BMRB Entry 15998

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15998

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Title:
Chemical shifts of the b'-x region of human protein disulfide isomerase
Deposition date:
2008-10-23
Original release date:
2009-07-17
Authors:
Byrne, Lee; Howard, Mark; Williamson, Richard; Sidhu, Ateesh; Freedman, Robert; Wallis, Katrine
Citation:

Citation: Byrne, Lee; Sidhu, Ateesh; Wallis, A. Katrine; Ruddock, Lloyd; Freedman, Robert; Howard, Mark; Williamson, Richard. "Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region."  Biochem. J. 423, 209-217 (2009).
PubMed: 19604149

Assembly members:

Assembly members:
b'-x, polymer, 140 residues, 16296.7 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: pET23b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
b'-x: KHNQLPLVIEFTEQTAPKIF GGEIKTHILLFLPKSVSDYD GKLSNFKTAAESFKGKILFI FIDSDHTDNQRILEFFGLKK EECPAVRLITLEEEMTKYKP ESEELTAERITEFCHRFLEG KIKPHLMSQELPEDWDKQPV

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts129
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1b'-x1

Entities:

Entity 1, b'-x 140 residues - 16296.7 Da.

1   LYSHISASNGLNLEUPROLEUVALILEGLU
2   PHETHRGLUGLNTHRALAPROLYSILEPHE
3   GLYGLYGLUILELYSTHRHISILELEULEU
4   PHELEUPROLYSSERVALSERASPTYRASP
5   GLYLYSLEUSERASNPHELYSTHRALAALA
6   GLUSERPHELYSGLYLYSILELEUPHEILE
7   PHEILEASPSERASPHISTHRASPASNGLN
8   ARGILELEUGLUPHEPHEGLYLEULYSLYS
9   GLUGLUCYSPROALAVALARGLEUILETHR
10   LEUGLUGLUGLUMETTHRLYSTYRLYSPRO
11   GLUSERGLUGLULEUTHRALAGLUARGILE
12   THRGLUPHECYSHISARGPHELEUGLUGLY
13   LYSILELYSPROHISLEUMETSERGLNGLU
14   LEUPROGLUASPTRPASPLYSGLNPROVAL

Samples:

sample_1: D2O 10%; H2O 90%; sodium phosphate 20 mM; sodium chloride 150 mM; b'-x, [U-99% 13C; U-99% 15N], 1.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CCPN_Analysis v1.15, CCPN - chemical shift assignment, data analysis, peak picking

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

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15303 15974
PDB
DBJ BAE79726 BAG37999 BAG59598 BAG60277 BAG62267
EMBL CAA28775 CAA30112 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