BMRB Entry 17128

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17128

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Title:
unbound Cation-independent mannose-6-phosphate receptor domain 11 E4 mutant
Deposition date:
2010-08-13
Original release date:
2014-03-04
Authors:
Williams, Christopher; Hoppe, Hans; Rezgui, Dellel; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E; Crump, Matthew; Hassan, A
Citation:

Citation: Williams, Christopher; Hoppe, Hans; Rezgui, Dellel; Strickland, Madeline; Frago, Susana; Ellis, Rosamund; Wattana-Amorn, Pakorn; Prince, Stuart; Zaccheo, Oliver; Forbes, Briony; Jones, E.; Crump, Matthew; Hassan, A.; Grutzner, Frank; Nolan, Catherine; Mungall, Andrew. "An exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution"  Science 338, 1209-1213 (2012).
PubMed: 23197533

Assembly members:

Assembly members:
domain_11, polymer, 142 residues, 15434.610 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
domain_11: MKSNEHDDCQVTNPSTGHLF DLSSLSGRAGFTAAYSKSGV VYMSICGENENCPPGVGACF GQTRISVGKANKRLRYVDQV LQLVYKDGSPCPSKSGLSYK SVISFVCRPEAGPTNRPMLI SLDKQTCTLFFSWHTPLACE PE

Data sets:
Data typeCount
13C chemical shifts593
15N chemical shifts145
1H chemical shifts922

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain 11 mutant1

Entities:

Entity 1, Domain 11 mutant 142 residues - 15434.610 Da.

Mutated Domain 11 of the Cytoplasmic region of the Cation-independent mannose-6-phosphate receptor

1   METLYSSERASNGLUHISASPASPCYSGLN
2   VALTHRASNPROSERTHRGLYHISLEUPHE
3   ASPLEUSERSERLEUSERGLYARGALAGLY
4   PHETHRALAALATYRSERLYSSERGLYVAL
5   VALTYRMETSERILECYSGLYGLUASNGLU
6   ASNCYSPROPROGLYVALGLYALACYSPHE
7   GLYGLNTHRARGILESERVALGLYLYSALA
8   ASNLYSARGLEUARGTYRVALASPGLNVAL
9   LEUGLNLEUVALTYRLYSASPGLYSERPRO
10   CYSPROSERLYSSERGLYLEUSERTYRLYS
11   SERVALILESERPHEVALCYSARGPROGLU
12   ALAGLYPROTHRASNARGPROMETLEUILE
13   SERLEUASPLYSGLNTHRCYSTHRLEUPHE
14   PHESERTRPHISTHRPROLEUALACYSGLU
15   PROGLU

Samples:

sample_1: D2O 5 ± 0.1 %; sodium acetate, [U-99% 2H], 10 ± 0.1 mM; entity, [U-98% 13C; U-98% 15N], 0.5 – 1 mM; EDTA 100 ± 0.1 uM; H2O 95 ± 0.1 %

sample_conditions_1: pH: 4.2; pressure: 1 atm; temperature: 273 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

Analysis v2.13, CCPN - chemical shift assignment, data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

iCing vr765, Vuister, Doreleijers, Sousa da Silva - refinement

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

  • Varian VNMRS 600 MHz

Related Database Links:

BMRB 17127 19117 19153
PDB

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