BMRB Entry 51864

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51864

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Title:
PDIA6 amide backbone assignment
Deposition date:
2023-03-02
Original release date:
2025-05-20
Authors:
Leder, Anna; Mas, Guillaume; Hiller, Sebastian
Citation:

Citation: Leder, Anna; Mas, Guillaume; Hiller, Sebastian. "ER stress switches PDIA6 function from LLPS folding factoreis to UPR attenuation"  Cell ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 421 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: p28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LYSSSDDVIELTPSNFNREV IQSDSLWLVEFYAPWCGHCQ RLTPEWKKAATALKDVVKVG AVDADKHHSLGGQYGVQGFP TIKIFGSNKNRPEDYQGGRT GEAIVDAALSALRQLVKDRL GGRSGGYSSGKQGRSDSSSK KDVIELTDDSFDKNVLDSED VWMVEFYAPWCGHCKNLEPE WAAAASEVKEQTKGKVKLAA VDATVNQVLASRYGIRGFPT IKIFQKGESPVDYDGGRTRS DIVSRALDLFSDNAPPPELL EIINEDIAKRTCEEHQLCVV AVLPHILDTGAAGRNSYLEV LLKLADKYKKKMWGWLWTEA GAQSELETALGIGGFGYPAM AAINARKMKFALLKGSFSEQ GINEFLRELSFGRGSTAPVG GGAFPTIVEREPWDGRDGEL PVEDDIDLSDVELDDLGKDE L

Data typeCount
15N chemical shifts349
1H chemical shifts349

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDIA61

Entities:

Entity 1, PDIA6 421 residues - Formula weight is not available

1   LEUTYRSERSERSERASPASPVALILEGLU
2   LEUTHRPROSERASNPHEASNARGGLUVAL
3   ILEGLNSERASPSERLEUTRPLEUVALGLU
4   PHETYRALAPROTRPCYSGLYHISCYSGLN
5   ARGLEUTHRPROGLUTRPLYSLYSALAALA
6   THRALALEULYSASPVALVALLYSVALGLY
7   ALAVALASPALAASPLYSHISHISSERLEU
8   GLYGLYGLNTYRGLYVALGLNGLYPHEPRO
9   THRILELYSILEPHEGLYSERASNLYSASN
10   ARGPROGLUASPTYRGLNGLYGLYARGTHR
11   GLYGLUALAILEVALASPALAALALEUSER
12   ALALEUARGGLNLEUVALLYSASPARGLEU
13   GLYGLYARGSERGLYGLYTYRSERSERGLY
14   LYSGLNGLYARGSERASPSERSERSERLYS
15   LYSASPVALILEGLULEUTHRASPASPSER
16   PHEASPLYSASNVALLEUASPSERGLUASP
17   VALTRPMETVALGLUPHETYRALAPROTRP
18   CYSGLYHISCYSLYSASNLEUGLUPROGLU
19   TRPALAALAALAALASERGLUVALLYSGLU
20   GLNTHRLYSGLYLYSVALLYSLEUALAALA
21   VALASPALATHRVALASNGLNVALLEUALA
22   SERARGTYRGLYILEARGGLYPHEPROTHR
23   ILELYSILEPHEGLNLYSGLYGLUSERPRO
24   VALASPTYRASPGLYGLYARGTHRARGSER
25   ASPILEVALSERARGALALEUASPLEUPHE
26   SERASPASNALAPROPROPROGLULEULEU
27   GLUILEILEASNGLUASPILEALALYSARG
28   THRCYSGLUGLUHISGLNLEUCYSVALVAL
29   ALAVALLEUPROHISILELEUASPTHRGLY
30   ALAALAGLYARGASNSERTYRLEUGLUVAL
31   LEULEULYSLEUALAASPLYSTYRLYSLYS
32   LYSMETTRPGLYTRPLEUTRPTHRGLUALA
33   GLYALAGLNSERGLULEUGLUTHRALALEU
34   GLYILEGLYGLYPHEGLYTYRPROALAMET
35   ALAALAILEASNALAARGLYSMETLYSPHE
36   ALALEULEULYSGLYSERPHESERGLUGLN
37   GLYILEASNGLUPHELEUARGGLULEUSER
38   PHEGLYARGGLYSERTHRALAPROVALGLY
39   GLYGLYALAPHEPROTHRILEVALGLUARG
40   GLUPROTRPASPGLYARGASPGLYGLULEU
41   PROVALGLUASPASPILEASPLEUSERASP
42   VALGLULEUASPASPLEUGLYLYSASPGLU
43   LEU

Samples:

sample_1: PDIA6 domain a0, [U-13C; U-15N; U-2H], 1.6 mM; D2O, [U-2H], 5%; HEPES 25 mM; KCl 150 mM; MgCl2 10 mM; DSS 1 mM; TCEP 10 mM

sample_2: PDIA6 domain a, [U-13C; U-15N; U-1H], 1.0 mM; D2O, [U-2H], 5%; HEPES 25 mM; KCl 150 mM; MgCl2 10 mM; DSS 1 mM; TCEP 10 mM

sample_3: PDIA6 domain a, [U-13C; U-15N; U-2H], 1.0 mM; D2O, [U-2H], 10%; HEPES 25 mM; KCl 150 mM; MgCl2 10 mM; DSS 1 mM; GSSG 10 mM

sample_conditions_1: ionic strength: 160 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 160 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
4D APSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_2
3D HNCAsample_3isotropicsample_conditions_2
3D HNCACBsample_3isotropicsample_conditions_2
3D HNCOsample_3isotropicsample_conditions_2
3D HNCACOsample_3isotropicsample_conditions_2
3D 1H-15N NOESYsample_3isotropicsample_conditions_2

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE NEO 700 MHz

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