BMRB Entry 27470

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27470

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Title:
1H, 15N, 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2 in complex with 1,4,5,6-tetrahydro-NAD
Deposition date:
2018-05-02
Original release date:
2019-05-22
Authors:
Iorgu, Andreea; Baxter, Nicola
Citation:

Citation: Iorgu, Andreea; Baxter, Nicola; Cliff, Matthew; Levy, Colin; Waltho, Jonathan; Hay, Sam; Scrutton, Nigel. "Nonequivalence of Second Sphere "Noncatalytic" Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes"  ACS Catal. 8, 11589-11599 (2018).

Assembly members:

Assembly members:
PETNR, polymer, 364 residues, 39358.13 Da.
entity_FMN, non-polymer, 456.344 Da.

Natural source:

Natural source:   Common Name: Enterobacter cloacae   Taxonomy ID: 550   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterobacter cloacae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBlueScript II SK(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PETNR: SAEKLFTPLKVGAVTAPNRV FMAPLTRLRSIEPGDIPTPL MGEYYRQRASAGLIISEATQ ISAQAKGYAGAPGLHSPEQI AAWKKITAGVHAEDGRIAVQ LWHTGRISHSSIQPGGQAPV SASALNANTRTSLRDENGNA IRVDTTTPRALELDEIPGIV NDFRQAVANAREAGFDLVEL HSAHGYLLHQFLSPSSNQRT DQYGGSVENRARLVLEVVDA VCNEWSADRIGIRVSPIGTF QNVDNGPNEEADALYLIEEL AKRGIAYLHMSETDLAGGKP YSEAFRQKVRERFHGVIIGA GAYTAEKAEDLIGKGLIDAV AFGRDYIANPDLVARLQKKA ELNPQRPESFYGGGAEGYTD YPSL

Data sets:
Data typeCount
13C chemical shifts1029
15N chemical shifts334
1H chemical shifts334

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PETNR1
2FMN2

Entities:

Entity 1, PETNR 364 residues - 39358.13 Da.

1   SERALAGLULYSLEUPHETHRPROLEULYS
2   VALGLYALAVALTHRALAPROASNARGVAL
3   PHEMETALAPROLEUTHRARGLEUARGSER
4   ILEGLUPROGLYASPILEPROTHRPROLEU
5   METGLYGLUTYRTYRARGGLNARGALASER
6   ALAGLYLEUILEILESERGLUALATHRGLN
7   ILESERALAGLNALALYSGLYTYRALAGLY
8   ALAPROGLYLEUHISSERPROGLUGLNILE
9   ALAALATRPLYSLYSILETHRALAGLYVAL
10   HISALAGLUASPGLYARGILEALAVALGLN
11   LEUTRPHISTHRGLYARGILESERHISSER
12   SERILEGLNPROGLYGLYGLNALAPROVAL
13   SERALASERALALEUASNALAASNTHRARG
14   THRSERLEUARGASPGLUASNGLYASNALA
15   ILEARGVALASPTHRTHRTHRPROARGALA
16   LEUGLULEUASPGLUILEPROGLYILEVAL
17   ASNASPPHEARGGLNALAVALALAASNALA
18   ARGGLUALAGLYPHEASPLEUVALGLULEU
19   HISSERALAHISGLYTYRLEULEUHISGLN
20   PHELEUSERPROSERSERASNGLNARGTHR
21   ASPGLNTYRGLYGLYSERVALGLUASNARG
22   ALAARGLEUVALLEUGLUVALVALASPALA
23   VALCYSASNGLUTRPSERALAASPARGILE
24   GLYILEARGVALSERPROILEGLYTHRPHE
25   GLNASNVALASPASNGLYPROASNGLUGLU
26   ALAASPALALEUTYRLEUILEGLUGLULEU
27   ALALYSARGGLYILEALATYRLEUHISMET
28   SERGLUTHRASPLEUALAGLYGLYLYSPRO
29   TYRSERGLUALAPHEARGGLNLYSVALARG
30   GLUARGPHEHISGLYVALILEILEGLYALA
31   GLYALATYRTHRALAGLULYSALAGLUASP
32   LEUILEGLYLYSGLYLEUILEASPALAVAL
33   ALAPHEGLYARGASPTYRILEALAASNPRO
34   ASPLEUVALALAARGLEUGLNLYSLYSALA
35   GLULEUASNPROGLNARGPROGLUSERPHE
36   TYRGLYGLYGLYALAGLUGLYTYRTHRASP
37   TYRPROSERLEU

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

1   FMN

Samples:

sample_1: PETNR:FMNox, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; potassium phosphate 50 mM; sodium azide 1 mM; TSP, [U-2H], 0.5 % v/v; D2O, [U-100% 2H], 10 % v/v; H2O 90 % v/v; NADH4 10 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

PDB
BMRB 27224

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