BMRB Entry 51046

Title:
AILV assignments of hpMR1 bound to bovien beta 2 microglobulin and Ac-6-FP
Deposition date:
2021-07-29
Original release date:
2021-08-30
Authors:
McShan, Andrew; Sgourakis, Nik
Citation:

Citation: McShan, Andrew; Devlin, Christine; Papadaki, Georgia; Sun, Yi; Green, Adam; Morozov, Giora; Burslem, George; Procko, Erik; Sgourakis, Nikolaos. "TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules"  Nat. Chem. Biol. 18, 859-868 (2022).
PubMed: 35725941

Assembly members:

Assembly members:
entity_1, polymer, 271 residues, Formula weight is not available
entity_2, polymer, 99 residues, Formula weight is not available
entity_30W, non-polymer, 233.184 Da.

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: pET28a

Data sets:
Data typeCount
13C chemical shifts87
1H chemical shifts291

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hpMR11
2bB2m2
3Ac6FP3

Entities:

Entity 1, hpMR1 271 residues - Formula weight is not available

1   METARGTHRHISSERLEUARGTYRPHEARG
2   LEUGLYVALSERASPPROILEHISGLYVAL
3   PROGLUPHEILESERVALGLYTYRVALASP
4   SERHISPROILETHRTHRTYRASPSERVAL
5   THRARGGLNLYSGLUPROARGALAPROTRP
6   METALAGLUASNLEUALAPROASPHISTRP
7   GLUARGTYRTHRGLNLEULEUARGGLYTRP
8   GLNGLNMETPHELYSVALGLULEULYSARG
9   LEUGLNARGHISTYRASNHISSERGLYSER
10   HISTHRTYRGLNARGMETILEGLYCYSGLU
11   LEULEUGLUASPGLYSERTHRTHRGLYPHE
12   LEUGLNTYRALATYRASPGLYGLNASPPHE
13   LEUILEPHEASNLYSASPTHRLEUSERTRP
14   LEUALAVALASPASNVALALAHISTHRILE
15   LYSGLNALATRPGLUALAASNGLNHISGLU
16   LEULEUTYRGLNLYSASNTRPLEUGLUGLU
17   GLUCYSILEALATRPLEULYSARGPHELEU
18   GLUTYRGLYLYSASPTHRLEUGLNARGTHR
19   GLUPROPROLYSVALARGVALASNHISLYS
20   GLUTHRPHEPROGLYILETHRTHRLEUTYR
21   CYSARGALATYRGLYPHETYRPROPROGLU
22   ILESERILEASNTRPMETLYSASNGLYGLU
23   GLUILEPHEGLNASPTHRASPTYRGLYGLY
24   ILELEUPROSERGLYASPGLYTHRTYRGLN
25   THRTRPVALSERVALGLULEUASPPROGLN
26   ASNGLYASPILETYRSERCYSHISVALGLU
27   HISGLYGLYVALHISMETVALLEUGLNGLY
28   PHE

Entity 2, bB2m 99 residues - Formula weight is not available

1   METILEGLNARGPROPROLYSILEGLNVAL
2   TYRSERARGHISPROPROGLUASPGLYLYS
3   PROASNTYRLEUASNCYSTYRVALTYRGLY
4   PHEHISPROPROGLNILEGLUILEASPLEU
5   LEULYSASNGLYGLULYSILELYSSERGLU
6   GLNSERASPLEUSERPHESERLYSASPTRP
7   SERPHETYRLEULEUSERHISALAGLUPHE
8   THRPROASNSERLYSASPGLNTYRSERCYS
9   ARGVALLYSHISVALTHRLEUGLUGLNPRO
10   ARGILEVALLYSTRPASPARGASPLEU

Entity 3, Ac6FP - C9 H7 N5 O3 - 233.184 Da.

1   30W

Samples:

sample_1: hpMR1, [U-12C; U-15N; U-2H; Ala CB, Ile CD1, Leu CD1/CD2, Val CG1/CG2], 250 uM; bB2m 250 uM; Acetyl-6-formylpterin 250 uM; NaCl 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

TOPSPIN - collection

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz