BMRB Entry 16772

Title:
SOLUTION STRUCTURE OF CI-MPR ligand-free domain 5
Deposition date:
2010-03-10
Original release date:
2012-08-03
Authors:
Olson, L.; Peterson, F.; Volkman, B.; Dahms, N.
Citation:

Citation: Olson, L.; Peterson, F.; Castonguay, A.; Bohnsack, R.; Kudo, M.; Gotschall, R.; Canfield, W.; Volkman, B.; Dahms, N.. "Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor."  Proc. Natl. Acad. Sci. U. S. A. 107, 12493-12498 (2010).
PubMed: 20615935

Assembly members:

Assembly members:
CI-MPR_domain5, polymer, 148 residues, 16759.471 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: Pichia pastoris   Vector: pPICZ-alpha-A

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts151
1H chemical shifts888

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CI-MPR domain51

Entities:

Entity 1, CI-MPR domain5 148 residues - 16759.471 Da.

Residues 578-583 are a cloning artifact.

1   GLUALAGLUALAGLUPHELEUSERARGTHR
2   GLUGLYASPASNCYSTHRVALPHEASPSER
3   GLNALAGLYPHESERPHEASPLEUTHRPRO
4   LEUTHRLYSLYSASPALATYRLYSVALGLU
5   THRASPLYSTYRGLUPHEHISILEASNVAL
6   CYSGLYPROVALSERVALGLYALACYSPRO
7   PROASPSERGLYALACYSGLNVALSERARG
8   SERASPARGLYSSERTRPASNLEUGLYARG
9   SERASNALALYSLEUSERTYRTYRASPGLY
10   METILEGLNLEUTHRTYRARGASPGLYTHR
11   PROTYRASNASNGLULYSARGTHRPROARG
12   ALATHRLEUILETHRPHELEUCYSASPARG
13   ASPALAGLYVALGLYPHEPROGLUTYRGLN
14   GLUGLUASPASNSERTHRTYRASNPHEARG
15   TRPTYRTHRSERTYRALACYSPRO

Samples:

sample: CI-MPR domain5, [U-100% 13C; U-100% 15N], 1 mM; bis-tris, [U-2H], 10 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sampleisotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16773
PDB

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