BMRB Entry 52895

Name: D233
Published: 2025-05-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52895

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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:

D233

Deposition date:

2025-02-11

Original release date:

2025-05-21

Authors:

Varga, Soma; Kaasen, Julie; Peterfia, Balint; Gaspari, Zoltan; Mulder, Frans

Citation:

Citation: Varga, Soma; Kaasen, Julie; Peterfia, Balint; Gaspari, Zoltan; Mulder, Frans. "Resonance assignment of the D233 actin-binding region of Drebrin" .

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMEEHRRKQQTLEAEEAK RRLKEQSIFGDHRDEEEETH MKKSESEVEEAAAIIAQRPD NPREFFKQQERVASASAGSC DVPSPFNHR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	81
1H chemical shifts	81

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	D233	1

Entities:

Entity 1, D233 89 residues - Formula weight is not available

1

GLY

SER

HIS

MET

GLU

HIS

ARG

LYS

2

GLN

THR

LEU

GLU

ALA

GLU

ALA

LYS

3

ARG

LEU

LYS

GLU

GLN

SER

ILE

PHE

GLY

4

ASP

HIS

ARG

ASP

GLU

THR

HIS

5

MET

LYS

SER

GLU

SER

GLU

VAL

GLU

6

ALA

ILE

ALA

GLN

ARG

PRO

ASP

7

ASN

PRO

ARG

GLU

PHE

LYS

GLN

GLU

8

ARG

VAL

ALA

SER

ALA

SER

ALA

GLY

SER

CYS

9

ASP

VAL

PRO

SER

PRO

PHE

ASN

HIS

ARG

Samples:

sample_1: Drebrin D233, [U-100% 13C; U-100% 15N], 300 ± 30 uM; D2O, [U-2H], 10 v/v; DSS 10 mM; sodium chloride 50 mM; sodium phosphate 20 mM; AEBSF protease inhibitor 1 mM; TCEP 5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
(HN)CO(CO)NH	sample_1	isotropic	sample_conditions_1
(H)CC(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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