BMRB Entry 27326

Name: Yes1 SH2 domain in complex with Cdc37-derived phosphopeptide
Published: 2018-01-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27326

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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:

Yes1 SH2 domain in complex with Cdc37-derived phosphopeptide

Deposition date:

2017-12-03

Original release date:

2018-01-16

Authors:

Bachman, Ashleigh; Keramisanou, Dimitra; Kumar M. V., Vasantha; Gelis, Ioannis

Citation:

Citation: Bachman, Ashleigh; Keramisanou, Dimitra; Xu, Wanping; Beebe, Kristin; Moses, Michael; Vasantha Kumar, M; Gray, Geoffrey; Noor, Radwan Ebna; van der Vaart, Arjan; Neckers, Len; Gelis, Ioannis. "Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation" Nat. Commun. 9, 265-265 (2018).
PubMed: 29343704

Assembly members:

Assembly members:
Yes1-SH2, polymer, 111 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: pGEX6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Yes1-SH2: SIQAEEWYFGKMGRKDAERL LLNPGNQRGIFLVRESETTK GAYSLSIRDWDEIRGDNVKH YKIRKLDNGGYYITTRAQFD TLQKLVKHYTEHADGLCHKL TTVCPTVKPQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	204
15N chemical shifts	107
1H chemical shifts	107

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH2 domain	1

Entities:

Entity 1, SH2 domain 111 residues - Formula weight is not available

1

SER

ILE

GLN

ALA

GLU

TRP

TYR

PHE

GLY

2

LYS

MET

GLY

ARG

LYS

ASP

ALA

GLU

ARG

LEU

3

LEU

ASN

PRO

GLY

ASN

GLN

ARG

GLY

ILE

4

PHE

LEU

VAL

ARG

GLU

SER

GLU

THR

LYS

5

GLY

ALA

TYR

SER

LEU

SER

ILE

ARG

ASP

TRP

6

ASP

GLU

ILE

ARG

GLY

ASP

ASN

VAL

LYS

HIS

7

TYR

LYS

ILE

ARG

LYS

LEU

ASP

ASN

GLY

8

TYR

ILE

THR

ARG

ALA

GLN

PHE

ASP

9

THR

LEU

GLN

LYS

LEU

VAL

LYS

HIS

TYR

THR

10

GLU

HIS

ALA

ASP

GLY

LEU

CYS

HIS

LYS

LEU

11

THR

VAL

CYS

PRO

THR

VAL

LYS

PRO

GLN

12

GLY

Samples:

sample_1: Yes1-SH2, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Agilent direct drive 800 MHz

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