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Structural polyprotein (PP) [Cleaved into: Precursor of VP2 (Pre-VP2); Capsid protein VP2; Structural peptide 1 (p1); Structural peptide 2 (p2); Structural peptide 3 (p3); Protease VP4 (EC 3.4.21.-) (Non-structural protein VP4) (NS); Capsid protein VP3]

 POLS_IPNVS              Reviewed;         972 AA.
Q703G9; P90205; Q4KTX8; Q69CH7; Q69CI0; Q69CI3; Q6U2N3; Q6U2N5;
Q6U2N8; Q6U2P1; Q6U2P5; Q6U2P7; Q6UAY7; Q82733; Q990Q0; Q9YJV0;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-MAY-2017, entry version 64.
RecName: Full=Structural polyprotein;
Short=PP;
Contains:
RecName: Full=Precursor of VP2;
Short=Pre-VP2;
Contains:
RecName: Full=Capsid protein VP2;
Contains:
RecName: Full=Structural peptide 1;
Short=p1;
Contains:
RecName: Full=Structural peptide 2;
Short=p2;
Contains:
RecName: Full=Structural peptide 3;
Short=p3;
Contains:
RecName: Full=Protease VP4;
EC=3.4.21.-;
AltName: Full=Non-structural protein VP4;
Short=NS;
Contains:
RecName: Full=Capsid protein VP3;
Infectious pancreatic necrosis virus (strain Sp) (IPNV).
Viruses; dsRNA viruses; Birnaviridae; Aquabirnavirus.
NCBI_TaxID=11005;
NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
NCBI_TaxID=8028; Salmo.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 443-457;
487-495 AND 496-508, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=31-75;
PubMed=15269363; DOI=10.1099/vir.0.80012-0;
Galloux M., Chevalier C., Henry C., Huet J.-C., Da Costa B.,
Delmas B.;
"Peptides resulting from the pVP2 C-terminal processing are present in
infectious pancreatic necrosis virus particles.";
J. Gen. Virol. 85:2231-2236(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Mason;
Mason C.L., Leong J.C.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Tseng;
Tseng C.-C., Lo C.-F., Kou G.-H.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate NVI-001, Isolate NVI-010, Isolate NVI-011,
Isolate NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020,
and Isolate NVI-023;
PubMed=15063114; DOI=10.1016/j.virol.2003.12.016;
Santi N., Vakharia V.N., Evensen O.;
"Identification of putative motifs involved in the virulence of
infectious pancreatic necrosis virus.";
Virology 322:31-40(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Sp103, Isolate Sp116, and Isolate Sp122;
PubMed=15584407; DOI=10.3354/dao061023;
Shivappa R.B., Song H., Yao K., Aas-Eng A., Evensen O., Vakharia V.N.;
"Molecular characterization of Sp serotype strains of infectious
pancreatic necrosis virus exhibiting differences in virulence.";
Dis. Aquat. Organ. 61:23-32(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Sp103;
PubMed=15994815; DOI=10.1128/JVI.79.14.9206-9216.2005;
Santi N., Song H., Vakharia V.N., Evensen O.;
"Infectious pancreatic necrosis virus VP5 is dispensable for virulence
and persistence.";
J. Virol. 79:9206-9216(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-968.
STRAIN=Isolate Blake;
PubMed=11463106; DOI=10.3354/dao045089;
Blake S., Ma J.Y., Caporale D.A., Jairath S., Nicholson B.L.;
"Phylogenetic relationships of aquatic birnaviruses based on deduced
amino acid sequences of genome segment A cDNA.";
Dis. Aquat. Organ. 45:89-102(2001).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 437-539.
STRAIN=Isolate Heppell;
PubMed=8337850; DOI=10.1006/viro.1993.1441;
Heppell J., Berthiaume L., Corbin F., Tarrab E., Lecomte J.,
Arella M.;
"Comparison of amino acid sequences deduced from a cDNA fragment
obtained from infectious pancreatic necrosis virus (IPNV) strains of
different serotypes.";
Virology 195:840-844(1993).
[9]
PROTEIN SEQUENCE OF 509-515; 716-723 AND 735-740, ACTIVE SITES OF
PROTEASE VP4, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS
OF 486-ALA-ALA-487; 495-ALA-ALA-496; 508-ALA-SER-509; HIS-547;
ASP-573; ASP-585; ASP-595; ASP-601; SER-633; ASP-644; 660-ASP-ASP-661;
ASP-672; LYS-674; ALA-675; ILE-676; ALA-677; ALA-678; HIS-679;
GLU-680; GLY-682; LEU-683; PRO-684; LEU-685; ILE-686; GLY-687;
GLN-689; ASP-693; HIS-704 AND 734-ALA-SER-735.
STRAIN=31-75;
PubMed=10666235; DOI=10.1128/JVI.74.5.2057-2066.2000;
Petit S., Lejal N., Huet J.-C., Delmas B.;
"Active residues and viral substrate cleavage sites of the protease of
the birnavirus infectious pancreatic necrosis virus.";
J. Virol. 74:2057-2066(2000).
[10]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY (15 ANGSTROMS) OF VIRAL
PARTICLES.
STRAIN=31-75;
PubMed=16033982; DOI=10.1099/vir.0.80942-0;
Pous J., Chevalier C., Ouldali M., Navaza J., Delmas B., Lepault J.;
"Structure of birnavirus-like particles determined by combined
electron cryomicroscopy and X-ray crystallography.";
J. Gen. Virol. 86:2339-2346(2005).
[11]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 514-716.
PubMed=17553791; DOI=10.1074/jbc.M701551200;
Lee J., Feldman A.R., Delmas B., Paetzel M.;
"Crystal structure of the VP4 protease from infectious pancreatic
necrosis virus reveals the acyl-enzyme complex for an intermolecular
self-cleavage reaction.";
J. Biol. Chem. 282:24928-24937(2007).
-!- FUNCTION: Capsid protein VP2 self assembles to form an icosahedral
capsid with a T=13 symmetry, about 70 nm in diameter, and
consisting of 260 VP2 trimers. The capsid encapsulates the genomic
dsRNA. VP2 is also involved in attachment and entry into the host
cell (By similarity). {ECO:0000250}.
-!- FUNCTION: The precursor of VP2 plays an important role in capsid
assembly. First, pre-VP2 and VP2 oligomers assemble to form a
procapsid. Then, the pre-VP2 intermediates may be processed into
VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the
mature virion. The final capsid is composed of pentamers and
hexamers but VP2 has a natural tendency to assemble into all-
pentameric structures. Therefore pre-VP2 may be required to allow
formation of the hexameric structures (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protease VP4 is a serine protease that cleaves the
polyprotein into its final products. Pre-VP2 is first partially
cleaved, and may be completely processed by VP4 upon capsid
maturation. {ECO:0000255|PROSITE-ProRule:PRU00881}.
-!- FUNCTION: Capsid protein VP3 plays a key role in virion assembly
by providing a scaffold for the capsid made of VP2. May self-
assemble to form a T=4-like icosahedral inner-capsid composed of
at least 180 trimers. Plays a role in genomic RNA packaging by
recruiting VP1 into the capsid and interacting with the dsRNA
genome segments to form a ribonucleoprotein complex. Additionally,
the interaction of the VP3 C-terminal tail with VP1 removes the
inherent structural blockade of the polymerase active site. Thus,
VP3 can also function as a transcriptional activator (By
similarity). {ECO:0000250}.
-!- FUNCTION: Structural peptide 1 is a small peptide derived from
pre-VP2 C-terminus. It destabilizes and perforates cell membranes,
suggesting a role during entry (By similarity). {ECO:0000250}.
-!- FUNCTION: Structural peptide 2 is a small peptide derived from
pVP2 C-terminus. It is not essential for the virus viability, but
viral growth is affected when missing (By similarity).
{ECO:0000250}.
-!- FUNCTION: Structural peptide 3 is a small peptide derived from
pVP2 C-terminus. It is not essential for the virus viability, but
viral growth is affected when missing (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent
metal stabilizes the VP2 trimer, possibly cobalt (By similarity).
Capsid protein VP3 is a homodimer. Capsid protein VP3 interacts
(via C-terminus) with VP1 in the cytoplasm Capsid VP3 interacts
with VP2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 1: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 2: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 3: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- PTM: Specific enzymatic cleavages yield mature proteins. The
capsid assembly seems to be regulated by polyprotein processing.
The protease VP4 cleaves itself off the polyprotein, thus
releasing pre-VP2 and VP3 within the infected cell. During capsid
assembly, the C-terminus of pre-VP2 is further processed by VP4,
giving rise to VP2, the external capsid protein and three small
peptides that all stay closely associated with the capsid (By
similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The sequence shown is that of strain 31-75. Isolate
Sp103 is VP5-deficient.
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EMBL; AJ622822; CAF22217.1; -; Genomic_RNA.
EMBL; U48225; AAD11535.1; -; Genomic_RNA.
EMBL; U56907; AAB39512.1; -; Genomic_RNA.
EMBL; AY374435; AAQ75364.1; -; Genomic_RNA.
EMBL; AY379735; AAQ75348.1; -; Genomic_RNA.
EMBL; AY379736; AAQ75350.1; -; Genomic_RNA.
EMBL; AY379737; AAQ75352.1; -; Genomic_RNA.
EMBL; AY379738; AAQ75354.1; -; Genomic_RNA.
EMBL; AY379740; AAQ75357.1; -; Genomic_RNA.
EMBL; AY379742; AAQ75360.1; -; Genomic_RNA.
EMBL; AY379744; AAQ75363.1; -; Genomic_RNA.
EMBL; AY354519; AAR10446.1; -; Genomic_RNA.
EMBL; AY354520; AAR10449.1; -; Genomic_RNA.
EMBL; AY354521; AAR10452.1; -; Genomic_RNA.
EMBL; AY823632; AAX24140.1; -; Genomic_RNA.
EMBL; AF342728; AAK32154.1; -; mRNA.
EMBL; L13988; AAB00986.1; -; Genomic_RNA.
PDB; 2PNL; X-ray; 2.21 A; A/B/C/D/E/F/G/H/I/J=514-716.
PDB; 2PNM; X-ray; 2.30 A; A=524-716.
PDB; 3IDE; X-ray; 3.35 A; A/B/C/D/E=1-442.
PDBsum; 2PNL; -.
PDBsum; 2PNM; -.
PDBsum; 3IDE; -.
ProteinModelPortal; Q703G9; -.
SMR; Q703G9; -.
MEROPS; S50.001; -.
PRIDE; Q703G9; -.
OrthoDB; VOG0900008M; -.
BRENDA; 3.4.21.115; 6986.
EvolutionaryTrace; Q703G9; -.
Proteomes; UP000007213; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
InterPro; IPR002662; Birna_VP2.
InterPro; IPR002663; Birna_VP3.
InterPro; IPR025775; Birna_VP4_Prtase_dom.
Pfam; PF01766; Birna_VP2; 1.
Pfam; PF01767; Birna_VP3; 1.
Pfam; PF01768; Birna_VP4; 1.
PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
1: Evidence at protein level;
3D-structure; Capsid protein; Complete proteome;
Direct protein sequencing; Host cytoplasm; Hydrolase; Metal-binding;
Protease; Serine protease; Virion.
CHAIN 1 508 Precursor of VP2.
/FTId=PRO_0000392599.
CHAIN 1 442 Capsid protein VP2.
/FTId=PRO_0000227873.
PEPTIDE 443 486 Structural peptide 1.
{ECO:0000269|PubMed:15269363}.
/FTId=PRO_0000227874.
PEPTIDE 487 495 Structural peptide 2.
{ECO:0000269|PubMed:15269363}.
/FTId=PRO_0000227875.
PEPTIDE 496 508 Structural peptide 3.
{ECO:0000269|PubMed:10666235}.
/FTId=PRO_0000227876.
CHAIN 509 734 Protease VP4.
/FTId=PRO_0000227877.
CHAIN 735 972 Capsid protein VP3.
/FTId=PRO_0000227878.
DOMAIN 509 734 Peptidase S50. {ECO:0000255|PROSITE-
ProRule:PRU00881}.
ACT_SITE 633 633 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00881,
ECO:0000269|PubMed:10666235}.
ACT_SITE 674 674 {ECO:0000255|PROSITE-ProRule:PRU00881,
ECO:0000269|PubMed:10666235}.
METAL 26 26 Divalent metal cation; shared with
trimeric partners. {ECO:0000250}.
SITE 442 443 Cleavage; by protease VP4.
SITE 486 487 Cleavage; by protease VP4.
SITE 495 496 Cleavage; by protease VP4.
SITE 508 509 Cleavage; by protease VP4.
SITE 715 716 Cleavage; by protease VP4; subsidiary.
SITE 734 735 Cleavage; by protease VP4.
VARIANT 36 36 Q -> P (in strain: Isolate Mason).
VARIANT 46 46 S -> P (in strain: Isolate Mason).
VARIANT 52 52 V -> I (in strain: Isolate Mason, Isolate
Tseng, Isolate Blake, Isolate Sp103,
Isolate Sp116, Isolate Sp122, Isolate
NVI-001, Isolate NVI-011, Isolate NVI-
013, Isolate NVI-015, Isolate NVI-016,
Isolate NVI-020 and NVI-023).
VARIANT 54 54 V -> I (in strain: Isolate NVI-010).
VARIANT 82 85 WLET -> CWRA (in strain: Isolate Mason).
VARIANT 152 152 V -> A (in strain: Isolate Mason, Isolate
Blake and Isolate Tseng).
VARIANT 192 192 K -> R (in strain: Isolate Mason, Isolate
Blake and Isolate Tseng).
VARIANT 199 199 I -> T (in strain: Isolate Sp103 and
Isolate Sp122).
VARIANT 212 212 R -> S (in strain: Isolate Mason, Isolate
Blake and Isolate Tseng).
VARIANT 217 217 P -> T (in strain: Isolate Sp122, Isolate
NVI-001, Isolate NVI-011, Isolate NVI-
013, Isolate NVI-015, Isolate NVI-020 and
Isolate NVI-023).
VARIANT 219 219 T -> I (in strain: Isolate NVI-010).
VARIANT 221 221 T -> A (in strain: Isolate NVI-001,
Isolate NVI-013, Isolate NVI-015, Isolate
Sp116 and Isolate NVI-023).
VARIANT 222 222 L -> P (in strain: Isolate NVI-011).
VARIANT 234 234 N -> S (in strain: Isolate Tseng).
VARIANT 247 247 A -> T (in strain: Isolate Sp122, Isolate
NVI-001, Isolate NVI-013, Isolate NVI-015
and Isolate NVI-023).
VARIANT 249 249 Q -> R (in strain: Isolate Tseng).
VARIANT 252 252 D -> N (in strain: Isolate Mason, Isolate
Tseng, Isolate Blake, Isolate Sp103,
Isolate NVI-010 and Isolate NVI-016).
VARIANT 252 252 D -> V (in strain: Isolate NVI-001,
Isolate NVI-011, Isolate NVI-013, Isolate
NVI-015, Isolate NVI-020, Isolate NVI-
023, Isolate Sp116 and Isolate Sp122).
VARIANT 255 255 K -> R (in strain: Isolate Mason, Isolate
Blake and Isolate Tseng).
VARIANT 262 262 F -> L (in strain: Isolate Mason).
VARIANT 288 288 V -> A (in strain: Isolate Sp116).
VARIANT 319 319 A -> E (in strain: Isolate NVI-016).
VARIANT 323 323 V -> A (in strain: Isolate NVI-020).
VARIANT 323 323 V -> F (in strain: Isolate NVI-016).
VARIANT 432 434 DFS -> EKT (in strain: Isolate Mason).
VARIANT 455 455 V -> I (in strain: Isolate Mason).
VARIANT 473 473 M -> T (in strain: Isolate Mason, Isolate
Heppel and Isolate Blake).
VARIANT 500 500 Y -> H (in strain: Isolate Heppel,
Isolate NVI-010, Isolate NVI-011, Isolate
NVI-020, Isolate Sp103 and Isolate
Sp116).
VARIANT 565 565 P -> R (in strain: Isolate Mason).
VARIANT 570 571 EL -> SF (in strain: Isolate Mason).
VARIANT 672 672 D -> A (in strain: Isolate NVI-016).
VARIANT 717 717 K -> Q (in strain: Isolate NVI-016).
VARIANT 788 788 D -> G (in strain: Isolate NVI-011).
VARIANT 788 788 D -> Y (in strain: Isolate NVI-001).
VARIANT 802 802 H -> R (in strain: Isolate NVI-015 and
Isolate NVI-016).
VARIANT 841 841 L -> M (in strain: Isolate NVI-016).
VARIANT 867 867 E -> Q (in strain: Isolate Mason and
Isolate Blake).
VARIANT 875 875 P -> S (in strain: Isolate NVI-016).
VARIANT 882 882 M -> T (in strain: Isolate Tseng).
VARIANT 953 954 AE -> GK (in strain: Isolate Mason).
VARIANT 959 960 GR -> DV (in strain: Isolate Mason).
VARIANT 968 968 D -> N (in strain: Isolate Sp116).
MUTAGEN 508 509 AS->QL: Complete loss of pVP2-VP4
cleavage. {ECO:0000269|PubMed:10666235}.
MUTAGEN 547 547 H->S: Strongly reduced VP4-VP3 cleavage.
No effect on pVP2-VP4 cleavage.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 573 573 D->Q: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 585 585 D->I: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 595 595 D->L: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 601 601 D->S: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 633 633 S->A,Q,T: Complete loss of protease
activity. {ECO:0000269|PubMed:10666235}.
MUTAGEN 633 633 S->C: Partial loss of protease activity.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 644 644 D->I: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 660 661 DD->GS: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 672 672 D->N: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 674 674 K->A,D,H,Q,R: Complete loss of protease
activity. {ECO:0000269|PubMed:10666235}.
MUTAGEN 675 675 A->D: 60% loss of pVP2-VP4 and VP4-VP3
cleavages. {ECO:0000269|PubMed:10666235}.
MUTAGEN 676 676 I->A: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 677 677 A->D: 60% loss of pVP2-VP4. Complete loss
of VP4-VP3 cleavage.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 678 678 A->S: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 679 679 H->L: Strongly reduced VP4-VP3 cleavage.
No effect on pVP2-VP4 cleavage.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 680 680 E->M: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 682 682 G->L: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 683 683 L->A: 60% loss of pVP2-VP4 and VP4-VP3
cleavages. {ECO:0000269|PubMed:10666235}.
MUTAGEN 684 684 P->Q: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 685 685 L->A: 60% loss of pVP2-VP4 and VP4-VP3
cleavages. {ECO:0000269|PubMed:10666235}.
MUTAGEN 686 686 I->A: 20% loss of pVP2-VP4 and VP4-VP3
cleavages. {ECO:0000269|PubMed:10666235}.
MUTAGEN 687 687 G->A: 20% loss of pVP2-VP4 and VP4-VP3
cleavages. {ECO:0000269|PubMed:10666235}.
MUTAGEN 689 689 Q->I: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 693 693 D->L: Strongly reduced VP4-VP3 cleavage.
No effect on pVP2-VP4 cleavage.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 704 704 H->S: No effect on polyprotein
processing.
{ECO:0000269|PubMed:10666235}.
MUTAGEN 734 735 AS->LE: Complete loss of VP4-VP3
cleavage. {ECO:0000269|PubMed:10666235}.
CONFLICT 883 883 N -> Y (in Ref. 5; AAR10446).
{ECO:0000305}.
HELIX 9 15 {ECO:0000244|PDB:3IDE}.
HELIX 17 19 {ECO:0000244|PDB:3IDE}.
STRAND 32 44 {ECO:0000244|PDB:3IDE}.
STRAND 51 55 {ECO:0000244|PDB:3IDE}.
STRAND 60 70 {ECO:0000244|PDB:3IDE}.
STRAND 74 84 {ECO:0000244|PDB:3IDE}.
HELIX 89 91 {ECO:0000244|PDB:3IDE}.
STRAND 93 107 {ECO:0000244|PDB:3IDE}.
STRAND 120 128 {ECO:0000244|PDB:3IDE}.
HELIX 130 132 {ECO:0000244|PDB:3IDE}.
HELIX 140 143 {ECO:0000244|PDB:3IDE}.
HELIX 148 150 {ECO:0000244|PDB:3IDE}.
STRAND 151 156 {ECO:0000244|PDB:3IDE}.
TURN 157 159 {ECO:0000244|PDB:3IDE}.
STRAND 161 164 {ECO:0000244|PDB:3IDE}.
STRAND 202 208 {ECO:0000244|PDB:3IDE}.
STRAND 210 212 {ECO:0000244|PDB:3IDE}.
STRAND 223 232 {ECO:0000244|PDB:3IDE}.
STRAND 236 248 {ECO:0000244|PDB:3IDE}.
STRAND 254 263 {ECO:0000244|PDB:3IDE}.
STRAND 271 280 {ECO:0000244|PDB:3IDE}.
TURN 282 286 {ECO:0000244|PDB:3IDE}.
STRAND 287 292 {ECO:0000244|PDB:3IDE}.
HELIX 298 300 {ECO:0000244|PDB:3IDE}.
STRAND 305 313 {ECO:0000244|PDB:3IDE}.
HELIX 317 319 {ECO:0000244|PDB:3IDE}.
STRAND 324 326 {ECO:0000244|PDB:3IDE}.
HELIX 327 329 {ECO:0000244|PDB:3IDE}.
STRAND 332 338 {ECO:0000244|PDB:3IDE}.
TURN 339 342 {ECO:0000244|PDB:3IDE}.
TURN 344 346 {ECO:0000244|PDB:3IDE}.
STRAND 350 357 {ECO:0000244|PDB:3IDE}.
STRAND 363 376 {ECO:0000244|PDB:3IDE}.
HELIX 378 381 {ECO:0000244|PDB:3IDE}.
HELIX 395 404 {ECO:0000244|PDB:3IDE}.
TURN 405 410 {ECO:0000244|PDB:3IDE}.
STRAND 413 416 {ECO:0000244|PDB:3IDE}.
HELIX 417 422 {ECO:0000244|PDB:3IDE}.
HELIX 425 427 {ECO:0000244|PDB:3IDE}.
SEQUENCE 972 AA; 106646 MW; 7B1448E99800E3C9 CRC64;
MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS GVLVCFPGAP
GSRIGAHYRW NANQTGLEFD QWLETSQDLK KAFNYGRLIS RKYDIQSSTL PAGLYALNGT
LNAATFEGSL SEVESLTYNS LMSLTTNPQD KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE
TPQGLQSMNG AKMRCTAAIA PRRYEIDLPS QRLPPVPATG TLTTLYEGNA DIVNSTTVTG
DINFSLAEQP ADETKFDFQL DFMGLDNDVP VVTVVSSVLA TNDNYRGVSA KMTQSIPTEN
ITKPITRVKL SYKINQQTAI GNVATLGTMG PASVSFSSGN GNVPGVLRPI TLVAYEKMTP
LSILTVAGVS NYELIPNPEL LKNMVTRYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
KERTRVFNEI TDFSSDLPTS KAWGWRDIVR GIRKVAAPVL STLFPMAAPL IGMADQFIGD
LTKTNAAGGR YHSMAAGGRY KDVLESWASG GPDGKFSRAL KNRLESANYE EVELPPPSKG
VIVPVVHTVK SAPGEAFGSL AIIIPGEYPE LLDANQQVLS HFANDTGSVW GIGEDIPFEG
DNMCYTALPL KEIKRNGNIV VEKIFAGPIM GPSAQLGLSL LVNDIEDGVP RMVFTGEIAD
DEETIIPICG VDIKAIAAHE QGLPLIGNQP GVDEEVRNTS LAAHLIQTGT LPVQRAKGSN
KRIKYLGELM ASNASGMDEE LQRLLNATMA RAKEVQDAEI YKLLKLMAWT RKNDLTDHMY
EWSKEDPDAL KFGKLISTPP KHPEKPKGPD QHHAQEARAT RISLDAVRAG ADFATPEWVA
LNNYRGPSPG QFKYYLITGR EPEPGDEYED YIKQPIVKPT DMNKIRRLAN SVYGLPHQEP
APEEFYDAVA AVFAQNGGRG PDQDQMQDLR ELARQMKRRP RNADAPRRTR APAEPAPPGR
SRFTPSGDNA EV


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