BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 30231

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30231
MolProbity Validation Chart

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Title: Solution structure of the oxidized iron-sulfur protein adrenodoxin from Encephalitozoon cuniculi. Seattle Structural Genomics Center for Infectious Disease target EncuA.00705.a

Deposition date: 2017-01-17 Original release date: 2017-01-26

Authors: Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation: Buchko, G.; Hewitt, S.; Van Voorhis, W.; Myler, P.. "Solution structure of the oxidized iron-sulfur protein andrenodoxin from Encephalitozoon cuniculi."  . ., .-..

Assembly members:
entity_1, polymer, 132 residues, 14377.485 Da.
entity_FES, non-polymer, 175.820 Da.

Natural source:   Common Name: Microsporidian parasite   Taxonomy ID: 6035   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Encephalitozoon cuniculi

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

Entity Sequences (FASTA):
entity_1: GPGSMDMFSAPDRIPEQIRI FFKTMKQVVPAKAVCGSTVL DVAHKNGVDLEGACEGNLAC STCHVILEEPLYRKLGEPSD KEYDLIDQAFGATGTSRLGC QLRVDKSFENAVFTVPRATK NMAVDGFKPKPH

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts107
1H chemical shifts591

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 132 residues - 14377.485 Da.

1   GLYPROGLYSERMETASPMETPHESERALA
2   PROASPARGILEPROGLUGLNILEARGILE
3   PHEPHELYSTHRMETLYSGLNVALVALPRO
4   ALALYSALAVALCYSGLYSERTHRVALLEU
5   ASPVALALAHISLYSASNGLYVALASPLEU
6   GLUGLYALACYSGLUGLYASNLEUALACYS
7   SERTHRCYSHISVALILELEUGLUGLUPRO
8   LEUTYRARGLYSLEUGLYGLUPROSERASP
9   LYSGLUTYRASPLEUILEASPGLNALAPHE
10   GLYALATHRGLYTHRSERARGLEUGLYCYS
11   GLNLEUARGVALASPLYSSERPHEGLUASN
12   ALAVALPHETHRVALPROARGALATHRLYS
13   ASNMETALAVALASPGLYPHELYSPROLYS
14   PROHIS

Entity 2, entity_2 - Fe2 S2 - 175.820 Da.

1   FES

Samples:

sample_1: DTT 1 ± 0.1 mM; E5, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; TRIS 20 ± 0.2 mM; sodium chloride 100 ± 2 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1anisotropicsample_conditions_1
deuterium exchangesample_1anisotropicsample_conditions_1
3D C(CO)NHsample_1anisotropicsample_conditions_1
3D H(CCO)NHsample_1anisotropicsample_conditions_1
2D HBCBCGCDHDsample_1anisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

SPARKY v3.115, Goddard - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian VXRS 750 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts