BMRB Entry 15788

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15788

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Title:
X-ray crystallographic and Solution State NMR Spectroscopic Investigations of NADP+ Binding to Ferredoxin-NADP Reductase (FPR) from Pseudomonas aeruginosa
Deposition date:
2008-05-29
Original release date:
2008-07-15
Authors:
Wang, An; Rivera, Mario
Citation:

Citation: Wang, An; Rodriguez, Juan Carlos; Han, Huijong; Schonbrunn, Ernst; Rivera, Mario. "X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP(+) Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa"  Biochemistry 47, 8080-8093 (2008).
PubMed: 18605699

Assembly members:

Assembly members:
Ferredoxin-NADP_Reductase_Polypeptide, polymer, 258 residues, Formula weight is not available
FAD, non-polymer, 785.550 Da.

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ferredoxin-NADP_Reductase_Polypeptide: MSNLYTERVLSVHHWNDTLF SFKTTRNPGLRFKTGQFVMI GLEVDGRPLMRAYSIASPNY EEHLEFFSIKVPDGPLTSRL QHLKEGDELMVSRKPTGTLV HDDLLPGKHLYLLSTGTGMA PFLSVIQDPETYERYEKVIL VHGVRWVSELAYADFITKVL PEHEYFGDQVKEKLIYYPLV TREPFRNQGRQTDLMRSGKL FEDIGLPPMNPQDDRAMICG SPSMLEETSAVLDSFGLKIS PRMGEPGDYLIERAFVEK

Data sets:
Data typeCount
13C chemical shifts682
15N chemical shifts223
1H chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2FAD cofactor2

Entities:

Entity 1, subunit 1 258 residues - Formula weight is not available

1   METSERASNLEUTYRTHRGLUARGVALLEU
2   SERVALHISHISTRPASNASPTHRLEUPHE
3   SERPHELYSTHRTHRARGASNPROGLYLEU
4   ARGPHELYSTHRGLYGLNPHEVALMETILE
5   GLYLEUGLUVALASPGLYARGPROLEUMET
6   ARGALATYRSERILEALASERPROASNTYR
7   GLUGLUHISLEUGLUPHEPHESERILELYS
8   VALPROASPGLYPROLEUTHRSERARGLEU
9   GLNHISLEULYSGLUGLYASPGLULEUMET
10   VALSERARGLYSPROTHRGLYTHRLEUVAL
11   HISASPASPLEULEUPROGLYLYSHISLEU
12   TYRLEULEUSERTHRGLYTHRGLYMETALA
13   PROPHELEUSERVALILEGLNASPPROGLU
14   THRTYRGLUARGTYRGLULYSVALILELEU
15   VALHISGLYVALARGTRPVALSERGLULEU
16   ALATYRALAASPPHEILETHRLYSVALLEU
17   PROGLUHISGLUTYRPHEGLYASPGLNVAL
18   LYSGLULYSLEUILETYRTYRPROLEUVAL
19   THRARGGLUPROPHEARGASNGLNGLYARG
20   GLNTHRASPLEUMETARGSERGLYLYSLEU
21   PHEGLUASPILEGLYLEUPROPROMETASN
22   PROGLNASPASPARGALAMETILECYSGLY
23   SERPROSERMETLEUGLUGLUTHRSERALA
24   VALLEUASPSERPHEGLYLEULYSILESER
25   PROARGMETGLYGLUPROGLYASPTYRLEU
26   ILEGLUARGALAPHEVALGLULYS

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

1   FAD

Samples:

2H_13C_15N_labeled_pa-FPR: labeled pa-FPR, [U-100% 13C; U-100% 15N; 80% 2H], 1.2 mM; sodium phosphate buffer pH7 50 mM

13C_15N_labeled_pa-FPR: labeled pa-FPR, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate buffer pH7 50 mM

15N_labeled_pa-FPR: labeled pa-FPR, [U-99% 15N], 1.2 mM; sodium phosphate buffer pH7 50 mM

selective_labeled_pa-FPR: labeled pa-FPR, [U-15N]-Leu, 1.2 mM; sodium phosphate buffer pH7 50 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_labeled_pa-FPRisotropicsample_conditions_1
3D HNCA13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D HNCO2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D HNCA2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D HNCACB2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D CBCA(CO)NH2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D HN(CO)CA2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1
3D (HCA)CO(CA)NH2H_13C_15N_labeled_pa-FPRisotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAK91356 BAP21977 BAP49607 BAQ38494 BAR66559
EMBL CAW26392 CCQ84255 CDH69932 CDH76013 CDI91808
GB AAG06785 ABJ12651 ABR86893 AEO74057 AFM63750
REF NP_252087 WP_003091832 WP_003124290 WP_003157318 WP_034031305

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