BMRB Entry 28009

Title:
HRASG12VGMPPNP
Deposition date:
2019-09-05
Original release date:
2021-08-17
Authors:
He, Yanan; Chen, Yingwei; Ruan, Biao; Simmerman, Richard; Chen, Yihong; Wang, Ruixue; Garagusi, Kyle; Godoy-Ruiz, Raquel; King, Harlan; Custer, Gregory; Gallagher, Travis; Rozak, David; Solomon, Melani; Muro, Silvia; Weber, David; Fuerst, Thomas; Toth, Eric A; Bryan, Philp; Orban, John
Citation:

Citation: Chen, Yingwei; Toth, Eric; Ruan, Biao; Choi, Eun Jung; Simmerman, Richard; Chen, Yihong; He, Yanan; Wang, Ruixue; Godoy-Ruiz, Raquel; King, Harlan; Custer, Gregory; Travis Gallagher, D.; Rozak, David; Solomon, Melani; Muro, Silvia; Weber, David; Orban, John; Fuerst, Thomas; Bryan, Philip. "Engineering subtilisin proteases that specifically degrade active RAS"  Commun. Biol. 4, 299-299 (2021).
PubMed: 33674772

Assembly members:

Assembly members:
HRASG12VGMPPNP, polymer, 170 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: pG58

Data sets:
Data typeCount
13C chemical shifts400
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HRASG12VGMPPNP1

Entities:

Entity 1, HRASG12VGMPPNP 170 residues - Formula weight is not available

1   GLYPROHISMETTHRGLUTYRLYSLEUVAL
2   VALVALGLYALAVALGLYVALGLYLYSSER
3   ALALEUTHRILEGLNLEUILEGLNASNHIS
4   PHEVALASPGLUTYRASPPROTHRILEGLU
5   ASPSERTYRARGLYSGLNVALVALILEASP
6   GLYGLUTHRCYSLEULEUASPILELEUASP
7   THRALAGLYGLNGLUGLUTYRSERALAMET
8   ARGASPGLNTYRMETARGTHRGLYGLUGLY
9   PHELEUCYSVALPHEALAILEASNASNTHR
10   LYSSERPHEGLUASPILEHISGLNTYRARG
11   GLUGLNILELYSARGVALLYSASPSERASP
12   ASPVALPROMETVALLEUVALGLYASNLYS
13   CYSASPLEUALAALAARGTHRVALGLUSER
14   ARGGLNALAGLNASPLEUALAARGSERTYR
15   GLYILEPROTYRILEGLUTHRSERALALYS
16   THRARGGLNGLYVALGLUASPALAPHETYR
17   THRLEUVALARGGLUILEARGGLNHISLYS

Samples:

sample_1: HRASG12VGMPPNP, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; NaCl 50 mM; MgCl2 5 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • 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