BMRB Entry 50219

Name: Mfd_RID
Published: 2020-10-12

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PDB ID: 6yhz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50219
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:

Mfd_RID

Deposition date:

2020-03-30

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: RNLAELHIGQPVVHLEHGVG RYAGMTTLEAGGITGEYLML TYANDAKLYVPVSSLHLISR YAGGAEENAPLHKLGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	303
15N chemical shifts	63
1H chemical shifts	488

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RID	1

Entities:

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

1

ARG

ASN

LEU

ALA

GLU

LEU

HIS

ILE

GLY

GLN

2

PRO

VAL

HIS

LEU

GLU

HIS

GLY

VAL

GLY

3

ARG

TYR

ALA

GLY

MET

THR

LEU

GLU

ALA

4

GLY

ILE

THR

GLY

GLU

TYR

LEU

MET

LEU

5

THR

TYR

ALA

ASN

ASP

ALA

LYS

LEU

TYR

VAL

6

PRO

VAL

SER

LEU

HIS

LEU

ILE

SER

ARG

7

TYR

ALA

GLY

ALA

GLU

ASN

ALA

PRO

8

LEU

HIS

LYS

LEU

GLY

Samples:

sample_1: RID, [U-100% 13C; U-100% 15N], 600 uM; 1x PBS buffer 152 mM

sample_conditions_1: ionic strength: 152 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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