BMRB Entry 27837

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for RepA
Published: 2019-12-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27837

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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 1H, 13C, and 15N Chemical Shift Assignments for RepA

Deposition date:

2019-03-15

Original release date:

2019-12-17

Authors:

Pantoja-Uceda, David; Oroz, Javier; Laurents, Douglas

Citation:

Citation: Pantoja-Uceda, David; Oroz, Javier; Fernandez, Cristina; de Alba, Eva; Giraldo, Rafael; Laurents, Douglas. "Conformational Priming of RepA-WH1 for Functional Amyloid Conversion Detected by NMR Spectroscopy" Structure 28, 336-347 (2020).
PubMed: 31918960

Assembly members:

Assembly members:
RepA, polymer, 132 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: pRG-H6-WH1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RepA: MVENQVTQSNKLIESSHTLT LNEKRLVLCAASLIDSRKPL PKDGYLTIRADTFAEVFGID VKHAYAALDDAATKLFNRDI RRYVKGKVVERMRWVFHVKY REGQGCVELGFSPTIIPHLT MLHKEFTSYQLK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	390
15N chemical shifts	126
1H chemical shifts	126

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RepA chain 1	1
2	RepA chain 2	1

Entities:

Entity 1, RepA chain 1 132 residues - Formula weight is not available

1

MET

VAL

GLU

ASN

GLN

VAL

THR

GLN

SER

ASN

2

LYS

LEU

ILE

GLU

SER

HIS

THR

LEU

THR

3

LEU

ASN

GLU

LYS

ARG

LEU

VAL

LEU

CYS

ALA

4

ALA

SER

LEU

ILE

ASP

SER

ARG

LYS

PRO

LEU

5

PRO

LYS

ASP

GLY

TYR

LEU

THR

ILE

ARG

ALA

6

ASP

THR

PHE

ALA

GLU

VAL

PHE

GLY

ILE

ASP

7

VAL

LYS

HIS

ALA

TYR

ALA

LEU

ASP

8

ALA

THR

LYS

LEU

PHE

ASN

ARG

ASP

ILE

9

ARG

TYR

VAL

LYS

GLY

LYS

VAL

GLU

10

ARG

MET

ARG

TRP

VAL

PHE

HIS

VAL

LYS

TYR

11

ARG

GLU

GLY

GLN

GLY

CYS

VAL

GLU

LEU

GLY

12

PHE

SER

PRO

THR

ILE

PRO

HIS

LEU

THR

13

MET

LEU

HIS

LYS

GLU

PHE

THR

SER

TYR

GLN

14

LEU

LYS

Samples:

sample_1: RepA, [U-99% 13C; U-99% 15N], 1.0 mM; deuterated acetic acid 1.0 mM; mQ 85%; D2O 15%; DSS 50 uM

sample_conditions_1: ionic strength: 0.001 M; pH: 4.0; pressure: 1 atm; temperature: 323.15 K

Experiments:

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

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0, Johnson, One Moon Scientific - data analysis, peak picking

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