BMRB Entry 25748

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25748
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
ddFLN5+110
Deposition date:
2015-08-10
Original release date:
2016-02-29
Authors:
Cabrita, Lisa; Cassaignau, Anais; Launay, Helene; Waudby, Christopher; Camilloni, Carlo; Robertson, Amy; Wang, Xiaolin; Wlodarski, Tomasz; Wentink, Anne; Vendruscolo, Michele; Dobson, Christopher; Christodoulou, John
Citation:

Citation: Cassaignau, Anais; Launay, Helene; Karyadi, Maria-Evangelia; Wang, Xiaolin; Waudby, Christopher; Deckert, Annika; Robertson, Amy; Christodoulou, John; Cabrita, Lisa. "A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy"  Nat. Protoc. 11, 1492-1507 (2016).
PubMed: 27466710

Assembly members:

Assembly members:
entity, polymer, 221 residues, 23420.918 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pLDC-17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: HHHHHHASKPAPSAEHSYAE GEGLVKVFDNAPAEFTIFAV DTKGVARTDGGDPFEVAING PDGLVVDAKVTDNNDGTYGV VYDAPVEGNYNVNVTLRGNP IKNMPIDVKCIEGANGEDSS FGSFTFTVAAKNKKGEVKTY GGDKFEVSITGPAEEITLDA IDNQDGTYTAAYSLVGNGRF STGVKLNGKHIEGSPFKQVL GNELFSTPVWISQAQGIRAG P

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts122
1H chemical shifts204

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 221 residues - 23420.918 Da.

1   HISHISHISHISHISHISALASERLYSPRO
2   ALAPROSERALAGLUHISSERTYRALAGLU
3   GLYGLUGLYLEUVALLYSVALPHEASPASN
4   ALAPROALAGLUPHETHRILEPHEALAVAL
5   ASPTHRLYSGLYVALALAARGTHRASPGLY
6   GLYASPPROPHEGLUVALALAILEASNGLY
7   PROASPGLYLEUVALVALASPALALYSVAL
8   THRASPASNASNASPGLYTHRTYRGLYVAL
9   VALTYRASPALAPROVALGLUGLYASNTYR
10   ASNVALASNVALTHRLEUARGGLYASNPRO
11   ILELYSASNMETPROILEASPVALLYSCYS
12   ILEGLUGLYALAASNGLYGLUASPSERSER
13   PHEGLYSERPHETHRPHETHRVALALAALA
14   LYSASNLYSLYSGLYGLUVALLYSTHRTYR
15   GLYGLYASPLYSPHEGLUVALSERILETHR
16   GLYPROALAGLUGLUILETHRLEUASPALA
17   ILEASPASNGLNASPGLYTHRTYRTHRALA
18   ALATYRSERLEUVALGLYASNGLYARGPHE
19   SERTHRGLYVALLYSLEUASNGLYLYSHIS
20   ILEGLUGLYSERPROPHELYSGLNVALLEU
21   GLYASNGLULEUPHESERTHRPROVALTRP
22   ILESERGLNALAGLNGLYILEARGALAGLY
23   PRO

Samples:

sample_1: ddFLN5+110, [U-15N], 10 uM; HEPES 10 mM; ammonium chloride 30 mM; MgCl2 12 mM; BME 2 mM; EDTA 1 mM

sample_2: ddFLN5+110, [U-100% 2H, Ile d1-13CH3], 10 uM; HEPES, [U-2H], 10 mM; ammonium chloride, [U-2H], 30 mM; MgCl2, [U-2H], 12 mM; BME, [U-2H], 2 mM; EDTA, [U-2H], 1 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N SOFAST HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_1

Software:

GROMACS v5.0.4, GROMACS - structure calculation using molecular dynamics simulations with chemical shifts restraints

NMR spectrometers:

  • Bruker Avance 700 MHz

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