BMRB Entry 16108

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16108

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Title:
Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086
Deposition date:
2009-01-05
Original release date:
2009-03-10
Authors:
Mascioni, Alessandro; Jaison, Jacob; Franklin, Moy; Deborah, Dilts; Pamela, Fink; Karl, Malakian; Scott, Sigethy; Yingxia, Wen; Elena, Novikova; Gary, Zlotnick; D sir e, Tsao
Citation:

Citation: Mascioni, Alessandro; Jacob, Jaison; Moy, Franklin; Dilts, Deborah; Fink, Pamela; Malakian, Karl; Sigethy, Scott; Wen, Yingxia; Novikova, Elena; Zlotnick, Gary; Tsao, D sir e. "Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086"  Biomol. NMR Assignments 3, 111-113 (2009).
PubMed: 19636959

Assembly members:

Assembly members:
LP2086, polymer, 261 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: pET9a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LP2086: MGSSGGGGSGGGGVTADIGT GLADALTAPLDHKDKGLKSL TLEDSISQNGTLTLSAQGAE KTYGNGDSLNTGKLKNDKVS RFDFIRQIEVDGQLITLESG EFQVYKQSHSALTALQTEQE QDPEHSEKMVAKRRFRIGDI AGEHTSFDKLPKDVMATYRG TAFGSDDAGGKLTYTIDFAA KQGHGKIEHLKSPELNVDLA VAYIKPDEKHHAVISGSVLY NQDEKGSYSLGIFGEKAQEV AGSAEVETANGIHHIGLAAK Q

Data sets:
Data typeCount
13C chemical shifts365
15N chemical shifts258
1H chemical shifts1483

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LP20861

Entities:

Entity 1, LP2086 261 residues - Formula weight is not available

1   METGLYSERSERGLYGLYGLYGLYSERGLY
2   GLYGLYGLYVALTHRALAASPILEGLYTHR
3   GLYLEUALAASPALALEUTHRALAPROLEU
4   ASPHISLYSASPLYSGLYLEULYSSERLEU
5   THRLEUGLUASPSERILESERGLNASNGLY
6   THRLEUTHRLEUSERALAGLNGLYALAGLU
7   LYSTHRTYRGLYASNGLYASPSERLEUASN
8   THRGLYLYSLEULYSASNASPLYSVALSER
9   ARGPHEASPPHEILEARGGLNILEGLUVAL
10   ASPGLYGLNLEUILETHRLEUGLUSERGLY
11   GLUPHEGLNVALTYRLYSGLNSERHISSER
12   ALALEUTHRALALEUGLNTHRGLUGLNGLU
13   GLNASPPROGLUHISSERGLULYSMETVAL
14   ALALYSARGARGPHEARGILEGLYASPILE
15   ALAGLYGLUHISTHRSERPHEASPLYSLEU
16   PROLYSASPVALMETALATHRTYRARGGLY
17   THRALAPHEGLYSERASPASPALAGLYGLY
18   LYSLEUTHRTYRTHRILEASPPHEALAALA
19   LYSGLNGLYHISGLYLYSILEGLUHISLEU
20   LYSSERPROGLULEUASNVALASPLEUALA
21   VALALATYRILELYSPROASPGLULYSHIS
22   HISALAVALILESERGLYSERVALLEUTYR
23   ASNGLNASPGLULYSGLYSERTYRSERLEU
24   GLYILEPHEGLYGLULYSALAGLNGLUVAL
25   ALAGLYSERALAGLUVALGLUTHRALAASN
26   GLYILEHISHISILEGLYLEUALAALALYS
27   GLN

Samples:

sample_1: LP2086, [U-100% 15N], 0.8 mM; sodium phosphate 30 mM; sodium chloride 90 mM; D2O 5%; sodium azide 0.03%; H2O 95%

sample_2: LP2086, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 30 mM; sodium chloride 90 mM; D2O 5%; sodium azide 0.03%; H2O 95%

sample_conditions_1: pH: 4.7; pressure: 1 atm; temperature: 303 K; temperature controller setting: 307.8 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
GB AAR84481 ACI46772

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