BMRB Entry 18637

Name: 1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus
Published: 2013-02-12

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PDB ID: 4uet
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18637
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus

Deposition date:

2012-08-03

Original release date:

2013-02-12

Authors:

Rey Burusco, M Florencia; Ibanez Shimabukuro, Marina; Cooper, Alan; Kennedy, Malcolm; Corsico, Betina; Smith, Brian

Citation:

Citation: Rey-Burusco, M. Florencia; Ibanez-Shimabukuro, Marina; Cooper, Alan; Kennedy, Malcolm; Corsico, Betina; Smith, Brian. "H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus." Biomol. NMR Assignments 8, 19-21 (2014).
PubMed: 23179061

Assembly members:

Assembly members:
rNa-FAR-1, polymer, 170 residues, 18779.5025 Da.

Natural source:

Natural source: Common Name: nematodes Taxonomy ID: 51031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Necator americanus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rNa-FAR-1: MGSSHHHHHHSSGHMFKYED IPADYRDLMPPEARDFLQNL SDGDKTVLKEVFKAGPYKNT EESIAALKKKSPELGAKVEK LHAMVKSKIAALGPEAKGFA EKSIEIARGIKARYYTGNEP TKDDLKASVKEVLKLYKAMS DAGKADFGKQFPFLAKVFES GKAAKFAGEN

Data sets:

Data type	Count
13C chemical shifts	862
15N chemical shifts	282
1H chemical shifts	1244

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	rNa-FAR-1	1

Entities:

Entity 1, rNa-FAR-1 170 residues - 18779.5025 Da.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	Na-FAR-1	isotropic	apoNaFAR-1
C HSQC3 (h[C]_H.through-space)	Na-FAR-1	isotropic	apoNaFAR-1
CBCACONH3 (H[N[co[{CA\|ca[C]}]]])	Na-FAR-1	isotropic	apoNaFAR-1
HNCACO3 (H[N[ca[CO]]])	Na-FAR-1	isotropic	apoNaFAR-1
HcccoNH3 (HccoNH)	Na-FAR-1	isotropic	apoNaFAR-1
3D C(CO)NH	Na-FAR-1	isotropic	apoNaFAR-1
3D HNCACB	Na-FAR-1	isotropic	apoNaFAR-1
3D HNCO	Na-FAR-1	isotropic	apoNaFAR-1
3D HCCH-TOCSY	Na-FAR-1	isotropic	apoNaFAR-1
hCCH TOCSY3 (hC_CH.relayed)	Na-FAR-1	isotropic	apoNaFAR-1
3D HCCH-COSY	Na-FAR-1	isotropic	apoNaFAR-1
3D 1H-15N NOESY	Na-FAR-1	isotropic	apoNaFAR-1
3D 1H-13C NOESY	Na-FAR-1	isotropic	apoNaFAR-1
CBHE (hbCBcgcdceHE)	Na-FAR-1	isotropic	apoNaFAR-1
CBHD (hbCBcgcdHD)	Na-FAR-1	isotropic	apoNaFAR-1

NEMBASE4	NAC00128
PDB	4UET 4XCP
GB	ETN71481
REF	XP_013293708

BMRB Entry 18637

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

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

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