BMRB Entry 27946

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for RA-bound Cellular Retinoic Acid Binding Protein 2
Published: 2019-11-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27946

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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 RA-bound Cellular Retinoic Acid Binding Protein 2

Deposition date:

2019-06-17

Original release date:

2019-11-08

Authors:

Lixa, Carolina; Iqbal, Anwar; Almeida, Fabio; Pinheiro, Anderson

Citation:

Citation: Lixa, Carolina; Clarkson, Michael; Iqbal, Anwar; Moon, Thomas; Almeida, Fabio; Peti, Wolfgang; Pinheiro, Anderson. "Retinoic Acid Binding Leads to CRABP2 Rigidification and Dimerization" Biochemistry 58, 4183-4194 (2019).
PubMed: 31566355

Assembly members:

Assembly members:
CRABP2, polymer, 140 residues, Formula weight is not available
RETINOIC ACID, non-polymer, 300.435 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CRABP2: GHMPNFSGNWKIIRSENFEE LLKVLGVNVMLRKIAVAAAS KPAVEIKQEGDTFYIKTSTT VRTTEINFKVGEEFEEQTVD GRPCKSLVKWESENKMVCEQ KLLKGEGPKTSWTRELTNDG ELILTMTADDVVCTRVYVRE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	126
1H chemical shifts	126

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CRABP2 monomer	1
2	RETINOIC ACID	2

Entities:

Entity 1, CRABP2 monomer 140 residues - Formula weight is not available

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

Entity 2, RETINOIC ACID - C20 H28 O2 - 300.435 Da.

1

REA

Samples:

sample_1: RA-bound CRABP2, [U-13C; U-15N], 1 mM; NaP 20 mM; NaCl 150 mM; DTT 5 mM; retinoic acid 1 mM

sample_conditions_1: ionic strength: 0.170 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

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

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

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