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 51631

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51631

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Title: 1H,13C,15N Backbone and side-chain assignments of tandem RRM domains of Npl3   PubMed: 36583366

Deposition date: 2022-09-16 Original release date: 2022-10-14

Authors: Kachariya, Nitin; Sattler, Michael

Citation: Keil, Philipp; Wulf, Alexander; Kachariya, Nitin; Reuscher, Samira; Huhn, Kristin; Silbern, Ivan; Altmuller, Janine; Keller, Mario; Stehle, Ralf; Zarnack, Kathi; Sattler, Michael; Urlaub, Henning; Strasser, Katja. "Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA"  Nucleic Acids Res. 51, 831-851 (2023).

Assembly members:
entity_1, polymer, 161 residues, Formula weight is not available

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-M11

Entity Sequences (FASTA):
entity_1: GELSNTRLFVRPFPLDVQES ELNEIFGPFGPMKEVKILNG FAFVEFEEAESAAKAIEEVH GKSFANQPLEVVYSKLPAKR YRITMKNLPEGCSWQDLKDL ARENSLETTFSSVNTRDFDG TGALEFPSEEILVEALERLN NIEFRGSVITVERDDNPPPI R

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts163
1H chemical shifts995

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Npl3 monomer1

Entities:

Entity 1, Npl3 monomer 161 residues - Formula weight is not available

Residues from 121 to 280 are assigned

1   GLYGLULEUSERASNTHRARGLEUPHEVAL
2   ARGPROPHEPROLEUASPVALGLNGLUSER
3   GLULEUASNGLUILEPHEGLYPROPHEGLY
4   PROMETLYSGLUVALLYSILELEUASNGLY
5   PHEALAPHEVALGLUPHEGLUGLUALAGLU
6   SERALAALALYSALAILEGLUGLUVALHIS
7   GLYLYSSERPHEALAASNGLNPROLEUGLU
8   VALVALTYRSERLYSLEUPROALALYSARG
9   TYRARGILETHRMETLYSASNLEUPROGLU
10   GLYCYSSERTRPGLNASPLEULYSASPLEU
11   ALAARGGLUASNSERLEUGLUTHRTHRPHE
12   SERSERVALASNTHRARGASPPHEASPGLY
13   THRGLYALALEUGLUPHEPROSERGLUGLU
14   ILELEUVALGLUALALEUGLUARGLEUASN
15   ASNILEGLUPHEARGGLYSERVALILETHR
16   VALGLUARGASPASPASNPROPROPROILE
17   ARG

Samples:

sample_1: Npl3, [U-100% 15N], 525 uM; Npl3, [U-100% 13C; U-100% 15N], 525 uM

sample_conditions_1: ionic strength: 70 mM; 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 HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5pl6 - collection, processing

NMRPipe v11.1 - processing

CcpNMR v2.5.0 - chemical shift assignment, data analysis, peak picking

NMRbox - data analysis

CNSSOLVE - refinement

NESSY - data analysis

PyMOL - structure solution

NMR spectrometers:

  • Bruker AVANCE III 500 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 900 MHz
  • Bruker AVANCE III 950 MHz

Related Database Links:

UNP Q01560
AlphaFold D6VT60

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