BMRB Entry 27443

Name: 13C and 15N assignment of C&#039;, CA, CB and N of quail Osteopontin at 310K
Published: 2018-11-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27443

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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:

13C and 15N assignment of C', CA, CB and N of quail Osteopontin at 310K

Deposition date:

2018-04-09

Original release date:

2018-11-16

Authors:

Mateos, Borja; Pierattelli, Roberta; Konrat, Robert; Felli, Isabella

Citation:

Citation: Mateos, Borja; Konrat, Robert; Pierattelli, Roberta; Felli, Isabella. "NMR characterization of long-range contacts in intrinsically disordered proteins from paramagnetic relaxation enhancement in 13C direct-detected experiments" Chembiochem. 20, 335-339 (2019).
PubMed: 30407719

Assembly members:

Assembly members:
Osteopontin, polymer, 220 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Osteopontin: MHQDHVDSQSQEHLQQTQND LASLQQTHYSSEENADVPEQ PDFPDVPSKSQETVDDDDDD DNDSNDTDESDEVFTDFPTE APVAPFNRGDNAGRGDSVAY GFRAKAHVVKASKIRKAARK LIEDDATTEDGDSQPAGLWW PKESREQNSRELPQHQSVEN DSRPKFDSREVDGGDSKASA GVDSRESQGSVPAVDASNQT LESAEDAEDRHSIENNEVTR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	678
15N chemical shifts	218

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Osteopontin monomer	1

Entities:

Entity 1, Osteopontin monomer 220 residues - Formula weight is not available

1	MET	HIS	GLN	ASP	HIS	VAL	ASP	SER	GLN	SER
2	GLN	GLU	HIS	LEU	GLN	GLN	THR	GLN	ASN	ASP
3	LEU	ALA	SER	LEU	GLN	GLN	THR	HIS	TYR	SER
4	SER	GLU	GLU	ASN	ALA	ASP	VAL	PRO	GLU	GLN
5	PRO	ASP	PHE	PRO	ASP	VAL	PRO	SER	LYS	SER
6	GLN	GLU	THR	VAL	ASP	ASP	ASP	ASP	ASP	ASP
7	ASP	ASN	ASP	SER	ASN	ASP	THR	ASP	GLU	SER
8	ASP	GLU	VAL	PHE	THR	ASP	PHE	PRO	THR	GLU
9	ALA	PRO	VAL	ALA	PRO	PHE	ASN	ARG	GLY	ASP
10	ASN	ALA	GLY	ARG	GLY	ASP	SER	VAL	ALA	TYR
11	GLY	PHE	ARG	ALA	LYS	ALA	HIS	VAL	VAL	LYS
12	ALA	SER	LYS	ILE	ARG	LYS	ALA	ALA	ARG	LYS
13	LEU	ILE	GLU	ASP	ASP	ALA	THR	THR	GLU	ASP
14	GLY	ASP	SER	GLN	PRO	ALA	GLY	LEU	TRP	TRP
15	PRO	LYS	GLU	SER	ARG	GLU	GLN	ASN	SER	ARG
16	GLU	LEU	PRO	GLN	HIS	GLN	SER	VAL	GLU	ASN
17	ASP	SER	ARG	PRO	LYS	PHE	ASP	SER	ARG	GLU
18	VAL	ASP	GLY	GLY	ASP	SER	LYS	ALA	SER	ALA
19	GLY	VAL	ASP	SER	ARG	GLU	SER	GLN	GLY	SER
20	VAL	PRO	ALA	VAL	ASP	ALA	SER	ASN	GLN	THR
21	LEU	GLU	SER	ALA	GLU	ASP	ALA	GLU	ASP	ARG
22	HIS	SER	ILE	GLU	ASN	ASN	GLU	VAL	THR	ARG

Name	Sample	Sample state	Sample conditions
2D CON	sample_1	isotropic	sample_conditions_1
3D (H)CBCACON	sample_1	isotropic	sample_conditions_1
3D (H)CBCANCO	sample_1	isotropic	sample_conditions_1
3D (H)COCON	sample_1	isotropic	sample_conditions_1
3D (H)CCCON	sample_1	isotropic	sample_conditions_1

BMRB Entry 27443

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	HIS	GLN	ASP	HIS	VAL	ASP	SER	GLN	SER
2	GLN	GLU	HIS	LEU	GLN	GLN	THR	GLN	ASN	ASP
3	LEU	ALA	SER	LEU	GLN	GLN	THR	HIS	TYR	SER
4	SER	GLU	GLU	ASN	ALA	ASP	VAL	PRO	GLU	GLN
5	PRO	ASP	PHE	PRO	ASP	VAL	PRO	SER	LYS	SER
6	GLN	GLU	THR	VAL	ASP	ASP	ASP	ASP	ASP	ASP
7	ASP	ASN	ASP	SER	ASN	ASP	THR	ASP	GLU	SER
8	ASP	GLU	VAL	PHE	THR	ASP	PHE	PRO	THR	GLU
9	ALA	PRO	VAL	ALA	PRO	PHE	ASN	ARG	GLY	ASP
10	ASN	ALA	GLY	ARG	GLY	ASP	SER	VAL	ALA	TYR
11	GLY	PHE	ARG	ALA	LYS	ALA	HIS	VAL	VAL	LYS
12	ALA	SER	LYS	ILE	ARG	LYS	ALA	ALA	ARG	LYS
13	LEU	ILE	GLU	ASP	ASP	ALA	THR	THR	GLU	ASP
14	GLY	ASP	SER	GLN	PRO	ALA	GLY	LEU	TRP	TRP
15	PRO	LYS	GLU	SER	ARG	GLU	GLN	ASN	SER	ARG
16	GLU	LEU	PRO	GLN	HIS	GLN	SER	VAL	GLU	ASN
17	ASP	SER	ARG	PRO	LYS	PHE	ASP	SER	ARG	GLU
18	VAL	ASP	GLY	GLY	ASP	SER	LYS	ALA	SER	ALA
19	GLY	VAL	ASP	SER	ARG	GLU	SER	GLN	GLY	SER
20	VAL	PRO	ALA	VAL	ASP	ALA	SER	ASN	GLN	THR
21	LEU	GLU	SER	ALA	GLU	ASP	ALA	GLU	ASP	ARG
22	HIS	SER	ILE	GLU	ASN	ASN	GLU	VAL	THR	ARG

1	MET	HIS	GLN	ASP	HIS	VAL	ASP	SER	GLN	SER
2	GLN	GLU	HIS	LEU	GLN	GLN	THR	GLN	ASN	ASP
3	LEU	ALA	SER	LEU	GLN	GLN	THR	HIS	TYR	SER
4	SER	GLU	GLU	ASN	ALA	ASP	VAL	PRO	GLU	GLN
5	PRO	ASP	PHE	PRO	ASP	VAL	PRO	SER	LYS	SER
6	GLN	GLU	THR	VAL	ASP	ASP	ASP	ASP	ASP	ASP
7	ASP	ASN	ASP	SER	ASN	ASP	THR	ASP	GLU	SER
8	ASP	GLU	VAL	PHE	THR	ASP	PHE	PRO	THR	GLU
9	ALA	PRO	VAL	ALA	PRO	PHE	ASN	ARG	GLY	ASP
10	ASN	ALA	GLY	ARG	GLY	ASP	SER	VAL	ALA	TYR
11	GLY	PHE	ARG	ALA	LYS	ALA	HIS	VAL	VAL	LYS
12	ALA	SER	LYS	ILE	ARG	LYS	ALA	ALA	ARG	LYS
13	LEU	ILE	GLU	ASP	ASP	ALA	THR	THR	GLU	ASP
14	GLY	ASP	SER	GLN	PRO	ALA	GLY	LEU	TRP	TRP
15	PRO	LYS	GLU	SER	ARG	GLU	GLN	ASN	SER	ARG
16	GLU	LEU	PRO	GLN	HIS	GLN	SER	VAL	GLU	ASN
17	ASP	SER	ARG	PRO	LYS	PHE	ASP	SER	ARG	GLU
18	VAL	ASP	GLY	GLY	ASP	SER	LYS	ALA	SER	ALA
19	GLY	VAL	ASP	SER	ARG	GLU	SER	GLN	GLY	SER
20	VAL	PRO	ALA	VAL	ASP	ALA	SER	ASN	GLN	THR
21	LEU	GLU	SER	ALA	GLU	ASP	ALA	GLU	ASP	ARG
22	HIS	SER	ILE	GLU	ASN	ASN	GLU	VAL	THR	ARG

1	MET	HIS	GLN	ASP	HIS	VAL	ASP	SER	GLN	SER
2	GLN	GLU	HIS	LEU	GLN	GLN	THR	GLN	ASN	ASP
3	LEU	ALA	SER	LEU	GLN	GLN	THR	HIS	TYR	SER
4	SER	GLU	GLU	ASN	ALA	ASP	VAL	PRO	GLU	GLN
5	PRO	ASP	PHE	PRO	ASP	VAL	PRO	SER	LYS	SER
6	GLN	GLU	THR	VAL	ASP	ASP	ASP	ASP	ASP	ASP
7	ASP	ASN	ASP	SER	ASN	ASP	THR	ASP	GLU	SER
8	ASP	GLU	VAL	PHE	THR	ASP	PHE	PRO	THR	GLU
9	ALA	PRO	VAL	ALA	PRO	PHE	ASN	ARG	GLY	ASP
10	ASN	ALA	GLY	ARG	GLY	ASP	SER	VAL	ALA	TYR
11	GLY	PHE	ARG	ALA	LYS	ALA	HIS	VAL	VAL	LYS
12	ALA	SER	LYS	ILE	ARG	LYS	ALA	ALA	ARG	LYS
13	LEU	ILE	GLU	ASP	ASP	ALA	THR	THR	GLU	ASP
14	GLY	ASP	SER	GLN	PRO	ALA	GLY	LEU	TRP	TRP
15	PRO	LYS	GLU	SER	ARG	GLU	GLN	ASN	SER	ARG
16	GLU	LEU	PRO	GLN	HIS	GLN	SER	VAL	GLU	ASN
17	ASP	SER	ARG	PRO	LYS	PHE	ASP	SER	ARG	GLU
18	VAL	ASP	GLY	GLY	ASP	SER	LYS	ALA	SER	ALA
19	GLY	VAL	ASP	SER	ARG	GLU	SER	GLN	GLY	SER
20	VAL	PRO	ALA	VAL	ASP	ALA	SER	ASN	GLN	THR
21	LEU	GLU	SER	ALA	GLU	ASP	ALA	GLU	ASP	ARG
22	HIS	SER	ILE	GLU	ASN	ASN	GLU	VAL	THR	ARG