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1281  structures 2961  species 0  interactions 312324  sequences 3711  architectures

Family: RRM_1 (PF00076)

Summary: RNA recognition motif. (a.k.a. RRM, RBD, or RNP 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 "RNA recognition motif". More...

RNA recognition motif Edit Wikipedia article

Typical architecture of an RRM domain, with a four-stranded antiparallel beta-sheet, stacked on two alpha helices
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
Identifiers
SymbolRRM_1
PfamPF00076
Pfam clanRRM CL0221 RRM
InterProIPR000504
PROSITEPDOC00030
SCOPe1sxl / SUPFAM

RNA recognition motif, RNP-1 is a putative RNA-binding domain of about 90 amino acids that are known to bind single-stranded RNAs. It was found in many eukaryotic proteins.[1][2][3]

The largest group of single strand RNA-binding protein is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence.[4][5]

RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF2, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu).[2][3][5] The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor appears to have two RRM-like domains with specialised features for protein recognition.[6] The motif also appears in a few single stranded DNA binding proteins.

The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases. A third helix is present during RNA binding in some cases.[7] The RRM is reviewed in a number of publications.[8][9][10]

Human proteins containing this domain

A2BP1; ACF; BOLL; BRUNOL4; BRUNOL5; BRUNOL6; CCBL2; CGI-96; CIRBP; CNOT4; CPEB2; CPEB3; CPEB4; CPSF7; CSTF2; CSTF2T; CUGBP1; CUGBP2; D10S102; DAZ1; DAZ2; DAZ3; DAZ4; DAZAP1; DAZL; DNAJC17; DND1; EIF3S4; EIF3S9; EIF4B; EIF4H; ELAVL1; ELAVL2; ELAVL3; ELAVL4; ENOX1; ENOX2; EWSR1; FUS; FUSIP1; G3BP; G3BP1; G3BP2; GRSF1; HNRNPL; HNRPA0; HNRPA1; HNRPA2B1; HNRPA3; HNRPAB; HNRPC; HNRPCL1; HNRPD; HNRPDL; HNRPF; HNRPH1; HNRPH2; HNRPH3; HNRPL; HNRPLL; HNRPM; HNRPR; HRNBP1; HSU53209; HTATSF1; IGF2BP1; IGF2BP2; IGF2BP3; LARP7; MKI67IP; MSI1; MSI2; MSSP-2; MTHFSD; MYEF2; NCBP2; NCL; NOL8; NONO; P14; PABPC1; PABPC1L; PABPC3; PABPC4; PABPC5; PABPN1; POLDIP3; PPARGC1; PPARGC1A; PPARGC1B; PPIE; PPIL4; PPRC1; PSPC1; PTBP1; PTBP2; PUF60; RALY; RALYL; RAVER1; RAVER2; RBM10; RBM11; RBM12; RBM12B; RBM14; RBM15; RBM15B; RBM16; RBM17; RBM18; RBM19; RBM22; RBM23; RBM24; RBM25; RBM26; RBM27; RBM28; RBM3; RBM32B; RBM33; RBM34; RBM35A; RBM35B; RBM38; RBM39; RBM4; RBM41; RBM42; RBM44; RBM45; RBM46; RBM47; RBM4B; RBM5; RBM7; RBM8A; RBM9; RBMS1; RBMS2; RBMS3; RBMX; RBMX2; RBMXL2; RBMY1A1; RBMY1B; RBMY1E; RBMY1F; RBMY2FP; RBPMS; RBPMS2; RDBP; RNPC3; RNPC4; RNPS1; ROD1; SAFB; SAFB2; SART3; SETD1A; SF3B14; SF3B4; SFPQ; SFRS1; SFRS10; SFRS11; SFRS12; SFRS15; SFRS2; SFRS2B; SFRS3; SFRS4; SFRS5; SFRS6; SFRS7; SFRS9; SLIRP; SLTM; SNRP70; SNRPA; SNRPB2; SPEN; SR140; SRRP35; SSB; SYNCRIP; TAF15; TARDBP; THOC4; TIA1; TIAL1; TNRC4; TNRC6C; TRA2A; TRSPAP1; TUT1; U1SNRNPBP; U2AF1; U2AF2; UHMK1; ZCRB1; ZNF638; ZRSR1; ZRSR2;

References

  1. ^ Swanson MS, Dreyfuss G, Pinol-Roma S (1988). "Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation". Trends Biochem. Sci. 13 (3): 86–91. doi:10.1016/0968-0004(88)90046-1. PMID 3072706.
  2. ^ a b Keene JD, Chambers JC, Kenan D, Martin BJ (1988). "Genomic structure and amino acid sequence domains of the human La autoantigen". J. Biol. Chem. 263 (34): 18043–51. PMID 3192525.
  3. ^ a b Davis RW, Sachs AB, Kornberg RD (1987). "A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability". Mol. Cell. Biol. 7 (9): 3268–76. PMC 367964. PMID 3313012.
  4. ^ Bandziulis RJ, Swanson MS, Dreyfuss G (1989). "RNA-binding proteins as developmental regulators". Genes Dev. 3 (4): 431–437. doi:10.1101/gad.3.4.431. PMID 2470643.
  5. ^ a b Keene JD, Query CC, Bentley RC (1989). "A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein". Cell. 57 (1): 89–101. doi:10.1016/0092-8674(89)90175-X. PMID 2467746.
  6. ^ Green MR, Kielkopf CL, Lucke S (2004). "U2AF homology motifs: protein recognition in the RRM world". Genes Dev. 18 (13): 1513–1526. doi:10.1101/gad.1206204. PMC 2043112. PMID 15231733.
  7. ^ Kumar S, Birney E, Krainer AR (1993). "Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors". Nucleic Acids Res. 21 (25): 5803–5816. doi:10.1093/nar/21.25.5803. PMC 310458. PMID 8290338.
  8. ^ Keene JD, Kenan DJ, Query CC (1991). "RNA recognition: towards identifying determinants of specificity". Trends Biochem. Sci. 16 (6): 214–20. doi:10.1016/0968-0004(91)90088-d. PMID 1716386.
  9. ^ Allain FH, Dominguez C, Maris C (2005). "The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression". FEBS J. 272 (9): 2118–31. doi:10.1111/j.1742-4658.2005.04653.x. PMID 15853797.
  10. ^ Teplova M, Yuan YR, Patel DJ, Malinina L, Teplov A, Phan AT, Ilin S (2006). "Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen". Mol. Cell. 21 (1): 75–85. doi:10.1016/j.molcel.2005.10.027. PMC 4689297. PMID 16387655.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR000504

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.

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) Provide feedback

The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

Literature references

  1. Birney E., Kumar S., Krainer A.R. , Nucleic Acid Res 1993;21:5803-5816.: Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. PUBMED:8290338 EPMC:8290338


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000504

Many eukaryotic proteins containing one or more copies of a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs [ PUBMED:3072706 , PUBMED:3192525 , PUBMED:3313012 ]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence [ PUBMED:2470643 , PUBMED:2467746 ]. RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu) [ PUBMED:3192525 , PUBMED:3313012 , PUBMED:2467746 ]. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialised features for protein recognition [ PUBMED:15231733 ]. The motif also appears in a few single stranded DNA binding proteins.

The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases. Specificity of RNA binding is determined by multiple contacts with surrounding amino acids. A third helix is present during RNA binding in some cases [ PUBMED:8290338 ]. The RRM is reviewed in a number of publications [ PUBMED:1716386 , PUBMED:15853797 , PUBMED:16387655 ].

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 RRM (CL0221), which has the following description:

This clan contains families that are related to the RNA recognition motif domains. However, not all these families are RNA binding.

The clan contains the following 32 members:

BRAP2 Calcipressin DbpA DUF1743 DUF1866 DUF4523 GlcNAc-1_reg GUCT Limkain-b1 Nup35_RRM Nup35_RRM_2 PHM7_cyt RL RNA_bind RRM_1 RRM_2 RRM_3 RRM_5 RRM_7 RRM_8 RRM_9 RRM_occluded RRM_Rrp7 SET_assoc Smg4_UPF3 Spo7_2_N Tap-RNA_bind Transposase_22 U1snRNP70_N xRRM XS YlmH_RBD

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
(68)
Full
(312324)
Representative proteomes UniProt
(572835)
RP15
(50373)
RP35
(137351)
RP55
(256417)
RP75
(350891)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

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  Seed
(68)
Full
(312324)
Representative proteomes UniProt
(572835)
RP15
(50373)
RP35
(137351)
RP55
(256417)
RP75
(350891)
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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
(68)
Full
(312324)
Representative proteomes UniProt
(572835)
RP15
(50373)
RP35
(137351)
RP55
(256417)
RP75
(350891)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped 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: Published_alignment
Previous IDs: rrm;
Type: Domain
Sequence Ontology: SO:0000417
Author: Eddy SR , Birney E
Number in seed: 68
Number in full: 312324
Average length of the domain: 67.40 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 22.53 %

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: 70
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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

Selections

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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 RRM_1 domain has been found. There are 1281 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
A0A023GRW3 View 3D Structure Click here
A0A087WNP0 View 3D Structure Click here
A0A087WPY7 View 3D Structure Click here
A0A087WR82 View 3D Structure Click here
A0A096P6L2 View 3D Structure Click here
A0A096PTJ8 View 3D Structure Click here
A0A096PTJ8 View 3D Structure Click here
A0A096Q2M8 View 3D Structure Click here
A0A096Q2M8 View 3D Structure Click here
A0A096Q2M8 View 3D Structure Click here
A0A096QLU9 View 3D Structure Click here
A0A096QLU9 View 3D Structure Click here
A0A096S6K6 View 3D Structure Click here
A0A096S6K6 View 3D Structure Click here
A0A096S6Y0 View 3D Structure Click here
A0A0B4J1A5 View 3D Structure Click here
A0A0B4J1B0 View 3D Structure Click here
A0A0B4J1B0 View 3D Structure Click here
A0A0B4KHI4 View 3D Structure Click here
A0A0B4KHI4 View 3D Structure Click here
A0A0B4KHI4 View 3D Structure Click here
A0A0B4KI17 View 3D Structure Click here
A0A0B4LGA2 View 3D Structure Click here
A0A0G2JNQ3 View 3D Structure Click here
A0A0G2JPF8 View 3D Structure Click here
A0A0G2JWE6 View 3D Structure Click here
A0A0G2JWR5 View 3D Structure Click here
A0A0G2JYJ7 View 3D Structure Click here
A0A0G2JYJ7 View 3D Structure Click here
A0A0G2JYP3 View 3D Structure Click here
A0A0G2JYV3 View 3D Structure Click here
A0A0G2K0Y2 View 3D Structure Click here
A0A0G2K1A3 View 3D Structure Click here
A0A0G2K2F4 View 3D Structure Click here
A0A0G2K3G4 View 3D Structure Click here
A0A0G2K3G4 View 3D Structure Click here
A0A0G2K402 View 3D Structure Click here
A0A0G2K402 View 3D Structure Click here
A0A0G2K402 View 3D Structure Click here
A0A0G2K6F9 View 3D Structure Click here
A0A0G2K6M1 View 3D Structure Click here
A0A0G2K6T6 View 3D Structure Click here
A0A0G2K8K0 View 3D Structure Click here
A0A0G2K8K0 View 3D Structure Click here
A0A0G2K904 View 3D Structure Click here
A0A0G2KPJ7 View 3D Structure Click here
A0A0G2KPJ7 View 3D Structure Click here
A0A0G2KT66 View 3D Structure Click here
A0A0G2KUM0 View 3D Structure Click here
A0A0G2KY64 View 3D Structure Click here
A0A0G2L7P5 View 3D Structure Click here
A0A0G2QC38 View 3D Structure Click here
A0A0K3AUP0 View 3D Structure Click here
A0A0K3AUP0 View 3D Structure Click here
A0A0K3AUP0 View 3D Structure Click here
A0A0N4SUF3 View 3D Structure Click here
A0A0N4SUH6 View 3D Structure Click here
A0A0N7KD12 View 3D Structure Click here
A0A0N7KDT5 View 3D Structure Click here
A0A0N7KDT5 View 3D Structure Click here
A0A0N7KF26 View 3D Structure Click here
A0A0N7KNJ2 View 3D Structure Click here
A0A0N7KNJ2 View 3D Structure Click here
A0A0N7KQI8 View 3D Structure Click here
A0A0N7KSQ1 View 3D Structure Click here
A0A0N7KSQ1 View 3D Structure Click here
A0A0N7KSQ1 View 3D Structure Click here
A0A0N7KUA3 View 3D Structure Click here
A0A0P0UYN0 View 3D Structure Click here
A0A0P0V1N4 View 3D Structure Click here
A0A0P0V8I6 View 3D Structure Click here
A0A0P0V8I6 View 3D Structure Click here
A0A0P0VEB3 View 3D Structure Click here
A0A0P0VFD5 View 3D Structure Click here
A0A0P0VFD5 View 3D Structure Click here
A0A0P0VFG2 View 3D Structure Click here
A0A0P0VG66 View 3D Structure Click here
A0A0P0VLM6 View 3D Structure Click here
A0A0P0VLM6 View 3D Structure Click here
A0A0P0VQQ7 View 3D Structure Click here
A0A0P0VST4 View 3D Structure Click here
A0A0P0VTH2 View 3D Structure Click here
A0A0P0VYT3 View 3D Structure Click here
A0A0P0W4V1 View 3D Structure Click here
A0A0P0WAK6 View 3D Structure Click here
A0A0P0WCA8 View 3D Structure Click here
A0A0P0WFG4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WGS4 View 3D Structure Click here
A0A0P0WH49 View 3D Structure Click here
A0A0P0WKE3 View 3D Structure Click here
A0A0P0WLH4 View 3D Structure Click here
A0A0P0WLH4 View 3D Structure Click here
A0A0P0WLK9 View 3D Structure Click here
A0A0P0WUL0 View 3D Structure Click here
A0A0P0WVY1 View 3D Structure Click here
A0A0P0WY24 View 3D Structure Click here
A0A0P0WY24 View 3D Structure Click here
A0A0P0WZZ1 View 3D Structure Click here
A0A0P0X0C9 View 3D Structure Click here
A0A0P0X229 View 3D Structure Click here
A0A0P0X2H7 View 3D Structure Click here
A0A0P0X2H7 View 3D Structure Click here
A0A0P0X3I7 View 3D Structure Click here
A0A0P0X3I7 View 3D Structure Click here
A0A0P0X3I7 View 3D Structure Click here
A0A0P0X3W0 View 3D Structure Click here
A0A0P0X887 View 3D Structure Click here
A0A0P0XCP2 View 3D Structure Click here
A0A0P0XCP2 View 3D Structure Click here
A0A0P0XCP2 View 3D Structure Click here
A0A0P0XMG9 View 3D Structure Click here
A0A0P0XQK8 View 3D Structure Click here
A0A0P0XR38 View 3D Structure Click here
A0A0P0XT31 View 3D Structure Click here
A0A0P0XYR1 View 3D Structure Click here
A0A0P0Y359 View 3D Structure Click here
A0A0P0Y5P0 View 3D Structure Click here
A0A0P0Y6K1 View 3D Structure Click here
A0A0P0Y6K1 View 3D Structure Click here
A0A0P0YBS5 View 3D Structure Click here
A0A0R0E5I3 View 3D Structure Click here
A0A0R0E5I3 View 3D Structure Click here
A0A0R0E5I3 View 3D Structure Click here
A0A0R0E5I3 View 3D Structure Click here
A0A0R0E5Y4 View 3D Structure Click here
A0A0R0E9J3 View 3D Structure Click here
A0A0R0E9J3 View 3D Structure Click here
A0A0R0EGA4 View 3D Structure Click here
A0A0R0EIA5 View 3D Structure Click here
A0A0R0EIA5 View 3D Structure Click here
A0A0R0EK66 View 3D Structure Click here
A0A0R0EL90 View 3D Structure Click here
A0A0R0EL90 View 3D Structure Click here
A0A0R0ERJ1 View 3D Structure Click here
A0A0R0ERJ1 View 3D Structure Click here
A0A0R0EWX2 View 3D Structure Click here
A0A0R0F2D9 View 3D Structure Click here
A0A0R0F2D9 View 3D Structure Click here
A0A0R0F5I2 View 3D Structure Click here
A0A0R0F8E2 View 3D Structure Click here
A0A0R0FE79 View 3D Structure Click here
A0A0R0FFQ3 View 3D Structure Click here
A0A0R0FIB0 View 3D Structure Click here
A0A0R0FJ89 View 3D Structure Click here
A0A0R0FRY7 View 3D Structure Click here
A0A0R0FSL3 View 3D Structure Click here
A0A0R0FWC0 View 3D Structure Click here
A0A0R0FY60 View 3D Structure Click here
A0A0R0G0B2 View 3D Structure Click here
A0A0R0G0X8 View 3D Structure Click here
A0A0R0G0X8 View 3D Structure Click here
A0A0R0G412 View 3D Structure Click here
A0A0R0G429 View 3D Structure Click here
A0A0R0G4H8 View 3D Structure Click here
A0A0R0G4H8 View 3D Structure Click here
A0A0R0G4R1 View 3D Structure Click here
A0A0R0GCY3 View 3D Structure Click here
A0A0R0GHK4 View 3D Structure Click here
A0A0R0GI77 View 3D Structure Click here
A0A0R0GI77 View 3D Structure Click here
A0A0R0GQ05 View 3D Structure Click here
A0A0R0GQ05 View 3D Structure Click here
A0A0R0GQ05 View 3D Structure Click here
A0A0R0GQ05 View 3D Structure Click here
A0A0R0GQ05 View 3D Structure Click here
A0A0R0GYR7 View 3D Structure Click here
A0A0R0GYR7 View 3D Structure Click here
A0A0R0GYR7 View 3D Structure Click here
A0A0R0H030 View 3D Structure Click here
A0A0R0H266 View 3D Structure Click here
A0A0R0H6J3 View 3D Structure Click here
A0A0R0HAB8 View 3D Structure Click here
A0A0R0HCT4 View 3D Structure Click here
A0A0R0HI47 View 3D Structure Click here
A0A0R0HRP1 View 3D Structure Click here
A0A0R0HTT1 View 3D Structure Click here
A0A0R0HXC9 View 3D Structure Click here
A0A0R0HZ49 View 3D Structure Click here
A0A0R0HZQ5 View 3D Structure Click here
A0A0R0I0F5 View 3D Structure Click here
A0A0R0I232 View 3D Structure Click here
A0A0R0I6L4 View 3D Structure Click here
A0A0R0I6T9 View 3D Structure Click here
A0A0R0I7Y1 View 3D Structure Click here
A0A0R0IF05 View 3D Structure Click here
A0A0R0IF05 View 3D Structure Click here
A0A0R0IJC5 View 3D Structure Click here
A0A0R0IJC5 View 3D Structure Click here
A0A0R0IJC5 View 3D Structure Click here
A0A0R0IKN2 View 3D Structure Click here
A0A0R0IPC8 View 3D Structure Click here
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