BMRB Entry 50595

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50595

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Title:
Backbone and aliphatic side chain of Gamma mini-lid R133A
Deposition date:
2020-11-26
Original release date:
2021-06-30
Authors:
Mahdi, Sam; Bezsonova, Irina; Beuning, Penny; Korzhnev, Dmitry
Citation:

Citation: Mahdi, Sam; Bezsonova, Irina; Beuning, Penny; Korzhnev, Dmitry. "NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex Gamma subunit"  Biomol. NMR Assign. 15, 281-285 (2021).
PubMed: 33761093

Assembly members:

Assembly members:
entity_1, polymer, 243 residues, 26764.61 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMSYQVLARKWRPQTFADVV GQEHVLTALANGLSLGRIHH AYLFSGTRGVGKTSIARLLA KGLNCETGITATPCGVCDNC REIEQGRFVDLIEIDAASRT KVEDTRDLLDNVQYAPARGR FKVYLIDEVHMLSAHSFNAL LKTLEEPPEHVKFLLATTDP QKLPVTILSRCLQFHLKALD VEQIRHQLEHILNEEHIAHE PRALQLLARAAEGSLRDALS LTDQAIASGDGQVSTQAVSA MLG

Data typeCount
13C chemical shifts870
15N chemical shifts214
1H chemical shifts1156

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Gamma Mini-Lid R133A1

Entities:

Entity 1, Gamma Mini-Lid R133A 243 residues - 26764.61 Da.

Sequence is mutated form of Wild Type (R133A)

1   SERMETSERTYRGLNVALLEUALAARGLYS
2   TRPARGPROGLNTHRPHEALAASPVALVAL
3   GLYGLNGLUHISVALLEUTHRALALEUALA
4   ASNGLYLEUSERLEUGLYARGILEHISHIS
5   ALATYRLEUPHESERGLYTHRARGGLYVAL
6   GLYLYSTHRSERILEALAARGLEULEUALA
7   LYSGLYLEUASNCYSGLUTHRGLYILETHR
8   ALATHRPROCYSGLYVALCYSASPASNCYS
9   ARGGLUILEGLUGLNGLYARGPHEVALASP
10   LEUILEGLUILEASPALAALASERARGTHR
11   LYSVALGLUASPTHRARGASPLEULEUASP
12   ASNVALGLNTYRALAPROALAARGGLYARG
13   PHELYSVALTYRLEUILEASPGLUVALHIS
14   METLEUSERALAHISSERPHEASNALALEU
15   LEULYSTHRLEUGLUGLUPROPROGLUHIS
16   VALLYSPHELEULEUALATHRTHRASPPRO
17   GLNLYSLEUPROVALTHRILELEUSERARG
18   CYSLEUGLNPHEHISLEULYSALALEUASP
19   VALGLUGLNILEARGHISGLNLEUGLUHIS
20   ILELEUASNGLUGLUHISILEALAHISGLU
21   PROARGALALEUGLNLEULEUALAARGALA
22   ALAGLUGLYSERLEUARGASPALALEUSER
23   LEUTHRASPGLNALAILEALASERGLYASP
24   GLYGLNVALSERTHRGLNALAVALSERALA
25   METLEUGLY

Samples:

sample_1: Gamma Mini-Lid R133A, [U-100% 13C; U-100% 15N], 0.6 mM; PO4 50 mM; NaCl 100 mM; DTT 10 mM; NaN3 2 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis

TALOS-N - data analysis

NMR spectrometers:

  • Varian VNMRS 800 MHz

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