BMRB Entry 30118

Name: Solution Structure of a repacked version of HIF-2 alpha PAS-B (CASP target)
Published: 2016-08-11

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PDB ID: 5kiz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30118
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of a repacked version of HIF-2 alpha PAS-B (CASP target)

Deposition date: 2016-06-17 Original release date: 2016-08-11

Authors: Correa, Fernando; Key, Jason; Kuhlman, Brian; Gardner, Kevin

Citation: Correa, Fernando; Key, Jason; Kuhlman, Brian; Gardner, Kevin. "Repacking of internal hydrated HIF-2 alpha cavity removes allosteric binding site" . ., .-..

Assembly members:
Endothelial PAS domain-containing protein 1, polymer, 114 residues, 13264.091 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
Endothelial PAS domain-containing protein 1: GEFLDSKTFLSRFSMDMKFT YCDDRITELIGYHPEELLGR SASEFWHALDSENMTKSHQN LCTKGQVVSGQYRMLAKHGG YVWLETQMTVIYNPRNLQPQ CIMAVNYVLSEIEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	505
15N chemical shifts	122
1H chemical shifts	817

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 114 residues - 13264.091 Da.

1

GLY

GLU

PHE

LEU

ASP

SER

LYS

THR

PHE

LEU

2

SER

ARG

PHE

SER

MET

ASP

MET

LYS

PHE

THR

3

TYR

CYS

ASP

ARG

ILE

THR

GLU

LEU

ILE

4

GLY

TYR

HIS

PRO

GLU

LEU

GLY

ARG

5

SER

ALA

SER

GLU

PHE

TRP

HIS

ALA

LEU

ASP

6

SER

GLU

ASN

MET

THR

LYS

SER

HIS

GLN

ASN

7

LEU

CYS

THR

LYS

GLY

GLN

VAL

SER

GLY

8

GLN

TYR

ARG

MET

LEU

ALA

LYS

HIS

GLY

9

TYR

VAL

TRP

LEU

GLU

THR

GLN

MET

THR

VAL

10

ILE

TYR

ASN

PRO

ARG

ASN

LEU

GLN

PRO

GLN

11

CYS

ILE

MET

ALA

VAL

ASN

TYR

VAL

LEU

SER

12

GLU

ILE

GLU

LYS

Samples:

sample_1: HIF-2 alpha D1, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%; Tris 50 mM; NaCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

VNMR, Varian - collection

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts