BMRB Entry 19301

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19301

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Title:
Redox-linked domain movements in the catalytic cycle of cytochrome P450 reductase
Deposition date:
2013-06-17
Original release date:
2014-02-13
Authors:
Huang, Wei-Cheng; Ellis, Jacqueline; Barsukov, Igor; Moody, Peter; Raven, Emma; Robert, Gordon
Citation:

Citation: Huang, Wei-Cheng; Ellis, Jacqueline; Moody, Peter; Raven, Emma; Roberts, Gordon. "Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase."  Structure 21, 1581-1589 (2013).
PubMed: 23911089

Assembly members:

Assembly members:
CPR, polymer, 614 residues, 70827.4 Da.
FLAVIN MONONUCLEOTIDE, non-polymer, 456.344 Da.
FLAVIN-ADENINE DINUCLEOTIDE, non-polymer, 785.550 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCS22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CPR: VRESSFVEKMKKTGRNIIVF YGSQTGTAEEFANRLSKDAH RYGMRGMSADPEEYDLADLS SLPEIDNALVVFCMATYGEG DPTDNAQDFYDWLQETDVDL SGVKFAVFGLGNKTYEHFNA MGKYVDKRLEQLGAQRIFEL GLGDDDGNLEEDFITWREQF WPAVCEHFGVEATGEESSIR QYELVVHTDIDAAKVYMGEM GRLKSYENQKPPFDAKNPFL AAVTTNRKLNQGTERHLMHL ELDISDSKIRYESGDHVAVY PANDSALVNQLGKILGADLD VVMSLNNLDEESNKKHPFPC PTSYRTALTYYLDITNPPRT NVLYELAQYASEPSEQELLR KMASSSGEGKELYLSWVVEA RRHILAILQDCPSLRPPIDH LCELLPRLQARYYSIASSSK VHPNSVHICAVVVEYETKAG RINKGVATNWLRAKEPAGEN GGRALVPMFVRKSQFRLPFK ATTPVIMVGPGTGVAPFIGF IQERAWLRQQGKEVGETLLY YGCRRSDEDYLYREELAQFH RDGALTQLNVAFSREQSHKV YVQHLLKQDREHLWKLIEGG AHIYVCGDARNMARDVQNTF YDIVAELGAMEHAQAVDYIK KLMTKGRYSLDVWS

Data sets:
Data typeCount
13C chemical shifts523
15N chemical shifts181
1H chemical shifts181

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CPR1
2FMN2
3FAD3

Entities:

Entity 1, CPR 614 residues - 70827.4 Da.

This is the cytoplasmic globular domain of a membrane human fibroblast CPR lacking the N-terminal 63 a.a. membrane-anchoring region.

1   VALARGGLUSERSERPHEVALGLULYSMET
2   LYSLYSTHRGLYARGASNILEILEVALPHE
3   TYRGLYSERGLNTHRGLYTHRALAGLUGLU
4   PHEALAASNARGLEUSERLYSASPALAHIS
5   ARGTYRGLYMETARGGLYMETSERALAASP
6   PROGLUGLUTYRASPLEUALAASPLEUSER
7   SERLEUPROGLUILEASPASNALALEUVAL
8   VALPHECYSMETALATHRTYRGLYGLUGLY
9   ASPPROTHRASPASNALAGLNASPPHETYR
10   ASPTRPLEUGLNGLUTHRASPVALASPLEU
11   SERGLYVALLYSPHEALAVALPHEGLYLEU
12   GLYASNLYSTHRTYRGLUHISPHEASNALA
13   METGLYLYSTYRVALASPLYSARGLEUGLU
14   GLNLEUGLYALAGLNARGILEPHEGLULEU
15   GLYLEUGLYASPASPASPGLYASNLEUGLU
16   GLUASPPHEILETHRTRPARGGLUGLNPHE
17   TRPPROALAVALCYSGLUHISPHEGLYVAL
18   GLUALATHRGLYGLUGLUSERSERILEARG
19   GLNTYRGLULEUVALVALHISTHRASPILE
20   ASPALAALALYSVALTYRMETGLYGLUMET
21   GLYARGLEULYSSERTYRGLUASNGLNLYS
22   PROPROPHEASPALALYSASNPROPHELEU
23   ALAALAVALTHRTHRASNARGLYSLEUASN
24   GLNGLYTHRGLUARGHISLEUMETHISLEU
25   GLULEUASPILESERASPSERLYSILEARG
26   TYRGLUSERGLYASPHISVALALAVALTYR
27   PROALAASNASPSERALALEUVALASNGLN
28   LEUGLYLYSILELEUGLYALAASPLEUASP
29   VALVALMETSERLEUASNASNLEUASPGLU
30   GLUSERASNLYSLYSHISPROPHEPROCYS
31   PROTHRSERTYRARGTHRALALEUTHRTYR
32   TYRLEUASPILETHRASNPROPROARGTHR
33   ASNVALLEUTYRGLULEUALAGLNTYRALA
34   SERGLUPROSERGLUGLNGLULEULEUARG
35   LYSMETALASERSERSERGLYGLUGLYLYS
36   GLULEUTYRLEUSERTRPVALVALGLUALA
37   ARGARGHISILELEUALAILELEUGLNASP
38   CYSPROSERLEUARGPROPROILEASPHIS
39   LEUCYSGLULEULEUPROARGLEUGLNALA
40   ARGTYRTYRSERILEALASERSERSERLYS
41   VALHISPROASNSERVALHISILECYSALA
42   VALVALVALGLUTYRGLUTHRLYSALAGLY
43   ARGILEASNLYSGLYVALALATHRASNTRP
44   LEUARGALALYSGLUPROALAGLYGLUASN
45   GLYGLYARGALALEUVALPROMETPHEVAL
46   ARGLYSSERGLNPHEARGLEUPROPHELYS
47   ALATHRTHRPROVALILEMETVALGLYPRO
48   GLYTHRGLYVALALAPROPHEILEGLYPHE
49   ILEGLNGLUARGALATRPLEUARGGLNGLN
50   GLYLYSGLUVALGLYGLUTHRLEULEUTYR
51   TYRGLYCYSARGARGSERASPGLUASPTYR
52   LEUTYRARGGLUGLULEUALAGLNPHEHIS
53   ARGASPGLYALALEUTHRGLNLEUASNVAL
54   ALAPHESERARGGLUGLNSERHISLYSVAL
55   TYRVALGLNHISLEULEULYSGLNASPARG
56   GLUHISLEUTRPLYSLEUILEGLUGLYGLY
57   ALAHISILETYRVALCYSGLYASPALAARG
58   ASNMETALAARGASPVALGLNASNTHRPHE
59   TYRASPILEVALALAGLULEUGLYALAMET
60   GLUHISALAGLNALAVALASPTYRILELYS
61   LYSLEUMETTHRLYSGLYARGTYRSERLEU
62   ASPVALTRPSER

Entity 2, FMN - C17 H21 N4 O9 P - 456.344 Da.

1   FMN

Entity 3, FAD - C27 H33 N9 O15 P2 - 785.550 Da.

1   FAD

Samples:

sample_1: NADPH-Cytochrome P450 reductase, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; FLAVIN MONONUCLEOTIDE, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; FLAVIN-ADENINE DINUCLEOTIDE, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; BES 30 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 12 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, CCPN - chemical shift assignment, collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UniProt P16435
PDB
DBJ BAB18572 BAD93111 BAE72975 BAF83218 BAG35442
EMBL CAH56151
GB AAB21814 AAD56649 AAF07050 AAF07052 AAF09458
REF NP_000932 NP_001248085 XP_001155755 XP_003276705 XP_003808966
SP P16435
AlphaFold Q9UDT3 P16435

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