BMRB Entry 17561

Title:
Solution Structure of the Dimeric Form of a Unliganded Bovine Neurophysin, Minimized Average Structure
Deposition date:
2011-03-31
Original release date:
2012-04-03
Authors:
Lee, Hunjoong; Naik, Mandar; Nguyen, Tam; Bracken, Clay; Breslow, Esther
Citation:

Citation: Lee, Hunjoong; Naik, Mandar; Bracken, Clay; Breslow, Esther. "Structural Basis of the Dimerization-Induced Increase in Neurophysin-Hormone Affinity: Interplay of Inter-Domain and Inter-Subunit Interactions"  .

Assembly members:

Assembly members:
Bovine Neurophysin, polymer, 92 residues, 9295.494 Da.

Natural source:

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: T7

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts86
15N chemical shifts154
1H chemical shifts708

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Neurophysin, 11
2Neurophysin, 21

Entities:

Entity 1, Neurophysin, 1 92 residues - 9295.494 Da.

1   ALAVALLEUASPLEUASPVALARGTHRCYS
2   LEUPROCYSGLYPROGLYGLYLYSGLYARG
3   CYSPHEGLYPROSERILECYSCYSGLYASP
4   GLULEUGLYCYSPHEVALGLYTHRALAGLU
5   ALALEUARGCYSGLNGLUGLUASNTYRLEU
6   PROSERPROCYSGLNSERGLYGLNLYSPRO
7   CYSGLYSERGLYGLYARGCYSALAALAALA
8   GLYILECYSCYSSERPROASPGLYCYSHIS
9   GLUASPPROALACYSASPPROGLUALAALA
10   PHESER

Samples:

sample_1: Bovine Neurophysin, [U-100% 15N], 1 mM

sample_conditions_1: pH: 2.7; pressure: 1 atm; temperature: 308 K

sample_conditions_2: pH: 2.7; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 10.15 mM; pH: 2.7; pressure: 1 atm; temperature: 314 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_3
2D 1H-15N HSQCsample_1isotropicsample_conditions_2

Software:

CNSSOLVE v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA v1.0, Linge, O'Donoghue and Nilges - processing

NMRPipe v1.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 17571
PDB
DBJ BAK09299 BAK09301 BAK09303
EMBL CAA23448 CAA23450 CAA25462 CAA38924 CAJ81049
GB AAA30680 AAI41998 AFU54450 ELK04017
PRF 0904308A 1005247A 1307200B
REF NP_789825 XP_006042791
SP P01175 P13389
TPG DAA23107
AlphaFold P13389 P01175

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