BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11561

Title: Redox protein (oxidized form)

Authors: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi

Citation: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi. "1H , 13C and 15N Assigned Chemical Shifts for PDI"  Not known ., .-..

Assembly members:
PDI, polymer, 121 residues, 13124.035 Da.

Natural source:   Common Name: Soft-rot fungus   Taxonomy ID: 34413   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Humicola isolens

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

Entity Sequences (FASTA):
PDI: GPLGSEGPVTVVVAKNYNEI VLDDTKDVLIEFYAPWCGHC KALAPKYEELGALYAKSEFK DRVVIAKVDATANDVPDEIQ GFPTIKLYPAGAKGQPVTYS GSRTVEDLIKFIAENGKYKA A

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts110
1H chemical shifts714

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 121 residues - 13124.035 Da.

Residues 1-5 represent a non-native affinity tag

1   GLYPROLEUGLYSERGLUGLYPROVALTHR
2   VALVALVALALALYSASNTYRASNGLUILE
3   VALLEUASPASPTHRLYSASPVALLEUILE
4   GLUPHETYRALAPROTRPCYSGLYHISCYS
5   LYSALALEUALAPROLYSTYRGLUGLULEU
6   GLYALALEUTYRALALYSSERGLUPHELYS
7   ASPARGVALVALILEALALYSVALASPALA
8   THRALAASNASPVALPROASPGLUILEGLN
9   GLYPHEPROTHRILELYSLEUTYRPROALA
10   GLYALALYSGLYGLNPROVALTHRTYRSER
11   GLYSERARGTHRVALGLUASPLEUILELYS
12   PHEILEALAGLUASNGLYLYSTYRLYSALA
13   ALA

Samples:

sample_1: PDI, [U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; H2O 90%; D2O 10%

sample_2: PDI, [U-13C; U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 0.16 M; pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement

SPARKY v3.1, Goddard - chemical shift assignment

xwinnmr v2.6, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • JEOL ECA 920 MHz

Related Database Links:

UNP P55059
BMRB 11562
PDB