BMRB Entry 27562

Name: GB1 crystalline protein U-13C,15N
Published: 2018-11-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27562

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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:

GB1 crystalline protein U-13C,15N

Deposition date:

2018-07-26

Original release date:

2018-11-15

Authors:

Pawlak, Tomasz

Citation:

Citation: Paluch, Piotr; Pawlak, Tomasz; awniczak, Karol; Trebosc, Julien; Lafon, Olivier; Amoreux, Jean; Potrzebowski, Marek. "Simple and Robust Study of Backbone Dynamics of Crystalline Proteins Employing 1H-15N Dipolar Coupling Dispersion" J. Phys. Chem. B. 122, 8146-8156 (2018).
PubMed: 30070484

Assembly members:

Assembly members:
GB1, polymer, 56 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: na Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GB1: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	149
15N chemical shifts	51
1H chemical shifts	51

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GB1, 1	1
2	GB1, 2	1
3	GB1, 3	1
4	GB1, 4	1

Entities:

Entity 1, GB1, 1 56 residues - Formula weight is not available

1

MET

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

PHE

Samples:

sample_1: GB1, [U-13C; U-15N; U-2H], NH back exchage, mM

sample_conditions_1: pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D hNH	sample_1	solid	sample_conditions_1
2D hNCO	sample_1	solid	sample_conditions_1
2D hNCA	sample_1	solid	sample_conditions_1
3D hCONH	sample_1	solid	sample_conditions_1
3D hCANH	sample_1	solid	sample_conditions_1
3D hCOcaNH	sample_1	solid	sample_conditions_1
3D hcoCAcoNH	sample_1	solid	sample_conditions_1
3D hcaCBcaNH	sample_1	solis	sample_conditions_1
3D hcaCBcacoNH	sample_1	solis	sample_conditions_1

Software:

SPARKY v3, Goddard - chemical shift assignment

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