BMRB Entry 34173

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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/BMR34173
MolProbity Validation Chart

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Title:
NMR solution structure of the external DII domain of Rvb2 from Saccharomyces cerevisiae
Deposition date:
2017-08-24
Original release date:
2018-03-23
Authors:
Rouillon, C.; Bragantini, B.; Charpentier, B.; Manival, X.; Quinternet, M.
Citation:

Citation: Bragantini, B.; Rouillon, C.; Charpentier, B.; Manival, X.; Quinternet, M.. "Structural and interaction analysis of the external DII domains of the yeast AAA+ ATPases Rvb1 and Rvb2"  Biomol NMR Assign 12, 243-247 (2018).
PubMed: 29569106

Assembly members:

Assembly members:
entity_1, polymer, 107 residues, 11845.531 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMETELIEGEVVEIQIDR SITGGHKQGKLTIKTTDMET IYELGNKMIDGLTKEKVLAG DVISIDKASGKITKLGRSFA RSRDYDAMGADTRFVQCPEG ELQKRKT

Data sets:
Data typeCount
13C chemical shifts459
15N chemical shifts109
1H chemical shifts755

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 107 residues - 11845.531 Da.

1   GLYPROHISMETGLUTHRGLULEUILEGLU
2   GLYGLUVALVALGLUILEGLNILEASPARG
3   SERILETHRGLYGLYHISLYSGLNGLYLYS
4   LEUTHRILELYSTHRTHRASPMETGLUTHR
5   ILETYRGLULEUGLYASNLYSMETILEASP
6   GLYLEUTHRLYSGLULYSVALLEUALAGLY
7   ASPVALILESERILEASPLYSALASERGLY
8   LYSILETHRLYSLEUGLYARGSERPHEALA
9   ARGSERARGASPTYRASPALAMETGLYALA
10   ASPTHRARGPHEVALGLNCYSPROGLUGLY
11   GLULEUGLNLYSARGLYSTHR

Samples:

sample_1: Rvb2DII, [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.2, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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