BMRB Entry 30321

Name: Solution structure of the sorting nexin 25 phox-homology domain
Published: 2018-07-30

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PDB ID: 5woe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30321
MolProbity Validation Chart

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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:

Solution structure of the sorting nexin 25 phox-homology domain

Deposition date:

2017-08-01

Original release date:

2018-07-30

Authors:

Chin, Y.; Mas, C.; Mobli, M.; Collins, B.

Citation:

Citation: Chandra, Mintu; Chin, Yanni K-Y; Mas, Caroline; Feathers, J Ryan; Paul, Blessy; Datta, Sanchari; Chen, Kai-En; Jia, Xinying; Yang, Zhe; Norwood, Suzanne; Mohanty, Biswaranjan; Bugarcic, Andrea; Teasdale, Rohan; Henne, W Mike; Mobli, Mehdi; Collins, Brett. "Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities" Nat. Commun. 10, 1528-1528 (2019).
PubMed: 30948714

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14245.309 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSNLGMWKASITSGEVTEEN GEQLPCYFVMVSLQEVGGVE TKNWTVPRRLSEFQNLHRKL SECVPSLKKVQLPSLSKLPF KSIDQKFMEKSKNQLNKFLQ NLLSDERLCQSEALYAFLSP SPDYL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	535
15N chemical shifts	131
1H chemical shifts	886

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_1 125 residues - 14245.309 Da.

1

GLY

SER

ASN

LEU

GLY

MET

TRP

LYS

ALA

SER

2

ILE

THR

SER

GLY

GLU

VAL

THR

GLU

ASN

3

GLY

GLU

GLN

LEU

PRO

CYS

TYR

PHE

VAL

MET

4

VAL

SER

LEU

GLN

GLU

VAL

GLY

VAL

GLU

5

THR

LYS

ASN

TRP

THR

VAL

PRO

ARG

LEU

6

SER

GLU

PHE

GLN

ASN

LEU

HIS

ARG

LYS

LEU

7

SER

GLU

CYS

VAL

PRO

SER

LEU

LYS

VAL

8

GLN

LEU

PRO

SER

LEU

SER

LYS

LEU

PRO

PHE

9

LYS

SER

ILE

ASP

GLN

LYS

PHE

MET

GLU

LYS

10

SER

LYS

ASN

GLN

LEU

ASN

LYS

PHE

LEU

GLN

11

ASN

LEU

SER

ASP

GLU

ARG

LEU

CYS

GLN

12

SER

GLU

ALA

LEU

TYR

ALA

PHE

LEU

SER

PRO

13

SER

PRO

ASP

TYR

LEU

Samples:

sample_1: DTT 2 mM; HEPES 20 mM; NaCl 100 mM; SNX25, [U-99% 13C; U-99% 15N], 0.8 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	anisotropic	sample_conditions_1
3D HNCACB	sample_1	anisotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

Rowland NMR ToolKit, Gregory P. Mullen - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceII 900 MHz

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