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- PDB-1afo: DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1afo | ||||||
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Title | DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES | ||||||
![]() | GLYCOPHORIN A | ||||||
![]() | INTEGRAL MEMBRANE PROTEIN / HUMAN GLYCOPHORIN A / TRANSMEMBRANE HELIX INTERACTIONS / MEMBRANE PROTEIN FOLDING | ||||||
Function / homology | ![]() ankyrin-1 complex / Cell surface interactions at the vascular wall / virus receptor activity / nucleoplasm / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING HYBRID | ||||||
![]() | Mackenzie, K.R. / Prestegard, J.H. / Engelman, D.M. | ||||||
![]() | ![]() Title: A transmembrane helix dimer: structure and implications. Authors: MacKenzie, K.R. / Prestegard, J.H. / Engelman, D.M. #1: ![]() Title: Structure Determination of the Dimeric Membrane Spanning Domain of Glycophorin a in Detergent Micelles by Triple Resonance Nuclear Magnetic Resonance Spectroscopy Authors: Mackenzie, K.R. #2: ![]() Title: Leucine Side-Chain Rotamers in a Glycophorin a Transmembrane Peptide as Revealed by Three-Bond Carbon-Carbon Couplings and 13C Chemical Shifts Authors: Mackenzie, K.R. / Prestegard, J.H. / Engelman, D.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 575.3 KB | Display | ![]() |
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PDB format | ![]() | 493.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.1 KB | Display | ![]() |
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Full document | ![]() | 587 KB | Display | |
Data in XML | ![]() | 37.3 KB | Display | |
Data in CIF | ![]() | 59 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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/peptide | Mass: 4454.414 Da / Num. of mol.: 2 / Fragment: TRANSMEMBRANE PEPTIDE Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6.0 / Temperature: 313 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
Software |
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NMR software |
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Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING HYBRID / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATIONS / Conformers calculated total number: 38 / Conformers submitted total number: 20 |