LOCUS       NP_001357805            3677 aa            linear   ROD 29-APR-2025
DEFINITION  dystrophin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001357805 XP_017457399
VERSION     NP_001357805.1
DBSOURCE    REFSEQ: accession NM_001370876.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3677)
  AUTHORS   Yamanouchi,K., Kato,S., Tanaka,Y., Ikeda,M., Oshimo,Y., Shiga,T.,
            Hatamoto,K., Chambers,J., Imamura,T., Hiramatsu,R., Uchida,K.,
            Matsuda,F., Matsuwaki,T. and Kohsaka,T.
  TITLE     Identification and characterization of dystrophin-locus-derived
            testis-specific protein: A testis-specific gene within the intronic
            region of the rat dystrophin gene
  JOURNAL   J Reprod Dev 70 (2), 55-64 (2024)
   PUBMED   38246612
  REMARK    GeneRIF: Identification and characterization of
            dystrophin-locus-derived testis-specific protein: A testis-specific
            gene within the intronic region of the rat dystrophin gene.
REFERENCE   2  (residues 1 to 3677)
  AUTHORS   Chikamoto,A., Tochinai,R., Sekizawa,S.I. and Kuwahara,M.
  TITLE     Plasticity occurs in a specific phenotype of neurons in the nucleus
            tractus solitarius of dystrophin gene-mutated rats
  JOURNAL   Eur J Neurosci 58 (11), 4282-4297 (2023)
   PUBMED   37933572
  REMARK    GeneRIF: Plasticity occurs in a specific phenotype of neurons in
            the nucleus tractus solitarius of dystrophin gene-mutated rats.
REFERENCE   3  (residues 1 to 3677)
  AUTHORS   Sanchez,A., Aragon,J., Ceja,V., Rendon,A. and Montanez,C.
  TITLE     Nuclear transport and subcellular localization of the dystrophin
            Dp71 and Dp40 isoforms in the PC12 cell line
  JOURNAL   Biochem Biophys Res Commun 630, 125-132 (2022)
   PUBMED   36155058
  REMARK    GeneRIF: Nuclear transport and subcellular localization of the
            dystrophin Dp71 and Dp40 isoforms in the PC12 cell line.
REFERENCE   4  (residues 1 to 3677)
  AUTHORS   Garcia-Cruz,C., Merino-Jimenez,C., Aragon,J., Ceja,V.,
            Gonzalez-Assad,B., Reyes-Grajeda,J.P. and Montanez,C.
  TITLE     Overexpression of the dystrophins Dp40 and Dp40L170P modifies
            neurite outgrowth and the protein expression profile of PC12 cells
  JOURNAL   Sci Rep 12 (1), 1410 (2022)
   PUBMED   35082358
  REMARK    GeneRIF: Overexpression of the dystrophins Dp40 and Dp40L170P
            modifies neurite outgrowth and the protein expression profile of
            PC12 cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3677)
  AUTHORS   Paul-Gonzalez,S., Aragon,J., Rodriguez-Martinez,G., Romo-Yanez,J.
            and Montanez,C.
  TITLE     Differential expression of Dp71 and Dp40 isoforms in proliferating
            and differentiated neural stem cells: Identification of Dp40
            splicing variants
  JOURNAL   Biochem Biophys Res Commun 560, 152-158 (2021)
   PUBMED   33989907
REFERENCE   6  (residues 1 to 3677)
  AUTHORS   Kim,T.W., Wu,K., Xu,J.L. and Black,I.B.
  TITLE     Detection of dystrophin in the postsynaptic density of rat brain
            and deficiency in a mouse model of Duchenne muscular dystrophy
  JOURNAL   Proc Natl Acad Sci U S A 89 (23), 11642-11644 (1992)
   PUBMED   1454857
REFERENCE   7  (residues 1 to 3677)
  AUTHORS   Gilgenkrantz,H., Hugnot,J.P., Lambert,M., Chafey,P., Kaplan,J.C.
            and Kahn,A.
  TITLE     Positive and negative regulatory DNA elements including a CCArGG
            box are involved in the cell type-specific expression of the human
            muscle dystrophin gene
  JOURNAL   J Biol Chem 267 (15), 10823-10830 (1992)
   PUBMED   1316911
REFERENCE   8  (residues 1 to 3677)
  AUTHORS   Blake,D.J., Love,D.R., Tinsley,J., Morris,G.E., Turley,H.,
            Gatter,K., Dickson,G., Edwards,Y.H. and Davies,K.E.
  TITLE     Characterization of a 4.8kb transcript from the Duchenne muscular
            dystrophy locus expressed in Schwannoma cells
  JOURNAL   Hum Mol Genet 1 (2), 103-109 (1992)
   PUBMED   1301145
REFERENCE   9  (residues 1 to 3677)
  AUTHORS   Rapaport,D., Lederfein,D., den Dunnen,J.T., Grootscholten,P.M., Van
            Ommen,G.J., Fuchs,O., Nudel,U. and Yaffe,D.
  TITLE     Characterization and cell type distribution of a novel, major
            transcript of the Duchenne muscular dystrophy gene
  JOURNAL   Differentiation 49 (3), 187-193 (1992)
   PUBMED   1377655
REFERENCE   10 (residues 1 to 3677)
  AUTHORS   Malhotra,S.B., Hart,K.A., Klamut,H.J., Thomas,N.S., Bodrug,S.E.,
            Burghes,A.H., Bobrow,M., Harper,P.S., Thompson,M.W., Ray,P.N. et
            al.
  TITLE     Frame-shift deletions in patients with Duchenne and Becker muscular
            dystrophy
  JOURNAL   Science 242 (4879), 755-759 (1988)
   PUBMED   3055295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jun 8, 2019 this sequence version replaced XP_017457399.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. This variant is based on
            transcript alignments from orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3677
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..3677
                     /product="dystrophin isoform 1"
                     /note="apodystrophin-3; apodystrophin-I; dystrophin,
                     muscular dystrophy; dystrophin-related"
                     /calculated_mol_wt=425699
     Region          1..240
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          11..121
                     /region_name="CH_DMD_rpt1"
                     /note="first calponin homology (CH) domain found in
                     dystrophin and similar proteins; cd21231"
                     /db_xref="CDD:409080"
     Site            order(11..13,16..17,19..21,23..24,27,112,115,119..121)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409080"
     Site            order(17,21,72,74..75,78..79,81,90..98,103,105..106,
                     108..109,112..113,116)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409080"
     Region          63..72
                     /region_name="ANK2-and ANK-3 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          136..246
                     /region_name="CH_DMD_rpt2"
                     /note="second calponin homology (CH) domain found in
                     dystrophin and similar proteins; cd21233"
                     /db_xref="CDD:409082"
     Site            order(136,140,191,193..194,197..198,200,209..217,224,
                     226..227,229..230,233..234,237)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409082"
     Site            order(139..140,210..214,217,220,222..227,230,233..234,
                     236..237,241..246)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409082"
     Region          342..447
                     /region_name="Spectrin 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          345..559
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            449..454
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          451..557
                     /region_name="Spectrin 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          560..668
                     /region_name="Spectrin 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          561..781
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            669..674
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          728..934
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          728..828
                     /region_name="Spectrin 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            830..835
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          831..935
                     /region_name="Spectrin 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          944..1153
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          944..1046
                     /region_name="Spectrin 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            1047..1052
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1049..1154
                     /region_name="Spectrin 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          1050..1264
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1127..2060
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            1156..1161
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1163..1264
                     /region_name="Spectrin 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          1268..1464
                     /region_name="Spectrin 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          1416..1914
                     /region_name="Interaction with SYNM.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          1878..1980
                     /region_name="Spectrin 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2001..2098
                     /region_name="Spectrin 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2106..2316
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2106..2209
                     /region_name="Spectrin 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            order(2210..2214,2216)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2215..2316
                     /region_name="Spectrin 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2317..2415
                     /region_name="Spectrin 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2464..2678
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2465..2569
                     /region_name="Spectrin 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            2570..2575
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2576..2678
                     /region_name="Spectrin 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2682..2925
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2682..2786
                     /region_name="Spectrin 21. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            2795..2800
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2800..2922
                     /region_name="Spectrin 22. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          2926..3032
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          2927..3032
                     /region_name="Spectrin 23. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            3033..3037
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          3050..3400
                     /region_name="Interaction with SYNM.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          3051..3080
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(3064,3075)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          3117..3278
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(3117..3118,3120..3121,3139,3143,3147,3149..3150,
                     3153,3164..3170,3172..3173,3176,3182,3195,3236..3237,3239)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          3117..3156
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3163..3197
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Site            3180..3182
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          3203..3239
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3252..3278
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3303..3351
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(3305,3308,3320,3323,3329,3332,3342,3346)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(3305,3308,3329,3332)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(3306,3317,3319,3325,3327)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(3318,3333,3348,3351)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(3320,3323,3342,3346)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          3458..3510
                     /region_name="Binds to SNTB1.
                     /evidence=ECO:0000250|UniProtKB:P11532"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            3475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Region          3520..3546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Region          3595..3677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11530.2)"
     Site            3604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3615
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     Site            3658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11532; propagated from
                     UniProtKB/Swiss-Prot (P11530.2)"
     CDS             1..3677
                     /gene="Dmd"
                     /gene_synonym="DNADMD1"
                     /coded_by="NM_001370876.1:245..11278"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24907"
                     /db_xref="RGD:2507"
ORIGIN      
        1 mlwweevedc yeredvqkkt ftkwinaqfs kfgkqhidnl fsdlqdgkrl ldllegltgq
       61 klpkekgstr vhalnnvnka lqvlqknnvd lvnigstdiv dgnhkltlgl iwniilhwqv
      121 knvmktimag lqqtnsekil lswvrestrn ypqvnvlnft sswsdglaln alihshrpdl
      181 fdwnsvvsqq satqrlehaf niakcqlgie klldpedvat typdkksilm yitslfqvlp
      241 qqvsieaire vemlprpskv treehfqlhh qmhysqqitv slaqgyeqts sspkprfksy
      301 aftqaayvat sdssqspyps qhleapgsks fgsslietev nldsyqtale evlswllsae
      361 dtlraqgeis kdveevkeqf hahegfmmdl tshqglvgnv lqlgsrlvgk gkltedeete
      421 vqeqmnllns rweclrvasm ekqsnlhkvl mdlqnqklke lddwltktee rtkkmeeepl
      481 gpdledlkcq vqqhkvlqed leqeqvrvns lthmvvvvde ssgdhataal eeqlkvlgdr
      541 wanickwted rwillqdill kwqrfteeqc lfskwlseke damkniqtsg fedqnemvss
      601 lqnisalkid lekkkqsmek lsslnqdlls alknksvtqk memwmenfaq rwdnltqkle
      661 kssaqisqav tttqpsltqt tvmetvtmvt treqimvkha qeelpppppq kkrqitvdse
      721 irkrldvdit elhswitrse avlqssefav yrkegnisdl kekvnaiare kaekfrklqd
      781 asrsaqalve qmvnegvnae sirqaseqln srwtefcqll servnwleyq nniitfynql
      841 qqleqmttta enllktqptt lseptaiksq lkickdevnr lsalqpqier lkiqsltlke
      901 kgqgpmflda dfvaftnhfn yvfdgvrare kelqtifdtl ppmryqetms sirtwiqqse
      961 nklsiphlsv teyeimeerl gklqalqssl keqqngfnyl natvkeiakk apseisqkyq
     1021 sefeevegrw kklstqlveh cqkleehmnk lrkfqnhkkt lqkwmaevdv flkeewpalg
     1081 daeilkkqlk qcrllvgdiq tiqpslnsvn eggqkiksea efefasrlek elkelntqwd
     1141 hicrqvytrk ealkagldkt vslqkdlsem hewmtqaeee ylerdfeykt pdelqtavee
     1201 mkrakeealq keakvkllte tvnsvisqap paaqealkke letlttnyqw lctrlngkck
     1261 tleevwacwh ellsylekan kwlnevelkl katenvpaga eeitevlesl enlmhhseen
     1321 pnqirllaqt ltdggvmdel ineeletfns rwrelheeav rkqklleqsi qsaqeieksl
     1381 hliqeslefi dkqlaayiad kvdaaqmpqe aqkiqsdlts heisleemkk hnqgkdanqr
     1441 vlsqidvaqk klqdvsikfr lfqkpanfeq rleeskmild evkmhlpale tksveqevvq
     1501 sqlshcvnly kslsevksev emviktgrqi vqkkqtenpk eldervtalk lhynelgakv
     1561 terkqqlekc lklsrkmrke mnvltewlaa tdteltkrsa vegmpsnlds evawgkatqk
     1621 eiekqkahlk svtelgdslk tvlgkketlv edkltllnsn wiavtsrvee wlnllleyqk
     1681 hmesfdqnve hitkwiihtd elldesekrk pqqkedilkr lkaemndirp kvdatrdqaa
     1741 klmanrgdyc rkivepqise lnrrfaaish riktgkasip lkeleqfnsd iqklleplea
     1801 eiqqgvnlke edfnkdmsed negtvnellq rgdnlqqrit derkreeikl kqqllqtkhn
     1861 alkdlrsqrr kkaleishqw yqyksqaddl lkcldeiekk laslpeprde rkikeidrel
     1921 qkkkeelnav rrqaeslsen gaamaveptq iqlskrwrei esnfaqfrrl nfaqihtlhe
     1981 etmvvttedm pldvsyvpst ylteishilq alseveqlln apelnakdfe dlfkqeeslk
     2041 nikenlqqis gridvihkkk taalqsatpm ervklqeavs qmdfhwekln rmykerqgrf
     2101 drsvekwrhf hydmkvfnqw lndveqffkk tqnpenweha kykwylkelq dgigqrqavv
     2161 rtlnatgeei iqqssktdan ilqeklgsls lrwhevckel aerrkrveeq knvfsefqrd
     2221 lnefvswlee adniattppg deeqlkekle qvkllteelp lrqgilkqln etggavlvsa
     2281 pirpeeqdkl ekklkqtnlq wikvsralpe kqgelevhik dfrqfeeqld hlllwlspir
     2341 nqleiynqps qpgpfdlket evtvqakqpd verllskgqh lykekpstqp vkrkledlrs
     2401 eweavnhllw elrtkqpdra pglsttgasa sqtvtvvtqp vdtketvisk lempssllle
     2461 vpaladfnra wteltdwlsl ldrviksqrv mvgdledine miikqkatlq dleqrrpqle
     2521 elitaaqnlk nktsnqeart iitdrieriq iqwdevqeql qnrrqqlnem lkdstqwlea
     2581 keeaeqvigq argkldswke gphtmdaiqk kitetkqlak dlrqrqinvd vandlalkll
     2641 rdysaddtrk vhmitenint swgnilkrvs ereaaleetq rllqqfpldl ekflawitea
     2701 ettanvlqda srkeklleds rgvrelmkpw qdlqgeieah tdiyhnlden gqkilrsleg
     2761 sdeapllqrr ldnmnfkwse lrkkslnirs hlevssdqwk rlhlslqell vwlqlkddel
     2821 srqapiggdf pavqkqndvh rafkrelktk epvimstlet vriflteqpl egleklyqep
     2881 relppeeraq nvtrllrkqa eevntewdkl nlhsadwqrk idealerlqe lqeaadeldl
     2941 klrqaevikg swqpvgdlli dslqdhlekv kalrgeiapl kenvnhvndl ahhlttlgiq
     3001 lspynlsile dlntrwrllq vavedrvrql heahrdfgpa sqhflstsvq gpweraispn
     3061 kvpyyinhet qttcwdhpkm telyqsladl nnvrfsayrt amklrrlqka lcldllslsa
     3121 acdaldqhnl kqndqpmdil qiinclttiy drleqehnnl vnvplcvdmc lnwllnvydt
     3181 grtgrirvls fktgiislck ahledkyryl fkqvasstgf cdqrrlglll hdsiqiprql
     3241 gevasfggsn iepsvrscfq fannkpeiea alfldwmrle pqsmvwlpvl hrvaaaetak
     3301 hqakcnicke cpiigfryrs lkhfnydicq scffsgrvak ghkmhypmve yctpttsged
     3361 vrdfakvlkn kfrtkryfak hprmgylpvq tvlegdnmet pvtlinfwpv dsapasspql
     3421 shddthsrie hyasrlaeme nsngsylnds ispnesidde hlliqhycqs lnqdsplsqp
     3481 rspaqilisl eseergeler iladleeenr nlqaeydrlk qqhehkglsp lpsppemmpt
     3541 spqsprdael iaeakllrqh kgrlearmqi ledhnkqles qlhrlrqlle qpqaeakvng
     3601 ttvsspstsl qrsdssqpml lrvvgsqtse smgeedllsp pqdtstglee vmeqlnnsfp
     3661 ssrgrnapgk pmredtm
//
