BMRB Entry 52208

Name: Backbone chemical shift assignments for HMG-D Y12F mutant free protein
Published: 2024-08-28

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PDB ID: 8r1x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52208
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:

Backbone chemical shift assignments for HMG-D Y12F mutant free protein

Deposition date:

2023-11-14

Original release date:

2024-08-28

Authors:

Yang, Ji-Chun; Hill, Guy; Neuhaus, David

Citation:

Citation: Hill, Guy; Yang, Ji-Chun; Easton, Laura; Cerdan, Rachel; McLaughlin, Stephen; Stott, Katherine; Travers, Andrew; Neuhaus, David. "A Single Interfacial Point Mutation Rescues Solution Structure Determination of the Complex of HMG-D with a DNA Bulge" Chembiochem ., .-. (2024).
PubMed: 39145407

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET13a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSDKPKRPLSAFMLWLNSAR ESIKRENPGIKVTEVAKRGG ELWRAMKDKSEWEAKAAKAK DDYDRAVKEFEANGGSSAAN GGGAKKRAKPAKKVAKKSKK EESDEDDDDESE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	71
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HMG-D Y12F	1

Entities:

Entity 1, HMG-D Y12F 112 residues - Formula weight is not available

1

MET

SER

ASP

LYS

PRO

LYS

ARG

PRO

LEU

SER

2

ALA

PHE

MET

LEU

TRP

LEU

ASN

SER

ALA

ARG

3

GLU

SER

ILE

LYS

ARG

GLU

ASN

PRO

GLY

ILE

4

LYS

VAL

THR

GLU

VAL

ALA

LYS

ARG

GLY

5

GLU

LEU

TRP

ARG

ALA

MET

LYS

ASP

LYS

SER

6

GLU

TRP

GLU

ALA

LYS

ALA

LYS

ALA

LYS

7

ASP

TYR

ASP

ARG

ALA

VAL

LYS

GLU

PHE

8

GLU

ALA

ASN

GLY

SER

ALA

ASN

9

GLY

ALA

LYS

ARG

ALA

LYS

PRO

10

ALA

LYS

VAL

ALA

LYS

SER

LYS

11

GLU

SER

ASP

GLU

ASP

GLU

12

SER

GLU

Samples:

sample_1: HMG-D Y12F, [U-13C; U-15N], 1.8 mM; sodium phosphate 10 mM; sodium chloride 20 mM; sodium azide 3 mM

sample_conditions_1: ionic strength: 83 mM; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 and 3.5 - processing

SPARKY v3.115 - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 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