45 publications

45 publications

A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization

Bruns, N.

Angew. Chem., Int. Ed., 2013, 10.1002/anie.201306798

The group II chaperonin thermosome (THS) from the archaea Thermoplasma acidophilum is reported as nanoreactor for atom‐transfer radical polymerization (ATRP). A copper catalyst was entrapped into the THS to confine the polymerization into this protein cage. THS possesses pores that are wide enough to release polymers into solution. The nanoreactor favorably influenced the polymerization of N‐isopropyl acrylamide and poly(ethylene glycol)methylether acrylate. Narrowly dispersed polymers with polydispersity indices (PDIs) down to 1.06 were obtained in the protein nanoreactor, while control reactions with a globular protein–catalyst conjugate only yielded polymers with PDIs above 1.84.


Metal: Cu
Host protein: Thermosome (THS)
Anchoring strategy: Covalent
Optimization: ---
Reaction: Polymerization
Max TON: ---
ee: ---
PDB: ---
Notes: Non-ROMP

A Clamp-Like Biohybrid Catalyst for DNA Oxidation

Nolte, R. J. M.

Nat. Chem., 2013, 10.1038/NCHEM.1752

In processive catalysis, a catalyst binds to a substrate and remains bound as it performs several consecutive reactions, as exemplified by DNA polymerases. Processivity is essential in nature and is often mediated by a clamp-like structure that physically tethers the catalyst to its (polymeric) template. In the case of the bacteriophage T4 replisome, a dedicated clamp protein acts as a processivity mediator by encircling DNA and subsequently recruiting its polymerase. Here we use this DNA-binding protein to construct a biohybrid catalyst. Conjugation of the clamp protein to a chemical catalyst with sequence-specific oxidation behaviour formed a catalytic clamp that can be loaded onto a DNA plasmid. The catalytic activity of the biohybrid catalyst was visualized using a procedure based on an atomic force microscopy method that detects and spatially locates oxidized sites in DNA. Varying the experimental conditions enabled switching between processive and distributive catalysis and influencing the sliding direction of this rotaxane-like catalyst.


Metal: Mn
Ligand type: Porphyrin
Host protein: gp45
Anchoring strategy: Covalent
Optimization: ---
Max TON: ---
ee: ---
PDB: 1CZD
Notes: ---

A Cofactor Approach to Copper-Dependent Catalytic Antibodies

Janda, K. D.; Nicholas, K. M.

Proc. Natl. Acad. Sci. U. S. A., 2002, 10.1073/pnas.052001099

A strategy for the preparation of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bis-imidazole cofactor is incorporated into the combining site of the aldolase antibody 38C2. Antibody 38C2 features a large hydrophobic-combining site pocket with a highly nucleophilic lysine residue, LysH93, that can be covalently modified. A comparison of several lactone and anhydride reagents shows that the latter are the most effective and general derivatizing agents for the 38C2 Lys residue. A bis-imidazole anhydride (5) was efficiently prepared from N-methyl imidazole. The 38C2–5-Cu conjugate was prepared by either (i) initial derivatization of 38C2 with 5 followed by metallation with CuCl2, or (ii) precoordination of 5 with CuCl2 followed by conjugation with 38C2. The resulting 38C2–5-Cu conjugate was an active catalyst for the hydrolysis of the coordinating picolinate ester 11, following Michaelis–Menten kinetics [kcat(11) = 2.3 min−1 and Km(11) 2.2 mM] with a rate enhancement [kcat(11)kuncat(11)] of 2.1 × 105. Comparison of the second-order rate constants of the modified 38C2 and the Cu(II)-bis-imidazolyl complex k(6-CuCl2) gives a rate enhancement of 3.5 × 104 in favor of the antibody complex with an effective molarity of 76.7 M, revealing a significant catalytic benefit to the binding of the bis-imidazolyl ligand into 38C2.


Metal: Cu
Ligand type: Bisimidazol
Host protein: Antibody 38C2
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

A General Method for Artificial Metalloenzyme Formationthrough Strain-Promoted Azide–Alkyne Cycloaddition

Lewis, J. C.

ChemBioChem, 2014, 10.1002/cbic.201300661

Strain‐promoted azide–alkyne cycloaddition (SPAAC) can be used to generate artificial metalloenzymes (ArMs) from scaffold proteins containing a p‐azido‐L‐phenylalanine (Az) residue and catalytically active bicyclononyne‐substituted metal complexes. The high efficiency of this reaction allows rapid ArM formation when using Az residues within the scaffold protein in the presence of cysteine residues or various reactive components of cellular lysate. In general, cofactor‐based ArM formation allows the use of any desired metal complex to build unique inorganic protein materials. SPAAC covalent linkage further decouples the native function of the scaffold from the installation process because it is not affected by native amino acid residues; as long as an Az residue can be incorporated, an ArM can be generated. We have demonstrated the scope of this method with respect to both the scaffold and cofactor components and established that the dirhodium ArMs generated can catalyze the decomposition of diazo compounds and both SiH and olefin insertion reactions involving these carbene precursors.


Metal: Rh
Ligand type: Poly-carboxylic acid
Host protein: tHisF
Anchoring strategy: Covalent
Optimization: ---
Reaction: Cyclopropanation
Max TON: 81
ee: ---
PDB: 1THF
Notes: ---

Metal: Rh
Ligand type: Poly-carboxylic acid
Host protein: tHisF
Anchoring strategy: Covalent
Optimization: ---
Reaction: Si-H Insertion
Max TON: 7
ee: ---
PDB: 1THF
Notes: ---

A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein

Okuda, J.

ACS Catal., 2015, 10.1021/acscatal.5b01792

A series of Grubbs–Hoveyda type catalyst precursors for olefin metathesis containing a maleimide moiety in the backbone of the NHC ligand was covalently incorporated in the cavity of the β-barrel protein nitrobindin. By using two protein mutants with different cavity sizes and choosing the suitable spacer length, an artificial metalloenzyme for olefin metathesis reactions in water in the absence of any organic cosolvents was obtained. High efficiencies reaching TON > 9000 in the ROMP of a water-soluble 7-oxanorbornene derivative and TON > 100 in ring-closing metathesis (RCM) of 4,4-bis(hydroxymethyl)-1,6-heptadiene in water under relatively mild conditions (pH 6, T = 25–40 °C) were observed.


Metal: Ru
Ligand type: Carbene
Host protein: Nitrobindin (Nb)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Olefin metathesis
Max TON: 9900
ee: ---
PDB: ---
Notes: ROMP (cis/trans: 48/52)

Metal: Ru
Ligand type: Carbene
Host protein: Nitrobindin (Nb)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Olefin metathesis
Max TON: 100
ee: ---
PDB: ---
Notes: RCM

A Hybrid Ring- Opening Metathesis Polymerization Catalyst Based on an Engineered Variant of the Beta-Barrel Protein FhuA

Okuda, J.; Schwaneberg, U.

Chem. - Eur. J., 2013, 10.1002/chem.201301515

A β‐barrel protein hybrid catalyst was prepared by covalently anchoring a Grubbs–Hoveyda type olefin metathesis catalyst at a single accessible cysteine amino acid in the barrel interior of a variant of β‐barrel transmembrane protein ferric hydroxamate uptake protein component A (FhuA). Activity of this hybrid catalyst type was demonstrated by ring‐opening metathesis polymerization of a 7‐oxanorbornene derivative in aqueous solution.


Metal: Ru
Ligand type: Carbene
Host protein: FhuA ΔCVFtev
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Olefin metathesis
Max TON: 955
ee: ---
PDB: ---
Notes: ROMP

A Metal Ion Regulated Artificial Metalloenzyme

Roelfes, G.

Dalton Trans., 2017, 10.1039/C7DT00533D

Regulation of enzyme activity is essential in living cells. The rapidly increasing number of designer enzymes with new-to-nature activities makes it necessary to develop novel strategies for controlling their catalytic activity. Here we present the development of a metal ion regulated artificial metalloenzyme created by combining two anchoring strategies, covalent and supramolecular, for introducing a regulatory and a catalytic site, respectively. This artificial metalloenzyme is activated in the presence of Fe2+ ions, but only marginally in the presence of Zn2+.


Metal: Fe
Ligand type: Bypyridine
Host protein: LmrR
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 14
ee: 75
PDB: ---
Notes: ---

Metal: Zn
Ligand type: Bypyridine
Host protein: LmrR
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 6
ee: 80
PDB: ---
Notes: ---

An Artificial Enzyme Made by Covalent Grafting of an FeII Complex into β-Lactoglobulin: Molecular Chemistry, Oxidation Catalysis, and Reaction-Intermediate Monitoring in a Protein

Banse, F.; Mahy, J.-P.

Chem. - Eur. J., 2015, 10.1002/chem.201501755

An artificial metalloenzyme based on the covalent grafting of a nonheme FeII polyazadentate complex into bovine β‐lactoglobulin has been prepared and characterized by using various spectroscopic techniques. Attachment of the FeII catalyst to the protein scaffold is shown to occur specifically at Cys121. In addition, spectrophotometric titration with cyanide ions based on the spin‐state conversion of the initial high spin (S=2) FeII complex into a low spin (S=0) one allows qualitative and quantitative characterization of the metal center’s first coordination sphere. This biohybrid catalyst activates hydrogen peroxide to oxidize thioanisole into phenylmethylsulfoxide as the sole product with an enantiomeric excess of up to 20 %. Investigation of the reaction between the biohybrid system and H2O2 reveals the generation of a high spin (S=5/2) FeIII(η2‐O2) intermediate, which is proposed to be responsible for the catalytic sulfoxidation of the substrate.


Metal: Fe
Ligand type: Poly-pyridine
Host protein: ß-lactoglobulin
Anchoring strategy: Covalent
Optimization: ---
Reaction: Sulfoxidation
Max TON: 5.6
ee: 20
PDB: ---
Notes: ---

An Artificial Metalloenzyme for Olefin Metathesis

Hilvert, D.; Ward, T. R.

Chem. Commun., 2011, 10.1039/c1cc15005g

A Grubbs–Hoveyda type olefin metathesis catalyst, equipped with an electrophilic bromoacetamide group, was used to modify a cysteine-containing variant of a small heat shock protein from Methanocaldococcus jannaschii. The resulting artificial metalloenzyme was found to be active under acidic conditions in a benchmark ring closing metathesis reaction.


Metal: Ru
Ligand type: Carbene
Anchoring strategy: Covalent
Optimization: ---
Reaction: Olefin metathesis
Max TON: 25
ee: ---
PDB: ---
Notes: RCM

An Enantioselective Artificial Metallo-Hydratase

Roelfes, G.

Chem. Sci., 2013, 10.1039/c3sc51449h

Direct addition of water to alkenes to generate important chiral alcohols as key motif in a variety of natural products still remains a challenge in organic chemistry. Here, we report the first enantioselective artificial metallo-hydratase, based on the transcription factor LmrR, which catalyses the conjugate addition of water to generate chiral β-hydroxy ketones with enantioselectivities up to 84% ee. A mutagenesis study revealed that an aspartic acid and a phenylalanine located in the active site play a key role in achieving efficient catalysis and high enantioselectivities.


Metal: Cu
Ligand type: Phenanthroline
Host protein: LmrR
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 30
ee: 84
PDB: 3F8B
Notes: ---

Aqueous Phase Transfer Hydrogenation of Aryl Ketones Catalysed by Achiral Ruthenium(II) and Rhodium(III) Complexes and their Papain Conjugates

Salmain, M.

Appl. Organomet. Chem., 2013, 10.1002/aoc.2929


Metal: Rh
Ligand type: Cp*; Poly-pyridine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 96
ee: 15
PDB: ---
Notes: ---

Artificial Copper Enzymes for Asymmetric Diels–AlderReactions

Kamer, P. C. J.; Laan, W.

ChemCatChem, 2012, 10.1002/cctc.201200671


Metal: Cu
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Max TON: 9.6
ee: 25
PDB: 1IKT
Notes: ---

Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials

Lombardi, A.; Nastri, F.

Int. J. Mol. Sci., 2018, 10.3390/ijms19102896


Metal: Fe
Ligand type: Amino acid; Porphyrin
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: Immobilization of the ArM on gold surfaces via a lipoic acid anchor.

Artificial Metalloenzymes based on Protein Cavities: Exploring the Effect of Altering the Metal Ligand Attachment Position by Site Directed Mutagenesis

Distefano, M. D.

Bioorg. Med. Chem. Lett., 1999, 10.1016/S0960-894X(98)00684-2


Metal: Cu
Ligand type: Phenanthroline
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 1 to 4
ee: 61 to 94
PDB: ---
Notes: Varied attachment position

Artificial Metalloenzymes Through Cysteine-Selective Conjugation of Phosphines to Photoactive Yellow Protein

Kamer, P. C. J.

ChemBioChem, 2010, 10.1002/cbic.201000159


Metal: Pd
Ligand type: Allyl; Phosphine
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Allylic amination
Max TON: 45
ee: ---
PDB: 2PHY
Notes: ---

A Semisynthetic Metalloenzyme based on a Protein Cavity that Catalyzes the Enantioselective Hydrolysis of Ester and Amide Substrates

Distefano, M. D.

J. Am. Chem. Soc., 1997, 10.1021/JA970820K

In an effort to prepare selective and efficient catalysts for ester and amide hydrolysis, we are designing systems that position a coordinated metal ion within a defined protein cavity. Here, the preparation of a protein-1,10-phenanthroline conjugate and the hydrolytic chemistry catalyzed by this construct are described. Iodoacetamido-1,10-phenanthroline was used to modify a unique cysteine residue in ALBP (adipocyte lipid binding protein) to produce the conjugate ALBP-Phen. The resulting material was characterized by electrospray mass spectrometry, UV/vis and fluorescence spectroscopy, gel filtration chromatography, and thiol titration. The stability of ALBP-Phen was evaluated by guanidine hydrochloride denaturation experiments, and the ability of the conjugate to bind Cu(II) was demonstrated by fluorescence spectroscopy. ALBP-Phen-Cu(II) catalyzes the enantioselective hydrolysis of several unactivated amino acid esters under mild conditions (pH 6.1, 25 °C) at rates 32−280-fold above the background rate in buffered aqueous solution. In 24 h incubations 0.70 to 7.6 turnovers were observed with enantiomeric excesses ranging from 31% ee to 86% ee. ALBP-Phen-Cu(II) also promotes the hydrolysis of an aryl amide substrate under more vigorous conditions (pH 6.1, 37 °C) at a rate 1.6 × 104-fold above the background rate. The kinetics of this amide hydrolysis reaction fit the Michaelis−Menten relationship characteristic of enzymatic processes. The rate enhancements for ester and amide hydrolysis reported here are 102−103 lower than those observed for free Cu(II) but comparable to those previously reported for Cu(II) complexes.


Metal: Cu
Ligand type: Phenanthroline
Anchoring strategy: Covalent
Optimization: ---
Max TON: 1 to 8
ee: 39 to 86
PDB: ---
Notes: ---

A Site-Selective Dual Anchoring Strategy for Artificial Metalloprotein Design

Lu, Y.

J. Am. Chem. Soc., 2004, 10.1021/ja046908x

Introducing nonnative metal ions or metal-containing prosthetic groups into a protein can dramatically expand the repertoire of its functionalities and thus its range of applications. Particularly challenging is the control of substrate-binding and thus reaction selectivity such as enantioselectivity. To meet this challenge, both non-covalent and single-point attachments of metal complexes have been demonstrated previously. Since the protein template did not evolve to bind artificial metal complexes tightly in a single conformation, efforts to restrict conformational freedom by modifying the metal complexes and/or the protein are required to achieve high enantioselectivity using the above two strategies. Here we report a novel site-selective dual anchoring (two-point covalent attachment) strategy to introduce an achiral manganese salen complex (Mn(salen)), into apo sperm whale myoglobin (Mb) with bioconjugation yield close to 100%. The enantioselective excess increases from 0.3% for non-covalent, to 12.3% for single point, and to 51.3% for dual anchoring attachments. The dual anchoring method has the advantage of restricting the conformational freedom of the metal complex in the protein and can be generally applied to protein incorporation of other metal complexes with minimal structural modification to either the metal complex or the protein.


Metal: Mn
Ligand type: Salen
Host protein: Myoglobin (Mb)
Anchoring strategy: Covalent
Optimization: Genetic
Reaction: Sulfoxidation
Max TON: 3.9
ee: 51
PDB: 1MBO
Notes: Sperm whale myoglobin

Autoxidation of Ascorbic Acid Catalyzed by a Semisynthetic Enzyme

Kaiser, E. T.

Biopolymers, 1990, 10.1002/bip.360290107


Metal: Cu
Ligand type: Bipyridine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: ---
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Chemical Conversion of a DNA-Binding Protein into a Site-Specific Nuclease

Sigman, D. S.

Science, 1987, 10.1126/science.2820056


Metal: Cu
Ligand type: Phenanthroline
Anchoring strategy: Covalent
Optimization: ---
Reaction: Oxidative cleavage
Max TON: <1
ee: ---
PDB: ---
Notes: Engineered sequence specificity

Chemically Engineered Papain as Artificial Formate Dehydrogenase for NAD(P)H Regeneration

Salmain, M.

Org. Biomol. Chem., 2011, 10.1039/c1ob05482a


Metal: Rh
Ligand type: Cp*; Poly-pyridine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Hydrogenation
Max TON: ---
ee: ---
PDB: ---
Notes: TOF = 52.1 h-1 for NAD+

Conversion of a Helix-Turn-Helix Motif Sequence-Specific DNA Binding Protein into a Site-Specific DNA Cleavage Agent

Ebright, R. H.; Gunasekeram, A.

Proc. Natl. Acad. Sci. U. S. A., 1990, 10.1073/pnas.87.8.2882


Metal: Cu
Ligand type: Phenanthroline
Anchoring strategy: Covalent
Optimization: ---
Reaction: Oxidative cleavage
Max TON: <1
ee: ---
PDB: ---
Notes: Engineered sequence specificity

Covalent Anchoring of a Racemization Catalyst to CALB-Beads: Towards Dual Immobilization of DKR Catalysts

Klein Gebbink, R. J. M.; van Koten, G.

Tetrahedron Lett., 2011, 10.1016/j.tetlet.2011.01.106


Metal: Ru
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Acylation
Max TON: ---
ee: >99%
PDB: ---
Notes: Lipase CALB is immobilized on a solid support (Novozym®435). Dynamic kinetic resolution (DKR) of 1-phenylethanol to the acylated product.

Creation of an Artificial Metalloprotein with a Hoveyda–Grubbs Catalyst Moiety through the Intrinsic Inhibition Mechanism of α-Chymotrypsin

Chem. Commun., 2012, 10.1039/c2cc16898g


Metal: Ru
Ligand type: Carbene
Host protein: α-chymotrypsin
Anchoring strategy: Covalent
Optimization: ---
Reaction: Olefin metathesis
Max TON: 20
ee: ---
PDB: ---
Notes: RCM

Enantioselective Artificial Metalloenzymes by Creation of a Novel Active Site at the Protein Dimer Interface

Roelfes, G.

Angew. Chem., Int. Ed., 2012, 10.1002/anie.201202070


Metal: Cu
Ligand type: Bipyridine; Phenanthroline
Host protein: LmrR
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 32.7
ee: 97
PDB: 3F8B
Notes: ---

Engineering a Dirhodium Artificial Metalloenzyme for Selective Olefin Cyclopropanation

Lewis, J. C.

Nat. Commun., 2015, 10.1038/ncomms8789


Metal: Rh
Ligand type: Poly-carboxylic acid
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: 74
ee: 92
PDB: ---
Notes: ---

Evolving Artificial Metalloenzymes via Random Mutagenesis

Lewis, J. C.

Nat. Chem., 2018, 10.1038/nchem.2927


Metal: Rh
Ligand type: OAc
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: 66
ee: 94
PDB: 5T88
Notes: Mutagenesis of the ArM by error-prone PCR

Metal: Rh
Ligand type: OAc
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: N-H Insertion
Max TON: 73
ee: 40
PDB: 5T88
Notes: Mutagenesis of the ArM by error-prone PCR

Metal: Rh
Ligand type: OAc
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: S-H Insertion
Max TON: 64
ee: 32
PDB: 5T88
Notes: Mutagenesis of the ArM by error-prone PCR

Metal: Rh
Ligand type: OAc
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Si-H Insertion
Max TON: 35
ee: 64
PDB: 5T88
Notes: Mutagenesis of the ArM by error-prone PCR

Helichrome: Synthesis and Enzymatic Activity of a Designed Hemeprotein

Kaiser, E. T.; Sasaki, T.

J. Am. Chem. Soc., 1989, 10.1021/ja00183a065


Metal: Fe
Ligand type: Porphyrin
Host protein: Artificial construct
Anchoring strategy: Covalent
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: Only 60 amino acids

Hybrid Ruthenium ROMP Catalysts Based on an Engineered Variant of β-Barrel Protein FhuA ΔCVFtev: Effect of Spacer Length

Okuda, J.

Chem. - Asian J., 2015, 10.1002/asia.201403005


Metal: Ru
Ligand type: Carbene
Host protein: FhuA ΔCVFtev
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Olefin metathesis
Max TON: 555
ee: ---
PDB: ---
Notes: ROMP; cis/trans = 58/42

Lipase Active Site Covalent Anchoring of Rh(NHC) Catalysts: Towards Chemoselective Artificial Metalloenzymes

Klein Gebbink, R. J. M.

Chem. Commun., 2015, 10.1039/c4cc09700a


Metal: Rh
Ligand type: Carbene
Host protein: Cutinase
Anchoring strategy: Covalent
Optimization: ---
Reaction: Hydrogenation
Max TON: 20
ee: rac.
PDB: 1CEX
Notes: ---

Metal: Rh
Ligand type: Carbene
Anchoring strategy: Covalent
Optimization: ---
Reaction: Hydrogenation
Max TON: 20
ee: rac.
PDB: 4K6G
Notes: ---

Manganese Terpyridine Artificial Metalloenzymes for Benzylic Oxygenation and Olefin Epoxidation

Lewis, J. C.

Tetrahedron, 2014, 10.1016/j.tet.2014.03.008


Metal: Mn
Ligand type: Poly-pyridine
Host protein: Nitrobindin (Nb)
Anchoring strategy: Covalent
Optimization: Chemical
Max TON: 19.2
ee: ---
PDB: 3EMM
Notes: ---

Metal: Mn
Ligand type: Poly-pyridine
Host protein: Nitrobindin (Nb)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Epoxidation
Max TON: 19.8
ee: ---
PDB: 3EMM
Notes: ---