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175  structures 819  species 0  interactions 26644  sequences 2626  architectures

Family: LRR_1 (PF00560)

Summary: Leucine Rich Repeat

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 "Leucine-rich repeat". More...

Leucine-rich repeat Edit Wikipedia article

2bnh topview.png
An example of a leucine-rich repeat protein, a porcine ribonuclease inhibitor
Identifiers
SymbolLRR_1
PfamPF00560
Pfam clanCL0022
InterProIPR001611
SCOPe2bnh / SUPFAM
Membranome605
Leucine rich repeat variant
PDB 1lrv EBI.jpg
a leucine-rich repeat variant with a novel repetitive protein structural motif
Identifiers
SymbolLRV
PfamPF01816
Pfam clanCL0020
InterProIPR004830
SCOPe1lrv / SUPFAM
Membranome737
LRR adjacent
PDB 1h6u EBI.jpg
internalin h: crystal structure of fused n-terminal domains.
Identifiers
SymbolLRR_adjacent
PfamPF08191
InterProIPR012569
Membranome341
Leucine rich repeat N-terminal domain
PDB 1xec EBI.jpg
dimeric bovine tissue-extracted decorin, crystal form 2
Identifiers
SymbolLRRNT
PfamPF01462
InterProIPR000372
SMARTLRRNT
SCOPe1m10 / SUPFAM
Membranome127
Leucine rich repeat N-terminal domain
PDB 1ogq EBI.jpg
the crystal structure of pgip (polygalacturonase inhibiting protein), a leucine rich repeat protein involved in plant defense
Identifiers
SymbolLRRNT_2
PfamPF08263
InterProIPR013210
SMARTLRRNT
SCOPe1m10 / SUPFAM
Leucine rich repeat C-terminal domain
PDB 1w8a EBI.jpg
third lrr domain of drosophila slit
Identifiers
SymbolLRRCT
PfamPF01463
InterProIPR000483
SMARTLRRCT
SCOPe1m10 / SUPFAM
LRV protein FeS4 cluster
PDB 1lrv EBI.jpg
a leucine-rich repeat variant with a novel repetitive protein structural motif
Identifiers
SymbolLRV_FeS
PfamPF05484
Pfam clanCL0020
InterProIPR008665
SCOPe1lrv / SUPFAM

A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold.[1][2] It is composed of repeating 20–30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. These tandem repeats commonly fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues.

Leucine-rich repeats are frequently involved in the formation of protein–protein interactions.[3][4]

Examples

Leucine-rich repeat motifs have been identified in a large number of functionally unrelated proteins.[5] The best-known example is the ribonuclease inhibitor, but other proteins such as the tropomyosin regulator tropomodulin and the toll-like receptor also share the motif. In fact, the toll-like receptor possesses 10 successive LRR motifs which serve to bind pathogen- and danger-associated molecular patterns.

Although the canonical LRR protein contains approximately one helix for every beta strand, variants that form beta-alpha superhelix folds sometimes have long loops rather than helices linking successive beta strands.

One leucine-rich repeat variant domain (LRV) has a novel repetitive structural motif consisting of alternating alpha- and 310-helices arranged in a right-handed superhelix, with the absence of the beta-sheets present in other leucine-rich repeats.[6]

Associated domains

Leucine-rich repeats are often flanked by N-terminal and C-terminal cysteine-rich domains, but not always as is the case with C5orf36

They also co-occur with LRR adjacent domains. These are small, all beta strand domains, which have been structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats, significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.[7][8][9]

An iron sulphur cluster is found at the N-terminus of some proteins containing the leucine-rich repeat variant domain (LRV). These proteins have a two-domain structure, composed of a small N-terminal domain containing a cluster of four Cysteine residues that houses the 4Fe:4S cluster, and a larger C-terminal domain containing the LRV repeats.[6] Biochemical studies revealed that the 4Fe:4S cluster is sensitive to oxygen, but does not appear to have reversible redox activity.

See also

References

  1. ^ Kobe B, Deisenhofer J (October 1994). "The leucine-rich repeat: a versatile binding motif". Trends Biochem. Sci. 19 (10): 415–21. doi:10.1016/0968-0004(94)90090-6. PMID 7817399.
  2. ^ Enkhbayar P, Kamiya M, Osaki M, Matsumoto T, Matsushima N (February 2004). "Structural principles of leucine-rich repeat (LRR) proteins". Proteins. 54 (3): 394–403. doi:10.1002/prot.10605. PMID 14747988.
  3. ^ Kobe B, Kajava AV (December 2001). "The leucine-rich repeat as a protein recognition motif". Curr. Opin. Struct. Biol. 11 (6): 725–32. doi:10.1016/S0959-440X(01)00266-4. PMID 11751054.
  4. ^ Gay NJ, Packman LC, Weldon MA, Barna JC (October 1991). "A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a beta-sheet structure". FEBS Lett. 291 (1): 87–91. doi:10.1016/0014-5793(91)81110-T. PMID 1657640.
  5. ^ Rothberg JM, Jacobs JR, Goodman CS, Artavanis-Tsakonas S (December 1990). "slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains". Genes Dev. 4 (12A): 2169–87. doi:10.1101/gad.4.12a.2169. PMID 2176636.
  6. ^ a b Peters JW, Stowell MH, Rees DC (December 1996). "A leucine-rich repeat variant with a novel repetitive protein structural motif". Nat. Struct. Biol. 3 (12): 991–4. doi:10.1038/nsb1296-991. PMID 8946850.
  7. ^ Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW (September 2001). "Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain". J. Mol. Biol. 312 (4): 783–94. doi:10.1006/jmbi.2001.4989. PMID 11575932.
  8. ^ Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW (December 2002). "Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin". Cell. 111 (6): 825–36. doi:10.1016/S0092-8674(02)01136-4. PMID 12526809.
  9. ^ Freiberg A, Machner MP, Pfeil W, Schubert WD, Heinz DW, Seckler R (March 2004). "Folding and stability of the leucine-rich repeat domain of internalin B from Listeri monocytogenes". J. Mol. Biol. 337 (2): 453–61. doi:10.1016/j.jmb.2004.01.044. PMID 15003459.

Further reading

External links

This article incorporates text from the public domain Pfam and InterPro: IPR012569
This article incorporates text from the public domain Pfam and InterPro: IPR013210
This article incorporates text from the public domain Pfam and InterPro: IPR000372
This article incorporates text from the public domain Pfam and InterPro: IPR000483
This article incorporates text from the public domain Pfam and InterPro: IPR004830
This article incorporates text from the public domain Pfam and InterPro: IPR004830

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Ribonuclease inhibitor". More...

Ribonuclease inhibitor Edit Wikipedia article

Leucine Rich Repeat
2bnh topview.png
Top view of porcine ribonuclease inhibitor, showing its horseshoe shape.[1] The outer layer is composed of α-helices and the inner layer of parallel β-strands. The inner and outer diameters are roughly 2.1 nm and 6.7 nm, respectively.
Identifiers
SymbolLRR_1
PfamPF00560
Pfam clanCL0022
InterProIPR003590
SMARTSM00368
SCOPe1bnh / SUPFAM

Ribonuclease inhibitor (RI) is a large (~450 residues, ~49 kDa), acidic (pI ~4.7), leucine-rich repeat protein that forms extremely tight complexes with certain ribonucleases. It is a major cellular protein, comprising ~0.1% of all cellular protein by weight, and appears to play an important role in regulating the lifetime of RNA.[2]

RI has a surprisingly high cysteine content (~6.5%, cf. 1.7% in typical proteins) and is sensitive to oxidation. RI is also rich in leucine (21.5%, compared to 9% in typical proteins) and commensurately lower in other hydrophobic residues, esp. valine, isoleucine, methionine, tyrosine, and phenylalanine.

Structure

Side view of porcine ribonuclease inhibitor;[1] ribbon is colored from blue (N-terminus) to red (C-terminus).

RI is the classic leucine-rich repeat protein, consisting of alternating α-helices and β-strands along its backbone. These secondary structure elements wrap around in a curved, right-handed solenoid that resembles a horseshoe. The parallel β-strands and α-helices form the inner and outer wall of the horseshoe, respectively. The structure appears to be stabilized by buried asparagines at the base of each turn, as it passes from α-helix to β-strand. The αβ repeats alternate between 28 and 29 residues in length, effectively forming a 57-residue unit that corresponds to its genetic structure (each exon codes for a 57-residue unit).

Binding to ribonucleases

Ribonuclease I (yellow) and inhibitor (pink helixes) complex heterotetramer, Human.

The affinity of RI for ribonucleases is among the highest for any protein-protein interaction; the dissociation constant of the RI-RNase A complex is in the femtomolar (fM) range under physiological conditions while that for the RI-angiogenin complex is less than 1 fM. Despite this high affinity, RI is able to bind a wide variety of RNases A despite their relatively low sequence identity. Both biochemical studies and crystallographic structures of RI-RNase A complexes suggest that the interaction is governed largely by electrostatic interactions, but also involves substantial buried surface area.[3][4] RI's affinity for ribonucleases is important, since many ribonucleases have cytotoxic and cytostatic effects that correlate well with ability to bind RI.[5]

Mammalian RIs are unable to bind certain pancreatic ribonuclease family members from other species. In particular, amphibian RNases, such ranpirnase and amphinase from the Northern leopard frog, escape mammalian RI and have been noted to have differential cytotoxicity against cancer cells.[6]

See also

References

  1. ^ a b PDB: 2BNH​; Kobe B, Deisenhofer J (1993). "Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats". Nature. 366 (6457): 751–6. doi:10.1038/366751a0. PMID 8264799.
  2. ^ Shapiro R (2001). "Cytoplasmic ribonuclease inhibitor". Methods in Enzymology. 341: 611–28. doi:10.1016/S0076-6879(01)41180-3. PMID 11582809.
  3. ^ Lee FS, Shapiro R, Vallee BL (Jan 1989). "Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor". Biochemistry. 28 (1): 225–30. doi:10.1021/bi00427a031. PMID 2706246.
  4. ^ Papageorgiou AC, Shapiro R, Acharya KR (Sep 1997). "Molecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution". The EMBO Journal. 16 (17): 5162–77. doi:10.1093/emboj/16.17.5162. PMC 1170149. PMID 9311977.
  5. ^ Makarov AA, Ilinskaya ON (April 2003). "Cytotoxic ribonucleases: molecular weapons and their targets". FEBS Letters. 540 (1–3): 15–20. doi:10.1016/s0014-5793(03)00225-4. PMID 12681476.
  6. ^ Ardelt W, Shogen K, Darzynkiewicz Z (Jun 2008). "Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes". Current Pharmaceutical Biotechnology. 9 (3): 215–25. doi:10.2174/138920108784567245. PMC 2586917. PMID 18673287.

Further reading

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Leucine Rich Repeat Provide feedback

CAUTION: This Pfam may not find all Leucine Rich Repeats in a protein. Leucine Rich Repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.

Literature references

  1. Kobe B, Deisenhofer J; , Trends Biochem Sci 1994;19:415-421.: The leucine-rich repeat: a versatile binding motif. PUBMED:7817399 EPMC:7817399

  2. Kobe B, Deisenhofer J; , Nature 1993;366:751-756.: Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. PUBMED:8264799 EPMC:8264799


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001611

Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ PUBMED:14747988 ]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [ PUBMED:11751054 , PUBMED:1657640 ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [ PUBMED:2176636 , PUBMED:21606681 ].

Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the beta-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions [ PUBMED:11751054 ]. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats [ PUBMED:11967365 ].

Gene Ontology

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Domain organisation

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

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Pfam Clan

This family is a member of clan LRR (CL0022), which has the following description:

Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. This Pfam entry contains Leucine Rich Repeats not recognised by the Pfam:PF00560 model.

The clan contains the following 17 members:

DUF285 FBXL18_C FNIP LRR_1 LRR_10 LRR_11 LRR_12 LRR_2 LRR_3 LRR_4 LRR_5 LRR_6 LRR_8 LRR_9 LRR_RI_capping Recep_L_domain TTSSLRR

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.

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(2294)
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(26644)
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(68978)
RP15
(4201)
RP35
(22762)
RP55
(35548)
RP75
(47885)
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(2294)
Full
(26644)
Representative proteomes UniProt
(68978)
RP15
(4201)
RP35
(22762)
RP55
(35548)
RP75
(47885)
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  Seed
(2294)
Full
(26644)
Representative proteomes UniProt
(68978)
RP15
(4201)
RP35
(22762)
RP55
(35548)
RP75
(47885)
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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: Reference 1
Previous IDs: LRR;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A
Number in seed: 2294
Number in full: 26644
Average length of the domain: 23.90 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 3.88 %

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 20.6 9.3
Trusted cut-off 20.6 10.3
Noise cut-off 20.5 -1000000.0
Model length: 23
Family (HMM) version: 35
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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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 LRR_1 domain has been found. There are 175 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
A0A0G2KM01 View 3D Structure Click here
A0A0N7KPJ8 View 3D Structure Click here
A0A0N7KPJ8 View 3D Structure Click here
A0A0N7KPJ8 View 3D Structure Click here
A0A0N7KSN8 View 3D Structure Click here
A0A0N7KSZ4 View 3D Structure Click here
A0A0P0V4W2 View 3D Structure Click here
A0A0P0VEY2 View 3D Structure Click here
A0A0P0VF15 View 3D Structure Click here
A0A0P0VF33 View 3D Structure Click here
A0A0P0VGF8 View 3D Structure Click here
A0A0P0VHL9 View 3D Structure Click here
A0A0P0VHL9 View 3D Structure Click here
A0A0P0VJH3 View 3D Structure Click here
A0A0P0VLJ3 View 3D Structure Click here
A0A0P0VWT6 View 3D Structure Click here
A0A0P0WFJ3 View 3D Structure Click here
A0A0P0WFJ3 View 3D Structure Click here
A0A0P0WIF5 View 3D Structure Click here
A0A0P0WR41 View 3D Structure Click here
A0A0P0WTL7 View 3D Structure Click here
A0A0P0WYI2 View 3D Structure Click here
A0A0P0WYL7 View 3D Structure Click here
A0A0P0X077 View 3D Structure Click here
A0A0P0XI79 View 3D Structure Click here
A0A0P0XKQ2 View 3D Structure Click here
A0A0P0XKQ2 View 3D Structure Click here
A0A0P0XM98 View 3D Structure Click here
A0A0P0XR54 View 3D Structure Click here
A0A0P0XS56 View 3D Structure Click here
A0A0P0XUB1 View 3D Structure Click here
A0A0P0XUB1 View 3D Structure Click here
A0A0P0XV52 View 3D Structure Click here
A0A0P0XV52 View 3D Structure Click here
A0A0P0XVI7 View 3D Structure Click here
A0A0P0XVK4 View 3D Structure Click here
A0A0P0XZM1 View 3D Structure Click here
A0A0P0XZM1 View 3D Structure Click here
A0A0P0Y052 View 3D Structure Click here
A0A0P0Y0F0 View 3D Structure Click here
A0A0P0Y0Y5 View 3D Structure Click here
A0A0P0Y0Y5 View 3D Structure Click here
A0A0P0Y2E2 View 3D Structure Click here
A0A0P0Y3E8 View 3D Structure Click here
A0A0P0Y3Q8 View 3D Structure Click here
A0A0P0Y5Z4 View 3D Structure Click here
A0A0P0Y814 View 3D Structure Click here
A0A0P0Y873 View 3D Structure Click here
A0A0P0Y8A4 View 3D Structure Click here
A0A0P0Y8G9 View 3D Structure Click here
A0A0P0YA81 View 3D Structure Click here
A0A0P0YE31 View 3D Structure Click here
A0A0R0E2F2 View 3D Structure Click here
A0A0R0E2R8 View 3D Structure Click here
A0A0R0E3W6 View 3D Structure Click here
A0A0R0E3X1 View 3D Structure Click here
A0A0R0E484 View 3D Structure Click here
A0A0R0E9I8 View 3D Structure Click here
A0A0R0EB96 View 3D Structure Click here
A0A0R0ECQ3 View 3D Structure Click here
A0A0R0EE32 View 3D Structure Click here
A0A0R0EEB9 View 3D Structure Click here
A0A0R0F4P6 View 3D Structure Click here
A0A0R0F4P6 View 3D Structure Click here
A0A0R0F4P6 View 3D Structure Click here
A0A0R0F4Z2 View 3D Structure Click here
A0A0R0F9Q1 View 3D Structure Click here
A0A0R0F9Q1 View 3D Structure Click here
A0A0R0F9Q1 View 3D Structure Click here
A0A0R0FDC0 View 3D Structure Click here
A0A0R0FDC0 View 3D Structure Click here
A0A0R0FEJ4 View 3D Structure Click here
A0A0R0FEJ4 View 3D Structure Click here
A0A0R0FMR6 View 3D Structure Click here
A0A0R0FMR6 View 3D Structure Click here
A0A0R0FP46 View 3D Structure Click here
A0A0R0FPY0 View 3D Structure Click here
A0A0R0FRM6 View 3D Structure Click here
A0A0R0FRN7 View 3D Structure Click here
A0A0R0FRS0 View 3D Structure Click here
A0A0R0FRV6 View 3D Structure Click here
A0A0R0FS47 View 3D Structure Click here
A0A0R0FS47 View 3D Structure Click here
A0A0R0FS75 View 3D Structure Click here
A0A0R0FS89 View 3D Structure Click here
A0A0R0FS89 View 3D Structure Click here
A0A0R0FS91 View 3D Structure Click here
A0A0R0FS93 View 3D Structure Click here
A0A0R0FS98 View 3D Structure Click here
A0A0R0FSA5 View 3D Structure Click here
A0A0R0FSB0 View 3D Structure Click here
A0A0R0FSB3 View 3D Structure Click here
A0A0R0FSB4 View 3D Structure Click here
A0A0R0FSB4 View 3D Structure Click here
A0A0R0FSB5 View 3D Structure Click here
A0A0R0FSC7 View 3D Structure Click here
A0A0R0FSE4 View 3D Structure Click here
A0A0R0FSF9 View 3D Structure Click here
A0A0R0FSJ5 View 3D Structure Click here
A0A0R0FSL9 View 3D Structure Click here
A0A0R0FSN3 View 3D Structure Click here
A0A0R0FSN4 View 3D Structure Click here
A0A0R0FSX4 View 3D Structure Click here
A0A0R0FV18 View 3D Structure Click here
A0A0R0FVB8 View 3D Structure Click here
A0A0R0FWE4 View 3D Structure Click here
A0A0R0FWE4 View 3D Structure Click here
A0A0R0FWU9 View 3D Structure Click here
A0A0R0FYQ0 View 3D Structure Click here
A0A0R0FYR4 View 3D Structure Click here
A0A0R0FYS8 View 3D Structure Click here
A0A0R0FZ28 View 3D Structure Click here
A0A0R0FZK4 View 3D Structure Click here
A0A0R0FZM3 View 3D Structure Click here
A0A0R0FZQ5 View 3D Structure Click here
A0A0R0FZQ5 View 3D Structure Click here
A0A0R0FZS5 View 3D Structure Click here
A0A0R0FZV5 View 3D Structure Click here
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