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PDBsum entry 7taa

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Hydrolase PDB id
7taa
Jmol
Contents
Protein chain
476 a.a.
Ligands
ABC
Metals
_CA
Waters ×465
HEADER    HYDROLASE                               06-OCT-97   7TAA
TITLE     FAMILY 13 ALPHA AMYLASE IN COMPLEX WITH ACARBOSE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TAKA AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE   3 ORGANISM_TAXID: 5062
KEYWDS    HYDROLASE, GLYCOSYL HYDROLASE, TAKA, AMYLASE, ACARBOSE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.J.DAVIES,A.M.BRZOZOWSKI
REVDAT   2   24-FEB-09 7TAA    1       VERSN
REVDAT   1   25-NOV-98 7TAA    0
JRNL        AUTH   A.M.BRZOZOWSKI,G.J.DAVIES
JRNL        TITL   STRUCTURE OF THE ASPERGILLUS ORYZAE ALPHA-AMYLASE
JRNL        TITL 2 COMPLEXED WITH THE INHIBITOR ACARBOSE AT 2.0 A
JRNL        TITL 3 RESOLUTION.
JRNL        REF    BIOCHEMISTRY                  V.  36 10837 1997
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   9283074
JRNL        DOI    10.1021/BI970539I
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0
REMARK   3   NUMBER OF REFLECTIONS             : 31015
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1553
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3688
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : 66
REMARK   3   SOLVENT ATOMS            : 465
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.014 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.033 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.037 ; 0.050
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.136 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.176 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.184 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.173 ; 0.300
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 4.300 ; 7.000
REMARK   3    STAGGERED                 (DEGREES) : 18.300; 20.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.266 ; 4.000
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.941 ; 6.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.183 ; 6.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.423 ; 8.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 7TAA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 1995
REMARK 200  TEMPERATURE           (KELVIN) : 120
REMARK 200  PH                             : 7.5
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
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : LONG MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63935
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.08800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NATIVE STRUCTURE
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   (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% MM PEG 5000, 5MM CALCIUM
REMARK 280  CHLORIDE, 0.1M HEPES BUFFER, PH 7.5. METHOD: HANGING DROP
REMARK 280  VAPOUR DIFFUSION. THE NATIVE CRYSTALS WERE SOAKED FOR 6 HOURS
REMARK 280  IN STABILIZING SOLUTION CONTAINING 15 MM OF ACARBOSE., VAPOR
REMARK 280  DIFFUSION - HANGING DROP
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       25.52000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.78000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.59150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.78000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.52000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.59150
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     SER A   477
REMARK 465     SER A   478
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   O    HOH A   554     O    HOH A   592              1.98
REMARK 500   O    HOH A   554     O    HOH A   684              2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   570     O    HOH A   762     3655     2.09
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    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP A  50   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TYR A  94   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR A  94   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    GLU A 109   OE1 -  CD  -  OE2 ANGL. DEV. =   8.3 DEGREES
REMARK 500    ASP A 206   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    CYS A 283   CA  -  CB  -  SG  ANGL. DEV. =  10.4 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    PHE A  19      -60.68    -92.75
REMARK 500    CYS A  30       84.39   -150.65
REMARK 500    ALA A  78       48.53    -86.23
REMARK 500    TRP A  83       67.45   -115.12
REMARK 500    SER A 141       20.75    -71.72
REMARK 500    ASP A 168     -159.49   -153.23
REMARK 500    THR A 207       44.27     39.79
REMARK 500    ASP A 340      124.91    -37.20
REMARK 500    ALA A 456      149.62   -176.89
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 831        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 909        DISTANCE =  5.62 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 480  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 210   O
REMARK 620 2 GLU A 162   O    80.3
REMARK 620 3 ASP A 175   OD2 163.3  83.2
REMARK 620 4 HOH A 505   O    80.7  70.4  91.2
REMARK 620 5 ASN A 121   OD1  77.2 154.9 119.5 116.2
REMARK 620 6 ASP A 175   OD1 139.4 116.0  52.4 139.0  76.1
REMARK 620 7 HOH A 492   O   116.4 128.3  72.4  65.5  72.7  83.7
REMARK 620 8 HOH A 507   O    78.2  76.6 100.6 143.2  88.0  70.8 151.2
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 ABC A 479
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 480
DBREF  7TAA A    1   478  UNP    P10529   AMYA_ASPOR      22    499
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER
HET    ABC  A 479      64
HET     CA  A 480       1
HETNAM     ABC MODIFIED ACARBOSE HEXASACCHARIDE
HETNAM      CA CALCIUM ION
FORMUL   2  ABC    C37 H63 N O26
FORMUL   3   CA    CA 2+
FORMUL   4  HOH   *465(H2 O)
HELIX    1   1 PRO A    3  SER A    8  1                                   6
HELIX    2   2 THR A   16  PHE A   19  1                                   4
HELIX    3   3 THR A   32  ASP A   34  5                                   3
HELIX    4   4 TRP A   42  MET A   55  1                                  14
HELIX    5   5 ALA A   97  ARG A  110  1                                  14
HELIX    6   6 GLY A  129  SER A  131  5                                   3
HELIX    7   7 TYR A  134  VAL A  136  5                                   3
HELIX    8   8 GLN A  143  TYR A  145  5                                   3
HELIX    9   9 GLN A  158  ASP A  163  1                                   6
HELIX   10  10 ASP A  181  TYR A  198  1                                  18
HELIX   11  11 VAL A  208  HIS A  210  5                                   3
HELIX   12  12 LYS A  213  ALA A  223  1                                  11
HELIX   13  13 PRO A  236  ASN A  244  1                                   9
HELIX   14  14 TYR A  252  LYS A  263  1                                  12
HELIX   15  15 MET A  269  ASP A  282  1                                  14
HELIX   16  16 SER A  286  LEU A  288  5                                   3
HELIX   17  17 PHE A  301  TYR A  304  1                                   4
HELIX   18  18 ILE A  308  LEU A  320  1                                  13
HELIX   19  19 GLN A  331  GLN A  333  5                                   3
HELIX   20  20 THR A  347  SER A  350  5                                   4
HELIX   21  21 GLU A  357  LYS A  375  1                                  19
HELIX   22  22 GLU A  467  LEU A  469  5                                   3
SHEET    1   A 6 PRO A 325  TYR A 328  0
SHEET    2   A 6 SER A  10  LEU A  14  1  N  ILE A  11   O  PRO A 325
SHEET    3   A 6 ALA A  59  ILE A  62  1  N  ALA A  59   O  TYR A  12
SHEET    4   A 6 TYR A 113  VAL A 118  1  N  TYR A 113   O  ILE A  60
SHEET    5   A 6 GLY A 202  ILE A 205  1  N  GLY A 202   O  VAL A 116
SHEET    6   A 6 TYR A 226  GLY A 229  1  N  TYR A 226   O  LEU A 203
SHEET    1   B 6 THR A 441  THR A 444  0
SHEET    2   B 6 GLN A 433  GLU A 436 -1  N  GLU A 436   O  THR A 441
SHEET    3   B 6 ARG A 461  PRO A 465 -1  N  TYR A 464   O  THR A 435
SHEET    4   B 6 ILE A 405  SER A 410 -1  N  ILE A 408   O  ARG A 461
SHEET    5   B 6 THR A 393  LYS A 398 -1  N  LYS A 398   O  ILE A 405
SHEET    6   B 6 TRP A 385  ASP A 390 -1  N  ASP A 390   O  THR A 393
SHEET    1   C 2 TYR A 419  LEU A 423  0
SHEET    2   C 2 VAL A 451  MET A 455 -1  N  MET A 455   O  TYR A 419
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.05
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.07
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  1.93
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  1.98
LINK        CA    CA A 480                 O   HIS A 210     1555   1555  2.54
LINK        CA    CA A 480                 O   GLU A 162     1555   1555  2.51
LINK        CA    CA A 480                 OD2 ASP A 175     1555   1555  2.54
LINK        CA    CA A 480                 O   HOH A 505     1555   1555  2.76
LINK        CA    CA A 480                 OD1 ASN A 121     1555   1555  2.52
LINK        CA    CA A 480                 OD1 ASP A 175     1555   1555  2.54
LINK        CA    CA A 480                 O   HOH A 492     1555   1555  2.41
LINK        CA    CA A 480                 O   HOH A 507     1555   1555  2.46
CISPEP   1 LYS A  138    PRO A  139          0         8.63
CISPEP   2 ASP A  340    PRO A  341          0         7.94
SITE     1 AC1 26 GLN A  35  TYR A  82  TRP A  83  HIS A 122
SITE     2 AC1 26 TYR A 155  ARG A 204  ASP A 206  THR A 207
SITE     3 AC1 26 LYS A 209  HIS A 210  GLU A 230  LEU A 232
SITE     4 AC1 26 ASP A 233  GLY A 234  TYR A 256  HIS A 296
SITE     5 AC1 26 ASP A 297  ASP A 340  ARG A 344  HOH A 513
SITE     6 AC1 26 HOH A 537  HOH A 563  HOH A 653  HOH A 693
SITE     7 AC1 26 HOH A 722  HOH A 751
SITE     1 AC2  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210
SITE     2 AC2  7 HOH A 492  HOH A 505  HOH A 507
CRYST1   51.040   67.183  133.560  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      0.019592  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014885  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007487        0.00000
      
PROCHECK
Go to PROCHECK summary
 References