BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17865

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17865
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2   PubMed: 22771296

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: 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).

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

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

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

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

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts114
1H chemical shifts793
heteronuclear NOE values94
spectral density values94
T1 relaxation values94
T2 relaxation values94

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ViCin1-D1D21

Entities:

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

Residue numbering corresponds to protein sequence

1   ALAASPVALPHEASPPROPROTHRGLNTYR
2   GLYTYRASPGLYLYSPROLEUASPALASER
3   PHECYSARGTHRALAGLYSERARGGLULYS
4   ASPCYSARGLYSASPVALGLNALACYSASP
5   LYSLYSTYRASPASPGLNGLYARGGLUTHR
6   ALACYSALALYSGLYILEARGGLULYSTYR
7   LYSPROALAVALVALTYRGLYTYRASPGLY
8   LYSPROLEUASPLEUGLYPHECYSTHRLEU
9   ALAGLYILEARGGLUVALASPCYSARGLYS
10   ASPALAGLNTHRCYSASPLYSLYSTYRGLU
11   SERASPLYSCYSLEUASNALAILELYSGLU
12   LYSTYRLYSPROVALVALASPPROASNPRO
13   PROALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCANsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D HBCBCGCDHGsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_2anisotropicsample_conditions_2
2D 1H-15N R2 relaxationsample_1isotropicsample_conditions_1
2D 1H-15N R1 relaxationsample_1isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_1isotropicsample_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

Related Database Links:

PDB

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