BMRB Entry 17571

Title:
(Revised) SOLUTION STRUCTURE OF THE MONOMERIC FORM OF A MUTANT UNLIGANDED BOVINE NEUROPHYSIN, 20 STRUCTURES.
Deposition date:
2011-04-01
Original release date:
2012-04-03
Authors:
Lee, Hunjoong; 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:
Mutant Unliganded Bovine Neurophysin, polymer, 92 residues, 9286.461 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):

Entity Sequences (FASTA):
Mutant Unliganded Bovine Neurophysin: AVLDLDVRTCLPCGPGGKGR CFGPSICCGDELGCFVGTAE ALRCQEENYLPSPCQSGQKP CGSGGRCAAAGICCSPDGCE EDPACDPEAAFS

Data sets:
Data typeCount
13C chemical shifts170
15N chemical shifts74
1H chemical shifts367

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mutant Unliganded Bovine Neurophysin1

Entities:

Entity 1, Mutant Unliganded Bovine Neurophysin 92 residues - 9286.461 Da.

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

Samples:

sample_1: entity, [U-100% 15N], 1.4 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 1.4 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 283 K

sample_conditions_2: pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_3
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_3
2D 1H-15N HSQCsample_2isotropicsample_conditions_3
2D 1H-15N HSQCsample_2anisotropicsample_conditions_3

Software:

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

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17561
PDB
DBJ BAK09299 BAK09301 BAK09303
EMBL CAA23448 CAA23450 CAA25462 CAJ81049
GB AAA30680 AAI41998 AFU54450 ELK04017
PRF 0904308A 1005247A 1307200B
REF NP_789825 XP_006042791
SP P01175
TPG DAA23107
AlphaFold P01175

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