BMRB Entry 27930

Name: Human Kibra WW domain chemical shift
Published: 2019-10-09

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27930

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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:

Human Kibra WW domain chemical shift

Deposition date:

2019-05-29

Original release date:

2019-10-09

Authors:

Nyarko, Afua

Citation:

Citation: Kwok, Ethiene; Rodriguez, Diego; Kremerskothen, Joachim; Nyarko, Afua. "Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin" J. Biol. Chem. 294, 17383-17394 (2019).
PubMed: 31597702

Assembly members:

Assembly members:
Kibra_WW_domain, polymer, 95 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 24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Kibra_WW_domain: GAHMMPRPELPLPEGWEEAR DFDGKVYYIDHTNRTTSWID PRDRYTKPLTFADCISDELP LGWEEAYDPQVGDYFIDHNT KTTQIEDPRVQWRRE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	116
15N chemical shifts	70
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Kibra WW domain	1

Entities:

Entity 1, Kibra WW domain 95 residues - Formula weight is not available

1

GLY

ALA

HIS

MET

PRO

ARG

PRO

GLU

LEU

2

PRO

LEU

PRO

GLU

GLY

TRP

GLU

ALA

ARG

3

ASP

PHE

ASP

GLY

LYS

VAL

TYR

ILE

ASP

4

HIS

THR

ASN

ARG

THR

SER

TRP

ILE

ASP

5

PRO

ARG

ASP

ARG

TYR

THR

LYS

PRO

LEU

THR

6

PHE

ALA

ASP

CYS

ILE

SER

ASP

GLU

LEU

PRO

7

LEU

GLY

TRP

GLU

ALA

TYR

ASP

PRO

GLN

8

VAL

GLY

ASP

TYR

PHE

ILE

ASP

HIS

ASN

THR

9

LYS

THR

GLN

ILE

GLU

ASP

PRO

ARG

VAL

10

GLN

TRP

ARG

GLU

Samples:

sample_1: Kibra WW domain, [U-13C; U-15N], 180 uM

sample_conditions_1: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis

NMR spectrometers:

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