# Database: Folding Rate DB # Date of preparation: Jan.03, 2007 # Total number of sequences: 79 # Total number of residues: N/A # Size: 13.796 kB # Version: 1 # This database consists of a set of proteins for which the folding rate (Kf) has been experimentally determined. The Kf values have been converted to natural logs. The folding rate values were obtained from several sources [1, 2, 3]. # Database Example Format File: # >Sequence name; SwissProt ID; PDB ID; ln (k) = 25.1 # MEILPQCDFKLGGAPRALDNQAGTRKEALKHLIAVNMAQPGDSGG # ANGLKCNMCSVLRIAGSSTHQNELANGAILVTQNGCLDIPANNAL # INASSTGLK # Reference: # 1. Gromiha MM, Thangakani AM, Selvaraj S. FOLD-RATE: prediction of protein folding rates from amino acid sequence. Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W70-4. # 2. Ivankov DN, Garbuzynskiy SO, Alm E, Plaxco KW, Baker D, Finkelstein AV. Contact order revisited: influence of protein size on the folding rate. Protein Sci. 2003 Sep;12(9):2057-62. # 3. Fulton KF, Bate MA, Faux NG, Mahmood K, Betts C, Buckle AM. Protein Folding Database (PFD 2.0): an online environment for the International Foldeomics Consortium. Nucleic Acids Res. 2007 Jan;35(Database issue):D304-7. >Lambda Repressor; P03034; 1LMB; ln(k)=8.50 STKKKPLTQEQLEDARRLKAIYEKKKNELGLSQESVADKMGMGQSGVGALFNGINALNAY NAALLAKILKVSVEEFSPSIAREIYEMYEAVS >Acyl-CoA-binding Protein; P07107; 2ABD; ln(k)=6.55 MSQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWN ELKGTSKEDAMKAYIDKVEELKKKYGI >Colicin-E9 Immunity Protein; P13479; 1IMQ; ln(k)=7.31 MELKHSISDYTEAEFLQLVTTICNADTSSEEELVKLVTHFEEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGKSGFKQG >Dihydrolipoamide Acetyltransferase; P11961; 2PDD; ln(k)=9.80 VIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGA >Horse Cytochrome c; P00004; 1HRC; ln(k)=8.76 MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITW KEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE >Yeast Cytochrome C; P00044; 1YCC; ln(k)=9.62 MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIK KNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE >E. coli Cytochrome b562; P0ABE7; 256B; ln(k)=12.20 ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYHQKYR >Villin; P02640; 1VII; ln(k)=11.52 MLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF >Protein A; P38507; 1BDD; ln(k)=11.75 TADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKA >Engrailed Homeo Domain; P02836; 1ENH; ln(k)=10.53 RPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKI >Dihydroplipoamide Acetyltransferase; P11961; 1EBD_C; ln(k)=9.68 IAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGG >Deoxy-myoglobin; P02185; 1A6N; ln(k)=1.10 VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRKDIAAKYKELGY >Colicin E7 immunity protein; Q03708; 1CEI; ln(k)=5.80 MELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDN RDDSPEGIVKEIKEWRAANGKPGFKQGKPGFKQG >Phage 434 Cro Protein; P03036; 2CRO; ln(k)=3.70 MQTLSERLKKRRIALKMTQTELATKAGVKQQSIQLIEAGVTKRPRFLFEIAMALNCDPVW LQYGTKRGKAA >Cyclin-dependent Kinase Inhibitor 2A; P42771; 2A5E; ln(k)=3.50 MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVMMMGSARVA ELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVRDAWGRLPVDLAEE LGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD >FYN Proto-oncogene SH3 Domain; P06241; 1NYF; ln(k)=4.54 TGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPV DSIQAEE >Phosphatidylinositol Kinase SH3 Domain; P27986; 1PKS; ln(k)=-1.05 MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYN ETTGERGDFPGTYVEYIGR >Alpha Spectrin SH3 Domain; P07751; 1SHG; ln(k)=1.41 MDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKK LD >SRC Tyrosine Kinase SH3 Domain; P00523; 1SRL; ln(k)=4.04 GALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNY VAPS >Fibronectin Domain 9; P02751; 1FNF-9; ln(k)=-0.91 LDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTN LTPGTEYVVSIVALNGREESPLLIGQQST >Tenascin; P24821; 1TEN; ln(k)=1.06 RLDAPSQIEVKDVTDTTALITWFKPLAEIDGIELTYGIKDVPGDRTTIDLTEDENQYSIG NLKPDTEYEVSLISRRGDMSSNPAKETFTT >Twitchin 18th Module; Q23551; 1WIT; ln(k)=0.41 LKPKILTASRKIKIKAGFTHNLEVDFIGAPDPTATWTVGDSGAALAPELLVDAKSSTTSI FFPSAKRADSGNYKLKVKNELGEDEAIFEVIVQ >Cold Shock Protein B; P32081; 1CSP; ln(k)=6.98 MLEGKVKWFNSEKGFGFIEVEGQDDVFVHFSAIQGEGFKTLEEGQAVSFEIVEGNRGPQA ANVTKEA >Cold Shock Protein A; P0A9X9; 1MJC; ln(k)=5.24 SGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKG PAAGNVTSL >Tendamistat; P01092; 2AIT; ln(k)=4.20 DTTVSEPAPSCVTLYQSWRYSQADNGCAETVTVKVVYEDDTEGLCYAVAPGQITTVGDGY IGSHGHARYLARCL >PI3 Kinase P85 SH3 Domain; P23727; 1PNJ; ln(k)=-1.10 GSMSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEAKPEEIGWLNG YNETTGERGDFPGTYVEYIGRKKISP >FYN Tyrosine Kinase SH3 Domain; P06241; 1SHF; ln(k)=4.50 VTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVD >Bacillus Cold Shock Protein; P41016; 1C9O; ln(k)=7.20 MQRGKVKWFNNEKGYGFIEVEGGSDVFVHFTAIQGEGFKTLEEGQEVSFEIVQGNRGPQA ANVVKL >Thermotoga Cold Shock Protein; O54310; 1G6P; ln(k)=6.30 MRGKVKWFDSKKGYGFITKDEGGDVFVHWSAIEMEGFKTLKEGQVVEFEIQEGKKGPQAA HVKVVE >Cyclophilin A; P23869; 1LOP; ln(k)=6.60 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMK QKATKEPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGY CVFAEVVDGMDEVDKIKGVATGRSGMHQDVPKEDVIIESVTVSE >Peptidyl-prolyl Cis-trans Isomerase; Q13526; 1PIN; ln(k)=9.44 KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSG >DNA Binding Protein 7A; P39476; 1C8C; ln(k)=6.91 MATVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLA KQKK >Photosystem I Accessory Protein; P31969; 1PSF; ln(k)=3.22 AIERGSKVKILRKESYWYGDVGTVASIDKSGIIYPVIVRFNKVNYNGFSGSAGGLNTNNF AEHELEVVG >Fibronectin Domain 10; P02751; 1FNF-10; ln(k)=5.48 VSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATIS GLKPGVDYTITVYAVTGRGDSPASSKPISINYRT >CD2 Adhesion Domain; P08921; 1HNG; ln(k)=2.89 RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILAN GDLKIKNLTRDDSGTYNVTVYSTNGTRILNKALDLRILEMVSKPMIYWECSNATLTCEVL EGTDVELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAVNRVSQESEMEVVNCPE >Chaperonin 10; P09621; 1HX5; ln(k)=0.74 MAKVNIKPLEDKILVQANEAETTTASGLVIPDTAKEKPQEGTVVAVGPGRWDEDGEKRIP LDVAEGDTVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK >Titin IG Repeat 27; Q8WZ42; 1TIT; ln(k)=3.47 LIEVEKPLYGVEVFVGETAHFEIELSEPDVHGQWKLKGQPLTASPDCEIIEDGKKHILIL HNCQLGMTGEVSFQAANAKSAANLKVKEL >Rat Fatty Acid Binding Protein; P02693; 1IFC; ln(k)=3.40 MAFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNID VVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTY EGVEAKRIFKKE >Ileal Lipid Binding Protein; P10289; 1EAL; ln(k)=1.30 AFTGKYEIESEKNYDEFMKRLALPSDAIDKARNLKIISEVKQDGQNFTWSQQYPGGHSIT NTFTIGKECDIETIGGKKFKATVQMEGGKVVVNSPNYHHTAEIVDGKLVEVSTVGGVSYE RVSKKLA >Retinol Binding Protein II; P06768; 1OPA; ln(k)=1.40 MTKDQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKIIVQDGDNFKTKTNSTFRN YDLDFTVGVEFDEHTKGLDGRNVKTLVTWEGNTLVCVQKGEKENRGWKQWVEGDKLYLEL TCGDQVCRQVFKKK >Retinoic Acid Binding Protein; P62965; 1CBI; ln(k)=-3.20 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRT TEINFKVGEGFEEETVDGRKCRSLPTWENENKIHCTQTLLEGDGPKTYWTRELANDELIL TFGADDVVCTRIYVRE >Acylphosphatase; P00818; 1APS; ln(k)=-1.48 STARPLKSVDYEVFGRVQGVCFRMYAEDEARKIGVVGWVKNTSKGTVTGQVQGPEEKVNS MKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSVRY >E. coli Histidine Carrier Proteiin HPr; 1HDN; ln(k)=2.70 MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV VTISAEGEDEQKAVEHLVKLMAELE >RNA Binding Splicesome Protein; P09012; 1URN; ln(k)=5.73 AVPETRPNHTIYINNLNEKIKKDELKKSLHAIFSRFGQILDILVSRSLKMRGQAFVIFKE VSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMK >MERP Mercury Ion Binding Protein; P04129; 2HQI; ln(k)=0.18 ATQTVTLAVPGMTCAACPITVKKALSKVEGVSKVDVGFEKREAVVTFDDTKASVQKLTKA TADAGYPSSVKQ >Procarboxypeptidase B Domain; P09955; 1PBA; ln(k)=6.80 HHSGEHFEGEKVFRVNVEDENDISELHELASTRQIDFWKPDSVTQIKPHSTVDFRVKAED ILAVEDFLEQNELQYEVLINN >Ubiquitin; P62988; 1UBQ; ln(k)=7.33 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG >Igg Binding Domain of Protein L; Q51912; 2PTL; ln(k)=4.10 ENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGE YTVDVADKGYTLNIKFAG >FK506 Binding Protein; P62942; 1FKB; ln(k)=1.46 GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE >Chymotrypsin Inhibitor 2; P01053; 1COA; ln(k)=3.87 MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNVAEV PRVG >Ribosomal Protein L9; P02417; 1DIV; ln(k)=6.58 MKVIFLKDVKGKGKKGEIKNVADGYANNFLFKQGLAIEATPANLKALEAQKQKEQRQAAE ELANAKKLKEQLEKLTVTIPAKAGEGGRLFGSITSKQIAESLQAQHGLKLDKRKIELADA IRALGYTNVPVKLHPEVTATLKVHVTEQK >Actin Severing Domain of Villin 14T; P02640; 2VIK; ln(k)=6.80 VELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYN IHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGG VASGMK >Chymotrypsin Inhibitor 2 Chimera; P01053; 1CIS; ln(k)=3.87 MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLEKQAVDNAYAEYRIDRVRLAVDKLDNIA QVPRVG >Procarboxypeptidase A; P09954; 1PCA; ln(k)=6.80 KEDFVGHQVLRISVDDEAQVQKVKELEDLEHLQLDFWRGPARPGFPIDVRVPFPSIQAVK VFLEAHGIRYTIMIEDVQLLLDEEQEQMFASQGR >B1 Domain of Protein L; Q51912; 1HZ6; ln(k)=4.10 MEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEWTVDVADKGYTLNI KFAG >B1 Domain of Protein G; P06654; 1PGB; ln(k)=6.00 MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE >Beta Hairpin from Protein G; P06654; 1PGB; ln(k)=12.00 GEWTYDDATKTFTVTE >Chymotrypsin Inhibitor 2; P01053; 2CI2; ln(k)=3.90 SSVEKKPEGVNTGAGDRHNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTME YRIDRVRLFVDKLDNIAEVPRVG >Short Synthetic Helix; NA; NA; ln(k)=15.50 AAAAAAAAAAAAAAAAAAAAA >Human Procarboxypeptidase A2; P48052; 1AYE; ln(k)=6.80 LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVK VFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRER >Ribosomal Protein S6; P23370; 1RIS; ln(k)=5.90 MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVEELGLRRLAYPIAKDPQGYF LWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLANA >Histidine Phosophocarrier Protein; P0AA04; 1POH; ln(k)=2.70 MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV VTISAEGEDEQKAVEHLVKLMAELE >Barstar; P00648; 1BRS; ln(k)=3.40 AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR >Bovine Acyl Phosphatase; P41500; 2ACY; ln(k)=0.92 AEGDTLISVDYEIFGKVQGVFFRKYTQAEGKKLGLVGWVQNTDQGTVQGQLQGPASKVRH MQEWLETKGSPKSHIDRASFHNEKVIVKLDYTDFQIVK >E. coli CheY Protein; P0AE67; 3CHY; ln(k)=1.00 ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN KIFEKLGM >Ribonuclease H; P0A7Y4; 2RN2; ln(k)=0.10 MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEW VKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV >Dihydrofolate Reductase; P0ABQ4; 1RA9; ln(k)=-2.50 MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNI ILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR >Barnase; P00648; 1BNI; ln(k)=2.60 AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR >Phage T4 Lysozyme; P00720; 2LZM; ln(k)=4.10 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITK DEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL >SUC1 Cyclin Dependent Kinase; 1SCE; ln(k)=4.20 MSKSGVPRLLTASERERLEPFIDQIHYSPRYADDEYEYRHVMLPKAMLKAIPTDYFNPET GTLRILQEEEWRGLGITQSLGWEMYEVHVPEPHILLFKREKDYQMKFSQQRGG >Hydrogenase Maturation Protein HYPF; P30131; 1GXT; ln(k)=4.38 MAKNTSCGVQLRIRGKVQGVGFRPFVWQLAQQLNLHGDVCNDGDGVEVRLREDPEVFLVQ LYQHCPPLARIDSVEREPFIWSQLPTEFTIR > Cyclin-dependent kinase inhibitor 2A; P42771; 2A5E; ln(k)=3.50 MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVMMMGSARVA ELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVRDAWGRLPVDLAEE LGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD >Phosphoglycerate Kinase N-domain; P18912; 1PHP; ln(k)=2.30 MNKKTIRDVDVRGKRVFCRVDFNVPMEQGAITDDTRIRAALPTIRYLIEHGAKVILASHL GRPKGKVVEELRLDAVAKRLGELLERPVAKTNEAVGDEVKAAVDRLNEGDVLLLENVRFY PGEEKNDPELAKAFAELADLYVNDAFGAAHRAHASTEGIAHYLPAVAGFLMEKELEVLGK >Phosphoglycerate Kinase C-domain; P18912; 1PHP; ln(k)=-3.45 ALSNPDRPFTAIIGGAKVKDKIGVIDNLLEKVDNLIIGGGLAYTFVKALGHDVGKSLLEE DKIELAKSFMEKAKEKGVRFYMPVDVVVADRFANDANTKVVPIDAIPADWSALDIGPKTR ELYRDVIRESKLVVWNGPMGVFEMDAFAHGTKAIAEALAEALDTYSVIGGGDSAAAVEKF GLADKMDHISTGGGASLEFMEGKQLPGVVALEDK >Tryptophan Synthase alpha chain; P00929; 1QOP; ln(k)-2.53 MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLAD GPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQ VGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLSRS GVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI IEKNLASPKQMLAELRSFVSAMKAASRA >Tryptophan Synthase beta chain; P0A2K1; 1QOP; ln(k)=-6.91 MTTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALT KCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASA LASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGS YETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGM FADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSI SAGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALK MMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI >Lyme Variable Surface Antigen VlsE; NA; 1L8W; ln(k)=1.97 GSSQVADKDDPTNKFYQSVIQLGNGFLDVFTSFGGLVAEAFGFKSDPKKSDVKTYFTTVA AKLEKTKTDLNSLPKEKSDISSTTGKPDSTGSVGTAVEGAIKEVSELLDKLVKAVKTAEG ASSGTAAIGEVVADADAAKVADKASVKGIAKGIKEIVEAAGGSEKLKAVAAAKGENNKGA GKLFGKAGAAAHGDSEAASKAAGAVSAVSGEQILSAIVTAADAAEQDGKKPEEAKNPIAA AIGDKDGGAEFGQDEMKKDDQIAAAIALRGMAKDGKFAVKDGEKEKAEGAIKGAAESAVR KVLGAITGLIGDAVSSGLRKVGDSVKAASKETPPALNK >U1A RNA Binding Protein; P09012; 1NU4; ln(k)=4.62 AVPETRPNHTIYINNLNEKIKKDELKKSLHAIFSRFGQILDILVSRSLKMRGQAFVIFKE VSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMK >Rous Sarcoma Src Sh2 Domain; P00524; 1IS0; ln(k)=8.74 QAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYK IRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSK