BMRB Entry 19356

Title:
Solution structure of the chimeric hydrophobin NChi2
Deposition date:
2013-07-10
Original release date:
2014-02-13
Authors:
Ren, Qin; Sunde, Margaret; Kwan, Ann
Citation:

Citation: Ren, Qin; Kwan, Ann; Sunde, Margaret. "Solution structure and interface-driven self-assembly of NC2, a new member of the Class II hydrophobin proteins."  Proteins 82, 990-1003 (2014).
PubMed: 24218020

Assembly members:

Assembly members:
Nchi2, polymer, 88 residues, 9014.035 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   Vector: pHUE

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts91
1H chemical shifts503
T1 relaxation values80
T2 relaxation values80
heteronuclear NOE values80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nchi21

Entities:

Entity 1, Nchi2 88 residues - 9014.035 Da.

1   SERPROALAALAMETGLUARGGLNVALPRO
2   TYRTHRPROCYSSERGLYLEUTYRGLYTHR
3   ALAGLNCYSCYSALATHRASPVALLEUGLY
4   VALALAASPLEUASPCYSALAASNPROPRO
5   ALATHRLEUALAASNALATHRHISPHEGLU
6   SERTHRCYSALAALAILEGLYGLNARGALA
7   ARGCYSCYSLYSASPASPVALTHRASNTHR
8   GLYASNSERPHELEUILEILEASNALAALA
9   ASNCYSGLNTHRPROALAGLYLEU

Samples:

sample_NChi2: Nchi2 0.50 mM; Glycine 50.00 mM; DSS 0.05 mM

sample_new_1: Nchi2 0.50 mM; Glycine 50.00 mM; DSS 0.05 mM

sample_new_2: Nchi2, [U-15N], 0.30 mM; Glycine 50.00 mM; DSS 0.05 mM

NChi2_1: ionic strength: 50.000 mM; pH: 2.500; pressure: 1.000 atm; temperature: 318.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_NChi2isotropicNChi2_1
H-H NOESYsample_new_1solutionNChi2_1
T1sample_new_2solutionNChi2_1
T2sample_new_2solutionNChi2_1
HETERONOEsample_new_2solutionNChi2_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - solution structure and refinement

AutoDep v4.3, Sen et al. - data deposition

CNS vany - data analysis

ANALYSIS v2.1, CCPN - peak picking and data analysis

DANGLE v1.1, Cheung, Maguire, Stevens and Broadhurst - Secondary structure prediction

MOLPROBITY v4.02B, Chen et al. - data analysis

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR v3.4, Laskowski and MacArthur - structure validation

TOPSPIN v2.1, Bruker Biospin - data collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

UNP Q7S3P5_NEUCR RODL_NEUCR
AlphaFold Q7S3P5 Q7SC53

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