BMRB Entry 36299

Name: Solution structure of SPA-2 SHD
Published: 2020-05-05

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PDB ID: 6lag
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36299
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 SPA-2 SHD

Deposition date:

2019-11-12

Original release date:

2020-05-05

Authors:

Fan, J.; Wong, J.; Zheng, P.; Yang, D.; Jedd, G.

Citation:

Citation: Fan, J.; Wong, J.; Zheng, P.; Yang, D.; Jedd, G.. "Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds" .

Assembly members:

Assembly members:
entity_1, polymer, 155 residues, 17781.943 Da.

Natural source:

Natural source: Common Name: Neurospora crassa Taxonomy ID: 5141 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Neurospora crassa

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MGENQELVLSDHYISLKRYL SATSRDGNPKPPPNKARDKL QRLTEVQFLELSTDVYDELK RREQVARRGPNAPPETAPPD FLLPQDNFHPKRNQARQKLS SLGPPRFRDLATDVFCELER RYPNFANLEMPLNAS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	458
15N chemical shifts	134
1H chemical shifts	779

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_1 155 residues - 17781.943 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLY

GLU

ASN

GLN

GLU

LEU

VAL

LEU

SER

4

ASP

HIS

TYR

ILE

SER

LEU

LYS

ARG

TYR

LEU

5

SER

ALA

THR

SER

ARG

ASP

GLY

ASN

PRO

LYS

6

PRO

ASN

LYS

ALA

ARG

ASP

LYS

LEU

7

GLN

ARG

LEU

THR

GLU

VAL

GLN

PHE

LEU

GLU

8

LEU

SER

THR

ASP

VAL

TYR

ASP

GLU

LEU

LYS

9

ARG

GLU

GLN

VAL

ALA

ARG

GLY

PRO

10

ASN

ALA

PRO

GLU

THR

ALA

PRO

ASP

11

PHE

LEU

PRO

GLN

ASP

ASN

PHE

HIS

PRO

12

LYS

ARG

ASN

GLN

ALA

ARG

GLN

LYS

LEU

SER

13

SER

LEU

GLY

PRO

ARG

PHE

ARG

ASP

LEU

14

ALA

THR

ASP

VAL

PHE

CYS

GLU

LEU

GLU

ARG

15

ARG

TYR

PRO

ASN

PHE

ALA

ASN

LEU

GLU

MET

16

PRO

LEU

ASN

ALA

SER

Samples:

sample_1: SHD, [U-13C; U-15N], 2 ± 0.1 mM; D2O, [U-2H], 10%; H2O 90%; disodium hydrogen phosphate 10 ± 0.1 mM; sodium dihydrogen phospahte 10 ± 0.1 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - data analysis

TopSpin, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE 800 MHz

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