BMRB Entry 18181

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18181
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure of GspC-HR of typeII secretion system
Deposition date:
2012-01-05
Original release date:
2012-03-09
Authors:
Gu, Shuang; Kelly, Geoff; Pickersgill, Richard
Citation:

Citation: Gu, Shuang; Kelly, Geoff; Wang, Xiaohui; Frenkiel, Tom; Shevchik, Vladimir; Pickersgill, Richard. "Solution structure of homology region (HR) domain of type II secretion system."  J. Biol. Chem. 287, 9072-9080 (2012).
PubMed: 22253442

Assembly members:

Assembly members:
entity, polymer, 104 residues, 11138.382 Da.

Natural source:

Natural source:   Common Name: Dickeya dadantii   Taxonomy ID: 204038   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Dickeya dadantii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMLEMAGALDASQMSNLP PSTLNLSLTGVMAGDDDSRS IAIISKDNEQFSRGVNEEVP GYNAKIVSIRPDRVVLQYQG RYEVLGLYSQEDSGSDGVPG AQVR

Data sets:
Data typeCount
13C chemical shifts260
15N chemical shifts72
1H chemical shifts436

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GspC-HR of typeII secretion system1

Entities:

Entity 1, GspC-HR of typeII secretion system 104 residues - 11138.382 Da.

1   GLYSERHISMETLEUGLUMETALAGLYALA
2   LEUASPALASERGLNMETSERASNLEUPRO
3   PROSERTHRLEUASNLEUSERLEUTHRGLY
4   VALMETALAGLYASPASPASPSERARGSER
5   ILEALAILEILESERLYSASPASNGLUGLN
6   PHESERARGGLYVALASNGLUGLUVALPRO
7   GLYTYRASNALALYSILEVALSERILEARG
8   PROASPARGVALVALLEUGLNTYRGLNGLY
9   ARGTYRGLUVALLEUGLYLEUTYRSERGLN
10   GLUASPSERGLYSERASPGLYVALPROGLY
11   ALAGLNVALARG

Samples:

sample_1: OutC-HRF3, [U-100% 13C; U-100% 15N], 0.5 mM; Tis 20 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1

Software:

TALOS, Cornilescu, Delaglio and Bax - data analysis

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAA46369
GB ADM99377
REF WP_013318811 WP_038923436
SP Q01564
AlphaFold Q01564

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