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- PDB-6eh7: F11 Human T-Cell Receptor specific for influenza virus haaemagglu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6eh7 | ||||||
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Title | F11 Human T-Cell Receptor specific for influenza virus haaemagglutinin epitope PKYVKQNTLKLAT carried by Human Leukocyte Antigen HLA-DR0101 | ||||||
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![]() | IMMUNE SYSTEM / Human T Cell Receptor / Human Leukocute Antigen / Influenza Haemagglutinin epitope / 3D structure | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / DI(HYDROXYETHYL)ETHER![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rizkallah, P.J. / Cole, D.K. | ||||||
![]() | ![]() Title: In Silicoand Structural Analyses Demonstrate That Intrinsic Protein Motions Guide T Cell Receptor Complementarity Determining Region Loop Flexibility. Authors: Holland, C.J. / MacLachlan, B.J. / Bianchi, V. / Hesketh, S.J. / Morgan, R. / Vickery, O. / Bulek, A.M. / Fuller, A. / Godkin, A. / Sewell, A.K. / Rizkallah, P.J. / Wells, S. / Cole, D.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.2 KB | Display | ![]() |
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PDB format | ![]() | 152.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6eh4C ![]() 6eh5C ![]() 6eh6C ![]() 6eh8C ![]() 6eh9C ![]() 6fr3C ![]() 6fr4C ![]() 6fr5C ![]() 6fr6C ![]() 6fr7C ![]() 6fr8C ![]() 6fr9C ![]() 6fraC ![]() 6frbC ![]() 6frcC ![]() 6fumC ![]() 6funC ![]() 6fuoC ![]() 6fupC ![]() 6fuqC ![]() 6furC ![]() 4gkzS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22438.043 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: AQSVTQLGSHVSVSEGALVLLRCNYSSSVPPYLFWYVQYPNQGLQLLLKYTSAATLVKGINGFEAEFKKSETSFHLTKPSAHMSDAAEYFCAVSE QDDKIIFGKGTRLHILPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIP EDTFFPS Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 27208.246 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-EDO / #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.57 Å3/Da / Density % sol: 73.09 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / Details: 25% PEG 1.5K, 100mM SPG buffer pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 13, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 1.89→46.3 Å / Num. obs: 37906 / % possible obs: 98.7 % / Redundancy: 6.5 % / Biso Wilson estimate: 28.5 Å2 / Net I/σ(I): 22.3 |
Reflection shell | Resolution: 1.89→1.94 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.706 / Mean I/σ(I) obs: 2.8 / Num. unique all: 2005 / CC1/2: 0.852 / Rrim(I) all: 0.765 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4GKZ Resolution: 1.89→46.3 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.943 / SU B: 7.141 / SU ML: 0.103 / Cross valid method: THROUGHOUT / ESU R: 0.144 / ESU R Free: 0.141 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.942 Å2
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Refinement step | Cycle: 1 / Resolution: 1.89→46.3 Å
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Refine LS restraints |
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