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426  structures 2214  species 0  interactions 23676  sequences 3852  architectures

Family: Ank (PF00023)

Summary: Ankyrin 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 "Ankyrin repeat". More...

Ankyrin repeat Edit Wikipedia article

Ankyrin repeat domain
Ankyrin R membrane-binding domain 1N11.png
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.[1]
Identifiers
SymbolAnk
PfamPF00023
InterProIPR002110
SMARTSM00248
PROSITEPDOC50088
SCOPe1awc / SUPFAM

The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin tandem repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.[2]

Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These domains are one of the most common protein–protein interaction platforms in nature. They occur in a large number of functionally diverse proteins, mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers.[3] The repeat has been found in proteins of diverse function such as transcriptional initiators, cell cycle regulators, cytoskeletal, ion transporters, and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or structure that is universally recognised by it.

Considering the atomic structures of individual ankyrin repeats, the loop is often a type 1 beta bulge loop, while both alpha-helices commonly have a Schellman loop at their N-terminus.

Role in protein folding

The ankyrin-repeat sequence motif has been studied using multiple sequence alignment to determine conserved amino acid residues critical for folding and stability. The residues on the wide lateral surface of ankyrin repeat structures are variable, often hydrophobic, and involved mainly in mediating protein–protein interactions. An artificial protein design based on a consensus sequence derived from sequence alignment has been synthesized and found to fold stably, representing the first designed protein with multiple repeats.[4] More extensive design strategies have used combinatorial sequences to "evolve" ankyrin-repeats that recognize particular protein targets, a technique that has been presented as an alternative to antibody design for applications requiring high-affinity binding.[5] A structure-based study involving a range of ankyrin proteins of known structures, shows that consensus-based ankyrin proteins are very stable since they maximize the energetic gap between the folding and unfolding structures, encoding a densely connected network of favourable interactions among conserved sequence motifs, like the TPLX motif.[6] The same study shows that insertions in the canonical framework of ankyrin repeats are enriched in conflictive interactions, that are related to function. The same applies to interactions surrounding deletion hotspots. These might be related to complex folding/unfolding transitions that are important to the partner recognition and interaction.

Ankyrin-repeat proteins present an unusual problem in the study of protein folding, which has largely focused on globular proteins that form well-defined tertiary structure stabilized by long-range, nonlocal residue-residue contacts. Ankyrin repeats, by contrast, contain very few such contacts (that is, they have a low contact order). Most studies have found that ankyrin repeats fold in a two-state folding mechanism, suggesting a high degree of folding cooperativity despite the local inter-residue contacts and the evident need for successful folding with varying numbers of repeats. Some evidence, based on synthesis of truncated versions of natural repeat proteins,[7] and on the examination of phi values,[8] suggests that the C-terminus forms the folding nucleation site.

Clinical significance

Ankyrin-repeat proteins have been associated with a number of human diseases. These proteins include the cell cycle inhibitor p16, which is associated with cancer, and the Notch protein (a key component of cell signalling pathways) which can cause the neurological disorder CADASIL when the repeat domain is disrupted by mutations.[2]

A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and regeneration of muscle tissue following damage due to injury and stress.[9]

A natural variation between glutamine and lysine at position 703 in the 11th ankyrin repeat of ANKK1, known as the TaqI A1 allele,[10] has been credited with encouraging addictive behaviours such as obesity, alcoholism, nicotine dependency and the Eros love style[citation needed] while discouraging juvenile delinquency and neuroticism-anxiety.[11][failed verification] The variation may affect the specificity of protein interactions made by the ANKK1 protein kinase through this repeat[citation needed].

Human proteins containing this repeat

ABTB1; ABTB2; ACBD6; ACTBL1; ANK1; ANK2; ANK3; ANKAR; ANKDD1A; ANKEF1; ANKFY1; ANKHD1; ANKIB1; ANKK1; ANKMY1; ANKMY2; ANKRA2; ANKRD1; ANKRD10; ANKRD11; ANKRD12; ANKRD13; ANKRD13A; ANKRD13B; ANKRD13C; ANKRD13D; ANKRD15; ANKRD16; ANKRD17; ANKRD18A; ANKRD18B; ANKRD19; ANKRD2; ANKRD20A1; ANKRD20A2; ANKRD20A3; ANKRD20A4; ANKRD21; ANKRD22; ANKRD23; ANKRD24; ANKRD25; ANKRD26; ANKRD27; ANKRD28; ANKRD30A; ANKRD30B; ANKRD30BL; ANKRD32; ANKRD33; ANKRD35; ANKRD36; ANKRD36B; ANKRD37; ANKRD38; ANKRD39; ANKRD40; ANKRD41; ANKRD42; ANKRD43; ANKRD44; ANKRD45; ANKRD46; ANKRD47; ANKRD49 [uk]; ANKRD50; ANKRD52; ANKRD53; ANKRD54; ANKRD55; ANKRD56; ANKRD57; ANKRD58; ANKRD60; ANKRD6; ANKRD7; ANKRD9; ANKS1A; ANKS3; ANKS4B; ANKS6; ANKZF1; ASB1; ASB10; ASB11; ASB12; ASB13; ASB14; ASB15; ASB16; ASB2; ASB3; ASB4; ASB5; ASB6; ASB7; ASB8; ASB9; ASZ1; BARD1; BAT4; BAT8; BCL3; BCOR; BCORL1; BTBD11; CAMTA1; CAMTA2; CASKIN1; CASKIN2; CCM1; CDKN2A; CDKN2B; CDKN2C; CDKN2D; CENTB1; CENTB2; CENTB5; CENTG1; CENTG2; CENTG3; CLIP3; CLIP4; CLPB; CTGLF1; CTGLF2; CTGLF3; CTGLF4; CTGLF5; CTTNBP2; DAPK1; DDEF1; DDEF2; DDEFL1; DGKI; DGKZ; DP58; DYSFIP1; DZANK; EHMT1; EHMT2; ESPN; FANK1; FEM1A; FEM1B; GABPB2; GIT1; GIT2; GLS; GLS2; HACE1; HECTD1; IBTK; ILK; INVS; KIDINS220; KRIT1; LRRK1; MAIL; MIB1; MIB2; MPHOSPH8; MTPN; MYO16; NFKB1; NFKB2; NFKBIA; NFKBIB; NFKBIE; NFKBIL1; NFKBIL2; NOTCH1; NOTCH2; NOTCH3; NOTCH4; NRARP; NUDT12; OSBPL1A; OSTF1; PLA2G6; POTE14; POTE15; POTE8; PPP1R12A; PPP1R12B; PPP1R12C; PPP1R13B; PPP1R13L; PPP1R16A; PPP1R16B; PSMD10; RAI14; RFXANK; RIPK4; RNASEL; SHANK1; SHANK2; SHANK3; SNCAIP; TA-NFKBH; TEX14; TNKS; TNKS2; TNNI3K; TP53BP2; TRP7; TRPA1; TRPC3; TRPC4; TRPC5; TRPC6; TRPC7; TRPV1; TRPV2; TRPV3; TRPV4; TRPV5; TRPV6; UACA; USH1G; ZDHHC13; ZDHHC17;

See also

  • DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats

References

  1. ^ PDB: 1N11​; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ANK1". EMBO J. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
  2. ^ a b Mosavi L, Cammett T, Desrosiers D, Peng Z (2004). "The ankyrin repeat as molecular architecture for protein recognition". Protein Sci. 13 (6): 1435–48. doi:10.1110/ps.03554604. PMC 2279977. PMID 15152081. Archived from the original on 2004-09-07.
  3. ^ Bork P (December 1993). "Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?". Proteins. 17 (4): 363–74. doi:10.1002/prot.340170405. PMID 8108379.
  4. ^ Mosavi LK, Minor DL, Peng ZY (Dec 2002). "Consensus-derived structural determinants of the ankyrin repeat motif". Proc Natl Acad Sci USA. 99 (25): 16029–34. Bibcode:2002PNAS...9916029M. doi:10.1073/pnas.252537899. PMC 138559. PMID 12461176.
  5. ^ Binz HK, Amstutz P, Kohl A, et al. (May 2004). "High-affinity binders selected from designed ankyrin repeat protein libraries". Nat. Biotechnol. 22 (5): 575–82. doi:10.1038/nbt962. PMID 15097997.
  6. ^ Parra RG, Espada R, Verstraete N, Ferreiro DU, et al. (Dec 2015). "Structural and Energetic Characterization of the Ankyrin Repeat Protein Family". PLoS Comput. Biol. 12 (11): 575–82. Bibcode:2015PLSCB..11E4659P. doi:10.1371/journal.pcbi.1004659. PMC 4687027. PMID 26691182.
  7. ^ Zhang B, Peng Z (Jun 2000). "A minimum folding unit in the ankyrin repeat protein p16(INK4)". J Mol Biol. 299 (4): 1121–32. doi:10.1006/jmbi.2000.3803. PMID 10843863.
  8. ^ Tang KS, Fersht AR, Itzhaki LS (Jan 2003). "Sequential unfolding of ankyrin repeats in tumor suppressor p16". Structure. 11 (1): 67–73. doi:10.1016/S0969-2126(02)00929-2. PMID 12517341.
  9. ^ Miller MK, Bang ML, Witt CC, et al. (Nov 2003). "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules". J Mol Biol. 333 (5): 951–64. doi:10.1016/j.jmb.2003.09.012. PMID 14583192.
  10. ^ Neville MJ, Johnstone EC, Walton RT (Jun 2004). "Identification and characterization of ANKK1: a novel kinase gene closely linked to DRD2 on chromosome band 11q23.1". Hum. Mutat. 23 (6): 540–5. doi:10.1002/humu.20039. PMID 15146457.
  11. ^ "NCBI Gene summary for DRD2". (interim reference)

External links

This article incorporates text from the public domain Pfam and InterPro: IPR002110

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.

Ankyrin repeat Provide feedback

Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity [2].

Literature references

  1. Lux SE, John KM, Bennett V; , Nature 1990;345:736-739.: Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. PUBMED:2141669 EPMC:2141669

  2. Michaely P, Tomchick DR, Machius M, Anderson RG;, EMBO J. 2002;21:6387-6396.: Crystal structure of a 12 ANK repeat stack from human ankyrinR. PUBMED:12456646 EPMC:12456646

  3. Michaely P, Bennett V;, Trends Cell Biol. 1992;2:127-129.: The ANK repeat: a ubiquitous motif involved in macromolecular recognition. PUBMED:14731966 EPMC:14731966


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002110

The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators [ PUBMED:31000436 ], cytoskeletal, ion transporters and signal transducers [ PUBMED:29769718 , PUBMED:8108379 ]. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it.

The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [ PUBMED:8875926 , PUBMED:9353127 , PUBMED:9461436 , PUBMED:9865693 ]. Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 o angle. The repeats stack together to form an L-shaped structure [ PUBMED:8875926 , PUBMED:12461176 ].

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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Pfam Clan

This family is a member of clan Ank (CL0465), which has the following description:

The ankyrin repeat is a short sequence region that is about 30-34 amino-acids in length. Multiple copies of the repeat composed of two beta strands and two alpha helices combine to form long arrays. In general these repeats are involved in protein-protein interactions. This superfamily also includes some families that are arrays of several repeats.

The clan contains the following 8 members:

Ank Ank_2 Ank_3 Ank_4 Ank_5 AnkUBD DUF3420 DUF3447

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
(1062)
Full
(23676)
Representative proteomes UniProt
(51400)
RP15
(5653)
RP35
(11324)
RP55
(19965)
RP75
(26580)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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(1062)
Full
(23676)
Representative proteomes UniProt
(51400)
RP15
(5653)
RP35
(11324)
RP55
(19965)
RP75
(26580)
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  Seed
(1062)
Full
(23676)
Representative proteomes UniProt
(51400)
RP15
(5653)
RP35
(11324)
RP55
(19965)
RP75
(26580)
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Gzipped Download   Download   Download   Download   Download   Download   Download  

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.

Note: You can also download the data file for the tree.

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: Swissprot_feature_table
Previous IDs: ank;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A , Sonnhammer ELL
Number in seed: 1062
Number in full: 23676
Average length of the domain: 33.60 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 4.36 %

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 21.1 14.7
Trusted cut-off 21.1 14.7
Noise cut-off 21.0 14.6
Model length: 33
Family (HMM) version: 32
Download: download the raw HMM for this family

Species distribution

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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 Ank domain has been found. There are 426 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
A0A0B4KHT3 View 3D Structure Click here
A0A0N7KFB4 View 3D Structure Click here
A0A0N7KNJ0 View 3D Structure Click here
A0A0N7KSB3 View 3D Structure Click here
A0A0P0W1F9 View 3D Structure Click here
A0A0P0W217 View 3D Structure Click here
A0A0P0WHC2 View 3D Structure Click here
A0A0P0WHN4 View 3D Structure Click here
A0A0P0X372 View 3D Structure Click here
A0A0P0X6N9 View 3D Structure Click here
A0A0P0XKI1 View 3D Structure Click here
A0A0P0XLS8 View 3D Structure Click here
A0A0P0Y2L3 View 3D Structure Click here
A0A0R0FX78 View 3D Structure Click here
A0A0R0GRA9 View 3D Structure Click here
A0A0R0IL26 View 3D Structure Click here
A0A0R0JDR7 View 3D Structure Click here
A0A0R0JJC2 View 3D Structure Click here
A0A0R4IK06 View 3D Structure Click here
A0A0R4J8R8 View 3D Structure Click here
A0A140LI88 View 3D Structure Click here
A0A1D6GI57 View 3D Structure Click here
A0A1D6H8W3 View 3D Structure Click here
A0A1D6HJJ9 View 3D Structure Click here
A0A1D6JTL6 View 3D Structure Click here
A0A1D6LKB5 View 3D Structure Click here
A0A1D6LZH9 View 3D Structure Click here
A0A1D6NWC1 View 3D Structure Click here
A0A1D6P3W0 View 3D Structure Click here
A0A1D6Q0B1 View 3D Structure Click here
A0A1D6QP36 View 3D Structure Click here
A0A1D8PCM9 View 3D Structure Click here
A0A1D8PED2 View 3D Structure Click here
A0A1P8B3M4 View 3D Structure Click here
A0A2R8PXZ5 View 3D Structure Click here
A0A2R8Q3Z4 View 3D Structure Click here
A0A2R8QIP1 View 3D Structure Click here
A0A2R8RK64 View 3D Structure Click here
A2BG42 View 3D Structure Click here
A4HS47 View 3D Structure Click here
A5WV38 View 3D Structure Click here
A6QL63 View 3D Structure Click here
B0G124 View 3D Structure Click here
B5DEH9 View 3D Structure Click here
B6SXU0 View 3D Structure Click here
B6SXU0 View 3D Structure Click here
B7F8U7 View 3D Structure Click here
B7WN72 View 3D Structure Click here
B8A2Y9 View 3D Structure Click here
B8JLP7 View 3D Structure Click here
C0HDR9 View 3D Structure Click here
C6T4N0 View 3D Structure Click here
D3Z8Q6 View 3D Structure Click here
D3ZCH1 View 3D Structure Click here
D3ZGR5 View 3D Structure Click here
D3ZHR4 View 3D Structure Click here
D3ZM27 View 3D Structure Click here
D3ZQF8 View 3D Structure Click here
D3ZSU6 View 3D Structure Click here
D4A1J6 View 3D Structure Click here
D4A1J6 View 3D Structure Click here
D4A6X3 View 3D Structure Click here
D4A731 View 3D Structure Click here
D4AC89 View 3D Structure Click here
D4ACT4 View 3D Structure Click here
D4ACT4 View 3D Structure Click here
E7EYI2 View 3D Structure Click here
E7EYI2 View 3D Structure Click here
E7F095 View 3D Structure Click here
E7F7Y4 View 3D Structure Click here
E7FFH0 View 3D Structure Click here
E9Q4F7 View 3D Structure Click here
E9QBZ2 View 3D Structure Click here
F1LVF8 View 3D Structure Click here
F1QQ98 View 3D Structure Click here
F1QZZ7 View 3D Structure Click here
F1R8I6 View 3D Structure Click here
F1RCM1 View 3D Structure Click here
F4JG84 View 3D Structure Click here
F4JVF4 View 3D Structure Click here
F4K1T0 View 3D Structure Click here
G5E893 View 3D Structure Click here
G5EDR9 View 3D Structure Click here
I1K3J5 View 3D Structure Click here
I1KDV5 View 3D Structure Click here
I1KL80 View 3D Structure Click here
I1KRY9 View 3D Structure Click here
I1LDT7 View 3D Structure Click here
I1MQ02 View 3D Structure Click here
I1MR51 View 3D Structure Click here
I1MU18 View 3D Structure Click here
I1N7F8 View 3D Structure Click here
I1N7L0 View 3D Structure Click here
I1NGR3 View 3D Structure Click here
K7KY41 View 3D Structure Click here
K7LU68 View 3D Structure Click here
K7U0L6 View 3D Structure Click here
M0R3T8 View 3D Structure Click here
O00221 View 3D Structure Click here
O00522 View 3D Structure Click here
O08764 View 3D Structure Click here
O08764 View 3D Structure Click here
O13987 View 3D Structure Click here
O14593 View 3D Structure Click here
O14593 View 3D Structure Click here
O14974 View 3D Structure Click here
O14974 View 3D Structure Click here
O14974 View 3D Structure Click here
O14974 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O15084 View 3D Structure Click here
O16632 View 3D Structure Click here
O16633 View 3D Structure Click here
O18152 View 3D Structure Click here
O18152 View 3D Structure Click here
O22265 View 3D Structure Click here
O35433 View 3D Structure Click here
O35516 View 3D Structure Click here
O35516 View 3D Structure Click here
O43150 View 3D Structure Click here
O44997 View 3D Structure Click here
O44997 View 3D Structure Click here
O44997 View 3D Structure Click here
O45398 View 3D Structure Click here
O45463 View 3D Structure Click here
O54910 View 3D Structure Click here
O55222 View 3D Structure Click here
O55222 View 3D Structure Click here
O55222 View 3D Structure Click here
O60237 View 3D Structure Click here
O60237 View 3D Structure Click here
O60733 View 3D Structure Click here
O60733 View 3D Structure Click here
O60733 View 3D Structure Click here
O60733 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O70511 View 3D Structure Click here
O74881 View 3D Structure Click here
O74881 View 3D Structure Click here
O74977 View 3D Structure Click here
O75762 View 3D Structure Click here
O75762 View 3D Structure Click here
O75762 View 3D Structure Click here
O75762 View 3D Structure Click here
O75762 View 3D Structure Click here
O75762 View 3D Structure Click here
O75912 View 3D Structure Click here
O88202 View 3D Structure Click here
O89019 View 3D Structure Click here
O89019 View 3D Structure Click here
O89019 View 3D Structure Click here
O89019 View 3D Structure Click here
O89019 View 3D Structure Click here
O89019 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O95271 View 3D Structure Click here
O97224 View 3D Structure Click here
P01129 View 3D Structure Click here
P0C0T2 View 3D Structure Click here
P0C6P7 View 3D Structure Click here
P0C7A6 View 3D Structure Click here
P13508 View 3D Structure Click here
P13508 View 3D Structure Click here
P14585 View 3D Structure Click here
P14585 View 3D Structure Click here
P14585 View 3D Structure Click here
P16157 View 3D Structure Click here
P16157 View 3D Structure Click here
P16157 View 3D Structure Click here
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