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41  structures 719  species 0  interactions 11357  sequences 205  architectures

Family: Inhibitor_I29 (PF08246)

Summary: Cathepsin propeptide inhibitor domain (I29)

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 "Protease inhibitor (biology)". More...

Protease inhibitor (biology) Edit Wikipedia article

In biology and biochemistry, protease inhibitors, or antiproteases,[1] are molecules that inhibit the function of proteases (enzymes that aid the breakdown of proteins). Many naturally occurring protease inhibitors are proteins.

In medicine, protease inhibitor is often used interchangeably with alpha 1-antitrypsin (A1AT, which is abbreviated PI for this reason).[2] A1AT is indeed the protease inhibitor most often involved in disease, namely in alpha-1 antitrypsin deficiency.

Classification

Protease inhibitors may be classified either by the type of protease they inhibit, or by their mechanism of action. In 2004 Rawlings and colleagues introduced a classification of protease inhibitors based on similarities detectable at the level of amino acid sequence.[3] This classification initially identified 48 families of inhibitors that could be grouped into 26 related superfamily (or clans) by their structure. According to the MEROPS database there are now 81 families of inhibitors. These families are named with an I followed by a number, for example, I14 contains hirudin-like inhibitors.

By protease

Classes of proteases are:

By mechanism

Classes of inhibitor mechanisms of action are:

Families

Inhibitor I4

This is a family of protease suicide inhibitors called the serpins. It contains inhibitors of multiple cysteine and serine protease families. Their mechanism of action relies on undergoing a large conformational change which inactivates their target's catalytic triad.

Inhibitor I9

Peptidase inhibitor I9
PDB 1spb EBI.jpg
subtilisin bpn' prosegment (77 residues) complexed with a mutant subtilisin bpn' (266 residues). crystal ph 4.6. crystallization temperature 20 c diffraction temperature-160 c
Identifiers
SymbolInhibitor_I9
PfamPF05922
InterProIPR010259
MEROPSI9
SCOPe1gns / SUPFAM

Proteinase propeptide inhibitors (sometimes referred to as activation peptides) are responsible for the modulation of folding and activity of the peptidase pro-enzyme or zymogen. The pro-segment docks into the enzyme, shielding the substrate binding site, thereby promoting inhibition of the enzyme. Several such propeptides share a similar topology, despite often low sequence identities.[4][5] The propeptide region has an open-sandwich antiparallel-alpha/antiparallel-beta fold, with two alpha-helices and four beta-strands with a (beta/alpha/beta)x2 topology. The peptidase inhibitor I9 family contains the propeptide domain at the N-terminus of peptidases belonging to MEROPS family S8A, subtilisins. The propeptide is removed by proteolytic cleavage; removal activating the enzyme.

Inhibitor I10

Serine endopeptidase inhibitors
PDB 1ixu EBI.jpg
solution structure of marinostatin, a protease inhibitor, containing two ester linkages
Identifiers
SymbolInhibitor_I10
PfamPF12559
InterProIPR022217

This family includes both microviridins and marinostatins. It seems likely that in both cases it is the C-terminus which becomes the active inhibitor after post-translational modifications of the full length, pre-peptide. It is the ester linkages within the key, 12-residue region that circularise the molecule giving it its inhibitory conformation.

Inhibitor I24

PinA peptidase inhibitor
Identifiers
SymbolInhibitor_I24
PfamPF10465
InterProIPR019506
MEROPSI24

This family includes PinA, which inhibits the endopeptidase La. It binds to the La homotetramer but does not interfere with the ATP binding site or the active site of La.

Inhibitor I29

Cathepsin propeptide inhibitor domain (I29)
PDB 1cjl EBI.jpg
crystal structure of a cysteine protease proform
Identifiers
SymbolInhibitor_I29
PfamPF08246
InterProIPR013201

The inhibitor I29 domain, which belongs to MEROPS peptidase inhibitor family I29, is found at the N-terminus of a variety of peptidase precursors that belong to MEROPS peptidase subfamily C1A; these include cathepsin L, papain, and procaricain.[6] It forms an alpha-helical domain that runs through the substrate-binding site, preventing access. Removal of this region by proteolytic cleavage results in activation of the enzyme. This domain is also found, in one or more copies, in a variety of cysteine peptidase inhibitors such as salarin.[7]

Inhibitor I34

Saccharopepsin inhibitor I34
PDB 1dp5 EBI.jpg
the structure of proteinase a complexed with an ia3 mutant inhibitor
Identifiers
SymbolInhibitor_I34
PfamPF10466
InterProIPR019507
MEROPSI34

The saccharopepsin inhibitor I34 is highly specific for the aspartic peptidase saccharopepsin. In the absence of saccharopepsin it is largely unstructured,[8] but in its presence, the inhibitor undergoes a conformational change forming an almost perfect alpha-helix from Asn2 to Met32 in the active site cleft of the peptidase.

Inhibitor I36

Peptidase inhibitor family I36
PDB 1bhu EBI.jpg
the 3d structure of the streptomyces metalloproteinase inhibitor, smpi, isolated from streptomyces nigrescens tk-23, nmr, minimized average structure
Identifiers
SymbolInhibitor_I36
PfamPF03995
Pfam clanCL0333
InterProIPR007141
MEROPSI36
SCOPe1bhu / SUPFAM

The peptidase inhibitor family I36 domain is only found in a small number of proteins restricted to Streptomyces species. All have four conserved cysteines that probably form two disulphide bonds. One of these proteins from Streptomyces nigrescens, is the well characterised metalloproteinase inhibitor SMPI.[9][10]

The structure of SMPI has been determined. It has 102 amino acid residues with two disulphide bridges and specifically inhibits metalloproteinases such as thermolysin, which belongs to MEROPS peptidase family M4. SMPI is composed of two beta-sheets, each consisting of four antiparallel beta-strands. The structure can be considered as two Greek key motifs with 2-fold internal symmetry, a Greek key beta-barrel. One unique structural feature found in SMPI is in its extension between the first and second strands of the second Greek key motif which is known to be involved in the inhibitory activity of SMPI. In the absence of sequence similarity, the SMPI structure shows clear similarity to both domains of the eye lens crystallins, both domains of the calcium sensor protein-S, as well as the single-domain yeast killer toxin. The yeast killer toxin structure was thought to be a precursor of the two-domain beta gamma-crystallin proteins, because of its structural similarity to each domain of the beta gamma-crystallins. SMPI thus provides another example of a single-domain protein structure that corresponds to the ancestral fold from which the two-domain proteins in the beta gamma-crystallin superfamily are believed to have evolved.[11]

Inhibitor I42

Chagasin family peptidase inhibitor I42
PDB 2fo8 EBI.jpg
solution structure of the trypanosoma cruzi cysteine protease inhibitor chagasin
Identifiers
SymbolInhibitor_I42
PfamPF09394
InterProIPR018990
MEROPSI42

Inhibitor family I42 includes chagasin, a reversible inhibitor of papain-like cysteine proteases.[12] Chagasin has a beta-barrel structure, which is a unique variant of the immunoglobulin fold with homology to human CD8alpha.[13][14]

Inhibitor I48

Peptidase inhibitor clitocypin
Identifiers
SymbolInhibitor_I48
PfamPF10467
InterProIPR019508
MEROPSI48

Inhibitor family I48 includes clitocypin, which binds and inhibits cysteine proteinases. It has no similarity to any other known cysteine proteinase inhibitors but bears some similarity to a lectin-like family of proteins from mushrooms.[15]

Inhibitor I53

Thrombin inhibitor Madanin
Identifiers
SymbolInhibitor_I53
PfamPF11714
InterProIPR021716
MEROPSI53

Members of this family are the peptidase inhibitor madanin proteins. These proteins were isolated from tick saliva.[16]

Inhibitor I67

Bromelain inhibitor VI
PDB 1bi6 EBI.jpg
nmr structure of bromelain inhibitor vi from pineapple stem
Identifiers
SymbolInhibitor_I67
PfamPF11405
InterProIPR022713
MEROPSI67

Bromelain inhibitor VI, in the Inhibitor I67 family, is a double-chain inhibitor consisting of an 11-residue and a 41-residue chain.

Inhibitor I68

Carboxypeptidase inhibitor I68
PDB 1zli EBI.jpg
crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase b
Identifiers
SymbolInhibitor_I68
PfamPF10468
InterProIPR019509
MEROPSI68

The Carboxypeptidase inhibitor I68 family represents a family of tick carboxypetidase inhibitors.

Inhibitor I78

Peptidase inhibitor I78 family
Identifiers
SymbolInhibitor_I78
PfamPF11720
Pfam clanCL0367
InterProIPR021719
MEROPSI78

The peptidase inhibitor I78 family includes Aspergillus elastase inhibitor.

Compounds

See also

References

  1. ^ "antiprotease". The Free Dictionary.
  2. ^ OMIM - PROTEASE INHIBITOR 1; PI
  3. ^ Rawlings ND, Tolle DP, Barrett AJ (March 2004). "Evolutionary families of peptidase inhibitors". Biochem. J. 378 (Pt 3): 705–16. doi:10.1042/BJ20031825. PMC 1224039. PMID 14705960.
  4. ^ Tangrea MA, Bryan PN, Sari N, Orban J (July 2002). "Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus". J. Mol. Biol. 320 (4): 801–12. doi:10.1016/S0022-2836(02)00543-0. PMID 12095256.
  5. ^ Jain SC, Shinde U, Li Y, Inouye M, Berman HM (November 1998). "The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution". J. Mol. Biol. 284 (1): 137–44. doi:10.1006/jmbi.1998.2161. PMID 9811547.
  6. ^ Groves MR, Taylor MA, Scott M, Cummings NJ, Pickersgill RW, Jenkins JA (October 1996). "The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft". Structure. 4 (10): 1193–203. doi:10.1016/s0969-2126(96)00127-x. PMID 8939744.
  7. ^ Olonen A, Kalkkinen N, Paulin L (July 2003). "A new type of cysteine proteinase inhibitor--the salarin gene from Atlantic salmon (Salmo salar L.) and Arctic charr (Salvelinus alpinus)". Biochimie. 85 (7): 677–81. doi:10.1016/S0300-9084(03)00128-7. PMID 14505823.
  8. ^ Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS (April 2004). "IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution". Biochemistry. 43 (14): 4071–81. doi:10.1021/bi034823n. PMID 15065849.
  9. ^ Tanaka K, Aoki H, Oda K, Murao S, Saito H, Takahashi H (November 1990). "Nucleotide sequence of the gene for a metalloproteinase inhibitor of Streptomyces nigrescens (SMPI)". Nucleic Acids Res. 18 (21): 6433. doi:10.1093/nar/18.21.6433. PMC 332545. PMID 2243793.
  10. ^ Murai H, Hara S, Ikenaka T, Oda K, Murao S (January 1985). "Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23". J. Biochem. 97 (1): 173–80. PMID 3888972.
  11. ^ Ohno A, Tate S, Seeram SS, Hiraga K, Swindells MB, Oda K, Kainosho M (September 1998). "NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure". J. Mol. Biol. 282 (2): 421–33. doi:10.1006/jmbi.1998.2022. PMID 9735297.
  12. ^ Monteiro AC, Abrahamson M, Lima AP, Vannier-Santos MA, Scharfstein J (November 2001). "Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi". J. Cell Sci. 114 (Pt 21): 3933–42. PMID 11719560.
  13. ^ Figueiredo da Silva AA; de Carvalho Vieira L; Krieger MA; Goldenberg S; Zanchin NI; Guimarães BG (February 2007). "Crystal structure of chagasin, the endogenous cysteine-protease inhibitor from Trypanosoma cruzi". J. Struct. Biol. 157 (2): 416–23. doi:10.1016/j.jsb.2006.07.017. PMID 17011790.
  14. ^ Wang SX, Pandey KC, Scharfstein J, Whisstock J, Huang RK, Jacobelli J, Fletterick RJ, Rosenthal PJ, Abrahamson M, Brinen LS, Rossi A, Sali A, McKerrow JH (May 2007). "The structure of chagasin in complex with a cysteine protease clarifies the binding mode and evolution of an inhibitor family". Structure. 15 (5): 535–43. doi:10.1016/j.str.2007.03.012. PMID 17502099.
  15. ^ Brzin J, Rogelj B, Popovic T, Strukelj B, Ritonja A (June 2000). "Clitocypin, a new type of cysteine proteinase inhibitor from fruit bodies of mushroom clitocybe nebularis". J. Biol. Chem. 275 (26): 20104–9. doi:10.1074/jbc.M001392200. PMID 10748021.
  16. ^ Iwanaga S, Okada M, Isawa H, Morita A, Yuda M, Chinzei Y (May 2003). "Identification and characterization of novel salivary thrombin inhibitors from the ixodidae tick, Haemaphysalis longicornis". Eur. J. Biochem. 270 (9): 1926–34. doi:10.1046/j.1432-1033.2003.03560.x. PMID 12709051.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR022217
This article incorporates text from the public domain Pfam and InterPro: IPR019506
This article incorporates text from the public domain Pfam and InterPro: IPR013201
This article incorporates text from the public domain Pfam and InterPro: IPR019507
This article incorporates text from the public domain Pfam and InterPro: IPR007141
This article incorporates text from the public domain Pfam and InterPro: IPR018990
This article incorporates text from the public domain Pfam and InterPro: IPR019508
This article incorporates text from the public domain Pfam and InterPro: IPR021716
This article incorporates text from the public domain Pfam and InterPro: IPR022713
This article incorporates text from the public domain Pfam and InterPro: IPR019509
This article incorporates text from the public domain Pfam and InterPro: IPR021719
This article incorporates text from the public domain Pfam and InterPro: IPR010259

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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.

Cathepsin propeptide inhibitor domain (I29) Provide feedback

This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin Q70SU8. This family is classified as I29 by MEROPS.

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013201

This entry represents a peptidase inhibitor domain, which belongs to MEROPS peptidase inhibitor family I29. The domain is also found at the N terminus of a variety of peptidase precursors that belong to MEROPS peptidase subfamily C1A; these include cathepsin L, papain, and procaricain ( SWISSPROT ) [ PUBMED:8939744 ]. It forms an alpha-helical domain that runs through the substrate-binding site, preventing access. Removal of this region by proteolytic cleavage results in activation of the enzyme. This domain is also found, in one or more copies, in a variety of cysteine peptidase inhibitors such as salarin [ PUBMED:14505823 ].

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
(56)
Full
(11357)
Representative proteomes UniProt
(22359)
RP15
(2265)
RP35
(6126)
RP55
(9919)
RP75
(12560)
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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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  Seed
(56)
Full
(11357)
Representative proteomes UniProt
(22359)
RP15
(2265)
RP35
(6126)
RP55
(9919)
RP75
(12560)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(56)
Full
(11357)
Representative proteomes UniProt
(22359)
RP15
(2265)
RP35
(6126)
RP55
(9919)
RP75
(12560)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
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: Pfam-B_14 (release 17.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 56
Number in full: 11357
Average length of the domain: 58.10 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 16.14 %

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 24.4 24.4
Trusted cut-off 24.4 24.4
Noise cut-off 24.3 24.3
Model length: 58
Family (HMM) version: 14
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 Inhibitor_I29 domain has been found. There are 41 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
A0A0G2JX50 View 3D Structure Click here
A0A0N7KCX2 View 3D Structure Click here
A0A0N7KMT7 View 3D Structure Click here
A0A0N7KRA0 View 3D Structure Click here
A0A0P0VBV2 View 3D Structure Click here
A0A0P0W3U6 View 3D Structure Click here
A0A0P0WNU3 View 3D Structure Click here
A0A0P0XQB7 View 3D Structure Click here
A0A0P0XQH0 View 3D Structure Click here
A0A0P0XQX8 View 3D Structure Click here
A0A0P0XR37 View 3D Structure Click here
A0A0P0XRA0 View 3D Structure Click here
A0A0R0EQB4 View 3D Structure Click here
A0A0R0F6I9 View 3D Structure Click here
A0A0R0F8Z1 View 3D Structure Click here
A0A0R0FYJ1 View 3D Structure Click here
A0A0R0G4W2 View 3D Structure Click here
A0A0R0GB30 View 3D Structure Click here
A0A0R0H4M2 View 3D Structure Click here
A0A0R0H4M8 View 3D Structure Click here
A0A0R0H550 View 3D Structure Click here
A0A0R0H5F5 View 3D Structure Click here
A0A0R0HDY3 View 3D Structure Click here
A0A0R0HE40 View 3D Structure Click here
A0A0R0HF84 View 3D Structure Click here
A0A0R0ITP6 View 3D Structure Click here
A0A0R0JBA3 View 3D Structure Click here
A0A0R0JMB1 View 3D Structure Click here
A0A0R0JSG8 View 3D Structure Click here
A0A0R0JSH1 View 3D Structure Click here
A0A0R0JUA1 View 3D Structure Click here
A0A0R0K177 View 3D Structure Click here
A0A0R0KC23 View 3D Structure Click here
A0A0R4J5M9 View 3D Structure Click here
A0A1D6DW35 View 3D Structure Click here
A0A1D6EEX8 View 3D Structure Click here
A0A1D6EEY9 View 3D Structure Click here
A0A1D6EEZ9 View 3D Structure Click here
A0A1D6EM70 View 3D Structure Click here
A0A1D6EM80 View 3D Structure Click here
A0A1D6ESI5 View 3D Structure Click here
A0A1D6EVL1 View 3D Structure Click here
A0A1D6F2H8 View 3D Structure Click here
A0A1D6F6N1 View 3D Structure Click here
A0A1D6FFM0 View 3D Structure Click here
A0A1D6GGX8 View 3D Structure Click here
A0A1D6GTM2 View 3D Structure Click here
A0A1D6HI75 View 3D Structure Click here
A0A1D6IIP0 View 3D Structure Click here
A0A1D6IIP1 View 3D Structure Click here
A0A1D6J4A8 View 3D Structure Click here
A0A1D6JG12 View 3D Structure Click here
A0A1D6KMS9 View 3D Structure Click here
A0A1D6LPA2 View 3D Structure Click here
A0A1D6LPA3 View 3D Structure Click here
A0A1D6LWA2 View 3D Structure Click here
A0A1D6N408 View 3D Structure Click here
A0A1D6NUP6 View 3D Structure Click here
A0A1D6NUQ6 View 3D Structure Click here
A0A1D6NYG3 View 3D Structure Click here
A0A1D6P8Y8 View 3D Structure Click here
A0A1D6PTB9 View 3D Structure Click here
A0A1D6PTC3 View 3D Structure Click here
A1Z9I0 View 3D Structure Click here
A1Z9I0 View 3D Structure Click here
A1Z9I0 View 3D Structure Click here
A1Z9I0 View 3D Structure Click here
A1ZAU4 View 3D Structure Click here
A1ZBK7 View 3D Structure Click here
A2BEM8 View 3D Structure Click here
A2BF64 View 3D Structure Click here
A4HTP0 View 3D Structure Click here
A4HYH2 View 3D Structure Click here
A5WVL6 View 3D Structure Click here
A7MCR6 View 3D Structure Click here
A8E588 View 3D Structure Click here
B4F9B5 View 3D Structure Click here
B4FS65 View 3D Structure Click here
B4FS90 View 3D Structure Click here
B4FX40 View 3D Structure Click here
B4FYA3 View 3D Structure Click here
B4FZ79 View 3D Structure Click here
B5KVP9 View 3D Structure Click here
B6TIC7 View 3D Structure Click here
B6TLC8 View 3D Structure Click here
B7ZXQ3 View 3D Structure Click here
C4IZ54 View 3D Structure Click here
C6TA48 View 3D Structure Click here
C6TDZ7 View 3D Structure Click here
C6TKC0 View 3D Structure Click here
D3ZFE5 View 3D Structure Click here
D3ZHI6 View 3D Structure Click here
D3ZP54 View 3D Structure Click here
D3ZZ07 View 3D Structure Click here
E7F2B2 View 3D Structure Click here
E7F8Y7 View 3D Structure Click here
E9Q623 View 3D Structure Click here
E9QBE2 View 3D Structure Click here
E9QE79 View 3D Structure Click here
F1Q8A0 View 3D Structure Click here
F1QCP8 View 3D Structure Click here
F1R4G6 View 3D Structure Click here
F1R7B3 View 3D Structure Click here
F1R8R0 View 3D Structure Click here
F1R8Y0 View 3D Structure Click here
F1R9W6 View 3D Structure Click here
F1RE14 View 3D Structure Click here
F4HZW2 View 3D Structure Click here
F4JNL3 View 3D Structure Click here
G3V9F8 View 3D Structure Click here
I1J446 View 3D Structure Click here
I1J447 View 3D Structure Click here
I1JSR6 View 3D Structure Click here
I1JT65 View 3D Structure Click here
I1JT73 View 3D Structure Click here
I1JTM0 View 3D Structure Click here
I1JXE2 View 3D Structure Click here
I1K268 View 3D Structure Click here
I1K795 View 3D Structure Click here
I1K796 View 3D Structure Click here
I1KC88 View 3D Structure Click here
I1KEJ9 View 3D Structure Click here
I1KEK2 View 3D Structure Click here
I1KEK3 View 3D Structure Click here
I1KEK6 View 3D Structure Click here
I1KEL0 View 3D Structure Click here
I1KEN8 View 3D Structure Click here
I1KES2 View 3D Structure Click here
I1KES3 View 3D Structure Click here
I1KLT2 View 3D Structure Click here
I1L1Q3 View 3D Structure Click here
I1LJ95 View 3D Structure Click here
I1LL41 View 3D Structure Click here
I1LPZ4 View 3D Structure Click here
I1LR49 View 3D Structure Click here
I1LR51 View 3D Structure Click here
I1LSC0 View 3D Structure Click here
I1LSF8 View 3D Structure Click here
I1LSI6 View 3D Structure Click here
I1LSJ1 View 3D Structure Click here
I1M8Q5 View 3D Structure Click here
I1MC68 View 3D Structure Click here
I1MER7 View 3D Structure Click here
I1MHG0 View 3D Structure Click here
I1MMG2 View 3D Structure Click here
I1MUK9 View 3D Structure Click here
I1MVT7 View 3D Structure Click here
I1MXL3 View 3D Structure Click here
K7K0Y1 View 3D Structure Click here
K7KXR2 View 3D Structure Click here
K7KXR4 View 3D Structure Click here
K7KXR5 View 3D Structure Click here
K7KXR6 View 3D Structure Click here
K7KXR7 View 3D Structure Click here
K7KXR8 View 3D Structure Click here
K7KXR9 View 3D Structure Click here
K7L2V8 View 3D Structure Click here
K7LUE4 View 3D Structure Click here
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