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(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val) details

Primary information
ID	antitb_1002,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis strain H37Rv (ATCC 27294)
Cell Line	MIC = 0.16 Î¼M
Inhibition Concentration	Both
Sequence	2015
Cytotoxicity	Vero cells (ATCC CRL-1586), J774.1 macrophage cell line, Caco-2 cell monolayers
In vivo Model	0.12 Î¼M, ecumicin reduced M. tuberculosis viabilities in J774 macrophages by 2 x log10
Lethal Dose	>63 Î¼M for vero cells
Immune Responce	Female BALB/c mice, male CD-1 mice
Mechanism of Action	20 mg/kg causes reductions in M. tuberculosis lung
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	Ecumicin encapsulated in micelles distributes to mouse lung tissue
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1003,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis strain H37Rv (ATCC 27294)
Cell Line	MIC = 0.16 Î¼M
Inhibition Concentration	Both
Sequence	2015
Cytotoxicity	Vero cells (ATCC CRL-1586), J774.1 macrophage cell line, Caco-2 cell monolayers
In vivo Model	0.12 Î¼M, ecumicin reduced M. tuberculosis viabilities in J774 macrophages by 2 x log10
Lethal Dose	>63 Î¼M for vero cells
Immune Responce	Female BALB/c mice, male CD-1 mice
Mechanism of Action	32 mg/kg reductions in M. tuberculosis lung CFU 1.
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	Ecumicin encapsulated in micelles distributes to mouse lung tissue
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1004,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis strain H37Rv (ATCC 27294)
Cell Line	MIC = 0.16 Î¼M
Inhibition Concentration	Both
Sequence	2015
Cytotoxicity	Vero cells (ATCC CRL-1586), J774.1 macrophage cell line, Caco-2 cell monolayers
In vivo Model	0.12 Î¼M, ecumicin reduced M. tuberculosis viabilities in J774 macrophages by 2 x log10
Lethal Dose	>63 Î¼M for vero cells
Immune Responce	Female BALB/c mice, male CD-1 mice
Mechanism of Action	Complete inhibition of M. tuberculosis growth in t
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	Ecumicin encapsulated in micelles distributes to mouse lung tissue
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1005,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis Erdman (ATCC 35801)
Cell Line	MIC = 0.16 Î¼M
Inhibition Concentration	Both
Sequence	2015
Cytotoxicity	J774.1 macrophage cell line
In vivo Model	0.12 Î¼M, ecumicin reduced M. tuberculosis viabilities in J774 macrophages by 2 x log10
Lethal Dose	>63 Î¼M for J774.1 cells
Immune Responce	Female BALB/c mice, male CD-1 mice
Mechanism of Action	20 mg/kg causes reductions in M. tuberculosis lung
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	Ecumicin encapsulated in micelles distributes to mouse lung tissue
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1006,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis Erdman (ATCC 35801)
Cell Line	MIC = 0.16 Î¼M
Inhibition Concentration	Both
Sequence	2015
Cytotoxicity	J774.1 macrophage cell line
In vivo Model	0.12 Î¼M, ecumicin reduced M. tuberculosis viabilities in J774 macrophages by 2 x log10
Lethal Dose	>63 Î¼M for J774.1 cells
Immune Responce	Female BALB/c mice, male CD-1 mice
Mechanism of Action	32 mg/kg reductions in M. tuberculosis lung CFU 1.
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	Ecumicin encapsulated in micelles distributes to mouse lung tissue
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1007,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to isoniazid (INH) (ATCC 35822)
Cell Line	MIC <0.12 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1008,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to rifampin (RMP) (ATCC 35838)
Cell Line	MIC = 0.19 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1009,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to streptomycin (SM) (ATCC 35820),
Cell Line	MIC <0.12 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1010,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to cycloserine (CS) (ATCC 35826)
Cell Line	MIC = <0.12 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1011,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to moxifloxacin (MFX)
Cell Line	MIC = 0.31 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1012,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium tuberculosis H37Rv strains with monoresistance to capreomycin (CAP)
Cell Line	MIC = 0.29 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1013,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium smegmatis
In Vitro/ In vivo	Mycobacterium smegmatis (ATCC 700084)
Cell Line	MIC = 1.7 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1014,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium chelonae
In Vitro/ In vivo	Mycobacterium chelonae (ATCC 35752)
Cell Line	MIC = 0.97 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1015,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium marinum
In Vitro/ In vivo	Mycobacterium marinum (ATCC 927)
Cell Line	MIC = 0.95 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1016,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium abscessus
In Vitro/ In vivo	Mycobacterium abscessus (ATCC 19977)
Cell Line	MIC >63 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1017,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium avium
In Vitro/ In vivo	Mycobacterium avium (ATCC 15769)
Cell Line	MIC = 0.35 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1018,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium kansasii
In Vitro/ In vivo	Mycobacterium kansasii (ATCC 12478)
Cell Line	MIC = <0.24 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1019,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobaterium tuberculosis MDR
Cell Line	MIC = 0.31 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1020,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobaterium tuberculosis XDR
Cell Line	MIC = 0.31â€“0.62 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1021,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Single nucleotide polymorphism (SNP) clusters: X001354 corresponding to the Indo-Oceanic lineage,
Cell Line	MIC = 0.13â€“0.38 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1022,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Single nucleotide polymorphism (SNP) clusters: X004439 and X004244 to the East Asian lineage
Cell Line	MIC = 0.13â€“0.38 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1023,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Single nucleotide polymorphism (SNP) clusters: X005282 and X005319 to the Euro-American lineage
Cell Line	MIC = 0.13â€“0.38 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1024,
Name	25421483
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123.
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Single nucleotide polymorphism (SNP) clusters: X001354 to the East African Indian lineage
Cell Line	MIC = 0.13â€“0.38 Î¼M
Inhibition Concentration	In vitro
Sequence	2015
Cytotoxicity	None
In vivo Model	NA
Lethal Dose	NA
Immune Responce	None
Mechanism of Action	None
Target	NA
Combination Therapy	Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin
Other activities	ClpC1 ATPase complex
PMID	None
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1713,
Name	25409285
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5123
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium Tuberculosis H37Rv resistant to streptomycin
Cell Line	IC90= < 0.20 Î¼g/ml
Inhibition Concentration	Both
Sequence	2014
Cytotoxicity	VERO cell line
In vivo Model	50 % bacteria is killed
Lethal Dose	No cytotoxicity
Immune Responce	NA
Mechanism of Action	NA
Target	NA
Combination Therapy	NA
Other activities	NA
PMID	NA
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1714,
Name	25409285
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5124
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium Tuberculosis H37Rv resistant to rifampicin
Cell Line	IC90= 0.30 Î¼g/ml
Inhibition Concentration	Both
Sequence	2014
Cytotoxicity	VERO cell line
In vivo Model	51 % bacteria is killed
Lethal Dose	No cytotoxicity
Immune Responce	NA
Mechanism of Action	NA
Target	NA
Combination Therapy	NA
Other activities	NA
PMID	NA
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),

Primary information
ID	antitb_1715,
Name	25409285
N-Terminal modification	Ecumicin
C-Terminal Modification	(N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val)
Chemical Modification	Free
Linear/Cyclic	Free
Length	N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe
Chirality	Macrocyclic
Nature	13
Source	L
Species	Natural
Strain	Produced by a genetically distinct Nonomuraea species, strain MJM5125
Inhibition Concentration	Mycobacterium tuberculosis
In Vitro/ In vivo	Mycobacterium Tuberculosis H37Rv resistant to cycloserine
Cell Line	IC90= < 0.20Î¼g/ml
Inhibition Concentration	Both
Sequence	2014
Cytotoxicity	VERO cell line
In vivo Model	52 % bacteria is killed
Lethal Dose	No cytotoxicity
Immune Responce	NA
Mechanism of Action	NA
Target	NA
Combination Therapy	NA
Other activities	NA
PMID	NA
Year of Publication	NA
Tertiary Structure (Technique)	Not Predicted),