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BMRB Entry 15958

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15958
MolProbity Validation Chart

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Title: NMR Structure of Shq1p N-terminal domain   PubMed: 19426738

Deposition date: 2008-09-18 Original release date: 2009-06-02

Authors: Godin, Katherine; Varani, Gabriele

Citation: Godin, Katherine; Walbott, Helene; Leulliot, Nicolas; van Tilbeurgh, Herman; Varani, Gabriele. "The Box H/ACA snoRNP Assembly Factor Shq1p is a Chaperone Protein Homologous to Hsp90 Cochaperones that Binds to the Cbf5p Enzyme."  J. Mol. Biol. 390, 231-244 (2009).

Assembly members:
Shq1_N-terminus, polymer, 134 residues, 15383.490 Da.

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
Shq1_N-terminus: GITPRFSITQDEEFIFLKIF ISNIRFSAVGLEIIIQENMI IFHLSPYYLRLRFPHELIDD ERSTAQYDSKDECINVKVAK LNKNEYFEDLDLPTKLLARQ GDLAGADALTENTDAKKTQK PLIQEVETDGVSNN

Data typeCount
13C chemical shifts379
15N chemical shifts136
1H chemical shifts942

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Shq1 N-terminus1

Entities:

Entity 1, Shq1 N-terminus 134 residues - 15383.490 Da.

1   GLYILETHRPROARGPHESERILETHRGLN
2   ASPGLUGLUPHEILEPHELEULYSILEPHE
3   ILESERASNILEARGPHESERALAVALGLY
4   LEUGLUILEILEILEGLNGLUASNMETILE
5   ILEPHEHISLEUSERPROTYRTYRLEUARG
6   LEUARGPHEPROHISGLULEUILEASPASP
7   GLUARGSERTHRALAGLNTYRASPSERLYS
8   ASPGLUCYSILEASNVALLYSVALALALYS
9   LEUASNLYSASNGLUTYRPHEGLUASPLEU
10   ASPLEUPROTHRLYSLEULEUALAARGGLN
11   GLYASPLEUALAGLYALAASPALALEUTHR
12   GLUASNTHRASPALALYSLYSTHRGLNLYS
13   PROLEUILEGLNGLUVALGLUTHRASPGLY
14   VALSERASNASN

Samples:

sample_1: Shq1 N-terminus, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%; KCl 50 mM; KPOx pH 7.0 50 mM; DTT 4 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7.0; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2

Software:

SPARKY v3.110, Goddard - peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Bruker DMX 750 MHz

Related Database Links:

PDB
DBJ GAA24017
EMBL CAA86276 CAY80405
GB AHY75903 AJP39371 AJR36664 AJR36859 AJR37050
REF NP_012162
SP P40486
TPG DAA08449

Download simulated HSQC data in one of the following formats:
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