
SHEET    5   A 6 GLY P 193  LEU P 196  1  N  GLY P 193   O  VAL P  95           
SHEET    6   A 6 PHE P 229  GLN P 232  1  N  PHE P 229   O  PHE P 194           
SHEET    1   B 3 GLN P 416  ARG P 421  0                                        
SHEET    2   B 3 GLY P 425  ASN P 430 -1  N  PHE P 429   O  VAL P 417           
SHEET    3   B 3 PHE P 487  HIS P 491 -1  N  ILE P 490   O  PHE P 426           
SHEET    1   C 2 LEU P 436  GLN P 441  0                                        
SHEET    2   C 2 THR P 474  ILE P 479 -1  N  ILE P 479   O  LEU P 436           
SHEET    1   D 2 GLY P 447  CYS P 450  0                                        
SHEET    2   D 2 LYS P 466  VAL P 469 -1  N  VAL P 469   O  GLY P 447           
SHEET    1   E 3 VAL T 812  GLN T 816  0                                        
SHEET    2   E 3 TYR T 820  ASN T 825 -1  N  ASP T 824   O  THR T 813           
SHEET    3   E 3 ILE T 853  ASP T 858 -1  N  GLY T 857   O  SER T 821           
SHEET    1   F 3 TYR T 846  VAL T 848  0                                        
SHEET    2   F 3 VAL T 831  TYR T 837 -1  N  VAL T 833   O  TYR T 846           
SHEET    3   F 3 ALA T 867  ARG T 872 -1  N  ALA T 871   O  LYS T 834           
SSBOND   1 CYS P   28    CYS P   86                          1555   1555  2.03  
SSBOND   2 CYS P   70    CYS P  115                          1555   1555  2.03  
SSBOND   3 CYS P  141    CYS P  160                          1555   1555  2.03  
SSBOND   4 CYS P  378    CYS P  384                          1555   1555  2.03  
SSBOND   5 CYS P  450    CYS P  462                          1555   1555  2.03  
SSBOND   6 CYS T  811    CYS T  827                          1555   1555  2.03  
SSBOND   7 CYS T  845    CYS T  873                          1555   1555  2.02  
LINK         OD1 ASN P 100                CA    CA P2001     1555   1555  2.69  
LINK         O   ARG P 158                CA    CA P2001     1555   1555  2.48  
LINK         OD1 ASP P 167                CA    CA P2001     1555   1555  2.57  
LINK         OD2 ASP P 167                CA    CA P2001     1555   1555  2.63  
LINK         O   HIS P 201                CA    CA P2001     1555   1555  2.51  
LINK        CA    CA P2001                 O   HOH P1152     1555   1555  2.96  
CISPEP   1 VAL P  129    PRO P  130          0        -6.43                     
SITE     1  AS  3 ASP P 197  GLU P 233  ASP P 300                               
SITE     1  CA  4 ASN P 100  ARG P 158  ASP P 167  HIS P 201                    
SITE     1  CL  3 ARG P 195  ASN P 298  ARG P 337                               
SITE     1 AC1  5 ASN P 100  ARG P 158  ASP P 167  HIS P 201                    
SITE     2 AC1  5 HOH P1152                                                     
SITE     1 AC2  2 ARG P 195  ARG P 337                                          
CRYST1   77.700   77.700  359.500  90.00  90.00 120.00 P 65 2 2     12          
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      0.012870  0.007430  0.000000        0.00000                         
SCALE2      0.000000  0.014861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002782        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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