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PDBsum entry 1wo2

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Hydrolase PDB id
1wo2
Jmol
Contents
Protein chain
496 a.a.
Ligands
GLC-GLC-BGC ×2
GLC-BGC
EDO ×6
Metals
_CL
_CA
Waters ×749
HEADER    HYDROLASE                               11-AUG-04   1WO2
TITLE     CRYSTAL STRUCTURE OF THE PIG PANCREATIC ALPHA-AMYLASE
TITLE    2 COMPLEXED WITH MALTO-OLIGOSAACHARIDES UNDER THE EFFECT OF
TITLE    3 THE CHLORIDE ION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   5 EC: 3.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 TISSUE: PANCREAS
KEYWDS    BETA-ALPHA-BARRELS, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.QIAN,F.PAYAN,V.NAHOUM
REVDAT   3   04-AUG-09 1WO2    1       HETATM HETNAM
REVDAT   2   24-FEB-09 1WO2    1       VERSN
REVDAT   1   15-MAR-05 1WO2    0
JRNL        AUTH   M.QIAN,E.H.AJANDOUZ,F.PAYAN,V.NAHOUM
JRNL        TITL   MOLECULAR BASIS OF THE EFFECTS OF CHLORIDE ION ON
JRNL        TITL 2 THE ACID-BASE CATALYST IN THE MECHANISM OF
JRNL        TITL 3 PANCREATIC ALPHA-AMYLASE
JRNL        REF    BIOCHEMISTRY                  V.  44  3194 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15736930
JRNL        DOI    10.1021/BI048201T
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.QIAN,V.NAHOUM,J.BONICEL,H.BISCHOFF,B.HENRISSAT,
REMARK   1  AUTH 2 F.PAYAN
REMARK   1  TITL   ENZYME-CATALYZED CONDENSATION REACTION IN A
REMARK   1  TITL 2 MAMMALIAN ALPHA-AMYLASE. HIGH-RESOLUTION STRUCTURAL
REMARK   1  TITL 3 ANALYSIS OF AN ENZYME-INHIBITOR COMPLEX
REMARK   1  REF    BIOCHEMISTRY                  V.  40  7700 2001
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   11412124
REMARK   1  DOI    10.1021/BI0102050
REMARK   1 REFERENCE 2
REMARK   1  AUTH   F.PAYAN,M.QIAN
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE PIG PANCREATIC
REMARK   1  TITL 2 ALPHA-AMYLASE COMPLEXED WITH MALTO-OLIGOSACCHARIDES
REMARK   1  REF    J.PROTEIN CHEM.               V.  22   275 2003
REMARK   1  REFN                   ISSN 0277-8033
REMARK   1  PMID   12962327
REMARK   1  DOI    10.1023/A:1025072520607
REMARK   2
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.843
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.6
REMARK   3   NUMBER OF REFLECTIONS             : 61363
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.184
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2479
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3956
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 117
REMARK   3   SOLVENT ATOMS            : 749
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 15.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.38
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.25
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1WO2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB023800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61363
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.17300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, CALCIUM CHLORIDE, SODIUM
REMARK 280  CHLORIDE, PH 8, EVAPORATION, TEMPERATURE 277K
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       35.04500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.61050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.64900
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.61050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.04500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.64900
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  31      -60.94   -140.14
REMARK 500    MET A 102     -143.59   -110.85
REMARK 500    ASP A 317       55.47   -118.13
REMARK 500    SER A 414     -104.79   -133.69
REMARK 500    ASP A 433       35.16    -88.92
REMARK 500    PRO A 486       42.84    -73.96
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     TRP A  59        25.0      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 A1199        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH A1409        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A1433        DISTANCE =  6.24 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 500  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100   OD1
REMARK 620 2 ARG A 158   O   151.9
REMARK 620 3 ASP A 167   OD1  84.0 121.3
REMARK 620 4 ASP A 167   OD2 128.8  79.3  51.8
REMARK 620 5 HIS A 201   O    71.1  81.1 138.8 159.6
REMARK 620 6 HOH A 520   O    71.1 123.8  75.4  73.3 123.2
REMARK 620 7 HOH A 539   O    97.7  73.2 135.6  98.1  81.4  63.7
REMARK 620 8 HOH A 527   O   100.9  78.5  71.7  89.6  81.1 146.8 148.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1990
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1991
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1992
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1994
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1995
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1996
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1998
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1999
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2000
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2001
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2002
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HX0   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH THE "TRUNCATE" ACARBOSE
REMARK 900 MOLECULE (PSEUDOTRISACCHARIDE)
REMARK 900 RELATED ID: 1UA3   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MALTO-OLIGOSACCHARIDES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE CONFLICTS ARE EXPLAINED IN REFERENCE AS FOLLOWING,
REMARK 999 M.QIAN,R.HASER,F.PAYAN
REMARK 999 STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG
REMARK 999 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION
REMARK 999 (J.MOL.BIOL. V. 231 785 1993)
DBREF  1WO2 A    1   496  UNP    P00690   AMYP_PIG        16    511
SEQADV 1WO2 PCA A    1  UNP  P00690    GLN    16 ENGINEERED
SEQADV 1WO2 LYS A  243  UNP  P00690    GLN   258 SEE REMARK 999
SEQADV 1WO2 SER A  310  UNP  P00690    ALA   325 SEE REMARK 999
SEQADV 1WO2 ILE A  323  UNP  P00690    VAL   338 SEE REMARK 999
SEQADV 1WO2 GLU A  352  UNP  P00690    GLN   367 SEE REMARK 999
SEQADV 1WO2 GLU A  390  UNP  P00690    GLN   405 SEE REMARK 999
SEQADV 1WO2 ASP A  411  UNP  P00690    ALA   426 SEE REMARK 999
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES  10 A  496  TYR CYS ASN PRO GLY ASN ARG GLU PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES  39 A  496  LYS LEU
MODRES 1WO2 PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET    GLC  A1990      11
HET    GLC  A1991      11
HET    BGC  A1992      12
HET    GLC  A1994      11
HET    GLC  A1995      11
HET    BGC  A1996      12
HET    GLC  A1998      11
HET    BGC  A1999      12
HET     CL  A 498       1
HET     CA  A 500       1
HET    EDO  A2000       4
HET    EDO  A2001       4
HET    EDO  A2002       4
HET    EDO  A2003       4
HET    EDO  A2004       4
HET    EDO  A2005       4
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  GLC    5(C6 H12 O6)
FORMUL   2  BGC    3(C6 H12 O6)
FORMUL   5   CL    CL 1-
FORMUL   6   CA    CA 2+
FORMUL   7  EDO    6(C2 H6 O2)
FORMUL  13  HOH   *749(H2 O)
HELIX    1   1 ARG A   20  TYR A   31  1                                  12
HELIX    2   2 PRO A   57  GLN A   63  5                                   7
HELIX    3   3 ASN A   75  VAL A   89  1                                  15
HELIX    4   4 ASN A  120  ARG A  124  5                                   5
HELIX    5   5 SER A  132  PHE A  136  5                                   5
HELIX    6   6 ASP A  153  CYS A  160  1                                   8
HELIX    7   7 LYS A  172  GLY A  190  1                                  19
HELIX    8   8 ALA A  198  MET A  202  5                                   5
HELIX    9   9 TRP A  203  ASP A  212  1                                  10
HELIX   10  10 LYS A  243  PHE A  248  5                                   6
HELIX   11  11 PHE A  256  ARG A  267  1                                  12
HELIX   12  12 LYS A  273  TRP A  280  5                                   8
HELIX   13  13 GLY A  281  GLY A  285  5                                   5
HELIX   14  14 PRO A  288  ASP A  290  5                                   3
HELIX   15  15 ASP A  300  GLY A  304  5                                   5
HELIX   16  16 GLY A  308  ILE A  312  5                                   5
HELIX   17  17 THR A  314  TRP A  316  5                                   3
HELIX   18  18 ASP A  317  HIS A  331  1                                  15
HELIX   19  19 CYS A  384  ARG A  387  5                                   4
HELIX   20  20 TRP A  388  VAL A  401  1                                  14
HELIX   21  21 GLU A  493  LYS A  495  5                                   3
SHEET    1   A 9 SER A  12  LEU A  16  0
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLN A  41   N  VAL A  14
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  ARG A 195   N  ALA A  97
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 229   N  PHE A 194
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  GLN A 232
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  LEU A 293   N  VAL A 253
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294
SHEET    9   A 9 SER A  12  LEU A  16  1  N  ILE A  13   O  VAL A 338
SHEET    1   B 2 HIS A 101  GLY A 104  0
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  CYS A 103
SHEET    1   C 2 PHE A 348  VAL A 349  0
SHEET    2   C 2 GLU A 352  ASP A 353 -1  O  GLU A 352   N  VAL A 349
SHEET    1   D 2 ASN A 362  ASN A 363  0
SHEET    2   D 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363
SHEET    1   E 4 PHE A 406  ASP A 411  0
SHEET    2   E 4 GLN A 416  ARG A 421 -1  O  GLY A 420   N  ALA A 407
SHEET    3   E 4 GLY A 425  ASN A 430 -1  O  PHE A 429   N  VAL A 417
SHEET    4   E 4 PHE A 487  HIS A 491 -1  O  ILE A 488   N  VAL A 428
SHEET    1   F 2 LEU A 436  GLN A 441  0
SHEET    2   F 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440
SHEET    1   G 2 GLY A 447  CYS A 450  0
SHEET    2   G 2 LYS A 466  VAL A 469 -1  O  VAL A 469   N  GLY A 447
SHEET    1   H 2 LYS A 457  VAL A 458  0
SHEET    2   H 2 SER A 461  CYS A 462 -1  O  SER A 461   N  VAL A 458
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.04
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.03
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.34
LINK         OD1 ASN A 100                CA    CA A 500     1555   1555  2.43
LINK         O   ARG A 158                CA    CA A 500     1555   1555  2.37
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.53
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.49
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.39
LINK         C1  GLC A1990                 O4  GLC A1991     1555   1555  1.40
LINK         C1  GLC A1991                 O4  BGC A1992     1555   1555  1.41
LINK         C1  GLC A1994                 O4  GLC A1995     1555   1555  1.40
LINK         C1  GLC A1995                 O4  BGC A1996     1555   1555  1.40
LINK         C1  GLC A1998                 O4  BGC A1999     1555   1555  1.41
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.61
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.59
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.45
CISPEP   1 ASN A   53    PRO A   54          0        -0.08
CISPEP   2 VAL A  129    PRO A  130          0        -0.66
SITE     1 AC1  6 GLN A  63  VAL A 163  HOH A1207  HOH A1218
SITE     2 AC1  6 GLC A1991  EDO A2002
SITE     1 AC2  9 TRP A  58  TRP A  59  TYR A  62  GLN A  63
SITE     2 AC2  9 ASP A 300  HOH A1159  HOH A1160  GLC A1990
SITE     3 AC2  9 BGC A1992
SITE     1 AC3 12 TRP A  58  TYR A  62  HIS A 101  ARG A 195
SITE     2 AC3 12 ASP A 197  ALA A 198  GLU A 233  HIS A 299
SITE     3 AC3 12 ASP A 300  HOH A1163  HOH A1267  GLC A1991
SITE     1 AC4  7 THR A  52  ASN A  53  LYS A 261  GLY A 283
SITE     2 AC4  7 TRP A 284  HOH A 743  GLC A1995
SITE     1 AC5  7 THR A  52  GLU A 272  TYR A 276  ASN A 279
SITE     2 AC5  7 HOH A1170  GLC A1994  BGC A1996
SITE     1 AC6  9 ALA A 108  TYR A 276  HOH A 879  HOH A1040
SITE     2 AC6  9 HOH A1051  HOH A1170  HOH A1213  HOH A1216
SITE     3 AC6  9 GLC A1995
SITE     1 AC7 10 ASP A 375  THR A 376  ARG A 387  TRP A 388
SITE     2 AC7 10 ARG A 389  GLU A 390  ARG A 392  HOH A 950
SITE     3 AC7 10 HOH A1138  BGC A1999
SITE     1 AC8  8 ALA A 318  LYS A 322  TRP A 388  GLU A 390
SITE     2 AC8  8 HOH A 661  HOH A1430  HOH A1509  GLC A1998
SITE     1 AC9  5 ARG A 195  GLU A 233  ASN A 298  ARG A 337
SITE     2 AC9  5 HOH A 525
SITE     1 BC1  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 BC1  7 HOH A 520  HOH A 527  HOH A 539
SITE     1 BC2  8 LYS A 213  LEU A 214  HIS A 215  LYS A 466
SITE     2 BC2  8 VAL A 467  TYR A 468  HOH A 717  EDO A2001
SITE     1 BC3  6 VAL A 467  GLN A 476  PHE A 477  SER A 478
SITE     2 BC3  6 HOH A1146  EDO A2000
SITE     1 BC4  5 TRP A  59  GLN A  63  HOH A 877  HOH A1208
SITE     2 BC4  5 GLC A1990
SITE     1 BC5  6 ARG A  30  ILE A 372  THR A 376  ARG A 387
SITE     2 BC5  6 HOH A 872  HOH A1007
SITE     1 BC6  6 PCA A   1  LEU A 211  ARG A 227  PRO A 228
SITE     2 BC6  6 ILE A 230  HOH A 939
SITE     1 BC7  5 ARG A  56  THR A 114  HOH A 654  HOH A1225
SITE     2 BC7  5 HOH A1230
CRYST1   70.090  113.298  117.221  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      0.014267  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008826  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008531        0.00000
      
PROCHECK
Go to PROCHECK summary
 References