BMRB Entry 52718

Name: RfaH-CTD major state
Published: 2025-11-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52718

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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:

RfaH-CTD major state

Deposition date:

2024-11-25

Original release date:

2025-11-20

Authors:

Cai, Mengli; Ying, Jinfa; Lopez, Juan; Huang, Ying; Clore, Marius

Citation:

Citation: Cai, Mengli; Ying, Jinfa; Lopez, Juan; Huang, Ying; Clore, Marius. "Unraveling structural transitions and kinetics along the fold-switching pathway of the RfaH C-terminal domain using exchange-based NMR" Proc. Natl. Acad. Sci. U. S. A. 122, e2506441122-e2506441122 (2025).
PubMed: 40366684

Assembly members:

Assembly members:
entity_1, polymer, 62 residues, Formula weight is not available

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 Vector: pet11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PKDIVDPATPYPGDKVIITE GAFEGFQAIFTEPDGEARSM LLLNLINKEIKHSVKNTEFR KL

Data sets:

RDCs
- RDCs_1
assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T1rho_relaxation
- heteronucl_T1rho_relaxation_1

Data type	Count
13C chemical shifts	169
15N chemical shifts	55
1H chemical shifts	106
T1 relaxation values	48
T1rho relaxation values	48
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	Rfah-CTD major state	1

Entities:

Entity 1, Rfah-CTD major state 62 residues - Formula weight is not available

1

PRO

LYS

ASP

ILE

VAL

ASP

PRO

ALA

THR

PRO

2

TYR

PRO

GLY

ASP

LYS

VAL

ILE

THR

GLU

3

GLY

ALA

PHE

GLU

GLY

PHE

GLN

ALA

ILE

PHE

4

THR

GLU

PRO

ASP

GLY

GLU

ALA

ARG

SER

MET

5

LEU

ASN

LEU

ILE

ASN

LYS

GLU

ILE

6

LYS

HIS

SER

VAL

LYS

ASN

THR

GLU

PHE

ARG

7

LYS

LEU

Samples:

sample_1: RfaH-CTD-major, [U-99% 13C; U-99% 15N], 1.0 mM; RfaH-CTD-major, [U-13C; U-15N; U-2H], 1.0 mM; Kpi 25 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T1rho/R1rho relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

PIPP - data analysis

NMR spectrometers:

Bruker AVANCE NEO 500 MHz
Bruker AVANCE NEO 600 MHz
Bruker AVANCE NEO 900 MHz
Bruker AVANCE NEO 700 MHz

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