BMRB Entry 51342

Name: SH2 domain from mouse SH2B1
Published: 2023-05-19

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PDB ID: 8atk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51342
MolProbity Validation Chart

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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:

SH2 domain from mouse SH2B1

Deposition date:

2022-03-01

Original release date:

2023-05-19

Authors:

Fowler, Nicholas; Albalwi, Marym; Lee, Subin; Hounslow, Andrea; Williamson, Mike

Citation:

Citation: Fowler, Nicholas; Albalwi, Marym; Lee, Subin; Hounslow, Andrea; Williamson, Mike. "Improved methodology for protein NMR structure calculation using hydrogen bond restraints and ANSURR validation: The SH2 domain of SH2B1" Structure 31, 975-986 (2023).
PubMed: 37311460

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 13664 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKIHHHHHHDQPLSGYPWFH GMLSRLKAAQLVLEGGTGSH GVFLVRQSETRRGEYVLTFN FQGKAKHLRLSLNEEGQCRV QHLWFQSIFDMLEHFRVHPI PLESGGSSDVVLVSYVPSQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	541
15N chemical shifts	140
1H chemical shifts	843

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 119 residues - 13664 Da.

This sequence corresponds to residues 519-628 from mouse SH2B1 (Uniprot Q91ZM2) with the addition of a 9-residue His tag at the N terminus. Thus the first included residue of the mouse sequence (D519) is Asp-10.

1

MET

LYS

ILE

HIS

ASP

2

GLN

PRO

LEU

SER

GLY

TYR

PRO

TRP

PHE

HIS

3

GLY

MET

LEU

SER

ARG

LEU

LYS

ALA

GLN

4

LEU

VAL

LEU

GLU

GLY

THR

GLY

SER

HIS

5

GLY

VAL

PHE

LEU

VAL

ARG

GLN

SER

GLU

THR

6

ARG

GLY

GLU

TYR

VAL

LEU

THR

PHE

ASN

7

PHE

GLN

GLY

LYS

ALA

LYS

HIS

LEU

ARG

LEU

8

SER

LEU

ASN

GLU

GLY

GLN

CYS

ARG

VAL

9

GLN

HIS

LEU

TRP

PHE

GLN

SER

ILE

PHE

ASP

10

MET

LEU

GLU

HIS

PHE

ARG

VAL

HIS

PRO

ILE

11

PRO

LEU

GLU

SER

GLY

SER

ASP

VAL

12

VAL

LEU

VAL

SER

TYR

VAL

PRO

SER

GLN

Samples:

sample_1: SH2, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; potassium phosphate 100 ± 1 mM; DSS 1 ± 0.05 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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
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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.05 - collection

Felix - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

UNP	Q91ZM2
AlphaFold	Q9WVM5