BMRB Entry 27439

Name: Sph15
Published: 2018-10-04

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PDB ID: 6g7g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27439
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:

Sph15

Deposition date:

2018-03-30

Original release date:

2018-10-04

Authors:

Coulthard, Rachel; Rajasekar, Karthik; Hyde, Eva; Smith, Lorna

Citation:

Citation: Coulthard, Rachel; Rajasekar, Karthik; Hyde, Eva; Smith, Lorna. "1H, 13C and 15N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thaliana" Biomol. NMR Assignments 13, 67-70 (2019).
PubMed: 30284185

Assembly members:

Assembly members:
Sph15, polymer, 115 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32b-SPH15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sph15: AMGCKEIEIVIKNTLGPSRI LQYHCRSGNTNVGVQYLNFK GTRIIKFKDDGTERSRWNCL FRQGINMKFFTEVEAYRPDL KHPLCGKRYELSARMDAIYF KMDERPPQPLNKWRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	105
1H chemical shifts	598

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sph15	1

Entities:

Entity 1, Sph15 115 residues - Formula weight is not available

1

ALA

MET

GLY

CYS

LYS

GLU

ILE

GLU

ILE

VAL

2

ILE

LYS

ASN

THR

LEU

GLY

PRO

SER

ARG

ILE

3

LEU

GLN

TYR

HIS

CYS

ARG

SER

GLY

ASN

THR

4

ASN

VAL

GLY

VAL

GLN

TYR

LEU

ASN

PHE

LYS

5

GLY

THR

ARG

ILE

LYS

PHE

LYS

ASP

6

GLY

THR

GLU

ARG

SER

ARG

TRP

ASN

CYS

LEU

7

PHE

ARG

GLN

GLY

ILE

ASN

MET

LYS

PHE

8

THR

GLU

VAL

GLU

ALA

TYR

ARG

PRO

ASP

LEU

9

LYS

HIS

PRO

LEU

CYS

GLY

LYS

ARG

TYR

GLU

10

LEU

SER

ALA

ARG

MET

ASP

ALA

ILE

TYR

PHE

11

LYS

MET

ASP

GLU

ARG

PRO

GLN

PRO

LEU

12

ASN

LYS

TRP

ARG

SER

Samples:

sample_1: Sph15, [U-99% 13C; U-99% 15N], 0.3 mM; sodium chloride 50 mM

sample_2: Sph15, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

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

CCPN vV2, CCPN - chemical shift assignment

ARIA v2.3, Linge, O'Donoghue and Nilges - data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Varian INOVA 800 MHz
Bruker Avance 600 MHz

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