BMRB Entry 19099

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19099

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Title:
1H, 13C and 15N chemical shifts of human beta-2-microglobulin in solution
Deposition date:
2013-03-18
Original release date:
2014-01-02
Authors:
Schmieder, Peter; Beerbaum, Monika; Ballaschk, Martin
Citation:

Citation: Beerbaum, Monika; Ballaschk, Martin; Erdmann, Natalja; Schnick, Christina; Diehl, Anne; Uchanska-Ziegler, Barbara; Ziegler, Andreas; Schmieder, Peter. "NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules."  J. Biomol. NMR 57, 167-178 (2013).
PubMed: 24006098

Assembly members:

Assembly members:
human_beta-2_microglobulin, 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: pHN1+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_beta-2_microglobulin: MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts76
1H chemical shifts334

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1beta-2 microglobulin monomer1

Entities:

Entity 1, beta-2 microglobulin monomer 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: human beta-2 microglobulin, [U-100% 13C; U-100% 15N], 20.6 mg/mL; sodium phosphate 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 160 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

CCPN v2.2.2 -

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15480 16587 17165 17166 19113 19116 19118 19119 19120 19121 19122 19123 3078 3079
PDB
DBJ BAA35182 BAG38125 BAG64583 BAG72952
EMBL CAA23830 CAG33347 CAH92078
GB AAA51811 AAA87972 AAA88008 AAB25312 AAB35347
REF NP_001009066 NP_001127503 NP_004039 XP_003266898 XP_004056148
SP P16213 P61769 P61770 P61771
AlphaFold P16213 P61769 P61770 P61771

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