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 16352

Title: Solution NMR structure of protein AF2094 from Archaeoglobus fulgidus. Northeast Structural Genomics Consotium (NESG) target GT2

Deposition date: 2009-06-15 Original release date: 2009-07-07

Authors: Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR structure of proterin AF2094 from Archaeoglobus fulgidus."  .

Assembly members:
AF2094, polymer, 95 residues, 10726.126 Da.

Natural source:   Common Name: Archaeoglobus fulgidus   Taxonomy ID: 2234   Superkingdom: Archaea   Kingdom: not available   Genus/species: Archaeoglobus fulgidus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p11

Entity Sequences (FASTA):
AF2094: QGHMDLICMYVFKGEESFGE SIDVYGDYLIVKVGTEFLAV PKKSIKSVEDGRIVIGEFDE EEARELGRKWLEEKSKPVTL EELKSYGFGEEGEGS

Data typeCount
13C chemical shifts391
15N chemical shifts91
1H chemical shifts640

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AF20941

Entities:

Entity 1, AF2094 95 residues - 10726.126 Da.

1   GLNGLYHISMETASPLEUILECYSMETTYR
2   VALPHELYSGLYGLUGLUSERPHEGLYGLU
3   SERILEASPVALTYRGLYASPTYRLEUILE
4   VALLYSVALGLYTHRGLUPHELEUALAVAL
5   PROLYSLYSSERILELYSSERVALGLUASP
6   GLYARGILEVALILEGLYGLUPHEASPGLU
7   GLUGLUALAARGGLULEUGLYARGLYSTRP
8   LEUGLUGLULYSSERLYSPROVALTHRLEU
9   GLUGLULEULYSSERTYRGLYPHEGLYGLU
10   GLUGLYGLUGLYSER

Samples:

sample_1: af2094 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_aromatic NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

PSVS, Bhattacharya and Montelione - structure validation

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAB89165 AIG99081
REF WP_010879585
SP O28186
AlphaFold O28186

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