LGRA_BREPA
ID LGRA_BREPA Reviewed; 2273 AA.
AC Q70LM7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Linear gramicidin synthase subunit A;
DE Includes:
DE RecName: Full=ATP-dependent valine/leucine adenylase;
DE Short=Val/LeuA;
DE AltName: Full=Valine/leucine activase;
DE Includes:
DE RecName: Full=ATP-dependent glycine adenylase;
DE Short=GlyA;
DE AltName: Full=Glycine activase;
GN Name=lgrA;
OS Brevibacillus parabrevis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB 8598
RC / IAM 1031;
RX PubMed=14670971; DOI=10.1074/jbc.m309658200;
RA Kessler N., Schuhmann H., Morneweg S., Linne U., Marahiel M.A.;
RT "The linear pentadecapeptide gramicidin is assembled by four multimodular
RT nonribosomal peptide synthetases that comprise 16 modules with 57 catalytic
RT domains.";
RL J. Biol. Chem. 279:7413-7419(2004).
CC -!- FUNCTION: Activates valine (or leucine, but much less frequently), and
CC then glycine and catalyzes the formation of the peptide bond in the
CC first step of peptide synthesis. This enzyme may also play a role in N-
CC formylation of the first amino acid residue in the synthesized
CC dipeptide.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.84 mM for valine;
CC KM=2.40 mM for isoleucine;
CC -!- SUBUNIT: Large multienzyme complex composed of 4 subunits; LgrA, LgrB,
CC LgrC and LgrD.
CC -!- DOMAIN: Two module-bearing peptide synthase with a C-terminal
CC epimerization domain, which is probably inactive. Each module
CC incorporates one amino acid into the peptide product and can be further
CC subdivided into domains responsible for substrate adenylation,
CC thiolation, condensation (not for the initiation module), and
CC epimerization (optional). At the N-terminus, contains a N-
CC formyltransferase domain that is probably responsible for the
CC formylation of the first incorporated amino acid.
CC -!- MISCELLANEOUS: Linear gramicidin is a pentadecapeptide antibiotic
CC produced during sporulation.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AJ566197; CAD92849.1; -; Genomic_DNA.
DR PDB; 5ES5; X-ray; 2.80 A; A/B=2-766.
DR PDB; 5ES6; X-ray; 2.46 A; A=2-684.
DR PDB; 5ES7; X-ray; 2.81 A; A=2-684.
DR PDB; 5ES8; X-ray; 2.55 A; A/B=2-766.
DR PDB; 5ES9; X-ray; 3.77 A; A/B=2-766.
DR PDB; 5JNF; X-ray; 2.75 A; A/B/C/D=2-584.
DR PDB; 6MFW; X-ray; 2.50 A; A=2-1198.
DR PDB; 6MFX; X-ray; 2.20 A; A=2-1198.
DR PDB; 6MFY; X-ray; 2.50 A; A=2-1716.
DR PDB; 6MFZ; X-ray; 6.00 A; A/B=2-1802.
DR PDB; 6MG0; X-ray; 6.00 A; A/B=2-1716.
DR PDB; 6ULZ; X-ray; 3.10 A; A=2-684.
DR PDBsum; 5ES5; -.
DR PDBsum; 5ES6; -.
DR PDBsum; 5ES7; -.
DR PDBsum; 5ES8; -.
DR PDBsum; 5ES9; -.
DR PDBsum; 5JNF; -.
DR PDBsum; 6MFW; -.
DR PDBsum; 6MFX; -.
DR PDBsum; 6MFY; -.
DR PDBsum; 6MFZ; -.
DR PDBsum; 6MG0; -.
DR PDBsum; 6ULZ; -.
DR AlphaFoldDB; Q70LM7; -.
DR SMR; Q70LM7; -.
DR STRING; 54914.AV540_01965; -.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..2273
FT /note="Linear gramicidin synthase subunit A"
FT /id="PRO_0000193089"
FT DOMAIN 693..767
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1724..1798
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..144
FT /note="GART"
FT MOD_RES 728
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1759
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 39..43
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5ES6"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 422..432
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:5ES6"
FT HELIX 545..551
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 561..571
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 577..584
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:5ES5"
FT STRAND 611..618
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:5ES8"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 656..663
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 697..710
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 721..725
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 728..738
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 747..752
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 763..766
FT /evidence="ECO:0007829|PDB:5ES8"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 787..798
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 806..813
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 819..832
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 834..837
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 838..843
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 846..851
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 866..868
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 869..876
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 887..894
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 899..906
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 907..909
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 912..926
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 938..948
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 952..964
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:6MFW"
FT STRAND 986..994
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 996..1008
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1013..1028
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1033..1041
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1047..1049
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1058..1065
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1072..1088
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 1089..1091
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1094..1100
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1114..1120
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1126..1129
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1131..1133
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1140..1150
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1153..1161
FT /evidence="ECO:0007829|PDB:6MFX"
FT TURN 1162..1164
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1167..1185
FT /evidence="ECO:0007829|PDB:6MFX"
FT STRAND 1188..1191
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1192..1194
FT /evidence="ECO:0007829|PDB:6MFX"
FT HELIX 1200..1210
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1222..1232
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1239..1241
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1248..1263
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1272..1275
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1281..1293
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1295..1299
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1306..1316
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1319..1322
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1325..1328
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1329..1331
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1335..1337
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1340..1342
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1343..1345
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1361..1368
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1376..1381
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1382..1395
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1403..1405
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1415..1420
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1423..1425
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1428..1430
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1434..1436
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1440..1449
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1454..1457
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1459..1467
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1480..1483
FT /evidence="ECO:0007829|PDB:6MFY"
FT TURN 1491..1493
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1494..1499
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1504..1509
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1512..1514
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1519..1523
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1535..1537
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1541..1546
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1559..1565
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1576..1582
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1583..1585
FT /evidence="ECO:0007829|PDB:6MFY"
FT HELIX 1587..1589
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1593..1603
FT /evidence="ECO:0007829|PDB:6MFY"
FT STRAND 1609..1614
FT /evidence="ECO:0007829|PDB:6MFY"
SQ SEQUENCE 2273 AA; 257859 MW; A2CAF8DF6CCE302C CRC64;
MRILFLTTFM SKGNKVVRYL ESLHHEVVIC QEKVHAQSAN LQEIDWIVSY AYGYILDKEI
VSRFRGRIIN LHPSLLPWNK GRDPVFWSVW DETPKGVTIH LIDEHVDTGD ILVQEEIAFA
DEDTLLDCYN KANQAIEELF IREWENIVHG RIAPYRQTAG GTLHFKADRD FYKNLNMTTV
RELLALKRLC AEPKRGEKPI DKTFHQLFEQ QVEMTPDHVA VVDRGQSLTY KQLNERANQL
AHHLRGKGVK PDDQVAIMLD KSLDMIVSIL AVMKAGGAYV PIDPDYPGER IAYMLADSSA
AILLTNALHE EKANGACDII DVHDPDSYSE NTNNLPHVNR PDDLVYVMYT SGSTGLAKGV
MIEHHNLVNF CEWYRPYFGV TPADKALVYS SFSFDGSALD IFTHLLAGAA LHIVPSERKY
DLDALNDYCN QEGITISYLP TGAAEQFMQM DNQSFRVVIT GGDVLKKIER NGTYKLYNGY
GPTECTIMVT MFEVDKPYAN IPIGKPIDRT RILILDEALA LQPIGVAGEL FIVGEGLGRG
YLNRPELTAE KFIVHPQTGE RMYRTGDRAR FLPDGNIEFL GRLDNLVKIR GYRIEPGEIE
PFLMNHPLIE LTTVLAKEQA DGRKYLVGYY VAPEEIPHGE LREWLGNDLP DYMIPTYFVH
MKAFPLTANG KVDRRALPDV QADAELLGED YVAPTDELEQ QLAQVWSHVL GIPQMGIDDH
FLERGGDSIK VMQLIHQLKN IGLSLRYDQL FTHPTIRQLK RLLTEQKQVS LEPLRELDEQ
AEYETSAVEK RMYIIQQQDV ESIAYNVVYT INFPLTVDTE QIRVALEQLV LRHEGLRSTY
HMRGDEIVKR IVPRAELSFV RQTGEEESVQ SLLAEQIKPF DLAKAPLLRA GVIETADKKV
LWFDSHHILL DGLSKSILAR ELQALLGQQV LSPVEKTYKS FARWQNEWFA SDEYEQQIAY
WKTLLQGELP AVQLPTKKRP PQLTFDGAIQ MYRVNPEITR KLKATAAKHD LTLYMLMLTI
VSIWLSKMNS DSNQVILGTV TDGRQHPDTR ELLGMFVNTL PLLLSIDHEE SFLHNLQQVK
AKLLPALQNQ YVPFDKILEA ARVKREGNRH PLFDVMFMMQ GAPETELESN MHHINAGISK
FDLTLEVLER ENGLNIVFEY NTHLFDEGMI LRMVAQFEHL LLQAVHGLDQ QVKRFELVTE
DEKRDLFLRV NDTAKAYPNK LIMSMLEDWA AATPDKTALV FREQRVTYRE LNERVNQLAH
TLREKGVQPD DLVMLMAERS VEMMVAIFAV LKAGGAYLPI DPHSPAERIA YIFADSGAKL
VLAQSPFVEK ASMAEVVLDL NSASSYAADT SNPPLVNQPG DLVYVMYTSG STGKPKGVMI
EHGALLNVLH GMQDEYPLLQ DDAFLLKTTY IFDISVAEIF GWVPGRGKLV ILEPEAEKNP
KAIWQAVVGA GITHINFVPS MLIPFVEYLE GRTEANRLRY ILACGEAMPD ELVPKVYEVL
PEVKLENIYG PTEATIYASR YSLAKGSQES PVPIGKPLPN YRMYIINRHG QLQPIGVPGE
LCIAGASLAR GYLNNPALTE EKFTPHPLEK GERIYRTGDL ARYREDGNIE YLGRMDHQVK
IRGYRIELDE IRSKLIQEET IQDAVVVARN DQNGQAYLCA YLLSEQEWTV GQLRELLRRE
LPEYMIPAHF VLLKQFPLTA NGKLDRKALP EPDGSVKAEA EYAAPRTELE ATLAHIWGEV
LGIERIGIRD NFFELGGDSI KGLQIASRLQ RINWTMVINH LFLYPTIEQI APFVTSEQVV
IEQGLVEGLV KLTPIQRDFF ERITADRHHW NQARMLFCRD GLEREWVVET LNALVLQHDA
LRMRFRETEQ GIVQFHQGNE GKLFGFHVFD CTEELDIAKK VEEQANVLQS GMNLQEGPLV
QAALFMTRTG DHLLLAIHQL VVDEASWRII LEDFQTAYKQ KAAGEPIALP NKTHSYQSWA
EELHNAANSK KLTSELGYWR KIASSPTRPL PQDQEPLSRT EQSTATAAIR FAKAETANLL
HEANHAYQTE AQELLLAALG MALRDWTRAD DVTVFLEKDG RESAAKGLDV SRTVGWFHSL
FPVVLSAARS GDPGEQIKQV KEMLRAIPHQ GSGYSILKQL TDLRHKHPDD FTLQPKIVVH
AWEQLDAGLE TDWLTLSHLP QGSVRGANAE RMQQLDVFSK ISNGELTIHI QYHRDEYRKA
TIDKLLELYQ AHLNALLAHC LQKTETELTP SDFVDKNLSR SELDDIMDLI SDL