BMRB Entry 7429

Name: Backbone 1H and 15N Chemical Shift Assignments for the Phosphotyrosine Binding Domain of Insulin Receptor Substrate 1 in the Apo and Phosphopeptide Bound Forms
Published: 2008-10-03

BMRB Entry DOI: doi:10.13018/BMR7429

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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: Backbone 1H and 15N Chemical Shift Assignments for the Phosphotyrosine Binding Domain of Insulin Receptor Substrate 1 in the Apo and Phosphopeptide Bound Forms PubMed: 19053277

Deposition date: 2008-09-18 Original release date: 2008-10-03

Authors: Stone, Martin; Jarymowycz, Virginia

Citation: Stone, Martin; Jarymowycz, Virginia. "Remote Changes in Dynamics of the Phosphotyrosine-Binding Domain of Insulin Receptor Substrate-1 Induced by Phosphopeptide Binding" Biochemistry 47, 13371-13382 (2008).

Assembly members:
Phosphotyrosine-Binding_Domain_of_Insulin_Receptor_Substrate-1, polymer, 111 residues, Formula weight is not available
Interleukin-4_Receptor_Phosphopeptide, polymer, 111 residues, 261.168 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: chemical synthesis Host organism: Escherichia coli

Entity Sequences (FASTA):
Phosphotyrosine-Binding_Domain_of_Insulin_Receptor_Substrate-1: GPAFKEVWQVILKPKGLGQT KNLIGIYRLCLTSKTISFVK LNSEAAAVVLQLMNIRRCGH SENFFFIEVGRSAVTGPGEF WMQVDDSVVAQNMHETILEA MRAMSDEFRPR
Interleukin-4_Receptor_Phosphopeptide: LVIAGNPAXRS

Data sets:

assigned_chemical_shifts
- PTB_Domain_of_IRS-1_Bound

Data type	Count
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Monomer	1
2	Peptide	2

Entities:

Entity 1, Monomer 111 residues - Formula weight is not available

1

GLY

PRO

ALA

PHE

LYS

GLU

VAL

TRP

GLN

VAL

2

ILE

LEU

LYS

PRO

LYS

GLY

LEU

GLY

GLN

THR

3

LYS

ASN

LEU

ILE

GLY

ILE

TYR

ARG

LEU

CYS

4

LEU

THR

SER

LYS

THR

ILE

SER

PHE

VAL

LYS

5

LEU

ASN

SER

GLU

ALA

VAL

LEU

6

GLN

LEU

MET

ASN

ILE

ARG

CYS

GLY

HIS

7

SER

GLU

ASN

PHE

ILE

GLU

VAL

GLY

8

ARG

SER

ALA

VAL

THR

GLY

PRO

GLY

GLU

PHE

9

TRP

MET

GLN

VAL

ASP

SER

VAL

ALA

10

GLN

ASN

MET

HIS

GLU

THR

ILE

LEU

GLU

ALA

11

MET

ARG

ALA

MET

SER

ASP

GLU

PHE

ARG

PRO

12

ARG

Entity 2, Peptide 111 residues - 261.168 Da.

1

LEU

VAL

ILE

ALA

GLY

ASN

PRO

ALA

PTR

ARG

2

SER

Samples:

PTB_Domain_of_IRS-1_Bound_State: Phosphotyrosine-Binding Domain of Insulin Receptor Substrate-1, [U-15N], 200 uM

PTB_Domain_of_IRS-1_Bound_Sample_Conditions: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	PTB_Domain_of_IRS-1_Bound_State	isotropic	PTB_Domain_of_IRS-1_Bound_Sample_Conditions
3D CBCA(CO)NH	PTB_Domain_of_IRS-1_Bound_State	isotropic	PTB_Domain_of_IRS-1_Bound_Sample_Conditions

Software:

FELIX, Accelrys Software Inc. - processing

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15959
PDB	1IRS 1QQG
DBJ	BAA11026 BAC32308 BAE24991 BAG10207
EMBL	CAA41264 CAA49378
GB	AAA39335 AAB21608 AAB27175 AAH53895 AAI56077
PRF	1712323A
REF	NP_005535 NP_034700 NP_037101 XP_001109882 XP_001134743
SP	P35568 P35569 P35570 Q28224

Biological Magnetic Resonance Data Bank