BMRB Entry 52048

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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/BMR52048
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Human PEX5 TPR domain
Deposition date:
2023-07-20
Original release date:
2026-10-01
Authors:
Gaussmann, Stefan; Emmanouilidis, Leonidas; Sattler, Michael
Citation:

Citation: Emmanouilidis, Leonidas. "Gatekeeping of peroxisomal import by an allosteric modulation of receptor/cargo interactions "  Nature Communications ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 328 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMLTSATYDKGYQFEEENP LRDHPQPFEEGLRRLQEGDL PNAVLLFEAAVQQDPKHMEA WQYLGTTQAENEQELLAISA LRRCLELKPDNQTALMALAV SFTNESLQRQACETLRDWLR YTPAYAHLVTPAEEGAGGAG LGPSKRILGSLLSDSLFLEV KELFLAAVRLDPTSIDPDVQ CGLGVLFNLSGEYDKAVDCF TAALSVRPNDYLLWNKLGAT LANGNQSEEAVAAYRRALEL QPGYIRSRYNLGISCINLGA HREAVEHFLEALNMQRKSRG PRGEGGAMSENIWSTLRLAL SMLGQSDAYGAADARDLSTL LTMFGLPQ

Data sets:
Data typeCount
13C chemical shifts628
15N chemical shifts185
1H chemical shifts275

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PEX5 TPR1

Entities:

Entity 1, PEX5 TPR 328 residues - Formula weight is not available

1   GLYALAMETLEUTHRSERALATHRTYRASP
2   LYSGLYTYRGLNPHEGLUGLUGLUASNPRO
3   LEUARGASPHISPROGLNPROPHEGLUGLU
4   GLYLEUARGARGLEUGLNGLUGLYASPLEU
5   PROASNALAVALLEULEUPHEGLUALAALA
6   VALGLNGLNASPPROLYSHISMETGLUALA
7   TRPGLNTYRLEUGLYTHRTHRGLNALAGLU
8   ASNGLUGLNGLULEULEUALAILESERALA
9   LEUARGARGCYSLEUGLULEULYSPROASP
10   ASNGLNTHRALALEUMETALALEUALAVAL
11   SERPHETHRASNGLUSERLEUGLNARGGLN
12   ALACYSGLUTHRLEUARGASPTRPLEUARG
13   TYRTHRPROALATYRALAHISLEUVALTHR
14   PROALAGLUGLUGLYALAGLYGLYALAGLY
15   LEUGLYPROSERLYSARGILELEUGLYSER
16   LEULEUSERASPSERLEUPHELEUGLUVAL
17   LYSGLULEUPHELEUALAALAVALARGLEU
18   ASPPROTHRSERILEASPPROASPVALGLN
19   CYSGLYLEUGLYVALLEUPHEASNLEUSER
20   GLYGLUTYRASPLYSALAVALASPCYSPHE
21   THRALAALALEUSERVALARGPROASNASP
22   TYRLEULEUTRPASNLYSLEUGLYALATHR
23   LEUALAASNGLYASNGLNSERGLUGLUALA
24   VALALAALATYRARGARGALALEUGLULEU
25   GLNPROGLYTYRILEARGSERARGTYRASN
26   LEUGLYILESERCYSILEASNLEUGLYALA
27   HISARGGLUALAVALGLUHISPHELEUGLU
28   ALALEUASNMETGLNARGLYSSERARGGLY
29   PROARGGLYGLUGLYGLYALAMETSERGLU
30   ASNILETRPSERTHRLEUARGLEUALALEU
31   SERMETLEUGLYGLNSERASPALATYRGLY
32   ALAALAASPALAARGASPLEUSERTHRLEU
33   LEUTHRMETPHEGLYLEUPROGLN

Samples:

sample_1: PEX5 TPR 1H, [U-99% 13C; U-99% 15N], 0.85 mM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: PEX5 TPR 2H, [U-99% 13C; U-99% 15N; U-90% 2H], 0.85 mM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_3: PEX5 TPR ILV, [U-13C; U-15N; U-2H; 99% 1HD-Ile,Leu; 99% 1HG-Val], 0.75 mM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 83 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 83 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 83 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_2
3D CBCANH TROSYsample_2isotropicsample_conditions_2
3D HNCO TROSYsample_2isotropicsample_conditions_2
3D HN(CA)CO TROSYsample_2isotropicsample_conditions_2
2D 1H-13C HSQC/HMQCsample_3isotropicsample_conditions_3
3D HCC FLOPSYsample_3isotropicsample_conditions_3
3D 15N 13C NOESY HSQCsample_3isotropicsample_conditions_3

Software:

TOPSPIN v3.5pl6 - collection

NMRPipe - processing

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

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

Related Database Links:

UNP P50542
AlphaFold P50542

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