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 15264

Title: Complete backbone 15N, 13C, and 1H resonance assignments for the N-terminal domain of AhpF   PubMed: 17919953

Authors: Benison, Gregory; Barbar, Elisar; Horita, David

Citation: Benison, Gregory; Berkholz, Donald; Barbar, Elisar. "Protein assignments without peak lists using higher-order spectra"  J. Magn. Reson. 189, 173-181 (2007).

Assembly members:
ahpfn, polymer, 202 residues, Formula weight is not available

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 602   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

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

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

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts191
1H chemical shifts191

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ahpfn1

Entities:

Entity 1, ahpfn 202 residues - Formula weight is not available

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: ahpfn, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; potassium phosphate 50 mM; potassium chloride 50 mM; DSS 1 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

Burrow-Owl v1.2, Greg Benison; Barbar Lab - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16265
PDB
DBJ BAA02486 BAH62352 BAJ35614 BAP06377 GAL49470
EMBL CAD05085 CAR32166 CAR36509 CAR60178 CBG23683
GB AAA16432 AAL19560 AAO69861 AAV78017 AAX64546
PIR AC0577
REF NP_455185 NP_459601 WP_000886405 WP_000887631 WP_000887632
SP P19480