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 16897

Title: The solution structure of MTH1821   PubMed: 21387412

Deposition date: 2010-04-23 Original release date: 2011-04-08

Authors: Lee, Weontae; Ko, Sunggeon

Citation: Ko, Sunggeon; Kim, Heeyoun; Yun, Jihye; Yee, Adelinda; Arrowsmith, Cheryl; Cheong, Chaejoon; Lee, Weontae. "Solution structure of MTH1821, a putative structure homologue to RNA polymerase subunit from Methanobacterium thermoautotrophicum."  Proteins 79, 1347-1351 (2011).

Assembly members:
MTH1821, polymer, 96 residues, 11484.018 Da.

Natural source:   Common Name: Methanobacterium thermoautotrophicum   Taxonomy ID: 145262   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanobacterium thermoautotrophicum

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

Entity Sequences (FASTA):
MTH1821: MVFYLKVKVEDFGFREDMGL NYVRYRVSGLDEELTEKLIE RLDEDTERDDGDLIITVFYE REYFPFGSEESKVKMADFIA REEIEMMVFLSSVLED

Data sets:
Data typeCount
13C chemical shifts375
15N chemical shifts92
1H chemical shifts651

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MTH18211

Entities:

Entity 1, MTH1821 96 residues - 11484.018 Da.

1   METVALPHETYRLEULYSVALLYSVALGLU
2   ASPPHEGLYPHEARGGLUASPMETGLYLEU
3   ASNTYRVALARGTYRARGVALSERGLYLEU
4   ASPGLUGLULEUTHRGLULYSLEUILEGLU
5   ARGLEUASPGLUASPTHRGLUARGASPASP
6   GLYASPLEUILEILETHRVALPHETYRGLU
7   ARGGLUTYRPHEPROPHEGLYSERGLUGLU
8   SERLYSVALLYSMETALAASPPHEILEALA
9   ARGGLUGLUILEGLUMETMETVALPHELEU
10   SERSERVALLEUGLUASP

Samples:

sample_1: MTH1821, [U-99% 15N], 1.2 mM; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

sample_3: MTH1821, [U-100% 13C], 1.2 mM; D2O 100%; HEPES 20 mM; NaCl 100 mM

sample_2: MTH1821, [U-99% 13C; U-99% 15N], 1.2 mM; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.2.5, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

xwinnmr, Bruker Biospin - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 900 MHz

Related Database Links:

PDB
GB AAB86287
REF WP_048061147

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