BMRB Entry 34235

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34235
MolProbity Validation Chart

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Title:
Solution NMR structure of Pseudomonas aeruginosa TonB CTD
Deposition date:
2018-01-19
Original release date:
2018-08-03
Authors:
Oeemig, J.; Samuli Ollila, O.; Heikkinen, H.; Iwai, H.
Citation:

Citation: Oeemig, Jesper; Ollila, O; Iwai, Hideo. "The NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa"  PeerJ 6, e5412-e5412 (2018).
PubMed: 30186676

Assembly members:

Assembly members:
entity_1, polymer, 99 residues, 11503.448 Da.

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pFGRSF15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SHMGSLNDSDIKPLRMDPPV YPRMAQARGIEGRVKVLFTI TSDGRIDDIQVLESVPSRMF DREVRQAMAKWRFEPRVSGG KIVARQATKMFFFKIEKRR

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts102
1H chemical shifts721

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 99 residues - 11503.448 Da.

1   SERHISMETGLYSERLEUASNASPSERASP
2   ILELYSPROLEUARGMETASPPROPROVAL
3   TYRPROARGMETALAGLNALAARGGLYILE
4   GLUGLYARGVALLYSVALLEUPHETHRILE
5   THRSERASPGLYARGILEASPASPILEGLN
6   VALLEUGLUSERVALPROSERARGMETPHE
7   ASPARGGLUVALARGGLNALAMETALALYS
8   TRPARGPHEGLUPROARGVALSERGLYGLY
9   LYSILEVALALAARGGLNALATHRLYSMET
10   PHEPHEPHELYSILEGLULYSARGARG

Samples:

sample_1: PaTonB96, [U-99% 13C; U-99% 15N], 1 mM; NaPO4 buffer 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC ctsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
(HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR v2.4.1, CCPN - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 800 MHz

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