BMRB Entry 15450

Name: ThrA3-DKP-insulin
Published: 2008-06-26

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PDB ID: 2jum
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15450
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:

ThrA3-DKP-insulin

Deposition date:

2007-08-31

Original release date:

2008-06-26

Authors:

Huang, Kun; Chan, Shu; Hua, Qing-xin; Chu, Ying-Chi; Wang, Run-ying; Klaproth, Birgit; Jia, Wenhua; Whittaker, Jonathan; De Meyts, Pierre; Nakagawa, Satoe; Steiner, Donald; Katsoyannis, Panayotis; Weiss, Michael

Citation:

Citation: Huang, Kun; Chan, Shu; Hua, Qing-xin; Chu, Ying-Chi; Wang, Run-ying; Klaproth, Birgit; Jia, Wenhua; Whittaker, Jonathan; De Meyts, Pierre; Nakagawa, Satoe; Steiner, Donald; Katsoyannis, Panayotis; Weiss, Michael. "The A-Chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice." J. Biol. Chem. 282, 35337-35349 (2007).
PubMed: 17884811

Assembly members:

Assembly members:
A-chain, polymer, 21 residues, 2385.673 Da.
B-chain, polymer, 30 residues, 3411.928 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A-chain: GITEQCCTSICSLYQLENYC N
B-chain: FVNQHLCGSDLVEALYLVCG ERGFFYTKPT

Data sets:

assigned_chemical_shifts
- A_chain

Data type	Count
1H chemical shifts	310

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	A-chain	1
2	B-chain	2

Entities:

Entity 1, A-chain 21 residues - 2385.673 Da.

1

GLY

ILE

THR

GLU

GLN

CYS

THR

SER

ILE

2

CYS

SER

LEU

TYR

GLN

LEU

GLU

ASN

TYR

CYS

3

ASN

Entity 2, B-chain 30 residues - 3411.928 Da.

1	PHE	VAL	ASN	GLN	HIS	LEU	CYS	GLY	SER	ASP
2	LEU	VAL	GLU	ALA	LEU	TYR	LEU	VAL	CYS	GLY
3	GLU	ARG	GLY	PHE	PHE	TYR	THR	LYS	PRO	THR

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D DQF-COSY	sample_3	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_3
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_3
2D DQF-COSY	sample_3	isotropic	sample_conditions_4
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_4
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_4
2D DQF-COSY	sample_3	isotropic	sample_conditions_5
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_5
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_5

BMRB Entry 15450

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	PHE	VAL	ASN	GLN	HIS	LEU	CYS	GLY	SER	ASP
2	LEU	VAL	GLU	ALA	LEU	TYR	LEU	VAL	CYS	GLY
3	GLU	ARG	GLY	PHE	PHE	TYR	THR	LYS	PRO	THR

PDB	2JUM 2W44 1K3M 1KMF 1LKQ 1VKT 2JMN 2JUM 2JUU 2JUV 2KQP 2L1Z 4IUZ
BMRB	15454 15455 16608 17108 1760 1762 5246

1	PHE	VAL	ASN	GLN	HIS	LEU	CYS	GLY	SER	ASP
2	LEU	VAL	GLU	ALA	LEU	TYR	LEU	VAL	CYS	GLY
3	GLU	ARG	GLY	PHE	PHE	TYR	THR	LYS	PRO	THR

1	PHE	VAL	ASN	GLN	HIS	LEU	CYS	GLY	SER	ASP
2	LEU	VAL	GLU	ALA	LEU	TYR	LEU	VAL	CYS	GLY
3	GLU	ARG	GLY	PHE	PHE	TYR	THR	LYS	PRO	THR