BMRB Entry 18178

Name: Solution structure of AGR2 residues 41-175
Published: 2013-01-07

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PDB ID: 2lns
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18178
MolProbity Validation Chart

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

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Title: Solution structure of AGR2 residues 41-175 PubMed: 23274113

Deposition date: 2012-01-04 Original release date: 2013-01-07

Authors: Patel, Pryank; Clarke, Christopher; Barraclough, Dong; Rudland, Philip; Barraclough, Roger; Lian, Lu-Yun

Citation: Patel, Pryank; Clarke, Christopher; Barraclough, Dong Liu; Jowitt, Thomas Adam; Rudland, Philip Spencer; Barraclough, Roger; Lian, Lu-Yun. "Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion." J. Mol. Biol. 425, 929-943 (2013).

Assembly members:
AGR2, polymer, 140 residues, 15615.084 Da.

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

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

Entity Sequences (FASTA):
AGR2: IDPFTPQTLSRGWGDQLIWT QTYEEALYKSKTSNKPLMII HHLDECPHSQALKKVFAENK EIQKLAEQFVLLNLVYETTD KHLSPDGQYVPRIMFVDPSL TVRADITGRYSNRLYAYEPA DTALLLDNMKKALKLLKTEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	480
15N chemical shifts	135
1H chemical shifts	313

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	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
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
IPAP	sample_3	isotropic	sample_conditions_1
IPAP	sample_4	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

BMRB	18179
PDB	2LNS 2LNT
DBJ	BAD96787 BAG35784
EMBL	CAH92219
GB	AAC77358 AAC82614 AAF22484 AAH15503 AAL54870
REF	NP_001127525 NP_001181233 NP_006399 XP_002751578 XP_002751579
SP	O95994 Q5R7P1
TPG	DAA30743

Biological Magnetic Resonance Data Bank

BMRB Entry 18178

Title: Solution structure of AGR2 residues 41-175 PubMed: 23274113

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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