spacer
spacer

PDBsum entry 1hxy

Go to PDB code: 
Top Page protein metals Protein-protein interface(s) links
Immune system/toxin PDB id
1hxy
Jmol
Contents
Protein chains
180 a.a. *
180 a.a. *
13 a.a. *
212 a.a. *
Metals
_ZN
Waters ×88
* Residue conservation analysis
HEADER    IMMUNE SYSTEM/TOXIN                     17-JAN-01   1HXY
TITLE     CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN
TITLE    2 COMPLEX WITH HUMAN MHC CLASS II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1
COMPND   8 BETA CHAIN;
COMPND   9 CHAIN: B;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: HEMAGGLUTININ;
COMPND  13 CHAIN: C;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 4;
COMPND  16 MOLECULE: ENTEROTOXIN H;
COMPND  17 CHAIN: D;
COMPND  18 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: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE   9 MOL_ID: 2;
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  11 ORGANISM_COMMON: HUMAN;
SOURCE  12 ORGANISM_TAXID: 9606;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  17 MOL_ID: 3;
SOURCE  18 SYNTHETIC: YES;
SOURCE  19 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED.
SOURCE  20 THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN
SOURCE  21 INFLUENZA A VIRUS.;
SOURCE  22 MOL_ID: 4;
SOURCE  23 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE  24 ORGANISM_TAXID: 1280;
SOURCE  25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  27 EXPRESSION_SYSTEM_STRAIN: UL635;
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  29 EXPRESSION_SYSTEM_PLASMID: PLR16
KEYWDS    COMPLEX, IMMUNE SYSTEM/TOXIN COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.PETERSSON,M.HAKANSSON,H.NILSSON,G.FORSBERG,L.A.SVENSSON,
AUTHOR   2 A.LILJAS,B.WALSE
REVDAT   2   24-FEB-09 1HXY    1       VERSN
REVDAT   1   27-JUN-01 1HXY    0
JRNL        AUTH   K.PETERSSON,M.HAKANSSON,H.NILSSON,G.FORSBERG,
JRNL        AUTH 2 L.A.SVENSSON,A.LILJAS,B.WALSE
JRNL        TITL   CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO MHC
JRNL        TITL 2 CLASS II DISPLAYS ZINC AND PEPTIDE DEPENDENCE
JRNL        REF    EMBO J.                       V.  20  3306 2001
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   11432818
JRNL        DOI    10.1093/EMBOJ/20.13.3306
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
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)   (%) : 96.0
REMARK   3   NUMBER OF REFLECTIONS             : 21105
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.202
REMARK   3   FREE R VALUE                     : 0.258
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1075
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            : 4739
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 88
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 55.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.30
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) : 0.31
REMARK   3   ESD FROM SIGMAA              (A) : 0.39
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1HXY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-01.
REMARK 100 THE RCSB ID CODE IS RCSB012671.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.1
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX II
REMARK 200  BEAMLINE                       : I711
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0232
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARXDS
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21105
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : 3.540
REMARK 200  R MERGE                    (I) : 0.09900
REMARK 200  R SYM                      (I) : 0.07100
REMARK 200   FOR THE DATA SET  : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.55
REMARK 200  R MERGE FOR SHELL          (I) : 0.36500
REMARK 200  R SYM FOR SHELL            (I) : 0.31400
REMARK 200   FOR SHELL         : 3.150
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: PDB ENTRY: 1ENF AND 1DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 MM MONO-POTASSIUM DIHYDROGEN
REMARK 280  PHOSPHATE, 20 % (W/V) POLYETHYLENE GLYCOL 8000, PH 5.1, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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       61.81200
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.42150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       61.81200
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.42150
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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     ILE A     1
REMARK 465     LYS A     2
REMARK 465     GLY B     1
REMARK 465     ASP B     2
REMARK 465     SER B   104
REMARK 465     LYS B   105
REMARK 465     THR B   106
REMARK 465     GLN B   107
REMARK 465     PRO B   108
REMARK 465     LEU B   109
REMARK 465     GLN B   110
REMARK 465     HIS B   111
REMARK 465     GLU D     1
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     GLU A  46    CG   CD   OE1  OE2
REMARK 470     GLU B  22    CG   CD   OE1  OE2
REMARK 470     GLU B 138    CG   CD   OE1  OE2
REMARK 470     VAL B 164    CG1  CG2
REMARK 470     ARG B 166    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B 167    OG
REMARK 470     LYS D  27    CG   CD   CE   NZ
REMARK 470     GLU D  38    CG   CD   OE1  OE2
REMARK 470     SER D  49    OG
REMARK 470     LYS D  65    CG   CD   CE   NZ
REMARK 470     LYS D  67    CG   CD   CE   NZ
REMARK 470     LYS D  84    CG   CD   CE   NZ
REMARK 470     ILE D  89    CG1  CG2  CD1
REMARK 470     LYS D 131    CG   CD   CE   NZ
REMARK 470     TYR D 187    CG   CD1  CD2  CE1  CE2  CZ   OH
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   CG1  VAL B   143     CG1  VAL B   143     2555     1.98
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    GLU A   4      -78.31   -104.95
REMARK 500    ASN A  78       35.97     72.08
REMARK 500    ARG A 100       -6.82     70.55
REMARK 500    PRO A 102      136.66    -39.20
REMARK 500    THR A 113      148.71   -177.99
REMARK 500    THR A 129      -18.47   -140.38
REMARK 500    THR A 130       94.53    -61.58
REMARK 500    ASN B  33     -103.46     55.32
REMARK 500    TYR B  78      -71.36   -102.83
REMARK 500    THR B  90      -68.61   -121.00
REMARK 500    PRO B 124     -177.67    -69.26
REMARK 500    TRP B 153       37.03     72.88
REMARK 500    THR B 157      142.83   -170.82
REMARK 500    ASN D  29      101.39     64.25
REMARK 500    GLU D  38      -17.85     64.86
REMARK 500    ASN D  45        9.93     59.67
REMARK 500    TYR D  79      -55.06   -121.46
REMARK 500    SER D  86     -159.42   -163.89
REMARK 500    ASP D 156       42.20   -101.34
REMARK 500    PRO D 171       26.14    -59.95
REMARK 500    ASP D 180       53.36    -93.10
REMARK 500    SER D 205      -71.34   -101.86
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                              ZN D 600  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 206   NE2
REMARK 620 2 ASP D 208   OD2 106.4
REMARK 620 3 HIS B  81   ND1 132.1 109.6
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ENF   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN MHC CLASS II IN COMPLEX WITH
REMARK 900 HEMAGGLUTIN VIRUS PEPTIDE
REMARK 900 RELATED ID: 1EWZ   RELATED DB: PDB
REMARK 900 ZINC LOADED STAPHYLOCOCCAL ENTEROTOXIN H
DBREF  1HXY A    1   182  UNP    P01903   2DRA_HUMAN      26    207
DBREF  1HXY B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1HXY C  306   318  GB     6470273  AAF13705       322    334
DBREF  1HXY D    1   213  UNP    P0A0M0   ETXH_STAAU      25    237
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 C   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 D  213  GLU ASP LEU HIS ASP LYS SER GLU LEU THR ASP LEU ALA
SEQRES   2 D  213  LEU ALA ASN ALA TYR GLY GLN TYR ASN HIS PRO PHE ILE
SEQRES   3 D  213  LYS GLU ASN ILE LYS SER ASP GLU ILE SER GLY GLU LYS
SEQRES   4 D  213  ASP LEU ILE PHE ARG ASN GLN GLY ASP SER GLY ASN ASP
SEQRES   5 D  213  LEU ARG VAL LYS PHE ALA THR ALA ASP LEU ALA GLN LYS
SEQRES   6 D  213  PHE LYS ASN LYS ASN VAL ASP ILE TYR GLY ALA SER PHE
SEQRES   7 D  213  TYR TYR LYS CYS GLU LYS ILE SER GLU ASN ILE SER GLU
SEQRES   8 D  213  CYS LEU TYR GLY GLY THR THR LEU ASN SER GLU LYS LEU
SEQRES   9 D  213  ALA GLN GLU ARG VAL ILE GLY ALA ASN VAL TRP VAL ASP
SEQRES  10 D  213  GLY ILE GLN LYS GLU THR GLU LEU ILE ARG THR ASN LYS
SEQRES  11 D  213  LYS ASN VAL THR LEU GLN GLU LEU ASP ILE LYS ILE ARG
SEQRES  12 D  213  LYS ILE LEU SER ASP LYS TYR LYS ILE TYR TYR LYS ASP
SEQRES  13 D  213  SER GLU ILE SER LYS GLY LEU ILE GLU PHE ASP MET LYS
SEQRES  14 D  213  THR PRO ARG ASP TYR SER PHE ASP ILE TYR ASP LEU LYS
SEQRES  15 D  213  GLY GLU ASN ASP TYR GLU ILE ASP LYS ILE TYR GLU ASP
SEQRES  16 D  213  ASN LYS THR LEU LYS SER ASP ASP ILE SER HIS ILE ASP
SEQRES  17 D  213  VAL ASN LEU TYR THR
HET     ZN  D 600       1
HETNAM      ZN ZINC ION
FORMUL   5   ZN    ZN 2+
FORMUL   6  HOH   *88(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 GLU A   55  SER A   77  1                                  23
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 ASP D    5  LEU D    9  5                                   5
HELIX    8   8 THR D   10  HIS D   23  1                                  14
HELIX    9   9 GLY D   47  ASN D   51  5                                   5
HELIX   10  10 THR D   59  LYS D   67  1                                   9
HELIX   11  11 LEU D  135  LYS D  151  1                                  17
HELIX   12  12 ASN D  185  ASP D  190  1                                   6
HELIX   13  13 LYS D  191  GLU D  194  5                                   4
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  O  HIS A  33   N  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  O  PHE A  22   N  VAL A  34
SHEET    4   A 8 HIS A   5  ASN A  15 -1  O  ILE A   8   N  ASP A  25
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B   7   N  ASN A  15
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18
SHEET    7   A 8 GLU B  35  ASP B  41 -1  N  GLU B  35   O  TYR B  32
SHEET    8   A 8 TYR B  47  ALA B  49 -1  N  ARG B  48   O  ARG B  39
SHEET    1   B 4 GLU A  88  THR A  93  0
SHEET    2   B 4 ASN A 103  PHE A 112 -1  N  ILE A 106   O  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  N  PHE A 145   O  PHE A 112
SHEET    4   B 4 SER A 133  GLU A 134 -1  O  SER A 133   N  TYR A 150
SHEET    1   C 4 GLU A  88  THR A  93  0
SHEET    2   C 4 ASN A 103  PHE A 112 -1  N  ILE A 106   O  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  N  PHE A 145   O  PHE A 112
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   D 4 LYS A 126  PRO A 127  0
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   D 4 LEU A 174  GLU A 179 -1  N  LEU A 174   O  VAL A 165
SHEET    1   E 4 LYS B  98  TYR B 102  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  N  VAL B 116   O  TYR B 102
SHEET    3   E 4 PHE B 155  THR B 163 -1  N  PHE B 155   O  PHE B 122
SHEET    4   E 4 VAL B 142  SER B 144 -1  O  VAL B 143   N  MET B 160
SHEET    1   F 4 LYS B  98  TYR B 102  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  N  VAL B 116   O  TYR B 102
SHEET    3   F 4 PHE B 155  THR B 163 -1  N  PHE B 155   O  PHE B 122
SHEET    4   F 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   G 4 GLN B 136  GLU B 137  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   G 4 VAL B 170  GLU B 176 -1  N  THR B 172   O  PHE B 132
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175
SHEET    1   H 3 PHE D  25  ILE D  30  0
SHEET    2   H 3 VAL D  71  GLY D  75 -1  N  VAL D  71   O  ILE D  30
SHEET    3   H 3 THR D  97  LEU D  99 -1  O  THR D  98   N  ASP D  72
SHEET    1   I 4 ASP D  40  PHE D  43  0
SHEET    2   I 4 ASP D  52  LYS D  56 -1  N  LEU D  53   O  PHE D  43
SHEET    3   I 4 SER D  90  TYR D  94  1  O  GLU D  91   N  ARG D  54
SHEET    4   I 4 SER D  77  PHE D  78 -1  O  PHE D  78   N  CYS D  92
SHEET    1   J 5 ASP D 173  ASP D 177  0
SHEET    2   J 5 LYS D 161  MET D 168 -1  N  ILE D 164   O  PHE D 176
SHEET    3   J 5 ILE D 204  TYR D 212 -1  N  SER D 205   O  ASP D 167
SHEET    4   J 5 LYS D 103  VAL D 116  1  O  GLY D 111   N  ILE D 207
SHEET    5   J 5 ILE D 119  GLN D 120 -1  O  ILE D 119   N  VAL D 116
SHEET    1   K 5 ASP D 173  ASP D 177  0
SHEET    2   K 5 LYS D 161  MET D 168 -1  N  ILE D 164   O  PHE D 176
SHEET    3   K 5 ILE D 204  TYR D 212 -1  N  SER D 205   O  ASP D 167
SHEET    4   K 5 LYS D 103  VAL D 116  1  O  GLY D 111   N  ILE D 207
SHEET    5   K 5 GLU D 124  LYS D 130 -1  N  GLU D 124   O  ALA D 112
SHEET    1   L 2 ASN D 132  THR D 134  0
SHEET    2   L 2 THR D 198  LYS D 200 -1  N  LEU D 199   O  VAL D 133
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.05
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.05
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   4 CYS D   82    CYS D   92                          1555   1555  2.04
LINK        ZN    ZN D 600                 NE2 HIS D 206     1555   1555  2.15
LINK        ZN    ZN D 600                 OD2 ASP D 208     1555   1555  2.05
LINK        ZN    ZN D 600                 ND1 HIS B  81     1555   1555  2.11
CISPEP   1 ASN A   15    PRO A   16          0        -0.72
CISPEP   2 THR A  113    PRO A  114          0        -0.34
CISPEP   3 TYR B  123    PRO B  124          0        -0.79
SITE     1 AC1  3 HIS B  81  HIS D 206  ASP D 208
CRYST1  123.624  122.843   48.513  90.00 100.13  90.00 C 1 2 1       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      0.008089  0.000000  0.001445        0.00000
SCALE2      0.000000  0.008140  0.000000        0.00000
SCALE3      0.000000  0.000000  0.020939        0.00000
      
PROCHECK
Go to PROCHECK summary
 References