ID RS7_ECOLI Reviewed; 179 AA.
AC P02359; Q2M706;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 29-MAY-2013, entry version 156.
DE RecName: Full=30S ribosomal protein S7;
GN Name=rpsG; OrderedLocusNames=b3341, JW3303;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-179.
RC STRAIN=B, and K;
RX PubMed=385062;
RA Reinbolt J., Tritsch D., Wittmann-Liebold B.;
RT "The primary structure of ribosomal protein S7 from E. coli strains K
RT and B.";
RL Biochimie 61:501-522(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 148-179.
RC STRAIN=K12;
RX PubMed=6989816;
RA Post L.E., Nomura M.;
RT "DNA sequences from the str operon of Escherichia coli.";
RL J. Biol. Chem. 255:4660-4666(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC STRAIN=B/R;
RX PubMed=1552908; DOI=10.1007/BF00299141;
RA Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.;
RT "Mutant sequences in the rpsL gene of Escherichia coli B/r:
RT mechanistic implications for spontaneous and ultraviolet light
RT mutagenesis.";
RL Mol. Gen. Genet. 232:89-96(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1398129; DOI=10.1016/0378-1119(92)90014-G;
RA Johanson U., Hughes D.;
RT "Comparison of the complete sequence of the str operon in Salmonella
RT typhimurium and Escherichia coli.";
RL Gene 120:93-98(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-156.
RC STRAIN=L44;
RA Weigel C.T.O.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 111-131, AND CROSS-LINKING TO RRNA.
RC STRAIN=MRE-600;
RX PubMed=7556101;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [9]
RP CROSS-LINKING TO IF3.
RC STRAIN=B;
RX PubMed=7000779;
RA MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.;
RT "Photochemical cross-linking of initiation factor-3 to Escherichia
RT coli 30 S ribosomal subunits.";
RL J. Biol. Chem. 255:10526-10531(1980).
RN [10]
RP CROSS-LINKING TO IF3.
RC STRAIN=MRE-600;
RX PubMed=6349681; DOI=10.1021/bi00282a020;
RA Boileau G., Butler P., Hershey J.W.B., Traut R.R.;
RT "Direct cross-links between initiation factors 1, 2, and 3 and
RT ribosomal proteins promoted by 2-iminothiolane.";
RL Biochemistry 22:3162-3170(1983).
RN [11]
RP ROLE IN SUBUNIT ASSEMBLY.
RC STRAIN=K12 / D10;
RX PubMed=2461734; DOI=10.1021/bi00418a057;
RA Nowotny V., Nierhaus K.H.;
RT "Assembly of the 30S subunit from Escherichia coli ribosomes occurs
RT via two assembly domains which are initiated by S4 and S7.";
RL Biochemistry 27:7051-7055(1988).
RN [12]
RP MECHANISM OF TRANSLATION REGULATION.
RC STRAIN=K12;
RX PubMed=7507167; DOI=10.1016/S0022-2836(05)80020-8;
RA Saito K., Mattheakis L.C., Nomura M.;
RT "Post-transcriptional regulation of the str operon in Escherichia
RT coli. Ribosomal protein S7 inhibits coupled translation of S7 but not
RT its independent translation.";
RL J. Mol. Biol. 235:111-124(1994).
RN [13]
RP CROSS-LINKING TO THE TRNA CENTRAL FOLD.
RC STRAIN=MRE-600;
RX PubMed=8524654; DOI=10.1093/nar/23.22.4635;
RA Osswald M., Doering T., Brimacombe R.;
RT "The ribosomal neighbourhood of the central fold of tRNA: cross-links
RT from position 47 of tRNA located at the A, P or E site.";
RL Nucleic Acids Res. 23:4635-4641(1995).
RN [14]
RP CROSS-LINKING TO MRNA.
RC STRAIN=B, and K;
RX PubMed=10606263; DOI=10.1017/S1355838299991550;
RA Greuer B., Thiede B., Brimacombe R.;
RT "The cross-link from the upstream region of mRNA to ribosomal protein
RT S7 is located in the C-terminal peptide: experimental verification of
RT a prediction from modeling studies.";
RL RNA 5:1521-1525(1999).
RN [15]
RP MUTAGENESIS OF CONSERVED SURFACE RESIDUES.
RC STRAIN=K;
RX PubMed=10772857; DOI=10.1006/jmbi.2000.3563;
RA Fredrick K., Dunny G.M., Noller H.F.;
RT "Tagging ribosomal protein S7 allows rapid identification of mutants
RT defective in assembly and function of 30S subunits.";
RL J. Mol. Biol. 298:379-394(2000).
RN [16]
RP MUTAGENESIS OF CONSERVED RESIDUES.
RC STRAIN=K12;
RX PubMed=11160889; DOI=10.1093/nar/29.3.677;
RA Robert F., Brakier-Gingras L.;
RT "Ribosomal protein S7 from Escherichia coli uses the same determinants
RT to bind 16S ribosomal RNA and its messenger RNA.";
RL Nucleic Acids Res. 29:677-682(2001).
RN [17]
RP MASS SPECTROMETRY.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [18]
RP MODELING OF IF-3/30S SUBUNIT INTERACTION.
RX PubMed=11684020; DOI=10.1016/S1097-2765(01)00356-2;
RA Dallas A., Noller H.F.;
RT "Interaction of translation initiation factor 3 with the 30S ribosomal
RT subunit.";
RL Mol. Cell 8:855-864(2001).
RN [19]
RP 3D-STRUCTURE MODELING.
RX PubMed=12244297; DOI=10.1038/nsb841;
RA Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
RT "All-atom homology model of the Escherichia coli 30S ribosomal
RT subunit.";
RL Nat. Struct. Biol. 9:750-755(2002).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
RC STRAIN=MRE-600;
RX PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
RA Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using
RT real-space refinement.";
RL Cell 113:789-801(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP STRUCTURES.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
RA Vila-Sanjurjo A., Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC directly to 16S rRNA where it nucleates assembly of the head
CC domain of the 30S subunit. Is located at the subunit interface
CC close to the decoding center, where it has been shown to contact
CC mRNA. Has been shown to contact tRNA in both the P and E sites; it
CC probably blocks exit of the E site tRNA.
CC -!- FUNCTION: Protein S7 is also a translational repressor protein; it
CC regulates the expression of the str operon members to different
CC degrees by binding to its mRNA.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9
CC and S11 (By similarity). Cross-links to IF3 and the P and E site
CC tRNAs.
CC -!- INTERACTION:
CC P0A707:infC; NbExp=3; IntAct=EBI-543074, EBI-546262;
CC P0A850:tig; NbExp=3; IntAct=EBI-543074, EBI-544862;
CC -!- MASS SPECTROMETRY: Mass=19888.7; Method=MALDI; Range=2-179;
CC Source=PubMed:10094780;
CC -!- MISCELLANEOUS: The strain K12 sequence is shown.
CC -!- MISCELLANEOUS: Has been predicted to contact the N-terminal domain
CC of IF-3 based on footprint studies (PubMed:11684020); exactly how
CC IF-3 interacts with the 30S subunit is controversial.
CC -!- SIMILARITY: Belongs to the ribosomal protein S7P family.
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DR EMBL; U18997; AAA58138.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76366.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77950.1; -; Genomic_DNA.
DR EMBL; V00355; CAA23649.1; -; Genomic_DNA.
DR EMBL; J01689; AAA50990.1; -; Genomic_DNA.
DR EMBL; X64592; CAA45881.1; -; Genomic_DNA.
DR EMBL; X65735; CAA46644.1; -; Genomic_DNA.
DR EMBL; J01688; AAA50989.1; -; Genomic_DNA.
DR PIR; H65127; R3EC7K.
DR RefSeq; NP_417800.1; NC_000913.2.
DR RefSeq; YP_492091.1; NC_007779.1.
DR PDB; 1EG0; EM; 11.50 A; D=1-146.
DR PDB; 1M5G; Model; -; G=3-156.
DR PDB; 1ML5; EM; 14.00 A; J=1-156.
DR PDB; 1P6G; EM; 12.30 A; G=2-179.
DR PDB; 1P87; EM; 11.50 A; G=2-179.
DR PDB; 1VS5; X-ray; 3.46 A; G=1-179.
DR PDB; 1VS7; X-ray; 3.46 A; G=1-179.
DR PDB; 2AVY; X-ray; 3.46 A; G=2-179.
DR PDB; 2AW7; X-ray; 3.46 A; G=2-179.
DR PDB; 2GY9; EM; 15.00 A; G=20-155.
DR PDB; 2GYB; EM; 15.00 A; G=20-155.
DR PDB; 2I2P; X-ray; 3.22 A; G=2-178.
DR PDB; 2I2U; X-ray; 3.22 A; G=2-178.
DR PDB; 2QAL; X-ray; 3.21 A; G=2-179.
DR PDB; 2QAN; X-ray; 3.21 A; G=2-179.
DR PDB; 2QB9; X-ray; 3.54 A; G=2-179.
DR PDB; 2QBB; X-ray; 3.54 A; G=2-179.
DR PDB; 2QBD; X-ray; 3.30 A; G=2-179.
DR PDB; 2QBF; X-ray; 3.30 A; G=2-179.
DR PDB; 2QBH; X-ray; 4.00 A; G=2-179.
DR PDB; 2QBJ; X-ray; 4.00 A; G=2-179.
DR PDB; 2QOU; X-ray; 3.93 A; G=2-179.
DR PDB; 2QOW; X-ray; 3.93 A; G=2-179.
DR PDB; 2QOY; X-ray; 3.50 A; G=2-179.
DR PDB; 2QP0; X-ray; 3.50 A; G=2-179.
DR PDB; 2VHO; X-ray; 3.74 A; G=2-179.
DR PDB; 2VHP; X-ray; 3.74 A; G=2-179.
DR PDB; 2WWL; EM; 5.80 A; G=3-152.
DR PDB; 2YKR; EM; 9.80 A; G=2-152.
DR PDB; 2Z4K; X-ray; 4.45 A; G=2-179.
DR PDB; 2Z4M; X-ray; 4.45 A; G=2-179.
DR PDB; 3DF1; X-ray; 3.50 A; G=2-178.
DR PDB; 3DF3; X-ray; 3.50 A; G=2-178.
DR PDB; 3E1A; EM; -; U=1-179.
DR PDB; 3E1C; EM; -; U=1-179.
DR PDB; 3FIH; EM; 6.70 A; G=3-152.
DR PDB; 3I1M; X-ray; 3.19 A; G=1-179.
DR PDB; 3I1O; X-ray; 3.19 A; G=1-179.
DR PDB; 3I1Q; X-ray; 3.81 A; G=1-179.
DR PDB; 3I1S; X-ray; 3.81 A; G=1-179.
DR PDB; 3I1Z; X-ray; 3.71 A; G=1-179.
DR PDB; 3I21; X-ray; 3.71 A; G=1-179.
DR PDB; 3IZV; EM; -; K=1-179.
DR PDB; 3IZW; EM; -; K=1-179.
DR PDB; 3J00; EM; -; G=2-179.
DR PDB; 3J0U; EM; 12.10 A; J=2-179.
DR PDB; 3J0V; EM; 14.70 A; J=2-179.
DR PDB; 3J0X; EM; 13.50 A; J=2-179.
DR PDB; 3J0Z; EM; 11.50 A; J=2-179.
DR PDB; 3J10; EM; 11.50 A; J=2-179.
DR PDB; 3J13; EM; 13.10 A; I=2-179.
DR PDB; 3J18; EM; 8.30 A; G=2-152.
DR PDB; 3J36; EM; 9.80 A; G=2-179.
DR PDB; 3KC4; EM; -; G=1-179.
DR PDB; 3OAQ; X-ray; 3.25 A; G=2-152.
DR PDB; 3OAR; X-ray; 3.25 A; G=3-152.
DR PDB; 3OFA; X-ray; 3.19 A; G=2-152.
DR PDB; 3OFB; X-ray; 3.19 A; G=3-152.
DR PDB; 3OFO; X-ray; 3.10 A; G=2-152.
DR PDB; 3OFP; X-ray; 3.10 A; G=3-152.
DR PDB; 3OFX; X-ray; 3.29 A; G=2-152.
DR PDB; 3OFY; X-ray; 3.29 A; G=3-152.
DR PDB; 3OR9; X-ray; 3.30 A; G=1-179.
DR PDB; 3ORA; X-ray; 3.30 A; G=1-179.
DR PDB; 3SFS; X-ray; 3.20 A; G=1-156.
DR PDB; 3UOQ; X-ray; 3.70 A; G=1-179.
DR PDB; 4A2I; EM; 16.50 A; G=3-152.
DR PDB; 4ADV; EM; 13.50 A; G=2-179.
DR PDB; 4GAQ; X-ray; 3.30 A; G=1-179.
DR PDB; 4GAS; X-ray; 3.30 A; G=1-179.
DR PDB; 4GD1; X-ray; 3.00 A; G=2-152.
DR PDB; 4GD2; X-ray; 3.00 A; G=2-152.
DR PDBsum; 1EG0; -.
DR PDBsum; 1M5G; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 1P6G; -.
DR PDBsum; 1P87; -.
DR PDBsum; 1VS5; -.
DR PDBsum; 1VS7; -.
DR PDBsum; 2AVY; -.
DR PDBsum; 2AW7; -.
DR PDBsum; 2GY9; -.
DR PDBsum; 2GYB; -.
DR PDBsum; 2I2P; -.
DR PDBsum; 2I2U; -.
DR PDBsum; 2QAL; -.
DR PDBsum; 2QAN; -.
DR PDBsum; 2QB9; -.
DR PDBsum; 2QBB; -.
DR PDBsum; 2QBD; -.
DR PDBsum; 2QBF; -.
DR PDBsum; 2QBH; -.
DR PDBsum; 2QBJ; -.
DR PDBsum; 2QOU; -.
DR PDBsum; 2QOW; -.
DR PDBsum; 2QOY; -.
DR PDBsum; 2QP0; -.
DR PDBsum; 2VHO; -.
DR PDBsum; 2VHP; -.
DR PDBsum; 2WWL; -.
DR PDBsum; 2YKR; -.
DR PDBsum; 2Z4K; -.
DR PDBsum; 2Z4M; -.
DR PDBsum; 3DF1; -.
DR PDBsum; 3DF3; -.
DR PDBsum; 3E1A; -.
DR PDBsum; 3E1C; -.
DR PDBsum; 3FIH; -.
DR PDBsum; 3I1M; -.
DR PDBsum; 3I1O; -.
DR PDBsum; 3I1Q; -.
DR PDBsum; 3I1S; -.
DR PDBsum; 3I1Z; -.
DR PDBsum; 3I21; -.
DR PDBsum; 3IZV; -.
DR PDBsum; 3IZW; -.
DR PDBsum; 3J00; -.
DR PDBsum; 3J0U; -.
DR PDBsum; 3J0V; -.
DR PDBsum; 3J0X; -.
DR PDBsum; 3J0Z; -.
DR PDBsum; 3J10; -.
DR PDBsum; 3J13; -.
DR PDBsum; 3J18; -.
DR PDBsum; 3J36; -.
DR PDBsum; 3KC4; -.
DR PDBsum; 3OAQ; -.
DR PDBsum; 3OAR; -.
DR PDBsum; 3OFA; -.
DR PDBsum; 3OFB; -.
DR PDBsum; 3OFO; -.
DR PDBsum; 3OFP; -.
DR PDBsum; 3OFX; -.
DR PDBsum; 3OFY; -.
DR PDBsum; 3OR9; -.
DR PDBsum; 3ORA; -.
DR PDBsum; 3SFS; -.
DR PDBsum; 3UOQ; -.
DR PDBsum; 4A2I; -.
DR PDBsum; 4ADV; -.
DR PDBsum; 4GAQ; -.
DR PDBsum; 4GAS; -.
DR PDBsum; 4GD1; -.
DR PDBsum; 4GD2; -.
DR ProteinModelPortal; P02359; -.
DR SMR; P02359; 2-179.
DR DIP; DIP-10783N; -.
DR IntAct; P02359; 150.
DR MINT; MINT-1236482; -.
DR STRING; 511145.b3341; -.
DR PhosSite; P0810434; -.
DR PaxDb; P02359; -.
DR PRIDE; P02359; -.
DR EnsemblBacteria; AAC76366; AAC76366; b3341.
DR EnsemblBacteria; BAE77950; BAE77950; BAE77950.
DR GeneID; 12933477; -.
DR GeneID; 947846; -.
DR KEGG; ecj:Y75_p3835; -.
DR KEGG; eco:b3341; -.
DR PATRIC; 32122114; VBIEscCol129921_3434.
DR EchoBASE; EB0899; -.
DR EcoGene; EG10906; rpsG.
DR eggNOG; COG0049; -.
DR HOGENOM; HOG000039067; -.
DR KO; K02992; -.
DR OMA; RREKTMT; -.
DR ProtClustDB; PRK05302; -.
DR BioCyc; EcoCyc:EG10906-MONOMER; -.
DR BioCyc; ECOL316407:JW3303-MONOMER; -.
DR EvolutionaryTrace; P02359; -.
DR Genevestigator; P02359; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:EcoCyc.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR Gene3D; 1.10.455.10; -; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1; -.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR PANTHER; PTHR11205:SF13; PTHR11205:SF13; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; Ribosomal_S7; 1.
DR TIGRFAMs; TIGR01029; rpsG_bact; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 179 30S ribosomal protein S7.
FT /FTId=PRO_0000124259.
FT VARIANT 157 179 Missing (in strain: B and L44).
FT MUTAGEN 2 18 Missing: Defective in ribosome assembly;
FT accumulates to abnormally high levels on
FT polysomes; significantly decreases
FT affinity for its own mRNA.
FT MUTAGEN 36 36 K->A,E: Defective in ribosome assembly.
FT MUTAGEN 116 116 M->G: Significantly decreases affinity
FT for its own mRNA.
FT CONFLICT 92 92 Missing (in Ref. 3; AA sequence).
FT TURN 16 18
FT HELIX 21 30
FT HELIX 32 34
FT HELIX 36 51
FT TURN 52 54
FT HELIX 59 69
FT STRAND 72 75
FT STRAND 78 80
FT STRAND 81 83
FT STRAND 88 90
FT HELIX 93 109
FT STRAND 113 115
FT HELIX 116 128
FT HELIX 134 147
FT HELIX 148 150
SQ SEQUENCE 179 AA; 20019 MW; 8627DB380C4A9C0D CRC64;
MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE
AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL
ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN
//
