BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27631

Title: Backbone amide and AILV methyl chemical shift assignments for HLA-A*02:01, a human class I major histocompatibility molecule heavy chain.   PubMed: 31796585

Deposition date: 2018-09-26 Original release date: 2018-11-01

Authors: McShan, Andrew; Sgourakis, Nik

Citation: McShan, Andrew; Devlin, Christine; Overall, Sarah; Park, Jihye; Toor, Jugmohit; Moschidi, Danai; Flores-Solis, David; Choi, Hannah; Tripathi, Sarvind; Procko, Erik; Sgourakis, Nikolaos. "Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection"  Proc. Natl. Acad. Sci. U.S.A. 116, 25602-25613 (2019).

Assembly members:
HLA-A*02:01, polymer, 276 residues, Formula weight is not available
TAX_peptide, polymer, 9 residues, Formula weight is not available
human_beta2m, polymer, 100 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET

Entity Sequences (FASTA):
HLA-A*02:01: GSHSMRYFFTSVSRPGRGEP RFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYW DGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYG CDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAA QTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQ RTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRD GEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCH VQHEGLPKPLTLRWEP
TAX_peptide: LLFGYPVYV
human_beta2m: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
13C chemical shifts796
15N chemical shifts235
1H chemical shifts490

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Heavy chain1
2Peptide2
3Light chain3

Entities:

Entity 1, Heavy chain 276 residues - Formula weight is not available

1   GLYSERHISSERMETARGTYRPHEPHETHR
2   SERVALSERARGPROGLYARGGLYGLUPRO
3   ARGPHEILEALAVALGLYTYRVALASPASP
4   THRGLNPHEVALARGPHEASPSERASPALA
5   ALASERGLNARGMETGLUPROARGALAPRO
6   TRPILEGLUGLNGLUGLYPROGLUTYRTRP
7   ASPGLYGLUTHRARGLYSVALLYSALAHIS
8   SERGLNTHRHISARGVALASPLEUGLYTHR
9   LEUARGGLYTYRTYRASNGLNSERGLUALA
10   GLYSERHISTHRVALGLNARGMETTYRGLY
11   CYSASPVALGLYSERASPTRPARGPHELEU
12   ARGGLYTYRHISGLNTYRALATYRASPGLY
13   LYSASPTYRILEALALEULYSGLUASPLEU
14   ARGSERTRPTHRALAALAASPMETALAALA
15   GLNTHRTHRLYSHISLYSTRPGLUALAALA
16   HISVALALAGLUGLNLEUARGALATYRLEU
17   GLUGLYTHRCYSVALGLUTRPLEUARGARG
18   TYRLEUGLUASNGLYLYSGLUTHRLEUGLN
19   ARGTHRASPALAPROLYSTHRHISMETTHR
20   HISHISALAVALSERASPHISGLUALATHR
21   LEUARGCYSTRPALALEUSERPHETYRPRO
22   ALAGLUILETHRLEUTHRTRPGLNARGASP
23   GLYGLUASPGLNTHRGLNASPTHRGLULEU
24   VALGLUTHRARGPROALAGLYASPGLYTHR
25   PHEGLNLYSTRPALAALAVALVALVALPRO
26   SERGLYGLNGLUGLNARGTYRTHRCYSHIS
27   VALGLNHISGLUGLYLEUPROLYSPROLEU
28   THRLEUARGTRPGLUPRO

Entity 2, Peptide 9 residues - Formula weight is not available

1   LEULEUPHEGLYTYRPROVALTYRVAL

Entity 3, Light chain 100 residues - Formula weight is not available

1   METILEGLNARGTHRPROLYSILEGLNVAL
2   TYRSERARGHISPROALAGLUASNGLYLYS
3   SERASNPHELEUASNCYSTYRVALSERGLY
4   PHEHISPROSERASPILEGLUVALASPLEU
5   LEULYSASNGLYGLUARGILEGLULYSVAL
6   GLUHISSERASPLEUSERPHESERLYSASP
7   TRPSERPHETYRLEULEUTYRTYRTHRGLU
8   PHETHRPROTHRGLULYSASPGLUTYRALA
9   CYSARGVALASNHISVALTHRLEUSERGLN
10   PROLYSILEVALLYSTRPASPARGASPMET

Samples:

sample_1: HLA-A*02:01, [U-100% 13C; U-100% 15N], 500 uM; human beta2m 500 uM; TAX peptide 500 uM

sample_2: HLA-A*02:01, 13C AILV methyl, [U]-15N, 500 uM; TAX peptide 500 uM; human beta2m 500 uM

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts