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BMRB Entry 17754

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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/BMR17754
MolProbity Validation Chart

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Title: Solution NMR structure of a MucBP domain (fragment 187-294) of the protein LBA1460 from Lactobacillus acidophilus, Northeast structural genomics consortium target LaR80A

Deposition date: 2011-06-30 Original release date: 2011-08-03

Authors: Feldmann, Erik; Ramelot, Theresa; Yang, Yunhuang; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Feldmann, Erik; Ramelot, Theresa; Yang, Yunhuang; Wang, Huang; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of a MucBP domain (fragment 187-294) of the protein LBA1460 from Lactobacillus acidophilus, Northeast structural genomics consortium target LaR80A"  Not known ., .-..

Assembly members:
MucBP, polymer, 366 residues, 14000 Da.

Natural source:   Common Name: Lactobacillus acidophilus   Taxonomy ID: 1579   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus acidophilus

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

Entity Sequences (FASTA):
MucBP: MIEPIKRTQVVTQTIHYRYE DGAVAHDDHVVSLIFTQSGK RDLTNGKEIWDSKWSLTQTF EALPSPVIIGYTADKPMVGP DEVTVDSKNFLDKQNREETV IYSANTITQNKKDGLEHHHH HHMIEPIKRTQVVTQTIHYR YEDGAVAHDDHVVSLIFTQS GKRDLTNGKEIWDSKWSLTQ TFEALPSPVIIGYTADKPMV GPDEVTVDSKNFLDKQNREE TVIYSANTITQNKKDGLEHH HHHHMIEPIKRTQVVTQTIH YRYEDGAVAHDDHVVSLIFT QSGKRDLTNGKEIWDSKWSL TQTFEALPSPVIIGYTADKP MVGPDEVTVDSKNFLDKQNR EETVIYSANTITQNKKDGLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts127
1H chemical shifts821

Time Domain Data

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1MucBP1

Entities:

Entity 1, MucBP 366 residues - 14000 Da.

1   METILEGLUPROILELYSARGTHRGLNVAL
2   VALTHRGLNTHRILEHISTYRARGTYRGLU
3   ASPGLYALAVALALAHISASPASPHISVAL
4   VALSERLEUILEPHETHRGLNSERGLYLYS
5   ARGASPLEUTHRASNGLYLYSGLUILETRP
6   ASPSERLYSTRPSERLEUTHRGLNTHRPHE
7   GLUALALEUPROSERPROVALILEILEGLY
8   TYRTHRALAASPLYSPROMETVALGLYPRO
9   ASPGLUVALTHRVALASPSERLYSASNPHE
10   LEUASPLYSGLNASNARGGLUGLUTHRVAL
11   ILETYRSERALAASNTHRILETHRGLNASN
12   LYSLYSASPGLYLEUGLUHISHISHISHIS
13   HISHISMETILEGLUPROILELYSARGTHR
14   GLNVALVALTHRGLNTHRILEHISTYRARG
15   TYRGLUASPGLYALAVALALAHISASPASP
16   HISVALVALSERLEUILEPHETHRGLNSER
17   GLYLYSARGASPLEUTHRASNGLYLYSGLU
18   ILETRPASPSERLYSTRPSERLEUTHRGLN
19   THRPHEGLUALALEUPROSERPROVALILE
20   ILEGLYTYRTHRALAASPLYSPROMETVAL
21   GLYPROASPGLUVALTHRVALASPSERLYS
22   ASNPHELEUASPLYSGLNASNARGGLUGLU
23   THRVALILETYRSERALAASNTHRILETHR
24   GLNASNLYSLYSASPGLYLEUGLUHISHIS
25   HISHISHISHISMETILEGLUPROILELYS
26   ARGTHRGLNVALVALTHRGLNTHRILEHIS
27   TYRARGTYRGLUASPGLYALAVALALAHIS
28   ASPASPHISVALVALSERLEUILEPHETHR
29   GLNSERGLYLYSARGASPLEUTHRASNGLY
30   LYSGLUILETRPASPSERLYSTRPSERLEU
31   THRGLNTHRPHEGLUALALEUPROSERPRO
32   VALILEILEGLYTYRTHRALAASPLYSPRO
33   METVALGLYPROASPGLUVALTHRVALASP
34   SERLYSASNPHELEUASPLYSGLNASNARG
35   GLUGLUTHRVALILETYRSERALAASNTHR
36   ILETHRGLNASNLYSLYSASPGLYLEUGLU
37   HISHISHISHISHISHIS

Samples:

NC_sample: MucBP, [U-100% 13C; U-100% 15N], 1.2 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; D2O 10%; H2O 90%

NC5_sample: MucBP, U-100% 15N and 5% 13C biosynthetically directed, 1.2 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; D2O 10%; H2O 90%

NC_sample_in_D2O: MucBP, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NUS NOESY_aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY_aromNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC-aromaticNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC_HisNC5_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, 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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance III 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts