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PDBsum entry 1uvq

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Top Page protein ligands metals Protein-protein interface(s) links
Immunology PDB id
1uvq
Jmol
Contents
Protein chains
182 a.a. *
181 a.a. *
20 a.a. *
Ligands
GLY
NAG ×2
NAG-FUC-NAG-BMA
ACY
Metals
_ZN
Waters ×371
* Residue conservation analysis
HEADER    IMMUNOLOGY                              22-JAN-04   1UVQ
TITLE     CRYSTAL STRUCTURE OF HLA-DQ0602 IN COMPLEX WITH A
TITLE    2 HYPOCRETIN PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: QA1*0602, DQ(5) ALPHA CHAIN, DC-1 ALPHA CHAIN;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN;
COMPND   8 CHAIN: B;
COMPND   9 SYNONYM: DQB1*0602, DQB1*0602 BETA CHAIN, DQ(5), DC-1;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: OREXIN;
COMPND  13 CHAIN: C;
COMPND  14 SYNONYM: HCRT, HYPOCRETIN-1, HCRT1, OREXIN-B,
COMPND  15  HYPOCRETIN-2, HCRT2;
COMPND  16 ENGINEERED: YES;
COMPND  17 OTHER_DETAILS: CHAIN C IS COVALENTLY CONNECTED AT THE
COMPND  18  N-TERMINUS OF CHAIN B VIA A GLYCINE-RICH LINKER. AS PER
COMPND  19  DEFINITION FOR THE MHC CLASS II MOLECULES, THE CHAINS OF
COMPND  20  THE PEPTIDE LIGAND (CHAIN C) AND THE BETA-CHAIN (CHAIN B)
COMPND  21  SHOULD BE DIFFERENT.
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL_LINE: S2;
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  10 ORGANISM_COMMON: HUMAN;
SOURCE  11 ORGANISM_TAXID: 9606;
SOURCE  12 CELL_LINE: S2;
SOURCE  13 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE  15 MOL_ID: 3;
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  17 ORGANISM_COMMON: HUMAN;
SOURCE  18 ORGANISM_TAXID: 9606;
SOURCE  19 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 7227
KEYWDS    IMMUNOLOGY, MHC CLASS II, DIABETES, NARCOLEPSY, AUTOIMMUNE
KEYWDS   2 DISEASE, STRUCTURAL PROTEOMICS IN EUROPE, SPINE,
KEYWDS   3 STRUCTURAL GENOMICS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.SIEBOLD,B.E.HANSEN,J.R.WYER,K.HARLOS,R.E.ESNOUF,
AUTHOR   2 A.SVEJGAARD,J.I.BELL,J.L.STROMINGER,E.Y.JONES,L.FUGGER
REVDAT   3   24-FEB-09 1UVQ    1       VERSN
REVDAT   2   19-FEB-04 1UVQ    1       JRNL
REVDAT   1   05-FEB-04 1UVQ    0
JRNL        AUTH   C.SIEBOLD,B.E.HANSEN,J.R.WYER,K.HARLOS,R.E.ESNOUF,
JRNL        AUTH 2 A.SVEJGAARD,J.I.BELL,J.L.STROMINGER,E.Y.JONES,
JRNL        AUTH 3 L.FUGGER
JRNL        TITL   CRYSTAL STRUCTURE OF HLA-DQ0602 THAT PROTECTS
JRNL        TITL 2 AGAINST TYPE 1 DIABETES AND CONFERS STRONG
JRNL        TITL 3 SUSCEPTIBILITY TO NARCOLEPSY
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  1999 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   14769912
JRNL        DOI    10.1073/PNAS.0308458100
REMARK   2
REMARK   2 RESOLUTION.    1.8  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.8
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.31
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.3
REMARK   3   NUMBER OF REFLECTIONS             : 47894
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.205
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 2386
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.3
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6060
REMARK   3   BIN R VALUE           (WORKING SET) : 0.224
REMARK   3   BIN FREE R VALUE                    : 0.249
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.1
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 326
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3078
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 83
REMARK   3   SOLVENT ATOMS            : 371
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) : -2.39
REMARK   3    B22 (A**2) : 0.65
REMARK   3    B33 (A**2) : 1.73
REMARK   3    B12 (A**2) : 0
REMARK   3    B13 (A**2) : 0
REMARK   3    B23 (A**2) : 0
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : 0.12
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5
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) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.3
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.5
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79
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) : 1.24  ; 1.50
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.24  ; 1.50
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.11  ; 2.00
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.19  ; 2.50
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UVQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-04.
REMARK 100 THE PDBE ID CODE IS EBI-14251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 3.80
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.956
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49489
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 7.500
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR, CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 54.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.03900
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.65200
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.03900
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.65200
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 GENERATING THE BIOMOLECULE
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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     GLU A     1
REMARK 465     GLU A   184
REMARK 465     ILE A   185
REMARK 465     PRO A   186
REMARK 465     ALA A   187
REMARK 465     PRO A   188
REMARK 465     MET A   189
REMARK 465     SER A   190
REMARK 465     GLU A   191
REMARK 465     LEU A   192
REMARK 465     THR A   193
REMARK 465     GLU A   194
REMARK 465     THR A   195
REMARK 465     VAL A   196
REMARK 465     ASP A   197
REMARK 465     ARG B   105
REMARK 465     THR B   106
REMARK 465     GLU B   107
REMARK 465     ALA B   108
REMARK 465     LEU B   109
REMARK 465     ASN B   110
REMARK 465     HIS B   111
REMARK 465     HIS B   112
REMARK 465     SER B   192
REMARK 465     GLU B   193
REMARK 465     SER B   194
REMARK 465     ALA B   195
REMARK 465     GLN B   196
REMARK 465     SER B   197
REMARK 465     LYS B   198
REMARK 465     VAL B   199
REMARK 465     ASP B   200
REMARK 465     GLU C    -4
REMARK 465     GLY C    -3
REMARK 465     ARG C    -2
REMARK 465     ASP C    -1
REMARK 465     SER C     0
REMARK 465     PRO C    21
REMARK 465     ARG C    22
REMARK 465     GLY C    23
REMARK 465     SER C    24
REMARK 465     GLY C    25
REMARK 465     GLY C    26
REMARK 465     GLY C    27
REMARK 465     GLY C    28
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     PRO A 183    CG   CD
REMARK 470     MET C   1    CG   SD   CE
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 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 116      128.51   -173.04
REMARK 500    ASN B  33     -108.30     62.85
REMARK 500    VAL B  78      -66.44   -107.04
REMARK 500    TRP B 153       32.21     71.09
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 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     GLY A 1186
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                              ZN B1192  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 165   OD1
REMARK 620 2 ASP A 165   OD2  57.7
REMARK 620 3 ASP B  76   OD2 160.1 102.5
REMARK 620 4 HIS B  81   NE2  87.7 125.5 104.3
REMARK 620 5 HIS A 180   ND1  94.4 113.6  96.5 109.3
REMARK 620 N                    1     2     3     4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B1194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B1197
DBREF  1UVQ A    1   196  UNP    P01907   HA25_HUMAN      24    219
DBREF  1UVQ A  197   197  PDB    1UVQ     1UVQ           197    197
DBREF  1UVQ B    3   198  UNP    P03992   HB25_HUMAN      35    230
DBREF  1UVQ B  199   200  PDB    1UVQ     1UVQ           199    200
DBREF  1UVQ C   -4     0  PDB    1UVQ     1UVQ            -4      0
DBREF  1UVQ C    1    12  UNP    O43612   OREX_HUMAN       1     12
DBREF  1UVQ C   13    28  PDB    1UVQ     1UVQ            13     28
SEQRES   1 A  197  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER CYS GLY VAL
SEQRES   2 A  197  ASN LEU TYR GLN PHE TYR GLY PRO SER GLY GLN TYR THR
SEQRES   3 A  197  HIS GLU PHE ASP GLY ASP GLU GLN PHE TYR VAL ASP LEU
SEQRES   4 A  197  GLU ARG LYS GLU THR ALA TRP ARG TRP PRO GLU PHE SER
SEQRES   5 A  197  LYS PHE GLY GLY PHE ASP PRO GLN GLY ALA LEU ARG ASN
SEQRES   6 A  197  MET ALA VAL ALA LYS HIS ASN LEU ASN ILE MET ILE LYS
SEQRES   7 A  197  ARG TYR ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU
SEQRES   8 A  197  VAL THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN
SEQRES   9 A  197  PRO ASN THR LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO
SEQRES  10 A  197  PRO VAL VAL ASN ILE THR TRP LEU SER ASN GLY GLN SER
SEQRES  11 A  197  VAL THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS
SEQRES  12 A  197  SER ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR PHE
SEQRES  13 A  197  LEU PRO SER ALA ASP GLU ILE TYR ASP CYS LYS VAL GLU
SEQRES  14 A  197  HIS TRP GLY LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU
SEQRES  15 A  197  PRO GLU ILE PRO ALA PRO MET SER GLU LEU THR GLU THR
SEQRES  16 A  197  VAL ASP
SEQRES   1 B  198  SER PRO GLU ASP PHE VAL PHE GLN PHE LYS GLY MET CYS
SEQRES   2 B  198  TYR PHE THR ASN GLY THR GLU ARG VAL ARG LEU VAL THR
SEQRES   3 B  198  ARG TYR ILE TYR ASN ARG GLU GLU TYR ALA ARG PHE ASP
SEQRES   4 B  198  SER ASP VAL GLY VAL TYR ARG ALA VAL THR PRO GLN GLY
SEQRES   5 B  198  ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS GLU VAL
SEQRES   6 B  198  LEU GLU GLY THR ARG ALA GLU LEU ASP THR VAL CYS ARG
SEQRES   7 B  198  HIS ASN TYR GLU VAL ALA PHE ARG GLY ILE LEU GLN ARG
SEQRES   8 B  198  ARG VAL GLU PRO THR VAL THR ILE SER PRO SER ARG THR
SEQRES   9 B  198  GLU ALA LEU ASN HIS HIS ASN LEU LEU VAL CYS SER VAL
SEQRES  10 B  198  THR ASP PHE TYR PRO GLY GLN ILE LYS VAL ARG TRP PHE
SEQRES  11 B  198  ARG ASN ASP GLN GLU GLU THR ALA GLY VAL VAL SER THR
SEQRES  12 B  198  PRO LEU ILE ARG ASN GLY ASP TRP THR PHE GLN ILE LEU
SEQRES  13 B  198  VAL MET LEU GLU MET THR PRO GLN ARG GLY ASP VAL TYR
SEQRES  14 B  198  THR CYS HIS VAL GLU HIS PRO SER LEU GLN SER PRO ILE
SEQRES  15 B  198  THR VAL GLU TRP ARG ALA GLN SER GLU SER ALA GLN SER
SEQRES  16 B  198  LYS VAL ASP
SEQRES   1 C   33  GLU GLY ARG ASP SER MET ASN LEU PRO SER THR LYS VAL
SEQRES   2 C   33  SER TRP ALA ALA VAL GLY GLY GLY GLY SER LEU VAL PRO
SEQRES   3 C   33  ARG GLY SER GLY GLY GLY GLY
HET    NAG  A1184      14
HET    NAG  A1185      14
HET    NAG  B1193      14
HET    FUC  B1194      10
HET    NAG  B1195      14
HET    BMA  B1196      11
HET     ZN  B1192       1
HET    GLY  A1186       4
HET    ACY  B1197       4
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM      ZN ZINC ION
HETNAM     GLY GLYCINE
HETNAM     ACY ACETIC ACID
HETSYN     NAG NAG
FORMUL   4  NAG    4(C8 H15 N O6)
FORMUL   6  FUC    C6 H12 O5
FORMUL   6  BMA    C6 H12 O6
FORMUL   7   ZN    ZN 2+
FORMUL   8  GLY    C2 H5 N O2
FORMUL   9  ACY    C2 H4 O2
FORMUL  10  HOH   *371(H2 O1)
HELIX    1   1 TRP A   48  GLY A   55  5                                   8
HELIX    2   2 ASP A   58  TYR A   80  1                                  23
HELIX    3   3 THR B   51  GLN B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  LEU B   91  1                                  28
SHEET    1  AA 8 GLU A  43  ALA A  45  0
SHEET    2  AA 8 ASP A  32  ASP A  38 -1  O  TYR A  36   N  ALA A  45
SHEET    3  AA 8 SER A  22  PHE A  29 -1  O  TYR A  25   N  VAL A  37
SHEET    4  AA 8 HIS A   7  GLN A  17 -1  O  SER A  10   N  GLU A  28
SHEET    5  AA 8 VAL B   8  THR B  18 -1  O  PHE B   9   N  TYR A  16
SHEET    6  AA 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  THR B  18
SHEET    7  AA 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32
SHEET    8  AA 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1  AB 4 GLU A  91  SER A  96  0
SHEET    2  AB 4 ASN A 106  ILE A 115 -1  O  ILE A 109   N  PHE A  95
SHEET    3  AB 4 PHE A 148  PHE A 156 -1  O  PHE A 148   N  ILE A 115
SHEET    4  AB 4 VAL A 135  GLU A 137 -1  O  SER A 136   N  TYR A 153
SHEET    1  AC 4 GLU A  91  SER A  96  0
SHEET    2  AC 4 ASN A 106  ILE A 115 -1  O  ILE A 109   N  PHE A  95
SHEET    3  AC 4 PHE A 148  PHE A 156 -1  O  PHE A 148   N  ILE A 115
SHEET    4  AC 4 LEU A 141  SER A 142 -1  O  LEU A 141   N  PHE A 149
SHEET    1  AD 4 GLN A 129  VAL A 131  0
SHEET    2  AD 4 ASN A 121  SER A 126 -1  O  TRP A 124   N  VAL A 131
SHEET    3  AD 4 TYR A 164  GLU A 169 -1  O  ASP A 165   N  LEU A 125
SHEET    4  AD 4 LEU A 177  HIS A 180 -1  O  LEU A 177   N  VAL A 168
SHEET    1  BA 4 THR B  98  PRO B 103  0
SHEET    2  BA 4 LEU B 114  PHE B 122 -1  O  VAL B 116   N  SER B 102
SHEET    3  BA 4 PHE B 155  GLU B 162 -1  O  PHE B 155   N  PHE B 122
SHEET    4  BA 4 VAL B 142  SER B 144 -1  O  VAL B 143   N  MET B 160
SHEET    1  BB 4 THR B  98  PRO B 103  0
SHEET    2  BB 4 LEU B 114  PHE B 122 -1  O  VAL B 116   N  SER B 102
SHEET    3  BB 4 PHE B 155  GLU B 162 -1  O  PHE B 155   N  PHE B 122
SHEET    4  BB 4 ILE B 148  ARG B 149 -1  O  ILE B 148   N  GLN B 156
SHEET    1  BC 4 GLN B 136  GLU B 138  0
SHEET    2  BC 4 LYS B 128  ARG B 133 -1  O  TRP B 131   N  GLU B 138
SHEET    3  BC 4 TYR B 171  GLU B 176 -1  O  THR B 172   N  PHE B 132
SHEET    4  BC 4 ILE B 184  TRP B 188 -1  O  ILE B 184   N  VAL B 175
SSBOND   1 CYS A  110    CYS A  166                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.05
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
LINK         ND2 ASN A  81                 C1  NAG A1185     1555   1555  1.45
LINK         ND2 ASN A 121                 C1  NAG A1184     1555   1555  1.45
LINK         ND2 ASN B  19                 C1  NAG B1193     1555   1555  1.45
LINK        ZN    ZN B1192                 OD2 ASP B  76     1555   1555  2.06
LINK        ZN    ZN B1192                 OD2 ASP A 165     1555   4556  2.03
LINK        ZN    ZN B1192                 OD1 ASP A 165     1555   4556  2.46
LINK        ZN    ZN B1192                 ND1 HIS A 180     1555   4556  2.09
LINK        ZN    ZN B1192                 NE2 HIS B  81     1555   1555  2.11
LINK         O6  NAG B1193                 C1  FUC B1194     1555   1555  1.40
LINK         O4  NAG B1193                 C1  NAG B1195     1555   1555  1.38
LINK         O4  NAG B1195                 C1  BMA B1196     1555   1555  1.38
CISPEP   1 CYS A   11    GLY A   12          0        -0.20
CISPEP   2 GLY A   20    PRO A   21          0        -0.75
CISPEP   3 PHE A  116    PRO A  117          0        -0.31
CISPEP   4 TYR B  123    PRO B  124          0         0.47
SITE     1 AC1  6 ASN A 121  GLU A 169  TRP A 171  HOH A2186
SITE     2 AC1  6 HOH A2187  HOH A2188
SITE     1 AC2  2 ARG A  79  ASN A  81
SITE     1 AC3  5 ASN B  19  GLU B  22  FUC B1194  NAG B1195
SITE     2 AC3  5 HOH B2164
SITE     1 AC4  9 LEU A 125  GLY A 128  GLN A 129  SER A 130
SITE     2 AC4  9 THR B  21  NAG B1193  NAG B1195  HOH B2165
SITE     3 AC4  9 HOH B2167
SITE     1 AC5  4 NAG B1193  FUC B1194  BMA B1196  HOH B2003
SITE     1 AC6  1 NAG B1195
SITE     1 AC7  4 ASP A 165  HIS A 180  ASP B  76  HIS B  81
SITE     1 AC8  5 ASP A 113  LYS A 143  PHE A 149  HOH A2189
SITE     2 AC8  5 HOH B2137
SITE     1 AC9  5 TYR A  80  THR A  83  ASN B  33  GLU B  35
SITE     2 AC9  5 HOH B2168
CRYST1  102.078  129.304   40.619  90.00  90.00  90.00 P 21 21 2     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      0.009796  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007734  0.000000        0.00000
SCALE3      0.000000  0.000000  0.024619        0.00000
      
PROCHECK
Go to PROCHECK summary
 References