BMRB Entry 17176

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17176
MolProbity Validation Chart

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Title:
Solution NMR structure of the BT_0084 lipoprotein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR376.
Deposition date:
2010-09-10
Original release date:
2010-11-05
Authors:
Ramelot, Theresa; Yang, Yunhuang; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron."  Proteins ., .-. (2011).
PubMed: 22116783

Assembly members:

Assembly members:
BT_0084, polymer, 130 residues, 15166 Da.

Natural source:

Natural source:   Common Name: Bacteroides thetaiotaomicron   Taxonomy ID: 818   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides thetaiotaomicron

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BT_0084: MNDDVDIQQSYPFSIETMPV PKKLKVGETAEIRCQLHRDG RFEETKYFIRYFQPDGAGTL KMSDGTVLLPNDLYPLPGET FRLYYTSASTDQQTVDVYFQ DSFGQLQQLTFSFNNDSSKE EELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts546
15N chemical shifts128
1H chemical shifts836

Time Domain Data

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BT_0084 lipoprotein1

Entities:

Entity 1, BT_0084 lipoprotein 130 residues - 15166 Da.

1   METASNASPASPVALASPILEGLNGLNSER
2   TYRPROPHESERILEGLUTHRMETPROVAL
3   PROLYSLYSLEULYSVALGLYGLUTHRALA
4   GLUILEARGCYSGLNLEUHISARGASPGLY
5   ARGPHEGLUGLUTHRLYSTYRPHEILEARG
6   TYRPHEGLNPROASPGLYALAGLYTHRLEU
7   LYSMETSERASPGLYTHRVALLEULEUPRO
8   ASNASPLEUTYRPROLEUPROGLYGLUTHR
9   PHEARGLEUTYRTYRTHRSERALASERTHR
10   ASPGLNGLNTHRVALASPVALTYRPHEGLN
11   ASPSERPHEGLYGLNLEUGLNGLNLEUTHR
12   PHESERPHEASNASNASPSERSERLYSGLU
13   GLUGLULEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± .05 mM; D2O 100%

NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1.0 ± .05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphNC_sampleisotropicsample_conditions_1
4D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aromNC_sampleisotropicsample_conditions_1
(H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlyNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCNC5_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

UNP Q8ABM6
SWS Q8ABM6_BACTN
PDB
GB AAO75191 EKN16719 EXY66436 KFX73674
REF NP_808997 WP_011107096 WP_028897891 WP_032582694 WP_044245674
AlphaFold Q8ABM6

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