BMRB Entry 25935

Name: Membrane-bound mouse CD28 cytoplasmic tail
Published: 2016-12-15

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PDB ID: 2nae
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25935
MolProbity Validation Chart

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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:

Membrane-bound mouse CD28 cytoplasmic tail

Deposition date:

2015-12-23

Original release date:

2016-12-15

Authors:

Li, Hua; Xu, Chenqi; Pan, Weiling

Citation:

Citation: Li, Hua; Xu, Chenqi; Pan, Weiling. "Membrane-bound mouse CD28 cytoplasmic tail" .

Assembly members:

Assembly members:
entity, polymer, 43 residues, 5093.833 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-41a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GTNSRRNRLLQSDYMNMTPR RPGLTRKPYQPYAPARDFAA YRP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	188
15N chemical shifts	48
1H chemical shifts	308

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 43 residues - 5093.833 Da.

1

GLY

THR

ASN

SER

ARG

ASN

ARG

LEU

2

GLN

SER

ASP

TYR

MET

ASN

MET

THR

PRO

ARG

3

ARG

PRO

GLY

LEU

THR

ARG

LYS

PRO

TYR

GLN

4

PRO

TYR

ALA

PRO

ALA

ARG

ASP

PHE

ALA

5

TYR

ARG

PRO

Samples:

sample_1: mCD28CD, [U-13C; U-15N], 0.5 mM; POPG 100 mM; DHPC 125 mM; sodium phosphate 20 mM; D2O, [U-2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY (NOEs to lipid)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (methyl; double 13C-filter)	sample_1	isotropic	sample_conditions_1
2D 1H-13C NOESY (aromatic; double 13C-filter)	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

NMRView v5.2.2, Johnson, One Moon Scientific - data analysis

KUJIRA v0.9843, Naohiro Kobayashi - data analysis

X-PLOR_NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

Bruker Avance 600 MHz

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