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PDBsum entry 1jwu

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Top Page protein Protein-protein interface(s) links
Immune system PDB id
1jwu
Jmol
Contents
Protein chains
180 a.a. *
187 a.a. *
13 a.a. *
232 a.a. *
Waters ×178
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           05-SEP-01   1JWU
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS II
TITLE    2 MOLECULE HLA-DR1 (HA PEPTIDE 306-318) WITH THE
TITLE    3 SUPERANTIGEN SEC3 VARIANT 3B2
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: HA PEPTIDE;
COMPND  13 CHAIN: C;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 4;
COMPND  16 MOLECULE: ENTEROTOXIN TYPE C-3;
COMPND  17 CHAIN: D;
COMPND  18 SYNONYM: SEC3;
COMPND  19 ENGINEERED: YES;
COMPND  20 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 MOL_ID: 2;
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   9 ORGANISM_COMMON: HUMAN;
SOURCE  10 ORGANISM_TAXID: 9606;
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  13 MOL_ID: 3;
SOURCE  14 SYNTHETIC: YES;
SOURCE  15 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED;
SOURCE  16 MOL_ID: 4;
SOURCE  17 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE  18 ORGANISM_TAXID: 1280;
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HLA-DR1 ALPHA SUBUNIT, HLA-DR1 BETA SUBUNIT, MUTATION,
KEYWDS   2 IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.J.SUNDBERG,P.S.ANDERSEN,P.M.SCHLIEVERT,K.KARJALAINEN,
AUTHOR   2 R.A.MARIUZZA
REVDAT   3   24-FEB-09 1JWU    1       VERSN
REVDAT   2   30-SEP-03 1JWU    1       AUTHOR JRNL
REVDAT   1   08-JUL-03 1JWU    0
JRNL        AUTH   E.J.SUNDBERG,P.S.ANDERSEN,P.M.SCHLIEVERT,
JRNL        AUTH 2 K.KARJALAINEN,R.A.MARIUZZA
JRNL        TITL   STRUCTURAL, ENERGETIC, AND FUNCTIONAL ANALYSIS OF
JRNL        TITL 2 A PROTEIN-PROTEIN INTERFACE AT DISTINCT STAGES OF
JRNL        TITL 3 AFFINITY MATURATION
JRNL        REF    STRUCTURE                     V.  11  1151 2003
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   12962633
JRNL        DOI    10.1016/S0969-2126(03)00187-4
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.30 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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 160762.020
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.8
REMARK   3   NUMBER OF REFLECTIONS             : 50448
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) : 0.200
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2548
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6439
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 338
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5015
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 178
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.58000
REMARK   3    B22 (A**2) : 2.22000
REMARK   3    B33 (A**2) : -4.80000
REMARK   3    B12 (A**2) : 5.37000
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) : 0.27
REMARK   3   ESD FROM SIGMAA              (A) : 0.24
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) : 0.33
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.40
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
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        : 0.34
REMARK   3   BSOL        : 28.82
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_REP.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 1JWU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-01.
REMARK 100 THE RCSB ID CODE IS RCSB014277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X12B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97813
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58678
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06700
REMARK 200   FOR THE DATA SET  : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.42100
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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   (%): 73.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, ETHYLENE
REMARK 280  GLYCOL, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       85.87650
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.58082
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.16300
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       85.87650
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.58082
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.16300
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       85.87650
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.58082
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.16300
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.16164
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       80.32600
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.16164
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       80.32600
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.16164
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       80.32600
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     PRO B   108
REMARK 465     LEU B   109
REMARK 465     GLN B   110
REMARK 465     ASP D    99
REMARK 465     ASN D   100
REMARK 465     VAL D   101
REMARK 465     GLY D   102
REMARK 465     LYS D   103
REMARK 465     VAL D   104
REMARK 465     THR D   105
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 D   1    CG   CD   OE1  OE2
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   O    LEU B     8     O    TYR B    32              2.13
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      -52.93   -122.98
REMARK 500    TYR B  32      -89.85    -72.98
REMARK 500    ASN B  33      -75.49    -91.52
REMARK 500    ASP B  76      -64.42    -97.61
REMARK 500    THR B  90      -78.24   -129.56
REMARK 500    THR B 106      -98.91   -156.87
REMARK 500    PRO B 124     -175.54    -66.80
REMARK 500    GLU B 137      136.44    -34.71
REMARK 500    PHE D  44      -63.45    -97.50
REMARK 500    LYS D  57      -93.52    -54.82
REMARK 500    TYR D  61      154.31    178.45
REMARK 500    PHE D  95      145.69    173.32
REMARK 500    SER D  97      116.40     69.45
REMARK 500    ASP D 124       64.01    -66.30
REMARK 500    ASN D 125       10.76    170.43
REMARK 500    PHE D 145     -169.37   -166.39
REMARK 500    LYS D 171       10.38   -140.52
REMARK 500    SER D 178      178.48     99.33
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 C 139        DISTANCE =  5.28 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JWM   RELATED DB: PDB
REMARK 900 1JWM CONTAINS COMPLEX OF THE MHC CLASS II MOLECULE HLA-DR1
REMARK 900 (HA PEPTIDE 306-318) WITH THE SUPERANTIGEN SEC3
REMARK 900 RELATED ID: 1JWS   RELATED DB: PDB
REMARK 900 1JWS CONTAINS K43G, F44M, L45F, A46N, H47W MUTATIONS IN SEC3
DBREF  1JWU A    1   182  UNP    P01903   2DRA_HUMAN      26    207
DBREF  1JWU B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1JWU D    1   239  UNP    P0A0L5   ENTC3_STAAU     28    266
DBREF  1JWU C  306   318  PDB    1JWU     1JWU           306    318
SEQADV 1JWU SER D   43  UNP  P0A0L5    LYS    70 ENGINEERED
SEQADV 1JWU PHE D   45  UNP  P0A0L5    LEU    72 ENGINEERED
SEQADV 1JWU LYS D   46  UNP  P0A0L5    ALA    73 ENGINEERED
SEQADV 1JWU TRP D   47  UNP  P0A0L5    HIS    74 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  239  GLU SER GLN PRO ASP PRO MET PRO ASP ASP LEU HIS LYS
SEQRES   2 D  239  SER SER GLU PHE THR GLY THR MET GLY ASN MET LYS TYR
SEQRES   3 D  239  LEU TYR ASP ASP HIS TYR VAL SER ALA THR LYS VAL LYS
SEQRES   4 D  239  SER VAL ASP SER PHE PHE LYS TRP ASP LEU ILE TYR ASN
SEQRES   5 D  239  ILE SER ASP LYS LYS LEU LYS ASN TYR ASP LYS VAL LYS
SEQRES   6 D  239  THR GLU LEU LEU ASN GLU ASP LEU ALA LYS LYS TYR LYS
SEQRES   7 D  239  ASP GLU VAL VAL ASP VAL TYR GLY SER ASN TYR TYR VAL
SEQRES   8 D  239  ASN CYS TYR PHE SER SER LYS ASP ASN VAL GLY LYS VAL
SEQRES   9 D  239  THR GLY GLY LYS THR CYS MET TYR GLY GLY ILE THR LYS
SEQRES  10 D  239  HIS GLU GLY ASN HIS PHE ASP ASN GLY ASN LEU GLN ASN
SEQRES  11 D  239  VAL LEU VAL ARG VAL TYR GLU ASN LYS ARG ASN THR ILE
SEQRES  12 D  239  SER PHE GLU VAL GLN THR ASP LYS LYS SER VAL THR ALA
SEQRES  13 D  239  GLN GLU LEU ASP ILE LYS ALA ARG ASN PHE LEU ILE ASN
SEQRES  14 D  239  LYS LYS ASN LEU TYR GLU PHE ASN SER SER PRO TYR GLU
SEQRES  15 D  239  THR GLY TYR ILE LYS PHE ILE GLU ASN ASN GLY ASN THR
SEQRES  16 D  239  PHE TRP TYR ASP MET MET PRO ALA PRO GLY ASP LYS PHE
SEQRES  17 D  239  ASP GLN SER LYS TYR LEU MET MET TYR ASN ASP ASN LYS
SEQRES  18 D  239  THR VAL ASP SER LYS SER VAL LYS ILE GLU VAL HIS LEU
SEQRES  19 D  239  THR THR LYS ASN GLY
FORMUL   5  HOH   *178(H2 O)
HELIX    1   1 GLU A   47  ALA A   52  1                                   6
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  SER B   63  1                                  10
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 MET D    7  LEU D   11  5                                   5
HELIX    8   8 LYS D   13  PHE D   17  5                                   5
HELIX    9   9 MET D   21  ASP D   29  1                                   9
HELIX   10  10 ASN D   70  ASP D   79  1                                  10
HELIX   11  11 ALA D  156  ASN D  172  1                                  17
HELIX   12  12 ASP D  209  MET D  215  1                                   7
HELIX   13  13 MET D  216  ASN D  220  5                                   5
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  PHE A  24   O  ILE A  31
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ALA A  10   O  MET A  23
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7
SHEET    6   A 8 ARG B  23  ILE B  31 -1  O  ARG B  25   N  HIS B  16
SHEET    7   A 8 GLU B  36  ASP B  41 -1  O  PHE B  40   N  GLU B  28
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  LEU A 151   N  LEU A 105
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  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  O  ILE A 106   N  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105
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  ARG A 164   N  THR A 120
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
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  O  GLN B 174   N  ARG B 130
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  TRP B 188   N  TYR B 171
SHEET    1   H 3 VAL D  33  VAL D  38  0
SHEET    2   H 3 VAL D  82  GLY D  86 -1  O  VAL D  82   N  VAL D  38
SHEET    3   H 3 ILE D 115  LYS D 117 -1  O  THR D 116   N  ASP D  83
SHEET    1   I 3 ASP D  48  ASN D  52  0
SHEET    2   I 3 LYS D  63  GLU D  67 -1  O  VAL D  64   N  TYR D  51
SHEET    3   I 3 LYS D 108  TYR D 112  1  O  MET D 111   N  GLU D  67
SHEET    1   J 5 ARG D 140  THR D 149  0
SHEET    2   J 5 GLN D 129  GLU D 137 -1  N  VAL D 133   O  PHE D 145
SHEET    3   J 5 LYS D 229  THR D 235  1  O  LEU D 234   N  TYR D 136
SHEET    4   J 5 THR D 183  ILE D 189 -1  N  LYS D 187   O  GLU D 231
SHEET    5   J 5 THR D 195  ASP D 199 -1  O  PHE D 196   N  PHE D 188
SHEET    1   K 2 SER D 153  THR D 155  0
SHEET    2   K 2 THR D 222  ASP D 224 -1  O  VAL D 223   N  VAL D 154
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   4 CYS D   93    CYS D  110                          1555   1555  2.04
CISPEP   1 ASN A   15    PRO A   16          0        -0.12
CISPEP   2 THR A  113    PRO A  114          0         0.19
CISPEP   3 TYR B  123    PRO B  124          0         0.09
CRYST1  171.753  171.753  120.489  90.00  90.00 120.00 H 3           9
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      0.005822  0.003362  0.000000        0.00000
SCALE2      0.000000  0.006723  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008300        0.00000
      
PROCHECK
Go to PROCHECK summary
 References