[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3547406 [NCBI, ExPASy, EBI, Israel, Japan] Sweetser D., Nonet M., Young R.A.; "Prokaryotic and eukaryotic RNA polymerases have homologous core subunits."; Proc. Natl. Acad. Sci. U.S.A. 84:1192-1196(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=S288c / FY1678; DOI=10.1002/(SICI)1097-0061(199701)13:1<73::AID-YEA52>3.3.CO;2-D; PubMed=9046089 [NCBI, ExPASy, EBI, Israel, Japan] Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.; "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae chromosome XV."; Yeast 13:73-83(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=S288c / FY1678; PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan] Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; Nature 387:98-102(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-773. STRAIN=ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632; DOI=10.1016/S1567-1356(03)00012-6; PubMed=12748053 [NCBI, ExPASy, EBI, Israel, Japan] Kurtzman C.P., Robnett C.J.; "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses."; FEMS Yeast Res. 3:417-432(2003).
[5]	PROTEIN SEQUENCE OF 837-844. PubMed=2204624 [NCBI, ExPASy, EBI, Israel, Japan] Riva M., Carles C., Sentenac A., Grachev M.A., Mustaev A.A., Zaychikov E.F.; "Mapping the active site of yeast RNA polymerase B (II)."; J. Biol. Chem. 265:16498-16503(1990).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915; THR-916 AND SER-919, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[7]	ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX. DOI=10.1016/S1097-2765(03)00387-3; PubMed=14580350 [NCBI, ExPASy, EBI, Israel, Japan] Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A., Kornberg R.D., Asturias F.J.; "RNA polymerase II/TFIIF structure and conserved organization of the initiation complex."; Mol. Cell 12:1003-1013(2003).
[8]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[9]	INTERACTION WITH RTT103. DOI=10.1038/nature03041; PubMed=15565157 [NCBI, ExPASy, EBI, Israel, Japan] Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F., Buratowski S.; "The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II."; Nature 432:517-522(2004).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND MASS SPECTROMETRY. DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.; "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."; J. Proteome Res. 6:1190-1197(2007).
[11]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX. DOI=10.1126/science.1059493; PubMed=11313498 [NCBI, ExPASy, EBI, Israel, Japan] Cramer P., Bushnell D.A., Kornberg R.D.; "Structural basis of transcription: RNA polymerase II at 2.8 Angstrom resolution."; Science 292:1863-1876(2001).
[12]	X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX. DOI=10.1126/science.1059495; PubMed=11313499 [NCBI, ExPASy, EBI, Israel, Japan] Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D.; "Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution."; Science 292:1876-1882(2001).
[13]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN COMPLEX WITH ALPHA-AMANITIN. DOI=10.1073/pnas.251664698; PubMed=11805306 [NCBI, ExPASy, EBI, Israel, Japan] Bushnell D.A., Cramer P., Kornberg R.D.; "Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution."; Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002).
[14]	X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH DST1. DOI=10.1016/S0092-8674(03)00598-1; PubMed=12914699 [NCBI, ExPASy, EBI, Israel, Japan] Kettenberger H., Armache K.J., Cramer P.; "Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage."; Cell 114:347-357(2003).
[15]	X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX. DOI=10.1073/pnas.1030608100; PubMed=12746495 [NCBI, ExPASy, EBI, Israel, Japan] Armache K.J., Kettenberger H., Cramer P.; "Architecture of initiation-competent 12-subunit RNA polymerase II."; Proc. Natl. Acad. Sci. U.S.A. 100:6964-6968(2003).
[16]	X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX. DOI=10.1073/pnas.1130601100; PubMed=12746498 [NCBI, ExPASy, EBI, Israel, Japan] Bushnell D.A., Kornberg R.D.; "Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription."; Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003).
[17]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX. DOI=10.1016/j.cell.2004.10.016; PubMed=15537538 [NCBI, ExPASy, EBI, Israel, Japan] Westover K.D., Bushnell D.A., Kornberg R.D.; "Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center."; Cell 119:481-489(2004).
[18]	X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS). DOI=10.1016/j.molcel.2004.11.040; PubMed=15610738 [NCBI, ExPASy, EBI, Israel, Japan] Kettenberger H., Armache K.J., Cramer P.; "Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS."; Mol. Cell 16:955-965(2004).
[19]	X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX. DOI=10.1126/science.1090838; PubMed=14963322 [NCBI, ExPASy, EBI, Israel, Japan] Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D.; "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms."; Science 303:983-988(2004).
[20]	X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX. DOI=10.1074/jbc.M413038200; PubMed=15591044 [NCBI, ExPASy, EBI, Israel, Japan] Armache K.J., Mitterweger S., Meinhart A., Cramer P.; "Structures of complete RNA polymerase II and its subcomplex, Rpb4/7."; J. Biol. Chem. 280:7131-7134(2005).
[21]	X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX WITH INHIBITING NON-CODING RNA. DOI=10.1038/nsmb1032; PubMed=16341226 [NCBI, ExPASy, EBI, Israel, Japan] Kettenberger H., Eisenfuhr A., Brueckner F., Theis M., Famulok M., Cramer P.; "Structure of an RNA polymerase II-RNA inhibitor complex elucidates transcription regulation by noncoding RNAs."; Nat. Struct. Mol. Biol. 13:44-48(2006).
[22]	X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX. DOI=10.1016/j.str.2006.04.003; PubMed=16765890 [NCBI, ExPASy, EBI, Israel, Japan] Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.; "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated structural model."; Structure 14:973-982(2006).

Comments

FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab the incoming DNA template. The fork loop 1 (RPB2) interacts with the RNA-DNA hybrid, possibly stabilizing it.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
SUBCELLULAR LOCATION: Nucleus.
MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits.
MISCELLANEOUS: Present with 18700 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the RNA polymerase beta chain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M15693; AAA68096.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U55020; AAC49637.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75059; CAA99357.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF527884; AAP57849.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25884; A25884.

RefSeq

NP_014794.1; -.

3D structure databases

PDB

1I3Q; X-ray; 3.10 A; B=1-1224.	[ExPASy / RCSB / EBI]
1I50; X-ray; 2.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
1I6H; X-ray; 3.30 A; B=1-1224.	[ExPASy / RCSB / EBI]
1K83; X-ray; 2.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
1NIK; X-ray; 4.10 A; B=1-1224.	[ExPASy / RCSB / EBI]
1NT9; X-ray; 4.20 A; B=1-1224.	[ExPASy / RCSB / EBI]
1PQV; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
1R5U; X-ray; 4.50 A; B=1-1224.	[ExPASy / RCSB / EBI]
1R9S; X-ray; 4.25 A; B=1-1224.	[ExPASy / RCSB / EBI]
1R9T; X-ray; 3.50 A; B=1-1224.	[ExPASy / RCSB / EBI]
1SFO; X-ray; 3.61 A; B=1-1224.	[ExPASy / RCSB / EBI]
1TWA; X-ray; 3.20 A; B=1-1224.	[ExPASy / RCSB / EBI]
1TWC; X-ray; 3.00 A; B=1-1224.	[ExPASy / RCSB / EBI]
1TWF; X-ray; 2.30 A; B=1-1224.	[ExPASy / RCSB / EBI]
1TWG; X-ray; 3.30 A; B=1-1224.	[ExPASy / RCSB / EBI]
1TWH; X-ray; 3.40 A; B=1-1224.	[ExPASy / RCSB / EBI]
1WCM; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
1Y1V; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
1Y1W; X-ray; 4.00 A; B=1-1224.	[ExPASy / RCSB / EBI]
1Y1Y; X-ray; 4.00 A; B=1-1224.	[ExPASy / RCSB / EBI]
1Y77; X-ray; 4.50 A; B=1-1224.	[ExPASy / RCSB / EBI]
2B63; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
2B8K; X-ray; 4.15 A; B=1-1224.	[ExPASy / RCSB / EBI]
2E2H; X-ray; 3.95 A; B=1-1224.	[ExPASy / RCSB / EBI]
2E2I; X-ray; 3.41 A; B=1-1224.	[ExPASy / RCSB / EBI]
2E2J; X-ray; 3.50 A; B=1-1224.	[ExPASy / RCSB / EBI]
2JA5; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
2JA6; X-ray; 4.00 A; B=1-1224.	[ExPASy / RCSB / EBI]
2JA7; X-ray; 3.80 A; B/N=1-1224.	[ExPASy / RCSB / EBI]
2JA8; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
2NVQ; X-ray; 2.90 A; B=1-1224.	[ExPASy / RCSB / EBI]
2NVT; X-ray; 3.36 A; B=1-1224.	[ExPASy / RCSB / EBI]
2NVX; X-ray; 3.60 A; B=1-1224.	[ExPASy / RCSB / EBI]
2NVY; X-ray; 3.40 A; B=1-1224.	[ExPASy / RCSB / EBI]
2NVZ; X-ray; 4.30 A; B=1-1224.	[ExPASy / RCSB / EBI]
2R7Z; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
2R92; X-ray; 3.80 A; B=1-1224.	[ExPASy / RCSB / EBI]
2R93; X-ray; 4.00 A; B=1-1224.	[ExPASy / RCSB / EBI]
2VUM; X-ray; 3.40 A; B=1-1224.	[ExPASy / RCSB / EBI]
2YU9; X-ray; 3.40 A; B=1-1224.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1I3Q; -.
1I50; -.
1I6H; -.
1K83; -.
1NIK; -.
1NT9; -.
1PQV; -.
1R5U; -.
1R9S; -.
1R9T; -.
1SFO; -.
1TWA; -.
1TWC; -.
1TWF; -.
1TWG; -.
1TWH; -.
1WCM; -.
1Y1V; -.
1Y1W; -.
1Y1Y; -.
1Y77; -.
2B63; -.
2B8K; -.
2E2H; -.
2E2I; -.
2E2J; -.
2JA5; -.
2JA6; -.
2JA7; -.
2JA8; -.
2NVQ; -.
2NVT; -.
2NVX; -.
2NVY; -.
2NVZ; -.
2R7Z; -.
2R92; -.
2R93; -.
2VUM; -.
2YU9; -.

ModBase

P08518.

Protein-protein interaction databases

DIP

DIP:14N; -.

Organism-specific databases

YOR151c; -.

S000005677; RPB2.

Gene expression databases

ArrayExpress

P08518; -.

GermOnline

YOR151C; Saccharomyces cerevisiae.

Ontologies

GO:0005665;	Cellular component: DNA-directed RNA polymerase II, core complex (traceable author statement from SGD).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0003899;	Molecular function: DNA-directed RNA polymerase activity (traceable author statement from SGD).
GO:0006366;	Biological process: transcription from RNA polymerase II promoter (traceable author statement from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR015712; DNA-dir_RNA_pol_su2.
IPR007120; DNA-dir_RNA_pol_su2_6.
IPR007121; RNA_pol_bsu_CS.
IPR007644; RNA_pol_bsu_protrusion.
IPR007642; RNA_pol_Rpb2_2.
IPR007645; RNA_pol_Rpb2_3.
IPR007646; RNA_pol_Rpb2_4.
IPR007647; RNA_pol_Rpb2_5.
IPR007641; RNA_pol_Rpb2_7.
Graphical view of domain structure.

PANTHER

PTHR20856; RNA_pol_I_sub2; 1.

Pfam

PF04563; RNA_pol_Rpb2_1; 1.
PF04561; RNA_pol_Rpb2_2; 1.
PF04565; RNA_pol_Rpb2_3; 1.
PF04566; RNA_pol_Rpb2_4; 1.
PF04567; RNA_pol_Rpb2_5; 1.
PF00562; RNA_pol_Rpb2_6; 1.
PF04560; RNA_pol_Rpb2_7; 1.
Pfam graphical view of domain structure.

PROSITE

PS01166; RNA_POL_BETA; 1.

Proteomic databases

P08518; -.

Genome annotation databases

Ensembl

YOR151C; Saccharomyces cerevisiae. [Contig view]

854322; -.

Y13140_GR; YOR151C.

sce:YOR151C; -.

fig|4932.3.peg.5899; -.

Phylogenomic databases

HOGENOM

P08518; -.

Other

LinkHub

P08518; -.

NextBio

976360; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Transcription; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1224`	`1224`	`DNA-directed RNA polymerase II subunit RPB2.`	`PRO_0000048091`
`ZN_FING`	`1163 1185`	`23`	`C4-type.`
`REGION`	`467 478`	`12`	`Fork loop 1.`
`METAL`	`837 837`		`Magnesium; shared with RPB1.`
`METAL`	`1163 1163`		`Zinc.`
`METAL`	`1166 1166`		`Zinc.`
`METAL`	`1182 1182`		`Zinc.`
`METAL`	`1185 1185`		`Zinc.`
`MOD_RES`	`915 915`		`Phosphothreonine.`
`MOD_RES`	`916 916`		`Phosphothreonine.`
`MOD_RES`	`919 919`		`Phosphoserine.`
`CONFLICT`	`1003 1006`		`AEGI -> RRRY (in Ref. 1; AAA68096).`
`HELIX`	`29 41`	`13`
`HELIX`	`45 56`	`12`
`HELIX`	`58 64`	`7`
`STRAND`	`96 102`	`7`
`STRAND`	`105 107`	`3`
`STRAND`	`109 111`	`3`
`HELIX`	`114 119`	`6`
`STRAND`	`125 129`	`5`
`STRAND`	`166 171`	`6`
`HELIX`	`180 182`	`3`
`HELIX`	`186 191`	`6`
`STRAND`	`202 205`	`4`
`STRAND`	`208 212`	`5`
`STRAND`	`214 218`	`5`
`STRAND`	`224 227`	`4`
`STRAND`	`232 241`	`10`
`STRAND`	`245 247`	`3`
`STRAND`	`253 260`	`8`
`STRAND`	`269 272`	`4`
`HELIX`	`282 288`	`7`
`HELIX`	`294 301`	`8`
`HELIX`	`308 320`	`13`
`TURN`	`321 323`	`3`
`HELIX`	`327 336`	`10`
`HELIX`	`345 358`	`14`
`TURN`	`362 364`	`3`
`STRAND`	`367 369`	`3`
`HELIX`	`371 389`	`19`
`HELIX`	`401 403`	`3`
`STRAND`	`404 407`	`4`
`HELIX`	`409 433`	`25`
`HELIX`	`451 463`	`13`
`STRAND`	`480 482`	`3`
`HELIX`	`488 495`	`8`
`STRAND`	`497 499`	`3`
`HELIX`	`516 518`	`3`
`TURN`	`519 521`	`3`
`HELIX`	`530 532`	`3`
`STRAND`	`536 539`	`4`
`HELIX`	`552 560`	`9`
`HELIX`	`566 568`	`3`
`HELIX`	`571 573`	`3`
`STRAND`	`578 582`	`5`
`STRAND`	`585 591`	`7`
`HELIX`	`593 606`	`14`
`STRAND`	`607 609`	`3`
`STRAND`	`614 618`	`5`
`TURN`	`619 622`	`4`
`STRAND`	`623 627`	`5`
`STRAND`	`633 641`	`9`
`STRAND`	`650 652`	`3`
`HELIX`	`655 666`	`12`
`HELIX`	`681 686`	`6`
`STRAND`	`689 694`	`6`
`HELIX`	`695 698`	`4`
`STRAND`	`703 706`	`4`
`HELIX`	`707 710`	`4`
`HELIX`	`745 748`	`4`
`HELIX`	`753 755`	`3`
`STRAND`	`756 758`	`3`