BMRB Entry 17611

Title:
Solution NMR structure of protein Rmet_5065 from Ralstonia metallidurans. Northeast Structural Genomics Consortium Target CrR115.
Deposition date:
2011-04-29
Original release date:
2011-06-01
Authors:
Ramelot, Theresa; Yang, Yunhuang; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rajesh, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Title: Solution NMR structure of protein Rmet_5065 from Ralstonia metallidurans. Northeast Structural Genomics Consortium Target CrR115."  .

Assembly members:

Assembly members:
Rmet_5065, polymer, 142 residues, 16136.968 Da.

Natural source:

Natural source:   Common Name: Ralstonia metallidurans   Taxonomy ID: 119219   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Ralstonia metallidurans

Experimental source:

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

Data typeCount
13C chemical shifts624
15N chemical shifts159
1H chemical shifts958

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein Rmet_50651

Entities:

Entity 1, protein Rmet_5065 142 residues - 16136.968 Da.

1   METASNILETHRVALGLUTHRTHRVALALA
2   ALAPROVALGLYLYSVALTRPARGALATYR
3   THRTHRPROGLUASPILELYSGLNTRPASN
4   ALAALASERASPASPTRPHISTHRTHRALA
5   ALATHRVALASPLEUARGGLUGLYGLYALA
6   PHESERSERARGMETGLUALALYSASPGLY
7   SERMETGLYPHEASPPHEALAGLYTHRTYR
8   THRLYSVALVALGLUASNLYSARGILEGLU
9   TYRALAPHEGLYASPARGTHRALALYSVAL
10   GLUPHELEUGLUALAPROGLNGLYVALTHR
11   VALARGVALSERPHEVALALAGLUTHRGLU
12   TYRPROVALGLUGLNGLNGLNGLNGLYTRP
13   GLNALAILELEUASNASNPHELYSARGHIS
14   VALGLUSERHISLEUGLUHISHISHISHIS
15   HISHIS

Samples:

NC_sample: protein, [U-100% 13C; U-100% 15N], 1.3 ± 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; H2O 90%; D2O 10%

NC5_sample: protein, U-100% 15N and 5% 13C biosynthetically directed, 1.1 ± 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 %; H2O 90%; D2O 10%

NC_sample_in_D2O: protein, [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; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 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 hetNOENC5_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

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - 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
  • Bruker Avance III 850 MHz

Related Database Links:

PDB
GB ABF11927 EKZ95695
REF WP_008651999 WP_011519477 WP_017515048 WP_029306526 WP_035883904

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