BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16430

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16430

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: 1H, 13C, 15N backbone resonance assginments of Nep1 from Methanococcus jannaschii   PubMed: 19779849

Deposition date: 2009-07-29 Original release date: 2009-09-08

Authors: Wurm, Philip; Duchardt, Elke; Meyer, Britta; Leal, Belinda; Koetter, Peter; Entian, Karl-Dieter

Citation: Wurm, Philip; Duchardt, Elke; Meyer, Britta; Leal, Belinda; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens. "Backbone resonance assignments of the 48 kDa dimeric putative rRNA-methyltransferase Nep1 from Methanocaldococcus jannaschii"  Biomol. NMR Assignments 3, 251-254 (2009).

Assembly members:
Nep1_chain, polymer, 205 residues, Formula weight is not available

Natural source:   Common Name: Methanococcus jannaschii   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus jannaschii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Entity Sequences (FASTA):
Nep1_chain: MTYNIILAKSALELIPEEIK NKIRKSRVYKYDILDSNYHY KAMEKLKDKEMRGRPDIIHI SLLNILDSPINHEKKLNIYI HTYDDKVLKINPETRLPRNY FRFLGVMEKVLKGERNHLIK MEEKTLEDLLNEINAKKIAI MTKTGKLTHPKLLKEYDTFI IGGFPYGKLKINKEKVFGDI KEISIYNKGLMAWTVCGIIC YSLSF

Data sets:
Data typeCount
13C chemical shifts1198
15N chemical shifts390
1H chemical shifts390

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer 11
2monomer 21

Entities:

Entity 1, monomer 1 205 residues - Formula weight is not available

1   METTHRTYRASNILEILELEUALALYSSER
2   ALALEUGLULEUILEPROGLUGLUILELYS
3   ASNLYSILEARGLYSSERARGVALTYRLYS
4   TYRASPILELEUASPSERASNTYRHISTYR
5   LYSALAMETGLULYSLEULYSASPLYSGLU
6   METARGGLYARGPROASPILEILEHISILE
7   SERLEULEUASNILELEUASPSERPROILE
8   ASNHISGLULYSLYSLEUASNILETYRILE
9   HISTHRTYRASPASPLYSVALLEULYSILE
10   ASNPROGLUTHRARGLEUPROARGASNTYR
11   PHEARGPHELEUGLYVALMETGLULYSVAL
12   LEULYSGLYGLUARGASNHISLEUILELYS
13   METGLUGLULYSTHRLEUGLUASPLEULEU
14   ASNGLUILEASNALALYSLYSILEALAILE
15   METTHRLYSTHRGLYLYSLEUTHRHISPRO
16   LYSLEULEULYSGLUTYRASPTHRPHEILE
17   ILEGLYGLYPHEPROTYRGLYLYSLEULYS
18   ILEASNLYSGLULYSVALPHEGLYASPILE
19   LYSGLUILESERILETYRASNLYSGLYLEU
20   METALATRPTHRVALCYSGLYILEILECYS
21   TYRSERLEUSERPHE

Samples:

sample_1: Nep1 dimer, [U-13C; U-15N], 300 uM; potassium chloride 50 mM; acetic acid 25 mM; beta-mercaptoethanol 2 mM; H2O 90%; D2O 10%

sample_2: Nep1 dimer, [U-13C; U-15N; U-2H], 200 uM; potassium chloride 50 mM; acetic acid 25 mM; beta-mercaptoethanol 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.063 M; pH: 4.5; pressure: 1 atm; temperature: 320 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

PDB
GB AAB98551
SP Q57977
AlphaFold Q57977

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