BMRB Entry 34761

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34761
MolProbity Validation Chart

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

Title:
Solution structure of tandem RRM1 and RRM2 domains of yeast NPL3
Deposition date:
2022-10-04
Original release date:
2025-07-07
Authors:
Kachariya, N.; Sattler, M.; Keil, P.; Strasser, K.
Citation:

Citation: Keil, P.; Wulf, A.; Kachariya, N.; Reuscher, S.; Huhn, K.; Silbern, I.; Altmuller, J.; Keller, M.; Stehle, R.; Zarnack, K.; Sattler, M.; Urlaub, H.; Strasser, K.. "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).
PubMed: 36583366

Assembly members:

Assembly members:
entity_1, polymer, 161 residues, 18228.414 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET family vector

Entity Sequences (FASTA):

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
1unit_11

Entities:

Entity 1, unit_1 161 residues - 18228.414 Da.

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: RRM1,2 of NPL3, [U-100% 15N], 150 uM

sample_2: RRM1,2 of NPL3, [U-100% 13C; U-100% 15N], 1000 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
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TopSpin v3.5pl6, Bruker Biospin - collection

TopSpin, Bruker Biospin - processing

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

CcpNmr Analysis v2.5.0, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

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

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