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Database: PDB
Entry: 1UA7
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HEADER    HYDROLASE                               03-MAR-03   1UA7              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF ALPHA-AMYLASE FROM BACILLUS             
TITLE    2 SUBTILIS COMPLEXED WITH ACARBOSE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 4-425;                                            
COMPND   5 SYNONYM: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;                        
COMPND   6 EC: 3.2.1.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;                                
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1423;                                       
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: 207-25;                                    
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNQ356                                    
KEYWDS    BETA-ALPHA-BARRELS, ACARBOSE, GREEK-KEY MOTIF, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KAGAWA,Z.FUJIMOTO,M.MOMMA,K.TAKASE,H.MIZUNO                         
REVDAT   2   24-FEB-09 1UA7    1       VERSN                                    
REVDAT   1   18-MAY-04 1UA7    0                                                
JRNL        AUTH   M.KAGAWA,Z.FUJIMOTO,M.MOMMA,K.TAKASE,H.MIZUNO                
JRNL        TITL   CRYSTAL STRUCTURE OF BACILLUS SUBTILIS                       
JRNL        TITL 2 ALPHA-AMYLASE IN COMPLEX WITH ACARBOSE                       
JRNL        REF    J.BACTERIOL.                  V. 185  6981 2003              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   14617662                                                     
JRNL        DOI    10.1128/JB.185.23.6981-6984.2003                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Z.FUJIMOTO,K.TAKASE,N.DOUI,M.MOMMA,T.MATSUMOTO,              
REMARK   1  AUTH 2 H.MIZUNO                                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF A CATALYTIC-SITE MUTANT                 
REMARK   1  TITL 2 ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED               
REMARK   1  TITL 3 WITH MALTOPENTAOSE                                           
REMARK   1  REF    J.MOL.BIOL.                   V. 277   393 1998              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1997.1599                                       
REMARK   1 REFERENCE 2                                                          
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  DOI    10.1006/JMBI.1993.1683                                       
REMARK   1 REFERENCE 3                                                          
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  DOI    10.1016/0167-4838(92)90249-D                                 
REMARK   1 REFERENCE 4                                                          
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.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 29744                          
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) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2974                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3991                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 440                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3303                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 437                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.47000                                             
REMARK   3    B22 (A**2) : -4.11000                                             
REMARK   3    B33 (A**2) : -6.36000                                             
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) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.73                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 56.56                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : XDICT_22141MOD.PARAM                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UA7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005609.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
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 ULTRAX 18                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31194                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 3.460                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, CALCIUM CHLORIDE, TRIS-        
REMARK 280  HCL, ACARBOSE, PH 7.2, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.16000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.86200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.10200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.86200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.16000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.10200            
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    LEU A 142       18.12     57.88                                   
REMARK 500    LEU A 244       34.03    -96.34                                   
REMARK 500    ASP A 259       -7.12    -56.58                                   
REMARK 500    TYR A 423      145.63    178.56                                   
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 982        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 983        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A 985        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 989        DISTANCE =  5.41 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GLC A  503                                                       
REMARK 610     ACI A  504                                                       
REMARK 610     G6D A  505                                                       
REMARK 610     BGC A  506                                                       
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 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 180   O                                                      
REMARK 620 2 HOH A 667   O    87.9                                              
REMARK 620 3 THR A 137   O    85.0  75.6                                        
REMARK 620 4 HOH A 608   O   118.4  69.5 136.3                                  
REMARK 620 5 ASN A 101   OD1  73.0 113.4 155.5  66.3                            
REMARK 620 6 ASP A 146   OD1 134.5 132.8 119.6  71.5  72.2                      
REMARK 620 7 ASP A 146   OD2 161.6  97.3  79.2  79.9 120.1  50.1                
REMARK 620 8 HOH A 798   O    80.9 148.6  74.2 141.2  91.4  71.7  85.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 716   O                                                      
REMARK 620 2 HOH A 796   O    70.1                                              
REMARK 620 3 HOH A 800   O    75.0  81.0                                        
REMARK 620 4 HOH A 801   O   147.3  97.2  73.3                                  
REMARK 620 5 GLY A 169   O   102.3 172.0  94.7  88.0                            
REMARK 620 6 ASP A 171   OD2  76.4  88.2 151.4 134.6  92.5                      
REMARK 620 7 ASP A 171   OD1 126.7  85.0 147.5  79.7 102.0  55.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 276   OE2                                                    
REMARK 620 2 GLY A 313   O   108.2                                              
REMARK 620 3 HOH A 795   O   148.9  88.1                                        
REMARK 620 4 HOH A 811   O    81.5 165.8  88.3                                  
REMARK 620 5 HOH A 905   O   131.7  78.9  76.3  86.8                            
REMARK 620 6 GLU A 276   OE1  52.8  88.0 157.0  90.0  80.7                      
REMARK 620 7 GLU A  89   OE2  72.3  96.1  80.0  96.8 155.9 123.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACI A 501                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLD A 502                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 503                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACI A 504                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6D A 505                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 506                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 602                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 603                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BAG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MALTOPENTAOSE                        
DBREF  1UA7 A    4   425  UNP    P00691   AMY_BACSU       45    466             
SEQADV 1UA7 PHE A  105  UNP  P00691    SER   146 SEE REMARK 999                 
SEQADV 1UA7 GLU A  163  UNP  P00691    ASP   204 SEE REMARK 999                 
SEQADV 1UA7 GLN A  356  UNP  P00691    ASN   397 ENGINEERED                     
SEQRES   1 A  422  PRO SER ILE LYS SER GLY THR ILE LEU HIS ALA TRP ASN          
SEQRES   2 A  422  TRP SER PHE ASN THR LEU LYS HIS ASN MET LYS ASP ILE          
SEQRES   3 A  422  HIS ASP ALA GLY TYR THR ALA ILE GLN THR SER PRO ILE          
SEQRES   4 A  422  ASN GLN VAL LYS GLU GLY ASN GLN GLY ASP LYS SER MET          
SEQRES   5 A  422  SER ASN TRP TYR TRP LEU TYR GLN PRO THR SER TYR GLN          
SEQRES   6 A  422  ILE GLY ASN ARG TYR LEU GLY THR GLU GLN GLU PHE LYS          
SEQRES   7 A  422  GLU MET CYS ALA ALA ALA GLU GLU TYR GLY ILE LYS VAL          
SEQRES   8 A  422  ILE VAL ASP ALA VAL ILE ASN HIS THR THR PHE ASP TYR          
SEQRES   9 A  422  ALA ALA ILE SER ASN GLU VAL LYS SER ILE PRO ASN TRP          
SEQRES  10 A  422  THR HIS GLY ASN THR GLN ILE LYS ASN TRP SER ASP ARG          
SEQRES  11 A  422  TRP ASP VAL THR GLN ASN SER LEU LEU GLY LEU TYR ASP          
SEQRES  12 A  422  TRP ASN THR GLN ASN THR GLN VAL GLN SER TYR LEU LYS          
SEQRES  13 A  422  ARG PHE LEU GLU ARG ALA LEU ASN ASP GLY ALA ASP GLY          
SEQRES  14 A  422  PHE ARG PHE ASP ALA ALA LYS HIS ILE GLU LEU PRO ASP          
SEQRES  15 A  422  ASP GLY SER TYR GLY SER GLN PHE TRP PRO ASN ILE THR          
SEQRES  16 A  422  ASN THR SER ALA GLU PHE GLN TYR GLY GLU ILE LEU GLN          
SEQRES  17 A  422  ASP SER ALA SER ARG ASP ALA ALA TYR ALA ASN TYR MET          
SEQRES  18 A  422  ASP VAL THR ALA SER ASN TYR GLY HIS SER ILE ARG SER          
SEQRES  19 A  422  ALA LEU LYS ASN ARG ASN LEU GLY VAL SER ASN ILE SER          
SEQRES  20 A  422  HIS TYR ALA SER ASP VAL SER ALA ASP LYS LEU VAL THR          
SEQRES  21 A  422  TRP VAL GLU SER HIS ASP THR TYR ALA ASN ASP ASP GLU          
SEQRES  22 A  422  GLU SER THR TRP MET SER ASP ASP ASP ILE ARG LEU GLY          
SEQRES  23 A  422  TRP ALA VAL ILE ALA SER ARG SER GLY SER THR PRO LEU          
SEQRES  24 A  422  PHE PHE SER ARG PRO GLU GLY GLY GLY ASN GLY VAL ARG          
SEQRES  25 A  422  PHE PRO GLY LYS SER GLN ILE GLY ASP ARG GLY SER ALA          
SEQRES  26 A  422  LEU PHE GLU ASP GLN ALA ILE THR ALA VAL ASN ARG PHE          
SEQRES  27 A  422  HIS ASN VAL MET ALA GLY GLN PRO GLU GLU LEU SER ASN          
SEQRES  28 A  422  PRO GLN GLY ASN ASN GLN ILE PHE MET ASN GLN ARG GLY          
SEQRES  29 A  422  SER HIS GLY VAL VAL LEU ALA ASN ALA GLY SER SER SER          
SEQRES  30 A  422  VAL SER ILE ASN THR ALA THR LYS LEU PRO ASP GLY ARG          
SEQRES  31 A  422  TYR ASP ASN LYS ALA GLY ALA GLY SER PHE GLN VAL ASN          
SEQRES  32 A  422  ASP GLY LYS LEU THR GLY THR ILE ASN ALA ARG SER VAL          
SEQRES  33 A  422  ALA VAL LEU TYR PRO ASP                                      
HET    ACI  A 501      12                                                       
HET    GLD  A 502      10                                                       
HET    GLC  A 503      11                                                       
HET    ACI  A 504      11                                                       
HET    G6D  A 505      10                                                       
HET    BGC  A 506      11                                                       
HET     CA  A 601       1                                                       
HET     CA  A 602       1                                                       
HET     CA  A 603       1                                                       
HETNAM     ACI 6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL               
HETNAM     GLD 4,6-DIDEOXYGLUCOSE                                               
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     G6D 6-DEOXY-ALPHA-D-GLUCOSE                                          
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  ACI    2(C7 H13 N O4)                                               
FORMUL   2  GLD    C6 H12 O4                                                    
FORMUL   2  GLC    C6 H12 O6                                                    
FORMUL   2  G6D    C6 H12 O5                                                    
FORMUL   2  BGC    C6 H12 O6                                                    
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  HOH   *437(H2 O)                                                    
HELIX    1   1 SER A   18  ASN A   25  1                                   8    
HELIX    2   2 ASN A   25  ALA A   32  1                                   8    
HELIX    3   3 GLY A   48  ASP A   52  5                                   5    
HELIX    4   4 SER A   54  TYR A   62  5                                   9    
HELIX    5   5 GLU A   77  GLU A   89  1                                  13    
HELIX    6   6 SER A  111  SER A  116  1                                   6    
HELIX    7   7 ASP A  132  ASN A  139  1                                   8    
HELIX    8   8 ASN A  151  ASP A  168  1                                  18    
HELIX    9   9 ALA A  177  ILE A  181  5                                   5    
HELIX   10  10 ASP A  186  GLY A  190  5                                   5    
HELIX   11  11 GLN A  192  THR A  198  1                                   7    
HELIX   12  12 ARG A  216  ASN A  222  1                                   7    
HELIX   13  13 ALA A  228  ARG A  242  1                                  15    
HELIX   14  14 GLY A  245  SER A  250  1                                   6    
HELIX   15  15 SER A  257  ASP A  259  5                                   3    
HELIX   16  16 SER A  267  ASN A  273  1                                   7    
HELIX   17  17 SER A  282  SER A  295  1                                  14    
HELIX   18  18 SER A  327  GLU A  331  5                                   5    
HELIX   19  19 ASP A  332  ALA A  346  1                                  15    
HELIX   20  20 ASN A  354  ASN A  358  5                                   5    
SHEET    1   A 9 ILE A  11  HIS A  13  0                                        
SHEET    2   A 9 ALA A  36  THR A  39  1  O  GLN A  38   N  LEU A  12           
SHEET    3   A 9 LYS A  93  ALA A  98  1  O  ILE A  95   N  ILE A  37           
SHEET    4   A 9 GLY A 172  PHE A 175  1  O  GLY A 172   N  VAL A  96           
SHEET    5   A 9 PHE A 204  GLY A 207  1  O  TYR A 206   N  PHE A 175           
SHEET    6   A 9 ASP A 225  THR A 227  1  O  ASP A 225   N  GLY A 207           
SHEET    7   A 9 LEU A 261  THR A 263  1  O  VAL A 262   N  VAL A 226           
SHEET    8   A 9 THR A 300  PHE A 304  1  O  LEU A 302   N  THR A 263           
SHEET    9   A 9 ILE A  11  HIS A  13  1  N  HIS A  13   O  PHE A 303           
SHEET    1   B 3 ASN A  43  VAL A  45  0                                        
SHEET    2   B 3 PRO A  64  ASN A  71 -1  O  THR A  65   N  GLN A  44           
SHEET    3   B 3 GLY A  75  THR A  76 -1  O  GLY A  75   N  ASN A  71           
SHEET    1   C 2 THR A 121  GLY A 123  0                                        
SHEET    2   C 2 ASP A 146  TRP A 147 -1  O  ASP A 146   N  GLY A 123           
SHEET    1   D 4 LEU A 352  SER A 353  0                                        
SHEET    2   D 4 ILE A 361  ARG A 366 -1  O  MET A 363   N  SER A 353           
SHEET    3   D 4 GLY A 370  ASN A 375 -1  O  ALA A 374   N  PHE A 362           
SHEET    4   D 4 SER A 418  LEU A 422 -1  O  SER A 418   N  ASN A 375           
SHEET    1   E 4 VAL A 381  ALA A 386  0                                        
SHEET    2   E 4 LYS A 409  ILE A 414 -1  O  LEU A 410   N  THR A 385           
SHEET    3   E 4 SER A 402  ASN A 406 -1  N  GLN A 404   O  THR A 411           
SHEET    4   E 4 GLY A 392  ASP A 395 -1  N  GLY A 392   O  VAL A 405           
LINK        CA    CA A 601                 O   HIS A 180     1555   1555  2.20  
LINK         N1  ACI A 501                 C4  GLD A 502     1555   1555  1.47  
LINK         O1  GLD A 502                 C4  GLC A 503     1555   1555  1.44  
LINK         O1  GLC A 503                 C4  ACI A 504     1555   1555  1.45  
LINK         O1  G6D A 505                 C4  BGC A 506     1555   1555  1.44  
LINK         N1  ACI A 504                 C4A G6D A 505     1555   1555  1.49  
LINK        CA    CA A 601                 O   HOH A 667     1555   1555  2.31  
LINK        CA    CA A 601                 O   THR A 137     1555   1555  2.43  
LINK        CA    CA A 601                 O   HOH A 608     1555   1555  2.38  
LINK        CA    CA A 601                 OD1 ASN A 101     1555   1555  2.54  
LINK        CA    CA A 601                 OD1 ASP A 146     1555   1555  2.55  
LINK        CA    CA A 601                 OD2 ASP A 146     1555   1555  2.62  
LINK        CA    CA A 601                 O   HOH A 798     1555   1555  2.47  
LINK        CA    CA A 602                 O   HOH A 716     1555   1555  2.63  
LINK        CA    CA A 602                 O   HOH A 796     1555   1555  2.43  
LINK        CA    CA A 602                 O   HOH A 800     1555   1555  2.41  
LINK        CA    CA A 602                 O   HOH A 801     1555   1555  2.45  
LINK        CA    CA A 602                 O   GLY A 169     1555   1555  2.30  
LINK        CA    CA A 602                 OD2 ASP A 171     1555   1555  2.33  
LINK        CA    CA A 602                 OD1 ASP A 171     1555   1555  2.34  
LINK        CA    CA A 603                 OE2 GLU A 276     1555   1555  2.41  
LINK        CA    CA A 603                 O   GLY A 313     1555   1555  2.30  
LINK        CA    CA A 603                 O   HOH A 795     1555   1555  2.39  
LINK        CA    CA A 603                 O   HOH A 811     1555   1555  2.50  
LINK        CA    CA A 603                 O   HOH A 905     1555   1555  2.29  
LINK        CA    CA A 603                 OE1 GLU A 276     1555   1555  2.52  
LINK        CA    CA A 603                 OE2 GLU A  89     1555   3555  2.55  
SITE     1 AC1  6 GLN A 126  LEU A 142  GLY A 143  GLD A 502                    
SITE     2 AC1  6 HOH A 645  HOH A 693                                          
SITE     1 AC2  6 LYS A  27  GLN A  63  PHE A 105  LEU A 142                    
SITE     2 AC2  6 ACI A 501  GLC A 503                                          
SITE     1 AC3 10 TRP A  58  TYR A  59  TYR A  62  GLN A  63                    
SITE     2 AC3 10 LEU A 142  ASP A 269  ASN A 273  GLD A 502                    
SITE     3 AC3 10 ACI A 504  HOH A 692                                          
SITE     1 AC4 10 TRP A  58  TYR A  62  HIS A 102  ARG A 174                    
SITE     2 AC4 10 ASP A 176  GLU A 208  HIS A 268  ASP A 269                    
SITE     3 AC4 10 GLC A 503  G6D A 505                                          
SITE     1 AC5  6 ALA A 177  HIS A 180  GLU A 208  LEU A 210                    
SITE     2 AC5  6 ACI A 504  BGC A 506                                          
SITE     1 AC6  6 TRP A 130  LYS A 179  ASP A 212  G6D A 505                    
SITE     2 AC6  6 HOH A 775  HOH A 960                                          
SITE     1 AC7  7 ASN A 101  THR A 137  ASP A 146  HIS A 180                    
SITE     2 AC7  7 HOH A 608  HOH A 667  HOH A 798                               
SITE     1 AC8  6 GLY A 169  ASP A 171  HOH A 716  HOH A 796                    
SITE     2 AC8  6 HOH A 800  HOH A 801                                          
SITE     1 AC9  6 GLU A  89  GLU A 276  GLY A 313  HOH A 795                    
SITE     2 AC9  6 HOH A 811  HOH A 905                                          
CRYST1   70.320   74.204  115.724  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      0.014221  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013476  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008641        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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