BMRBj - BMREntryMaster

Found 1 Document (1.236 seconds)

BMRB: 16343

8ONP

NMR STRUCTURE OF HUMAN INSULIN MUTANT GLU-B21-D-GLU, HIS-B10 ASP PRO-B28-LYS, LYS-B29-PRO, 20 STRUCTURES

Authors

Hua, Q.X., Huang, K., Hu, S.Q., Katsoyanni, P., Weiss, M.A.

Assembly

INSULIN A CHAIN, INSULIN B CHAIN

Entity

1. INSULIN A CHAIN (polymer, Thiol state: all disulfide bound), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N

2. INSULIN B CHAIN (polymer, Thiol state: all disulfide bound), 30 monomers, 3407.868 Da Detail

FVNQHLCGSD LVEALYLVCG XRGFFYTKPT

Total weight

5791.564 Da

Max. entity weight

3407.868 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.1 %, Completeness: 91.5 %, Completeness (bb): 87.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	91.5 % (269 of 294)	91.5 % (269 of 294)
Backbone	87.4 % (90 of 103)	87.4 % (90 of 103)
Sidechain	93.7 % (179 of 191)	93.7 % (179 of 191)
Aromatic	87.9 % (29 of 33)	87.9 % (29 of 33)
Methyl	100.0 % (28 of 28)	100.0 % (28 of 28)

1. INSULIN A CHAIN

GIVEQCCTSI CSLYQLENYC N

2. INSULIN B CHAIN

FVNQHLCGSD LVEALYLVCG XRGFFYTKPT

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1.0 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	INSULIN A CHAIN	natural abundance	0.5 mM
2	INSULIN B CHAIN	natural abundance	0.5 mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

Release date

2010-05-18

Citation

An Achilles' heel in an amyloidogenic protein and its repair: insulin fibrillation and therapeutic design
Yang, Y., Petkova, A., Huang, K., Xu, B., Hua, Q., Ye, I., Chu, Y., Hu, S., Phillips, N.B., Whittaker, J., Ismail-Beigi, F., Mackin, R.B., Katsoyannis, P.G., Tycko, R., Weiss, M.A.
J. Biol. Chem. (2010), 285, 10806-10821, PubMed 20106984 , DOI 10.1074/jbc.M109.067850 , Abstract

Related entities 1. INSULIN A CHAIN, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. INSULIN B CHAIN, : 1 : 117 : 101 entities Detail

Interaction partners 1. INSULIN A CHAIN, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. INSULIN B CHAIN, : 6 : 1 interactors Detail

More details for 7 interactors identified by 7 citations

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr16343_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
2	21	DGL	D-GLUTAMIC ACID	Assigned chemical shifts

Content subtype: bmr16343_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	332		95.2 (chain: 1, length: 21), 96.7 (chain: 2, length: 30)
1	Chemical shift references	chemical_shift_reference_1	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 21, Sequence coverage: 95.2%
  - Entity_assembly_ID: 2, Chain length: 30, Sequence coverage: 96.7%
- Total number of assignments
  - ¹H chemical shifts: 332
- Completeness of assignments
  - Entity_assemble_ID: 1
  - Entity_assemble_ID: 2
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
  - Chain_ID: 2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	110	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	36	83.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	74	96.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	11	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0

Comp_index_ID	Comp_ID
21	DGL

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	174	160	92.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	55	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	114	105	92.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	25	21	84.0

Keywords FIBRILLATION, HORMONE, HUMAN INSULIN, MUTANT, STABILITY

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Found 1 Document (1.236 seconds)

BMRB: 16343

Sample

Related entities 1. INSULIN A CHAIN, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. INSULIN B CHAIN, : 1 : 117 : 101 entities Detail

Interaction partners 1. INSULIN A CHAIN, : 1 : 1 interactors Detail

Interaction partners 2. INSULIN B CHAIN, : 6 : 1 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail