BMRB Entry 18179

Title:
Solution structure of E60A mutant AGR2
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:

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).
PubMed: 23274113

Assembly members:

Assembly members:
AGR2_E60A, polymer, 140 residues, 14457.855 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: pET-151D

Data sets:
Data typeCount
13C chemical shifts424
15N chemical shifts110
1H chemical shifts651

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1E60A mutant AGR21

Entities:

Entity 1, E60A mutant AGR2 140 residues - 14457.855 Da.

Residues 1-5 (IDPFT) represents a non-native affinity tag.

1   ILEASPPROPHETHRPROGLNTHRLEUSER
2   ARGGLYTRPGLYASPGLNLEUILETRPTHR
3   GLNTHRTYRGLUALAALALEUTYRLYSSER
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 E60A, [U-13C; U-15N], 0.3 mM; H2O 90%; D2O 10%; MES 20 mM; NaCl 100 mM

sample_2: AGR2 E60A, [U-15N], 0.3 mM; Pf1 phage 10 mg; 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_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
IPAPsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1

Software:

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

Analysis, CCPN - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18178
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
AlphaFold Q5R7P1 O95994

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