BMRB Entry 50218

Name: UvrD_CTD
Published: 2020-10-12

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PDB ID: 6yi2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50218
MolProbity Validation Chart

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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:

UvrD_CTD

Deposition date:

2020-03-29

Original release date:

2020-10-12

Authors:

Kawale, Ashish; Burmann, Bjorn

Citation:

Citation: Kawale, Ashish; Burmann, Bjorn. "UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain" Commun. Biol. 3, 607-607 (2020).
PubMed: 33154434

Assembly members:

Assembly members:
entity_1, polymer, 76 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: pET28b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RLRATVSRPVSHQRMGTPMV ENDSGYKLGQRVRHAKFGEG TIVNMEGSGEHSRLQVAFQG QGIKWLVAAYARLESV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	315
15N chemical shifts	71
1H chemical shifts	482

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UvrD_CTD	1

Entities:

Entity 1, UvrD_CTD 76 residues - Formula weight is not available

1

ARG

LEU

ARG

ALA

THR

VAL

SER

ARG

PRO

VAL

2

SER

HIS

GLN

ARG

MET

GLY

THR

PRO

MET

VAL

3

GLU

ASN

ASP

SER

GLY

TYR

LYS

LEU

GLY

GLN

4

ARG

VAL

ARG

HIS

ALA

LYS

PHE

GLY

GLU

GLY

5

THR

ILE

VAL

ASN

MET

GLU

GLY

SER

GLY

GLU

6

HIS

SER

ARG

LEU

GLN

VAL

ALA

PHE

GLN

GLY

7

GLN

GLY

ILE

LYS

TRP

LEU

VAL

ALA

TYR

8

ALA

ARG

LEU

GLU

SER

VAL

Samples:

sample_1: UvrD_CTD, [U-100% 13C; U-100% 15N], 650 uM; potassium phosphate buffer 20 mM; KCl 50 mM

sample_conditions_1: ionic strength: 0.070 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
15N-(1H) NOE	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.413 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz
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