BMRB Entry 50269

Title:
Fe+2-containing acireductone dioxygenase (Homo sapiens)
Deposition date:
2020-05-11
Original release date:
2020-11-13
Authors:
Pochapsky, Thomas; Deshpande, Aditi; Liu, Xinyue
Citation:

Citation: Liu, Xinyue; Garber, Abigail; Ryan, Julia; Deshpande, Aditi; Ringe, Dagmar; Pochapsky, Thomas. "Solution structure of human Fe(II)-bound acireductone dioxygenase and interactions with the regulatory domain of matrix metalloproteinase I (MMP-1)"  Biochemistry 59, 4238-4249 (2020).
PubMed: 33135413

Assembly members:

Assembly members:
entity_1, polymer, 179 residues, Formula weight is not available
entity_FE2, non-polymer, 55.845 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: pET19

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts153
1H chemical shifts989

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1acireductone dioxygenase1
2FE (II) ION2

Entities:

Entity 1, acireductone dioxygenase 179 residues - Formula weight is not available

1   METVALGLNALATRPTYRMETASPASPALA
2   PROGLYASPPROARGGLNPROHISARGPRO
3   ASPPROGLYARGPROVALGLYLEUGLUGLN
4   LEUARGARGLEUGLYVALLEUTYRTRPLYS
5   LEUASPALAASPLYSTYRGLUASNASPPRO
6   GLULEUGLULYSILEARGARGGLUARGASN
7   TYRSERTRPMETASPILEILETHRILECYS
8   LYSASPLYSLEUPROASNTYRGLUGLULYS
9   ILELYSMETPHETYRGLUGLUHISLEUHIS
10   LEUASPASPGLUILEARGTYRILELEUASP
11   GLYSERGLYTYRPHEASPVALARGASPLYS
12   GLUASPGLNTRPILEARGILEPHEMETGLU
13   LYSGLYASPMETVALTHRLEUPROALAGLY
14   ILETYRHISARGPHETHRVALASPGLULYS
15   ASNTYRTHRLYSALAMETARGLEUPHEVAL
16   GLYGLUPROVALTRPTHRALATYRASNARG
17   PROALAASPHISPHEGLUALAARGGLYGLN
18   TYRVALLYSPHELEUALAGLNTHRALA

Entity 2, FE (II) ION - Fe - 55.845 Da.

1   FE2

Samples:

sample_1: acireductone dioxygenase, [U-100% 13C; U-100% 15N], 500 uM; HEPES 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY vNMRFAM - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9BV57 (MTND_HUMAN)
AlphaFold Q9NV57

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