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- PDB-1fcc: CRYSTAL STRUCTURE OF THE C2 FRAGMENT OF STREPTOCOCCAL PROTEIN G I... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fcc | ||||||
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Title | CRYSTAL STRUCTURE OF THE C2 FRAGMENT OF STREPTOCOCCAL PROTEIN G IN COMPLEX WITH THE FC DOMAIN OF HUMAN IGG | ||||||
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![]() | COMPLEX (ANTIBODY/ANTIGEN) / COMPLEX (ANTIBODY-ANTIGEN) / COMPLEX (ANTIBODY-ANTIGEN) complex | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Sauer-Eriksson, A.E. / Kleywegt, G.J. / Uhlen, M. / Jones, T.A. | ||||||
![]() | ![]() Title: Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Authors: Sauer-Eriksson, A.E. / Kleywegt, G.J. / Uhlen, M. / Jones, T.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 101.8 KB | Display | ![]() |
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PDB format | ![]() | 80 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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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 374 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.700155, -0.700538, -0.138305), Vector ![]() Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED IN THIS ENTRY WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES OF THE OTHER MONOMERS IN THE ASYMMETRIC UNIT NOT PRESENTED IN THIS ENTRY. | |
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Components
#1: Protein | Mass: 23519.654 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein | ![]() Mass: 6157.665 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() Compound details | FIVE AMINO ACIDS DIFFER IN THEIR AMIDATION STATES AND TWO HAVE THE ALLOTYPIC MARKER: E119, M121. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.13 Å3/Da / Density % sol: 70.2 % |
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Crystal grow![]() | *PLUS Method: vapor diffusion, hanging dropDetails: Jancarik, J., (1991) J. Appl. Crystallogr., 24, 409. |
Components of the solutions | *PLUS Conc.: 10 mg/ml / Common name: protein |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 12297 / % possible obs: 72 % |
Reflection | *PLUS Highest resolution: 3.2 Å / Lowest resolution: 9999 Å / Num. measured all: 41581 / Rmerge(I) obs: 0.089 |
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Processing
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Refinement | Resolution: 3.2→8 Å
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Displacement parameters | Biso mean: 41.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 3.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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