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PDBsum entry 1ua7

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Hydrolase PDB id
1ua7
Jmol
Contents
Protein chain
422 a.a. *
Ligands
ACI-GLD-GLC-ACI-
G6D-BGC
Metals
_CA ×3
Waters ×437
* Residue conservation analysis
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   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   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
      
PROCHECK
Go to PROCHECK summary
 References