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PDBsum entry 1xd0

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Hydrolase PDB id
1xd0
Jmol
Contents
Protein chain
496 a.a.
Ligands
NAG
ARE
Metals
_CL
_CA
Waters ×142
HEADER    HYDROLASE                               03-SEP-04   1XD0
TITLE     ACARBOSE REARRANGEMENT MECHANISM IMPLIED BY THE KINETIC AND STRUCTURAL
TITLE    2 ANALYSIS OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH ANALOGUES
TITLE    3 AND THEIR ELONGATED COUNTERPARTS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE, PANCREATIC ALPHA-
COMPND   5 AMYLASE, PA;
COMPND   6 EC: 3.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AMY2A;
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS    AMYLASE, ACARBOSE, ACARBOSE ANALOGUES, INHIBITOR, ACARVIOSINE,
KEYWDS   2 ISOACARBOSE, ENZYME, CATALYSIS, ENZYME MECHANISM, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.LI,A.BEGUM,S.NUMAO,K.H.PARK,S.G.WITHERS,G.D.BRAYER
REVDAT   4   13-JUL-11 1XD0    1       VERSN
REVDAT   3   24-FEB-09 1XD0    1       VERSN
REVDAT   2   15-MAR-05 1XD0    1       JRNL
REVDAT   1   07-DEC-04 1XD0    0
JRNL        AUTH   C.LI,A.BEGUM,S.NUMAO,K.H.PARK,S.G.WITHERS,G.D.BRAYER
JRNL        TITL   ACARBOSE REARRANGEMENT MECHANISM IMPLIED BY THE KINETIC AND
JRNL        TITL 2 STRUCTURAL ANALYSIS OF HUMAN PANCREATIC ALPHA-AMYLASE IN
JRNL        TITL 3 COMPLEX WITH ANALOGUES AND THEIR ELONGATED COUNTERPARTS
JRNL        REF    BIOCHEMISTRY                  V.  44  3347 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15736945
JRNL        DOI    10.1021/10.1021/BI048334E
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 30887
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                     : 0.199
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1540
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            : 3946
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 71
REMARK   3   SOLVENT ATOMS            : 142
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 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) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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 1XD0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-04.
REMARK 100 THE RCSB ID CODE IS RCSB030220.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : MIRRORS
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   : 30887
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYLPENTANE-2,4-DIOL, PH 7.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       26.45000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.45000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.45000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.45000
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      -58.93   -140.16
REMARK 500    MET A 102     -148.35   -112.69
REMARK 500    LEU A 217      150.30    -42.60
REMARK 500    ASP A 317       50.31   -106.17
REMARK 500    SER A 414     -110.55   -123.54
REMARK 500    PRO A 486       37.66    -73.28
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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        24.7      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 498  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 167   OD1
REMARK 620 2 HOH A 546   O   133.7
REMARK 620 3 ASN A 100   OD1  83.2 102.3
REMARK 620 4 HIS A 201   O   141.6  81.8  73.6
REMARK 620 5 ASP A 167   OD2  52.4  94.7 129.4 156.7
REMARK 620 6 HOH A 536   O    78.7  60.8  71.1 119.9  76.8
REMARK 620 7 ARG A 158   O   116.3  76.6 154.7  81.3  75.5 126.2
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 NAG A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XCW   RELATED DB: PDB
REMARK 900 RELATED ID: 1XCX   RELATED DB: PDB
REMARK 900 RELATED ID: 1XD1   RELATED DB: PDB
DBREF  1XD0 A    1   496  UNP    P04746   AMYP_HUMAN      16    511
SEQADV 1XD0 PCA A    1  UNP  P04746    GLN    16 MODIFIED RESIDUE
SEQRES   1 A  496  PCA TYR SER PRO ASN THR GLN GLN 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 ALA PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE TYR
SEQRES   5 A  496  ASN PRO PHE 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 ASP GLU
SEQRES   7 A  496  PHE ARG ASN 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  ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES  10 A  496  TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES  13 A  496  VAL ARG ASP CYS ARG LEU THR GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES  15 A  496  MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  LEU ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP 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 ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  VAL 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 ALA SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET 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 PRO ARG GLN PHE GLN ASN GLY
SEQRES  28 A  496  ASN ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES  31 A  496  ILE ARG ASN MET VAL ILE PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLN PRO PHE THR ASN TRP TYR 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 SER PHE SER LEU THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES  37 A  496  VAL SER ASP ASP GLY LYS ALA HIS 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 1XD0 ASN A  461  ASN  GLYCOSYLATION SITE
MODRES 1XD0 PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET    NAG  A 499      14
HET    ARE  A 501      55
HET     CA  A 498       1
HET     CL  A 500       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     ARE ACARBOSE DERIVED PENTASACCHARIDE
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETSYN     ARE 4-O-(4,6-DIDEOXY-4-{[4-[(4-O-
HETSYN   2 ARE  HEXOPYRANOSYLHEXOPYRANOSYL)OXY]-5,6-DIHYDROXY-3-
HETSYN   3 ARE  (HYDROXYMETHYL)CYCLOHEX-2-EN-1-
HETSYN   4 ARE  YL]AMINO}HEXOPYRANOSYL)HEXOPYRANOSE
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  NAG    C8 H15 N O6
FORMUL   3  ARE    C31 H53 N O23
FORMUL   4   CA    CA 2+
FORMUL   5   CL    CL 1-
FORMUL   6  HOH   *142(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 ARG A  161  THR A  163  5                                   3
HELIX    8   8 LYS A  172  GLY A  190  1                                  19
HELIX    9   9 ALA A  198  MET A  202  5                                   5
HELIX   10  10 TRP A  203  ASP A  212  1                                  10
HELIX   11  11 LYS A  243  PHE A  248  5                                   6
HELIX   12  12 GLU A  255  ARG A  267  1                                  13
HELIX   13  13 LYS A  268  GLU A  272  5                                   5
HELIX   14  14 LYS A  273  TRP A  280  5                                   8
HELIX   15  15 GLY A  281  GLY A  285  5                                   5
HELIX   16  16 PRO A  288  ASP A  290  5                                   3
HELIX   17  17 ASP A  300  GLY A  304  5                                   5
HELIX   18  18 GLY A  308  ILE A  312  5                                   5
HELIX   19  19 THR A  314  TRP A  316  5                                   3
HELIX   20  20 ASP A  317  HIS A  331  1                                  15
HELIX   21  21 CYS A  384  ARG A  387  5                                   4
HELIX   22  22 TRP A  388  ASP A  402  1                                  15
HELIX   23  23 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  LEU 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  ILE A 230
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  GLN A 349  0
SHEET    2   C 2 ASN A 352  ASP A 353 -1  O  ASN A 352   N  GLN 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  THR 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 PHE A 436  GLN A 441  0
SHEET    2   F 2 LYS A 474  ILE A 479 -1  O  ILE A 479   N  PHE A 436
SHEET    1   G 2 GLY A 447  CYS A 450  0
SHEET    2   G 2 LYS A 466  VAL A 469 -1  O  ILE A 467   N  TYR A 449
SHEET    1   H 2 LYS A 457  ILE A 458  0
SHEET    2   H 2 ASN A 461  CYS A 462 -1  O  ASN A 461   N  ILE A 458
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.02
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03
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         ND2 ASN A 461                 C1  NAG A 499     1555   1555  1.46
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.36
LINK        CA    CA A 498                 OD1 ASP A 167     1555   1555  2.46
LINK        CA    CA A 498                 O   HOH A 546     1555   1555  2.62
LINK        CA    CA A 498                 OD1 ASN A 100     1555   1555  2.43
LINK        CA    CA A 498                 O   HIS A 201     1555   1555  2.48
LINK        CA    CA A 498                 OD2 ASP A 167     1555   1555  2.51
LINK        CA    CA A 498                 O   HOH A 536     1555   1555  2.53
LINK        CA    CA A 498                 O   ARG A 158     1555   1555  2.42
CISPEP   1 ASN A   53    PRO A   54          0         2.06
CISPEP   2 VAL A  129    PRO A  130          0        -1.93
SITE     1 AC1  6 LYS A 140  GLU A 171  TRP A 203  ASP A 206
SITE     2 AC1  6 ASN A 459  ASN A 461
SITE     1 AC2 22 TRP A  58  TRP A  59  TYR A  62  GLN A  63
SITE     2 AC2 22 HIS A 101  TYR A 151  THR A 163  ARG A 195
SITE     3 AC2 22 ASP A 197  ALA A 198  LYS A 200  HIS A 201
SITE     4 AC2 22 GLU A 233  ILE A 235  GLU A 240  HIS A 299
SITE     5 AC2 22 ASP A 300  HIS A 305  ALA A 307  ASP A 433
SITE     6 AC2 22 HOH A 588  HOH A 766
SITE     1 AC3  6 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC3  6 HOH A 536  HOH A 546
SITE     1 AC4  3 ARG A 195  ASN A 298  ARG A 337
CRYST1   52.900   68.900  132.000  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      0.018904  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014514  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007576        0.00000
      
PROCHECK
Go to PROCHECK summary
 References