BMRB Entry 11397

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11397

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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:

Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4

Deposition date:

2010-09-09

Original release date:

2011-09-08

Authors:

Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.

Citation:

Citation: Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4" .

Assembly members:

Assembly members:
BACK domain, polymer, 105 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: cell free synthesis Host organism: E. coli - cell free Vector: P060821-14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BACK domain: GSSGSSGVQVGNCLQVMWLA DRHSDPELYTAAKHCAKTHL AQLQNTEEFLHLPHRLLTDI ISDGVPCSQNPTEAIEAWIN FNKEEREAFAESLRTSLKEI GENVH

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	435
15N chemical shifts	107
1H chemical shifts	695

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BACK domain	1

Entities:

Entity 1, BACK domain 105 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

VAL

GLN

VAL

2

GLY

ASN

CYS

LEU

GLN

VAL

MET

TRP

LEU

ALA

3

ASP

ARG

HIS

SER

ASP

PRO

GLU

LEU

TYR

THR

4

ALA

LYS

HIS

CYS

ALA

LYS

THR

HIS

LEU

5

ALA

GLN

LEU

GLN

ASN

THR

GLU

PHE

LEU

6

HIS

LEU

PRO

HIS

ARG

LEU

THR

ASP

ILE

7

ILE

SER

ASP

GLY

VAL

PRO

CYS

SER

GLN

ASN

8

PRO

THR

GLU

ALA

ILE

GLU

ALA

TRP

ILE

ASN

9

PHE

ASN

LYS

GLU

ARG

GLU

ALA

PHE

ALA

10

GLU

SER

LEU

ARG

THR

SER

LEU

LYS

GLU

ILE

11

GLY

GLU

ASN

VAL

HIS

Samples:

sample_1: BACK domain, [U-13C; U-15N], 1.15 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20060702, Delaglio F. - processing

NMRView v5.0.4, Johnson B.A. - data analysis

Kujira v0.9820, Kobayashi N. - data analysis

CYANA v2.1, Guntert P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2EQX
DBJ	BAA91616 BAA91880 BAB03555 BAB27317 BAB29305
EMBL	CAD28521 CAG33551 CAH90011 CAH93240
GB	AAH02736 AAH25103 ADZ15413 AIC51824 EAW67898
REF	NP_001101216 NP_001126905 NP_001247465 NP_001267133 NP_001298045
SP	Q5R4S6 Q8R179 Q9N010 Q9NVX7
AlphaFold	Q5R4S6 Q8R179 Q9N010 Q9NVX7