BMRB Entry 15958

Name: NMR Structure of Shq1p N-terminal domain
Published: 2009-06-02

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PDB ID: 2k8q
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
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of Shq1p N-terminal domain

Deposition date:

2008-09-18

Original release date:

2009-06-02

Authors:

Godin, Katherine; Varani, Gabriele

Citation:

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).
PubMed: 19426738

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	379
15N chemical shifts	136
1H chemical shifts	942

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Shq1 N-terminus	1

Entities:

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

1

GLY

ILE

THR

PRO

ARG

PHE

SER

ILE

THR

GLN

2

ASP

GLU

PHE

ILE

PHE

LEU

LYS

ILE

PHE

3

ILE

SER

ASN

ILE

ARG

PHE

SER

ALA

VAL

GLY

4

LEU

GLU

ILE

GLN

GLU

ASN

MET

ILE

5

ILE

PHE

HIS

LEU

SER

PRO

TYR

LEU

ARG

6

LEU

ARG

PHE

PRO

HIS

GLU

LEU

ILE

ASP

7

GLU

ARG

SER

THR

ALA

GLN

TYR

ASP

SER

LYS

8

ASP

GLU

CYS

ILE

ASN

VAL

LYS

VAL

ALA

LYS

9

LEU

ASN

LYS

ASN

GLU

TYR

PHE

GLU

ASP

LEU

10

ASP

LEU

PRO

THR

LYS

LEU

ALA

ARG

GLN

11

GLY

ASP

LEU

ALA

GLY

ALA

ASP

ALA

LEU

THR

12

GLU

ASN

THR

ASP

ALA

LYS

THR

GLN

LYS

13

PRO

LEU

ILE

GLN

GLU

VAL

GLU

THR

ASP

GLY

14

VAL

SER

ASN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_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

PDB	2K8Q 3EUD
DBJ	GAA24017
EMBL	CAA86276 CAY80405
GB	AHY75903 AJP39371 AJR36664 AJR36859 AJR37050
REF	NP_012162
SP	P40486
TPG	DAA08449
AlphaFold	P40486