BMRB Entry 52348

Name: NMR Backbone Assignment (1H, 15N, and 13C) resonances of RfaH protein
Published: 2024-08-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52348

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR Backbone Assignment (1H, 15N, and 13C) resonances of RfaH protein

Deposition date:

2024-03-12

Original release date:

2024-08-03

Authors:

Cai, Mengli; Agarwal, Nipanshu; Clore, Marius

Citation:

Citation: Cai, Mengli; Agarwal, Nipanshu; Garrett, Daniel; Baber, James; Clore, G Marius. "A Transient, Excited Species of the Autoinhibited a-State of the Bacterial Transcription Factor RfaH May Represent an Early Intermediate on the Fold-Switching Pathway" Biochemistry 63, 2030-2039 (2024).
PubMed: 39088556

Assembly members:

Assembly members:
entity_1, polymer, 162 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: MQSWYLLYCKRGQLQRAQEH LERQAVNCLAPMITLEKIVR GKRTAVSEPLFPNYLFVEFD PEVIHTTTINATRGVSHFVR FGASPAIVPSAVIHQLSVYK PKDIVDPATPYPGDKVIITE GAFEGFQAIFTEPDGEARSM LLLNLINKEIKHSVKNTEFR KL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	456
15N chemical shifts	148
1H chemical shifts	148

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RfaH	1

Entities:

Entity 1, RfaH 162 residues - Formula weight is not available

1

MET

GLN

SER

TRP

TYR

LEU

TYR

CYS

LYS

2

ARG

GLY

GLN

LEU

GLN

ARG

ALA

GLN

GLU

HIS

3

LEU

GLU

ARG

GLN

ALA

VAL

ASN

CYS

LEU

ALA

4

PRO

MET

ILE

THR

LEU

GLU

LYS

ILE

VAL

ARG

5

GLY

LYS

ARG

THR

ALA

VAL

SER

GLU

PRO

LEU

6

PHE

PRO

ASN

TYR

LEU

PHE

VAL

GLU

PHE

ASP

7

PRO

GLU

VAL

ILE

HIS

THR

ILE

ASN

8

ALA

THR

ARG

GLY

VAL

SER

HIS

PHE

VAL

ARG

9

PHE

GLY

ALA

SER

PRO

ALA

ILE

VAL

PRO

SER

10

ALA

VAL

ILE

HIS

GLN

LEU

SER

VAL

TYR

LYS

11

PRO

LYS

ASP

ILE

VAL

ASP

PRO

ALA

THR

PRO

12

TYR

PRO

GLY

ASP

LYS

VAL

ILE

THR

GLU

13

GLY

ALA

PHE

GLU

GLY

PHE

GLN

ALA

ILE

PHE

14

THR

GLU

PRO

ASP

GLY

GLU

ALA

ARG

SER

MET

15

LEU

ASN

LEU

ILE

ASN

LYS

GLU

ILE

16

LYS

HIS

SER

VAL

LYS

ASN

THR

GLU

PHE

ARG

17

LYS

LEU

Samples:

sample_1: RfaH, [U-100% 13C; U-100% 15N; U-80% 2H], 0.35 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 289 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

Xipp - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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