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- PDB-1k3m: NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-ALA, HIS-B10-ASP, PR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1k3m | ||||||
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Title | NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-ALA, HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES | ||||||
![]() | (INSULIN![]() | ||||||
![]() | HORMONE/GROWTH FACTOR / ![]() ![]() ![]() | ||||||
Function / homology | ![]() negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / nitric oxide-cGMP-mediated signaling / IRS activation / Insulin processing / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Method | ![]() ![]() | ||||||
![]() | Xu, B. / Hua, Q.-X. / Nakagawa, S.H. / Jia, W. / Chu, Y.-C. / Katsoyannis, P.G. / Weiss, M.A. | ||||||
![]() | ![]() Title: A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix. Authors: Xu, B. / Hua, Q.X. / Nakagawa, S.H. / Jia, W. / Chu, Y.C. / Katsoyannis, P.G. / Weiss, M.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 226.9 KB | Display | ![]() |
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PDB format | ![]() | 196 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | ![]() Mass: 2341.618 Da / Num. of mol.: 1 / Fragment: INSULIN A CHAIN (residues 90-110) / Mutation: I2A / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human). References: UniProt: P01308 |
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#2: Protein/peptide | ![]() Mass: 3410.894 Da / Num. of mol.: 1 / Fragment: INSULIN B CHAIN (residues 25-54) / Mutation: H10D, P28K, K29P / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human). References: UniProt: P01308 |
-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
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Sample preparation
Details |
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Sample conditions |
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Crystal grow![]() | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model![]() |
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Processing
NMR software |
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Refinement | Method: distance geometry, ![]() Details: The structure is based on a total of 416 restraints, 367 are NOE-derived distance constraints, 32 dihedral angle restraints, 17 distance restraints from hydrogen bonds. | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 15 |