BMRB Entry 27119

Name: SH2B1 SH2 Domain
Published: 2017-11-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27119

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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:

SH2B1 SH2 Domain

Deposition date:

2017-05-30

Original release date:

2017-11-16

Authors:

McKercher, Marissa; Guan, Xiaoyang; Tan, Zhongping; Wuttke, Deborah

Citation:

Citation: McKercher, Marissa; Guan, Xiaoyang; Tan, Zhongping; Wuttke, Deborah. "Diversity in Peptide Recognition by the SH2 Domain of SH2B1" Proteins 86, 164-176 (2018).
PubMed: 29127727

Assembly members:

Assembly members:
SH2B1_SH2_Domain, polymer, 114 residues, 12811.5 Da.

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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH2B1_SH2_Domain: GSHMDQPLSGYPWFHGMLSR LKAAQLVLTGGTGSHGVFLV RQSETRRGEYVLTFNFQGKA KHLRLSLNEEGQCRVQHLWF QSIFDMLEHFRVHPIPLESG GSSDVVLVSYVPSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	97
15N chemical shifts	97
1H chemical shifts	97

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH2B1 SH2 Domain	1

Entities:

Entity 1, SH2B1 SH2 Domain 114 residues - 12811.5 Da.

First four residues (GSHM) are carried over after thrombin protease cleavage of the 6X-His affinity tag

1

GLY

SER

HIS

MET

ASP

GLN

PRO

LEU

SER

GLY

2

TYR

PRO

TRP

PHE

HIS

GLY

MET

LEU

SER

ARG

3

LEU

LYS

ALA

GLN

LEU

VAL

LEU

THR

GLY

4

GLY

THR

GLY

SER

HIS

GLY

VAL

PHE

LEU

VAL

5

ARG

GLN

SER

GLU

THR

ARG

GLY

GLU

TYR

6

VAL

LEU

THR

PHE

ASN

PHE

GLN

GLY

LYS

ALA

7

LYS

HIS

LEU

ARG

LEU

SER

LEU

ASN

GLU

8

GLY

GLN

CYS

ARG

VAL

GLN

HIS

LEU

TRP

PHE

9

GLN

SER

ILE

PHE

ASP

MET

LEU

GLU

HIS

PHE

10

ARG

VAL

HIS

PRO

ILE

PRO

LEU

GLU

SER

GLY

11

GLY

SER

ASP

VAL

LEU

VAL

SER

TYR

12

VAL

PRO

SER

Samples:

sample_1: SH2B1 SH2 Domain, [U-100% 13C; U-100% 15N], 1 mM; TRIS 50 mM; sodium chloride 50 mM; EDTA 1 mM; DTT 1 mM; TSP 0.15 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Oxford INOVA 600 MHz

UNP	Q9NRF2-1
AlphaFold	Q9Y3Y3