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- PDB-2clr: THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2clr | ||||||
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Title | THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE | ||||||
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Function / homology | ![]() Calnexin/calreticulin cycle / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Collins, E.J. / Garboczi, D.N. / Wiley, D.C. | ||||||
![]() | ![]() Title: Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Authors: Collins, E.J. / Garboczi, D.N. / Wiley, D.C. #1: ![]() Title: Five Viral Peptide-Hla-A2 Co-Crystals: Simultaneous Space Group Determination and X-Ray Data Collection Authors: Garboczi, D.N. / Madden, D.R. / Wiley, D.C. #2: ![]() Title: Comparison of the P2 Specificity Pocket in Three Human Histocompatibility Antigens: Hla-A(Asterisk)6801, Hla-A(Asterisk)0201, and Hla-B(Asterisk)2705 Authors: Guo, H.-C. / Madden, D.R. / Silver, M.L. / Jardetzky, T.S. / Gorga, J.C. / Strominger, J.L. / Wiley, D.C. #3: ![]() Title: The Antigenic Identity of Peptide-Mhc Complexes a Comparison of the Conformations of Five Viral Peptides Presented by Hla-A2 Authors: Madden, D.R. / Garboczi, D.N. / Wiley, D.C. #4: ![]() Title: Hla-A2-Peptide Complexes: Refolding and Crystallization of Molecules Expressed in Escherichia Coli and Complexed with Single Antigenic Peptides Authors: Garboczi, D.N. / Hung, D.T. / Wiley, D.C. #5: ![]() Title: Refined Structure of the Human Histocompatibility Antigen Hla-A2 at 2.6 Angstroms Resolution Authors: Saper, M.A. / Bjorkman, P.J. / Wiley, D.C. #6: ![]() Title: Structure of the Human Class I Histocompatibility Antigen, Hla-A2 Authors: Bjorkman, P.J. / Saper, M.A. / Samraoui, B. / Bennett, W.S. / Strominger, J.L. / Wiley, D.C. #7: ![]() Title: The Foreign Antigen Binding Site and T Cell Recognition Regions of Class I Histocompatibility Antigens Authors: Bjorkman, P.J. / Saper, M.A. / Samraoui, B. / Bennett, W.S. / Strominger, J.L. / Wiley, D.C. #8: ![]() Title: Crystallization and X-Ray Diffraction Studies on the Histocompatibility Antigens Hla-A2 and Hla-A28 from Human Cell Membranes Authors: Bjorkman, P.J. / Strominger, J.L. / Wiley, D.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 160.3 KB | Display | ![]() |
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PDB format | ![]() | 129.3 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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2 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 210 / 2: CIS PROLINE - PRO B 32 / 3: CIS PROLINE - PRO D 210 / 4: CIS PROLINE - PRO E 32 | ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES AS FOLLOWS: MTRIX 1: APPLIED TO CHAIN D RESIDUES 1 - 183, APPROXIMATELY GENERATES CHAIN A RESIDUES 1 - 183 MTRIX 1: APPLIED TO CHAIN F RESIDUES 1 - 10, APPROXIMATELY GENERATES CHAIN C RESIDUES 1 - 10 MTRIX 2: APPLIED TO CHAIN D RESIDUES 184 - 275, APPROXIMATELY GENERATES CHAIN A RESIDUES 184 - 275 MTRIX 3: APPLIED TO CHAIN E RESIDUES 1 - 99, APPROXIMATELY GENERATES CHAIN B RESIDUES 1 - 99 |
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Components
#1: Protein | Mass: 31854.203 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein | ![]() Mass: 11879.356 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #3: Protein/peptide | Mass: 1055.375 Da / Num. of mol.: 2 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 | Density Matthews: 2.51 Å3/Da / Density % sol: 50.92 % | ||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Method: vapor diffusion / PH range low: 6.5 / PH range high: 6.2 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.9 Å / Rmerge(I) obs: 0.054 |
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Reflection shell | *PLUS Highest resolution: 2.07 Å / Lowest resolution: 2.16 Å / Rmerge(I) obs: 0.205 |
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Processing
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Refinement | Resolution: 2→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |