Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule

Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule

MarR household proteins regulate the transcription of a number of antibiotic-resistance genes and are broadly present in micro organism and archaea. Lately, a brand new MarR household gene was recognized by genome evaluation of the psychrophilic bacterium Paenisporosarcina sp.
TG-14, which was remoted from sediment-laden basal ice in Antarctica. On this research, the crystal construction of the MarR protein from Paenisporosarcina sp. TG-14 (PaMarR) was decided at 1.6 Å decision. Within the crystal construction, a novel lipid-type compound (palmitic acid) was present in a deep cavity, which was assumed to be an effector-binding web site.
Comparative structural evaluation of homologous MarR household proteins from a mesophile and a hyperthermophile confirmed that the DNA-binding area of PaMarR exhibited comparatively excessive mobility, with a disordered area between the β1 and β2 strands.
As well as, structural comparability with different homologous advanced constructions means that this construction constitutes a conformer reworked by palmitic acid. Biochemical evaluation additionally demonstrated that PaMarR binds to cognate DNA, the place PaMarR is understood to acknowledge two putative binding websites relying on its molar focus, indicating that PaMarR binds to its cognate DNA in a stoichiometric method.
The current research offers structural data on the cold-adaptive MarR protein with an aliphatic compound as its putative effector, extending the scope of MarR household protein analysis.

AlphaFold 2: Why It Works and Its Implications for Understanding the Relationships of Protein Sequence, Construction, and Operate

AlphaFold 2 (AF2) was the star of CASP14, the final biannual construction prediction experiment. Utilizing novel deep studying, AF2 predicted the constructions of many troublesome protein targets at or close to experimental decision. Right here, we current our perspective of why AF2 works and present that it’s a very refined fold recognition algorithm that exploits the completeness of the library of single area PDB constructions.
It has additionally realized native aspect chain packing rearrangements that allow it to refine proteins to excessive decision. The advantages and limitations of its potential to foretell the constructions of many extra proteins at or near atomic element are mentioned.

Forces concerned in freeze-induced egg yolk gelation: Results of assorted bond dissociation reagents on gel properties and protein construction adjustments

Urea, sodium dodecyl sulfate (SDS) and β-mercaptoethanol (2-ME) had been used to observe the roles of hydrogen bonds, hydrophobic interactions and disulfide bonds in frozen egg yolk. Yolk samples had been ready with a denaturant, and the textural traits, turbidity properties, protein patterns and constructions had been analysed.
The outcomes confirmed that SDS or 2-ME addition to egg yolk promoted its turbidity and texture properties, however urea modified the turbidity in another way. SDS-PAGE outcomes confirmed that yolk protein patterns with urea barely diminished the quantity of excessive molecular weight substances, whereas SDS and 2-ME addition elevated the quantity.
ATR-FTIR spectroscopy revealed that the protein secondary constructions modified from ordered constructions to random coils. The feel properties had been correlated with the protein secondary construction, particularly β-sheets and β-turns. Thus, the three bond dissociation reagents induced protein denaturation. Hydrogen bonds had been the vital power affecting frozen egg yolk gelation, adopted by hydrophobic interactions and disulfide bonds.

The First Cytoplasmic Loop within the Core Construction of the ABCC1 (Multidrug Resistance Protein 1; MRP1) Transporter Accommodates A number of Amino Acids Important for Its Expression

ABCC1 (human multidrug resistance protein 1 (hMRP1)) is an ATP-binding cassette transporter which effluxes xeno- and endobiotic natural anions and confers multidrug resistance by means of energetic drug efflux. The 17 transmembrane α-helices of hMRP1 are distributed amongst three membrane spanning domains (MSD0, 1, 2) with MSD1,2 every adopted by a nucleotide binding area to type the 4-domain core construction.
Eight conserved residues within the first cytoplasmic loop (CL4) of MSD1 within the descending α-helix (Gly392, Tyr404, Arg405), the perpendicular coupling helix (Asn412, Arg415, Lys416), and the ascending α-helix (Glu422, Phe434) had been focused for mutagenesis.
Mutants with each alanine and identical cost substitutions of the coupling helix residues had been expressed in HEK cells at wild-type hMRP1 ranges and their transport exercise was solely reasonably compromised. In distinction, mutants of the flanking amino acids (G392I, Y404A, R405A/Ok, E422A/D, and F434Y) had been very poorly expressed though Y404F, E422D, and F434A had been readily expressed and transport competent.
Modeling analyses indicated that Glu422 and Arg615 may type an ion pair that may stabilize transporter expression. Nevertheless, this was not supported by change mutations E422R/R615E which did not enhance hMRP1 ranges. Further constructions accompanied by rigorous biochemical validations are wanted to higher perceive the bonding interactions essential for steady hMRP1 expression.

Construction dictates the mechanism of ligand recognition within the histidine and maltose binding proteins

Two mechanisms, induced match (IF) and conformational choice (CS), have been proposed to elucidate ligand recognition coupled conformational adjustments. The histidine binding protein (HisJ) adopts the CS mechanism, through which a pre-equilibrium is established between the open and the closed states with the ligand binding to the closed state.
Regardless of being structurally just like HisJ, the maltose binding protein (MBP) adopts the IF mechanism, through which the ligand binds the open state and induces a transition to the closed state. To know the molecular determinants of this distinction, we carried out molecular dynamics (MD) simulations of coarse-grained twin construction based mostly fashions.
We discover that intra-protein contacts distinctive to the closed state are ample to advertise the conformational transition in HisJ, indicating a CS-like mechanism. In distinction, further ligand-mimicking contacts are required to “induce” the conformational transition in MBP suggesting an IF-like mechanism.
Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
In settlement with experiments, destabilizing modifications to 2 structural options, the backbone helix (SH) and the balancing interface (BI), current in MBP however absent in HisJ, scale back the necessity for ligand-mimicking contacts indicating that SH and BI act as structural restraints that maintain MBP within the open state.
We introduce an SH like ingredient into HisJ and observe that this will impede the conformational transition rising the significance of ligand-mimicking contacts. Equally, simultaneous mutations to BI and SH in MBP scale back the barrier to conformational transitions considerably and promote a CS-like mechanism.

Recombinant Mouse Macrophage Receptor MARCO/MARCO (N-8His)

CU63-50ug 50ug
EUR 327.6
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Recombinant Mouse Macrophage Receptor MARCO/MARCO (N-8His)

AP76480 1mg
EUR 2369

OPCD00816-10UG - MARCO Recombinant Protein

OPCD00816-10UG 10ug
EUR 119

OPCD00816-50UG - MARCO Recombinant Protein

OPCD00816-50UG 50ug
EUR 299

OPCD00817-10UG - MARCO Recombinant Protein

OPCD00817-10UG 10ug
EUR 129

OPCD00817-50UG - MARCO Recombinant Protein

OPCD00817-50UG 50ug
EUR 309

OPCD00816-200UG - MARCO Recombinant Protein

OPCD00816-200UG 200ug
EUR 589

OPCD00817-200UG - MARCO Recombinant Protein

OPCD00817-200UG 200ug
EUR 619

Mouse MARCO Protein, His Tag

E40MOP1250 20ug
EUR 495

Mouse MARCO Protein, His Tag

MAR-M5245 100ug
EUR 2749.9
Description: Mouse MARCO, His Tag (MAR-M5245) is expressed from human 293 cells (HEK293). It contains AA Gln 70 - Ser 518 (Accession # Q60754-1).

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51188-100ug 100ug
EUR 468.6

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51188-1mg 1mg
EUR 2074.8

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51188-50ug 50ug
EUR 376.2

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPC614Mu01 10ug
EUR 152

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

4-RPC614Mu01
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  • 100 ug
  • 10ug
  • 1 mg
  • 200 ug
  • 500 ug
  • 50ug
  • 5 mg
Description: Recombinant Mouse Macrophage Receptor With Collagenous Structure expressed in: E.coli

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPC614Ra01 10ug
EUR 160

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

4-RPC614Ra01
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  • 100 ug
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  • 5 mg
Description: Recombinant Rat Macrophage Receptor With Collagenous Structure expressed in: E.coli

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51565-100ug 100ug
EUR 492.8

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51565-1mg 1mg
EUR 2184

Recombinant Macrophage Receptor With Collagenous Structure (MARCO)

RPU51565-50ug 50ug
EUR 396

March1 Recombinant Protein (Mouse)

RP149426 100 ug Ask for price

March1 Recombinant Protein (Mouse)

RP149429 100 ug Ask for price

March1 Recombinant Protein (Mouse)

RP149432 100 ug Ask for price

March2 Recombinant Protein (Mouse)

RP149444 100 ug Ask for price

March2 Recombinant Protein (Mouse)

RP149447 100 ug Ask for price

March3 Recombinant Protein (Mouse)

RP149450 100 ug Ask for price

March4 Recombinant Protein (Mouse)

RP149453 100 ug Ask for price

March5 Recombinant Protein (Mouse)

RP149456 100 ug Ask for price

March5 Recombinant Protein (Mouse)

RP149459 100 ug Ask for price

March5 Recombinant Protein (Mouse)

RP149462 100 ug Ask for price

March7 Recombinant Protein (Mouse)

RP149468 100 ug Ask for price

March8 Recombinant Protein (Mouse)

RP149471 100 ug Ask for price

MARCH9 Recombinant Protein (Mouse)

RP149474 100 ug Ask for price

MARCKS Recombinant Protein (Mouse)

RP149477 100 ug Ask for price

March10 Recombinant Protein (Mouse)

RP149435 100 ug Ask for price

March10 Recombinant Protein (Mouse)

RP149438 100 ug Ask for price

March11 Recombinant Protein (Mouse)

RP149441 100 ug Ask for price

MARCKSL1 Recombinant Protein (Mouse)

RP149480 100 ug Ask for price

MARCO Protein Vector (Mouse) (pPM-C-HA)

PV199316 500 ng
EUR 723.6

MARCO Protein Vector (Mouse) (pPB-C-His)

PV199314 500 ng
EUR 723.6

MARCO Protein Vector (Mouse) (pPB-N-His)

PV199315 500 ng
EUR 723.6

MARCO Protein Vector (Mouse) (pPM-C-His)

PV199317 500 ng
EUR 723.6

Mouse Macrophage Receptor With Collagenous Structure (MARCO) Protein

20-abx650074
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Mouse Macrophage receptor MARCO, Marco ELISA KIT

ELI-16328m 96 Tests
EUR 1038

Mouse Macrophage Receptor MARCO (MARCO) ELISA Kit

abx389793-96tests 96 tests
EUR 1093.2

Mouse Macrophage receptor MARCO (MARCO) ELISA Kit

RK13444 96T
EUR 280

Human MARCO Protein, His Tag

MAR-H5243 100ug
EUR 2749.9
Description: Human MARCO, His Tag (MAR-H5243) is expressed from human 293 cells (HEK293). It contains AA Met 79 - Val 520 (Accession # Q9UEW3-1).

Human MARCO Protein Lysate 20ug

IHUMARCOPLLY20UG each
EUR 213
Description: Human MARCO Protein Lysate 20ug

MARS2 Recombinant Protein (Mouse)

RP149516 100 ug Ask for price

Cynomolgus MARCO Protein, His Tag

MAR-C5248 100ug
EUR 2749.9
Description: Cynomolgus MARCO, His Tag (MAR-C5248) is expressed from human 293 cells (HEK293). It contains AA Met 79 - Ile 520 (Accession # A0A2K5X0Z2-1).

MARC1 Recombinant Protein (Rat)

RP210866 100 ug Ask for price

MARC2 Recombinant Protein (Rat)

RP210869 100 ug Ask for price

MARVELD1 Recombinant Protein (Mouse)

RP149519 100 ug Ask for price

MARVELD2 Recombinant Protein (Mouse)

RP149522 100 ug Ask for price

MARVELD2 Recombinant Protein (Mouse)

RP149525 100 ug Ask for price

MARVELD3 Recombinant Protein (Mouse)

RP149528 100 ug Ask for price

MARVELD3 Recombinant Protein (Mouse)

RP149531 100 ug Ask for price

OCOA11954-20UG - MARCO Protein Lysate

OCOA11954-20UG 20ug
EUR 169

Marco ELISA Kit| Mouse Macrophage receptor MARCO ELISA Kit

EF015428 96 Tests
EUR 826.8

MARC1 Recombinant Protein (Human)

RP069942 100 ug Ask for price

MARC2 Recombinant Protein (Human)

RP069945 100 ug Ask for price

Mouse MARCO Antibody

GWB-Q01556 0.25 mg Ask for price

Mouse MARCO Antibody

GWB-D42395 0.025 mg Ask for price

RECOMBINANT MOUSE PROTEIN

RPM-100 APRIL / 16.4kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-101 APRIL / 16.4kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-102 APRIL / 16.4kDa MW / 1x100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-103 APRIL / 16.4kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-104 APRIL / 16.4kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-105 APRIL / 16.4kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-110 #IL-1B / 17.4kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-111 #IL-1B / 17.4kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-112 #IL-1B / 17.4kDa MW / 1x100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-113 #IL-1B / 17.4kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-114 #IL-1B / 17.4kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-115 #IL-1B / 17.4kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-120 #IL-17A / 15.0kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-121 #IL-17A / 15.0kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-122 #IL-17A / 15.0kDa MW / 1x100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-123 #IL-17A / 15.0kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-124 #IL-17A / 15.0kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-125 #IL-17A/15.0kDa MW/10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-130 VEGF-A / 19.3kDa MW / 1x5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-131 VEGF-A / 19.3kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-132 VEGF-A / 19.3kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-133 VEGF-A / 19.3kDa MW / 1x100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-134 VEGF-A / 19.3kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-135 VEGF-A / 19.3kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-136 VEGF-A / 19.3kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-140 #IL-2 / 17.6kDa MW / 1x5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-141 #IL-2 / 17.2kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-142 #IL-2 / 17.6kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-143 #IL-2 / 17.6kDa MW / 1x100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-144 #IL-2 / 17.6kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-145 #IL-2 / 17.6kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-146 #IL-2 / 17.6kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-150 #IL-6 / 21.7kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-151 #IL-6 / 21.7kDa MW / 1x25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-152 #IL-6 / 21.7kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-160 #IL-10 / 18.8kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-161 #IL-10 / 18.8kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-162 #IL-10 / 18.8kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-170 TNF / 17.3kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-171 TNFx / 17.3kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-172 TNFx / 17.3kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-180 IFN / 15.5kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-181 IFN / 15.5kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-182 IFN / 15.5kDa MW / 2X25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-183 IFN / 15.5kDa MW / 100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-184 IFN / 15.5kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-185 IFN / 15.5kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-186 IFN / 15.5kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-190 GM-CSF / 14.1kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-191 GM-CSF / 14.1kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-192 GM-CSF / 14.1kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-193 GM-CSF / 14.1kDa MW / 100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-194 GM-CSF / 14.1kDa MW / 2x100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-195 GM-CSF / 14.1kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-196 GM-CSF / 14.1kDa MW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-200 FGF BASIC / 16.2kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-201 FGF BASIC / 16.2kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-202 FGF BASIC/16.2kDa MW/2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-210 CXCL12 / 11.6kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-211 CXCL12 / 11.6kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-212 CXCL12 / 11.6kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-220 BAFF / 20.6kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-221 BAFF / 20.6kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-222 BAFF / 20.6kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-230 TNFSF11 / 19.8kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-231 TNFSF11 / 19.8kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-232 TNFSF11 / 19.8kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-233 TNFSF11 / 19.8kDa MW / 100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-234 TNFSF11 / 19.8kDa MW / 2x100ug
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-235 TNFSF11 / 19.8kDa MW / 5x100uG
EUR 4997

RECOMBINANT MOUSE PROTEIN

RPM-236 TNFSF11 / 19.8kDaMW / 10x100uG
EUR 9903.14

RECOMBINANT MOUSE PROTEIN

RPM-240 #IL-4 / 13.6kDa MW / 5uG
EUR 195

RECOMBINANT MOUSE PROTEIN

RPM-241 #IL-4 / 13.6kDa MW / 25uG
EUR 374.72

RECOMBINANT MOUSE PROTEIN

RPM-242 #IL-4 / 13.6kDa MW / 2x25uG
EUR 703.9

RECOMBINANT MOUSE PROTEIN

RPM-243 #IL-4 / 13.6kDa MW / 100uG
EUR 1065.33

RECOMBINANT MOUSE PROTEIN

RPM-244 #IL-4 / 13.6kDa MW / 2X100uG
EUR 2043.61

RECOMBINANT MOUSE PROTEIN

RPM-245 #IL-4 / 13.6kDa MW / 5x100uG
EUR 4997
Collectively, our outcomes present that structural restraints current within the protein construction can decide the mechanism of conformational transitions and even easy fashions that accurately seize such structural options can predict their positions. MD simulations of such fashions can thus be used, together with mutational experiments, to manage protein ligand interactions, and modulate ligand binding affinities.

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