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 18180

Title: Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11.

Authors: Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation: Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11."  To be published ., .-..

Assembly members:
HmR11, polymer, 185 residues, 21399.959 Da.

Natural source:   Common Name: Haloarcula marismortui   Taxonomy ID: 2238   Superkingdom: Archaea   Kingdom: not available   Genus/species: Haloarcula marismortui

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

Entity Sequences (FASTA):
HmR11: MDEDTEDWETQLQANRDEKD RFFSEHRQSPIPPEERDDFD GLSYFDPDPDYRVEATVTVH ETPESVDLETSDDRTVRYLH VATLSFDLDGESRDLHAFRQ AADESRTLFVPFRDKTTGQQ SYDGGRYMELEPDRDLSDGD EITLDFNLAYSPFCAYSDTF SCPLPPESNWLETAVTAGER TDLEH

Data sets:
Data typeCount
13C chemical shifts803
15N chemical shifts197
1H chemical shifts1209

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HmR111

Entities:

Entity 1, HmR11 185 residues - 21399.959 Da.

1   METASPGLUASPTHRGLUASPTRPGLUTHR
2   GLNLEUGLNALAASNARGASPGLULYSASP
3   ARGPHEPHESERGLUHISARGGLNSERPRO
4   ILEPROPROGLUGLUARGASPASPPHEASP
5   GLYLEUSERTYRPHEASPPROASPPROASP
6   TYRARGVALGLUALATHRVALTHRVALHIS
7   GLUTHRPROGLUSERVALASPLEUGLUTHR
8   SERASPASPARGTHRVALARGTYRLEUHIS
9   VALALATHRLEUSERPHEASPLEUASPGLY
10   GLUSERARGASPLEUHISALAPHEARGGLN
11   ALAALAASPGLUSERARGTHRLEUPHEVAL
12   PROPHEARGASPLYSTHRTHRGLYGLNGLN
13   SERTYRASPGLYGLYARGTYRMETGLULEU
14   GLUPROASPARGASPLEUSERASPGLYASP
15   GLUILETHRLEUASPPHEASNLEUALATYR
16   SERPROPHECYSALATYRSERASPTHRPHE
17   SERCYSPROLEUPROPROGLUSERASNTRP
18   LEUGLUTHRALAVALTHRALAGLYGLUARG
19   THRASPLEUGLUHIS

Samples:

sample_1: HmR11-1, [U-100% 13C; U-100% 15N], 0.7 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM

sample_2: HmR11-1, [U-5% 13C; U-100% 15N], 1.2 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM

sample_3: HmR11, [U-5% 13C; U-100% 15N], 0.75 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D hetnoesample_2isotropicsample_conditions_1
1D T1 inv.recsample_2isotropicsample_conditions_1
1D T2 CPMGsample_2isotropicsample_conditions_1
2D 1H-13C HSQC highressample_2isotropicsample_conditions_1
Jmod 15N TROSYsample_3anisotropicsample_conditions_1
jmod 15N TROSYsample_3anisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAV45400 EMA13016 EMA22096
REF WP_004962568 WP_007188424 WP_011222974