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 17447

Title: 1H, 15N and 13C resonance assignment of a common Major Urinary Protein of the mouse   PubMed: 20703836

Deposition date: 2011-02-07 Original release date: 2012-08-30

Authors: Phelan, Marie; McLean, Lynn; Simpson, Deborah; Hurst, Jane; Beynon, Robert; Lian, Lu-Yun

Citation: Phelan, Marie; McLean, Lynn; Simpson, Deborah; Hurst, Jane; Beynon, Robert; Lian, Lu-Yun. "1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein."  Biomol NMR Assign 4, 239-241 (2010).

Assembly members:
MUP11, polymer, 176 residues, 20336.5 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):
MUP11: MGSSHHHHHHIEGREEASST GRNFNVEKINGEWHTIILAS DKREKIEDNGNFRLFLEQIH VLENSLVLKFHTVRDEECSE LSMVADKTEKAGEYSVTYDG FNTFTIPKTDYDNFLMAHLI NEKDGETFQLMGLYGREPDL SSDIKERFAQLCEEHGILRE NIIDLSNANRCLQARE

Data sets:
Data typeCount
13C chemical shifts714
15N chemical shifts170
1H chemical shifts1074

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MUP111

Entities:

Entity 1, MUP11 176 residues - 20336.5 Da.

residues 20 to 181 correspond to the native MUP residues 6 to 19 correspond to the cloning and purification tag

1   METGLYSERSERHISHISHISHISHISHIS
2   ILEGLUGLYARGGLUGLUALASERSERTHR
3   GLYARGASNPHEASNVALGLULYSILEASN
4   GLYGLUTRPHISTHRILEILELEUALASER
5   ASPLYSARGGLULYSILEGLUASPASNGLY
6   ASNPHEARGLEUPHELEUGLUGLNILEHIS
7   VALLEUGLUASNSERLEUVALLEULYSPHE
8   HISTHRVALARGASPGLUGLUCYSSERGLU
9   LEUSERMETVALALAASPLYSTHRGLULYS
10   ALAGLYGLUTYRSERVALTHRTYRASPGLY
11   PHEASNTHRPHETHRILEPROLYSTHRASP
12   TYRASPASNPHELEUMETALAHISLEUILE
13   ASNGLULYSASPGLYGLUTHRPHEGLNLEU
14   METGLYLEUTYRGLYARGGLUPROASPLEU
15   SERSERASPILELYSGLUARGPHEALAGLN
16   LEUCYSGLUGLUHISGLYILELEUARGGLU
17   ASNILEILEASPLEUSERASNALAASNARG
18   CYSLEUGLNALAARGGLU

Samples:

sample_1: MUP11, [U-98% 13C; U-98% 15N], 1 mM; potassium phosphate 25 mM; sodium azide 0.2%; H2O 90%; D2O 10%

sample_2: MUP11, [U-98% 13C; U-98% 15N], 1 mM; potassium phosphate 25 mM; sodium azide 0.2%; D2O 100%

sample_conditions_1: ionic strength: 25 mM; pH: 6.8; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aromatic)sample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.1.5, CCPN - chemical shift assignment, data analysis

DANGLE v1.1, CCPN - Secondary structure calculation

AZARA, Boucher - processing

TOPSPIN v2.1, Bruker Biospin - collection, refinement

CSI, David Wishart, Brian Sykes - Secondary structure calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q9CXU6
MGI 3709617
BMRB 4340
PDB
DBJ BAB28753 BAB29093
EMBL CAA26953 CAA27227 CAA27729 CAC34259 CAQ11104
GB AAA39764 AAA39765 AAA39767 AAA39768 AAB47130
REF NP_001039015 NP_001116119 NP_001128116 NP_001128146 NP_001128147
SP B5X0G2 P02762 P04938 P11588 P11589
TPG DAA06299 DAA06300 DAA06301 DAA06302 DAA06303
AlphaFold Q9CXU6 P11589 B5X0G2 P02762 P04938 P11588

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