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Database: PDB
Entry: 1BLI
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Original site: 1BLI 
HEADER    HYDROLASE                               07-JAN-98   1BLI              
TITLE     BACILLUS LICHENIFORMIS ALPHA-AMYLASE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GLUCANOTRANSFERASE, ALPHA-1,4-GLUCAN-4-                     
COMPND   5 GLUCANOHYDROLASE;                                                    
COMPND   6 EC: 3.2.1.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: PROTEIN PRODUCED BY NOVO NORDISK A/S,                 
COMPND  10 DENMARK                                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;                         
SOURCE   3 ORGANISM_TAXID: 1402;                                                
SOURCE   4 CELL_LINE: 293;                                                      
SOURCE   5 ATCC: ATCC 6598;                                                     
SOURCE   6 COLLECTION: ATCC 6598;                                               
SOURCE   7 GENE: AMYL;                                                          
SOURCE   8 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;                                
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 1423;                                       
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: 293;                                       
SOURCE  11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETED;                       
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PINA9C9                                   
KEYWDS    HYDROLASE, GLYCOSYLTRANSFERASE, ALPHA-AMYLASE, STARCH                 
KEYWDS   2 DEGRADATION, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE,                    
KEYWDS   3 THERMOSTABILITY, CALCIUM, SODIUM                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MACHIUS,N.DECLERCK,R.HUBER,G.WIEGAND                                
REVDAT   2   24-FEB-09 1BLI    1       VERSN                                    
REVDAT   1   23-MAR-99 1BLI    0                                                
JRNL        AUTH   M.MACHIUS,N.DECLERCK,R.HUBER,G.WIEGAND                       
JRNL        TITL   ACTIVATION OF BACILLUS LICHENIFORMIS ALPHA-AMYLASE           
JRNL        TITL 2 THROUGH A DISORDER-->ORDER TRANSITION OF THE                 
JRNL        TITL 3 SUBSTRATE-BINDING SITE MEDIATED BY A                         
JRNL        TITL 4 CALCIUM-SODIUM-CALCIUM METAL TRIAD.                          
JRNL        REF    STRUCTURE                     V.   6   281 1998              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9551551                                                      
JRNL        DOI    10.1016/S0969-2126(98)00032-X                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.Y.HWANG,H.K.SONG,C.CHANG,J.LEE,S.Y.LEE,K.K.KIM,            
REMARK   1  AUTH 2 S.CHOE,R.M.SWEET,S.W.SUH                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF THERMOSTABLE ALPHA-AMYLASE              
REMARK   1  TITL 2 FROM BACILLUS LICHENIFORMIS REFINED AT 1.7 A                 
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    MOL.CELLS                     V.   7   251 1997              
REMARK   1  REFN                   ISSN 1016-8478                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.MACHIUS,G.WIEGAND,R.HUBER                                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF CALCIUM-DEPLETED BACILLUS               
REMARK   1  TITL 2 LICHENIFORMIS ALPHA-AMYLASE AT 2.2 A RESOLUTION              
REMARK   1  REF    J.MOL.BIOL.                   V. 246   545 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 45685                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2291                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3790                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 204                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3905                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 221                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 4.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
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) : 1.380 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.990 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.110 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.730 ; 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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TIP3P.PARAMETER                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1BLI 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        : MAY-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 278                                
REMARK 200  PH                             : 7.0                                
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                  : NI FILTER                          
REMARK 200  OPTICS                         : BEAM FOCUSSING MIRROR SYSTEM       
REMARK 200                                   (MSC, USA)                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46801                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PATTERSON SEARCH             
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BPL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       45.90000            
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       91.80000            
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       68.85000            
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      114.75000            
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       22.95000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   7   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  58       74.83     44.60                                   
REMARK 500    LEU A  64       40.04    -89.87                                   
REMARK 500    TYR A 150      -29.11     75.17                                   
REMARK 500    LEU A 196      -61.95   -120.99                                   
REMARK 500    TYR A 198     -145.80     53.34                                   
REMARK 500    MET A 256       71.74     45.96                                   
REMARK 500    PHE A 279       27.67     47.34                                   
REMARK 500    SER A 337       54.95   -167.92                                   
REMARK 500    PHE A 403       62.71   -118.38                                   
REMARK 500    ASP A 407      -60.07   -120.29                                   
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 195         0.09    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 A 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 181   O                                                      
REMARK 620 2 ASP A 183   OD1 106.7                                              
REMARK 620 3 ASP A 202   OD1 164.2  89.0                                        
REMARK 620 4 ASP A 204   OD2  92.5  73.3  93.8                                  
REMARK 620 5 ASP A 161   OD1  86.5 129.9  81.9 155.9                            
REMARK 620 6 ASP A 161   OD2  85.8  81.7  94.9 153.4  50.6                      
REMARK 620 7 HOH A2079   O    84.2 153.8  82.3  82.6  73.4 123.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 104   OD1                                                    
REMARK 620 2 ASP A 194   O   102.2                                              
REMARK 620 3 HIS A 235   O    81.8  91.1                                        
REMARK 620 4 ASP A 194   OD1 159.2  81.3  77.6                                  
REMARK 620 5 ASP A 200   OD1  87.3  79.1 163.5 113.5                            
REMARK 620 6 ASP A 200   OD2 129.6  87.3 148.2  70.7  45.6                      
REMARK 620 7 HOH A2080   O    86.2 161.3 106.8  96.9  84.6  74.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 700  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 302   O                                                      
REMARK 620 2 ASP A 407   OD1 149.4                                              
REMARK 620 3 HOH A2069   O    75.8  81.4                                        
REMARK 620 4 HIS A 406   O    77.6  78.7  80.6                                  
REMARK 620 5 ASP A 430   OD1 116.5  84.0 164.9  93.4                            
REMARK 620 6 ASP A 430   OD2  82.0 127.4 144.3 121.6  50.1                      
REMARK 620 7 GLY A 300   O   107.9  87.4  79.5 157.2 103.1  81.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 800  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 194   OD2                                                    
REMARK 620 2 ASP A 200   OD2  88.6                                              
REMARK 620 3 ILE A 201   O   159.8  89.0                                        
REMARK 620 4 ASP A 161   OD2  86.0 117.4 112.8                                  
REMARK 620 5 ASP A 183   OD2  88.1 150.0  84.0  92.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CS                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE.                                    
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE. THIS CALCIUM BINDING         
REMARK 800  SITE IS CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND           
REMARK 800  RELATED ENZYMES.                                                    
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE. THIS CALCIUM BINDING         
REMARK 800  SITE IS NOT CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND       
REMARK 800  RELATED ENZYMES.                                                    
REMARK 800 SITE_IDENTIFIER: NA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: SODIUM BINDING SITE. THIS IS THE FIRST SODIUM      
REMARK 800  BINDING SITE OBSERVED IN AN ALPHA-AMYLASE OR RELATED ENZYME.        
REMARK 800  THIS SODIUM TOGETHER WITH THE CALCIUM IONS CA1 AND CA2 FORM A       
REMARK 800  LINEAR TRIADIC ARRAY WITH THE CALCIUM IONS 4.1 AND 4.5 A FROM       
REMARK 800  THE CENTRAL SODIUM ION.                                             
REMARK 800 SITE_IDENTIFIER: CA3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE. THIS CALCIUM BINDING         
REMARK 800  SITE LOCATED IN THE INTERFACE BETWEEN DOMAIN A AND C IS NOT         
REMARK 800  CONSERVED IN ALL STRUCTURES OF ALPHA-AMYLASES AND RELATED           
REMARK 800  ENZYMES.                                                            
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 600                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 800                  
DBREF  1BLI A    1   483  UNP    P06278   AMY_BACLI       30    512             
SEQADV 1BLI LEU A  134  UNP  P06278    ARG   163 CONFLICT                       
SEQADV 1BLI PHE A  190  UNP  P06278    ASN   219 ENGINEERED MUTATION            
SEQADV 1BLI SER A  264  UNP  P06278    GLN   293 ENGINEERED MUTATION            
SEQADV 1BLI TYR A  265  UNP  P06278    ASN   294 ENGINEERED MUTATION            
SEQADV 1BLI GLY A  310  UNP  P06278    SER   339 CONFLICT                       
SEQADV 1BLI SER A  320  UNP  P06278    ALA   349 CONFLICT                       
SEQADV 1BLI ALA A  465  UNP  P06278    GLU   494 CONFLICT                       
SEQRES   1 A  483  ALA ASN LEU ASN GLY THR LEU MET GLN TYR PHE GLU TRP          
SEQRES   2 A  483  TYR MET PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN          
SEQRES   3 A  483  ASN ASP SER ALA TYR LEU ALA GLU HIS GLY ILE THR ALA          
SEQRES   4 A  483  VAL TRP ILE PRO PRO ALA TYR LYS GLY THR SER GLN ALA          
SEQRES   5 A  483  ASP VAL GLY TYR GLY ALA TYR ASP LEU TYR ASP LEU GLY          
SEQRES   6 A  483  GLU PHE HIS GLN LYS GLY THR VAL ARG THR LYS TYR GLY          
SEQRES   7 A  483  THR LYS GLY GLU LEU GLN SER ALA ILE LYS SER LEU HIS          
SEQRES   8 A  483  SER ARG ASP ILE ASN VAL TYR GLY ASP VAL VAL ILE ASN          
SEQRES   9 A  483  HIS LYS GLY GLY ALA ASP ALA THR GLU ASP VAL THR ALA          
SEQRES  10 A  483  VAL GLU VAL ASP PRO ALA ASP ARG ASN ARG VAL ILE SER          
SEQRES  11 A  483  GLY GLU HIS LEU ILE LYS ALA TRP THR HIS PHE HIS PHE          
SEQRES  12 A  483  PRO GLY ARG GLY SER THR TYR SER ASP PHE LYS TRP HIS          
SEQRES  13 A  483  TRP TYR HIS PHE ASP GLY THR ASP TRP ASP GLU SER ARG          
SEQRES  14 A  483  LYS LEU ASN ARG ILE TYR LYS PHE GLN GLY LYS ALA TRP          
SEQRES  15 A  483  ASP TRP GLU VAL SER ASN GLU PHE GLY ASN TYR ASP TYR          
SEQRES  16 A  483  LEU MET TYR ALA ASP ILE ASP TYR ASP HIS PRO ASP VAL          
SEQRES  17 A  483  ALA ALA GLU ILE LYS ARG TRP GLY THR TRP TYR ALA ASN          
SEQRES  18 A  483  GLU LEU GLN LEU ASP GLY PHE ARG LEU ASP ALA VAL LYS          
SEQRES  19 A  483  HIS ILE LYS PHE SER PHE LEU ARG ASP TRP VAL ASN HIS          
SEQRES  20 A  483  VAL ARG GLU LYS THR GLY LYS GLU MET PHE THR VAL ALA          
SEQRES  21 A  483  GLU TYR TRP SER TYR ASP LEU GLY ALA LEU GLU ASN TYR          
SEQRES  22 A  483  LEU ASN LYS THR ASN PHE ASN HIS SER VAL PHE ASP VAL          
SEQRES  23 A  483  PRO LEU HIS TYR GLN PHE HIS ALA ALA SER THR GLN GLY          
SEQRES  24 A  483  GLY GLY TYR ASP MET ARG LYS LEU LEU ASN GLY THR VAL          
SEQRES  25 A  483  VAL SER LYS HIS PRO LEU LYS SER VAL THR PHE VAL ASP          
SEQRES  26 A  483  ASN HIS ASP THR GLN PRO GLY GLN SER LEU GLU SER THR          
SEQRES  27 A  483  VAL GLN THR TRP PHE LYS PRO LEU ALA TYR ALA PHE ILE          
SEQRES  28 A  483  LEU THR ARG GLU SER GLY TYR PRO GLN VAL PHE TYR GLY          
SEQRES  29 A  483  ASP MET TYR GLY THR LYS GLY ASP SER GLN ARG GLU ILE          
SEQRES  30 A  483  PRO ALA LEU LYS HIS LYS ILE GLU PRO ILE LEU LYS ALA          
SEQRES  31 A  483  ARG LYS GLN TYR ALA TYR GLY ALA GLN HIS ASP TYR PHE          
SEQRES  32 A  483  ASP HIS HIS ASP ILE VAL GLY TRP THR ARG GLU GLY ASP          
SEQRES  33 A  483  SER SER VAL ALA ASN SER GLY LEU ALA ALA LEU ILE THR          
SEQRES  34 A  483  ASP GLY PRO GLY GLY ALA LYS ARG MET TYR VAL GLY ARG          
SEQRES  35 A  483  GLN ASN ALA GLY GLU THR TRP HIS ASP ILE THR GLY ASN          
SEQRES  36 A  483  ARG SER GLU PRO VAL VAL ILE ASN SER ALA GLY TRP GLY          
SEQRES  37 A  483  GLU PHE HIS VAL ASN GLY GLY SER VAL SER ILE TYR VAL          
SEQRES  38 A  483  GLN ARG                                                      
HET     CA  A 500       1                                                       
HET     CA  A 600       1                                                       
HET     CA  A 700       1                                                       
HET     NA  A 800       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *221(H2 O)                                                    
HELIX    1   1 HIS A   21  GLU A   34  1                                  14    
HELIX    2   2 LYS A   80  ARG A   93  1                                  14    
HELIX    3   3 TRP A  157  HIS A  159  5                                   3    
HELIX    4   4 PRO A  206  LEU A  223  1                                  18    
HELIX    5   5 VAL A  233  HIS A  235  5                                   3    
HELIX    6   6 PHE A  238  THR A  252  1                                  15    
HELIX    7   7 LEU A  267  LYS A  276  1                                  10    
HELIX    8   8 VAL A  286  THR A  297  1                                  12    
HELIX    9   9 MET A  304  LEU A  308  5                                   5    
HELIX   10  10 VAL A  312  LYS A  315  1                                   4    
HELIX   11  11 THR A  341  THR A  353  1                                  13    
HELIX   12  12 TYR A  363  TYR A  367  1                                   5    
HELIX   13  13 LYS A  381  GLN A  393  1                                  13    
HELIX   14  14 ARG A  442  ASN A  444  5                                   3    
SHEET    1   A 7 VAL A 321  PHE A 323  0                                        
SHEET    2   A 7 TYR A 358  PHE A 362  1  N  TYR A 358   O  THR A 322           
SHEET    3   A 7 LEU A   7  GLN A   9  1  N  LEU A   7   O  VAL A 361           
SHEET    4   A 7 ALA A  39  ILE A  42  1  N  ALA A  39   O  MET A   8           
SHEET    5   A 7 ASN A  96  VAL A 101  1  N  ASN A  96   O  VAL A  40           
SHEET    6   A 7 GLY A 227  LEU A 230  1  N  GLY A 227   O  GLY A  99           
SHEET    7   A 7 PHE A 257  ALA A 260  1  N  PHE A 257   O  PHE A 228           
SHEET    1   B 3 TYR A 175  PHE A 177  0                                        
SHEET    2   B 3 ALA A 111  GLU A 119 -1  N  VAL A 118   O  LYS A 176           
SHEET    3   B 3 HIS A 133  HIS A 140 -1  N  HIS A 140   O  ALA A 111           
SHEET    1   C 5 GLN A 399  TYR A 402  0                                        
SHEET    2   C 5 ILE A 408  ARG A 413 -1  N  THR A 412   O  HIS A 400           
SHEET    3   C 5 LEU A 424  THR A 429 -1  N  ILE A 428   O  VAL A 409           
SHEET    4   C 5 VAL A 477  GLN A 482 -1  N  TYR A 480   O  ALA A 425           
SHEET    5   C 5 TRP A 449  ASP A 451 -1  N  HIS A 450   O  VAL A 481           
SHEET    1   D 2 GLY A 434  TYR A 439  0                                        
SHEET    2   D 2 TRP A 467  VAL A 472 -1  N  VAL A 472   O  GLY A 434           
LINK        CA    CA A 500                 O   ALA A 181     1555   1555  2.39  
LINK        CA    CA A 500                 OD1 ASP A 183     1555   1555  2.36  
LINK        CA    CA A 500                 OD1 ASP A 202     1555   1555  2.40  
LINK        CA    CA A 600                 OD1 ASN A 104     1555   1555  2.35  
LINK        CA    CA A 600                 O   ASP A 194     1555   1555  2.36  
LINK        CA    CA A 600                 O   HIS A 235     1555   1555  2.38  
LINK        CA    CA A 700                 O   TYR A 302     1555   1555  2.28  
LINK        CA    CA A 700                 OD1 ASP A 407     1555   1555  2.31  
LINK        CA    CA A 500                 OD2 ASP A 204     1555   1555  2.54  
LINK        CA    CA A 500                 OD1 ASP A 161     1555   1555  2.58  
LINK        CA    CA A 500                 OD2 ASP A 161     1555   1555  2.55  
LINK        CA    CA A 500                 O   HOH A2079     1555   1555  2.54  
LINK        CA    CA A 600                 OD1 ASP A 194     1555   1555  2.41  
LINK        CA    CA A 600                 OD1 ASP A 200     1555   1555  2.42  
LINK        CA    CA A 600                 OD2 ASP A 200     1555   1555  3.05  
LINK        CA    CA A 600                 O   HOH A2080     1555   1555  2.50  
LINK        CA    CA A 700                 O   HOH A2069     1555   1555  2.81  
LINK        CA    CA A 700                 O   HIS A 406     1555   1555  2.54  
LINK        CA    CA A 700                 OD1 ASP A 430     1555   1555  2.59  
LINK        CA    CA A 700                 OD2 ASP A 430     1555   1555  2.61  
LINK        CA    CA A 700                 O   GLY A 300     1555   1555  2.47  
LINK        NA    NA A 800                 OD2 ASP A 194     1555   1555  2.47  
LINK        NA    NA A 800                 OD2 ASP A 200     1555   1555  2.43  
LINK        NA    NA A 800                 O   ILE A 201     1555   1555  2.50  
LINK        NA    NA A 800                 OD2 ASP A 161     1555   1555  2.44  
LINK         OD2 ASP A 183                NA    NA A 800     1555   1555  2.71  
CISPEP   1 TRP A  184    GLU A  185          0        12.07                     
SITE     1  CS  3 MET A 197  VAL A 233  GLY A 300                               
SITE     1 CA1  4 ASN A 104  ASP A 194  ASP A 200  HIS A 235                    
SITE     1 CA2  5 ASP A 161  ALA A 181  ASP A 183  ASP A 202                    
SITE     2 CA2  5 ASP A 204                                                     
SITE     1 NA1  5 ASP A 161  ASP A 183  ASP A 194  ASP A 200                    
SITE     2 NA1  5 ILE A 201                                                     
SITE     1 CA3  5 GLY A 300  TYR A 302  HIS A 406  ASP A 407                    
SITE     2 CA3  5 ASP A 430                                                     
SITE     1 AC1  6 ASP A 161  ALA A 181  ASP A 183  ASP A 202                    
SITE     2 AC1  6 ASP A 204  HOH A2079                                          
SITE     1 AC2  5 ASN A 104  ASP A 194  ASP A 200  HIS A 235                    
SITE     2 AC2  5 HOH A2080                                                     
SITE     1 AC3  6 GLY A 300  TYR A 302  HIS A 406  ASP A 407                    
SITE     2 AC3  6 ASP A 430  HOH A2069                                          
SITE     1 AC4  5 ASP A 161  ASP A 183  ASP A 194  ASP A 200                    
SITE     2 AC4  5 ILE A 201                                                     
CRYST1   91.300   91.300  137.700  90.00  90.00 120.00 P 61          6          
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      0.010953  0.006324  0.000000        0.00000                         
SCALE2      0.000000  0.012647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007262        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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