BMRB Entry 16750

Name: backbone chemical shifts assignments of acid-denatured c-src SH3 with increasing urea concentration
Published: 2010-05-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16750

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

backbone chemical shifts assignments of acid-denatured c-src SH3 with increasing urea concentration

Deposition date:

2010-03-03

Original release date:

2010-05-03

Authors:

Poulsen, Flemming; Roesner, Heike

Citation:

Citation: Rosner, Heike; Poulsen, Flemming. "Residue-specific description of non-native transient structures in the ensemble of acid-denatured structures of the all-beta protein c-src SH3." Biochemistry 49, 3246-3253 (2010).
PubMed: 20218679

Assembly members:

Assembly members:
c-src_SH3, polymer, 80 residues, Formula weight is not available

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: pET_csrcSH3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-src_SH3: MGSSHHHHHHSSGLVPRGSH MVTTFVALYDYESRTETDLS FKKGERLQIVNNTEGDWWLA HSLTTGQTGYIPSNYVAPSN

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	762
15N chemical shifts	372
1H chemical shifts	372

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c-src_SH3	1

Entities:

Entity 1, c-src_SH3 80 residues - Formula weight is not available

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

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 HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
3D HNCO	sample_4	isotropic	sample_conditions_1
3D HNCA	sample_4	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_1
3D HNCO	sample_5	isotropic	sample_conditions_1
3D HNCA	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_6	isotropic	sample_conditions_1
3D HNCO	sample_6	isotropic	sample_conditions_1
3D HNCA	sample_6	isotropic	sample_conditions_1

BMRB	3433
PDB	1PRL 1PRM 1RLP 1RLQ 1SRL 1SRM 2PTK 3FJ5
EMBL	CAA23696 CAA36156
GB	AAA42565 AAA42583 AAA49078 AAC37877 AAD24180
REF	NP_990788 XP_001372060 XP_002191434 XP_003212004 XP_005057157
SP	P00523 P00524 P00525 P14084 P14085
AlphaFold	P00523 P00524 P00525 P14084 P14085

BMRB Entry 16750

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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