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 11470

Title: NMR chemical shift assignments for the cytoplasmic region of the Mg2+-transporter MgtE in the Mg2+ unbound state   PubMed: 22477092

Deposition date: 2012-01-12 Original release date: 2019-08-30

Authors: Maruyama, Tatsuro; Imai, Shunsuke; Osawa, Masanori; Shimada, Ichio

Citation: Maruyama, Tatsuro; Imai, Shunsuke; Osawa, Masanori; Hattori, Motoyuki; Ishitani, Ryuichi; Nureki, Osamu; Shimada, Ichio. "Backbone resonance assignments for the cytoplasmic region of the Mg(2+) transporter MgtE in the Mg (2+)-unbound state"  Biomol. NMR Assign. 7, 93-96 (2013).

Assembly members:
MgtECP_dimer, polymer, 263 residues, Formula weight is not available

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
MgtECP_dimer: GPLHMEEKLAVSLQEALQEG DTRALREVLEEIHPQDLLAL WDELKGEHRYVVLTLLPKAK AAEVLSHLSPEEQAEYLKTL PPWRLREILEELSLDDLADA LQAVRKEDPAYFQRLKDLLD PRTRAEVEALARYEEDEAGG LMTPEYVAVREGMTVEEVLR FLRRAAPDAETIYYIYVVDE KGRLKGVLSLRDLIVADPRT RVAEIMNPKVVYVRTDTDQE EVARLMADYDFTVLPVVDEE GRLVGIVTVDDVLDVLEAEA TED

Data sets:
Data typeCount
13C chemical shifts602
15N chemical shifts205
1H chemical shifts205

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1The cytoplasmic region of MgtE, chain 11
2The cytoplasmic region of MgtE, chain 21

Entities:

Entity 1, The cytoplasmic region of MgtE, chain 1 263 residues - Formula weight is not available

1   GLYPROLEUHISMETGLUGLULYSLEUALA
2   VALSERLEUGLNGLUALALEUGLNGLUGLY
3   ASPTHRARGALALEUARGGLUVALLEUGLU
4   GLUILEHISPROGLNASPLEULEUALALEU
5   TRPASPGLULEULYSGLYGLUHISARGTYR
6   VALVALLEUTHRLEULEUPROLYSALALYS
7   ALAALAGLUVALLEUSERHISLEUSERPRO
8   GLUGLUGLNALAGLUTYRLEULYSTHRLEU
9   PROPROTRPARGLEUARGGLUILELEUGLU
10   GLULEUSERLEUASPASPLEUALAASPALA
11   LEUGLNALAVALARGLYSGLUASPPROALA
12   TYRPHEGLNARGLEULYSASPLEULEUASP
13   PROARGTHRARGALAGLUVALGLUALALEU
14   ALAARGTYRGLUGLUASPGLUALAGLYGLY
15   LEUMETTHRPROGLUTYRVALALAVALARG
16   GLUGLYMETTHRVALGLUGLUVALLEUARG
17   PHELEUARGARGALAALAPROASPALAGLU
18   THRILETYRTYRILETYRVALVALASPGLU
19   LYSGLYARGLEULYSGLYVALLEUSERLEU
20   ARGASPLEUILEVALALAASPPROARGTHR
21   ARGVALALAGLUILEMETASNPROLYSVAL
22   VALTYRVALARGTHRASPTHRASPGLNGLU
23   GLUVALALAARGLEUMETALAASPTYRASP
24   PHETHRVALLEUPROVALVALASPGLUGLU
25   GLYARGLEUVALGLYILEVALTHRVALASP
26   ASPVALLEUASPVALLEUGLUALAGLUALA
27   THRGLUASP

Samples:

U-2H-13C-15N_MgtECP: MgtECP dimer, [U-13C; U-15N; U-2H], 570 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

U-2H-15N_MgtECP: MgtECP dimer, [U-2H; U-15N], 300 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

15N_Arg_MgtECP: MgtECP dimer, [U-15N]-Arg, 120 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

15N_Ile_MgtECP: MgtECP dimer, [U-15N]-Ile, 270 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

15N_His_MgtECP: MgtECP dimer, [U-15N]-His, 180 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

15N_Lys_MgtECP: MgtECP dimer, [U-15N]-Lys, 120 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

U-15N_1-13C_Pro_MgtECP: MgtECP dimer, [U-15N]; [1-13C]-Pro, 170 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

U-15N_1-13C_Gly_MgtECP: MgtECP dimer, [U-15N]; [1-13C]-Gly, 380 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

U-15N_1-13C_Leu_MgtECP: MgtECP dimer, [U-15N]; [1-13C]-Leu, 570 uM; HEPES 20 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.10; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHNCAU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHNCACBU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHNCOU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHN(CO)CAU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHN(CO)CACBU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D trHNCACOU-2H-13C-15N_MgtECPisotropicsample_conditions_1
3D 15N-edited NOESY-TROSYU-2H-15N_MgtECPisotropicsample_conditions_1
2D 1H-15N HSQC15N_Arg_MgtECPisotropicsample_conditions_1
2D 1H-15N HSQC15N_Ile_MgtECPisotropicsample_conditions_1
2D 1H-15N HSQC15N_His_MgtECPisotropicsample_conditions_1
2D 1H-15N HSQC15N_Lys_MgtECPisotropicsample_conditions_1
2D HNCO (1H-15N plane)U-15N_1-13C_Pro_MgtECPisotropicsample_conditions_1
2D HNCO (1H-15N plane)U-15N_1-13C_Gly_MgtECPisotropicsample_conditions_1
2D HNCO (1H-15N plane)U-15N_1-13C_Leu_MgtECPisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

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

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