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Database: PDB
Entry: 1BAG
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HEADER    ALPHA-AMYLASE                           30-JAN-98   1BAG              
TITLE     ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH                   
TITLE    2 MALTOPENTAOSE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-AMYLASE;                                              
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: COMPLEXED WITH MALTOPENTAOSE                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: AMY;                                                           
SOURCE   5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;                                
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 1423;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: 207-25;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PUB110;                                    
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTUB111;                                  
SOURCE  11 EXPRESSION_SYSTEM_GENE: AMY                                          
KEYWDS    ALPHA-AMYLASE, BACILLUS SUBTILIS, MALTOPENTAOSE, CATALYTIC-           
KEYWDS   2 SITE MUTANT                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.FUJIMOTO,H.MIZUNO,K.TAKASE,N.DOUI                                   
REVDAT   3   04-AUG-09 1BAG    1       ATOM   COMPND CONECT HET                 
REVDAT   3 2                   1       HETATM HETNAM LINK   SITE                
REVDAT   2   24-FEB-09 1BAG    1       VERSN                                    
REVDAT   1   21-OCT-98 1BAG    0                                                
JRNL        AUTH   Z.FUJIMOTO,K.TAKASE,N.DOUI,M.MOMMA,T.MATSUMOTO,              
JRNL        AUTH 2 H.MIZUNO                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A CATALYTIC-SITE MUTANT                 
JRNL        TITL 2 ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH          
JRNL        TITL 3 MALTOPENTAOSE.                                               
JRNL        REF    J.MOL.BIOL.                   V. 277   393 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9514750                                                      
JRNL        DOI    10.1006/JMBI.1997.1599                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.MIZUNO,Y.MORIMOTO,T.TSUKIHARA,T.MATSUMOTO,                 
REMARK   1  AUTH 2 K.TAKASE                                                     
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF             
REMARK   1  TITL 2 WILD TYPE AND CATALYTIC-SITE MUTANT ALPHA-AMYLASE            
REMARK   1  TITL 3 FROM BACILLUS SUBTILIS                                       
REMARK   1  REF    J.MOL.BIOL.                   V. 234  1282 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.TAKASE,T.MATSUMOTO,H.MIZUNO,K.YAMANE                       
REMARK   1  TITL   SITE-DIRECTED MUTAGENESIS OF ACTIVE SITE RESIDUES            
REMARK   1  TITL 2 IN BACILLUS SUBTILIS ALPHA-AMYLASE                           
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1120   281 1992              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.YAMANE,Y.HIRATA,T.FURUSATO,H.YAMAZAKI,A.NAKAYAMA           
REMARK   1  TITL   CHANGES IN THE PROPERTIES AND MOLECULAR WEIGHTS OF           
REMARK   1  TITL 2 BACILLUS SUBTILIS M-TYPE AND N-TYPE ALPHA-AMYLASES           
REMARK   1  TITL 3 RESULTING FROM A SPONTANEOUS DELETION                        
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V.  96  1849 1984              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
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) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17162                          
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) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1676                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1563                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 174                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3322                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.90                          
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) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
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) : 3.240 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.420 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.440 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.800 ; 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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  3  : PARAM19X.ION                                   
REMARK   3  PARAMETER FILE  4  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : TOPH19X.ION                                    
REMARK   3  TOPOLOGY FILE  4   : TOPH19X.SOL                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BAG 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        : OCT-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 288                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : COLLIMATOR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
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     (%) : 44.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 10%        
REMARK 280  PEG 3350, 3.5 MM CALCIUM CHLORIDE, 10 MM TRIS/HCL, PH 7.5.          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.29500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.50500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.50500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.29500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.03000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  67       34.99    -95.08                                   
REMARK 500    THR A 103     -167.35   -123.85                                   
REMARK 500    GLU A 182      159.65    -49.87                                   
REMARK 500    THR A 200     -167.97   -120.80                                   
REMARK 500    ASP A 212     -161.33   -172.13                                   
REMARK 500    ALA A 214       34.05    -98.89                                   
REMARK 500    LEU A 244       37.23    -90.45                                   
REMARK 500    ILE A 249       35.49    -90.28                                   
REMARK 500    MET A 281      170.00    -49.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASP A 425        23.5      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 542        DISTANCE =  6.01 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 431  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 509   O                                                      
REMARK 620 2 HIS A 180   O    82.0                                              
REMARK 620 3 THR A 137   O    73.2  80.7                                        
REMARK 620 4 ASN A 101   OD1 122.0  69.4 142.6                                  
REMARK 620 5 ASP A 146   OD1 135.2 141.8 113.7  80.6                            
REMARK 620 6 ASP A 146   OD2  99.1 154.3  75.2 127.9  47.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 432  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 482   O                                                      
REMARK 620 2 GLY A 169   O    76.5                                              
REMARK 620 3 HOH A 470   O    91.0 165.8                                        
REMARK 620 4 HOH A 538   O    99.9  96.3  92.6                                  
REMARK 620 5 ASP A 171   OD2 111.0  80.8  97.8 147.1                            
REMARK 620 6 ASP A 171   OD1  67.4  92.7  76.0 162.3  49.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 433  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 276   OE2                                                    
REMARK 620 2 HOH A 526   O   144.3                                              
REMARK 620 3 GLY A 313   O    94.4  85.8                                        
REMARK 620 4 HOH A 524   O    70.9 104.3 165.1                                  
REMARK 620 5 HOH A 494   O   137.7  78.0  90.0 102.7                            
REMARK 620 6 GLU A 276   OE1  50.2 163.1  83.6  88.8  88.8                      
REMARK 620 7 GLU A  89   OE2  73.9  70.4  87.2  85.9 148.4 122.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.                              
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE (ADVENTITIOUS).               
REMARK 800 SITE_IDENTIFIER: CA3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE (ADVENTITIOUS).               
DBREF  1BAG A    1   425  UNP    P00691   AMY_BACSU       42    466             
SEQADV 1BAG PHE A  105  UNP  P00691    SER   146 VARIANT STRAIN                 
SEQADV 1BAG GLU A  163  UNP  P00691    ASP   204 VARIANT STRAIN                 
SEQADV 1BAG GLN A  208  UNP  P00691    GLU   249 ENGINEERED                     
SEQRES   1 A  425  LEU THR ALA PRO SER ILE LYS SER GLY THR ILE LEU HIS          
SEQRES   2 A  425  ALA TRP ASN TRP SER PHE ASN THR LEU LYS HIS ASN MET          
SEQRES   3 A  425  LYS ASP ILE HIS ASP ALA GLY TYR THR ALA ILE GLN THR          
SEQRES   4 A  425  SER PRO ILE ASN GLN VAL LYS GLU GLY ASN GLN GLY ASP          
SEQRES   5 A  425  LYS SER MET SER ASN TRP TYR TRP LEU TYR GLN PRO THR          
SEQRES   6 A  425  SER TYR GLN ILE GLY ASN ARG TYR LEU GLY THR GLU GLN          
SEQRES   7 A  425  GLU PHE LYS GLU MET CYS ALA ALA ALA GLU GLU TYR GLY          
SEQRES   8 A  425  ILE LYS VAL ILE VAL ASP ALA VAL ILE ASN HIS THR THR          
SEQRES   9 A  425  PHE ASP TYR ALA ALA ILE SER ASN GLU VAL LYS SER ILE          
SEQRES  10 A  425  PRO ASN TRP THR HIS GLY ASN THR GLN ILE LYS ASN TRP          
SEQRES  11 A  425  SER ASP ARG TRP ASP VAL THR GLN ASN SER LEU LEU GLY          
SEQRES  12 A  425  LEU TYR ASP TRP ASN THR GLN ASN THR GLN VAL GLN SER          
SEQRES  13 A  425  TYR LEU LYS ARG PHE LEU GLU ARG ALA LEU ASN ASP GLY          
SEQRES  14 A  425  ALA ASP GLY PHE ARG PHE ASP ALA ALA LYS HIS ILE GLU          
SEQRES  15 A  425  LEU PRO ASP ASP GLY SER TYR GLY SER GLN PHE TRP PRO          
SEQRES  16 A  425  ASN ILE THR ASN THR SER ALA GLU PHE GLN TYR GLY GLN          
SEQRES  17 A  425  ILE LEU GLN ASP SER ALA SER ARG ASP ALA ALA TYR ALA          
SEQRES  18 A  425  ASN TYR MET ASP VAL THR ALA SER ASN TYR GLY HIS SER          
SEQRES  19 A  425  ILE ARG SER ALA LEU LYS ASN ARG ASN LEU GLY VAL SER          
SEQRES  20 A  425  ASN ILE SER HIS TYR ALA SER ASP VAL SER ALA ASP LYS          
SEQRES  21 A  425  LEU VAL THR TRP VAL GLU SER HIS ASP THR TYR ALA ASN          
SEQRES  22 A  425  ASP ASP GLU GLU SER THR TRP MET SER ASP ASP ASP ILE          
SEQRES  23 A  425  ARG LEU GLY TRP ALA VAL ILE ALA SER ARG SER GLY SER          
SEQRES  24 A  425  THR PRO LEU PHE PHE SER ARG PRO GLU GLY GLY GLY ASN          
SEQRES  25 A  425  GLY VAL ARG PHE PRO GLY LYS SER GLN ILE GLY ASP ARG          
SEQRES  26 A  425  GLY SER ALA LEU PHE GLU ASP GLN ALA ILE THR ALA VAL          
SEQRES  27 A  425  ASN ARG PHE HIS ASN VAL MET ALA GLY GLN PRO GLU GLU          
SEQRES  28 A  425  LEU SER ASN PRO ASN GLY ASN ASN GLN ILE PHE MET ASN          
SEQRES  29 A  425  GLN ARG GLY SER HIS GLY VAL VAL LEU ALA ASN ALA GLY          
SEQRES  30 A  425  SER SER SER VAL SER ILE ASN THR ALA THR LYS LEU PRO          
SEQRES  31 A  425  ASP GLY ARG TYR ASP ASN LYS ALA GLY ALA GLY SER PHE          
SEQRES  32 A  425  GLN VAL ASN ASP GLY LYS LEU THR GLY THR ILE ASN ALA          
SEQRES  33 A  425  ARG SER VAL ALA VAL LEU TYR PRO ASP                          
HET    GLC  A 426      11                                                       
HET    GLC  A 427      11                                                       
HET    GLC  A 428      11                                                       
HET    GLC  A 429      11                                                       
HET    BGC  A 430      12                                                       
HET     CA  A 431       1                                                       
HET     CA  A 432       1                                                       
HET     CA  A 433       1                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  GLC    4(C6 H12 O6)                                                 
FORMUL   2  BGC    C6 H12 O6                                                    
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  HOH   *146(H2 O)                                                    
HELIX    1 AA1 PHE A   19  ASP A   31  1                                  13    
HELIX    2 AA2 GLU A   77  GLU A   89  1                                  13    
HELIX    3 BH1 ASN A  112  LYS A  115  1                                   4    
HELIX    4 BA1 ARG A  133  GLN A  138  1                                   6    
HELIX    5 AA3 THR A  152  ASP A  168  1                                  17    
HELIX    6 AA4 PHE A  193  ILE A  197  1                                   5    
HELIX    7 AA5 ASP A  217  TYR A  223  1                                   7    
HELIX    8 AA6 SER A  229  LEU A  244  1                                  16    
HELIX    9 AH1 HIS A  268  ALA A  272  1                                   5    
HELIX   10 AA7 ASP A  283  ALA A  294  1                                  12    
HELIX   11 AA8 ASP A  332  VAL A  344  1                                  13    
SHEET    1 AS1 8 ILE A  11  HIS A  13  0                                        
SHEET    2 AS1 8 ALA A  36  GLN A  38  1  N  GLN A  38   O  LEU A  12           
SHEET    3 AS1 8 LYS A  93  ALA A  98  1  N  ILE A  95   O  ILE A  37           
SHEET    4 AS1 8 GLY A 172  PHE A 175  1  N  ARG A 174   O  VAL A  96           
SHEET    5 AS1 8 PHE A 204  GLY A 207  1  N  TYR A 206   O  PHE A 173           
SHEET    6 AS1 8 ASP A 225  THR A 227  1  N  ASP A 225   O  GLN A 205           
SHEET    7 AS1 8 LEU A 261  THR A 263  1  N  VAL A 262   O  VAL A 226           
SHEET    8 AS1 8 THR A 300  PHE A 304  1  N  THR A 300   O  LEU A 261           
SHEET    1 AS2 2 ASN A  43  VAL A  45  0                                        
SHEET    2 AS2 2 PRO A  64  TYR A  67 -1  N  SER A  66   O  GLN A  44           
SHEET    1 AS3 2 ILE A  69  ASN A  71  0                                        
SHEET    2 AS3 2 GLY A  75  THR A  76 -1  N  GLY A  75   O  ASN A  71           
SHEET    1 BS1 3 HIS A 102  THR A 103  0                                        
SHEET    2 BS1 3 TYR A 145  TRP A 147 -1  N  TYR A 145   O  THR A 103           
SHEET    3 BS1 3 THR A 121  GLY A 123 -1  N  GLY A 123   O  ASP A 146           
SHEET    1 CS1 4 GLU A 350  SER A 353  0                                        
SHEET    2 CS1 4 ILE A 361  ARG A 366 -1  N  GLN A 365   O  GLU A 351           
SHEET    3 CS1 4 GLY A 370  ASN A 375 -1  N  VAL A 372   O  ASN A 364           
SHEET    4 CS1 4 SER A 418  LEU A 422 -1  N  ALA A 420   O  LEU A 373           
SHEET    1 CS2 4 VAL A 381  ALA A 386  0                                        
SHEET    2 CS2 4 LYS A 409  ILE A 414 -1  N  LEU A 410   O  THR A 385           
SHEET    3 CS2 4 SER A 402  ASN A 406 -1  N  GLN A 404   O  THR A 411           
SHEET    4 CS2 4 GLY A 392  ASP A 395 -1                                        
LINK         C1  GLC A 426                 O4  GLC A 427     1555   1555  1.40  
LINK         C1  GLC A 427                 O4  GLC A 428     1555   1555  1.39  
LINK         C1  GLC A 428                 O4  GLC A 429     1555   1555  1.42  
LINK        CA    CA A 431                 O   HOH A 509     1555   1555  2.46  
LINK        CA    CA A 431                 O   HIS A 180     1555   1555  2.34  
LINK        CA    CA A 431                 O   THR A 137     1555   1555  2.43  
LINK        CA    CA A 431                 OD1 ASN A 101     1555   1555  2.45  
LINK        CA    CA A 431                 OD1 ASP A 146     1555   1555  2.52  
LINK        CA    CA A 431                 OD2 ASP A 146     1555   1555  2.90  
LINK        CA    CA A 432                 O   HOH A 482     1555   1555  2.53  
LINK        CA    CA A 432                 O   GLY A 169     1555   1555  2.31  
LINK        CA    CA A 432                 O   HOH A 470     1555   1555  2.45  
LINK        CA    CA A 432                 O   HOH A 538     1555   1555  2.42  
LINK        CA    CA A 432                 OD2 ASP A 171     1555   1555  2.59  
LINK        CA    CA A 432                 OD1 ASP A 171     1555   1555  2.60  
LINK        CA    CA A 433                 OE2 GLU A 276     1555   1555  2.56  
LINK        CA    CA A 433                 O   HOH A 526     1555   1555  2.37  
LINK        CA    CA A 433                 O   GLY A 313     1555   1555  2.32  
LINK        CA    CA A 433                 O   HOH A 524     1555   1555  2.45  
LINK        CA    CA A 433                 O   HOH A 494     1555   1555  2.61  
LINK        CA    CA A 433                 OE1 GLU A 276     1555   1555  2.60  
LINK        CA    CA A 433                 OE2 GLU A  89     1555   3555  2.71  
LINK         C1  GLC A 429                 O4  BGC A 430     1555   1555  1.40  
SITE     1 CA1  5 ASN A 101  THR A 137  ASP A 146  HIS A 180                    
SITE     2 CA1  5 HOH A 509                                                     
SITE     1 CA2  5 GLY A 169  ASP A 171  HOH A 470  HOH A 482                    
SITE     2 CA2  5 HOH A 538                                                     
SITE     1 CA3  6 GLU A  89  GLU A 276  GLY A 313  HOH A 494                    
SITE     2 CA3  6 HOH A 524  HOH A 526                                          
CRYST1   72.590   74.060  117.010  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013776  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013503  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008546        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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