BMRB Entry 17865

Name: Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2
Published: 2012-07-16

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PDB ID: 2lht
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17865
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2

Deposition date:

2011-08-16

Original release date:

2012-07-16

Authors:

Mesarich, Carl; Schmitz, Michael; Tremouilhac, Pierre; Greenwood, David; McGillivray, Duncan; Templeton, Matthew; Dingley, Andrew

Citation:

Citation: Mesarich, Carl; Schmitz, Michael; Tremouilhac, Pierre; McGillivray, Duncan; Templeton, Matthew; Dingley, Andrew. "Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus." Biochim. Biophys. Acta 1824, 1118-1128 (2012).
PubMed: 22771296

Assembly members:

Assembly members:
ViCin1-D1D2, polymer, 122 residues, 13649.491 Da.

Natural source:

Natural source: Common Name: Venturia inaequalis Taxonomy ID: 5025 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Venturia inaequalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pPICZaBCin1-2D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ViCin1-D1D2: ADVFDPPTQYGYDGKPLDAS FCRTAGSREKDCRKDVQACD KKYDDQGRETACAKGIREKY KPAVVYGYDGKPLDLGFCTL AGIREVDCRKDAQTCDKKYE SDKCLNAIKEKYKPVVDPNP PA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
spectral_density_values
- spectral_density_list_1

Data type	Count
13C chemical shifts	499
15N chemical shifts	114
1H chemical shifts	793
heteronuclear NOE values	94
spectral density values	94
T1 relaxation values	94
T2 relaxation values	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ViCin1-D1D2	1

Entities:

Entity 1, ViCin1-D1D2 122 residues - 13649.491 Da.

Residue numbering corresponds to protein sequence

1

ALA

ASP

VAL

PHE

ASP

PRO

THR

GLN

TYR

2

GLY

TYR

ASP

GLY

LYS

PRO

LEU

ASP

ALA

SER

3

PHE

CYS

ARG

THR

ALA

GLY

SER

ARG

GLU

LYS

4

ASP

CYS

ARG

LYS

ASP

VAL

GLN

ALA

CYS

ASP

5

LYS

TYR

ASP

GLN

GLY

ARG

GLU

THR

6

ALA

CYS

ALA

LYS

GLY

ILE

ARG

GLU

LYS

TYR

7

LYS

PRO

ALA

VAL

TYR

GLY

TYR

ASP

GLY

8

LYS

PRO

LEU

ASP

LEU

GLY

PHE

CYS

THR

LEU

9

ALA

GLY

ILE

ARG

GLU

VAL

ASP

CYS

ARG

LYS

10

ASP

ALA

GLN

THR

CYS

ASP

LYS

TYR

GLU

11

SER

ASP

LYS

CYS

LEU

ASN

ALA

ILE

LYS

GLU

12

LYS

TYR

LYS

PRO

VAL

ASP

PRO

ASN

PRO

13

PRO

ALA

Samples:

sample_1: ViCin1-D1D2, [U-99% 13C; U-99% 15N], 0.6-0.8 mM; potassium phosphate 25 mM; H2O 95%; D2O 5%

sample_2: ViCin1-D1D2, [U-99% 13C; U-99% 15N], 1.0 mM; potassium phosphate 25 mM; polyacrylamide gel 5-6%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.050 M; pH: 6.2; pressure: 1 atm; temperature: 298.15 K

sample_conditions_2: ionic strength: 0.050 M; pH: 6.2; pressure: 1 atm; temperature: 298.15 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 CBCANH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCAN	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHG	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N IPAP-HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N IPAP-HSQC	sample_2	anisotropic	sample_conditions_2
2D 1H-15N R2 relaxation	sample_1	isotropic	sample_conditions_1
2D 1H-15N R1 relaxation	sample_1	isotropic	sample_conditions_1
2D 1H-15N heteronuclear NOE	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1pl3, Bruker Biospin - collection

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

CcpNMR v2.07, CCPN - chemical shift assignment, peak picking

UNIO v2.0, Herrmann - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 600 MHz