BMRB Entry 26741

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26741

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone and Partial Side-Chain Chemical Shift Assignments and Dynamics Measurements for The Catalytic Domain of Human Prolyl Hydroxylase Domain 2 (PHD2) With Zn(II) and 2-Oxoglutarate (2OG)
Deposition date:
2016-02-04
Original release date:
2016-08-26
Authors:
Leung, Ivanhoe; Schofield, Christopher; Claridge, Timothy; Landrieu, Isabelle; Cantrelle, Francois-Xavier; Hardy, Adam
Citation:

Citation: Abboud, Martine; McAllister, Tom; Leung, Ivanhoe; Chowdhury, Rasheduzzaman; Jorgensen, Christian; Domene, Carmen; Mecinovic, Jasmin; Lippl, Kerstin; Hancock, Rebecca; Hopkinson, Richard; Kawamura, Akane; Claridge, Timothy; Schofield, Christopher. "2-Oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2."  Chem. Commun. (Camb.) 54, 3130-3133 (2018).
PubMed: 29522057

Assembly members:

Assembly members:
PHD2, polymer, 228 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
entity_AKG, non-polymer, 146.098 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHD2: GSHMASPNGQTKPLPALKLA LEYIVPCMNKHGICVVDDFL GKETGQQIGDEVRALHDTGK FTDGQLVSQKSDSSKDIRGD KITWIEGKEPGCETIGLLMS SMDDLIRHCNGKLGSYKING RTKAMVACYPGNGTGYVRHV DNPNGDGRCVTCIYYLNKDW DAKVSGGILRIFPEGKAQFA DIEPKFDRLLFFWSDRRNPH EVQPAYATRYAITVWYFDAD ERARAKVK

Data sets:
Data typeCount
13C chemical shifts564
15N chemical shifts183
1H chemical shifts183
T1 relaxation values173
T2 relaxation values170
heteronuclear NOE values173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PHD21
2ZINC ION2
3Co-substrate3

Entities:

Entity 1, PHD2 228 residues - Formula weight is not available

The first six amino acids of the sequence (GSHMAS) are non-native N-terminal residues that remained from thrombin protease cleavage of poly-histidine tag. The rest of the sequence represents the catalytic domain of PHD2 (residues 181-402).

1   GLYSERHISMETALASERPROASNGLYGLN
2   THRLYSPROLEUPROALALEULYSLEUALA
3   LEUGLUTYRILEVALPROCYSMETASNLYS
4   HISGLYILECYSVALVALASPASPPHELEU
5   GLYLYSGLUTHRGLYGLNGLNILEGLYASP
6   GLUVALARGALALEUHISASPTHRGLYLYS
7   PHETHRASPGLYGLNLEUVALSERGLNLYS
8   SERASPSERSERLYSASPILEARGGLYASP
9   LYSILETHRTRPILEGLUGLYLYSGLUPRO
10   GLYCYSGLUTHRILEGLYLEULEUMETSER
11   SERMETASPASPLEUILEARGHISCYSASN
12   GLYLYSLEUGLYSERTYRLYSILEASNGLY
13   ARGTHRLYSALAMETVALALACYSTYRPRO
14   GLYASNGLYTHRGLYTYRVALARGHISVAL
15   ASPASNPROASNGLYASPGLYARGCYSVAL
16   THRCYSILETYRTYRLEUASNLYSASPTRP
17   ASPALALYSVALSERGLYGLYILELEUARG
18   ILEPHEPROGLUGLYLYSALAGLNPHEALA
19   ASPILEGLUPROLYSPHEASPARGLEULEU
20   PHEPHETRPSERASPARGARGASNPROHIS
21   GLUVALGLNPROALATYRALATHRARGTYR
22   ALAILETHRVALTRPTYRPHEASPALAASP
23   GLUARGALAARGALALYSVALLYS

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Entity 3, Co-substrate - C5 H6 O5 - 146.098 Da.

1   AKG

Samples:

Sample_Assignment: PHD2, [U-13C; U-15N; U-2H], 0.4 mM; 2-Oxoglutarate 0.9167 mM; Zinc ion 0.6875 mM; DSS 0.0667 mM; TRIS, [U-2H], 50 mM; sodium azide 0.02%

Sample_T1T2NOE: PHD2, [U-15N], 1 mM; Zinc ion 1.5 mM; 2-Oxoglutarate 2 mM; TRIS, [U-2H], 50 mM; sodium azide 0.02%

sample_conditions_assignment: pH: 6.6; temperature: 310 K

sample_conditions_t1t2noe: pH: 6.6; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSample_Assignmentisotropicsample_conditions_assignment
3D HNCOSample_Assignmentisotropicsample_conditions_assignment
3D HNCASample_Assignmentisotropicsample_conditions_assignment
3D HNCACBSample_Assignmentisotropicsample_conditions_assignment
3D HNCOCACBSample_Assignmentisotropicsample_conditions_assignment
3D HNCOCASample_Assignmentisotropicsample_conditions_assignment
3D HNCACOSample_Assignmentisotropicsample_conditions_assignment
3D Heteronuclear NOESample_T1T2NOEisotropicsample_conditions_t1t2noe
3D T1Sample_T1T2NOEisotropicsample_conditions_t1t2noe
3D T2Sample_T1T2NOEisotropicsample_conditions_t1t2noe
2D 1H-15N HSQCSample_T1T2NOEisotropicsample_conditions_t1t2noe

Software:

TOPSPIN, Bruker Biospin - collection, processing

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

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