BMRB Entry 6695

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6695

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Title:
Backbone 1H, 13C and 15N Chemical Shift Assignments for Ferredoxin-NADP+ Reductase
Deposition date:
2005-06-20
Original release date:
2005-11-10
Authors:
Maeda, Masahiro; Young-Ho, Lee; Ikegami, Takahisa; Tamura, Kohsuke; Hoshino, Masaru; Yamazaki, Toshio; Nakayama, Masato; Hase, Toshiharu; Goto, Yuji
Citation:

Citation: Masahiro, Maeda; Young-Ho, Lee; Ikegami, Takahisa; Tamura, Kohsuke; Hoshino, Masaru; Yamazaki, Toshio; Nakayama, Masato; Hase, Toshiharu; Goto, Yuji. "Identification of the N- and C-Terminal Substrate Binding Segments of Ferredoxin-NADP+ Reductase by NMR"  Biochemistry 44, 10644-10653 (2005).
PubMed: 16060673

Assembly members:

Assembly members:
polypeptide, polymer, 314 residues, 35249 Da.
FAD, non-polymer, 785.550 Da.

Natural source:

Natural source:   Common Name: maize (corn)   Taxonomy ID: 4577   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Zea mays

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
polypeptide: IRAQASAVEAPATAKAKKES KKQEEGVVTNLYKPKEPYVG RCLLNTKITGDDAPGETWHM VFSTEGKIPYREGQSIGVIA DGVDKNGKPHKVRLYSIASS AIGDFGDSKTVSLCVKRLIY TNDAGEIVKGVCSNFLCDLQ PGDNVQITGPVGKEMLMPKD PNATIIMLATGTGIAPFRSF LWKMFFEKHDDYKFNGLGWL FLGVPTSSSLLYKEEFGKMK ERAPENFRVDYAVSREQTNA AGERMYIQTRMAEYKEELWE LLKKDNTYVYMCGLKGMEKG IDDIMVSLAEKDGIDWFDYK KQLKRGDQWNVEVY

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts878
15N chemical shifts285
1H chemical shifts285

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1polypeptide1
2FAD2

Entities:

Entity 1, polypeptide 314 residues - 35249 Da.

1   ILEARGALAGLNALASERALAVALGLUALA
2   PROALATHRALALYSALALYSLYSGLUSER
3   LYSLYSGLNGLUGLUGLYVALVALTHRASN
4   LEUTYRLYSPROLYSGLUPROTYRVALGLY
5   ARGCYSLEULEUASNTHRLYSILETHRGLY
6   ASPASPALAPROGLYGLUTHRTRPHISMET
7   VALPHESERTHRGLUGLYLYSILEPROTYR
8   ARGGLUGLYGLNSERILEGLYVALILEALA
9   ASPGLYVALASPLYSASNGLYLYSPROHIS
10   LYSVALARGLEUTYRSERILEALASERSER
11   ALAILEGLYASPPHEGLYASPSERLYSTHR
12   VALSERLEUCYSVALLYSARGLEUILETYR
13   THRASNASPALAGLYGLUILEVALLYSGLY
14   VALCYSSERASNPHELEUCYSASPLEUGLN
15   PROGLYASPASNVALGLNILETHRGLYPRO
16   VALGLYLYSGLUMETLEUMETPROLYSASP
17   PROASNALATHRILEILEMETLEUALATHR
18   GLYTHRGLYILEALAPROPHEARGSERPHE
19   LEUTRPLYSMETPHEPHEGLULYSHISASP
20   ASPTYRLYSPHEASNGLYLEUGLYTRPLEU
21   PHELEUGLYVALPROTHRSERSERSERLEU
22   LEUTYRLYSGLUGLUPHEGLYLYSMETLYS
23   GLUARGALAPROGLUASNPHEARGVALASP
24   TYRALAVALSERARGGLUGLNTHRASNALA
25   ALAGLYGLUARGMETTYRILEGLNTHRARG
26   METALAGLUTYRLYSGLUGLULEUTRPGLU
27   LEULEULYSLYSASPASNTHRTYRVALTYR
28   METCYSGLYLEULYSGLYMETGLULYSGLY
29   ILEASPASPILEMETVALSERLEUALAGLU
30   LYSASPGLYILEASPTRPPHEASPTYRLYS
31   LYSGLNLEULYSARGGLYASPGLNTRPASN
32   VALGLUVALTYR

Entity 2, FAD - C27 H33 N9 O15 P2 - 785.550 Da.

1   FAD

Samples:

buffer: polypeptide, [U-95% 13C; U-98% 15N; U-80% 2H], 0.4 mM; FAD 0.4 mM; Sodium perchlorate 50 mM; Na Phosphate 25 mM

condition_1: pH: 6.5; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCbuffernot availablecondition_1
TROSY-1H-15N HSQCbuffernot availablecondition_1
TROSY-HNCObuffernot availablecondition_1
TROSY-HN(CA)CObuffernot availablecondition_1
TROSY-HNCACBbuffernot availablecondition_1
TROSY-HN(CO)CACBbuffernot availablecondition_1
CBCANHbuffernot availablecondition_1

Software:

X-WINNMR -

NMRPipe -

PIPP -

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAA88236
GB ACG31602 ACL53609 AFW86197
REF NP_001105568 XP_008659023

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