SERVERNAME: frsvr_SDP TARGET: T0044 PARAMETERS: excludefolds: 1kja 1hli include h3p2 URL: http://www.cs.bgu.ac.il/~dfischer/cafasp1/frsvr_SDP.t0044 SERVER'S URL: http://www.doe-mbi.ucla.edu/people/frsvr/submit.html RANK FOLD SCORE LENGTH_ALIGNMENT SEQ_ID% 1 1chd 4.53 181 23 2 8adh 4.00 305 19 3 1masa 3.95 281 21 4 1ede 3.68 262 18 5 2cmd 3.44 260 23 6 1eps1 3.28 273 19 7 1rlaa 3.17 272 21 8 1phh_1-394 3.02 248 23 9 2pola 2.99 296 23 10 2gsaa 2.90 310 21 11 1efva 2.84 227 26 12 8adh_1-373 2.67 191 21 13 1fmca 2.60 240 24 14 1pysa 2.47 241 22 15 1hlpa 2.40 252 23 END The three-dimensional fold predicted for your amino acid sequence is in the table below. HERE I INCLUDE ONLY THE RESULTS OF THE gonnet+predss METHOD. THE OTHER RESULTS CAN BE FOUND AT THE URL (www page) SPECIFIED AT THE END OF THIS MESSAGE. Please cite: Fischer, D. and Eisenberg, D. Fold Recognition Using Sequence-Derived Predictions. Protein Science, 5, 947-955, 1996. * * * * N O T E * * * * PLEASE CONSULT ALSO THE RESULTS OF gonnet+predss+multi Your sequence was translated to: seq.seq Length: 347 December 31, 1998 16:56 Type: P Check: 6794 .. 1 MVKRMIALDG AQGEGGGQIL RSALSLSMIT GQPFTITSIR AGRAKPGLLR 51 QHLTAVKAAT EICGATVEGA ELGSQRLLFR PGTVRGGDYR FAIGSAGSCT 101 LVLQTVLPAL WFADGPSRVE VSGGTDNPSA PPADFIRRVL EPLLAKIGIH 151 QQTTLLRHGF YPAGGGVVAT EVSPVASFNT LQLGERGNIV QMRGEVLLAG 201 VPRHVAEREI ATLAGSFSLH EQNIHNLPRD QGPGNTVSLE VESENITERF 251 FVVGEKRVSA EVVAAQLVKE VKRYLASTAA VGEYLADQLV LPMALAGAGE 301 FTVAHPSCHL LTNIAVVERF LPVRFSLIET DGVTRVSIEG SHHHHHH NAME: t044 FROM: dfischer@indigo.cs.bgu.ac.il BY YOUR REQUEST I HAVE NOT USED THE FOLLOWING FOLDS: 1an3b 1az7 1bd9a 1bg8a 1bl0a 1cdaa 1hli 1illg 1kja The method used for this prediction was: gonnet+predss . Most similar fold: 1chd MOL_ID: 1; 2 MOLECULE: CHEB METHYLESTERASE; 3 CHAIN: NULL; 4 DOMAIN: METHYLESTERASE DOMAIN (C-TERMINAL RESIDU 5 349); 6 EC: 3.1.1.61; 7 ENGINEERED: YES RANK Z-SCORE FOLD LENGTHALI %ID 1 4.53 1chd 181 23 3-22 a/b ; CheB methylesterase domain (C-terminal residues 152-349)] 3-22-1-1-1-1- 2 4.00 8adh 305 19 99--2-20--3-15 [beta ; GroES-like] [ a/b ; NAD(P)-binding Rossmann-fold domains] 2-20-1-2-1-1-8-1 R, [MULTIDOMAIN ; ] 99--2-20--3-15 [beta ; GroES-like] [(a/b) ; NAD(P)-binding Rossmann-fold domains] 2-20-1-2-1-1-8-1 R 3 3.95 1masa 281 21 1997 new ; PURINE NUCLEOSIDE HYDROLA 4 3.68 1ede 262 18 3-44 a/b ; alpha/beta-Hydrolases] 3-44-1-3-1-1- 5 3.44 2cmd 260 23 99--3-15--4-74 [ a/b ; NAD(P)-binding Rossmann-fold domains] [(a+b) ; Lactate & malate dehydrogenases, C-terminal domain] [MULTIDOMAIN ; ] 99--3-15--4-74 [(a/b) ; NAD(P)-binding Rossmann-fold domains] [ (a+b) ; Lactate & malate dehydrogenases, C-terminal domain] 6 3.28 1eps1 273 19 199 7 3.17 1rlaa 272 21 1997 new ; THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, 8 3.02 1phh_1-394 248 23 3-4 a/b ; FAD (also NAD)-binding motif] 3-4-1-2-2-1-4-1 R 9 2.99 2pola 296 23 99--4-62--4-62--4-62 [(a+b) ; DNA clamp] [(a+b) ; DNA clamp] [ (a+b) ; DNA clamp] [MULTIDOMAIN ; ] 99--4-62--4-62--4-62 [(a+b) ; DNA clamp] [ (a+b) ; DNA clamp] [ (a+b) ; DNA clamp] 10 2.90 2gsaa 310 21 1998 11 2.84 1efva 227 26 1998 12 2.67 8adh_1-373 191 21 2-20 beta ; GroES-like] 2-20-1-2-1-1-8-1 R 13 2.60 1fmca 240 24 1997 new ; 7-ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEX WITH NADH A 14 2.47 1pysa 241 22 1997 new ; PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPH 15 2.40 1hlpa 252 23 99--3-15--4-74 [ a/b ; NAD(P)-binding Rossmann-fold domains] [(a+b) ; Lactate & malate dehydrogenases, C-terminal domain] [MULTIDOMAIN ; ] 99--3-15--4-74 [(a/b) ; NAD(P)-binding Rossmann-fold domains] [ (a+b) ; Lactate & malate dehydrogenases, C-terminal domain] LEGEND: COL. 1: RANK. The ranks are obtained by sorting the fold library, by Z-SCORES, in decreasing order. Only the 15 structures that are most compatible to your sequence are shown. COL. 2: Z-SCORE. The z-scores are computed using the distribution of raw scores (not shown) of all folds. COL. 3: FOLD. Protein Data Bank codes for the coordinates of the 3D structures. COL. 4: LENGTHALI. The number of residues from your sequence that were aligned to the fold. COL. 5: % ID. Percentage of identical residues in the alignment. RELIABILITY OF THIS PREDICTION: With this method the confidence threshold is a z-score of 4.8 +- 1.0. YOUR HIGHEST SCORING FOLD IS BELOW THIS THRESHOLD YOUR PREDICTION IS NOT RELIABLE. You may conclude that: IF the fold of your sequence is similar to one already observed, THEN: - Our method is not sensitive enough to assign a fold for your sequence, and/or - It may be contained within a larger fold, and/or - The fold of your sequence is not included in our library of folds. IF your sequence corresponds to a new, unobserved fold, THEN: - Our method reflects this by a below threshold score. Below is the alignment of your sequence with the top hit structure. In the near future, all the alignments in a more readable format will be made available. bbbbbb bbbb bb bbbbbb hh VKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQ || | | | | || || | SEKLIAIGASTG..GTEAIRHVLQPLPLSSPAVIITQ....HMPPGFTRS bbbbbbb h hhhhhhhhhh bbbbbb b hhhhh hhhhhhhhhhhh bbbb bbbbbb bbbb bbb HLTAVKAATEICGATVEGAELGSQRLLFRPGTVRGGDYRFAIGSAGSCTL | | || | | | || | FAERLN...KLCQISVKEAEDG.ERVLPGHAYIAPGDKHMELARSGANY. hhhhhh hhh bbbbb bbbbbb bbbbbbb bb bbbb bb bbbbb hhhhhhhhhhhhh bb VLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQ | | | ................QIKIHDGPPVNRHRPS..VDVLFHSVAKHAGRNA bbbbb h hhhhhhhhhhhh bb bbbb bbbbbb QTTLLRH..........GFYPAGGGVVATEVSPVASF....NTLQLGERG | | || | | | VGVILTGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAINMGGVS bbbbb hhhhhhhhhhh bbbbbb hhhhhhhhh bbbbbbbbbbb hhhhhhhhhhhh hh NIVQMRGEVLLAGVPRHVAEREIATLAGSFSL | | | EVVDL..........SQVSQQMLAKISAGQAI bbbhh hhhhhhhhhhhh 18% Additional information for your prediction can be found at the url: http://www.doe-mbi.ucla.edu/people/frsvr/preds/24519t044/24519t044.html