BMRB Entry 19523

Name: N-terminal domain of Bilbo1 from Trypanosoma brucei
Published: 2014-01-02

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PDB ID: 2mek
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19523
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:

N-terminal domain of Bilbo1 from Trypanosoma brucei

Deposition date:

2013-09-24

Original release date:

2014-01-02

Authors:

Vidilaseris, Keni; Morriswood, Brooke; Kontaxis, Georg; Dong, Gang

Citation:

Citation: Vidilaseris, Keni; Morriswood, Brooke; Kontaxis, Georg; Dong, Gang. "Structure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch." J. Biol. Chem. 289, 3724-3735 (2014).
PubMed: 24362019

Assembly members:

Assembly members:
Bil_NTD, polymer, 110 residues, 12899.675 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: Protista Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bil_NTD: MAFLVQVAADIFNNKVNFEL SFPSRPSISELTRSAETAFS NEISLRRPDNVPSHKFHSSK IKMYDEELNKWVDLIREDQL TDYCQLYVFQPPNEWHKESQ KEIPPAMKPP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	409
15N chemical shifts	107
1H chemical shifts	595

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain of Bilbo1	1

Entities:

Entity 1, N-terminal domain of Bilbo1 110 residues - 12899.675 Da.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

PDB	2MEK
EMBL	CBH18240
GB	AAY90076 EAN80165
REF	XP_011780504 XP_829277

BMRB Entry 19523

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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