BMRB Entry 27305

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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/BMR27305
MolProbity Validation Chart

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Title:
Chemical Shift Assignments of Retinal Degeneration 3 Protein (RD3)
Deposition date:
2017-11-07
Original release date:
2018-01-22
Authors:
Ames, James; Lim, Sunghyuk
Citation:

Citation: Lim, Sunghyuk; Cudia, Diana; Peshenko, Igor; Dizhoor, Alexander; Ames, James. "Chemical shift assignments of retinal degeneration 3 protein (RD3)"  Biomol. NMR Assignments 12, 167-170 (2018).
PubMed: 29327102

Assembly members:

Assembly members:
RD3, polymer, 143 residues, Formula weight is not available

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: pET-11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RD3: ARSPAEMVLETLMMELTGQM REAERQQRERSNAVRKVCTG VDYSWLASTPDSTYDLSPIE RLQLEDVCVKIHPSYCGPAI LRFRQLLAEQEPEVQEVSQL FRSVLQEVLERMKQEEEAHK LTRQWSLRPRGSLATFETEA EID

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts142
1H chemical shifts909

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RD3 monomer1

Entities:

Entity 1, RD3 monomer 143 residues - Formula weight is not available

1   ALAARGSERPROALAGLUMETVALLEUGLU
2   THRLEUMETMETGLULEUTHRGLYGLNMET
3   ARGGLUALAGLUARGGLNGLNARGGLUARG
4   SERASNALAVALARGLYSVALCYSTHRGLY
5   VALASPTYRSERTRPLEUALASERTHRPRO
6   ASPSERTHRTYRASPLEUSERPROILEGLU
7   ARGLEUGLNLEUGLUASPVALCYSVALLYS
8   ILEHISPROSERTYRCYSGLYPROALAILE
9   LEUARGPHEARGGLNLEULEUALAGLUGLN
10   GLUPROGLUVALGLNGLUVALSERGLNLEU
11   PHEARGSERVALLEUGLNGLUVALLEUGLU
12   ARGMETLYSGLNGLUGLUGLUALAHISLYS
13   LEUTHRARGGLNTRPSERLEUARGPROARG
14   GLYSERLEUALATHRPHEGLUTHRGLUALA
15   GLUILEASP

Samples:

sample_2: TRIS, [U-99% 2H], 5 mM; DTT, [U-99% 2H], 3 mM; sodium azide 0.04 % w/v; EDTA, [U-99% 2H], 50 uM; RD3, [U-99% 13C; U-99% 15N], 0.9 mM

sample_1: TRIS, [U-99% 2H], 5 mM; DTT, [U-99% 2H], 3 mM; sodium azide 0.04 % w/v; EDTA, [U-99% 2H], 50 uM; RD3, [U-99% 15N], 0.9 mM

sample_conditions_1: ionic strength: 4 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D H(CC)(CO)NHsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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