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141  structures 1373  species 0  interactions 67929  sequences 666  architectures

Family: HLH (PF00010)

Summary: Helix-loop-helix DNA-binding domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Basic helix-loop-helix". More...

Basic helix-loop-helix Edit Wikipedia article

basic helix-loop-helix DNA-binding domain
Basic helix loop helix.png
Basic helix-loop-helix structural motif of ARNT. Two α-helices (blue) are connected by a short loop (red).[1]
Identifiers
SymbolbHLH
PfamPF00010
InterProIPR001092
SMARTSM00353
PROSITEPDOC00038
SCOPe1mdy / SUPFAM
CDDcd00083

A basic helix-loop-helix (bHLH) is a protein structural motif that characterizes one of the largest families of dimerizing transcription factors.[2][3][4][5]

bHLH transcription factors are often important in development or cell activity. BMAL1-Clock is a core transcription complex in the molecular circadian clock. Other genes, like c-Myc and HIF-1, have been linked to cancer due to their effects on cell growth and metabolism.

It should not be confused with the helix-turn-helix domain.

Structure

The motif is characterized by two α-helices connected by a loop. In general, transcription factors including this domain are dimeric, each with one helix containing basic amino acid residues that facilitate DNA binding.[6] In general, one helix is smaller, and, due to the flexibility of the loop, allows dimerization by folding and packing against another helix. The larger helix typically contains the DNA-binding regions. bHLH proteins typically bind to a consensus sequence called an E-box, CANNTG.[7] The canonical E-box is CACGTG (palindromic), however some bHLH transcription factors, notably those of the bHLH-PAS family, bind to related non-palindromic sequences, which are similar to the E-box. bHLH TFs may homodimerize or heterodimerize with other bHLH TFs and form a large variety of dimers, each one with specific functions.[8]

Examples

A phylogenetic analysis suggested that bHLH proteins fall into 6 major groups, indicated by letters A through F. [9] Examples of transcription factors containing a bHLH include:

Group A

Group B

Group C

These proteins contain two additional PAS domains after the bHLH domain.

Group D

Group E

Group F

These proteins contain an additional COE domain

Regulation

Since many bHLH transcription factors are heterodimeric,[8] their activity is often highly regulated by the dimerization of the subunits. One subunit's expression or availability is often controlled, whereas the other subunit is constitutively expressed. Many of the known regulatory proteins, such as the Drosophila extramacrochaetae protein, have the helix-loop-helix structure but lack the basic region, making them unable to bind to DNA on their own. They are, however, able to form heterodimers with proteins that have the bHLH structure, and inactivate their abilities as transcription factors.[10]

History

  • 1989: Murre et al. showed that dimers of various bHLH proteins bind to a short DNA motif (later called E-Box).[11] This E-box consists of the DNA sequence CANNTG, where N can be any nucleotide.[7]
  • 1994: Harrison's[12] and Pabo's[13] groups crystallize bHLH proteins bound to E-boxes, demonstrating that the parallel 4-helix bundle motif loop orients the basic sequences to interact with specific nucleotides in the major groove of the E-box.
  • 1994: Wharton et al. identified asymmetric E-boxes bound by a subset of bHLH proteins with PAS domains (bHLH-PAS proteins), including Single-minded (Sim) and the aromatic hydrocarbon receptor.[14]
  • 1995: Semenza's group identifies hypoxia-inducible factor (HIF) as a bHLH-PAS heterodimer that binds a related asymmetric E-box.[15]
  • 2009: Grove, De Masi et al., identified novel short DNA motifs, bound by a subset of bHLH proteins, which they defined as "E-box-like sequences". These are in the form of CAYRMK, where Y stands for C or T, R is A or G, M is A or C and K is G or T.[16]

Human proteins with helix-loop-helix DNA-binding domain

AHR; AHRR; ARNT; ARNT2; ARNTL; ARNTL2; ASCL1; ASCL2; ASCL3; ASCL4; ATOH1; ATOH7; ATOH8; BHLHB2; BHLHB3; BHLHB4; BHLHB5; BHLHB8; CLOCK; EPAS1; FERD3L; FIGLA; HAND1; HAND2; HES1; HES2; HES3; HES4; HES5; HES6; HES7; HEY1; HEY2; HIF1A; ID1; ID2; ID3; ID4; KIAA2018; LYL1; MASH1; MATH2; MAX; MESP1; MESP2; MIST1; MITF; MLX; MLXIP; MLXIPL; MNT; MSC; MSGN1; MXD1; MXD3; MXD4; MXI1; MYC; MYCL1; MYCL2; MYCN; MYF5; MYF6; MYOD1; MYOG; NCOA1; NCOA3; NEUROD1; NEUROD2; NEUROD4; NEUROD6; NEUROG1; NEUROG2; NEUROG3; NHLH1; NHLH2; NPAS1; NPAS2; NPAS3; NPAS4; OAF1; OLIG1; OLIG2; OLIG3; PTF1A; SCL; SCXB; SIM1; SIM2; SOHLH1; SOHLH2; SREBF1; SREBF2; TAL1; TAL2; TCF12; TCF15; TCF21; TCF3; TCF4; TCFL5; TFAP4; TFE3; TFEB; TFEC; TWIST1; TWIST2; USF1; USF2;

References

  1. ^ PDB: 1x0o​; Card PB, Erbel PJ, Gardner KH (October 2005). "Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization". J. Mol. Biol. 353 (3): 664–77. doi:10.1016/j.jmb.2005.08.043. PMID 16181639.
  2. ^ Murre C, Bain G, van Dijk MA, Engel I, Furnari BA, Massari ME, Matthews JR, Quong MW, Rivera RR, Stuiver MH (June 1994). "Structure and function of helix-loop-helix proteins". Biochim. Biophys. Acta. 1218 (2): 129–35. doi:10.1016/0167-4781(94)90001-9. PMID 8018712.
  3. ^ Littlewood TD, Evan GI (1995). "Transcription factors 2: helix-loop-helix". Protein Profile. 2 (6): 621–702. PMID 7553065.
  4. ^ Massari ME, Murre C (January 2000). "Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms". Mol. Cell. Biol. 20 (2): 429–40. doi:10.1128/MCB.20.2.429-440.2000. PMC 85097. PMID 10611221.
  5. ^ Amoutzias, Grigoris D.; Robertson, David L.; Van de Peer, Yves; Oliver, Stephen G. (2008-05-01). "Choose your partners: dimerization in eukaryotic transcription factors". Trends in Biochemical Sciences. 33 (5): 220–229. doi:10.1016/j.tibs.2008.02.002. ISSN 0968-0004. PMID 18406148.
  6. ^ Lawrence Zipursky; Arnold Berk; Monty Krieger; Darnell, James E.; Lodish, Harvey F.; Kaiser, Chris; Matthew P Scott; Matsudaira, Paul T. (2003-08-22). McGill Lodish 5E Package - Molecular Cell Biology & McGill Activation Code. San Francisco: W. H. Freeman. ISBN 0-7167-8635-4.
  7. ^ a b Chaudhary J, Skinner MK (1999). "Basic helix-loop-helix proteins can act at the E-box within the serum response element of the c-fos promoter to influence hormone-induced promoter activation in Sertoli cells". Mol. Endocrinol. 13 (5): 774–86. doi:10.1210/mend.13.5.0271. PMID 10319327.
  8. ^ a b Amoutzias, Gregory D.; Robertson, David L.; Oliver, Stephen G.; Bornberg-Bauer, Erich (2004-03-01). "Convergent evolution of gene networks by single-gene duplications in higher eukaryotes". EMBO Reports. 5 (3): 274–279. doi:10.1038/sj.embor.7400096. ISSN 1469-221X. PMC 1299007. PMID 14968135.
  9. ^ Ledent, V; Paquet, O; Vervoort, M (2002). "Phylogenetic analysis of the human basic helix-loop-helix proteins". Genome Biology. 3 (6): research0030.1. doi:10.1186/gb-2002-3-6-research0030. PMC 116727. PMID 12093377.
  10. ^ Cabrera CV, Alonso MC, Huikeshoven H (1994). "Regulation of scute function by extramacrochaete in vitro and in vivo". Development. 120 (12): 3595–603. PMID 7821225.
  11. ^ Murre C, McCaw PS, Vaessin H, et al. (1989). "Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence". Cell. 58 (3): 537–44. doi:10.1016/0092-8674(89)90434-0. PMID 2503252.
  12. ^ Ellenberger T, Fass D, Arnaud M, Harrison SC (April 1994). "Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer". Genes Dev. 8 (8): 970–80. doi:10.1101/gad.8.8.970. PMID 7926781.
  13. ^ Ma PC, Rould MA, Weintraub H, Pabo CO (May 1994). "Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation". Cell. 77 (3): 451–9. doi:10.1016/0092-8674(94)90159-7. PMID 8181063.
  14. ^ Wharton KA, Franks RG, Kasai Y, Crews ST (December 1994). "Control of CNS midline transcription by asymmetric E-box-like elements: similarity to xenobiotic responsive regulation". Development. 120 (12): 3563–9. PMID 7821222.
  15. ^ Wang GL, Jiang BH, Rue EA, Semenza GL (June 1995). "Hypoxia-inducible factor 1 is a basic helix-loop-helix-PAS heterodimer regulated by cellular O2 tension". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5510–4. doi:10.1073/pnas.92.12.5510. PMC 41725. PMID 7539918.
  16. ^ Grove C, De Masi F, et al. (2009). "A multiparameter network reveals extensive divergence between C. elegans bHLH transcription factors". Cell. 138 (2): 314–27. doi:10.1016/j.cell.2009.04.058. PMC 2774807. PMID 19632181.

External links

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Helix-loop-helix DNA-binding domain Provide feedback

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Literature references

  1. Littlewood TD, Evan GI; , Protein Profile 1995;2:621-702.: Transcription factors 2: helix-loop-helix. PUBMED:7553065 EPMC:7553065


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011598

A number of eukaryotic proteins, which probably are sequence specific DNA-binding proteins that act as transcription factors, share a conserved domain of 40 to 50 amino acid residues. It has been proposed [ PUBMED:2493990 ] that this domain is formed of two amphipathic helices joined by a variable length linker region that could form a loop. This 'helix-loop-helix' (HLH) domain mediates protein dimerization and has been found in the proteins listed below [ PUBMED:1521738 ]. Most of these proteins have an extra basic region of about 15 amino acid residues that is adjacent to the HLH domain and specifically binds to DNA. They are referred as basic helix-loop-helix proteins (bHLH), and are classified in two groups: class A (ubiquitous) and class B (tissue-specific). Members of the bHLH family bind variations on the core sequence 'CANNTG', also referred to as the E-box motif. The homo- or heterodimerization mediated by the HLH domain is independent of, but necessary for DNA binding, as two basic regions are required for DNA binding activity. The HLH proteins lacking the basic domain (Emc, Id) function as negative regulators, since they form heterodimers, but fail to bind DNA. The hairy-related proteins (hairy, E(spl), deadpan) also repress transcription although they can bind DNA. The proteins of this subfamily act together with co-repressor proteins, like groucho, through their -terminal motif WRPW.

Proteins containing a HLH domain include:

  • The myc family of cellular oncogenes [ PUBMED:2175254 ], which is currently known to contain four members: c-myc, N-myc, L-myc, and B-myc. The myc genes are thought to play a role in cellular differentiation and proliferation.
  • Proteins involved in myogenesis (the induction of muscle cells). In mammals MyoD1 (Myf-3), myogenin (Myf-4), Myf-5, and Myf-6 (Mrf4 or herculin), in birds CMD1 (QMF-1), in Xenopus MyoD and MF25, in Caenorhabditis elegans CeMyoD, and in Drosophila nautilus (nau).
  • Vertebrate proteins that bind specific DNA sequences ('E boxes') in various immunoglobulin chains enhancers: E2A or ITF-1 (E12/pan-2 and E47/pan-1), ITF-2 (tcf4), TFE3, and TFEB.
  • Vertebrate neurogenic differentiation factor 1 that acts as differentiation factor during neurogenesis.
  • Vertebrate MAX protein, a transcription regulator that forms a sequence- specific DNA-binding protein complex with myc or mad.
  • Vertebrate Max Interacting Protein 1 (MXI1 protein) which acts as a transcriptional repressor and may antagonize myc transcriptional activity by competing for max.
  • Proteins of the bHLH/PAS superfamily which are transcriptional activators. In mammals, AH receptor nuclear translocator (ARNT), single-minded homologues (SIM1 and SIM2), hypoxia-inducible factor 1 alpha (HIF1A), AH receptor (AHR), neuronal pas domain proteins (NPAS1 and NPAS2), endothelial pas domain protein 1 (EPAS1), mouse ARNT2, and human BMAL1. In Drosophila, single-minded (SIM), AH receptor nuclear translocator (ARNT), trachealess protein (TRH), and similar protein (SIMA).
  • Mammalian transcription factors HES, which repress transcription by acting on two types of DNA sequences, the E box and the N box.
  • Mammalian MAD protein (max dimerizer) which acts as transcriptional repressor and may antagonize myc transcriptional activity by competing for max.
  • Mammalian Upstream Stimulatory Factor 1 and 2 (USF1 and USF2), which bind to a symmetrical DNA sequence that is found in a variety of viral and cellular promoters.
  • Human lyl-1 protein; which is involved, by chromosomal translocation, in T- cell leukemia.
  • Human transcription factor AP-4.
  • Mouse helix-loop-helix proteins MATH-1 and MATH-2 which activate E box- dependent transcription in collaboration with E47.
  • Mammalian stem cell protein (SCL) (also known as tal1), a protein which may play an important role in hemopoietic differentiation. SCL is involved, by chromosomal translocation, in stem-cell leukemia.
  • Mammalian proteins Id1 to Id4 [ PUBMED:8139914 ]. Id (inhibitor of DNA binding) proteins lack a basic DNA-binding domain but are able to form heterodimers with other HLH proteins, thereby inhibiting binding to DNA.
  • Drosophila extra-macrochaetae (emc) protein, which participates in sensory organ patterning by antagonizing the neurogenic activity of the achaete- scute complex. Emc is the homologue of mammalian Id proteins.
  • Human Sterol Regulatory Element Binding Protein 1 (SREBP-1), a transcriptional activator that binds to the sterol regulatory element 1 (SRE-1) found in the flanking region of the LDLR gene and in other genes.
  • Drosophila achaete-scute (AS-C) complex proteins T3 (l'sc), T4 (scute), T5 (achaete) and T8 (asense). The AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.
  • Mammalian homologues of achaete-scute proteins, the MASH-1 and MASH-2 proteins.
  • Drosophila atonal protein (ato) which is involved in neurogenesis.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(144)
Full
(67929)
Representative proteomes UniProt
(112980)
RP15
(9177)
RP35
(29219)
RP55
(56773)
RP75
(76909)
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  Seed
(144)
Full
(67929)
Representative proteomes UniProt
(112980)
RP15
(9177)
RP35
(29219)
RP55
(56773)
RP75
(76909)
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  Seed
(144)
Full
(67929)
Representative proteomes UniProt
(112980)
RP15
(9177)
RP35
(29219)
RP55
(56773)
RP75
(76909)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Unknown
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Eddy SR
Number in seed: 144
Number in full: 67929
Average length of the domain: 53.50 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 13.32 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 54
Family (HMM) version: 28
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HLH domain has been found. There are 141 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A060CUY1 View 3D Structure Click here
A0A060CVJ8 View 3D Structure Click here
A0A060CZ29 View 3D Structure Click here
A0A060CZB6 View 3D Structure Click here
A0A060D4L2 View 3D Structure Click here
A0A060D780 View 3D Structure Click here
A0A060D7Y3 View 3D Structure Click here
A0A096MIW8 View 3D Structure Click here
A0A096SYH2 View 3D Structure Click here
A0A0B4KFD8 View 3D Structure Click here
A0A0B4LH78 View 3D Structure Click here
A0A0G2JWM6 View 3D Structure Click here
A0A0G2JYQ8 View 3D Structure Click here
A0A0G2K1T7 View 3D Structure Click here
A0A0K2CT67 View 3D Structure Click here
A0A0N7KGH6 View 3D Structure Click here
A0A0N7KGS8 View 3D Structure Click here
A0A0N7KIY3 View 3D Structure Click here
A0A0N7KJ26 View 3D Structure Click here
A0A0P0UXA8 View 3D Structure Click here
A0A0P0UYC0 View 3D Structure Click here
A0A0P0UZP9 View 3D Structure Click here
A0A0P0UZQ6 View 3D Structure Click here
A0A0P0V4D3 View 3D Structure Click here
A0A0P0V4E3 View 3D Structure Click here
A0A0P0V8W1 View 3D Structure Click here
A0A0P0VGJ8 View 3D Structure Click here
A0A0P0VQW6 View 3D Structure Click here
A0A0P0VUZ8 View 3D Structure Click here
A0A0P0VV20 View 3D Structure Click here
A0A0P0W2I2 View 3D Structure Click here
A0A0P0W3G1 View 3D Structure Click here
A0A0P0W8E2 View 3D Structure Click here
A0A0P0WRG0 View 3D Structure Click here
A0A0P0WTF9 View 3D Structure Click here
A0A0P0WTJ8 View 3D Structure Click here
A0A0P0WUF9 View 3D Structure Click here
A0A0P0WXG4 View 3D Structure Click here
A0A0P0X2F6 View 3D Structure Click here
A0A0P0X817 View 3D Structure Click here
A0A0P0XIW1 View 3D Structure Click here
A0A0P0XNJ4 View 3D Structure Click here
A0A0P0XQ00 View 3D Structure Click here
A0A0P0XS11 View 3D Structure Click here
A0A0P0XX67 View 3D Structure Click here
A0A0P0Y1V2 View 3D Structure Click here
A0A0P0Y4I9 View 3D Structure Click here
A0A0P0YC64 View 3D Structure Click here
A0A0P0YCR0 View 3D Structure Click here
A0A0R0ELN4 View 3D Structure Click here
A0A0R0EZ65 View 3D Structure Click here
A0A0R0F2U2 View 3D Structure Click here
A0A0R0F904 View 3D Structure Click here
A0A0R0FCR4 View 3D Structure Click here
A0A0R0FFK3 View 3D Structure Click here
A0A0R0FFQ5 View 3D Structure Click here
A0A0R0FIC8 View 3D Structure Click here
A0A0R0FQW3 View 3D Structure Click here
A0A0R0FQW7 View 3D Structure Click here
A0A0R0GCR6 View 3D Structure Click here
A0A0R0H312 View 3D Structure Click here
A0A0R0HGH7 View 3D Structure Click here
A0A0R0HNQ2 View 3D Structure Click here
A0A0R0ICN4 View 3D Structure Click here
A0A0R0ICZ3 View 3D Structure Click here
A0A0R0IN34 View 3D Structure Click here
A0A0R0INZ0 View 3D Structure Click here
A0A0R0IQG8 View 3D Structure Click here
A0A0R0IQG9 View 3D Structure Click here
A0A0R0IT59 View 3D Structure Click here
A0A0R0IZW0 View 3D Structure Click here
A0A0R0J517 View 3D Structure Click here
A0A0R0JBH0 View 3D Structure Click here
A0A0R0JBZ7 View 3D Structure Click here
A0A0R0JHC2 View 3D Structure Click here
A0A0R0JJ69 View 3D Structure Click here
A0A0R0JPU6 View 3D Structure Click here
A0A0R0JZA5 View 3D Structure Click here
A0A0R0KI95 View 3D Structure Click here
A0A0R0KNC3 View 3D Structure Click here
A0A0R0L105 View 3D Structure Click here
A0A0R0L4V1 View 3D Structure Click here
A0A0R0L6Z7 View 3D Structure Click here
A0A0R0LAI5 View 3D Structure Click here
A0A0R0LCY9 View 3D Structure Click here
A0A0R4I9I4 View 3D Structure Click here
A0A0R4IBL7 View 3D Structure Click here
A0A0R4IH97 View 3D Structure Click here
A0A0R4IRV6 View 3D Structure Click here
A0A0R4IX50 View 3D Structure Click here
A0A0R4J2M0 View 3D Structure Click here
A0A0U1RRY7 View 3D Structure Click here
A0A1D6DZ90 View 3D Structure Click here
A0A1D6E1J0 View 3D Structure Click here
A0A1D6E9Z9 View 3D Structure Click here
A0A1D6EAS7 View 3D Structure Click here
A0A1D6EDF3 View 3D Structure Click here
A0A1D6EPT7 View 3D Structure Click here
A0A1D6EPV1 View 3D Structure Click here
A0A1D6ERR7 View 3D Structure Click here
A0A1D6ES35 View 3D Structure Click here
A0A1D6ESY4 View 3D Structure Click here
A0A1D6EY17 View 3D Structure Click here
A0A1D6F039 View 3D Structure Click here
A0A1D6F5G0 View 3D Structure Click here
A0A1D6F5S9 View 3D Structure Click here
A0A1D6FGD1 View 3D Structure Click here
A0A1D6FNI4 View 3D Structure Click here
A0A1D6FXZ1 View 3D Structure Click here
A0A1D6G466 View 3D Structure Click here
A0A1D6GAF6 View 3D Structure Click here
A0A1D6GG70 View 3D Structure Click here
A0A1D6GIG8 View 3D Structure Click here
A0A1D6GWK9 View 3D Structure Click here
A0A1D6GYM4 View 3D Structure Click here
A0A1D6H6F7 View 3D Structure Click here
A0A1D6H6X0 View 3D Structure Click here
A0A1D6HAY7 View 3D Structure Click here
A0A1D6HCJ0 View 3D Structure Click here
A0A1D6HGI9 View 3D Structure Click here
A0A1D6HH16 View 3D Structure Click here
A0A1D6HHL2 View 3D Structure Click here
A0A1D6HHV4 View 3D Structure Click here
A0A1D6HJ33 View 3D Structure Click here
A0A1D6HN74 View 3D Structure Click here
A0A1D6HNP6 View 3D Structure Click here
A0A1D6HW08 View 3D Structure Click here
A0A1D6I4D4 View 3D Structure Click here
A0A1D6I624 View 3D Structure Click here
A0A1D6I690 View 3D Structure Click here
A0A1D6I7X9 View 3D Structure Click here
A0A1D6I8R4 View 3D Structure Click here
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