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PDBsum entry 4ah2

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Immune system PDB id
4ah2
Jmol
Contents
Protein chains
177 a.a.
198 a.a.
Ligands
GOL ×4
Waters ×220
HEADER    IMMUNE SYSTEM                           03-FEB-12   4AH2
TITLE     HLA-DR1 WITH COVALENTLY LINKED CLIP106-120 IN CANONICAL ORIENTATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 26-217;
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN, HLA
COMPND   9  CLASS II HISTOCOMPATIBILITY ANTIGEN\,DRB1-1 BETA CHAIN;
COMPND  10 CHAIN: B;
COMPND  11 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 106-120,30-227;
COMPND  12 SYNONYM: HLA-DR ANTIGENS-ASSOCIATED INVARIANT CHAIN, IA ANTIGEN-
COMPND  13  ASSOCIATED INVARIANT CHAIN\,II, P33, CD74, MHC CLASS II ANTIGEN
COMPND  14  DRB1*1, DR-1, DR;
COMPND  15 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: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET11A;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS, HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN, HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606, 9606;
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PET24D
KEYWDS    MHC II, IMMUNE SYSTEM, SELF ANTIGEN, INVARIANT CHAIN, CLIP
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.SCHLUNDT,S.GUENTHER,J.STICHT,M.WIECZOREK,Y.ROSKE,U.HEINEMANN,
AUTHOR   2 C.FREUND
REVDAT   2   10-OCT-12 4AH2    1       JRNL
REVDAT   1   01-AUG-12 4AH2    0
JRNL        AUTH   A.SCHLUNDT,S.GUNTHER,J.STICHT,M.WIECZOREK,Y.ROSKE,
JRNL        AUTH 2 U.HEINEMANN,C.FREUND
JRNL        TITL   PEPTIDE LINKAGE TO THE ALPHA-SUBUNIT OF MHCII CREATES A
JRNL        TITL 2 STABLY INVERTED ANTIGEN PRESENTATION COMPLEX.
JRNL        REF    J.MOL.BIOL.                   V. 423   294 2012
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   22820093
JRNL        DOI    10.1016/J.JMB.2012.07.008
REMARK   2
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.833
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.99
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.90
REMARK   3   NUMBER OF REFLECTIONS             : 21132
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1939
REMARK   3   R VALUE            (WORKING SET) : 0.1914
REMARK   3   FREE R VALUE                     : 0.2402
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1057
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 32.8359 -  4.7160    1.00     2656   140  0.1815 0.2080
REMARK   3     2  4.7160 -  3.7449    1.00     2540   134  0.1515 0.2075
REMARK   3     3  3.7449 -  3.2720    1.00     2513   132  0.1852 0.2334
REMARK   3     4  3.2720 -  2.9731    1.00     2487   131  0.1973 0.2593
REMARK   3     5  2.9731 -  2.7601    1.00     2474   130  0.2152 0.2627
REMARK   3     6  2.7601 -  2.5975    1.00     2492   131  0.2279 0.2985
REMARK   3     7  2.5975 -  2.4674    1.00     2449   129  0.2384 0.3043
REMARK   3     8  2.4674 -  2.3600    1.00     2464   130  0.2320 0.2621
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.20
REMARK   3   SHRINKAGE RADIUS   : 0.98
REMARK   3   K_SOL              : 0.343
REMARK   3   B_SOL              : 27.165
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.76
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.41
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 27.9
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.8
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -6.9457
REMARK   3    B22 (A**2) : -4.6013
REMARK   3    B33 (A**2) : 11.5470
REMARK   3    B12 (A**2) : 0.0000
REMARK   3    B13 (A**2) : 0.0000
REMARK   3    B23 (A**2) : 0.0000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           3161
REMARK   3   ANGLE     :  1.019           4285
REMARK   3   CHIRALITY :  0.071            461
REMARK   3   PLANARITY :  0.005            555
REMARK   3   DIHEDRAL  : 15.999           1155
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES A0 TO A3, A181 TO A192, B-16 TO
REMARK   3  B-1, B105 TO B110, B190 TO B198 ARE MISSING COMPLETELY DUE TO
REMARK   3  DISORDER, RESIDUES B111, B112, B166 COULD ONLY BE MODELED TO THE
REMARK   3  CBETA-ATOM DUE TO DISORDER
REMARK   4
REMARK   4 4AH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-12.
REMARK 100 THE PDBE ID CODE IS EBI-51139.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21133
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.36
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.84
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 4.8
REMARK 200  R MERGE                    (I) : 0.13
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.9
REMARK 200  R MERGE FOR SHELL          (I) : 0.70
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3PDO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LICL, 20% (W/V) PEG6000, 0.1 M
REMARK 280  HEPES, PH 7.0
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       28.82200
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.66550
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.80800
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.66550
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.82200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.80800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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     MET A     0
REMARK 465     ILE A     1
REMARK 465     LYS A     2
REMARK 465     GLU A     3
REMARK 465     ASP A   181
REMARK 465     ALA A   182
REMARK 465     PRO A   183
REMARK 465     SER A   184
REMARK 465     PRO A   185
REMARK 465     LEU A   186
REMARK 465     PRO A   187
REMARK 465     GLU A   188
REMARK 465     THR A   189
REMARK 465     THR A   190
REMARK 465     GLU A   191
REMARK 465     ASN A   192
REMARK 465     PRO B   -16
REMARK 465     MET B   -15
REMARK 465     GLY B   -14
REMARK 465     GLY B   -13
REMARK 465     GLY B   -12
REMARK 465     GLY B   -11
REMARK 465     SER B   -10
REMARK 465     GLY B    -9
REMARK 465     GLY B    -8
REMARK 465     GLY B    -7
REMARK 465     GLY B    -6
REMARK 465     SER B    -5
REMARK 465     GLY B    -4
REMARK 465     GLY B    -3
REMARK 465     GLY B    -2
REMARK 465     GLY B    -1
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     ALA B   190
REMARK 465     ARG 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 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     HIS B 111    CG   ND1  CD2  CE1  NE2
REMARK 470     HIS B 112    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG B 166    CG   CD   NE   CZ   NH1  NH2
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    ARG A 100       14.63     47.87
REMARK 500    ASN B  33     -105.11     51.84
REMARK 500    TYR B  78      -63.76   -130.64
REMARK 500    THR B  90      -73.65   -124.08
REMARK 500    HIS B 112      -64.13   -151.80
REMARK 500    ASN B 134     -120.23     42.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1190
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A6A   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC
REMARK 900  MATURATION: CLIP BOUND TO HLA-DR3
REMARK 900 RELATED ID: 1AQD   RELATED DB: PDB
REMARK 900  HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II
REMARK 900  HISTOCOMPATIBILITYPROTEIN (EXTRACELLULAR DOMAIN) COMPLEXED
REMARK 900  WITH ENDOGENOUSPEPTIDE
REMARK 900 RELATED ID: 1D5M   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH
REMARK 900  PEPTIDE
REMARK 900 RELATED ID: 1D5X   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH
REMARK 900  DIPEPTIDE MIMETIC
REMARK 900 RELATED ID: 1D5Z   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH
REMARK 900  PEPTIDOMIMETIC
REMARK 900 RELATED ID: 1D6E   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR4 COMPLEX WITH PEPTIDOMIMETIC
REMARK 900   AND SEB
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 RELATED ID: 1FV1   RELATED DB: PDB
REMARK 900  STRUCTURAL BASIS FOR THE BINDING OF AN
REMARK 900  IMMUNODOMINANTPEPTIDE FROM MYELIN BASIC PROTEIN IN
REMARK 900  DIFFERENT REGISTERS BYTWO HLA-DR2 ALLELES
REMARK 900 RELATED ID: 1FYT   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA
REMARK 900  -T CELLRECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC
REMARK 900   CLASS IIMOLECULE, HLA-DR1
REMARK 900 RELATED ID: 1H15   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HLA-DRA1*0101/DRB5*0101
REMARK 900  COMPLEXED WITH A PEPTIDE FROM EPSTEIN BARR VIRUS DNA
REMARK 900  POLYMERASE.
REMARK 900 RELATED ID: 1HXY   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H
REMARK 900  INCOMPLEX WITH HUMAN MHC CLASS II
REMARK 900 RELATED ID: 1ICF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II
REMARK 900  FRAGMENT IN COMPLEX WITH CATHEPSIN L
REMARK 900 RELATED ID: 1IIE   RELATED DB: PDB
REMARK 900  MHC CLASS II-ASSOCIATED INVARIANT CHAIN (II) HUMAN
REMARK 900  ECTOPLASMIC TRIMERIZATION DOMAIN
REMARK 900 RELATED ID: 1J8H   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA
REMARK 900  -T CELLRECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC
REMARK 900   CLASS IIMOLECULE, HLA-DR4
REMARK 900 RELATED ID: 1JWM   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900  IIMOLECULE HLA-DR1(HA PEPTIDE 306-318) WITH THE
REMARK 900  SUPERANTIGENSEC3
REMARK 900 RELATED ID: 1JWS   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900  IIMOLECULE HLA-DR1 (HA PEPTIDE 306-318) WITH
REMARK 900  THESUPERANTIGEN SEC3 VARIANT 3B1
REMARK 900 RELATED ID: 1JWU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900  IIMOLECULE HLA-DR1 (HA PEPTIDE 306-318) WITH
REMARK 900  THESUPERANTIGEN SEC3 VARIANT 3B2
REMARK 900 RELATED ID: 1KG0   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE EPSTEIN-BARR VIRUS GP42 PROTEIN BOUND
REMARK 900   TOTHE MHC CLASS II RECEPTOR HLA-DR1
REMARK 900 RELATED ID: 1KLG   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR1/TPI(23-37, THR28-->ILE
REMARK 900   MUTANT)COMPLEXED WITH STAPHYLOCOCCAL ENTEROTOXIN C3
REMARK 900  VARIANT 3B2(SEC3-3B2)
REMARK 900 RELATED ID: 1KLU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR1/TPI(23-37) COMPLEXED
REMARK 900  WITHSTAPHYLOCOCCAL ENTEROTOXIN C3 VARIANT 3B2 (SEC3-3B2)
REMARK 900 RELATED ID: 1L3H   RELATED DB: PDB
REMARK 900  NMR STRUCTURE OF P41ICF, A POTENT INHIBITOR OF
REMARK 900  HUMANCATHEPSIN L
REMARK 900 RELATED ID: 1LO5   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE D227A VARIANT OF
REMARK 900  STAPHYLOCOCCALENTEROTOXIN A IN COMPLEX WITH HUMAN MHC
REMARK 900  CLASS II
REMARK 900 RELATED ID: 1MUJ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MURINE CLASS II MHC I-AB IN
REMARK 900  COMPLEXWITH A HUMAN CLIP PEPTIDE
REMARK 900 RELATED ID: 1SEB   RELATED DB: PDB
REMARK 900  COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-
REMARK 900  DR1 ANDTHE BACTERIAL SUPERANTIGEN SEB
REMARK 900 RELATED ID: 1SJE   RELATED DB: PDB
REMARK 900  HLA-DR1 COMPLEXED WITH A 16 RESIDUE HIV CAPSID
REMARK 900  PEPTIDEBOUND IN A HAIRPIN CONFORMATION
REMARK 900 RELATED ID: 1SJH   RELATED DB: PDB
REMARK 900  HLA-DR1 COMPLEXED WITH A 13 RESIDUE HIV CAPSID
REMARK 900  PEPTIDE
REMARK 900 RELATED ID: 1T5W   RELATED DB: PDB
REMARK 900  HLA-DR1 IN COMPLEX WITH A SYNTHETIC PEPTIDE(
REMARK 900  AAYSDQATPLLLSPR)
REMARK 900 RELATED ID: 1T5X   RELATED DB: PDB
REMARK 900  HLA-DR1 IN COMPLEX WITH A SYNTHETIC PEPTIDE(
REMARK 900  AAYSDQATPLLLSPR) AND THE SUPERANTIGEN SEC3-3B2
REMARK 900 RELATED ID: 1YMM   RELATED DB: PDB
REMARK 900  TCR/HLA-DR2B/MBP-PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1ZGL   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF 3A6 TCR BOUND TO MBP/HLA-DR2A
REMARK 900 RELATED ID: 2G9H   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN I (SEI)
REMARK 900  INCOMPLEX WITH A HUMAN MHC CLASS II MOLECULE
REMARK 900 RELATED ID: 2SEB   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH A
REMARK 900   PEPTIDE FROM HUMAN COLLAGEN II
REMARK 900 RELATED ID: 2XN9   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN HUMAN
REMARK 900  T CELL RECEPTOR, STAPHYLOCOCCAL ENTEROTOXIN H AND HUMAN
REMARK 900   MAJOR HISTOCOMPATIBILITY COMPLEX CLASS II
REMARK 900 RELATED ID: 3PDO   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR1 WITH CLIP102-120
REMARK 900 RELATED ID: 3PGC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR1 WITH CLIP106-120, FLIPPED
REMARK 900  PEPTIDE ORIENTATION
REMARK 900 RELATED ID: 3PGD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HLA-DR1 WITH CLIP106-120, CANONICAL
REMARK 900   PEPTIDE ORIENTATION
REMARK 900 RELATED ID: 4AEN   RELATED DB: PDB
REMARK 900  HLA-DR1 WITH COVALENTLY LINKED CLIP106-120 IN REVERSED
REMARK 900   ORIENTATION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLIP WAS ATTACHED TO THE N-TERMINUS OF MHC BETA-CHAIN DURING
REMARK 999 EXPRESSION VIA A (GGGGS)3 LINKER.
DBREF  4AH2 A    1   192  UNP    P01903   DRA_HUMAN       26    217
DBREF  4AH2 B  -29   -15  UNP    P04233   HG2A_HUMAN     106    120
DBREF  4AH2 B    1   198  UNP    P04229   2B11_HUMAN      30    227
SEQADV 4AH2 MET A    0  UNP  P01903              EXPRESSION TAG
SEQADV 4AH2 MET B  -30  UNP  P04229              EXPRESSION TAG
SEQADV 4AH2 GLY B  -14  UNP  P04229              LINKER
SEQADV 4AH2 GLY B  -13  UNP  P04229              LINKER
SEQADV 4AH2 GLY B  -12  UNP  P04229              LINKER
SEQADV 4AH2 GLY B  -11  UNP  P04229              LINKER
SEQADV 4AH2 SER B  -10  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -9  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -8  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -7  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -6  UNP  P04229              LINKER
SEQADV 4AH2 SER B   -5  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -4  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -3  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -2  UNP  P04229              LINKER
SEQADV 4AH2 GLY B   -1  UNP  P04229              LINKER
SEQADV 4AH2 SER B    0  UNP  P04229              LINKER
SEQRES   1 A  193  MET ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE
SEQRES   2 A  193  TYR LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP
SEQRES   3 A  193  PHE ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS
SEQRES   4 A  193  LYS GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE
SEQRES   5 A  193  ALA SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA
SEQRES   6 A  193  VAL ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER
SEQRES   7 A  193  ASN TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR
SEQRES   8 A  193  VAL LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN
SEQRES   9 A  193  VAL LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL
SEQRES  10 A  193  VAL ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR
SEQRES  11 A  193  THR GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP
SEQRES  12 A  193  HIS LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO
SEQRES  13 A  193  SER THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP
SEQRES  14 A  193  GLY LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES  15 A  193  ALA PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 B  229  MET LYS MET ARG MET ALA THR PRO LEU LEU MET GLN ALA
SEQRES   2 B  229  LEU PRO MET GLY GLY GLY GLY SER GLY GLY GLY GLY SER
SEQRES   3 B  229  GLY GLY GLY GLY SER GLY ASP THR ARG PRO ARG PHE LEU
SEQRES   4 B  229  TRP GLN LEU LYS PHE GLU CYS HIS PHE PHE ASN GLY THR
SEQRES   5 B  229  GLU ARG VAL ARG LEU LEU GLU ARG CYS ILE TYR ASN GLN
SEQRES   6 B  229  GLU GLU SER VAL ARG PHE ASP SER ASP VAL GLY GLU TYR
SEQRES   7 B  229  ARG ALA VAL THR GLU LEU GLY ARG PRO ASP ALA GLU TYR
SEQRES   8 B  229  TRP ASN SER GLN LYS ASP LEU LEU GLU GLN ARG ARG ALA
SEQRES   9 B  229  ALA VAL ASP THR TYR CYS ARG HIS ASN TYR GLY VAL GLY
SEQRES  10 B  229  GLU SER PHE THR VAL GLN ARG ARG VAL GLU PRO LYS VAL
SEQRES  11 B  229  THR VAL TYR PRO SER LYS THR GLN PRO LEU GLN HIS HIS
SEQRES  12 B  229  ASN LEU LEU VAL CYS SER VAL SER GLY PHE TYR PRO GLY
SEQRES  13 B  229  SER ILE GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU
SEQRES  14 B  229  LYS ALA GLY VAL VAL SER THR GLY LEU ILE GLN ASN GLY
SEQRES  15 B  229  ASP TRP THR PHE GLN THR LEU VAL MET LEU GLU THR VAL
SEQRES  16 B  229  PRO ARG SER GLY GLU VAL TYR THR CYS GLN VAL GLU HIS
SEQRES  17 B  229  PRO SER VAL THR SER PRO LEU THR VAL GLU TRP ARG ALA
SEQRES  18 B  229  ARG SER GLU SER ALA GLN SER LYS
HET    GOL  A1181       6
HET    GOL  A1182       6
HET    GOL  A1183       6
HET    GOL  B1190       6
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  GOL    4(C3 H8 O3)
FORMUL   4  HOH   *220(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  SER B   63  1                                  10
HELIX    5   5 GLN B   64  GLU B   87  1                                  24
HELIX    6   6 SER B   88  THR B   90  5                                   3
SHEET    1  AA 8 GLU A  40  TRP A  43  0
SHEET    2  AA 8 ASP A  29  ASP A  35 -1  O  HIS A  33   N  VAL A  42
SHEET    3  AA 8 SER A  19  PHE A  26 -1  O  PHE A  22   N  VAL A  34
SHEET    4  AA 8 HIS A   5  ASN A  15 -1  O  ILE A   8   N  ASP A  25
SHEET    5  AA 8 PHE B   7  PHE B  18 -1  O  PHE B   7   N  ASN A  15
SHEET    6  AA 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18
SHEET    7  AA 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32
SHEET    8  AA 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1  AB 4 GLU A  88  THR A  93  0
SHEET    2  AB 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3  AB 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  PHE A 112
SHEET    4  AB 4 LEU A 138  PRO A 139  1  O  LEU A 138   N  ARG A 146
SHEET    1  AC 4 GLU A  88  THR A  93  0
SHEET    2  AC 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3  AC 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  PHE A 112
SHEET    4  AC 4 SER A 133  GLU A 134 -1  O  SER A 133   N  TYR A 150
SHEET    1  AD 2 LEU A 138  PRO A 139  0
SHEET    2  AD 2 PHE A 145  PHE A 153  1  O  ARG A 146   N  LEU A 138
SHEET    1  AE 4 LYS A 126  PRO A 127  0
SHEET    2  AE 4 ASN A 118  ARG A 123 -1  O  ARG A 123   N  LYS A 126
SHEET    3  AE 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4  AE 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165
SHEET    1  BA 4 LYS B  98  PRO B 103  0
SHEET    2  BA 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3  BA 4 PHE B 155  THR B 163 -1  O  PHE B 155   N  PHE B 122
SHEET    4  BA 4 ILE B 148  GLN B 149  1  O  ILE B 148   N  GLN B 156
SHEET    1  BB 4 LYS B  98  PRO B 103  0
SHEET    2  BB 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3  BB 4 PHE B 155  THR B 163 -1  O  PHE B 155   N  PHE B 122
SHEET    4  BB 4 VAL B 142  SER B 144 -1  O  VAL B 143   N  MET B 160
SHEET    1  BC 2 ILE B 148  GLN B 149  0
SHEET    2  BC 2 PHE B 155  THR B 163  1  O  GLN B 156   N  ILE B 148
SHEET    1  BD 4 GLN B 136  GLU B 137  0
SHEET    2  BD 4 GLU B 128  ARG B 133 -1  O  ARG B 133   N  GLN B 136
SHEET    3  BD 4 TYR B 171  GLU B 176 -1  O  THR B 172   N  PHE B 132
SHEET    4  BD 4 LEU B 184  TRP B 188 -1  O  LEU B 184   N  VAL B 175
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.08
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.08
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.08
CISPEP   1 ASN A   15    PRO A   16          0         4.17
CISPEP   2 THR A  113    PRO A  114          0        -0.28
CISPEP   3 TYR B  123    PRO B  124          0         5.11
SITE     1 AC1  5 ARG A  44  VAL A 104  TYR A 150  HOH A2098
SITE     2 AC1  5 ASP B 152
SITE     1 AC2  5 ASN A  84  TRP A 168  ASP B   2  THR B   3
SITE     2 AC2  5 ARG B   4
SITE     1 AC3  7 LYS A 126  GLU A 141  ASP A 142  HIS A 143
SITE     2 AC3  7 HOH A2117  HOH A2136  GLU B  36
SITE     1 AC4  4 SER B  88  ARG B  94  HOH B2045  HOH B2049
CRYST1   57.644   65.616  131.331  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      0.017348  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015240  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007614        0.00000
      
PROCHECK
Go to PROCHECK summary
 References