BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27632

Title: Backbone amide and AILV methyl chemical shift assignments for HLA-A*01:01, 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*01:01, polymer, 280 residues, Formula weight is not available
NRAS_Q61K_peptide, polymer, 10 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

Entity Sequences (FASTA):
HLA-A*01:01: GSHSMRYFFTSVSRPGRGEP RFIAVGYVDDTQFVRFDSDA ASQKMEPRAPWIEQEGPEYW DQETRNMKAHSQTDRANLGT LRGYYNQSEDGSHTIQIMYG CDVGPDGRFLRGYRQDAYDG KDYIALNEDLRSWTAADMAA QITKRKWEAVHAAEQRRVYL EGRCVNGLRRYLENGKETLQ RTDPPKTHMTHHHISDHEAT LRCWALGFYPAEITLTWQRD GEDQTQDTELVETRPAGDGT FQKWAAVVVPSGEEQRYTCH VQHEGLPKPLTLRWELSSQP
NRAS_Q61K_peptide: ILDTAGKEEY
human_beta2m: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
13C chemical shifts786
15N chemical shifts247
1H chemical shifts557

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 280 residues - Formula weight is not available

1   GLYSERHISSERMETARGTYRPHEPHETHR
2   SERVALSERARGPROGLYARGGLYGLUPRO
3   ARGPHEILEALAVALGLYTYRVALASPASP
4   THRGLNPHEVALARGPHEASPSERASPALA
5   ALASERGLNLYSMETGLUPROARGALAPRO
6   TRPILEGLUGLNGLUGLYPROGLUTYRTRP
7   ASPGLNGLUTHRARGASNMETLYSALAHIS
8   SERGLNTHRASPARGALAASNLEUGLYTHR
9   LEUARGGLYTYRTYRASNGLNSERGLUASP
10   GLYSERHISTHRILEGLNILEMETTYRGLY
11   CYSASPVALGLYPROASPGLYARGPHELEU
12   ARGGLYTYRARGGLNASPALATYRASPGLY
13   LYSASPTYRILEALALEUASNGLUASPLEU
14   ARGSERTRPTHRALAALAASPMETALAALA
15   GLNILETHRLYSARGLYSTRPGLUALAVAL
16   HISALAALAGLUGLNARGARGVALTYRLEU
17   GLUGLYARGCYSVALASNGLYLEUARGARG
18   TYRLEUGLUASNGLYLYSGLUTHRLEUGLN
19   ARGTHRASPPROPROLYSTHRHISMETTHR
20   HISHISHISILESERASPHISGLUALATHR
21   LEUARGCYSTRPALALEUGLYPHETYRPRO
22   ALAGLUILETHRLEUTHRTRPGLNARGASP
23   GLYGLUASPGLNTHRGLNASPTHRGLULEU
24   VALGLUTHRARGPROALAGLYASPGLYTHR
25   PHEGLNLYSTRPALAALAVALVALVALPRO
26   SERGLYGLUGLUGLNARGTYRTHRCYSHIS
27   VALGLNHISGLUGLYLEUPROLYSPROLEU
28   THRLEUARGTRPGLULEUSERSERGLNPRO

Entity 2, Peptide 10 residues - Formula weight is not available

1   ILELEUASPTHRALAGLYLYSGLUGLUTYR

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*01:01, [U-100% 13C; U-100% 15N], 500 uM; NRAS Q61K peptide 500 uM; human beta2m 500 uM

sample_2: HLA-A*01:01, 13C AILV methyl [U-15N], 500 uM; NRAS Q61K 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

NMRPipe, 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