BMRB Entry 30375

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30375
MolProbity Validation Chart

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Title:
Structure of two-domain translational regulator Yih1 reveals a possible mechanism of action
Deposition date:
2017-11-27
Original release date:
2018-11-19
Authors:
Harjes, E.; Jameson, G.; Edwards, P.; Goroncy, A.; Loo, T.; Norris, G.
Citation:

Citation: Harjes, Elena; Jameson, Geoffrey; Tu, Yi-Hsuan; Burr, Natalie; Loo, Trevor; Goroncy, Alexander; Edwards, Patrick; Harjes, Stefan; Munro, Ben; Gobl, Christoph; Sattlegger, Evelyn; Norris, Gillian. "Experimentally based structural model of Yih1 provides insight into its function in controlling the key translational regulator Gcn2"  FEBS Lett. 595, 324-340 (2021).
PubMed: 33156522

Assembly members:

Assembly members:
entity_1, polymer, 258 residues, 29047.422 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDDDHEQLVEELEAVEAIYP DLLSKKQEDGSIIVVKVPQH EYMTLQISFPTHYPSEEAPN VIEVGVCTSLAKRDLYDTKY LQHLFQEVMDSVFHRGSVCL FDFLTELDGVLYVEPEEETE PVQQSDIPTDPFEGWTASDP ITDRGSTFMAFAAHVTSEEQ AFAMLDLLKTDSKMRKANHV MSAWRIKQDGSAATYQDSDD DGETAAGSRMLHLITIMDVW NVIVVVARWFGGAHIGPDRF KHINSTAREAVVRAGFDS

Data sets:
Data typeCount
13C chemical shifts921
15N chemical shifts244
1H chemical shifts1517

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 258 residues - 29047.422 Da.

1   METASPASPASPHISGLUGLNLEUVALGLU
2   GLULEUGLUALAVALGLUALAILETYRPRO
3   ASPLEULEUSERLYSLYSGLNGLUASPGLY
4   SERILEILEVALVALLYSVALPROGLNHIS
5   GLUTYRMETTHRLEUGLNILESERPHEPRO
6   THRHISTYRPROSERGLUGLUALAPROASN
7   VALILEGLUVALGLYVALCYSTHRSERLEU
8   ALALYSARGASPLEUTYRASPTHRLYSTYR
9   LEUGLNHISLEUPHEGLNGLUVALMETASP
10   SERVALPHEHISARGGLYSERVALCYSLEU
11   PHEASPPHELEUTHRGLULEUASPGLYVAL
12   LEUTYRVALGLUPROGLUGLUGLUTHRGLU
13   PROVALGLNGLNSERASPILEPROTHRASP
14   PROPHEGLUGLYTRPTHRALASERASPPRO
15   ILETHRASPARGGLYSERTHRPHEMETALA
16   PHEALAALAHISVALTHRSERGLUGLUGLN
17   ALAPHEALAMETLEUASPLEULEULYSTHR
18   ASPSERLYSMETARGLYSALAASNHISVAL
19   METSERALATRPARGILELYSGLNASPGLY
20   SERALAALATHRTYRGLNASPSERASPASP
21   ASPGLYGLUTHRALAALAGLYSERARGMET
22   LEUHISLEUILETHRILEMETASPVALTRP
23   ASNVALILEVALVALVALALAARGTRPPHE
24   GLYGLYALAHISILEGLYPROASPARGPHE
25   LYSHISILEASNSERTHRALAARGGLUALA
26   VALVALARGALAGLYPHEASPSER

Samples:

sample_1: Yih1 (Yeast Impact Homologue), [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 30 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

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