BMRB Entry 18779

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18779

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Title:
Backbone resonance assignments of FrpD from Neisseria meningitidis
Deposition date:
2012-10-11
Original release date:
2013-01-29
Authors:
Bumba, Ladislav; Sviridova, Ekaterina; Kuta Smatanova, Ivana; Rezacova, Pavlina; Veverka, Vaclav
Citation:

Citation: Bumba, Ladislav; Sviridova, Ekaterina; Kuta Smatanova, Ivana; Rezaova, Pavlina; Veverka, Vaclav. "Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis."  Biomol. NMR Assignments ., .-. (2012).
PubMed: 23225222

Assembly members:

Assembly members:
FrpD, polymer, 237 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Neisseria meningitidis   Taxonomy ID: 487   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria meningitidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FrpD: MAKEQTSFNNPEPMTGFEHT VTFDFQGTKMVIPYGYLARY TQDNATKWLSDTPGQDAYSI NLIEISVYYKKTDQGWVLEP YNQQNKAHFIQFLRDGLDSV DDIVIRKDACSLSTTMGERL LTYGVKKMPSAYPEYEAYED KRHIPENPYFHEFYYIKKGE NPAIITHRNNRINQTEEDSY STSVGSCINGFTVQYYPFIR EKQQLTQQELVGYHQQVEQL VQSFVNNSNKKENLYFQ

Data sets:
Data typeCount
13C chemical shifts687
15N chemical shifts217
1H chemical shifts217

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FrpD_protein1

Entities:

Entity 1, FrpD_protein 237 residues - Formula weight is not available

1   METALALYSGLUGLNTHRSERPHEASNASN
2   PROGLUPROMETTHRGLYPHEGLUHISTHR
3   VALTHRPHEASPPHEGLNGLYTHRLYSMET
4   VALILEPROTYRGLYTYRLEUALAARGTYR
5   THRGLNASPASNALATHRLYSTRPLEUSER
6   ASPTHRPROGLYGLNASPALATYRSERILE
7   ASNLEUILEGLUILESERVALTYRTYRLYS
8   LYSTHRASPGLNGLYTRPVALLEUGLUPRO
9   TYRASNGLNGLNASNLYSALAHISPHEILE
10   GLNPHELEUARGASPGLYLEUASPSERVAL
11   ASPASPILEVALILEARGLYSASPALACYS
12   SERLEUSERTHRTHRMETGLYGLUARGLEU
13   LEUTHRTYRGLYVALLYSLYSMETPROSER
14   ALATYRPROGLUTYRGLUALATYRGLUASP
15   LYSARGHISILEPROGLUASNPROTYRPHE
16   HISGLUPHETYRTYRILELYSLYSGLYGLU
17   ASNPROALAILEILETHRHISARGASNASN
18   ARGILEASNGLNTHRGLUGLUASPSERTYR
19   SERTHRSERVALGLYSERCYSILEASNGLY
20   PHETHRVALGLNTYRTYRPROPHEILEARG
21   GLULYSGLNGLNLEUTHRGLNGLNGLULEU
22   VALGLYTYRHISGLNGLNVALGLUGLNLEU
23   VALGLNSERPHEVALASNASNSERASNLYS
24   LYSGLUASNLEUTYRPHEGLN

Samples:

sample_1: FrpD, [U-100% 13C; U-100% 15N], 0.250 mM; sodium phosphate 6 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

EMBL CAM09823 CAM10568 CBA03514 CBA04365 CBA08292
GB AAA99901 AAF40807 AAF41012 AAF41775 ABX73920
REF NP_273413 NP_273628 NP_274426 WP_002218733 WP_002221985

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