FMO DATABASE

FMODB ID: Z9G4N

Calculation Name: 4TSX-A-Xray547

Preferred Name:

Target Type:

Ligand Name: (2s)-tert-butoxy[4-(3,4-dihydro-2h-chromen-6-yl)-2-methylquinolin-3-yl]ethanoic acid | s-dimethylarsinoyl-cysteine

Ligand 3-letter code: LF0 | CAF

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4TSX

Chain ID: A

ChEMBL ID:

UniProt ID: F2WR39

Base Structure: X-ray

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1431622.330321
FMO2-HF: Nuclear repulsion	1372259.931002
FMO2-HF: Total energy	-59362.399319
FMO2-MP2: Total energy	-59535.650329

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:55:ASP)

Summations of interaction energy for fragment #1(A:55:ASP)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-18.756	-17.202	-0.012	-0.658	-0.882	0.002

Interaction energy analysis for fragmet #1(A:55:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.076 / q_NPA : -0.049

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	57	SER	0	0.045	0.033	3.879	-5.918	-4.668	-0.008	-0.635	-0.606	0.002
26	A	80	ALA	0	-0.013	0.006	4.641	0.821	0.868	-0.001	-0.007	-0.039	0.000
88	A	142	PRO	0	0.024	0.025	5.131	-0.321	-0.282	-0.001	-0.001	-0.036	0.000
90	A	144	ASN	0	0.016	0.016	4.608	-1.697	-1.594	-0.001	-0.014	-0.088	0.000
91	A	145	PRO	0	0.028	0.031	5.276	1.107	1.222	-0.001	-0.001	-0.113	0.000
4	A	58	PRO	0	0.095	0.044	6.495	1.027	1.027	0.000	0.000	0.000	0.000
5	A	59	GLY	0	0.060	0.046	7.902	0.844	0.844	0.000	0.000	0.000	0.000
6	A	60	ILE	0	-0.043	-0.023	7.616	0.661	0.661	0.000	0.000	0.000	0.000
7	A	61	TRP	0	-0.001	-0.007	10.420	-0.305	-0.305	0.000	0.000	0.000	0.000
8	A	62	GLN	0	-0.030	-0.014	12.960	0.518	0.518	0.000	0.000	0.000	0.000
9	A	63	LEU	0	-0.013	-0.018	14.912	-0.265	-0.265	0.000	0.000	0.000	0.000
10	A	64	ASP	-1	-0.754	-0.845	18.378	0.867	0.867	0.000	0.000	0.000	0.000
11	A	65	CYS	0	-0.001	0.009	21.285	-0.123	-0.123	0.000	0.000	0.000	0.000
12	A	66	THR	0	-0.010	-0.003	23.664	0.060	0.060	0.000	0.000	0.000	0.000
13	A	67	HIS	0	-0.025	-0.014	26.045	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	68	LEU	0	-0.014	-0.023	29.119	0.033	0.033	0.000	0.000	0.000	0.000
15	A	69	GLU	-1	-0.787	-0.865	31.531	0.045	0.045	0.000	0.000	0.000	0.000
16	A	70	GLY	0	0.005	0.013	35.023	-0.018	-0.018	0.000	0.000	0.000	0.000
17	A	71	LYS	1	0.893	0.948	33.065	-0.070	-0.070	0.000	0.000	0.000	0.000
18	A	72	VAL	0	0.052	0.018	28.523	0.034	0.034	0.000	0.000	0.000	0.000
19	A	73	ILE	0	-0.015	-0.004	24.969	-0.051	-0.051	0.000	0.000	0.000	0.000
20	A	74	LEU	0	0.036	0.019	23.068	0.065	0.065	0.000	0.000	0.000	0.000
21	A	75	VAL	0	-0.019	-0.023	18.880	-0.082	-0.082	0.000	0.000	0.000	0.000
22	A	76	ALA	0	0.012	0.009	17.280	0.099	0.099	0.000	0.000	0.000	0.000
23	A	77	VAL	0	-0.006	-0.015	12.070	-0.108	-0.108	0.000	0.000	0.000	0.000
24	A	78	HIS	0	0.066	0.055	8.502	0.255	0.255	0.000	0.000	0.000	0.000
25	A	79	VAL	0	-0.026	-0.024	7.489	-0.401	-0.401	0.000	0.000	0.000	0.000
27	A	81	SER	0	0.045	0.001	5.372	-1.400	-1.400	0.000	0.000	0.000	0.000
28	A	82	GLY	0	0.007	-0.003	8.141	0.720	0.720	0.000	0.000	0.000	0.000
29	A	83	TYR	0	-0.087	-0.054	10.856	0.385	0.385	0.000	0.000	0.000	0.000
30	A	84	ILE	0	-0.025	-0.016	13.444	0.115	0.115	0.000	0.000	0.000	0.000
31	A	85	GLU	-1	-0.728	-0.816	16.439	-0.972	-0.972	0.000	0.000	0.000	0.000
32	A	86	ALA	0	0.006	-0.005	19.519	0.109	0.109	0.000	0.000	0.000	0.000
33	A	87	GLU	-1	-0.880	-0.927	22.690	-0.331	-0.331	0.000	0.000	0.000	0.000
34	A	88	VAL	0	-0.050	-0.015	26.287	0.051	0.051	0.000	0.000	0.000	0.000
35	A	89	ILE	0	-0.006	0.008	27.973	-0.025	-0.025	0.000	0.000	0.000	0.000
36	A	90	PRO	0	-0.024	-0.008	30.764	0.028	0.028	0.000	0.000	0.000	0.000
37	A	91	ALA	0	0.025	-0.003	33.314	0.020	0.020	0.000	0.000	0.000	0.000
38	A	92	GLU	-1	-0.832	-0.903	28.113	0.265	0.265	0.000	0.000	0.000	0.000
39	A	93	THR	0	-0.001	-0.001	30.512	0.005	0.005	0.000	0.000	0.000	0.000
40	A	94	GLY	0	0.051	0.025	29.185	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	95	GLN	0	0.010	-0.014	29.378	-0.026	-0.026	0.000	0.000	0.000	0.000
42	A	96	GLU	-1	-0.870	-0.937	29.362	-0.117	-0.117	0.000	0.000	0.000	0.000
43	A	97	THR	0	-0.034	-0.019	24.328	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	98	ALA	0	0.002	-0.005	25.128	-0.043	-0.043	0.000	0.000	0.000	0.000
45	A	99	TYR	0	0.020	0.008	26.474	-0.061	-0.061	0.000	0.000	0.000	0.000
46	A	100	PHE	0	-0.013	-0.010	20.087	-0.053	-0.053	0.000	0.000	0.000	0.000
47	A	101	LEU	0	0.008	-0.003	20.287	-0.075	-0.075	0.000	0.000	0.000	0.000
48	A	102	LEU	0	0.006	0.005	22.291	-0.086	-0.086	0.000	0.000	0.000	0.000
49	A	103	LYS	1	0.835	0.922	24.261	0.238	0.238	0.000	0.000	0.000	0.000
50	A	104	LEU	0	-0.048	-0.006	16.944	-0.057	-0.057	0.000	0.000	0.000	0.000
51	A	105	ALA	0	0.036	-0.004	19.373	-0.144	-0.144	0.000	0.000	0.000	0.000
52	A	106	GLY	0	-0.028	0.002	20.432	-0.060	-0.060	0.000	0.000	0.000	0.000
53	A	107	ARG	1	0.810	0.906	19.145	0.782	0.782	0.000	0.000	0.000	0.000
54	A	108	TRP	0	-0.007	-0.025	15.054	-0.232	-0.232	0.000	0.000	0.000	0.000
55	A	109	PRO	0	0.067	0.042	13.194	0.222	0.222	0.000	0.000	0.000	0.000
56	A	110	VAL	0	-0.066	-0.030	14.076	-0.210	-0.210	0.000	0.000	0.000	0.000
57	A	111	LYS	1	0.916	0.970	10.449	1.898	1.898	0.000	0.000	0.000	0.000
58	A	112	THR	0	-0.106	-0.083	12.437	0.043	0.043	0.000	0.000	0.000	0.000
59	A	113	VAL	0	0.029	0.017	14.181	-0.120	-0.120	0.000	0.000	0.000	0.000
60	A	114	HIS	1	0.841	0.918	13.518	-1.379	-1.379	0.000	0.000	0.000	0.000
61	A	115	THR	0	-0.004	-0.016	15.557	-0.158	-0.158	0.000	0.000	0.000	0.000
62	A	116	ASP	-1	-0.837	-0.925	16.489	1.633	1.633	0.000	0.000	0.000	0.000
63	A	117	ASN	0	-0.001	0.030	19.084	0.013	0.013	0.000	0.000	0.000	0.000
64	A	118	GLY	0	0.057	0.018	21.817	-0.080	-0.080	0.000	0.000	0.000	0.000
65	A	119	SER	0	-0.052	-0.047	22.541	-0.089	-0.089	0.000	0.000	0.000	0.000
66	A	120	ASN	0	0.026	0.027	22.600	-0.091	-0.091	0.000	0.000	0.000	0.000
67	A	121	PHE	0	-0.002	-0.007	19.038	-0.080	-0.080	0.000	0.000	0.000	0.000
68	A	122	THR	0	-0.049	-0.039	24.857	-0.038	-0.038	0.000	0.000	0.000	0.000
69	A	123	SER	0	0.026	0.016	27.840	-0.040	-0.040	0.000	0.000	0.000	0.000
70	A	124	THR	0	0.028	-0.006	29.451	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	125	THR	0	0.033	0.023	30.804	-0.031	-0.031	0.000	0.000	0.000	0.000
72	A	126	VAL	0	0.031	0.028	25.076	-0.036	-0.036	0.000	0.000	0.000	0.000
73	A	127	LYS	1	0.882	0.948	26.432	-0.223	-0.223	0.000	0.000	0.000	0.000
74	A	128	ALA	0	-0.001	0.005	27.436	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	129	ALA	0	0.029	0.012	26.160	-0.038	-0.038	0.000	0.000	0.000	0.000
76	A	130	CYS	0	-0.064	-0.034	23.081	-0.047	-0.047	0.000	0.000	0.000	0.000
77	A	131	TRP	0	-0.030	-0.018	23.891	-0.062	-0.062	0.000	0.000	0.000	0.000
78	A	132	TRP	0	-0.025	-0.010	26.175	-0.048	-0.048	0.000	0.000	0.000	0.000
79	A	133	ALA	0	0.009	0.006	22.638	-0.041	-0.041	0.000	0.000	0.000	0.000
80	A	134	GLY	0	-0.004	0.013	21.918	-0.093	-0.093	0.000	0.000	0.000	0.000
81	A	135	ILE	0	-0.051	-0.008	18.321	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	136	LYS	1	0.913	0.948	17.948	0.402	0.402	0.000	0.000	0.000	0.000
83	A	137	GLN	0	0.002	-0.002	18.049	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	138	GLU	-1	-0.863	-0.916	11.542	0.994	0.994	0.000	0.000	0.000	0.000
85	A	139	PHE	0	-0.015	-0.031	14.307	0.035	0.035	0.000	0.000	0.000	0.000
86	A	140	GLY	0	-0.009	0.001	12.705	0.008	0.008	0.000	0.000	0.000	0.000
87	A	141	ILE	0	0.002	0.005	8.981	0.551	0.551	0.000	0.000	0.000	0.000
89	A	143	TYR	0	0.016	-0.019	5.856	0.422	0.422	0.000	0.000	0.000	0.000
92	A	146	GLN	0	0.000	-0.022	5.970	-4.172	-4.172	0.000	0.000	0.000	0.000
93	A	147	SER	0	-0.016	-0.001	8.750	-0.172	-0.172	0.000	0.000	0.000	0.000
94	A	148	GLN	0	-0.094	-0.058	10.547	-0.940	-0.940	0.000	0.000	0.000	0.000
95	A	149	GLY	0	0.045	0.029	10.472	0.250	0.250	0.000	0.000	0.000	0.000
96	A	150	VAL	0	0.049	0.006	8.331	-0.518	-0.518	0.000	0.000	0.000	0.000
97	A	151	ILE	0	-0.025	-0.010	8.522	-0.498	-0.498	0.000	0.000	0.000	0.000
98	A	152	GLU	-1	-0.699	-0.820	12.404	0.589	0.589	0.000	0.000	0.000	0.000
99	A	153	SER	0	-0.115	-0.089	13.592	0.398	0.398	0.000	0.000	0.000	0.000
100	A	154	MET	0	0.021	0.007	12.336	-0.124	-0.124	0.000	0.000	0.000	0.000
101	A	155	ASN	0	0.007	-0.004	16.545	-0.265	-0.265	0.000	0.000	0.000	0.000
102	A	156	LYS	0	-0.011	0.006	17.652	-0.088	-0.088	0.000	0.000	0.000	0.000
103	A	157	GLU	-1	-0.867	-0.925	17.680	0.144	0.144	0.000	0.000	0.000	0.000
104	A	158	LEU	0	0.018	0.015	20.222	-0.086	-0.086	0.000	0.000	0.000	0.000
105	A	159	LYS	1	0.933	0.955	21.872	-0.412	-0.412	0.000	0.000	0.000	0.000
106	A	160	LYS	1	0.856	0.934	21.181	-0.420	-0.420	0.000	0.000	0.000	0.000
107	A	161	ILE	0	-0.021	-0.007	20.968	-0.041	-0.041	0.000	0.000	0.000	0.000
108	A	162	ILE	0	0.012	0.001	25.176	-0.035	-0.035	0.000	0.000	0.000	0.000
109	A	163	GLY	0	-0.018	-0.011	27.692	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	164	GLN	0	-0.071	-0.041	26.120	-0.022	-0.022	0.000	0.000	0.000	0.000
111	A	165	VAL	0	-0.001	-0.004	28.589	-0.024	-0.024	0.000	0.000	0.000	0.000
112	A	166	ARG	1	0.714	0.824	31.184	-0.042	-0.042	0.000	0.000	0.000	0.000
113	A	167	ASP	-1	-0.869	-0.937	33.188	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	168	GLN	0	-0.059	-0.012	32.546	-0.036	-0.036	0.000	0.000	0.000	0.000
115	A	169	ALA	0	-0.008	-0.012	33.986	-0.027	-0.027	0.000	0.000	0.000	0.000
116	A	170	GLU	-1	-0.896	-0.932	35.920	-0.039	-0.039	0.000	0.000	0.000	0.000
117	A	171	THR	0	-0.006	-0.006	35.791	0.014	0.014	0.000	0.000	0.000	0.000
118	A	172	LEU	0	0.050	0.030	29.964	-0.021	-0.021	0.000	0.000	0.000	0.000
119	A	173	LYS	1	0.968	0.969	30.481	0.129	0.129	0.000	0.000	0.000	0.000
120	A	174	THR	0	-0.017	-0.005	30.009	-0.040	-0.040	0.000	0.000	0.000	0.000
121	A	175	ALA	0	0.075	0.026	29.835	-0.027	-0.027	0.000	0.000	0.000	0.000
122	A	176	VAL	0	-0.010	-0.005	25.321	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	177	GLN	0	0.020	-0.001	25.087	-0.053	-0.053	0.000	0.000	0.000	0.000
124	A	178	MET	0	-0.023	0.001	25.463	-0.050	-0.050	0.000	0.000	0.000	0.000
125	A	179	ALA	0	0.028	0.012	24.306	-0.031	-0.031	0.000	0.000	0.000	0.000
126	A	180	VAL	0	0.007	0.005	20.371	-0.023	-0.023	0.000	0.000	0.000	0.000
127	A	181	PHE	0	-0.017	-0.009	20.669	-0.117	-0.117	0.000	0.000	0.000	0.000
128	A	182	ILE	0	-0.001	-0.010	21.653	-0.079	-0.079	0.000	0.000	0.000	0.000
129	A	183	HIS	0	-0.020	0.004	14.944	0.131	0.131	0.000	0.000	0.000	0.000
130	A	184	ASN	0	-0.015	-0.015	16.837	-0.075	-0.075	0.000	0.000	0.000	0.000
131	A	185	LYS	1	0.948	0.983	17.261	0.695	0.695	0.000	0.000	0.000	0.000
132	A	186	LYS	1	0.894	0.957	18.416	0.201	0.201	0.000	0.000	0.000	0.000
133	A	187	ARG	1	0.998	1.000	16.865	0.403	0.403	0.000	0.000	0.000	0.000
134	A	188	LYS	1	0.861	0.925	13.641	0.294	0.294	0.000	0.000	0.000	0.000
135	A	189	GLY	0	0.008	0.008	15.971	-0.109	-0.109	0.000	0.000	0.000	0.000
136	A	190	GLY	0	0.013	0.013	14.019	0.176	0.176	0.000	0.000	0.000	0.000
137	A	191	ILE	0	0.004	-0.018	15.103	-0.161	-0.161	0.000	0.000	0.000	0.000
138	A	192	GLY	0	0.038	0.029	14.068	-0.028	-0.028	0.000	0.000	0.000	0.000
139	A	193	GLY	0	-0.031	0.002	15.088	-0.155	-0.155	0.000	0.000	0.000	0.000
140	A	194	TYR	0	0.038	0.001	11.658	0.043	0.043	0.000	0.000	0.000	0.000
141	A	195	SER	0	-0.054	-0.051	13.244	0.060	0.060	0.000	0.000	0.000	0.000
142	A	196	ALA	0	-0.013	-0.011	12.132	-0.334	-0.334	0.000	0.000	0.000	0.000
143	A	197	GLY	0	-0.001	-0.007	12.812	-0.293	-0.293	0.000	0.000	0.000	0.000
144	A	198	GLU	-1	-0.866	-0.890	14.461	-1.586	-1.586	0.000	0.000	0.000	0.000
145	A	199	ARG	1	0.829	0.896	8.501	2.114	2.114	0.000	0.000	0.000	0.000
146	A	200	ILE	0	-0.017	0.002	9.776	-0.779	-0.779	0.000	0.000	0.000	0.000
147	A	201	VAL	0	-0.007	-0.004	11.398	-0.169	-0.169	0.000	0.000	0.000	0.000
148	A	202	ASP	-1	-0.922	-0.958	10.084	-4.698	-4.698	0.000	0.000	0.000	0.000
149	A	203	ILE	0	-0.037	-0.016	5.562	-0.286	-0.286	0.000	0.000	0.000	0.000
150	A	204	ILE	0	-0.039	-0.026	8.756	-0.218	-0.218	0.000	0.000	0.000	0.000
151	A	205	ALA	0	-0.020	-0.008	11.604	0.213	0.213	0.000	0.000	0.000	0.000
152	A	206	THR	0	0.001	-0.013	9.626	0.246	0.246	0.000	0.000	0.000	0.000
153	A	207	ASP	-1	-0.965	-0.984	9.934	-4.677	-4.677	0.000	0.000	0.000	0.000
154	A	208	ILE	0	-0.119	-0.050	11.566	0.530	0.530	0.000	0.000	0.000	0.000
155	A	209	GLN	-1	-0.970	-0.973	14.491	-2.655	-2.655	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:55:ASP)