BMRB Entry 11043

Name: Structure of chimeric variant of SH3 domain - SHH
Published: 2009-05-21

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PDB ID: 2rot
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11043
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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:

Structure of chimeric variant of SH3 domain - SHH

Deposition date:

2008-04-10

Original release date:

2009-05-21

Authors:

Kutyshenko, Victor; Prokhorov, Dmitry; Timchenko, Maria; Kudrevatykh, Yuri; Gushchina, Lyubov; Khristoforov, Vladimir; Filimonov, Vladimir

Citation:

Citation: Viguera, A.; Serrano, L.; Wilmanns, M.. "Different folding transition states may result in the same native structure." Nat. Struct. Biol. 3, 874-880 (1996).
PubMed: 8836105

Assembly members:

Assembly members:
alpha-spectrin SHH, polymer, 70 residues, 8125 Da.

Natural source:

Natural source: Common Name: Chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-spectrin SHH: MDETGKELVLALYDYQEKSP REVTMKKGDILTLLNSTNKD WWKVEVKITVNGKTYERQGF VPAAYVKKLD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	328
15N chemical shifts	73
1H chemical shifts	515

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha-spectrin SHH	1

Entities:

Entity 1, alpha-spectrin SHH 70 residues - 8125 Da.

SHH was constructed on the basis of alpa-spectrin wild type SH3-domain, containing 10 extra residues placed between 45th and 48th polypeptides' residues. Insertion of beta sheet includes 48-56 residues (KITVNGKTYE) between 45-48 of SH3-pwt (1SHG)

1	MET	ASP	GLU	THR	GLY	LYS	GLU	LEU	VAL	LEU
2	ALA	LEU	TYR	ASP	TYR	GLN	GLU	LYS	SER	PRO
3	ARG	GLU	VAL	THR	MET	LYS	LYS	GLY	ASP	ILE
4	LEU	THR	LEU	LEU	ASN	SER	THR	ASN	LYS	ASP
5	TRP	TRP	LYS	VAL	GLU	VAL	LYS	ILE	THR	VAL
6	ASN	GLY	LYS	THR	TYR	GLU	ARG	GLN	GLY	PHE
7	VAL	PRO	ALA	ALA	TYR	VAL	LYS	LYS	LEU	ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY-ali	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY-aro	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY-ali	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY-aro	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

BMRB	11026
PDB	2OAW 2RMO 2ROT
REF	XP_012717136

BMRB Entry 11043

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	ASP	GLU	THR	GLY	LYS	GLU	LEU	VAL	LEU
2	ALA	LEU	TYR	ASP	TYR	GLN	GLU	LYS	SER	PRO
3	ARG	GLU	VAL	THR	MET	LYS	LYS	GLY	ASP	ILE
4	LEU	THR	LEU	LEU	ASN	SER	THR	ASN	LYS	ASP
5	TRP	TRP	LYS	VAL	GLU	VAL	LYS	ILE	THR	VAL
6	ASN	GLY	LYS	THR	TYR	GLU	ARG	GLN	GLY	PHE
7	VAL	PRO	ALA	ALA	TYR	VAL	LYS	LYS	LEU	ASP

1	MET	ASP	GLU	THR	GLY	LYS	GLU	LEU	VAL	LEU
2	ALA	LEU	TYR	ASP	TYR	GLN	GLU	LYS	SER	PRO
3	ARG	GLU	VAL	THR	MET	LYS	LYS	GLY	ASP	ILE
4	LEU	THR	LEU	LEU	ASN	SER	THR	ASN	LYS	ASP
5	TRP	TRP	LYS	VAL	GLU	VAL	LYS	ILE	THR	VAL
6	ASN	GLY	LYS	THR	TYR	GLU	ARG	GLN	GLY	PHE
7	VAL	PRO	ALA	ALA	TYR	VAL	LYS	LYS	LEU	ASP

1	MET	ASP	GLU	THR	GLY	LYS	GLU	LEU	VAL	LEU
2	ALA	LEU	TYR	ASP	TYR	GLN	GLU	LYS	SER	PRO
3	ARG	GLU	VAL	THR	MET	LYS	LYS	GLY	ASP	ILE
4	LEU	THR	LEU	LEU	ASN	SER	THR	ASN	LYS	ASP
5	TRP	TRP	LYS	VAL	GLU	VAL	LYS	ILE	THR	VAL
6	ASN	GLY	LYS	THR	TYR	GLU	ARG	GLN	GLY	PHE
7	VAL	PRO	ALA	ALA	TYR	VAL	LYS	LYS	LEU	ASP