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- PDB-2bf1: Structure of an unliganded and fully-glycosylated SIV gp120 envel... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bf1 | ||||||||||||
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Title | Structure of an unliganded and fully-glycosylated SIV gp120 envelope glycoprotein | ||||||||||||
![]() | EXTERIOR MEMBRANE GLYCOPROTEIN GP120 | ||||||||||||
![]() | VIRUS PROTEIN / SIV / GP120 / ENVELOPE GLYCOPROTEIN / AIDS / COAT PROTEIN | ||||||||||||
Function / homology | ![]() membrane fusion involved in viral entry into host cell / host cell endosome membrane / symbiont entry into host cell / viral envelope / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Chen, B. / Vogan, E.M. / Gong, H. / Skehel, J.J. / Wiley, D.C. / Harrison, S.C. | ||||||||||||
![]() | ![]() Title: Structure of an Unliganded Simian Immunodeficiency Virus Gp120 Core Authors: Chen, B. / Vogan, E.M. / Gong, H. / Skehel, J.J. / Wiley, D.C. / Harrison, S.C. #1: Journal: Structure / Year: 2005 Title: Determining the Structure of the Unliganded and Fully-Glycosylated Siv Gp120 Envelope Glycoprotein. Authors: Chen, B. / Vogan, E.M. / Gong, H. / Skehel, J.J. / Wiley, D.C. / Harrison, S.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 | ![]() | 90.8 KB | Display | ![]() |
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PDB format | ![]() | 74.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.1 MB | Display | ![]() |
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Full document | ![]() | 3.1 MB | Display | |
Data in XML | ![]() | 23.2 KB | Display | |
Data in CIF | ![]() | 29.9 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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Unit cell |
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Details | ALTHOUGH THIS ENTRY DESCRIBES THE MONOMERIC STRUCTURE OFGP120, A THEORETICAL MODEL OF THE TRIMERIC FORM OF THEPROTEIN HAS BEEN GENERATED. THE DETAILS OF THE TRIMER ANDTHE MATRICES RELATING CHAIN A OF THIS ENTRY TO THECONSTITUENTS OF THE TRIMERIC STRUCTURE CAN BE FOUND INREMARK 400 BELOW. |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 36833.723 Da / Num. of mol.: 1 / Fragment: GP120 CORE, RESIDUES 66-109,209-311,342-502 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 8 types, 13 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #6: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Polysaccharide | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #8: Polysaccharide | alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #9: Sugar | |
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-Details
Compound details | GP120 IS PRODUCED FROM A PRECURSOR PROTEIN, GP160. THE PRECURSOR ASSEMBLES INTO A TRIMER, WHICH ...GP120 IS PRODUCED FROM A PRECURSOR PROTEIN, GP160. THE PRECURSOR ASSEMBLES INTO A TRIMER, WHICH REMAINS INTACT AFTER CLEAVAGE OF GP160 TO GP120 AND GP41. A THEORETICA |
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Sequence details | IN THE EXPRESSION CONSTRUCT, SHORT LINKERS, GAG HAVE BEEN SUBSTITUTED FOR THE V1V2 AND V3 LOOPS. ...IN THE EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 68.8 % |
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Crystal grow | Temperature: 293 K / pH: 5 Details: PROTEIN WAS CRYSTALLIZED FROM 15% PEG 6000, 100 MM SODIUM CITRATE, PH 5.0 AND 8% PEG 400 AT 20 DEGREES C. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 7, 2002 / Details: RH-COATED SI MIRROR |
Radiation | Monochromator: BENT TRIANGULAR ASYMMETRIC CUT SI(111) MONOCHROMATER Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.916 Å / Relative weight: 1 |
Reflection | Resolution: 4→26 Å / Num. obs: 100402 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Biso Wilson estimate: 141.1 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12 |
Reflection shell | Resolution: 4→4.09 Å / Redundancy: 4 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 1.3 / % possible all: 94.3 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: MAXIMUM LIKELIHOODWITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. PLEASE NOTE THAT BECAUSE OF THE LOW RESOLUTION OF THE EXPERIMENTAL DATA USED TO DETERMINE THIS STRUCTURE, THE PRECISION OF THE MODEL, ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. PLEASE NOTE THAT BECAUSE OF THE LOW RESOLUTION OF THE EXPERIMENTAL DATA USED TO DETERMINE THIS STRUCTURE, THE PRECISION OF THE MODEL, PARTICULARLY WITH RESPECT TO SIDE CHAIN POSITIONS, IS REDUCED.
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Solvent computation | Ion probe radii: 3 Å / Shrinkage radii: 2.8 Å / VDW probe radii: 3 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 128.8 Å2
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Refinement step | Cycle: LAST / Resolution: 4→26 Å
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Refine LS restraints |
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