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1AGE

ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYRL-7R MUTATION)

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]187
Detector technologyIMAGE PLATE
Collection date1994-11-21
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths50.700, 81.200, 110.600
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution14.000 - 2.300
R-factor0.171
Rwork0.171
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)HLA B27
RMSD bond length0.011
RMSD bond angle1.600
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]14.0002.400
High resolution limit [Å]2.3002.300
Rmerge0.0880.178
Total number of observations119501

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Number of reflections25985
<I/σ(I)>7.2
Completeness [%]97.693.5
Redundancy4.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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8

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21

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Reid, S.W., (1996) Febs Lett., 383, 119.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropTris20 (mM)
31reservoirPEG400030 (%)
41reservoirsodium citrate0.1 (M)
51reservoirammonium acetate0.03 (M)

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