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Open data
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Basic information
Entry | Database: PDB / ID: 1mek | ||||||
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Title | HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES | ||||||
![]() | PROTEIN DISULFIDE ISOMERASE![]() | ||||||
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Function / homology | ![]() regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / procollagen-proline 4-dioxygenase complex / interleukin-23-mediated signaling pathway / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kemmink, J. / Darby, N.J. / Dijkstra, K. / Nilges, M. / Creighton, T.E. | ||||||
![]() | ![]() Title: Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Authors: Kemmink, J. / Darby, N.J. / Dijkstra, K. / Nilges, M. / Creighton, T.E. #1: ![]() Title: Nuclear Magnetic Resonance Characterization of the N-Terminal Thioredoxin-Like Domain of Protein Disulfide Isomerase Authors: Kemmink, J. / Darby, N.J. / Dijkstra, K. / Scheek, R.M. / Creighton, T.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.5 MB | Display | ![]() |
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PDB format | ![]() | 1.4 MB | 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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NMR ensembles |
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Components
#1: Protein | ![]() Mass: 13276.909 Da / Num. of mol.: 1 / Fragment: PROLYL 4-HYDROXYLASE BETA SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow![]() | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
Refinement | Software ordinal: 1 Details: STRUCTURES WERE DETERMINED USING A HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING APPROACH (M. NILGES, G.M. CLORE, A.M. GRONENBORN, FEBS LETT. 229, 317, 1988). THE STRUCTURES ARE BASED ON 1270 ...Details: STRUCTURES WERE DETERMINED USING A HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING APPROACH (M. NILGES, G.M. CLORE, A.M. GRONENBORN, FEBS LETT. 229, 317, 1988). THE STRUCTURES ARE BASED ON 1270 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 34 HYDROGEN BOND DISTANCE RESTRAINTS DERIVED FROM 17 SLOWLY EXCHANGING AMIDE PROTONS AND OBSERVED NOE PATTERNS; AND 5 DISTANCE RESTRAINTS WHICH DEFINE THE DISULFIDE BOND BETWEEN CYS 36 AND CYS 39. | ||||||||||||
NMR ensemble | Conformers submitted total number: 40 |