BMRB Entry 15784

Name: 1H, 13C, and 15N Chemical Shift Assignments for NikA(1-51)
Published: 2008-11-25

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15784

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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 NikA(1-51)

Deposition date:

2008-05-28

Original release date:

2008-11-25

Authors:

Yoshida, Hitoshi; Furuya, Nobuhisa; Lin, Yi-Jan; Guntert, Peter; Komano, Teruya; Kainosho, Masatsune

Citation:

Citation: Yoshida, Hitoshi; Furuya, Nobuhisa; Lin, Yi-Jan; Guntert, Peter; Komano, Teruya; Kainosho, Masatsune. "Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation." J. Mol. Biol. 384, 690-701 (2008).
PubMed: 18929573

Assembly members:

Assembly members:
NikA(1-51), polymer, 51 residues, Formula weight is not available

Natural source:

Natural source: Common Name: R64 plasmid Taxonomy ID: 602 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NikA(1-51): SDSAVRKKSEVRQKTVVRTL RFSPVEDETIRKKAEDSGLT VSAYIRNAALN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	201
15N chemical shifts	51
1H chemical shifts	316

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NikA(1-51)	1

Entities:

Entity 1, NikA(1-51) 51 residues - Formula weight is not available

1

SER

ASP

SER

ALA

VAL

ARG

LYS

SER

GLU

2

VAL

ARG

GLN

LYS

THR

VAL

ARG

THR

LEU

3

ARG

PHE

SER

PRO

VAL

GLU

ASP

GLU

THR

ILE

4

ARG

LYS

ALA

GLU

ASP

SER

GLY

LEU

THR

5

VAL

SER

ALA

TYR

ILE

ARG

ASN

ALA

LEU

6

ASN

Samples:

sample_1: NikA(1-51), [U-13C; U-15N], 2 mM; phosphate buffer 50 mM; sodium chloride 50 mM; sodium azide 0.02% w/v; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
triple resonance	sample_1	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert - structure solution

OPALp, Koradi, Billeter, Guntert - refinement

NMR spectrometers:

Bruker AV 500 MHz
Bruker DRX 600 MHz

PDB	2BA3
DBJ	BAA75139 BAA78022 BAB91643 BAG80276 BAK64475
EMBL	CBL93594 CCE57555 CCQ26867 CDH80849 CDO67566
GB	AAS76382 AAZ05364 ACF56917 ACF65722 ACQ42156
REF	NP_052500 NP_863435 WP_000325007 WP_001283946 WP_001283947