BMRB Entry 17743

Name: Backbone 1H, 13C and 15N chemical shift assignments for the N-terminal domain of insulin-like growth factor binding protein-2 (IGFBP-2)
Published: 2011-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17743

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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:

Backbone 1H, 13C and 15N chemical shift assignments for the N-terminal domain of insulin-like growth factor binding protein-2 (IGFBP-2)

Deposition date:

2011-06-28

Original release date:

2011-07-14

Authors:

Galea, Charles; Mobli, Mehdi; McNeil, Kerrie; Mulhern, Terrence; Wallace, John; King, Glenn; Forbes, Briony; Norton, Raymond

Citation:

Citation: Galea, Charles; Mobli, Mehdi; McNeil, Kerrie; Mulhern, Terrence; Wallace, John; King, Glenn; Forbes, Briony; Norton, Raymond. "Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain." Biochimie 94, 608-616 (2012).
PubMed: 21951978

Assembly members:

Assembly members:
IGFBP-2_N-domain, polymer, 100 residues, 10222.9 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32(a)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IGFBP-2_N-domain: GPEVLFRCPPCTPERLAACG PPPVAPPAAVAAVAGGARMP CAELVREPGCGCCSVCARLE GEACGVYTPRCGQGLRCYPH PGSELPLQALVMGEGTCEKR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	234
15N chemical shifts	80
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-BP-2, chain 1	1
2	N-BP-2, chain 2	1

Entities:

Entity 1, N-BP-2, chain 1 100 residues - 10222.9 Da.

Residues -1 and -2 are part of the 3C protease cleavage site and remain after removal of the thioredoxin fusion tag.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

DBJ	BAD92746
EMBL	CAA34373
GB	AAA03246 AAA36048 AAB22308 AAH04312 AAH09902
REF	NP_000588 XP_001087071 XP_003254105 XP_003780748 XP_003907977
SP	P18065
AlphaFold	P18065

BMRB Entry 17743

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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