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📄 iep.input

📁 emboss的linux版本的源代码
💻 INPUT
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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-&gt;H: BROADENING OF SPECIFICITY.FT   MUTAGEN      22     22       R-&gt;N: RECOGNIZE AN OPERATOR VARIANT.FT   VARIANT     282    282       Y -&gt; D (IN T41 MUTANT).FT   CONFLICT    286    286       S -&gt; 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 -&gt; R (in alpha-2B and alpha-2C).FT                                /FTId=VAR_004012.FT   VARIANT      57     57       H -&gt; 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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