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Biological Magnetic Resonance Data Bank


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BMRB Entry 18178

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PDB ID:
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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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:
Data typeCount
13C chemical shifts480
15N chemical shifts135
1H chemical shifts313

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 140 residues - 15615.084 Da.

Residues 1-5 represents a non-native affinity tag

1   ILEASPPROPHETHRPROGLNTHRLEUSER
2   ARGGLYTRPGLYASPGLNLEUILETRPTHR
3   GLNTHRTYRGLUGLUALALEUTYRLYSSER
4   LYSTHRSERASNLYSPROLEUMETILEILE
5   HISHISLEUASPGLUCYSPROHISSERGLN
6   ALALEULYSLYSVALPHEALAGLUASNLYS
7   GLUILEGLNLYSLEUALAGLUGLNPHEVAL
8   LEULEUASNLEUVALTYRGLUTHRTHRASP
9   LYSHISLEUSERPROASPGLYGLNTYRVAL
10   PROARGILEMETPHEVALASPPROSERLEU
11   THRVALARGALAASPILETHRGLYARGTYR
12   SERASNARGLEUTYRALATYRGLUPROALA
13   ASPTHRALALEULEULEUASPASNMETLYS
14   LYSALALEULYSLEULEULYSTHRGLULEU

Samples:

sample_1: AGR2, [U-13C; U-15N; U-2H], 1 mM; H2O 90%; D2O 10%; MES 20 mM; NaCl 100 mM

sample_2: AGR2, [U-13C; U-15N; U-2H], 1 mM; H2O 90%; D2O 10%; MES 20 mM; NaCl 100 mM

sample_3: AGR2, [U-15N], 1 mM; Pf1 phage 10 mg; H2O 90%; D2O 10%; MES 20 mM; NaCl 100 mM

sample_4: AGR2, [U-15N], 1 mM; PEG:Hexanol 5%; H2O 90%; D2O 10%; MES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
IPAPsample_3isotropicsample_conditions_1
IPAPsample_4isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

Analysis, CCPN - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18179
PDB
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

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts