FMO DATABASE

FMODB ID: Z96VN

Calculation Name: 7CTO-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7CTO

Chain ID: B

ChEMBL ID:

UniProt ID:

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1313690.406041
FMO2-HF: Nuclear repulsion	1257820.96428
FMO2-HF: Total energy	-55869.44176
FMO2-MP2: Total energy	-56032.739065

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-524.156	-515.946	2.627	-4.631	-6.207	-0.049

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.769 / q_NPA : 1.875

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	5	ASP	-1	-0.703	-0.852	2.768	-112.943	-107.811	0.859	-2.711	-3.281	-0.025
4	A	6	LYS	1	0.846	0.913	1.969	82.052	83.641	1.744	-1.337	-1.996	-0.021
5	A	7	SER	0	-0.081	-0.039	2.977	-0.509	0.761	0.025	-0.551	-0.744	-0.003
6	A	8	GLU	-1	-0.877	-0.929	4.512	-49.694	-49.475	-0.001	-0.032	-0.186	0.000
7	A	9	LEU	0	-0.023	-0.009	7.703	-0.257	-0.257	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.034	-0.056	10.248	2.862	2.862	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.908	-0.943	12.867	-35.265	-35.265	0.000	0.000	0.000	0.000
10	A	12	ILE	0	0.001	-0.003	14.002	-0.749	-0.749	0.000	0.000	0.000	0.000
11	A	13	GLU	-1	-0.773	-0.862	12.647	-45.262	-45.262	0.000	0.000	0.000	0.000
12	A	14	TYR	0	-0.001	0.032	7.736	-4.459	-4.459	0.000	0.000	0.000	0.000
13	A	15	ILE	0	0.016	0.012	11.945	0.674	0.674	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.049	-0.017	15.390	1.151	1.151	0.000	0.000	0.000	0.000
15	A	17	THR	0	-0.017	-0.024	11.592	-0.997	-0.997	0.000	0.000	0.000	0.000
16	A	18	GLN	0	-0.084	-0.044	9.304	-1.594	-1.594	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.943	-0.978	12.699	-35.739	-35.739	0.000	0.000	0.000	0.000
18	A	20	ASN	0	-0.010	0.008	16.032	1.384	1.384	0.000	0.000	0.000	0.000
19	A	21	GLY	0	-0.002	0.013	17.996	1.905	1.905	0.000	0.000	0.000	0.000
20	A	22	THR	0	-0.055	-0.040	19.841	0.176	0.176	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.679	-0.803	20.531	-28.960	-28.960	0.000	0.000	0.000	0.000
22	A	24	PRO	0	-0.017	-0.016	22.206	1.049	1.049	0.000	0.000	0.000	0.000
23	A	25	PRO	0	0.042	0.021	25.590	-0.229	-0.229	0.000	0.000	0.000	0.000
24	A	26	PHE	0	-0.068	-0.036	28.106	0.417	0.417	0.000	0.000	0.000	0.000
25	A	27	MET	0	-0.105	-0.040	25.742	0.511	0.511	0.000	0.000	0.000	0.000
26	A	28	ASN	0	-0.035	-0.036	23.479	-0.168	-0.168	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.897	-0.933	20.446	-29.819	-29.819	0.000	0.000	0.000	0.000
28	A	30	TYR	0	0.003	-0.031	19.070	0.599	0.599	0.000	0.000	0.000	0.000
29	A	31	TRP	0	0.042	0.034	24.538	0.724	0.724	0.000	0.000	0.000	0.000
30	A	32	ASN	0	-0.028	-0.017	27.519	0.595	0.595	0.000	0.000	0.000	0.000
31	A	33	HIS	0	-0.002	0.030	24.791	0.650	0.650	0.000	0.000	0.000	0.000
32	A	34	PHE	0	0.054	0.021	28.376	-0.204	-0.204	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.056	-0.008	26.661	0.690	0.690	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.975	0.984	27.409	19.106	19.106	0.000	0.000	0.000	0.000
35	A	37	GLY	0	0.077	0.041	24.120	-0.248	-0.248	0.000	0.000	0.000	0.000
36	A	38	ILE	0	0.043	0.055	18.419	0.800	0.800	0.000	0.000	0.000	0.000
37	A	39	TYR	0	-0.057	-0.045	19.504	-0.141	-0.141	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.014	0.015	14.142	0.483	0.483	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.697	-0.839	12.147	-47.920	-47.920	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.828	0.928	11.303	45.759	45.759	0.000	0.000	0.000	0.000
41	A	43	ILE	0	-0.082	-0.053	6.672	-6.868	-6.868	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.029	-0.050	7.535	-7.580	-7.580	0.000	0.000	0.000	0.000
43	A	45	GLY	0	-0.019	0.008	9.181	-0.097	-0.097	0.000	0.000	0.000	0.000
44	A	46	LYS	1	0.971	1.005	11.466	37.729	37.729	0.000	0.000	0.000	0.000
45	A	47	PRO	0	0.033	0.004	13.898	-0.227	-0.227	0.000	0.000	0.000	0.000
46	A	48	LEU	0	-0.036	-0.003	16.202	-0.497	-0.497	0.000	0.000	0.000	0.000
47	A	49	PHE	0	0.053	0.037	19.551	1.120	1.120	0.000	0.000	0.000	0.000
48	A	50	THR	0	0.093	0.056	22.499	-0.703	-0.703	0.000	0.000	0.000	0.000
49	A	51	SER	0	-0.060	-0.074	25.094	0.717	0.717	0.000	0.000	0.000	0.000
50	A	52	GLU	-1	-0.974	-0.976	27.054	-19.238	-19.238	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.752	-0.868	28.232	-18.960	-18.960	0.000	0.000	0.000	0.000
52	A	54	LYS	1	0.769	0.913	26.315	22.717	22.717	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.036	-0.037	29.571	0.783	0.783	0.000	0.000	0.000	0.000
54	A	56	HIS	0	-0.035	-0.019	31.467	-0.387	-0.387	0.000	0.000	0.000	0.000
55	A	57	SER	0	0.027	-0.005	30.524	0.537	0.537	0.000	0.000	0.000	0.000
56	A	58	GLU	-1	-0.974	-0.995	33.651	-16.237	-16.237	0.000	0.000	0.000	0.000
57	A	59	CYS	0	-0.064	-0.035	30.714	0.104	0.104	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.019	0.024	30.212	-0.344	-0.344	0.000	0.000	0.000	0.000
59	A	61	TRP	0	-0.023	-0.018	24.507	-0.290	-0.290	0.000	0.000	0.000	0.000
60	A	62	PRO	0	0.005	0.005	22.998	1.001	1.001	0.000	0.000	0.000	0.000
61	A	63	SER	0	-0.017	-0.006	26.093	0.221	0.221	0.000	0.000	0.000	0.000
62	A	64	PHE	0	0.038	0.030	23.915	0.251	0.251	0.000	0.000	0.000	0.000
63	A	65	SER	0	-0.029	-0.032	28.499	0.403	0.403	0.000	0.000	0.000	0.000
64	A	66	LYS	1	0.780	0.877	29.129	19.919	19.919	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.053	0.024	23.713	-0.207	-0.207	0.000	0.000	0.000	0.000
66	A	68	LEU	0	-0.071	-0.013	24.739	-0.197	-0.197	0.000	0.000	0.000	0.000
67	A	69	ASP	-1	-0.895	-0.968	21.835	-25.297	-25.297	0.000	0.000	0.000	0.000
68	A	70	ASP	-1	-0.987	-0.986	20.918	-28.202	-28.202	0.000	0.000	0.000	0.000
69	A	71	ASP	-1	-0.915	-0.966	23.258	-22.451	-22.451	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.931	-0.953	18.550	-28.636	-28.636	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.052	-0.049	18.521	-2.471	-2.471	0.000	0.000	0.000	0.000
72	A	74	ILE	0	0.001	0.024	17.985	1.492	1.492	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.828	-0.912	21.062	-23.587	-23.587	0.000	0.000	0.000	0.000
74	A	76	LEU	0	-0.045	-0.025	20.196	0.508	0.508	0.000	0.000	0.000	0.000
75	A	77	VAL	0	-0.026	-0.020	24.692	0.577	0.577	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.689	-0.795	25.062	-24.109	-24.109	0.000	0.000	0.000	0.000
77	A	79	LYS	1	0.898	0.954	26.905	19.647	19.647	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.013	-0.030	25.921	0.427	0.427	0.000	0.000	0.000	0.000
79	A	81	PHE	0	-0.017	-0.029	24.930	0.749	0.749	0.000	0.000	0.000	0.000
80	A	82	GLY	0	-0.054	-0.028	30.849	0.486	0.486	0.000	0.000	0.000	0.000
81	A	83	MET	0	-0.030	0.002	30.032	0.610	0.610	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.009	-0.014	31.659	-0.104	-0.104	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.830	0.901	25.342	23.308	23.308	0.000	0.000	0.000	0.000
84	A	86	THR	0	0.053	0.028	26.517	0.141	0.141	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.849	-0.911	19.687	-29.381	-29.381	0.000	0.000	0.000	0.000
86	A	88	VAL	0	0.031	0.018	20.732	0.216	0.216	0.000	0.000	0.000	0.000
87	A	89	ARG	1	0.801	0.878	14.577	34.572	34.572	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.006	-0.024	13.730	1.607	1.607	0.000	0.000	0.000	0.000
89	A	91	GLU	-1	-0.926	-0.966	15.340	-33.284	-33.284	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-1.004	-0.993	10.366	-49.602	-49.602	0.000	0.000	0.000	0.000
91	A	93	SER	0	-0.064	-0.050	9.783	-4.415	-4.415	0.000	0.000	0.000	0.000
92	A	94	ASN	0	0.023	0.017	10.395	0.294	0.294	0.000	0.000	0.000	0.000
93	A	95	SER	0	-0.008	0.015	11.342	-0.408	-0.408	0.000	0.000	0.000	0.000
94	A	96	HIS	0	-0.096	-0.056	12.964	2.419	2.419	0.000	0.000	0.000	0.000
95	A	97	LEU	0	0.031	0.001	15.726	-1.352	-1.352	0.000	0.000	0.000	0.000
96	A	98	GLY	0	0.013	0.005	18.354	0.589	0.589	0.000	0.000	0.000	0.000
97	A	99	HIS	0	-0.054	-0.021	21.885	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.020	0.029	25.194	0.075	0.075	0.000	0.000	0.000	0.000
99	A	101	PHE	0	-0.042	-0.015	27.943	0.439	0.439	0.000	0.000	0.000	0.000
100	A	102	ASN	0	0.016	-0.004	31.741	-0.100	-0.100	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.862	-0.904	33.781	-17.949	-17.949	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.055	0.049	34.768	-0.058	-0.058	0.000	0.000	0.000	0.000
103	A	105	PRO	0	0.024	0.017	34.746	0.668	0.668	0.000	0.000	0.000	0.000
104	A	106	LYS	1	0.829	0.892	37.419	15.958	15.958	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.939	-0.960	39.796	-15.237	-15.237	0.000	0.000	0.000	0.000
106	A	108	SER	0	0.020	0.001	34.499	0.197	0.197	0.000	0.000	0.000	0.000
107	A	109	GLY	0	0.052	0.026	34.703	-0.491	-0.491	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.070	-0.025	35.986	0.019	0.019	0.000	0.000	0.000	0.000
109	A	111	LEU	0	-0.022	-0.011	30.877	0.150	0.150	0.000	0.000	0.000	0.000
110	A	112	ARG	1	0.826	0.866	30.196	19.775	19.775	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.005	0.008	24.464	0.271	0.271	0.000	0.000	0.000	0.000
112	A	114	CYS	0	-0.062	-0.034	26.445	0.356	0.356	0.000	0.000	0.000	0.000
113	A	115	ILE	0	0.002	0.008	19.190	-0.347	-0.347	0.000	0.000	0.000	0.000
114	A	116	ASN	0	-0.009	-0.014	19.000	1.060	1.060	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.061	-0.073	19.359	-0.951	-0.951	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.006	-0.004	16.522	-1.243	-1.243	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.010	0.002	14.721	-2.731	-2.731	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.055	-0.021	14.815	-1.403	-1.403	0.000	0.000	0.000	0.000
119	A	121	GLN	0	-0.001	-0.001	14.663	-3.128	-3.128	0.000	0.000	0.000	0.000
120	A	122	PHE	0	0.008	0.000	16.723	0.616	0.616	0.000	0.000	0.000	0.000
121	A	123	ILE	0	-0.011	-0.006	15.425	-1.232	-1.232	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.031	-0.017	19.816	0.961	0.961	0.000	0.000	0.000	0.000
123	A	125	TYR	0	0.068	0.036	22.871	-0.614	-0.614	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.943	-0.984	25.184	-22.652	-22.652	0.000	0.000	0.000	0.000
125	A	127	LYS	1	0.863	0.921	20.401	26.191	26.191	0.000	0.000	0.000	0.000
126	A	128	LEU	0	0.028	0.039	20.261	-1.445	-1.445	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.917	-0.967	20.170	-24.263	-24.263	0.000	0.000	0.000	0.000
128	A	130	GLU	-1	-1.029	-1.011	19.360	-28.064	-28.064	0.000	0.000	0.000	0.000
129	A	131	LEU	0	-0.069	-0.043	14.935	-1.450	-1.450	0.000	0.000	0.000	0.000
130	A	132	GLY	0	-0.037	-0.003	15.633	-1.922	-1.922	0.000	0.000	0.000	0.000
131	A	133	TYR	0	0.002	-0.017	13.932	-0.808	-0.808	0.000	0.000	0.000	0.000
132	A	134	GLY	0	0.041	0.014	19.742	0.986	0.986	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.932	-0.974	20.867	-26.776	-26.776	0.000	0.000	0.000	0.000
134	A	136	LEU	0	0.006	-0.010	20.050	0.604	0.604	0.000	0.000	0.000	0.000
135	A	137	ILE	0	-0.062	-0.022	23.845	0.225	0.225	0.000	0.000	0.000	0.000
136	A	138	SER	0	-0.009	-0.023	26.454	0.623	0.623	0.000	0.000	0.000	0.000
137	A	139	HIS	0	-0.023	0.004	25.724	0.661	0.661	0.000	0.000	0.000	0.000
138	A	140	PHE	0	-0.083	-0.049	25.064	0.210	0.210	0.000	0.000	0.000	0.000
139	A	141	ASP	-2	-1.910	-1.931	30.391	-35.760	-35.760	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)