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 17743

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17743

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Title: Backbone 1H, 13C and 15N chemical shift assignments for the N-terminal domain of insulin-like growth factor binding protein-2 (IGFBP-2)   PubMed: 21951978

Deposition date: 2011-06-28 Original release date: 2011-07-14

Authors: Galea, Charles; Mobli, Mehdi; McNeil, Kerrie; Mulhern, Terrence; Wallace, John; King, Glenn; Forbes, Briony; Norton, Raymond

Citation: Galea, Charles; Mobli, Mehdi; McNeil, Kerrie; Mulhern, Terrence; Wallace, John; King, Glenn; Forbes, Briony; Norton, Raymond. "Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain."  Biochimie 94, 608-616 (2012).

Assembly members:
IGFBP-2_N-domain, polymer, 100 residues, 10222.9 Da.

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

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

Entity Sequences (FASTA):
IGFBP-2_N-domain: GPEVLFRCPPCTPERLAACG PPPVAPPAAVAAVAGGARMP CAELVREPGCGCCSVCARLE GEACGVYTPRCGQGLRCYPH PGSELPLQALVMGEGTCEKR

Data sets:
Data typeCount
13C chemical shifts234
15N chemical shifts80
1H chemical shifts80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-BP-2, chain 11
2N-BP-2, chain 21

Entities:

Entity 1, N-BP-2, chain 1 100 residues - 10222.9 Da.

Residues -1 and -2 are part of the 3C protease cleavage site and remain after removal of the thioredoxin fusion tag.

1   GLYPROGLUVALLEUPHEARGCYSPROPRO
2   CYSTHRPROGLUARGLEUALAALACYSGLY
3   PROPROPROVALALAPROPROALAALAVAL
4   ALAALAVALALAGLYGLYALAARGMETPRO
5   CYSALAGLULEUVALARGGLUPROGLYCYS
6   GLYCYSCYSSERVALCYSALAARGLEUGLU
7   GLYGLUALACYSGLYVALTYRTHRPROARG
8   CYSGLYGLNGLYLEUARGCYSTYRPROHIS
9   PROGLYSERGLULEUPROLEUGLNALALEU
10   VALMETGLYGLUGLYTHRCYSGLULYSARG

Samples:

sample_1: IGFBP-2 N-domain, [U-100% 15N], 0.07 mM; IGFBP-2 N-domain, [U-100% 13C; U-100% 15N], 0.07 mM; sodium citrate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.02 M; pH: 5.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(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 HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v0.3, Bruker Biospin - collection, processing

NMRView v8.0, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis, peak picking

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

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

RNMRTK v3.0, (RNMRTK) Hoch and Stern - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

DBJ BAD92746
EMBL CAA34373
GB AAA03246 AAA36048 AAB22308 AAH04312 AAH09902
REF NP_000588 XP_001087071 XP_003254105 XP_003780748 XP_003907977
SP P18065

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