BMRB Entry 52382

Name: Double-hydroxylated HIF-1alpha oxygen-dependent degradation domain
Published: 2024-08-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52382

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Double-hydroxylated HIF-1alpha oxygen-dependent degradation domain

Deposition date:

2024-04-01

Original release date:

2024-08-20

Authors:

He, Wenguang; Gasmi-Seabrook, Genevieve; Ikura, Mitsuhiko; Lee, Jeffrey; Ohh, Michael

Citation:

Citation: He, Wenguang; Gasmi-Seabrook, Genevieve; Ikura, Mitsuhiko; Lee, Jeffrey; Ohh, Michael. "Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1a" Proc. Natl. Acad. Sci. U. S. A. 121, e2408104121-e2408104121 (2024).
PubMed: 39231207

Assembly members:

Assembly members:
entity_1, polymer, 181 residues, 20029.06 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCDF Ek/LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PDALTLLAXAAGDTIISLDF GSNDTETDDQQLEEVPLYND VMLPSPNEKLQNINLAMSPL PTAETPKPLRSSADPALNQE VALKLEPNPESLELSFTMPQ IQDQTPSPSDGSTRQSSPEP NSPSEYCFYVDSDMVNEFKL ELVEKLFAEDTEAKNPFSTQ DTDLDLEMLAXYIPMDDDFQ L

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	525
15N chemical shifts	173
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIF-1alpha ODD_HyP	1

Entities:

Entity 1, HIF-1alpha ODD_HyP 181 residues - 20029.06 Da.

1

PRO

ASP

ALA

LEU

THR

LEU

ALA

HYP

ALA

2

ALA

GLY

ASP

THR

ILE

SER

LEU

ASP

PHE

3

GLY

SER

ASN

ASP

THR

GLU

THR

ASP

GLN

4

GLN

LEU

GLU

VAL

PRO

LEU

TYR

ASN

ASP

5

VAL

MET

LEU

PRO

SER

PRO

ASN

GLU

LYS

LEU

6

GLN

ASN

ILE

ASN

LEU

ALA

MET

SER

PRO

LEU

7

PRO

THR

ALA

GLU

THR

PRO

LYS

PRO

LEU

ARG

8

SER

ALA

ASP

PRO

ALA

LEU

ASN

GLN

GLU

9

VAL

ALA

LEU

LYS

LEU

GLU

PRO

ASN

PRO

GLU

10

SER

LEU

GLU

LEU

SER

PHE

THR

MET

PRO

GLN

11

ILE

GLN

ASP

GLN

THR

PRO

SER

PRO

SER

ASP

12

GLY

SER

THR

ARG

GLN

SER

PRO

GLU

PRO

13

ASN

SER

PRO

SER

GLU

TYR

CYS

PHE

TYR

VAL

14

ASP

SER

ASP

MET

VAL

ASN

GLU

PHE

LYS

LEU

15

GLU

LEU

VAL

GLU

LYS

LEU

PHE

ALA

GLU

ASP

16

THR

GLU

ALA

LYS

ASN

PRO

PHE

SER

THR

GLN

17

ASP

THR

ASP

LEU

ASP

LEU

GLU

MET

LEU

ALA

18

HYP

TYR

ILE

PRO

MET

ASP

PHE

GLN

19

LEU

Samples:

sample_1: HIF-1alpha ODD_HyP, [U-100% 13C; U-100% 15N], 230 uM; D2O, [U-100% 2H], 5%; H2O 95%; sodium chloride 100 mM; TRIS 50 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.1.4 - collection

NMR spectrometers:

Bruker US2 800 MHz