BMRB Entry 18031

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18031

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the ribosoaml assembly factor Fap7 from Pyrococcus horikoshii in its AP5A bound form
Deposition date:
2011-10-31
Original release date:
2012-11-09
Authors:
Hellmich, Ute; Duchardt-Ferner, Elke; Woehnert, Jens
Citation:

Citation: Hellmich, Ute; Duchardt-Ferner, Elke; Woehnert, Jens. "1H, 15N, 13C Assigned Backbone Chemical Shifts for Fap7 in the AP5A-bound form"  Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
Fap7, polymer, 180 residues, 20178.1 Da.
AP5, non-polymer, 916.367 Da.

Natural source:

Natural source:   Common Name: Pyrococcus horikoshii   Taxonomy ID: 53953   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus horikoshii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fap7: MLIAITGTPGVGKTTVAKLL AKKLNYEYVSLKDFALEKGC GRRVNDEVEVEIDELAYFIE RELKGKNAVLDGHLSHLMPV DLVVVLRAHPKLIGERLRER GYDREKIGENVEAELVDAVL IEAIEEHENVIEVDTTNKSP EDVVEEIVSLINSGIKKRVG IVDWSEVYDEIIPYLRLGGE

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts155
1H chemical shifts155

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fap71
2AP5A2

Entities:

Entity 1, Fap7 180 residues - 20178.1 Da.

1   METLEUILEALAILETHRGLYTHRPROGLY
2   VALGLYLYSTHRTHRVALALALYSLEULEU
3   ALALYSLYSLEUASNTYRGLUTYRVALSER
4   LEULYSASPPHEALALEUGLULYSGLYCYS
5   GLYARGARGVALASNASPGLUVALGLUVAL
6   GLUILEASPGLULEUALATYRPHEILEGLU
7   ARGGLULEULYSGLYLYSASNALAVALLEU
8   ASPGLYHISLEUSERHISLEUMETPROVAL
9   ASPLEUVALVALVALLEUARGALAHISPRO
10   LYSLEUILEGLYGLUARGLEUARGGLUARG
11   GLYTYRASPARGGLULYSILEGLYGLUASN
12   VALGLUALAGLULEUVALASPALAVALLEU
13   ILEGLUALAILEGLUGLUHISGLUASNVAL
14   ILEGLUVALASPTHRTHRASNLYSSERPRO
15   GLUASPVALVALGLUGLUILEVALSERLEU
16   ILEASNSERGLYILELYSLYSARGVALGLY
17   ILEVALASPTRPSERGLUVALTYRASPGLU
18   ILEILEPROTYRLEUARGLEUGLYGLYGLU

Entity 2, AP5A - C20 H29 N10 O22 P5 - 916.367 Da.

1   AP5

Samples:

sample_1: Fap7, [U-100% 13C; U-100% 15N; U-80% 2H], 250 uM; BisTris 50 mM; NaCl 50 mM; H2O 90%; D2O 10%; AP5A 2.5 mM

sample_2: Fap7, [U-100% 13C-Pro; U-100% 15N-Lys], 250 uM; BisTris 50 mM; NaCl 50 mM; H2O 90%; D2O 10%; AP5A 2.5 mM

sample_3: Fap7, [U-100% 13C-Pro; U-100% 15N-Tyr], 250 uM; BisTris 50 mM; NaCl 50 mM; H2O 90%; D2O 10%; AP5A 2.5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, BRUKER - collection, processing

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

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz

Related Database Links:

DBJ BAA30356
REF WP_010885344
SP O58998
AlphaFold O58998

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