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 16265

Title: Complete backbone 15N, 13C and 1H resonance assignments for the oxidized form of the N-terminal domain of AhpF   PubMed: 19459661

Deposition date: 2009-04-27 Original release date: 2009-05-29

Authors: Hall, Andrea; Horita, David; Barbar, Elisar

Citation: Hall, Andrea; Parsonage, Derek; Horita, David; Karplus, P. Andrew; Poole, Leslie; Barbar, Elisar. "Redox Dependent Dynamics of a Dual Thioredoxin-Fold Protein: Evolution of Specialized Folds"  Biochemistry 48, 5984-5993 (2009).

Assembly members:
N-terminal_domain_of_AhpF, polymer, 202 residues, 44635.20 Da.

Natural source:   Common Name: not available   Taxonomy ID: 28901   Superkingdom: not available   Kingdom: Salmonella   Genus/species: typhimurium not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
N-terminal_domain_of_AhpF: MLDTNMKTQLRAYLEKLTKP VELIATLDDSAKSAEIKELL AEIAELSDKVTFKEDNTLPV RKPSFLITNPGSQQGPRFAG SPLGHEFTSLVLALLWTGGH PSKEAQSLLEQIRDIDGDFE FETYYSLSCHNCPDVVQALN LMAVLNPRIKHTAIDGGTFQ NEITERNVMGVPAVFVNGKE FGQGRMTLTEIVAKVDTGAE KR

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts188
1H chemical shifts188

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain1

Entities:

Entity 1, N-terminal domain 202 residues - 44635.20 Da.

The N-terminal domain contains residues 1 through 202 of the alkyl hydroperoxide subunit F (AhpF) protein. This construct has previously been referred to as AhpFn.

1   METLEUASPTHRASNMETLYSTHRGLNLEU
2   ARGALATYRLEUGLULYSLEUTHRLYSPRO
3   VALGLULEUILEALATHRLEUASPASPSER
4   ALALYSSERALAGLUILELYSGLULEULEU
5   ALAGLUILEALAGLULEUSERASPLYSVAL
6   THRPHELYSGLUASPASNTHRLEUPROVAL
7   ARGLYSPROSERPHELEUILETHRASNPRO
8   GLYSERGLNGLNGLYPROARGPHEALAGLY
9   SERPROLEUGLYHISGLUPHETHRSERLEU
10   VALLEUALALEULEUTRPTHRGLYGLYHIS
11   PROSERLYSGLUALAGLNSERLEULEUGLU
12   GLNILEARGASPILEASPGLYASPPHEGLU
13   PHEGLUTHRTYRTYRSERLEUSERCYSHIS
14   ASNCYSPROASPVALVALGLNALALEUASN
15   LEUMETALAVALLEUASNPROARGILELYS
16   HISTHRALAILEASPGLYGLYTHRPHEGLN
17   ASNGLUILETHRGLUARGASNVALMETGLY
18   VALPROALAVALPHEVALASNGLYLYSGLU
19   PHEGLYGLNGLYARGMETTHRLEUTHRGLU
20   ILEVALALALYSVALASPTHRGLYALAGLU
21   LYSARG

Samples:

sample_1: N-terminal domain of AhpF' '[U-100% 13C; U-100% 15N]; natural abundance; .; . mM; .; . 16265; .

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

Burrow_Owl, Greg Benison - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

GB AAA16432 AAL19560 AAO69861 AAV78017 AAX64546 AAA16432 AAL19560 AAO69861 AAV78017 AAX64546
PIR AC0577 AC0577
BMRB 15264
PDB
DBJ BAA02486 BAH62352 BAJ35614 BAP06377 GAL49470
EMBL CAD05085 CAR32166 CAR36509 CAR60178 CBG23683
REF NP_455185 NP_459601 WP_000886405 WP_000887631 WP_000887632
SP P19480

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