BMRB Entry 17279

Title:
Solution NMR structure of protein lipocalin 12 from rat epididymis
Deposition date:
2010-11-03
Original release date:
2011-05-05
Authors:
Peng, Yu; Lin, Donghai
Citation:

Citation: Peng, Yu; Zhang, Xu; Liu, Jiafu; Liu, Qiang; Guo, Chenyun; Zhang, Yonglian; Lin, Donghai. "Solution structure of the protein lipocalin 12 from rat epididymis."  Proteins 79, 2316-2320 (2011).
PubMed: 21538546

Assembly members:

Assembly members:
rat_epididymal_lipocalin_12, polymer, 184 residues, 20124.996 Da.

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Data sets:
Data typeCount
13C chemical shifts728
15N chemical shifts182
1H chemical shifts1098

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rat epididymal lipocalin 121

Entities:

Entity 1, rat epididymal lipocalin 12 184 residues - 20124.996 Da.

1   METGLYGLNSERPROTHRMETPROGLNGLY
2   PHESERGLNMETTHRSERPHEGLNSERASN
3   LYSPHEGLNGLYGLUTRPPHEVALLEUGLY
4   LEUALAASPASNTHRTYRLYSARGGLUHIS
5   ARGPROLEULEUHISSERPHEILETHRLEU
6   PHELYSLEUARGASPASNSERGLUPHEGLN
7   VALTHRASNSERMETTHRARGGLYLYSHIS
8   CYSSERTHRTRPSERTYRTHRLEUILEPRO
9   THRASNLYSPROGLYGLNPHETHRARGASP
10   ASNARGGLYSERGLYPROGLYALAASPLYS
11   GLUASNILEGLNVALILEGLUTHRASPTYR
12   VALLYSPHEALALEUVALLEUSERLEUARG
13   GLNALASERASNGLNASNILETHRARGVAL
14   SERLEULEUGLYARGASPTRPLYSILETHR
15   HISLYSTHRILEASPARGPHEILEALALEU
16   THRLYSTHRGLNASNLEUTHRLYSASNASN
17   LEULEUPHEPROASPLEUTHRASPTRPLEU
18   LEUASPPROLYSVALCYSLEUGLUHISHIS
19   HISHISHISHIS

Samples:

sample: rLcn12, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaAC 20 MM; EDTA 0.5 MM

sample_conditions_1: ionic strength: 20 mM; pH: 4.5; pressure: 1 Pa; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
4D 1H-15N NOESYsampleisotropicsample_conditions_1
4D 1H-13C NOESYsampleisotropicsample_conditions_1
3D MQ-CCH-TOCSYsampleisotropicsample_conditions_1
3D HN(CO)CAsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - refinement

ARIA v2.2, Linge, O'Donoghue and Nilges - chemical shift assignment

NMR spectrometers:

  • Bruker Advance III 800 MHz

Related Database Links:

PDB
GB ABG24235 EDL93574
REF NP_001121610
SP B3EY83
AlphaFold B3EY83

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