BMRB Entry 15303

Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15303

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Title:
1H, 15N, 13C resonance assignments for bb' domains of human protein disulfide isomerase (PDI)
Deposition date:
2007-06-13
Original release date:
2007-08-08
Authors:
Denisov, Alexey; Maattanen, Pekka; Thomas, David; Gehring, Kalle
Citation:

Citation: Denisov, Alexey Yu; Maattanen, Pekka; Sprules, Tara; Thomas, David; Gehring, Kalle. "1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase"  Biomol. NMR Assignments 1, 129-130 (2007).
PubMed: 19636846

Assembly members:

Assembly members:
bb-PDI, polymer, 228 residues, 25500 Da.

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: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
bb-PDI: GPLGSPAATTLPDGAAAESL VESSEVAVIGFFKDVESDSA KQFLQAAEAIDDIPFGITSN SDVFSKYQLDKDGVVLFKKF DEGRNNFEGEVTKENLLDFI KHNQLPLVIEFTEQTAPKIF GGEIKTHILLFLPKSVSDYD GKLSNFKTAAESFKGKILFI FIDSDHTDNQRILEFFGLKK EECPAVRLITLEEEMTKYKP ESEELTAERITEFCHRFLEG KIKPHLMS

Data sets:
Data typeCount
13C chemical shifts685
15N chemical shifts223
1H chemical shifts1161

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1bb-PDI monomer, major conformer1
2bb-PDI monomer, minor conformer1

Entities:

Entity 1, bb-PDI monomer, major conformer 228 residues - 25500 Da.

Residues 1-5 represent a non-native tag

1   GLYPROLEUGLYSERPROALAALATHRTHR
2   LEUPROASPGLYALAALAALAGLUSERLEU
3   VALGLUSERSERGLUVALALAVALILEGLY
4   PHEPHELYSASPVALGLUSERASPSERALA
5   LYSGLNPHELEUGLNALAALAGLUALAILE
6   ASPASPILEPROPHEGLYILETHRSERASN
7   SERASPVALPHESERLYSTYRGLNLEUASP
8   LYSASPGLYVALVALLEUPHELYSLYSPHE
9   ASPGLUGLYARGASNASNPHEGLUGLYGLU
10   VALTHRLYSGLUASNLEULEUASPPHEILE
11   LYSHISASNGLNLEUPROLEUVALILEGLU
12   PHETHRGLUGLNTHRALAPROLYSILEPHE
13   GLYGLYGLUILELYSTHRHISILELEULEU
14   PHELEUPROLYSSERVALSERASPTYRASP
15   GLYLYSLEUSERASNPHELYSTHRALAALA
16   GLUSERPHELYSGLYLYSILELEUPHEILE
17   PHEILEASPSERASPHISTHRASPASNGLN
18   ARGILELEUGLUPHEPHEGLYLEULYSLYS
19   GLUGLUCYSPROALAVALARGLEUILETHR
20   LEUGLUGLUGLUMETTHRLYSTYRLYSPRO
21   GLUSERGLUGLULEUTHRALAGLUARGILE
22   THRGLUPHECYSHISARGPHELEUGLUGLY
23   LYSILELYSPROHISLEUMETSER

Samples:

sample_1: bb-PDI, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 25 mM; sodium chloride 70 mM; EDTA 0.5 mM; DTT 5 mM

sample_2: bb-PDI, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 25 mM; sodium chloride 70 mM; EDTA 0.5 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

XEASY v1.3.13, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 15974 15998
PDB
DBJ BAE79726 BAE87231 BAE88032 BAG37999 BAG60277
EMBL CAA28775 CAH93050
GB AAA61169 AAC13652 AAH10859 AAH29617 AAH71892
REF NP_000909 NP_001126805 NP_001233358 XP_002764185 XP_003282223
SP P07237 Q2HWU2 Q5R5B6
AlphaFold P07237 Q2HWU2 Q5R5B6

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