BMRB Entry 34698

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34698
MolProbity Validation Chart

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Title:
Regulatory domain dimer of tryptophan hydroxylase 2 in complex with L-Phe
Deposition date:
2022-01-11
Original release date:
2023-04-25
Authors:
Vedel, I.; Prestel, A.; Harris, P.; Peters, G.; Kragelund, B.
Citation:

Citation: Vedel, I.; Prestel, A.; Zhang, Z.; Skawinska, N.; Stark, H.; Harris, P.; Kragelund, B.; Peters, G.. "L-Phe is implicated in serotonin biosynthesis: Overrules L-Trp as the superior allosteric regulator of human tryptophan hydroxylase 2"  .

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, 11283.862 Da.
entity_PHE, non-polymer, 165.189 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGNKGSSKREAATESGKTA VVFSLKNEVGGLVKALRLFQ EKRVNMVHIESRKSRRRSSE VEIFVDCECGKTEFNELIQL LKFQTTIVTLNPPENIWTEE

Data typeCount
13C chemical shifts341
15N chemical shifts75
1H chemical shifts487

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_32
4unit_42

Entities:

Entity 1, unit_1 100 residues - 11283.862 Da.

1   GLYPROGLYASNLYSGLYSERSERLYSARG
2   GLUALAALATHRGLUSERGLYLYSTHRALA
3   VALVALPHESERLEULYSASNGLUVALGLY
4   GLYLEUVALLYSALALEUARGLEUPHEGLN
5   GLULYSARGVALASNMETVALHISILEGLU
6   SERARGLYSSERARGARGARGSERSERGLU
7   VALGLUILEPHEVALASPCYSGLUCYSGLY
8   LYSTHRGLUPHEASNGLULEUILEGLNLEU
9   LEULYSPHEGLNTHRTHRILEVALTHRLEU
10   ASNPROPROGLUASNILETRPTHRGLUGLU

Entity 2, unit_3 - C9 H11 N O2 - 165.189 Da.

1   PHE

Samples:

sample_1: Tryptophan hydroxylase 2 (GP+ 48 to 145), [U-99% 13C; U-99% 15N], 1.1 mM; L-Phe, none, 10 mM; sodium phosphate, none, 20 mM; ammonium sulfate, none, 100 mM; DSS, none, 125 uM

sample_2: Tryptophan hydroxylase 2 (GP+ 48 to 145), none, 0.45 mM; L-Phe, [U-13C; U-15N], 2.6 mM; sodium phosphate, none, 20 mM; ammonium sulfate, none, 100 mM; DSS, none, 125 uM

sample_conditions_1: ionic strength: 0.344 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic 13C/15N filteredsample_1isotropicsample_conditions_1
3D 1H-15N NOESY 13C/15N filteredsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic amino acid specificsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.44, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA v3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin v3.5, Bruker Biospin - processing

qMDD, Kazimierczuk, Orekhov - processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 750 MHz
  • Bruker AVANCE III 600 MHz

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