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<a name="input.1"></a><h3>Input files for usage example </h3>'tsw:laci_ecoli' is a sequence entry in the example protein database 'tsw'<p><p><h3>Database entry: tsw:laci_ecoli</h3><table width="90%"><tr><td bgcolor="#FFCCFF"><pre>ID LACI_ECOLI STANDARD; PRT; 360 AA.AC P03023; P71309; Q47338; O09196;DT 21-JUL-1986 (Rel. 01, Created)DT 01-NOV-1997 (Rel. 35, Last sequence update)DT 15-DEC-1998 (Rel. 37, Last annotation update)DE LACTOSE OPERON REPRESSOR.GN LACI.OS Escherichia coli.OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;OC Escherichia.RN [1]RP SEQUENCE FROM N.A.RX MEDLINE; 78246991.RA FARABAUGH P.J.;RT "Sequence of the lacI gene.";RL Nature 274:765-769(1978).RN [2]RP SEQUENCE FROM N.A.RC STRAIN=K12 / MG1655;RX MEDLINE; 97426617.RA BLATTNER F.R., PLUNKETT G. III, BLOCH C.A., PERNA N.T., BURLAND V.,RA RILEY M., COLLADO-VIDES J., GLASNER F.D., RODE C.K., MAYHEW G.F.,RA GREGOR J., DAVIS N.W., KIRKPATRICK H.A., GOEDEN M.A., ROSE D.J.,RA MAU B., SHAO Y.;RT "The complete genome sequence of Escherichia coli K-12.";RL Science 277:1453-1474(1997).RN [3]RP SEQUENCE FROM N.A.RC STRAIN=K12 / MG1655;RA DUNCAN M., ALLEN E., ARAUJO R., APARICIO A.M., CHUNG E., DAVIS K.,RA FEDERSPIEL N., HYMAN R., KALMAN S., KOMP C., KURDI O., LEW H.,RA LIN D., NAMATH A., OEFNER P., ROBERTS D., SCHRAMM S., DAVIS R.W.;RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.RN [4]RP SEQUENCE FROM N.A.RA CHEN J., MATTHEWS K.K.S.M.;RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.RN [5]RP SEQUENCE FROM N.A.RA MARSH S.;RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.RN [6]RP SEQUENCE OF 1-147; 159-230 AND 233-360.RX MEDLINE; 76091932.RA BEYREUTHER K., ADLER K., FANNING E., MURRAY C., KLEMM A., GEISLER N.;RT "Amino-acid sequence of lac repressor from Escherichia coli.RT Isolation, sequence analysis and sequence assembly of trypticRT peptides and cyanogen-bromide fragments.";RL Eur. J. Biochem. 59:491-509(1975).RN [7]<font color=red> [Part of this file has been deleted for brevity]</font>CC between the Swiss Institute of Bioinformatics and the EMBL outstation -CC the European Bioinformatics Institute. There are no restrictions on itsCC use by non-profit institutions as long as its content is in no wayCC modified and this statement is not removed. Usage by and for commercialCC entities requires a license agreement (See http://www.isb-sib.ch/announce/CC or send an email to license@isb-sib.ch).CC --------------------------------------------------------------------------DR EMBL; V00294; CAA23569.1; -.DR EMBL; J01636; AAA24052.1; -.DR EMBL; AE000141; AAC73448.1; -.DR EMBL; U73857; AAB18069.1; ALT_INIT.DR EMBL; X58469; CAA41383.1; -.DR EMBL; U86347; AAB47270.1; ALT_INIT.DR EMBL; U72488; AAB36549.1; -.DR EMBL; U78872; AAB37348.1; -.DR EMBL; U78873; AAB37351.1; -.DR EMBL; U78874; AAB37354.1; -.DR PIR; A03558; RPECL.DR PIR; S02540; S02540.DR PDB; 1LCC; 31-JAN-94.DR PDB; 1LCD; 31-JAN-94.DR PDB; 1LTP; 31-OCT-93.DR PDB; 1TLF; 31-JUL-95.DR PDB; 1LBG; 11-JUL-96.DR PDB; 1LBH; 11-JUL-96.DR PDB; 1LBI; 11-JUL-96.DR PDB; 1LQC; 12-FEB-97.DR ECO2DBASE; H039.0; 6TH EDITION.DR ECOGENE; EG10525; LACI.DR PFAM; PF00356; lacI; 1.DR PFAM; PF00532; Peripla_BP_like; 1.DR PROSITE; PS00356; HTH_LACI_FAMILY; 1.KW Transcription regulation; DNA-binding; Repressor; 3D-structure.FT DNA_BIND 6 25 H-T-H MOTIF.FT MUTAGEN 17 17 Y->H: BROADENING OF SPECIFICITY.FT MUTAGEN 22 22 R->N: RECOGNIZE AN OPERATOR VARIANT.FT VARIANT 282 282 Y -> D (IN T41 MUTANT).FT CONFLICT 286 286 S -> L (IN AAA24052, REF. 2, 4 AND 5).FT HELIX 6 13FT TURN 14 14FT HELIX 17 24FT HELIX 32 44FT TURN 49 50SQ SEQUENCE 360 AA; 38564 MW; 4CA5A1D6 CRC32; MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPSTTIK QDFRLLGQTS VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ//</pre></td></tr></table><p><a name="input.2"></a><h3>Input files for usage example 2</h3><p><h3>Database entry: tsw:ifna2_human</h3><table width="90%"><tr><td bgcolor="#FFCCFF"><pre>ID IFNA2_HUMAN STANDARD; PRT; 188 AA.AC P01563; P01564; Q14606; Q96KI6;DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.DT 21-JUL-1986, sequence version 1.DT 27-JUN-2006, entry version 72.DE Interferon alpha-2 precursor (Interferon alpha-A) (LeIF A).GN Name=IFNA2;OS Homo sapiens (Human).OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;OC Catarrhini; Hominidae; Homo.OX NCBI_TaxID=9606;RN [1]RP NUCLEOTIDE SEQUENCE.RX MEDLINE=81052322; PubMed=6159538; DOI=10.1038/287411a0;RA Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G.,RA Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R.,RA Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M.,RA Familletti P.C., Pestka S.;RT "Human leukocyte interferon produced by E. coli is biologicallyRT active.";RL Nature 287:411-416(1980).RN [2]RP NUCLEOTIDE SEQUENCE.RX MEDLINE=81148795; PubMed=6163083; DOI=10.1038/290020a0;RA Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M.,RA McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.;RT "The structure of eight distinct cloned human leukocyte interferonRT cDNAs.";RL Nature 290:20-26(1981).RN [3]RP NUCLEOTIDE SEQUENCE.RX MEDLINE=82060261; PubMed=6170983;RA Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.;RT "DNA sequence of a major human leukocyte interferon gene.";RL Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981).RN [4]RP NUCLEOTIDE SEQUENCE.RC TISSUE=Bone marrow tumor;RX MEDLINE=86069501; PubMed=3906813;RA Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.;RT "Cloning of human leukocyte interferon cDNA and a strategy for itsRT production in E. coli.";RL Rev. Latinoam. Microbiol. 27:141-150(1985).RN [5]RP NUCLEOTIDE SEQUENCE.RC TISSUE=Placenta;RX MEDLINE=98357449; PubMed=9694076;RA Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P.,RA Mannoni P., Chabannon C.;<font color=red> [Part of this file has been deleted for brevity]</font>DR Ensembl; ENSG00000188379; Homo sapiens.DR HGNC; HGNC:5423; IFNA2.DR MIM; 147562; gene.DR LinkHub; P01563; -.DR RZPD-ProtExp; A0813; -.DR RZPD-ProtExp; IOH35221; -.DR RZPD-ProtExp; RZPDo834E0933; -.DR GO; GO:0005132; F:interferon-alpha/beta receptor binding; TAS.DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS.DR GO; GO:0007267; P:cell-cell signaling; TAS.DR GO; GO:0006917; P:induction of apoptosis; TAS.DR GO; GO:0006954; P:inflammatory response; TAS.DR InterPro; IPR009079; 4_helix_cytokine.DR InterPro; IPR000471; Interferon_abd.DR PANTHER; PTHR11691; Interferon_abd; 1.DR Pfam; PF00143; Interferon; 1.DR PRINTS; PR00266; INTERFERONAB.DR ProDom; PD000550; Interferon_abd; 1.DR SMART; SM00076; IFabd; 1.DR PROSITE; PS00252; INTERFERON_A_B_D; 1.KW 3D-structure; Antiviral defense; Cytokine; Direct protein sequencing;KW Glycoprotein; Pharmaceutical; Polymorphism; Signal.FT SIGNAL 1 23FT CHAIN 24 188 Interferon alpha-2.FT /FTId=PRO_0000016360.FT CARBOHYD 129 129 O-linked (GalNAc...).FT /FTId=CAR_000049.FT DISULFID 24 121FT DISULFID 52 161FT VARIANT 46 46 K -> R (in alpha-2B and alpha-2C).FT /FTId=VAR_004012.FT VARIANT 57 57 H -> R (in alpha-2C).FT /FTId=VAR_013001.FT HELIX 33 44FT TURN 49 54FT HELIX 63 66FT HELIX 76 91FT HELIX 93 98FT HELIX 101 123FT TURN 126 127FT TURN 133 133FT HELIX 134 155FT TURN 156 157FT HELIX 160 178FT TURN 179 182SQ SEQUENCE 188 AA; 21550 MW; 101DD21D394CBF97 CRC64; MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL QESLRSKE//</pre></td></tr></table><p>
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