BMRB Entry 16343

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16343

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Title:
NMR STRUCTURE OF HUMAN INSULIN MUTANT GLU-B21-D-GLU, HIS-B10 ASP PRO-B28-LYS, LYS-B29-PRO, 20 STRUCTURES
Deposition date:
2009-06-10
Original release date:
2010-05-19
Authors:
Hua, Q.; Huang, K.; Hu, S.; Katsoyanni, P.; Weiss, M.
Citation:

Citation: Yang, Yanwu; Petkova, Aneta; Huang, Kun; Xu, Bin; Hua, Qing-Xin; Ye, I-Ju; Chu, Ying-Chi; Hu, Shi-Quan; Phillips, Nelson; Whittaker, Jonathan; Ismail-Beigi, Faramarz; Mackin, Robert; Katsoyannis, Panayotis; Tycko, Robert; Weiss, Michael. "An Achilles' heel in an amyloidogenic protein and its repair: insulin fibrillation and therapeutic design."  J. Biol. Chem. 285, 10806-10821 (2010).
PubMed: 20106984

Assembly members:

Assembly members:
INSULIN_A_CHAIN, polymer, 21 residues, 2383.700 Da.
INSULIN_B_CHAIN, polymer, 30 residues, 3410.921 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: chemical synthesis

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
1H chemical shifts332

Additional metadata:

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

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 - 3410.921 Da.

1   PHEVALASNGLNHISLEUCYSGLYSERASP
2   LEUVALGLUALALEUTYRLEUVALCYSGLY
3   DGLARGGLYPHEPHETYRTHRLYSPROTHR

Samples:

sample_1: INSULIN A CHAIN 0.5 mM; INSULIN B CHAIN 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 mM; pH: 7.0; pressure: 1.0 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 mM; pH: 2.0; pressure: 1.0 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.1 mM; pH: 7.6; pressure: 1.0 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D TOCSYsample_1isotropicsample_conditions_1
NOESYsample_1isotropicsample_conditions_1
COSYsample_1isotropicsample_conditions_1

Software:

X-PLOR v3.85, BRUNGER - refinement

xwinnmr v3.5, Bruker Biospin - structure solution

NMR spectrometers:

  • BRUKER DRX 700 MHz

Related Database Links:

BMRB 1000 1002 1004 1006 1008 1010 1012 1014 1016 1018 1020 1022 1023 11016 1344 15464 1585 1587 16026 16027 1632 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