BMRB Entry 16027

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16027
MolProbity Validation Chart

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Title:
ENHANCING THE ACTIVITY OF INSULIN BY STEREOSPECIFIC UNFOLDING
Deposition date:
2008-11-07
Original release date:
2009-04-17
Authors:
Hua, Q.; Xu, B.; Huang, K.; Hu, S.; Nakarawa, S.; Jia, W.; Philips, N.; Wittaker, L.; Wittaker, J.; Katsoyannis, P.; Weiss, M.
Citation:

Citation: Hua, Q.; Xu, B.; Huang, K.; Hu, S.; Nakarawa, S.; Jia, W.; Wang, S.; Wittaker, J.; Katsoyannis, P.; Weiss, M.. "Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins"  J. Biol. Chem. 284, 14586-14596 (2009).
PubMed: 19321436

Assembly members:

Assembly members:
INSULIN_A_CHAIN, polymer, 21 residues, 2383.700 Da.
INSULIN_B_CHAIN, polymer, 30 residues, 3334.823 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: pBR322

Entity Sequences (FASTA):

Entity Sequences (FASTA):
INSULIN_A_CHAIN: GIVEQCCTSICSLYQLENYC N
INSULIN_B_CHAIN: FVNQHLCGSDLVEALYLVCG ERGAFYTKPT

Data sets:
Data typeCount
1H chemical shifts320

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1INSULIN A CHAIN1
2INSULIN B CHAIN2

Entities:

Entity 1, INSULIN A CHAIN 21 residues - 2383.700 Da.

1   GLYILEVALGLUGLNCYSCYSTHRSERILE
2   CYSSERLEUTYRGLNLEUGLUASNTYRCYS
3   ASN

Entity 2, INSULIN B CHAIN 30 residues - 3334.823 Da.

1   PHEVALASNGLNHISLEUCYSGLYSERASP
2   LEUVALGLUALALEUTYRLEUVALCYSGLY
3   GLUARGGLYALAPHETYRTHRLYSPROTHR

Samples:

sample: INSULIN A CHAIN 0.5-0.8 mM; INSULIN B CHAIN 0.5-0.8 mM; H2O 90%; D2O 10%; ACETIC ACID 20%

sample_conditions_1: pH: 7.4; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D TOCSYsampleisotropicsample_conditions_1
NOESYsampleisotropicsample_conditions_1
COSYsampleisotropicsample_conditions_1

Software:

X-PLOR v3.85, BRUNGER, A.T. ET AL. - refinement

VNMR_6.1B v6.1B, Varian - structure solution

NMR spectrometers:

  • VARIAN INOVA 600 MHz

Related Database Links:

BMRB 1000 1002 1004 1006 1008 1010 1012 1014 1016 1018 1020 1022 1023 11016 1344 15464 1585 1587 16026 1632 16343 16608 16663 16915 17107 1761 17803 18858 18859 18921 18923 18924 18925 19822 19978 19979 20052 20053 25260 25261 4266
PDB
DBJ BAH59081 BAJ17943 BAM29044
EMBL CAA23424 CAA23475 CAA23828 CAA43403 CAA43405
GB AAA17540 AAA19033 AAA36849 AAA59172 AAA59173
PRF 0601246A 1006230A 550086A 560164B 580107B
REF NP_000198 NP_001008996 NP_001075804 NP_001103242 NP_001123565
SP P01308 P01311 P01315 P01321 P30406
AlphaFold P01308 P01311 P01315 P01321 P30406