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Experiments 39 - 71 as of March 19, 2014

Experiment Status Navigation

1 - 18 / 19 - 38 / 39 - 71 / 72 - 102 / 103 - 120 / 121 - 166

Corresponding Batches
1-3702 / 4000-26810 / 26811-97214 / 97215-281070 / 281071-552394 / 552395-908573

Experiments 52-71: 100% completed

Experiments 52 to 71 = AD Vina Exp. 11 to 30, 100% completed

Experiments 52 through 71 (AD Vina Experiments 11 to 30) target the three allosteric sites of HIV reverse transcriptase as well as the known non-nucleoside reverse trasciptase inhibitor (NNRTI) site. These experiments involve screening 5 large libraries (Full NCI, Enamine, ChemBridge, Asinex and Vitas-M) with AD Vina against several crystal structures and molecular dynamics (MD) snapshots from the McCammon Lab, UCSD. Among the crystal structures are those from our collaborators in the Arnold Lab. The MD snapshots were graciously provided by Sara Nichols, from simulations on PDB 1VRT (see the supporting information of Predictive Power of Molecular Dynamics Receptor Structures in Virtual Screening by Nichols et. al.). Positive control dockings were first performed to choose appropriate MD snapshots for each target. While performing these initial studies, different docking parameters were tested involving placement of the docking bounding box in which docking calculations are performed.

Experiment summary by site:

  • Exp. 52 - 56: incoming nucleotide binding site (INuB) of HIV-1 Reverse Transcriptase (RT)
  • Exp. 57 - 61: knuckles binding site (KNUC) of HIV-1 Reverse Transcriptase (RT)
  • Exp. 62 - 66: NNRTI adjacent site (NNRTIadj) of HIV-1 Reverse Trascriptase (RT)
  • Exp. 67 - 71: NNRTI binding site (NNRTI site) of HIV-1 Reverse Transcriptase (RT)

    TARGET: Incoming Nucleotide Binding Site (INuB) of HIV-1 Reverse Transcriptase (RT)
    AD Exp. 52
    Vina Exp. 11
    AD Exp. 53
    Vina Exp. 12
    AD Exp. 54
    Vina Exp. 13
    AD Exp. 55
    Vina Exp. 14
    AD Exp. 56
    Vina Exp. 15
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    MD snapshot uc1_frame_96363526 - 6355764006 - 6424067531 - 6763269061 - 6911169826 - 69976
    MD snapshot apa_frame_163363558 - 6358964241 - 6447567633 - 6773469112 - 6916269977 - 70127
    MD snapshot apa_frame_159863590 - 6362164476 - 6471067735 - 6783669163 - 6921370128 - 70278
    MD snapshot apa_frame_169363622 - 6365364711 - 6494567837 - 6793869214 - 6926470279 - 70429
    MD snapshot apa_frame_164963654 - 6368564946 - 6518067939 - 6804069265 - 6931570430 - 70580
    MD snapshot uc1_frame_45563686 - 6371765181 - 6541568041 - 6814269316 - 6936670581 - 70731
    MD snapshot uc1_frame_124163718 - 6374965416 - 6565068143 - 6824469367 - 6941770732 - 70882
    MD snapshot uc1_frame_119863750 - 6378165651 - 6588568245 - 6834669418 - 6946870883 - 71033
    PDB 1VRU, w/NNRTI*63782 - 6381365886 - 6612068347 - 6844869469 - 6951971034 - 71184
    PDB 1VRU, w/out NNRTI*63814 - 6384566121 - 6635568449 - 6855069520 - 6957071185 - 71335
    PDB 2ZD1, w/out NNRTI*63846 - 6387766356 - 6659068551 - 6865269571 - 6962171336 - 71486
    PDB 4ICL, w/out NNRTI*63878 - 6390966591 - 6682568653 - 6875469622 - 6967271487 - 71637
    PDB 4ICL, w/NNRTI*63910 - 6394166826 - 6706068755 - 6885669673 - 6972371638 - 71788
    PDB 4KFB, w/out NNRTI*63942 - 6397367061 - 6729568857 - 6895869724 - 6977471789 - 71939
    PDB 4KFB, w/NNRTI*63974 - 6400567296 - 6753068959 - 6906069775 - 6982571940 - 72090
    COMPLETION100%100%100%100%100%
    *"NNRTI" is non-nucleoside HIV reverse transcriptase inhibitor.



    TARGET: Knuckles Binding Site (KNUC) of HIV-1 Reverse Transcriptase (RT)
    AD Exp. 57
    AD Vina Exp. 16
    AD Exp. 58
    AD Vina Exp. 17
    AD Exp. 59
    AD Vina Exp. 18
    AD Exp. 60
    AD Vina Exp. 19
    AD Exp. 61
    AD Vina Exp. 20
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    MD snapshot apa_frame_170172091 - 7212272411 - 7264574761 - 7486275781 - 7583176291 - 76441
    MD snapshot apa_frame_1702 72123 - 7215472646 - 7288074863 - 7496475832 - 7588276442 - 76592
    PDB 1FK9, w/NNRTI* 72155 - 7218672881 - 7311574965 - 7506675883 - 7593376593 - 76743
    PDB 1FK9, w/out NNRTI* 72187 - 7221873116 - 7335075067 - 7516875934 - 7598476744 - 76894
    PDB 4IFY, w/out NNRTI*
    [KNUC and INuB sites centered]
    72219 - 7225073351 - 7358575169 - 7527075985 - 7603576895 - 77045
    PDB 4IFY, w/out NNRTI*
    [KNUC site centered]
    72251 - 7228273586 - 7382075271 - 7537276036 - 7608677046 - 77196
    PDB 4IFY, w/NNRTI*
    [KNUC and INuB sites centered]
    72283 - 7231473821 - 7405575373 - 7547476087 - 7613777197 - 77347
    PDB 4KFB, w/out NNRTI*
    [KNUC and INuB sites centered]
    72315 - 7234674056 - 7429075475 - 7557676138 - 7618877348 - 77498
    PDB 4KFB, w/out NNRTI*
    [KNUC site centered]
    72347 - 7237874291 - 7452575577 - 7567876189 - 7623977499 - 77649
    PDB 4KFB, w/NNRTI*
    [KNUC and INuB sites centered]
    72379 - 7241074526 - 7476075679 - 7578076240 - 7629077650 - 77800
    COMPLETION100%100%100%100%100%
    *"NNRTI" is non-nucleoside HIV reverse transcriptase inhibitor.



    TARGET: NNRTI Adjacent Site (NNRTIadj) of HIV-1 Reverse Transcriptase (RT)
    AD Exp. 62
    AD Vina Exp. 21
    AD Exp. 63
    AD Vina Exp. 22
    AD Exp. 64
    AD Vina Exp. 23
    AD Exp. 65
    AD Vina Exp. 24
    AD Exp. 66
    AD Vina Exp. 25
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    PDB 2ZD1, w/NNRTI*77801 - 7783277897 - 7813178602 - 7870378908 - 7895879061 - 79211
    PDB 4IFY, w/NNRTI*77833 - 7786478132 - 7836678704 - 7880578959 - 7900979212 - 79362
    PDB 4KFB, w/NNRTI*77865 - 7789678367 - 7860178806 - 7890779010 - 7906079363 - 79513
    COMPLETION100%100%100%100%100%
    *"NNRTI" is non-nucleoside HIV reverse transcriptase inhibitor.



    TARGET: NNRTI Site of HIV-1 Reverse Transcriptase (RT)
    AD Exp. 67
    AD Vina Exp. 26
    AD Exp. 68
    AD Vina Exp. 27
    AD Exp. 69
    AD Vina Exp. 28
    AD Exp. 70
    AD Vina Exp. 29
    AD Exp. 71
    AD Vina Exp. 30
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    MD snapshot uc1_frame_963 79514 - 7954580506 - 8074087791 - 8789290953 - 9100392534 - 92684
    MD snapshot uc1_frame_209 79546 - 7957780741 - 8097587893 - 8799491004 - 9105492685 - 92835
    MD snapshot uc1_frame_1452 79578 - 7960980976 - 8121087995 - 8809691055 - 9110592836 - 92986
    MD snapshot apa_frame_1701 79610 - 7964181211 - 8144588097 - 8819891106 - 9115692987 - 93137
    MD snapshot uc1_frame_1781 79642 - 7967381446 - 8168088199 - 8830091157 - 9120793138 - 93288
    MD snapshot uc1_frame_326 79674 - 7970581681 - 8191588301 - 8840291208 - 9125893289 - 93439
    MD snapshot uc1_frame_63 79706 - 7973781916 - 8215088403 - 8850491259 - 9130993440 - 93590
    MD snapshot uc1_frame_693 79738 - 7976982151 - 8238588505 - 8860691310 - 9136093591 - 93741
    MD snapshot uc1_frame_1076 79770 - 7980182386 - 8262088607 - 8870891361 - 9141193742 - 93892
    MD snapshot uc1_frame_978 79802 - 7983382621 - 8285588709 - 8881091412 - 9146293893 - 94043
    MD snapshot uc1_frame_1038 79834 - 7986582856 - 8309088811 - 8891291463 - 9151394044 - 94194
    MD snapshot apa_frame_1301 79866 - 7989783091 - 8332588913 - 8901491514 - 9156494195 - 94345
    MD snapshot uc1_frame_205 79898 - 7992983326 - 8356089015 - 8911691565 - 9161594346 - 94496
    MD snapshot apa_frame_1845 79930 - 7996183561 - 8379589117 - 8921891616 - 9166694497 - 94647
    MD snapshot uc1_frame_1062 79962 - 7999383796 - 8403089219 - 8932091667 - 9171794648 - 94798
    MD snapshot uc1_frame_455 79994 - 8002584031 - 8426589321 - 8942291718 - 9176894799 - 94949
    MD snapshot uc1_frame_128 80026 - 8005784266 - 8450089423 - 8952491769 - 9181994950 - 95100
    MD snapshot uc1_frame_572 80058 - 8008984501 - 8473589525 - 8962691820 - 9187095101 - 95251
    MD snapshot uc1_frame_653 80090 - 8012184736 - 8497089627 - 8972891871 - 9192195252 - 95402
    MD snapshot apa_frame_1628 80122 - 8015384971 - 8520589729 - 8983091922 - 9197295403 - 95553
    MD snapshot uc1_frame_1198 80154 - 8018585206 - 8544089831 - 8993291973 - 9202395554 - 95704
    PDB 1BQM 80186 - 8021785441 - 8567589933 - 9003492024 - 9207495705 - 95855
    PDB 1EP4 80218 - 8024985676 - 8591090035 - 9013692075 - 9212595856 - 96006
    PDB 1FK9 80250 - 8028185911 - 8614590137 - 9023892126 - 9217696007 - 96157
    PDB 1KLM 80282 - 8031386146 - 8638090239 - 9034092177 - 9222796158 - 96308
    PDB 1RT1 80314 - 8034586381 - 8661590341 - 9044292228 - 9227896309 - 96459
    PDB 1RT4 80346 - 8037786616 - 8685090443 - 9054492279 - 9232996460 - 96610
    PDB 1VRT 80378 - 8040986851 - 8708590545 - 9064692330 - 9238096611 - 96761
    PDB 1VRU 80410 - 8044187086 - 8732090647 - 9074892381 - 9243196762 - 96912
    PDB 2ZD1 80442 - 8047387321 - 8755590749 - 9085092432 - 9248296913 - 97063
    PDB 4IFY 80474 - 8050587556 - 8779090851 - 9095292483 - 9253397064 - 97214
    COMPLETION100%99.9%99.9%100%100%

    Experiments 47-51: 100% completed

    Experiments 47 to 51 = AD Vina Exp. 6 to 10, 100% completed

    Experiments 47 through 51 (that is, AD Vina Experiments 6 to 10) target the three recently-discovered allosteric sites of HIV integrase. These experiments involve screening ~ 5.6 million compounds against 30 models of different crystal structures of HIV integrase (or "IN"). Each of these crystal structures (3-D, atomically-detailed maps of the location of all of the atoms of the protein) involved an allosteric inhibitor bound to at least one of these three allosteric sites (but some of these allosteric inhibitors were fragments that bound to two or three of these different allosteric sites simultaneously). Thus, we are screening compounds against allosteric-inhibitor-induced conformations (or shapes) of HIV integrase.

    HIV integrase is one of the three viral enzymes that must work properly in order for HIV to replicate itself and spread. Specifically, HIV integrase processes and then permanently attaches (or "integrates") the viral cDNA into the human genomic DNA of the cells that HIV infects.

    To learn what "allosteric inhibitors are," see page 4 of Volume 11 of our FightAIDS@Home Newsletter.

    In these 5 experiments with AD Vina, we will search for new compounds that can bind to at least one of the three allosteric sites of HIV integrase, which are called the LEDGF site, the FBP Site (for Fragment Binding Pocket), or the Y3 site (which is adjacent to the region underneath the "140s loop"). To learn more about these allosteric sites on the catalytic core domain of HIV integrase, see this paper by the Deadman group, this paper by the Scanlon group, this newer paper by the Scanlon group, or see this paper by Alan Engelman, Jacques J. Kessl, and Mamuka Kvaratskhelia.

    The Engelman and Kvaratskhelia labs, and several other labs at 6 different institutions around the country, recently started collaborating with the Olson lab, as part of the new NIH-funded Center called the "HIVE."

    TARGET: FBP, LEDGF, and Y3 Sites of IN
    AD Exp. 47
    AD Vina Exp. 6
    AD Exp. 48
    AD Vina Exp. 7
    AD Exp. 49
    AD Vina Exp. 8
    AD Exp. 50
    AD Vina Exp. 9
    AD Exp. 51
    AD Vina Exp. 10
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    FBP allosteric site of IN from PDB 3AO146396-4642747356-4759054406-5450757466-5751658996-59146
    FBP allosteric site of IN from PDB 3AO246428-4645947591-4782554508-5460957517-5756759147-59297
    FBP allosteric site of IN from PDB 3NF8_B46460-4649147826-4806054610-5471157568-5761859298-59448
    FBP allosteric site of IN from PDB 3VQ446492-4652348061-4829554712-5481357619-5766959449-59599
    FBP allosteric site of IN from PDB 3VQ5_A46524-4655548296-4853054814-5491557670-5772059600-59750
    FBP allosteric site of IN from PDB 3VQ746556-4658748531-4876554916-5501757721-5777159751-59901
    FBP allosteric site of IN from PDB 3VQA46588-4661948766-4900055018-5511957772-5782259902-60052
    FBP allosteric site of IN from PDB 3VQD46620-4665149001-4923555120-5522157823-5787360053-60203
    FBP allosteric site of IN from PDB 3VQE_A46652-4668349236-4947055222-5532357874-5792460204-60354
    FBP allosteric site of IN from PDB 4AHR_A46684-4671549471-4970555324-5542557925-5797560355-60505
    LEDGF allosteric site of IN from PDB 3NF6_A46716-4674749706-4994055426-5552757976-5802660506-60656
    LEDGF allosteric site of IN from PDB 3NF8_A46748-4677949941-5017555528-5562958027-5807760657-60807
    LEDGF allosteric site of IN from PDB 3VQ8_B46780-4681150176-5041055630-5573158078-5812860808-60958
    LEDGF allosteric site of IN from PDB 3ZCM_A46812-4684350411-5064555732-5583358129-5817960959-61109
    LEDGF allosteric site of IN from PDB 3ZSO_B46844-4687550646-5088055834-5593558180-5823061110-61260
    LEDGF allosteric site of IN from PDB 3ZSW_B46876-4690750881-5111555936-5603758231-5828161261-61411
    LEDGF allosteric site of IN from PDB 3ZT1_A46908-4693951116-5135056038-5613958282-5833261412-61562
    LEDGF allosteric site of IN from PDB 3ZT2_A46940-4697151351-5158556140-5624158333-5838361563-61713
    LEDGF allosteric site of IN from PDB 3ZT3_A46972-4700351586-5182056242-5634358384-5843461714-61864
    LEDGF allosteric site of IN from PDB 3ZT4_B47004-4703551821-5205556344-5644558435-5848561865-62015
    Y3 allosteric site of IN from PDB 3NF6_A47036-4706752056-5229056446-5654758486-5853662016-62166
    Y3 allosteric site of IN from PDB 3NF6_B47068-4709952291-5252556548-5664958537-5858762167-62317
    Y3 allosteric site of IN from PDB 3NF7_A47100-4713152526-5276056650-5675158588-5863862318-62468
    Y3 allosteric site of IN from PDB 3NF7_B47132-4716352761-5299556752-5685358639-5868962469-62619
    Y3 allosteric site of IN from PDB 3NF8_A47164-4719552996-5323056854-5695558690-5874062620-62770
    Y3 allosteric site of IN from PDB 3NF8_B47196-4722753231-5346556956-5705758741-5879162771-62921
    Y3 allosteric site of IN from PDB 3NF9_A47228-4725953466-5370057058-5715958792-5884262922-63072
    Y3 allosteric site of IN from PDB 3NF9_B47260-4729153701-5393557160-5726158843-5889363073-63223
    Y3 allosteric site of IN from PDB 3NFA_A47292-4732353936-5417057262-5736358894-5894463224-63374
    Y3 allosteric site of IN from PDB 3NFA_B47324-4735554171-5440557364-5746558945-5899563375-63525
    COMPLETION100%100%100%100%100%



    Experiments 42-46: 100% completed

    Experiments 42 to 46 = AD Vina Exp. 1 to 5, 100% completed

    Experiments 42 through 46 (that is, AD Vina Experiments 1 to 5) involve screening ~ 5.6 million compounds against two models of a recently-discovered allosteric site of HIV reverse transcriptase. Reverse transcriptase (or "RT") is one of the three viral enzymes that must work properly in order for HIV to replicate itself and spread. These are the first FightAIDS@Home experiments that target the RT system.

    To learn what "allosteric inhibitors are," see page 4 of Volume 11 of our FightAIDS@Home Newsletter.

    In these first 5 experiments with AD Vina (see http://vina.scripps.edu), we will be trying to discover new compounds that can bind to the "NNRTI adjacent" allosteric site of RT. This NNRTI adjacent allosteric site, and two other recently-discovered allosteric sites on HIV reverse transcriptase, were discovered by Eddy Arnold's lab at Rutgers University.

    Eddy Arnold's lab, and several other labs at 6 different institutions around the country, recently started collaborating with the Olson lab, as part of the new NIH-funded Center called the "HIVE."

    TARGET: NNRTI Adjacent Site of RT
    AD Exp. 42
    AD Vina Exp. 1
    AD Exp. 43
    AD Vina Exp. 2
    AD Exp. 44
    AD Vina Exp. 3
    AD Exp. 45
    AD Vina Exp. 4
    AD Exp. 46
    AD Vina Exp. 5
    Receptor StructureFull NCIEnamineChemBridgeAsinexVitas-M
    NNRTI Adjacent site of RT from PDB 4I7G45756-4578745489-4572345890-4599146043-4609346245-46395
    NNRTI Adjacent site of RT from PDB 4I7G with NNRTI45724-4575545254-4548845788-4588945992-4604246094-46244
    COMPLETION100%100%100%100%100%


    Experiment 41: 100% completed

    Experiment 41: 100% Completed

    Experiment 41 involves screening the Enamine library of 2.345 million compounds against the two allosteric sites on the surface of HIV protease. Experiment 41 and all previous FAAH experiments were performed with the software "AutoDock" (see http://autodock.scripps.edu ). This experiment is similar to Exp. 36 (see page 2 of the Status for a description of Exp. 36), but a different, much larger library of compounds is being screened, and some new targets are being included. The first part of this experiment involves docking compounds against the two allosteric-fragment-bound crystal structures presented in our recent article in Chemical Biology and Drug Design, vol. 75: 257-268 (March 2010). Three other, brand new crystal structures from Dave Stout's lab that involve allosteric fragments bound to these two sites on the surface of HIV protease are also being used as targets. Two of these new targets are presented in a new research manuscript from the Stout lab that is currently being peer-reviewed. When this paper is accepted, we will describe these targets in more detail and provide a link to this new paper.


    This is by far the largest experiment we have submitted to FightAIDS@Home; it involves faah33,529 - faah45,253.

    The results of these calculations started arriving at TSRI on 5/15/2012, and the experiment finished 7/15/2013.


    Experiment 40: 100% completed

    Experiment 40: 100% Completed

    Experiment 40 involves screening the ChemBridge library of 1,013,483 models of compounds against the newly-discovered allosteric binding site on HIV-1 integrase. This new allosteric binding site (which we are also targeting in Experiments 38 and 39) was discovered by Professor John J. Deadman's group, and it was described in "Structural basis for a new mechanism of inhibition of HIV-1 integrase identified by fragment screening and structure-based design," by D.I. Rhodes, T.S. Peat, J.J. Deadman, et al., published in the journal Antiviral Chemistry and Chemotherapy, 21: 155-168 (2011). The new crystal structure from this paper that contains the atomically-detailed, 3-D data on this new allosteric site is called "3NF6.pdb". We are screening compounds against this allosteric site to try to discover new, larger, more potent allosteric inhibitors of HIV-1 integrase. It is hoped that these new allosteric inhibitors of integrase will be effective at disabling the current drug-resistant mutant superbugs of HIV integrase. For more information about this new allosteric site, see Volume 10 of the FightAIDS@Home newsletter or our recent World AIDS Day webinar (both are linked at the top of the homepage for this site).

    Similar to Experiment 39, in Experiment 40 we are screening one million compounds against the new allosteric site on HIV-1 integrase using two slightly different docking approaches: in the first half of these calculations, we are using the smaller dimensions of the "grid box" (the region that the compounds are allowed to explore during the docking calculations) that produced the best results in the "positive control" docking calculations that reproduced the known binding mode of this new allosteric fragment (see the figures in Volume 10 of the FAAH Newsletter, page 8). In the second half of these calculations, we are using a larger grid box, to try to find even larger allosteric inhibitors that can bind strongly with both the allosteric site and other sub-pockets that are adjacent to it.


    This experiment involves faah31,501 - faah33,528.

    These results began arriving at TSRI on 3/24/2012, and the experiment finished 5/29/2012.


    Experiment 39: 100% completed

    Experiment 39: 100% Completed

    Experiment 39 involves screening the Enamine library of 2,345,014 compounds against the newly-discovered allosteric binding site on HIV-1 integrase. This new allosteric binding site (which we are also targeting in Experiment 38) was discovered by Professor John J. Deadman's group, and it was described in "Structural basis for a new mechanism of inhibition of HIV-1 integrase identified by fragment screening and structure-based design," by D.I. Rhodes, T.S. Peat, J.J. Deadman, et al., published in the journal Antiviral Chemistry and Chemotherapy, 21: 155-168 (2011). The new crystal structure from this paper that contains the atomically-detailed, 3-D data on this new allosteric site is called "3NF6.pdb". We are screening compounds against this allosteric site to try to discover new, larger, more potent allosteric inhibitors of HIV-1 integrase. It is hoped that these new allosteric inhibitors of integrase will be effective at disabling the current drug-resistant mutant superbugs of HIV integrase. For more information about this new allosteric site, see Volume 10 of the FightAIDS@Home newsletter or our recent World AIDS Day webinar (both are linked at the top of the homepage for this site).

    In Experiment 39, we are screening these 2.3 million compounds against the new allosteric site on HIV-1 integrase using two slightly different docking approaches: in the first half of these calculations, we are using the smaller dimensions of the "grid box" (the region that the compounds are allowed to explore during the docking calculations) that produced the best results in the "positive control" docking calculations that reproduced the known binding mode of this new allosteric fragment (see the figures in Volume 10 of the FAAH Newsletter, page 8). In the second half of these calculations, we are using a larger grid box, to try to find even larger allosteric inhibitors that can bind strongly with both the allosteric site and other sub-pockets that are adjacent to it.


    This experiment involves faah26,811 - faah31,500.

    These calculations began (that is, the results started arriving at TSRI) on 12/17/2011. The last batch of results arrived 5/15/2012.

  • Experiment Status Navigation

    1 - 18 / 19 - 38 / 39 - 71 / 72 - 102 / 103 - 120 / 121 - 166

    Corresponding Batches
    1-3702 / 4000-26810 / 26811-97214 / 97215-281070 / 281071-552394 / 552395-908573


    Results of these FightAIDS@Home experiments are available to the public as raw, unprocessed AutoDock dlg files upon request. E-mail Dr. Daniel N. Santiago = dsantiag ]~[ scripps . edu (use the @ symbol to replace the ]~[ and remove the spaces) for further information. Please include the phrase "FAAH data" in the subject line of your e-mail. Since the amount of data is on the order of many terabytes, you will need to provide suitable media (such as external hard drives) for receiving a copy of these results.






    Image above of an ensemble of target conformations of the G140S/Q148H drug-resistant mutant of HIV integrase was created by Alex Perryman.

    Created by Dr. Garrett M. Morris and curated by Dr. Alex L. Perryman from 2007 to August, 2013. Now curated by Dr. Daniel N. Santiago. The HIVE logo above was created by Dr. Stefano Forli.


    Last modified: 03/19/2014 by Daniel N. Santiago, Ph.D.


    ©2003-2014 The Olson Laboratory, The Scripps Research Institute, All Rights Reserved.