BMRB Entry 51097

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51097

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Title:
Resonance assignments and Residual Dipolar Couplings for Human Beta-2 microglobulin (b2m)
Deposition date:
2021-09-23
Original release date:
2022-10-12
Authors:
Truong, Hau; Sgourakis, Nikolaos
Citation:

Citation: Jiang, Jiansheng; Taylor, Daniel; Kim, Ellen; Boyd, Lisa; Ahmad, Javeed; Mage, Michael; Truong, Hau; Woodward, Claire; Sgourakis, Nikolaos; Cresswell, Peter; Margulies, David; Natarajan, Kannan. "Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation"  Nat. Commun. 13, 5470-5470 (2022).
PubMed: 36115831

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet22B+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts87
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Beta-2 microglobulin1

Entities:

Entity 1, Beta-2 microglobulin 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: beta-2 microglobulin, [U-13C; U-15N; U-2H], 500 uM; sodium phosphate 20 mM; sodium chloride 150 mM; sodium azide 1.6 mM; EDTA 5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1anisotropicsample_conditions_2

Software:

NMRPipe - processing

SPARKY - chemical shift assignment

TALOS+ - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE III 800 MHz
  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks