BMRB Entry 26989

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26989

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for fluoroacetate dehalogenase from Rhodopseudomonas palustris
Deposition date:
2017-01-04
Original release date:
2021-07-22
Authors:
Kim, Tae Hun; Prosser, R Scott; Mehrabi, Pedram; Ren, Zhong; Ing, Christopher; Bezginov, Alexandr; Ye, Libin; Pom s, R gis; Pai, Emil
Citation:

Citation: Kim, Tae Hun; Mehrabi, Pedram; Ren, Zhong; Sljoka, Adnan; Ing, Christopher; Bezginov, Alexandr; Ye, Libin; Pomes, Regis; Prosser, R Scott; Pai, Emil. "The role of dimer asymmetry and protomer dynamics in enzyme catalysis"  Science 355, .-. (2017).
PubMed: 28104837

Assembly members:

Assembly members:
Fluoroacetate_dehalogenase, polymer, 306 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rhodopseudomonas palustris   Taxonomy ID: 1076   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustris

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Rhodopseudomonas palustris   Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fluoroacetate_dehalogenase: GHMPDLADLFPGFGSEWINT SSGRIFARVGGDGPPLLLLH GFPQTHVMWHRVAPKLAERF KVIVADLPGYGWSDMPESDE QHTPYTKRAMAKQLIEAMEQ LGHVHFALAGHNRGARVSYR LALDSPGRLSKLAVLDILPT YEYWQRMNRAYALKIYHWSF LAQPAPLPENLLGGDPDFYV KAKLASWTRAGDLSAFDPRA VEHYRIAFADPMRRHVMCED YRAGAYADFEHDKIDVEAGN KIPVPMLALWGASGIAQSAA TPLDVWRKWASDVQGAPIES GHFLPEEAPDQTAEALVRFF SAAPGS

Data sets:
Data typeCount
13C chemical shifts568
15N chemical shifts219
1H chemical shifts219

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Protomer 11

Entities:

Entity 1, Protomer 1 306 residues - Formula weight is not available

1   GLYHISMETPROASPLEUALAASPLEUPHE
2   PROGLYPHEGLYSERGLUTRPILEASNTHR
3   SERSERGLYARGILEPHEALAARGVALGLY
4   GLYASPGLYPROPROLEULEULEULEUHIS
5   GLYPHEPROGLNTHRHISVALMETTRPHIS
6   ARGVALALAPROLYSLEUALAGLUARGPHE
7   LYSVALILEVALALAASPLEUPROGLYTYR
8   GLYTRPSERASPMETPROGLUSERASPGLU
9   GLNHISTHRPROTYRTHRLYSARGALAMET
10   ALALYSGLNLEUILEGLUALAMETGLUGLN
11   LEUGLYHISVALHISPHEALALEUALAGLY
12   HISASNARGGLYALAARGVALSERTYRARG
13   LEUALALEUASPSERPROGLYARGLEUSER
14   LYSLEUALAVALLEUASPILELEUPROTHR
15   TYRGLUTYRTRPGLNARGMETASNARGALA
16   TYRALALEULYSILETYRHISTRPSERPHE
17   LEUALAGLNPROALAPROLEUPROGLUASN
18   LEULEUGLYGLYASPPROASPPHETYRVAL
19   LYSALALYSLEUALASERTRPTHRARGALA
20   GLYASPLEUSERALAPHEASPPROARGALA
21   VALGLUHISTYRARGILEALAPHEALAASP
22   PROMETARGARGHISVALMETCYSGLUASP
23   TYRARGALAGLYALATYRALAASPPHEGLU
24   HISASPLYSILEASPVALGLUALAGLYASN
25   LYSILEPROVALPROMETLEUALALEUTRP
26   GLYALASERGLYILEALAGLNSERALAALA
27   THRPROLEUASPVALTRPARGLYSTRPALA
28   SERASPVALGLNGLYALAPROILEGLUSER
29   GLYHISPHELEUPROGLUGLUALAPROASP
30   GLNTHRALAGLUALALEUVALARGPHEPHE
31   SERALAALAPROGLYSER

Samples:

sample_1: Fluoroacetate dehalogenase, [U-100% 13C; U-100% 15N; U-80% 2H], 2.5 mM

sample_conditions_1: ionic strength: 0 mM; pH: 8.5; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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