BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17370

Title: Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155.

Authors: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155."  Not known ., .-..

Assembly members:
protein_BVU, polymer, 248 residues, 14645.2 Da.

Natural source:   Common Name: Bacteroides Vulgatus   Taxonomy ID: 821   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides Vulgatus

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

Entity Sequences (FASTA):
protein_BVU: MNELDIQQEYPFTVESMPVA DEIAGDETVEIRLEIKPSGN FIGTVYTLRYFQPDGKGSLK MEDGTVLKPNDRYLLNEWKF RLYYTSQSDKEAQTIDLYFE DNWGNLQQLTYDFNGKLEHH HHHHMNELDIQQEYPFTVES MPVADEIAGDETVEIRLEIK PSGNFIGTVYTLRYFQPDGK GSLKMEDGTVLKPNDRYLLN EWKFRLYYTSQSDKEAQTID LYFEDNWGNLQQLTYDFNGK LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts132
1H chemical shifts858

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1protein BVU 1572(27-141)1

Entities:

Entity 1, protein BVU 1572(27-141) 248 residues - 14645.2 Da.

1   METASNGLULEUASPILEGLNGLNGLUTYR
2   PROPHETHRVALGLUSERMETPROVALALA
3   ASPGLUILEALAGLYASPGLUTHRVALGLU
4   ILEARGLEUGLUILELYSPROSERGLYASN
5   PHEILEGLYTHRVALTYRTHRLEUARGTYR
6   PHEGLNPROASPGLYLYSGLYSERLEULYS
7   METGLUASPGLYTHRVALLEULYSPROASN
8   ASPARGTYRLEULEUASNGLUTRPLYSPHE
9   ARGLEUTYRTYRTHRSERGLNSERASPLYS
10   GLUALAGLNTHRILEASPLEUTYRPHEGLU
11   ASPASNTRPGLYASNLEUGLNGLNLEUTHR
12   TYRASPPHEASNGLYLYSLEUGLUHISHIS
13   HISHISHISHISMETASNGLULEUASPILE
14   GLNGLNGLUTYRPROPHETHRVALGLUSER
15   METPROVALALAASPGLUILEALAGLYASP
16   GLUTHRVALGLUILEARGLEUGLUILELYS
17   PROSERGLYASNPHEILEGLYTHRVALTYR
18   THRLEUARGTYRPHEGLNPROASPGLYLYS
19   GLYSERLEULYSMETGLUASPGLYTHRVAL
20   LEULYSPROASNASPARGTYRLEULEUASN
21   GLUTRPLYSPHEARGLEUTYRTYRTHRSER
22   GLNSERASPLYSGLUALAGLNTHRILEASP
23   LEUTYRPHEGLUASPASNTRPGLYASNLEU
24   GLNGLNLEUTHRTYRASPPHEASNGLYLYS
25   LEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: conjugate transposon protein BVU_1572(27-141), [U-100% 13C; U-100% 15N], 0.53 ± 0.05 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 mM; DTT 10 ± 0.5 mM; D2O 10%; H2O 90%

NC5_sample: conjugate transposon protein BVU_1572(27-141), [U-5% 13C; U-100% 15N], 0.48 ± 0.05 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 mM; D2O 10%; H2O 90%

NC_sample_in_D2O: conjugate transposon protein BVU_1572(27-141), [U-100% 13C; U-100% 15N], 0.53 ± 0.05 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 NOESYNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY-aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC-NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C HSQC-aromaticNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sample_in_D2Oisotropicsample_conditions_1
3D HCCH-COSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNHANC5_sampleisotropicsample_conditions_1
2D 1H-15N HSQC 150ppmNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlyNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromatic no CTNC_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

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, chemical shift assignment

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
  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

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