FMO DATABASE

FMODB ID: 7NL7K

Calculation Name: 7AMC-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 4-[(2s,4r)-1-acetyl-4-[(4-chlorophenyl)amino]-2-methyl-1,2,3,4-tetrahydroquinolin-6-yl]benzoic acid | glycerol | 1,2-ethanediol

Ligand 3-letter code: 73B | GOL | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7AMC

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-04

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-965264.11061
FMO2-HF: Nuclear repulsion	918546.904988
FMO2-HF: Total energy	-46717.205622
FMO2-MP2: Total energy	-46853.230756

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:15:LEU)

Summations of interaction energy for fragment #1(A:15:LEU)

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.
-83.193	-79.494	5.288	-1.27	-7.717	-0.031

Interaction energy analysis for fragmet #1(A:15:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.865 / q_NPA : 0.937

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	17	LEU	0	0.025	0.024	2.637	-2.403	0.928	1.014	-1.265	-3.080	-0.009
4	A	18	SER	0	0.124	0.056	4.404	0.701	0.793	-0.001	-0.019	-0.073	0.000
61	A	75	GLU	-1	-0.895	-0.929	3.229	-37.036	-36.127	0.081	-0.348	-0.642	-0.002
62	A	76	SER	0	-0.074	-0.059	2.658	-10.415	-8.801	1.032	-1.077	-1.569	-0.013
63	A	77	GLY	0	-0.006	-0.017	2.463	-2.845	-2.314	2.748	-1.196	-2.082	-0.005
64	A	78	GLN	0	-0.076	-0.044	2.835	8.052	5.274	0.414	2.635	-0.271	-0.002
5	A	19	GLU	-1	-0.755	-0.869	8.074	-27.018	-27.018	0.000	0.000	0.000	0.000
6	A	20	ALA	0	0.036	0.037	10.831	0.422	0.422	0.000	0.000	0.000	0.000
7	A	21	LEU	0	0.067	0.026	5.484	0.156	0.156	0.000	0.000	0.000	0.000
8	A	22	LYS	1	0.767	0.864	7.552	28.335	28.335	0.000	0.000	0.000	0.000
9	A	23	ALA	0	0.011	0.011	9.086	0.907	0.907	0.000	0.000	0.000	0.000
10	A	24	CYS	0	-0.019	0.001	9.658	1.318	1.318	0.000	0.000	0.000	0.000
11	A	25	SER	0	0.004	0.001	7.879	0.986	0.986	0.000	0.000	0.000	0.000
12	A	26	ASN	0	-0.040	-0.040	9.932	0.218	0.218	0.000	0.000	0.000	0.000
13	A	27	ILE	0	0.044	0.030	13.291	1.015	1.015	0.000	0.000	0.000	0.000
14	A	28	LEU	0	0.013	0.020	10.647	0.852	0.852	0.000	0.000	0.000	0.000
15	A	29	LYS	1	0.899	0.959	10.165	26.251	26.251	0.000	0.000	0.000	0.000
16	A	30	ASP	-1	-0.810	-0.885	14.676	-13.070	-13.070	0.000	0.000	0.000	0.000
17	A	31	ILE	0	0.033	0.029	16.739	0.700	0.700	0.000	0.000	0.000	0.000
18	A	32	SER	0	0.023	0.001	15.670	0.594	0.594	0.000	0.000	0.000	0.000
19	A	33	SER	0	-0.057	-0.028	18.090	0.467	0.467	0.000	0.000	0.000	0.000
20	A	34	GLN	0	0.031	0.002	19.987	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	35	ARG	1	0.837	0.905	21.993	13.129	13.129	0.000	0.000	0.000	0.000
22	A	36	TYR	0	0.036	0.028	21.799	0.605	0.605	0.000	0.000	0.000	0.000
23	A	37	ARG	1	0.791	0.888	20.712	13.070	13.070	0.000	0.000	0.000	0.000
24	A	38	ASP	-1	-0.862	-0.946	25.408	-10.397	-10.397	0.000	0.000	0.000	0.000
25	A	39	LEU	0	-0.005	-0.002	25.355	0.120	0.120	0.000	0.000	0.000	0.000
26	A	40	ASN	0	0.003	-0.014	21.162	0.126	0.126	0.000	0.000	0.000	0.000
27	A	41	HIS	0	-0.018	-0.006	22.343	-0.594	-0.594	0.000	0.000	0.000	0.000
28	A	42	PHE	0	0.001	-0.002	23.676	-0.193	-0.193	0.000	0.000	0.000	0.000
29	A	43	PHE	0	0.026	0.011	20.483	-0.042	-0.042	0.000	0.000	0.000	0.000
30	A	44	LEU	0	-0.045	-0.018	18.717	-0.855	-0.855	0.000	0.000	0.000	0.000
31	A	45	LYS	1	0.890	0.940	16.825	15.206	15.206	0.000	0.000	0.000	0.000
32	A	46	PRO	0	-0.015	0.004	18.102	0.407	0.407	0.000	0.000	0.000	0.000
33	A	47	VAL	0	0.020	0.014	20.584	0.306	0.306	0.000	0.000	0.000	0.000
34	A	48	ASP	-1	-0.853	-0.917	24.252	-10.548	-10.548	0.000	0.000	0.000	0.000
35	A	49	VAL	0	0.019	-0.016	26.595	0.243	0.243	0.000	0.000	0.000	0.000
36	A	50	VAL	0	-0.020	0.004	29.705	0.356	0.356	0.000	0.000	0.000	0.000
37	A	51	ALA	0	-0.031	-0.020	29.162	0.291	0.291	0.000	0.000	0.000	0.000
38	A	52	LEU	0	-0.038	-0.019	27.444	0.140	0.140	0.000	0.000	0.000	0.000
39	A	53	GLY	0	-0.008	0.008	31.745	0.181	0.181	0.000	0.000	0.000	0.000
40	A	54	LEU	0	-0.059	-0.024	29.252	0.165	0.165	0.000	0.000	0.000	0.000
41	A	55	HIS	0	-0.015	-0.002	33.386	0.155	0.155	0.000	0.000	0.000	0.000
42	A	56	ASP	-1	-0.835	-0.920	34.239	-8.173	-8.173	0.000	0.000	0.000	0.000
43	A	57	TYR	0	-0.012	-0.005	25.153	-0.338	-0.338	0.000	0.000	0.000	0.000
44	A	58	TYR	0	-0.021	-0.036	24.243	-0.363	-0.363	0.000	0.000	0.000	0.000
45	A	59	ASP	-1	-0.913	-0.930	29.089	-8.838	-8.838	0.000	0.000	0.000	0.000
46	A	60	VAL	0	-0.033	-0.003	29.524	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	61	VAL	0	-0.089	-0.050	24.335	-0.260	-0.260	0.000	0.000	0.000	0.000
48	A	62	LYS	1	0.963	0.978	24.144	11.036	11.036	0.000	0.000	0.000	0.000
49	A	63	LYS	1	0.897	0.947	15.133	15.683	15.683	0.000	0.000	0.000	0.000
50	A	64	ALA	0	0.062	0.044	21.317	0.056	0.056	0.000	0.000	0.000	0.000
51	A	65	MET	0	-0.065	-0.035	14.744	-1.032	-1.032	0.000	0.000	0.000	0.000
52	A	66	ASP	-1	-0.694	-0.806	16.630	-15.686	-15.686	0.000	0.000	0.000	0.000
53	A	67	LEU	0	0.081	0.026	15.155	-1.091	-1.091	0.000	0.000	0.000	0.000
54	A	68	SER	0	-0.113	-0.067	13.407	-1.360	-1.360	0.000	0.000	0.000	0.000
55	A	69	THR	0	-0.004	-0.019	12.232	-1.790	-1.790	0.000	0.000	0.000	0.000
56	A	70	ILE	0	0.019	0.006	11.051	-1.724	-1.724	0.000	0.000	0.000	0.000
57	A	71	LYS	1	0.841	0.891	9.233	24.233	24.233	0.000	0.000	0.000	0.000
58	A	72	THR	0	-0.020	-0.021	7.456	-3.102	-3.102	0.000	0.000	0.000	0.000
59	A	73	LYS	1	0.826	0.931	6.881	17.626	17.626	0.000	0.000	0.000	0.000
60	A	74	LEU	0	-0.003	0.018	5.236	-2.627	-2.627	0.000	0.000	0.000	0.000
65	A	79	TYR	0	-0.088	-0.065	5.582	2.761	2.761	0.000	0.000	0.000	0.000
66	A	80	HIS	0	0.015	0.011	5.944	-3.929	-3.929	0.000	0.000	0.000	0.000
67	A	81	THR	0	-0.023	-0.010	8.060	0.210	0.210	0.000	0.000	0.000	0.000
68	A	82	LYS	1	0.829	0.879	10.168	15.857	15.857	0.000	0.000	0.000	0.000
69	A	83	TYR	0	0.002	-0.009	11.826	0.906	0.906	0.000	0.000	0.000	0.000
70	A	84	ASP	-1	-0.769	-0.873	10.341	-19.982	-19.982	0.000	0.000	0.000	0.000
71	A	85	PHE	0	-0.017	-0.022	9.479	0.130	0.130	0.000	0.000	0.000	0.000
72	A	86	ALA	0	-0.008	-0.007	11.346	0.686	0.686	0.000	0.000	0.000	0.000
73	A	87	ASP	-1	-0.910	-0.944	14.961	-14.003	-14.003	0.000	0.000	0.000	0.000
74	A	88	ASP	-1	-0.752	-0.864	13.081	-17.319	-17.319	0.000	0.000	0.000	0.000
75	A	89	VAL	0	0.000	0.003	14.228	0.604	0.604	0.000	0.000	0.000	0.000
76	A	90	ARG	1	0.917	0.963	16.738	14.331	14.331	0.000	0.000	0.000	0.000
77	A	91	LEU	0	-0.059	-0.008	17.893	0.660	0.660	0.000	0.000	0.000	0.000
78	A	92	MET	0	-0.051	-0.007	18.483	0.333	0.333	0.000	0.000	0.000	0.000
79	A	93	PHE	0	0.014	0.006	20.021	0.456	0.456	0.000	0.000	0.000	0.000
80	A	94	ASN	0	0.035	0.000	23.029	0.660	0.660	0.000	0.000	0.000	0.000
81	A	95	ASN	0	-0.042	-0.032	22.041	0.779	0.779	0.000	0.000	0.000	0.000
82	A	96	CYS	0	-0.023	0.014	24.950	0.477	0.477	0.000	0.000	0.000	0.000
83	A	97	TYR	0	-0.006	-0.033	25.415	0.442	0.442	0.000	0.000	0.000	0.000
84	A	98	LYS	1	0.862	0.942	25.396	10.975	10.975	0.000	0.000	0.000	0.000
85	A	99	TYR	0	-0.036	-0.017	29.347	0.123	0.123	0.000	0.000	0.000	0.000
86	A	100	ASN	0	-0.032	-0.028	28.852	0.341	0.341	0.000	0.000	0.000	0.000
87	A	101	GLY	0	0.053	0.045	32.487	0.287	0.287	0.000	0.000	0.000	0.000
88	A	102	GLU	-1	-0.832	-0.928	31.091	-9.320	-9.320	0.000	0.000	0.000	0.000
89	A	103	ASP	-1	-0.862	-0.919	33.544	-7.745	-7.745	0.000	0.000	0.000	0.000
90	A	104	SER	0	-0.031	-0.018	32.906	0.040	0.040	0.000	0.000	0.000	0.000
91	A	105	GLU	-1	-0.880	-0.956	33.351	-8.398	-8.398	0.000	0.000	0.000	0.000
92	A	106	VAL	0	0.010	0.000	27.739	-0.201	-0.201	0.000	0.000	0.000	0.000
93	A	107	ALA	0	0.018	0.013	28.476	-0.396	-0.396	0.000	0.000	0.000	0.000
94	A	108	ARG	1	0.818	0.913	29.628	7.882	7.882	0.000	0.000	0.000	0.000
95	A	109	VAL	0	0.017	0.006	27.652	-0.154	-0.154	0.000	0.000	0.000	0.000
96	A	110	GLY	0	0.030	0.012	25.565	-0.375	-0.375	0.000	0.000	0.000	0.000
97	A	111	LYS	1	0.801	0.901	25.625	9.339	9.339	0.000	0.000	0.000	0.000
98	A	112	GLN	0	-0.018	-0.006	27.378	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	113	LEU	0	-0.010	-0.006	21.270	-0.240	-0.240	0.000	0.000	0.000	0.000
100	A	114	GLN	0	0.023	0.035	22.384	-0.309	-0.309	0.000	0.000	0.000	0.000
101	A	115	ALA	0	0.007	0.008	23.134	-0.273	-0.273	0.000	0.000	0.000	0.000
102	A	116	ILE	0	-0.005	0.005	22.027	-0.161	-0.161	0.000	0.000	0.000	0.000
103	A	117	PHE	0	-0.018	-0.001	15.322	-0.600	-0.600	0.000	0.000	0.000	0.000
104	A	118	ASP	-1	-0.835	-0.944	19.992	-12.821	-12.821	0.000	0.000	0.000	0.000
105	A	119	GLU	-1	-0.903	-0.931	21.893	-11.489	-11.489	0.000	0.000	0.000	0.000
106	A	120	ASN	0	-0.028	-0.040	19.274	-0.061	-0.061	0.000	0.000	0.000	0.000
107	A	121	PHE	0	0.008	-0.003	14.159	-0.467	-0.467	0.000	0.000	0.000	0.000
108	A	122	ALA	0	-0.016	-0.009	18.356	-0.307	-0.307	0.000	0.000	0.000	0.000
109	A	123	LYS	1	0.770	0.882	19.925	12.676	12.676	0.000	0.000	0.000	0.000
110	A	124	VAL	0	-0.054	-0.009	13.706	-0.529	-0.529	0.000	0.000	0.000	0.000
111	A	125	PRO	0	0.002	0.006	14.322	0.539	0.539	0.000	0.000	0.000	0.000
112	A	126	ASP	-1	-0.834	-0.920	15.515	-16.158	-16.158	0.000	0.000	0.000	0.000
113	A	127	ASP	-1	-0.820	-0.916	11.655	-20.711	-20.711	0.000	0.000	0.000	0.000
114	A	128	GLU	-1	-0.989	-0.987	11.351	-20.515	-20.515	0.000	0.000	0.000	0.000
115	A	129	SER	-1	-0.987	-0.999	12.422	-20.513	-20.513	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:15:LEU)