BMRB Entry 27228

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27228

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for SLP-65
Deposition date:
2017-08-22
Original release date:
2018-03-08
Authors:
Wong, Leo; Maier, Joachim; Becker, Stefan; Griesinger, Christian
Citation:

Citation: Wong, Leo; Maier, Joachim; Wienands, Juergen; Becker, Stefan; Griesinger, Christian. "Sensitivity-Enhanced Four-Dimensional Amide-Amide Correlation NMR Experiments for Sequential Assignment of Proline-Rich Disordered Proteins"  J. Am. Chem. Soc. 140, 3518-3522 (2018).
PubMed: 29489342

Assembly members:

Assembly members:
SLP-65, polymer, 293 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SLP-65: GHMVKAPPSVPRRDYASESP ADEEEQWSDDFDSDYENPDE HSDSEMYVMPAEENADDSYE PPPVEQETRPVHPALPFARG EYIDNRSSQRHSPPFSKTLP SKPSWPSEKARLTSTLPALT ALQKPQVPPKPKGLLEDEAD YVVPVEDNDENYIHPTESSS PPPEKAPMVNRSTKPNSSTP ASPPGTASGRNSGAWETKSP PPAAPSPLPRAGKKPTTPLK TTPVASQQNASSVCEEKPIP AERHRGSSHRQEAVQSPVFP PAQKQIHQKPIPLPRFTEGG NPTVDGPLPSFSS

Data sets:
Data typeCount
13C chemical shifts698
15N chemical shifts236
1H chemical shifts236

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SLP-651

Entities:

Entity 1, SLP-65 293 residues - Formula weight is not available

1   GLYHISMETVALLYSALAPROPROSERVAL
2   PROARGARGASPTYRALASERGLUSERPRO
3   ALAASPGLUGLUGLUGLNTRPSERASPASP
4   PHEASPSERASPTYRGLUASNPROASPGLU
5   HISSERASPSERGLUMETTYRVALMETPRO
6   ALAGLUGLUASNALAASPASPSERTYRGLU
7   PROPROPROVALGLUGLNGLUTHRARGPRO
8   VALHISPROALALEUPROPHEALAARGGLY
9   GLUTYRILEASPASNARGSERSERGLNARG
10   HISSERPROPROPHESERLYSTHRLEUPRO
11   SERLYSPROSERTRPPROSERGLULYSALA
12   ARGLEUTHRSERTHRLEUPROALALEUTHR
13   ALALEUGLNLYSPROGLNVALPROPROLYS
14   PROLYSGLYLEULEUGLUASPGLUALAASP
15   TYRVALVALPROVALGLUASPASNASPGLU
16   ASNTYRILEHISPROTHRGLUSERSERSER
17   PROPROPROGLULYSALAPROMETVALASN
18   ARGSERTHRLYSPROASNSERSERTHRPRO
19   ALASERPROPROGLYTHRALASERGLYARG
20   ASNSERGLYALATRPGLUTHRLYSSERPRO
21   PROPROALAALAPROSERPROLEUPROARG
22   ALAGLYLYSLYSPROTHRTHRPROLEULYS
23   THRTHRPROVALALASERGLNGLNASNALA
24   SERSERVALCYSGLUGLULYSPROILEPRO
25   ALAGLUARGHISARGGLYSERSERHISARG
26   GLNGLUALAVALGLNSERPROVALPHEPRO
27   PROALAGLNLYSGLNILEHISGLNLYSPRO
28   ILEPROLEUPROARGPHETHRGLUGLYGLY
29   ASNPROTHRVALASPGLYPROLEUPROSER
30   PHESERSER

Samples:

sample_1: SLP-65, [U-13C; U-15N], 0.65 mM; DSS 0.35 mM; MES 20 mM; TCEP 1 mM; AEBSF protease inhibitor 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D HNcocaNHsample_1isotropicsample_conditions_1
4D HNcocancaNH x-P-xsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection

CARA v1.9.0, Keller and Wuthrich - data analysis

GAPRO v0.9.8, Sebastian Hiller - data analysis

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