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Yorodumi- PDB-1igm: THREE DIMENSIONAL STRUCTURE OF AN FV FROM A HUMAN IGM IMMUNOGLOBULIN -
+Open data
-Basic information
Entry | Database: PDB / ID: 1igm | ||||||
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Title | THREE DIMENSIONAL STRUCTURE OF AN FV FROM A HUMAN IGM IMMUNOGLOBULIN | ||||||
Components |
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Keywords | IMMUNOGLOBULIN | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / : Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Fan, Z.-C. / Guddat, L.W. / Edmundson, A.B. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Three-dimensional structure of an Fv from a human IgM immunoglobulin. Authors: Fan, Z.C. / Shan, L. / Guddat, L.W. / He, X.M. / Gray, W.R. / Raison, R.L. / Edmundson, A.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1igm.cif.gz | 57 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1igm.ent.gz | 44.7 KB | Display | PDB format |
PDBx/mmJSON format | 1igm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1igm_validation.pdf.gz | 373.6 KB | Display | wwPDB validaton report |
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Full document | 1igm_full_validation.pdf.gz | 384 KB | Display | |
Data in XML | 1igm_validation.xml.gz | 7.7 KB | Display | |
Data in CIF | 1igm_validation.cif.gz | 11.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ig/1igm ftp://data.pdbj.org/pub/pdb/validation_reports/ig/1igm | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-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: RESIDUES 8 AND 95 OF L CHAIN ARE CIS PROLINES. |
-Components
#1: Antibody | Mass: 12470.749 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: GenBank: 5524145 |
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#2: Antibody | Mass: 13789.396 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.24 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20-22 ℃ / pH: 6.8 / Method: vapor diffusion, hanging drop / Details: seeding | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 9999 Å / Num. all: 10089 / Num. obs: 8539 / % possible obs: 84.6 % / Observed criterion σ(I): 0.5 / Num. measured all: 30357 / Rmerge(I) obs: 0.0695 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.201 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 8 Å / Num. reflection obs: 8225 / Rfactor obs: 0.201 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |