BMRB Entry 51428

Name: Variant 5 isolated CTD
Published: 2022-05-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51428

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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:

Variant 5 isolated CTD

Deposition date:

2022-05-06

Original release date:

2022-05-16

Authors:

Porter, Lauren; Starich, Mary

Citation:

Citation: Porter, Lauren; Kim, Allen; Rimal, Swechha; Looger, Loren; Majumdar, Ananya; Mensh, Brett; Starich, Mary; Strub, Marie-Paule. "Many dissimilar NusG protein domains switch between alpha-helix and beta-sheet folds" Nat. Commun. 13, 3802-3802 (2022).
PubMed: 35778397

Assembly members:

Assembly members:
entity_1, polymer, 68 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Calditerrivibrio nitroreducens Taxonomy ID: 477976 Superkingdom: Bacteria Kingdom: not available Genus/species: Calditerrivibrio nitroreducens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pPAL7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVDGFIDTKSEEFKKGDTIL IKDGPFKDFVGIFQEELDSK GRVSILLKTLALQPRITVDK DMIEKLHN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	179
15N chemical shifts	64
1H chemical shifts	64

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Variant 5 CTD	1

Entities:

Entity 1, Variant 5 CTD 68 residues - Formula weight is not available

1

MET

VAL

ASP

GLY

PHE

ILE

ASP

THR

LYS

SER

2

GLU

PHE

LYS

GLY

ASP

THR

ILE

LEU

3

ILE

LYS

ASP

GLY

PRO

PHE

LYS

ASP

PHE

VAL

4

GLY

ILE

PHE

GLN

GLU

LEU

ASP

SER

LYS

5

GLY

ARG

VAL

SER

ILE

LEU

LYS

THR

LEU

6

ALA

LEU

GLN

PRO

ARG

ILE

THR

VAL

ASP

LYS

7

ASP

MET

ILE

GLU

LYS

LEU

HIS

ASN

Samples:

sample_1: Variant 5 CTD, [U-100% 13C; U-100% 15N], 135 uM; HEPES 25 mM; NaCl 50 mM; deuterated glycerol (Sigma Aldrich) 5%; DTT 1 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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