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PDBsum entry 1s9v

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Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
1s9v
Jmol
Contents
Protein chains
179 a.a. *
181 a.a. *
11 a.a. *
Ligands
EDO ×4
Waters ×354
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           05-FEB-04   1S9V
TITLE     CRYSTAL STRUCTURE OF HLA-DQ2 COMPLEXED WITH DEAMIDATED
TITLE    2 GLIADIN PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ(3)
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A, D;
COMPND   5 FRAGMENT: RESIDUES (-1)-191;
COMPND   6 SYNONYM: HLA-DQ2 ALPHA CHAIN, HLA-DQA1*0501, DC-ALPHA, HLA-
COMPND   7 DCA;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ(1)
COMPND  11 BETA CHAIN;
COMPND  12 CHAIN: B, E;
COMPND  13 FRAGMENT: RESIDUES 1-198;
COMPND  14 SYNONYM: HLA-DQ2 BETA CHAIN, DQB1*0201, DC-3 BETA CHAIN;
COMPND  15 ENGINEERED: YES;
COMPND  16 MOL_ID: 3;
COMPND  17 MOLECULE: ALPHA-I GLIADIN;
COMPND  18 CHAIN: C, F;
COMPND  19 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PACAB3;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PACAB3;
SOURCE  21 MOL_ID: 3;
SOURCE  22 SYNTHETIC: YES;
SOURCE  23 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS    IMMUNE SYSTEM, HLA-DQ2
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.-Y.KIM,H.QUARSTEN,E.BERGSENG,C.KHOSLA,L.M.SOLLID
REVDAT   3   24-FEB-09 1S9V    1       VERSN
REVDAT   2   06-APR-04 1S9V    1       JRNL
REVDAT   1   02-MAR-04 1S9V    0
JRNL        AUTH   C.-Y.KIM,H.QUARSTEN,E.BERGSENG,C.KHOSLA,L.M.SOLLID
JRNL        TITL   STRUCTURAL BASIS FOR HLA-DQ2-MEDIATED PRESENTATION
JRNL        TITL 2 OF GLUTEN EPITOPES IN CELIAC DISEASE
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  4175 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   15020763
JRNL        DOI    10.1073/PNAS.0306885101
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.22 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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             : 44458
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.221
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 5960
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 354
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) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
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 1S9V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021548.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-02
REMARK 200  TEMPERATURE           (KELVIN) : 200
REMARK 200  PH                             : 3.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44458
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, AMMONIUM ACETATE,
REMARK 280  AMMONIUM SULFATE, ETHYLENE GLYCOL, PEG 3350, PH 3.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 300K
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       45.55500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.36000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.87500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.36000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.55500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.87500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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     ASP A     0
REMARK 465     ILE A     1
REMARK 465     GLU A   181
REMARK 465     ILE A   182
REMARK 465     PRO A   183
REMARK 465     ALA A   184
REMARK 465     PRO A   185
REMARK 465     MET A   186
REMARK 465     SER A   187
REMARK 465     GLU A   188
REMARK 465     LEU A   189
REMARK 465     THR A   190
REMARK 465     GLU A   191
REMARK 465     ARG B     1
REMARK 465     ASP B     2
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     GLN B   191
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     GLU D    -1
REMARK 465     ASP D     0
REMARK 465     ILE D     1
REMARK 465     GLU D   179
REMARK 465     PRO D   180
REMARK 465     GLU D   181
REMARK 465     ILE D   182
REMARK 465     PRO D   183
REMARK 465     ALA D   184
REMARK 465     PRO D   185
REMARK 465     MET D   186
REMARK 465     SER D   187
REMARK 465     GLU D   188
REMARK 465     LEU D   189
REMARK 465     THR D   190
REMARK 465     GLU D   191
REMARK 465     ARG E     1
REMARK 465     ASP E     2
REMARK 465     ARG E   105
REMARK 465     THR E   106
REMARK 465     GLU E   107
REMARK 465     ALA E   108
REMARK 465     LEU E   109
REMARK 465     ASN E   110
REMARK 465     HIS E   111
REMARK 465     HIS E   112
REMARK 465     GLN E   191
REMARK 465     SER E   192
REMARK 465     GLU E   193
REMARK 465     SER E   194
REMARK 465     ALA E   195
REMARK 465     GLN E   196
REMARK 465     SER E   197
REMARK 465     LYS E   198
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     ASP B 135    CB   CG   OD1  OD2
REMARK 470     LEU C   1    CB   CG   CD1  CD2
REMARK 470     GLN C   2    CB   CG   CD   OE1  NE2
REMARK 470     TYR C  11    CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     TYR C  11    OH
REMARK 470     ASP E 135    CB   CG   OD1  OD2
REMARK 470     GLN E 136    CB   CG   CD   OE1  NE2
REMARK 470     LEU F   1    CB   CG   CD1  CD2
REMARK 470     GLN F   2    CB   CG   CD   OE1  NE2
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 113      127.33   -174.98
REMARK 500    ASN B  33      -99.28     59.98
REMARK 500    VAL B  78      -73.24    -90.91
REMARK 500    THR B  89      -87.94   -135.22
REMARK 500    ASN B 134       35.86   -152.90
REMARK 500    ASP B 135       -3.29    111.05
REMARK 500    ASP B 152       40.04   -107.42
REMARK 500    PHE D 113      129.57   -174.01
REMARK 500    PRO D 115       67.24    -68.39
REMARK 500    ASN E  33     -102.37     58.60
REMARK 500    VAL E  78      -72.21   -107.49
REMARK 500    THR E  89      -93.30   -136.15
REMARK 500    ASP E 135      -15.93     77.22
REMARK 500    TRP E 153       31.50     71.50
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 E 206        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH B 219        DISTANCE =  7.69 ANGSTROMS
REMARK 525    HOH D 542        DISTANCE = 14.31 ANGSTROMS
REMARK 525    HOH D 543        DISTANCE =  6.81 ANGSTROMS
REMARK 525    HOH A 547        DISTANCE =  8.94 ANGSTROMS
REMARK 525    HOH B 243        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH D 550        DISTANCE =  7.47 ANGSTROMS
REMARK 525    HOH B 248        DISTANCE =  8.50 ANGSTROMS
REMARK 525    HOH B 252        DISTANCE =  6.19 ANGSTROMS
REMARK 525    HOH A 564        DISTANCE =  9.95 ANGSTROMS
REMARK 525    HOH B 259        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH B 268        DISTANCE =  6.76 ANGSTROMS
REMARK 525    HOH E 270        DISTANCE = 10.85 ANGSTROMS
REMARK 525    HOH D 597        DISTANCE =  6.12 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 502
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 503
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
DBREF  1S9V A   -1   191  UNP    P01909   HA23_HUMAN      24    216
DBREF  1S9V B    1   198  UNP    P01918   HB21_HUMAN      33    230
DBREF  1S9V D   -1   191  UNP    P01909   HA23_HUMAN      24    216
DBREF  1S9V E    1   198  UNP    P01918   HB21_HUMAN      33    230
DBREF  1S9V C    1    11  PDB    1S9V     1S9V             1     11
DBREF  1S9V F    1    11  PDB    1S9V     1S9V             1     11
SEQRES   1 A  193  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES   2 A  193  ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR THR
SEQRES   3 A  193  HIS GLU PHE ASP GLY ASP GLU GLN PHE TYR VAL ASP LEU
SEQRES   4 A  193  GLY ARG LYS GLU THR VAL TRP CYS LEU PRO VAL LEU ARG
SEQRES   5 A  193  GLN PHE ARG PHE ASP PRO GLN PHE ALA LEU THR ASN ILE
SEQRES   6 A  193  ALA VAL LEU LYS HIS ASN LEU ASN SER LEU ILE LYS ARG
SEQRES   7 A  193  SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU VAL
SEQRES   8 A  193  THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN PRO
SEQRES   9 A  193  ASN ILE LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO PRO
SEQRES  10 A  193  VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER VAL
SEQRES  11 A  193  THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS SER
SEQRES  12 A  193  ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR LEU LEU
SEQRES  13 A  193  PRO SER ALA GLU GLU SER TYR ASP CYS LYS VAL GLU HIS
SEQRES  14 A  193  TRP GLY LEU ASP LYS PRO LEU LEU LYS HIS TRP GLU PRO
SEQRES  15 A  193  GLU ILE PRO ALA PRO MET SER GLU LEU THR GLU
SEQRES   1 B  198  ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE LYS GLY
SEQRES   2 B  198  MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  198  VAL SER ARG SER ILE TYR ASN ARG GLU GLU ILE VAL ARG
SEQRES   4 B  198  PHE ASP SER ASP VAL GLY GLU PHE ARG ALA VAL THR LEU
SEQRES   5 B  198  LEU GLY LEU PRO ALA ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  198  ASP ILE LEU GLU ARG LYS ARG ALA ALA VAL ASP ARG VAL
SEQRES   7 B  198  CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR THR LEU
SEQRES   8 B  198  GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER PRO SER
SEQRES   9 B  198  ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  198  SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS VAL ARG
SEQRES  11 B  198  TRP PHE ARG ASN ASP GLN GLU GLU THR ALA GLY VAL VAL
SEQRES  12 B  198  SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  198  ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG GLY ASP
SEQRES  14 B  198  VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU GLN SER
SEQRES  15 B  198  PRO ILE THR VAL GLU TRP ARG ALA GLN SER GLU SER ALA
SEQRES  16 B  198  GLN SER LYS
SEQRES   1 C   11  LEU GLN PRO PHE PRO GLN PRO GLU LEU PRO TYR
SEQRES   1 D  193  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES   2 D  193  ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR THR
SEQRES   3 D  193  HIS GLU PHE ASP GLY ASP GLU GLN PHE TYR VAL ASP LEU
SEQRES   4 D  193  GLY ARG LYS GLU THR VAL TRP CYS LEU PRO VAL LEU ARG
SEQRES   5 D  193  GLN PHE ARG PHE ASP PRO GLN PHE ALA LEU THR ASN ILE
SEQRES   6 D  193  ALA VAL LEU LYS HIS ASN LEU ASN SER LEU ILE LYS ARG
SEQRES   7 D  193  SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU VAL
SEQRES   8 D  193  THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN PRO
SEQRES   9 D  193  ASN ILE LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO PRO
SEQRES  10 D  193  VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER VAL
SEQRES  11 D  193  THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS SER
SEQRES  12 D  193  ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR LEU LEU
SEQRES  13 D  193  PRO SER ALA GLU GLU SER TYR ASP CYS LYS VAL GLU HIS
SEQRES  14 D  193  TRP GLY LEU ASP LYS PRO LEU LEU LYS HIS TRP GLU PRO
SEQRES  15 D  193  GLU ILE PRO ALA PRO MET SER GLU LEU THR GLU
SEQRES   1 E  198  ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE LYS GLY
SEQRES   2 E  198  MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 E  198  VAL SER ARG SER ILE TYR ASN ARG GLU GLU ILE VAL ARG
SEQRES   4 E  198  PHE ASP SER ASP VAL GLY GLU PHE ARG ALA VAL THR LEU
SEQRES   5 E  198  LEU GLY LEU PRO ALA ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 E  198  ASP ILE LEU GLU ARG LYS ARG ALA ALA VAL ASP ARG VAL
SEQRES   7 E  198  CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR THR LEU
SEQRES   8 E  198  GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER PRO SER
SEQRES   9 E  198  ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 E  198  SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS VAL ARG
SEQRES  11 E  198  TRP PHE ARG ASN ASP GLN GLU GLU THR ALA GLY VAL VAL
SEQRES  12 E  198  SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR PHE GLN
SEQRES  13 E  198  ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG GLY ASP
SEQRES  14 E  198  VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU GLN SER
SEQRES  15 E  198  PRO ILE THR VAL GLU TRP ARG ALA GLN SER GLU SER ALA
SEQRES  16 E  198  GLN SER LYS
SEQRES   1 F   11  LEU GLN PRO PHE PRO GLN PRO GLU LEU PRO TYR
HET    EDO  A 501       4
HET    EDO  D 502       4
HET    EDO  D 503       4
HET    EDO  A 504       4
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   7  EDO    4(C2 H6 O2)
FORMUL  11  HOH   *354(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 ASP A   55  SER A   77  1                                  23
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  GLN B   64  1                                  11
HELIX    5   5 GLN B   64  ARG B   72  1                                   9
HELIX    6   6 ALA B   73  VAL B   78  1                                   6
HELIX    7   7 VAL B   78  ARG B   88  1                                  11
HELIX    8   8 THR B   89  ARG B   93  5                                   5
HELIX    9   9 LEU D   45  PHE D   51  5                                   7
HELIX   10  10 PRO D   56  SER D   77  1                                  22
HELIX   11  11 THR E   51  LEU E   53  5                                   3
HELIX   12  12 GLY E   54  SER E   63  1                                  10
HELIX   13  13 GLN E   64  VAL E   78  1                                  15
HELIX   14  14 VAL E   78  THR E   89  1                                  12
HELIX   15  15 THR E   90  ARG E   93  5                                   4
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  HIS A  24   O  GLN A  31
SHEET    4   A 8 HIS A   5  GLN A  14 -1  N  GLN A  14   O  SER A  19
SHEET    5   A 8 VAL B   8  THR B  18 -1  O  PHE B  17   N  HIS A   5
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ILE B  31   N  GLN B  10
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  VAL B  38   N  SER B  30
SHEET    8   A 8 PHE B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 4 GLU A  88  SER A  93  0
SHEET    2   B 4 ASN A 103  ILE A 112 -1  O  ASP A 110   N  GLU A  88
SHEET    3   B 4 PHE A 145  LEU A 153 -1  O  PHE A 145   N  ILE A 112
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   C 4 GLU A  88  SER A  93  0
SHEET    2   C 4 ASN A 103  ILE A 112 -1  O  ASP A 110   N  GLU A  88
SHEET    3   C 4 PHE A 145  LEU A 153 -1  O  PHE A 145   N  ILE A 112
SHEET    4   C 4 LEU A 138  SER A 139 -1  N  LEU A 138   O  PHE A 146
SHEET    1   D 4 HIS A 126  SER A 127  0
SHEET    2   D 4 ASN A 118  SER A 123 -1  N  SER A 123   O  HIS A 126
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  LYS A 164   N  THR A 120
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161
SHEET    1   E 4 THR B  98  PRO B 103  0
SHEET    2   E 4 LEU B 114  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   E 4 PHE B 155  GLU B 162 -1  O  VAL B 159   N  CYS B 117
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 THR B  98  PRO B 103  0
SHEET    2   F 4 LEU B 114  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   F 4 PHE B 155  GLU B 162 -1  O  VAL B 159   N  CYS B 117
SHEET    4   F 4 ILE B 148  ARG B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   G 4 GLU B 137  GLU B 138  0
SHEET    2   G 4 LYS B 128  PHE B 132 -1  N  TRP B 131   O  GLU B 138
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  HIS B 174   N  ARG B 130
SHEET    4   G 4 ILE B 184  ARG B 189 -1  O  TRP B 188   N  TYR B 171
SHEET    1   H 8 GLU D  40  TRP D  43  0
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  ASP D  35   O  GLU D  40
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  HIS D  24   O  GLN D  31
SHEET    4   H 8 HIS D   5  GLN D  14 -1  N  GLN D  14   O  SER D  19
SHEET    5   H 8 VAL E   8  THR E  18 -1  O  TYR E   9   N  TYR D  13
SHEET    6   H 8 ARG E  23  TYR E  32 -1  O  ILE E  31   N  GLN E  10
SHEET    7   H 8 GLU E  35  ASP E  41 -1  O  GLU E  35   N  TYR E  32
SHEET    8   H 8 PHE E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1   I 4 GLU D  88  SER D  93  0
SHEET    2   I 4 ASN D 103  ILE D 112 -1  O  ILE D 106   N  PHE D  92
SHEET    3   I 4 PHE D 145  LEU D 153 -1  O  PHE D 145   N  ILE D 112
SHEET    4   I 4 VAL D 132  GLU D 134 -1  N  SER D 133   O  TYR D 150
SHEET    1   J 4 GLU D  88  SER D  93  0
SHEET    2   J 4 ASN D 103  ILE D 112 -1  O  ILE D 106   N  PHE D  92
SHEET    3   J 4 PHE D 145  LEU D 153 -1  O  PHE D 145   N  ILE D 112
SHEET    4   J 4 LEU D 138  SER D 139 -1  N  LEU D 138   O  PHE D 146
SHEET    1   K 4 HIS D 126  SER D 127  0
SHEET    2   K 4 ASN D 118  SER D 123 -1  N  SER D 123   O  HIS D 126
SHEET    3   K 4 TYR D 161  GLU D 166 -1  O  LYS D 164   N  THR D 120
SHEET    4   K 4 LEU D 174  TRP D 178 -1  O  LEU D 174   N  VAL D 165
SHEET    1   L 4 THR E  98  PRO E 103  0
SHEET    2   L 4 LEU E 114  PHE E 122 -1  O  SER E 118   N  THR E 100
SHEET    3   L 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   M 4 THR E  98  PRO E 103  0
SHEET    2   M 4 LEU E 114  PHE E 122 -1  O  SER E 118   N  THR E 100
SHEET    3   M 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115
SHEET    4   M 4 ILE E 148  ARG E 149 -1  N  ILE E 148   O  GLN E 156
SHEET    1   N 4 GLN E 136  GLU E 138  0
SHEET    2   N 4 LYS E 128  ARG E 133 -1  N  ARG E 133   O  GLN E 136
SHEET    3   N 4 VAL E 170  GLU E 176 -1  O  HIS E 174   N  ARG E 130
SHEET    4   N 4 ILE E 184  ARG E 189 -1  O  TRP E 188   N  TYR E 171
SSBOND   1 CYS A  107    CYS A  163                          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  2.04
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.03
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.05
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.03
CISPEP   1 GLY A   17    PRO A   18          0        -0.11
CISPEP   2 PHE A  113    PRO A  114          0         0.77
CISPEP   3 TYR B  123    PRO B  124          0        -0.68
CISPEP   4 GLY D   17    PRO D   18          0        -0.19
CISPEP   5 PHE D  113    PRO D  114          0        -0.06
CISPEP   6 TYR E  123    PRO E  124          0         1.10
SITE     1 AC1  5 PHE A  54  ASP A  55  PHE A  58  THR A  98
SITE     2 AC1  5 LEU A  99
SITE     1 AC2  8 PHE D  58  THR D  61  ASN D  62  THR D  98
SITE     2 AC2  8 GLN D 101  PRO D 102  HOH D 564  PRO F   7
SITE     1 AC3  5 PHE D  54  ASP D  55  PHE D  58  LEU D  99
SITE     2 AC3  5 HOH D 511
SITE     1 AC4  5 TYR A   9  HIS A  24  GLN A  31  GLU B  86
SITE     2 AC4  5 PRO C   3
CRYST1   91.110   93.750  102.720  90.00  90.00  90.00 P 21 21 21    8
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      0.010976  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010667  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009735        0.00000
      
PROCHECK
Go to PROCHECK summary
 References