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PDBsum entry 1lo5

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Top Page protein Protein-protein interface(s) links
Immune system/toxin PDB id
1lo5
Jmol
Contents
Protein chains
179 a.a. *
188 a.a. *
13 a.a. *
233 a.a. *
Waters ×23
* Residue conservation analysis
HEADER    IMMUNE SYSTEM/TOXIN                     06-MAY-02   1LO5
TITLE     CRYSTAL STRUCTURE OF THE D227A VARIANT OF STAPHYLOCOCCAL
TITLE    2 ENTEROTOXIN A IN 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 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   6 SYNONYM: MHC CLASS II (HLA-DR1, DRA 0101)-CHAIN A;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1
COMPND  10 BETA CHAIN;
COMPND  11 CHAIN: B;
COMPND  12 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  13 SYNONYM: MHC CLASS II (HLA-DR1, DRB1 0101)-CHAIN B;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: HEMAGGLUTININ PEPTIDE;
COMPND  17 CHAIN: C;
COMPND  18 ENGINEERED: YES;
COMPND  19 MOL_ID: 4;
COMPND  20 MOLECULE: ENTEROTOXIN A;
COMPND  21 CHAIN: D;
COMPND  22 ENGINEERED: YES;
COMPND  23 MUTATION: 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 SEQUENCE IS PEPTIDE FROM INFLUENZA
SOURCE  20 VIRUS, HEMAGGLUTININ PEPTIDE;
SOURCE  21 MOL_ID: 4;
SOURCE  22 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE  23 ORGANISM_TAXID: 1280;
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: UL635;
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PLR16;
SOURCE  29 EXPRESSION_SYSTEM_GENE: K12
KEYWDS    PROTEIN-PROTEIN COMPLEX, IMMUNE SYSTEM/TOXIN COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.PETERSSON,M.THUNNISSEN,G.FORSBERG,B.WALSE
REVDAT   3   24-FEB-09 1LO5    1       VERSN
REVDAT   2   30-SEP-03 1LO5    1       DBREF
REVDAT   1   18-DEC-02 1LO5    0
JRNL        AUTH   K.PETERSSON,M.THUNNISSEN,G.FORSBERG,B.WALSE
JRNL        TITL   CRYSTAL STRUCTURE OF A SEA VARIANT IN COMPLEX WITH
JRNL        TITL 2 MHC CLASS II REVEALS THE ABILITY OF SEA TO
JRNL        TITL 3 CROSSLINK MHC MOLECULES
JRNL        REF    STRUCTURE                     V.  10  1619 2002
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   12467569
JRNL        DOI    10.1016/S0969-2126(02)00895-X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.20 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) : 3.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1275926.280
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.9
REMARK   3   NUMBER OF REFLECTIONS             : 12279
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) : 0.245
REMARK   3   FREE R VALUE                     : 0.339
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 1003
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011
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) : 3.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1769
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160
REMARK   3   BIN FREE R VALUE                    : 0.4170
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.10
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 155
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5032
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 23
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 46.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.55000
REMARK   3    B22 (A**2) : -11.80000
REMARK   3    B33 (A**2) : 13.34000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39
REMARK   3   ESD FROM SIGMAA              (A) : 0.46
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) : 0.60
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.73
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.98
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 : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 45.40
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1LO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-02.
REMARK 100 THE RCSB ID CODE IS RCSB016129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
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) : 1.076
REMARK 200  MONOCHROMATOR                  : SI 111 MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12279
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200
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     (%) : 91.6
REMARK 200  DATA REDUNDANCY                : 3.100
REMARK 200  R MERGE                    (I) : 0.10100
REMARK 200  R SYM                      (I) : 0.10100
REMARK 200   FOR THE DATA SET  : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.24600
REMARK 200  R SYM FOR SHELL            (I) : 0.24600
REMARK 200   FOR SHELL         : 3.100
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: 1ESF AND 1DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M MES, 24%(W/V)
REMARK 280  POLYETHYLEN GLYCOL MONOMETHYL ETHER 5000, PH 6.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
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       26.00400
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.04100
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.89600
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.04100
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.00400
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.89600
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 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     GLU A     3
REMARK 465     GLY B     1
REMARK 465     ASP B     2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OD2  ASP D   156     NH2  ARG D   160              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    PHE B 122   N   -  CA  -  C   ANGL. DEV. =  17.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A  46      -33.40    -37.49
REMARK 500    ALA A  52     -156.56   -107.19
REMARK 500    PHE A  54      110.85   -177.67
REMARK 500    GLU A  55       81.71    -59.66
REMARK 500    ALA A  56      -35.99    -38.45
REMARK 500    ILE A  72      -71.80    -49.33
REMARK 500    THR A  90       83.71   -152.78
REMARK 500    PRO A  96      104.12    -35.74
REMARK 500    PRO A 102      157.59    -39.54
REMARK 500    THR A 129       28.14   -149.46
REMARK 500    VAL A 136      172.49    -54.96
REMARK 500    PHE A 153      145.73   -172.76
REMARK 500    PRO A 155      167.89    -39.60
REMARK 500    SER A 156     -173.05   -177.92
REMARK 500    PRO A 173      160.18    -39.83
REMARK 500    THR B  21       -8.56   -172.37
REMARK 500    ASN B  33      -89.80     67.14
REMARK 500    GLN B  34       11.65   -143.52
REMARK 500    GLU B  52      -38.22    -35.48
REMARK 500    TYR B  60      -98.70    -55.07
REMARK 500    TRP B  61      -58.15    -26.14
REMARK 500    ARG B  71       -9.62    -45.52
REMARK 500    ALA B  74       -6.69    -46.53
REMARK 500    TYR B  78      -83.52   -107.57
REMARK 500    THR B  90      -70.77   -119.84
REMARK 500    LYS B 105       67.07     87.44
REMARK 500    THR B 106      121.71    -32.36
REMARK 500    LEU B 109      135.45      2.34
REMARK 500    GLN B 110       -5.77     78.94
REMARK 500    HIS B 112      129.11     -3.92
REMARK 500    ASN B 113     -163.42   -128.45
REMARK 500    PHE B 122      178.23    -14.60
REMARK 500    TYR B 123      117.24    116.92
REMARK 500    PRO B 124     -172.81    -64.16
REMARK 500    SER B 126      102.66    -36.98
REMARK 500    VAL B 142       72.04   -104.88
REMARK 500    TRP B 153       46.47     77.09
REMARK 500    GLN B 156      102.49   -167.53
REMARK 500    THR B 163     -153.93   -149.90
REMARK 500    PRO B 165       77.30    -51.13
REMARK 500    PRO B 178        0.58    -65.48
REMARK 500    LYS D  10      149.25    -33.24
REMARK 500    GLU D  17        4.00    -60.70
REMARK 500    THR D  21       -0.44    -42.83
REMARK 500    TYR D  31      -64.79   -100.45
REMARK 500    ASN D  33      158.00    -49.09
REMARK 500    LYS D  37       81.82   -174.20
REMARK 500    SER D  43      146.24    132.01
REMARK 500    PHE D  47      -84.09   -117.35
REMARK 500    PHE D  54       75.66   -107.03
REMARK 500    LYS D  55      121.01    -39.51
REMARK 500    ASP D  60       35.46    103.81
REMARK 500    TRP D  63      -57.08   -132.66
REMARK 500    ASN D  65        3.84   -168.76
REMARK 500    TYR D  88       74.01   -174.18
REMARK 500    GLN D  95      -43.12    100.13
REMARK 500    PRO D 101      137.50    -36.18
REMARK 500    ASN D 102      -15.75     54.44
REMARK 500    ASP D 115      137.68    -33.50
REMARK 500    LEU D 131       78.62   -113.55
REMARK 500    ASP D 132       49.28     83.56
REMARK 500    THR D 145      129.77   -175.29
REMARK 500    PHE D 175       42.54    -66.89
REMARK 500    ASP D 176      100.78     33.60
REMARK 500    LYS D 178      -48.59    -26.34
REMARK 500    ASN D 223      -19.10     74.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ESF   RELATED DB: PDB
REMARK 900 1ESF CONTAINS CRYSTAL STRUCTURE OF STAPHYLOCOCCAL
REMARK 900 ENTEROTOXIN A
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 1DLH CONTAINS CRYSTAL STRUCTURE OF HUMAN MHC CLASS II
REMARK 900 COMPLEXED WITH HEMAGGLUTININ PEPTIDE
DBREF  1LO5 A    1   182  UNP    P01903   2DRA_HUMAN      26    207
DBREF  1LO5 B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1LO5 D    1   233  UNP    P0A0L2   ETXA_STAAU      25    257
DBREF  1LO5 C  306   318  PDB    1LO5     1LO5           306    318
SEQADV 1LO5 ALA D  227  UNP  P0A0L2    ASP   251 ENGINEERED
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  233  SER GLU LYS SER GLU GLU ILE ASN GLU LYS ASP LEU ARG
SEQRES   2 D  233  LYS LYS SER GLU LEU GLN GLY THR ALA LEU GLY ASN LEU
SEQRES   3 D  233  LYS GLN ILE TYR TYR TYR ASN GLU LYS ALA LYS THR GLU
SEQRES   4 D  233  ASN LYS GLU SER HIS ASP GLN PHE LEU GLN HIS THR ILE
SEQRES   5 D  233  LEU PHE LYS GLY PHE PHE THR ASP HIS SER TRP TYR ASN
SEQRES   6 D  233  ASP LEU LEU VAL ASP PHE ASP SER LYS ASP ILE VAL ASP
SEQRES   7 D  233  LYS TYR LYS GLY LYS LYS VAL ASP LEU TYR GLY ALA TYR
SEQRES   8 D  233  TYR GLY TYR GLN CYS ALA GLY GLY THR PRO ASN LYS THR
SEQRES   9 D  233  ALA CYS MET TYR GLY GLY VAL THR LEU HIS ASP ASN ASN
SEQRES  10 D  233  ARG LEU THR GLU GLU LYS LYS VAL PRO ILE ASN LEU TRP
SEQRES  11 D  233  LEU ASP GLY LYS GLN ASN THR VAL PRO LEU GLU THR VAL
SEQRES  12 D  233  LYS THR ASN LYS LYS ASN VAL THR VAL GLN GLU LEU ASP
SEQRES  13 D  233  LEU GLN ALA ARG ARG TYR LEU GLN GLU LYS TYR ASN LEU
SEQRES  14 D  233  TYR ASN SER ASP VAL PHE ASP GLY LYS VAL GLN ARG GLY
SEQRES  15 D  233  LEU ILE VAL PHE HIS THR SER THR GLU PRO SER VAL ASN
SEQRES  16 D  233  TYR ASP LEU PHE GLY ALA GLN GLY GLN TYR SER ASN THR
SEQRES  17 D  233  LEU LEU ARG ILE TYR ARG ASP ASN LYS THR ILE ASN SER
SEQRES  18 D  233  GLU ASN MET HIS ILE ALA ILE TYR LEU TYR THR SER
FORMUL   5  HOH   *23(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 ALA A   56  SER A   77  1                                  22
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  ASN B   62  1                                   9
HELIX    5   5 GLN B   64  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLY B   86  1                                   9
HELIX    7   7 GLU B   87  THR B   90  5                                   4
HELIX    8   8 THR D   21  TYR D   31  1                                  11
HELIX    9   9 SER D   73  LYS D   81  1                                   9
HELIX   10  10 PRO D  139  THR D  142  5                                   4
HELIX   11  11 VAL D  152  ASN D  168  1                                  17
HELIX   12  12 TYR D  205  LEU D  210  1                                   6
HELIX   13  13 ARG D  211  ASN D  216  5                                   6
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  24   O  PHE A  32
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  LEU A  14   O  SER A  19
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  29   N  LYS B  12
SHEET    7   A 8 GLU B  35  PHE B  40 -1  O  VAL B  38   N  CYS B  30
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  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  O  ILE A 106   N  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109
SHEET    4   B 4 SER A 133  PRO A 139 -1  N  SER A 133   O  TYR A 150
SHEET    1   C 3 ASN A 118  ARG A 123  0
SHEET    2   C 3 TYR A 161  GLU A 166 -1  O  GLU A 166   N  ASN A 118
SHEET    3   C 3 HIS A 177  TRP A 178 -1  O  TRP A 178   N  TYR A 161
SHEET    1   D 2 ASN B 113  SER B 118  0
SHEET    2   D 2 LEU B 158  THR B 163 -1  O  LEU B 161   N  LEU B 115
SHEET    1   E 4 GLN B 136  GLU B 138  0
SHEET    2   E 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   E 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   E 4 LEU B 184  ARG B 189 -1  O  VAL B 186   N  CYS B 173
SHEET    1   F 3 THR D  51  LEU D  53  0
SHEET    2   F 3 ASP D  66  ASP D  70 -1  O  VAL D  69   N  ILE D  52
SHEET    3   F 3 THR D 104  MET D 107  1  O  ALA D 105   N  LEU D  68
SHEET    1   G 2 VAL D  85  LEU D  87  0
SHEET    2   G 2 VAL D 111  LEU D 113 -1  O  THR D 112   N  ASP D  86
SHEET    1   H 2 ARG D 118  VAL D 125  0
SHEET    2   H 2 VAL D 143  LYS D 147 -1  O  VAL D 143   N  VAL D 125
SHEET    1   I 5 GLN D 135  ASN D 136  0
SHEET    2   I 5 ILE D 127  TRP D 130 -1  N  LEU D 129   O  ASN D 136
SHEET    3   I 5 HIS D 225  TYR D 231  1  O  ILE D 228   N  ASN D 128
SHEET    4   I 5 ARG D 181  HIS D 187 -1  N  LEU D 183   O  TYR D 229
SHEET    5   I 5 VAL D 194  ASN D 195 -1  O  VAL D 194   N  PHE D 186
SHEET    1   J 2 ASN D 149  THR D 151  0
SHEET    2   J 2 THR D 218  ASN D 220 -1  O  ILE D 219   N  VAL D 150
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04
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   96    CYS D  106                          1555   1555  2.03
CISPEP   1 ASN A   15    PRO A   16          0         2.05
CISPEP   2 THR A  113    PRO A  114          0        -0.40
CISPEP   3 TYR B  123    PRO B  124          0        -0.11
CRYST1   52.008   75.792  198.082  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      0.019228  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013194  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005048        0.00000
      
PROCHECK
Go to PROCHECK summary
 References