BMRB Entry 25167

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for CS domain of human Shq1
Published: 2015-10-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25167

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for CS domain of human Shq1

Deposition date:

2014-08-20

Original release date:

2015-10-23

Authors:

Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli

Citation:

Citation: Singh, Mahavir; Wang, Zhonghua; Cascio, Duilio; Feigon, Juli. "Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1" J. Mol. Biol. 427, 807-823 (2015).
PubMed: 25553844

Assembly members:

Assembly members:
Human_Shq1_CS_domain, polymer, 133 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: pET46

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human_Shq1_CS_domain: GSTAIGMKETAAAKFERQHM DSPDLGTGGGSGDDDDKMLT PAFDLSQDPDFLTIAIRVPY ARVSEFDVYFEGSDFKFYAK PYFLRLTLPGRIVENGSEQG SYDADKGIFTIRLPKETPGQ HFEGLNMLTALLA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	261
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human Shq1 CS domain	1

Entities:

Entity 1, Human Shq1 CS domain 133 residues - Formula weight is not available

GSTAIGMKETAAAKFERQHMDSPDLGTGGGSGDDDDK (residues -37 to -1) are from the vector after GST tag cleavage

1

GLY

SER

THR

ALA

ILE

GLY

MET

LYS

GLU

THR

2

ALA

LYS

PHE

GLU

ARG

GLN

HIS

MET

3

ASP

SER

PRO

ASP

LEU

GLY

THR

GLY

4

SER

GLY

ASP

LYS

MET

LEU

THR

5

PRO

ALA

PHE

ASP

LEU

SER

GLN

ASP

PRO

ASP

6

PHE

LEU

THR

ILE

ALA

ILE

ARG

VAL

PRO

TYR

7

ALA

ARG

VAL

SER

GLU

PHE

ASP

VAL

TYR

PHE

8

GLU

GLY

SER

ASP

PHE

LYS

PHE

TYR

ALA

LYS

9

PRO

TYR

PHE

LEU

ARG

LEU

THR

LEU

PRO

GLY

10

ARG

ILE

VAL

GLU

ASN

GLY

SER

GLU

GLN

GLY

11

SER

TYR

ASP

ALA

ASP

LYS

GLY

ILE

PHE

THR

12

ILE

ARG

LEU

PRO

LYS

GLU

THR

PRO

GLY

GLN

13

HIS

PHE

GLU

GLY

LEU

ASN

MET

LEU

THR

ALA

14

LEU

ALA

Samples:

sample_1: Human Shq1 CS domain, [U-100% 15N], 0.2 – 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 2 mM; H2O 93%; D2O 7%; sodium azide 0.02%

sample_2: Human Shq1 CS domain, [U-100% 13C; U-100% 15N], 0.2 – 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 2 mM; H2O 93%; D2O 7%; sodium azide 0.02%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN vBruker, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 600 MHz
Bruker Avance 800 MHz

BMRB	19910
PDB	2MNW 4PBD 4PCK
GB	AAH17204 AAH17274 AAH25270 AAH32671 AAH39830
REF	NP_060600 XP_001082636 XP_001141951 XP_001493794 XP_003132372
SP	Q6PI26
AlphaFold	Q6PI26