BMRB Entry 31004

Name: Structure of the N-terminal domain of ViaA
Published: 2023-03-20

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PDB ID: 7ugc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31004
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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:

Structure of the N-terminal domain of ViaA

Deposition date:

2022-03-24

Original release date:

2023-03-20

Authors:

Lemak, A.; Reichheld, S.; Bhandari, V.; Houliston, S.; Arrowsmith, C.; Sharpe, S.; Houry, W.

Citation:

Citation: Lemak, A.; Reichheld, S.; Bhandari, V.; Houliston, S.; Arrowsmith, C.; Sharpe, S.; Houry, W.. "Structure of the N-terminal domain of ViaA" .

Assembly members:

Assembly members:
entity_1, polymer, 191 residues, 21777.018 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLTLDTLNVMLAVSEEGLIE EMIIALLASPQLAVFFEKFP RLKAAITDDVPRWREALRSR LKDARVPPELTEEVMCYQQS QLLSTPQFIVQLPQILDLLH RLNSPWAEQARQLVDANSTI TSALHTLFLQRWRLSLIVQA TTLNQQLLEEEREQLLSEVQ ERMTLSGQLEPILADNNTAA GRLWDMSAGQL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	733
15N chemical shifts	158
1H chemical shifts	1171

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 191 residues - 21777.018 Da.

1

MET

LEU

THR

LEU

ASP

THR

LEU

ASN

VAL

MET

2

LEU

ALA

VAL

SER

GLU

GLY

LEU

ILE

GLU

3

GLU

MET

ILE

ALA

LEU

ALA

SER

PRO

4

GLN

LEU

ALA

VAL

PHE

GLU

LYS

PHE

PRO

5

ARG

LEU

LYS

ALA

ILE

THR

ASP

VAL

6

PRO

ARG

TRP

ARG

GLU

ALA

LEU

ARG

SER

ARG

7

LEU

LYS

ASP

ALA

ARG

VAL

PRO

GLU

LEU

8

THR

GLU

VAL

MET

CYS

TYR

GLN

SER

9

GLN

LEU

SER

THR

PRO

GLN

PHE

ILE

VAL

10

GLN

LEU

PRO

GLN

ILE

LEU

ASP

LEU

HIS

11

ARG

LEU

ASN

SER

PRO

TRP

ALA

GLU

GLN

ALA

12

ARG

GLN

LEU

VAL

ASP

ALA

ASN

SER

THR

ILE

13

THR

SER

ALA

LEU

HIS

THR

LEU

PHE

LEU

GLN

14

ARG

TRP

ARG

LEU

SER

LEU

ILE

VAL

GLN

ALA

15

THR

LEU

ASN

GLN

LEU

GLU

16

GLU

ARG

GLU

GLN

LEU

SER

GLU

VAL

GLN

17

GLU

ARG

MET

THR

LEU

SER

GLY

GLN

LEU

GLU

18

PRO

ILE

LEU

ALA

ASP

ASN

THR

ALA

19

GLY

ARG

LEU

TRP

ASP

MET

SER

ALA

GLY

GLN

20

LEU

Samples:

sample_1: ViaA-NTD, [U-100% 13C; U-100% 15N], 500 uM; HEPES 50 mM; NaCl 100 mM; beta-mercaptoethanol 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

FMCGUI, Lemak and Arrowsmith - chemical shift assignment

NMRFAM-SPARKY, Lee, W., Tonelli, M., and Markley, J.L. - peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE II 800 MHz

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