BMRB Entry 30296

Name: Solution NMR structure of the HMG domain of human FACT complex subunit SSRP1
Published: 2018-05-17

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PDB ID: 5vwe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30296
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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:

Solution NMR structure of the HMG domain of human FACT complex subunit SSRP1

Deposition date:

2017-05-21

Original release date:

2018-05-17

Authors:

Hu, Q.; Botuyan, M.; Mer, G.

Citation:

Citation: Hu, Q.; Botuyan, M.; Mer, G.. "Solution NMR structure of the HMG domain of human FACT complex subunit SSRP1" .

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 8050.128 Da.

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: pTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSAYMLWLNASREKIKSD HPGISITDLSKKAGEIWKGM SKEKKEEWDRKAEDARRDYE KAMKEYEGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	269
15N chemical shifts	68
1H chemical shifts	453

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 69 residues - 8050.128 Da.

1

GLY

HIS

MET

SER

ALA

TYR

MET

LEU

TRP

LEU

2

ASN

ALA

SER

ARG

GLU

LYS

ILE

LYS

SER

ASP

3

HIS

PRO

GLY

ILE

SER

ILE

THR

ASP

LEU

SER

4

LYS

ALA

GLY

GLU

ILE

TRP

LYS

GLY

MET

5

SER

LYS

GLU

LYS

GLU

TRP

ASP

ARG

6

LYS

ALA

GLU

ASP

ALA

ARG

ASP

TYR

GLU

7

LYS

ALA

MET

LYS

GLU

TYR

GLU

GLY

Samples:

sample_1: Human SSRP1 HMG Domain, [U-100% 13C; U-100% 15N], 0.6 mM; NaCl 50 mM; Sodium phosphate buffer 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D CCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	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

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker AvanceIII 700 MHz

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