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PDBsum entry 1ua3

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Hydrolase PDB id
1ua3
Jmol
Contents
Protein chain
496 a.a. *
Ligands
BGC
MAL
MLR ×2
EDO-EDO
EDO ×4
Metals
_CL ×2
_CA
Waters ×759
* Residue conservation analysis
HEADER    HYDROLASE                               27-FEB-03   1UA3
TITLE     CRYSTAL STRUCTURE OF THE PIG PANCREATIC A-AMYLASE COMPLEXED
TITLE    2 WITH MALTO-OLIGOSACCHARIDES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;
COMPND   3 CHAIN: A;
COMPND   4 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
KEYWDS    BETA-ALPHA-BARRELS, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.PAYAN,M.QIAN
REVDAT   3   04-AUG-09 1UA3    1       FORMUL HET    HETATM HETNAM
REVDAT   3 2                   1       SITE
REVDAT   2   24-FEB-09 1UA3    1       VERSN
REVDAT   1   14-OCT-03 1UA3    0
JRNL        AUTH   F.PAYAN,M.QIAN
JRNL        TITL   CRYSTAL STRUCTURE OF THE PIG PANCREATIC
JRNL        TITL 2 ALPHA-AMYLASE COMPLEXED WITH MALTO-OLIGOSACCHARIDES
JRNL        REF    J.PROTEIN CHEM.               V.  22   275 2003
JRNL        REFN                   ISSN 0277-8033
JRNL        PMID   12962327
JRNL        DOI    10.1023/A:1025072520607
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.QIAN,S.SPINELLI,H.DRIGUEZ,F.PAYAN
REMARK   1  TITL   STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A
REMARK   1  TITL 2 SUBSTRATE ANALOGUE AT 2.03 A RESOLUTION
REMARK   1  REF    PROTEIN SCI.                  V.   6  2285 1997
REMARK   1  REFN                   ISSN 0961-8368
REMARK   2
REMARK   2 RESOLUTION.    2.01 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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
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)   (%) : 98.3
REMARK   3   NUMBER OF REFLECTIONS             : 61298
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) : 0.175
REMARK   3   FREE R VALUE                     : 0.196
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1849
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            : 3939
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 129
REMARK   3   SOLVENT ATOMS            : 759
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) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 0.85
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.00
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 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 1UA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-MAR-03.
REMARK 100 THE RCSB ID CODE IS RCSB005605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-96
REMARK 200  TEMPERATURE           (KELVIN) : 298.0
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU 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          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61298
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) : 0.05500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.21800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.600
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   (%): 63.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, CALSIUM CHLORIDE,
REMARK 280  PH 8.0, LIQUID DIFFUSION, 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       34.89050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.46200
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.59150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.46200
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.89050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.59150
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLN A   1    N
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O2   EDO A  2000     C1   EDO A  2001              1.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLN A   1   OE1 -  CD  -  NE2 ANGL. DEV. =  17.1 DEGREES
REMARK 500    GLN A   1   CG  -  CD  -  NE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    TYR A  31      -60.65   -143.73
REMARK 500    CYS A  70       93.70   -161.80
REMARK 500    MET A 102     -140.97   -101.14
REMARK 500    VAL A 163       54.20     27.28
REMARK 500    ASP A 317       60.07   -110.03
REMARK 500    SER A 414     -106.23   -132.36
REMARK 500    ASP A 433       35.27    -88.27
REMARK 500    PRO A 486       43.38    -82.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ARG A  303     GLY A  304                  137.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  20         0.12    SIDE_CHAIN
REMARK 500    ARG A 303         0.17    SIDE_CHAIN
REMARK 500    ARG A 343         0.11    SIDE_CHAIN
REMARK 500    ARG A 392         0.10    SIDE_CHAIN
REMARK 500    ARG A 421         0.09    SIDE_CHAIN
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 706        DISTANCE = 12.36 ANGSTROMS
REMARK 525    HOH A 761        DISTANCE =  6.40 ANGSTROMS
REMARK 525    HOH A 782        DISTANCE =  7.67 ANGSTROMS
REMARK 525    HOH A 815        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A 849        DISTANCE =  5.76 ANGSTROMS
REMARK 525    HOH A1054        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH A1213        DISTANCE =  6.10 ANGSTROMS
REMARK 525    HOH A1298        DISTANCE =  7.00 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     EDO A 2001
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   153.9
REMARK 620 3 ASP A 167   OD1  83.7 120.3
REMARK 620 4 ASP A 167   OD2 127.0  79.0  49.2
REMARK 620 5 HIS A 201   O    71.4  82.9 140.2 160.6
REMARK 620 6 HOH A 527   O    99.7  80.9  71.1  87.8  82.6
REMARK 620 7 HOH A 520   O    69.7 123.1  75.5  75.3 121.1 145.9
REMARK 620 8 HOH A 539   O    99.9  72.0 132.6  97.4  83.3 150.8  62.3
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 BGC A 1997
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL A 1998
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 499
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLR A 1990
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLR A 1994
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2000
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2001
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2002
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004
REMARK 800 SITE_IDENTIFIER: BC4
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: 1JFH   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A SUBSTRATE ANALOGUE
DBREF  1UA3 A    1   496  UNP    P00690   AMYP_PIG         1    496
SEQADV 1UA3 ASN A  123  UNP  P00690    SER   123 CONFLICT
SEQADV 1UA3 LYS A  243  UNP  P00690    GLN   243 CONFLICT
SEQADV 1UA3 SER A  310  UNP  P00690    ALA   310 CONFLICT
SEQADV 1UA3 ILE A  323  UNP  P00690    VAL   323 CONFLICT
SEQADV 1UA3 GLN A  404  UNP  P00690    GLU   404 CONFLICT
SEQRES   1 A  496  GLN 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
HET    BGC  A1997      12
HET    MAL  A1998      23
HET     CL  A 498       1
HET     CL  A 499       1
HET     CA  A 500       1
HET    MLR  A1990      34
HET    MLR  A1994      34
HET    EDO  A2000       4
HET    EDO  A2001       3
HET    EDO  A2002       4
HET    EDO  A2003       4
HET    EDO  A2004       4
HET    EDO  A2005       4
HETNAM     BGC BETA-D-GLUCOSE
HETNAM     MAL MALTOSE
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
HETNAM     MLR MALTOTRIOSE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     MLR AMYLOTRIOSE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   2  BGC    C6 H12 O6
FORMUL   3  MAL    C12 H22 O11
FORMUL   4   CL    2(CL 1-)
FORMUL   6   CA    CA 2+
FORMUL   7  MLR    2(C18 H32 O16)
FORMUL   9  EDO    6(C2 H6 O2)
FORMUL  15  HOH   *759(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  ASP A  402  1                                  15
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  THR A 254   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  PHE A 477   N  SER A 438
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         OD1 ASN A 100                CA    CA A 500     1555   1555  2.54
LINK         O   ARG A 158                CA    CA A 500     1555   1555  2.49
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.65
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.64
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.49
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.62
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.66
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.70
CISPEP   1 ASN A   53    PRO A   54          0        -3.12
CISPEP   2 VAL A  129    PRO A  130          0        -6.60
SITE     1 AC1  9 LYS A 140  TRP A 203  GLY A 205  ASP A 206
SITE     2 AC1  9  CL A 499  HOH A 577  HOH A1027  HOH A1082
SITE     3 AC1  9 HOH A1197
SITE     1 AC2 16 ALA A 318  LYS A 322  THR A 376  THR A 377
SITE     2 AC2 16 ARG A 387  TRP A 388  ARG A 389  GLU A 390
SITE     3 AC2 16 HOH A 661  HOH A 750  HOH A 967  HOH A1035
SITE     4 AC2 16 HOH A1080  HOH A1162  HOH A1198  HOH A1199
SITE     1 AC3  3 ARG A 195  ASN A 298  ARG A 337
SITE     1 AC4  4 TRP A 203  PRO A 204  GLY A 205  BGC A1997
SITE     1 AC5  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC5  7 HOH A 520  HOH A 527  HOH A 539
SITE     1 AC6 16 TRP A  58  TRP A  59  TYR A  62  GLN A  63
SITE     2 AC6 16 HIS A 101  GLY A 104  VAL A 163  ARG A 195
SITE     3 AC6 16 ASP A 197  GLU A 233  HIS A 299  ASP A 300
SITE     4 AC6 16 HOH A 812  HOH A1092  HOH A1187  HOH A1190
SITE     1 AC7 15 THR A  52  ASN A  53  ALA A 108  LYS A 261
SITE     2 AC7 15 GLU A 272  TYR A 276  ASN A 279  GLY A 283
SITE     3 AC7 15 TRP A 284  HOH A1134  HOH A1146  HOH A1191
SITE     4 AC7 15 HOH A1193  HOH A1195  HOH A1282
SITE     1 AC8  4 SER A 132  ASP A 135  TYR A 174  EDO A2001
SITE     1 AC9  4 ASP A 135  LYS A 172  TYR A 174  EDO A2000
SITE     1 BC1  5 THR A 114  CYS A 115  GLY A 116  HOH A1025
SITE     2 BC1  5 HOH A1266
SITE     1 BC2  9 LYS A 213  LEU A 214  HIS A 215  LYS A 466
SITE     2 BC2  9 VAL A 467  TYR A 468  HOH A 841  HOH A1307
SITE     3 BC2  9 EDO A2004
SITE     1 BC3  7 LYS A 466  VAL A 467  GLN A 476  PHE A 477
SITE     2 BC3  7 SER A 478  HOH A1307  EDO A2003
SITE     1 BC4  5 ARG A  30  THR A 376  ARG A 387  HOH A1256
SITE     2 BC4  5 HOH A1287
CRYST1   69.781  113.183  116.924  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      0.014331  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008835  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008553        0.00000
      
PROCHECK
Go to PROCHECK summary
 References