BMRB Entry 25909

Name: 1H, 13C, and 15N Chemical Shift Assignments for in vitro GB1
Published: 2016-12-21

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PDB ID: 2n9k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25909
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:

1H, 13C, and 15N Chemical Shift Assignments for in vitro GB1

Deposition date:

2015-11-26

Original release date:

2016-12-21

Authors:

Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka

Citation:

Citation: Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka. "Improved in-cell structure determination of proteins at near-physiological concentration" Sci. Rep. 6, 38312-38312 (2016).
PubMed: 27910948

Assembly members:

Assembly members:
entity, polymer, 57 residues, 6258.896 Da.

Natural source:

Natural source: Common Name: firmicutes Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET47b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGTYKLILNGKTLKGETTTE AVDAATAEKVFKQYANDNGV DGEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	251
15N chemical shifts	62
1H chemical shifts	384

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 57 residues - 6258.896 Da.

1

MET

GLY

THR

TYR

LYS

LEU

ILE

LEU

ASN

GLY

2

LYS

THR

LEU

LYS

GLY

GLU

THR

GLU

3

ALA

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

4

PHE

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

5

ASP

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

6

LYS

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: Protein G B1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.31 M; pH: 7.0; pressure: 1 atm; temperature: 295 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 CBCANH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	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 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

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

AZARA v2.8.1, Boucher - processing

TALOS v1, Cornilescu, Delaglio and Bax - chemical shift calculation

OPAL v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol v2.6, Koradi, Billeter and Wuthrich - structure solution

ANSIG v3.3, Kraulis - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - collection

CcpNMR, CCPN - 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