BMRB Entry 50172

Title:
Rab1b bound to GTP
Deposition date:
2020-01-28
Original release date:
2020-05-30
Authors:
Kang, Hyun-Seo; Barthelmes, Katja; Sattler, Michael
Citation:

Citation: Barthelmes, Katja; Ramcke, Evelyn; Kang, Hyun-Seo; Sattler, Michael; Itzen, Aymelt. "Conformational Control of Small GTPases by AMPylation"  Proc. Natl. Acad. Sci. U.S.A. 117, 5772-5781 (2020).
PubMed: 32123090

Assembly members:

Assembly members:
entity_1_Rab1b, polymer, 173 residues, Formula weight is not available
entity_GTP, non-polymer, 523.180 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: pMAL

Data sets:
Data typeCount
13C chemical shifts378
15N chemical shifts142
1H chemical shifts156

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rab1b1
2GTP2

Entities:

Entity 1, Rab1b 173 residues - Formula weight is not available

1   METPROGLUTYRASPTYRLEUPHELYSLEU
2   LEULEUILEGLYASPSERGLYVALGLYLYS
3   SERCYSLEULEULEUARGPHEALAASPASP
4   THRTYRTHRGLUSERTYRILESERTHRILE
5   GLYVALASPPHELYSILEARGTHRILEGLU
6   LEUASPGLYLYSTHRILELYSLEUGLNILE
7   TRPASPTHRALAGLYALAGLUARGPHEARG
8   THRILETHRSERSERTYRTYRARGGLYALA
9   HISGLYILEILEVALVALTYRASPVALTHR
10   ASPGLNGLUSERTYRALAASNVALLYSGLN
11   TRPLEUGLNGLUILEASPARGTYRALASER
12   GLUASNVALASNLYSLEULEUVALGLYASN
13   LYSSERASPLEUTHRTHRLYSLYSVALVAL
14   ASPASNTHRTHRALALYSGLUPHEALAASP
15   SERLEUGLYILEPROPHELEUGLUTHRSER
16   ALALYSASNALATHRASNVALGLUGLNALA
17   PHEMETTHRMETALAALAGLUILELYSLYS
18   ARGMETGLY

Entity 2, GTP - C10 H16 N5 O14 P3 - 523.180 Da.

1   GTP

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.3 mM; HEPES 20 mM; DTE 2 mM; sodium chloride 50 mM; MgCl2 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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