BMRB Entry 50115

Name: Backbone 13C, and 15N Chemical Shift Assignments for ChiZ N-terminal Domain
Published: 2020-06-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50115

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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:

Backbone 13C, and 15N Chemical Shift Assignments for ChiZ N-terminal Domain

Deposition date:

2019-12-06

Original release date:

2020-06-23

Authors:

Escobar, Cristian; Cross, Timothy

Citation:

Citation: Hicks, Alan; Escobar, Cristian; Cross, Timothy; Zhou, Huan-Xiang. "Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ" Biomolecules 10, 946-946 (2020).

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTBSG1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNAMTPVRPPHTPDPLNLRG PLDGPRWRRAEPAQSRRPGR SRPGGAPLRYHRTGVGMSRT GHGSRPV

Data sets:

H_exch_rates
- H_exch_rates_1
assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	183
15N chemical shifts	52
1H chemical shifts	52
H exchange rates	50
T1 relaxation values	50
T2 relaxation values	50
heteronuclear NOE values	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain	1

Entities:

Entity 1, N-terminal domain 67 residues - Formula weight is not available

ChiZ residues 1 to 64 plus first 3 residues (SNA) left from TEV protease cleavage site. Residues 1-64 correspond to the cytoplasmatic soluble domain of ChiZ membrane protein.

1

SER

ASN

ALA

MET

THR

PRO

VAL

ARG

PRO

2

HIS

THR

PRO

ASP

PRO

LEU

ASN

LEU

ARG

GLY

3

PRO

LEU

ASP

GLY

PRO

ARG

TRP

ARG

ALA

4

GLU

PRO

ALA

GLN

SER

ARG

PRO

GLY

ARG

5

SER

ARG

PRO

GLY

ALA

PRO

LEU

ARG

TYR

6

HIS

ARG

THR

GLY

VAL

GLY

MET

SER

ARG

THR

7

GLY

HIS

GLY

SER

ARG

PRO

VAL

Samples:

sample_1: entity_1, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; DSS 50 uM; D2O 10 % v/v; sodium chloride 25 mM

sample_conditions_1: ionic strength: 45 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
HN(CA)CO	sample_1	isotropic	sample_conditions_1
15N-(1H) NOE	sample_1	isotropic	sample_conditions_1
Het. Nuc. T1 relaxation	sample_1	isotropic	sample_conditions_1
Het. Nuc. T2 relaxation	sample_1	isotropic	sample_conditions_1
CLEANEX-PM (15N-HSQC)	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

CcpNMR v2.4.2, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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