FMO DATABASE

FMODB ID: 97432

Calculation Name: 3FP9-F-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FP9

Chain ID: F

ChEMBL ID:

UniProt ID: P9WQN4

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	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1249465.432262
FMO2-HF: Nuclear repulsion	1192905.76312
FMO2-HF: Total energy	-56559.669142
FMO2-MP2: Total energy	-56726.691178

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:98:PRO)

Summations of interaction energy for fragment #1(A:98:PRO)

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.
-193.615	-185.205	11.38	-11.171	-8.619	-0.129

Interaction energy analysis for fragmet #1(A:98:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.780 / q_NPA : 0.868

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	100	GLY	0	0.033	0.040	3.862	0.861	2.811	-0.023	-0.951	-0.976	-0.002
48	A	145	GLU	-1	-0.820	-0.924	1.822	-122.519	-116.059	11.403	-10.220	-7.643	-0.127
4	A	101	TYR	0	0.031	-0.001	6.567	0.178	0.178	0.000	0.000	0.000	0.000
5	A	102	GLY	0	0.002	0.010	10.323	0.142	0.142	0.000	0.000	0.000	0.000
6	A	103	VAL	0	0.002	0.031	13.724	-0.006	-0.006	0.000	0.000	0.000	0.000
7	A	104	LEU	0	0.006	0.006	17.496	0.028	0.028	0.000	0.000	0.000	0.000
8	A	105	LEU	0	-0.041	-0.016	19.542	0.739	0.739	0.000	0.000	0.000	0.000
9	A	106	ALA	0	-0.023	-0.034	22.395	0.771	0.771	0.000	0.000	0.000	0.000
10	A	107	THR	0	0.064	0.045	22.632	-0.725	-0.725	0.000	0.000	0.000	0.000
11	A	108	HIS	0	-0.087	-0.057	23.263	1.009	1.009	0.000	0.000	0.000	0.000
12	A	109	ASP	-1	-0.894	-0.950	26.074	-10.726	-10.726	0.000	0.000	0.000	0.000
13	A	110	ASP	-1	-0.824	-0.865	24.689	-12.882	-12.882	0.000	0.000	0.000	0.000
14	A	111	ASP	-1	-0.884	-0.927	22.242	-13.534	-13.534	0.000	0.000	0.000	0.000
15	A	112	THR	0	-0.117	-0.080	20.371	-1.071	-1.071	0.000	0.000	0.000	0.000
16	A	113	VAL	0	0.028	-0.007	17.752	0.589	0.589	0.000	0.000	0.000	0.000
17	A	114	ASP	-1	-0.861	-0.907	19.250	-13.904	-13.904	0.000	0.000	0.000	0.000
18	A	115	VAL	0	0.014	-0.003	14.679	0.010	0.010	0.000	0.000	0.000	0.000
19	A	116	PHE	0	0.012	0.010	17.340	0.053	0.053	0.000	0.000	0.000	0.000
20	A	117	THR	0	0.038	-0.022	11.366	-1.123	-1.123	0.000	0.000	0.000	0.000
21	A	118	SER	0	-0.030	-0.014	11.045	0.216	0.216	0.000	0.000	0.000	0.000
22	A	119	GLY	0	0.001	0.004	13.053	0.709	0.709	0.000	0.000	0.000	0.000
23	A	120	ARG	1	0.907	0.962	15.850	18.079	18.079	0.000	0.000	0.000	0.000
24	A	121	LYS	1	0.935	0.974	17.225	12.186	12.186	0.000	0.000	0.000	0.000
25	A	122	MET	0	-0.086	-0.041	12.918	-0.266	-0.266	0.000	0.000	0.000	0.000
26	A	123	ARG	1	0.858	0.923	18.057	13.323	13.323	0.000	0.000	0.000	0.000
27	A	124	LEU	0	-0.040	-0.013	13.121	-0.297	-0.297	0.000	0.000	0.000	0.000
28	A	125	THR	0	0.061	0.024	15.729	0.601	0.601	0.000	0.000	0.000	0.000
29	A	126	CYS	0	-0.001	0.009	15.456	-1.647	-1.647	0.000	0.000	0.000	0.000
30	A	127	SER	0	-0.007	-0.002	13.474	0.641	0.641	0.000	0.000	0.000	0.000
31	A	128	PRO	0	0.009	-0.012	15.582	0.567	0.567	0.000	0.000	0.000	0.000
32	A	129	ASN	0	-0.085	-0.039	14.110	1.376	1.376	0.000	0.000	0.000	0.000
33	A	130	ILE	0	-0.049	-0.014	15.015	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	131	ASP	-1	-0.834	-0.914	18.419	-12.375	-12.375	0.000	0.000	0.000	0.000
35	A	132	ALA	0	0.030	0.002	21.692	-0.038	-0.038	0.000	0.000	0.000	0.000
36	A	133	ALA	0	-0.001	0.006	22.571	0.192	0.192	0.000	0.000	0.000	0.000
37	A	134	SER	0	-0.102	-0.048	22.893	0.160	0.160	0.000	0.000	0.000	0.000
38	A	135	LEU	0	-0.059	-0.023	19.067	-0.195	-0.195	0.000	0.000	0.000	0.000
39	A	136	LYS	1	0.954	0.975	22.132	12.723	12.723	0.000	0.000	0.000	0.000
40	A	137	LYS	1	0.907	0.952	22.454	10.873	10.873	0.000	0.000	0.000	0.000
41	A	138	GLY	0	0.063	0.009	22.112	0.346	0.346	0.000	0.000	0.000	0.000
42	A	139	GLN	0	-0.018	-0.007	18.584	-0.050	-0.050	0.000	0.000	0.000	0.000
43	A	140	THR	0	-0.017	-0.017	13.824	-0.315	-0.315	0.000	0.000	0.000	0.000
44	A	141	VAL	0	0.013	0.005	13.971	-0.050	-0.050	0.000	0.000	0.000	0.000
45	A	142	ARG	1	0.807	0.882	6.403	34.217	34.217	0.000	0.000	0.000	0.000
46	A	143	LEU	0	-0.002	0.001	8.204	1.264	1.264	0.000	0.000	0.000	0.000
47	A	144	ASN	0	0.041	0.010	5.868	-5.961	-5.961	0.000	0.000	0.000	0.000
49	A	146	ALA	0	-0.055	-0.016	5.748	3.813	3.813	0.000	0.000	0.000	0.000
50	A	147	LEU	0	-0.022	-0.015	8.643	3.350	3.350	0.000	0.000	0.000	0.000
51	A	148	THR	0	-0.017	0.000	10.364	2.393	2.393	0.000	0.000	0.000	0.000
52	A	149	VAL	0	0.047	0.011	10.715	-3.074	-3.074	0.000	0.000	0.000	0.000
53	A	150	VAL	0	-0.033	-0.033	8.521	0.947	0.947	0.000	0.000	0.000	0.000
54	A	151	GLU	-1	-0.825	-0.892	11.135	-25.090	-25.090	0.000	0.000	0.000	0.000
55	A	152	ALA	0	0.012	0.010	13.355	-0.552	-0.552	0.000	0.000	0.000	0.000
56	A	153	GLY	0	0.018	0.019	15.561	0.077	0.077	0.000	0.000	0.000	0.000
57	A	154	THR	0	0.007	0.002	16.297	0.622	0.622	0.000	0.000	0.000	0.000
58	A	155	PHE	0	0.045	0.019	19.197	-0.097	-0.097	0.000	0.000	0.000	0.000
59	A	156	GLU	0	-0.099	-0.071	17.625	-0.371	-0.371	0.000	0.000	0.000	0.000
60	A	157	ALA	0	0.075	0.033	19.534	0.565	0.565	0.000	0.000	0.000	0.000
61	A	158	VAL	0	-0.026	-0.014	18.584	0.368	0.368	0.000	0.000	0.000	0.000
62	A	159	GLY	0	-0.003	-0.010	20.249	-0.644	-0.644	0.000	0.000	0.000	0.000
63	A	160	GLU	-1	-0.914	-0.943	22.143	-10.841	-10.841	0.000	0.000	0.000	0.000
64	A	161	ILE	0	0.024	0.010	25.382	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	162	SER	0	-0.039	-0.018	28.753	0.188	0.188	0.000	0.000	0.000	0.000
66	A	163	THR	0	-0.007	0.005	31.479	-0.031	-0.031	0.000	0.000	0.000	0.000
67	A	164	LEU	0	-0.037	-0.013	34.816	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	165	ARG	1	0.864	0.937	36.115	7.689	7.689	0.000	0.000	0.000	0.000
69	A	166	GLU	-1	-0.893	-0.952	38.108	-7.314	-7.314	0.000	0.000	0.000	0.000
70	A	167	ILE	0	0.017	0.010	36.139	-0.251	-0.251	0.000	0.000	0.000	0.000
71	A	168	LEU	0	-0.022	-0.011	35.434	0.246	0.246	0.000	0.000	0.000	0.000
72	A	169	ALA	0	0.008	-0.009	38.479	-0.028	-0.028	0.000	0.000	0.000	0.000
73	A	170	ASP	-1	-0.834	-0.896	35.620	-8.867	-8.867	0.000	0.000	0.000	0.000
74	A	171	GLY	0	0.005	0.004	37.198	-0.067	-0.067	0.000	0.000	0.000	0.000
75	A	172	HIS	0	0.034	0.012	31.905	-0.384	-0.384	0.000	0.000	0.000	0.000
76	A	173	ARG	1	0.815	0.895	31.262	8.791	8.791	0.000	0.000	0.000	0.000
77	A	174	ALA	0	0.036	0.017	32.577	0.326	0.326	0.000	0.000	0.000	0.000
78	A	175	LEU	0	-0.027	-0.002	33.257	-0.253	-0.253	0.000	0.000	0.000	0.000
79	A	176	VAL	0	0.004	-0.006	30.744	0.127	0.127	0.000	0.000	0.000	0.000
80	A	177	VAL	0	0.039	0.012	34.251	-0.037	-0.037	0.000	0.000	0.000	0.000
81	A	178	GLY	0	0.020	0.017	32.238	-0.135	-0.135	0.000	0.000	0.000	0.000
82	A	179	HIS	1	0.886	0.935	30.355	9.906	9.906	0.000	0.000	0.000	0.000
83	A	180	ALA	0	-0.058	-0.044	33.662	0.167	0.167	0.000	0.000	0.000	0.000
84	A	181	ASP	-1	-0.894	-0.929	36.079	-7.703	-7.703	0.000	0.000	0.000	0.000
85	A	182	GLU	-1	-0.890	-0.943	31.579	-9.314	-9.314	0.000	0.000	0.000	0.000
86	A	183	GLU	-1	-0.896	-0.951	33.889	-8.112	-8.112	0.000	0.000	0.000	0.000
87	A	184	ARG	1	0.832	0.904	26.678	10.560	10.560	0.000	0.000	0.000	0.000
88	A	185	VAL	0	-0.013	-0.001	32.212	0.156	0.156	0.000	0.000	0.000	0.000
89	A	186	VAL	0	-0.046	-0.014	27.848	-0.329	-0.329	0.000	0.000	0.000	0.000
90	A	187	TRP	0	-0.020	-0.017	26.367	0.531	0.531	0.000	0.000	0.000	0.000
91	A	188	LEU	0	-0.005	-0.001	28.246	-0.210	-0.210	0.000	0.000	0.000	0.000
92	A	189	ALA	0	0.013	0.006	25.158	-0.128	-0.128	0.000	0.000	0.000	0.000
93	A	190	ASP	-1	-0.797	-0.897	26.848	-11.301	-11.301	0.000	0.000	0.000	0.000
94	A	191	PRO	0	-0.056	-0.034	25.741	0.362	0.362	0.000	0.000	0.000	0.000
95	A	192	LEU	0	-0.045	-0.012	28.810	0.290	0.290	0.000	0.000	0.000	0.000
96	A	193	ILE	0	-0.068	-0.033	31.197	0.347	0.347	0.000	0.000	0.000	0.000
97	A	194	ALA	0	0.008	0.026	31.775	0.135	0.135	0.000	0.000	0.000	0.000
98	A	195	GLU	-1	-0.937	-0.981	33.713	-8.245	-8.245	0.000	0.000	0.000	0.000
99	A	196	ASP	-1	-0.971	-0.987	34.773	-8.871	-8.871	0.000	0.000	0.000	0.000
100	A	197	LEU	0	0.025	0.024	33.019	0.112	0.112	0.000	0.000	0.000	0.000
101	A	198	PRO	0	-0.106	-0.050	37.637	0.089	0.089	0.000	0.000	0.000	0.000
102	A	199	ASP	-1	-0.782	-0.891	40.210	-7.678	-7.678	0.000	0.000	0.000	0.000
103	A	200	GLY	0	-0.051	-0.025	42.328	0.163	0.163	0.000	0.000	0.000	0.000
104	A	201	LEU	0	-0.015	-0.020	44.529	-0.049	-0.049	0.000	0.000	0.000	0.000
105	A	202	PRO	0	0.056	0.044	41.712	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	203	GLU	-1	-0.837	-0.928	41.697	-7.248	-7.248	0.000	0.000	0.000	0.000
107	A	204	ALA	0	-0.027	0.009	43.677	0.043	0.043	0.000	0.000	0.000	0.000
108	A	205	LEU	0	0.042	0.013	42.756	-0.163	-0.163	0.000	0.000	0.000	0.000
109	A	206	ASN	0	-0.043	-0.024	40.882	-0.142	-0.142	0.000	0.000	0.000	0.000
110	A	207	ASP	-1	-0.836	-0.914	40.278	-7.357	-7.357	0.000	0.000	0.000	0.000
111	A	208	ASP	-1	-0.747	-0.844	37.840	-8.424	-8.424	0.000	0.000	0.000	0.000
112	A	209	THR	0	-0.033	-0.003	36.193	-0.291	-0.291	0.000	0.000	0.000	0.000
113	A	210	ARG	1	0.779	0.870	35.213	7.530	7.530	0.000	0.000	0.000	0.000
114	A	211	PRO	0	-0.013	-0.012	31.600	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	212	ARG	1	0.757	0.844	33.928	8.368	8.368	0.000	0.000	0.000	0.000
116	A	213	LYS	1	0.921	0.963	35.838	7.494	7.494	0.000	0.000	0.000	0.000
117	A	214	LEU	0	0.017	0.013	33.305	0.109	0.109	0.000	0.000	0.000	0.000
118	A	215	ARG	1	0.772	0.857	37.661	7.731	7.731	0.000	0.000	0.000	0.000
119	A	216	PRO	0	0.005	-0.003	39.097	-0.169	-0.169	0.000	0.000	0.000	0.000
120	A	217	GLY	0	0.020	0.015	39.435	0.152	0.152	0.000	0.000	0.000	0.000
121	A	218	ASP	-1	-0.731	-0.826	35.431	-8.457	-8.457	0.000	0.000	0.000	0.000
122	A	219	SER	0	-0.026	-0.011	32.829	-0.097	-0.097	0.000	0.000	0.000	0.000
123	A	220	LEU	0	0.031	0.012	29.977	-0.092	-0.092	0.000	0.000	0.000	0.000
124	A	221	LEU	0	-0.004	0.021	22.937	-0.040	-0.040	0.000	0.000	0.000	0.000
125	A	222	VAL	0	-0.018	-0.028	25.502	-0.083	-0.083	0.000	0.000	0.000	0.000
126	A	223	ASP	-1	-0.783	-0.846	19.280	-15.427	-15.427	0.000	0.000	0.000	0.000
127	A	224	THR	0	-0.033	-0.032	22.763	0.016	0.016	0.000	0.000	0.000	0.000
128	A	225	LYS	1	0.860	0.929	20.106	13.345	13.345	0.000	0.000	0.000	0.000
129	A	226	ALA	0	0.007	-0.005	19.323	0.107	0.107	0.000	0.000	0.000	0.000
130	A	227	GLY	0	-0.013	0.005	21.186	0.222	0.222	0.000	0.000	0.000	0.000
131	A	228	TYR	0	-0.018	-0.013	23.123	0.368	0.368	0.000	0.000	0.000	0.000
132	A	229	ALA	0	0.036	0.028	25.153	-0.135	-0.135	0.000	0.000	0.000	0.000
133	A	230	PHE	0	-0.031	-0.043	20.974	-0.234	-0.234	0.000	0.000	0.000	0.000
134	A	231	GLU	-1	-0.897	-0.952	25.624	-11.593	-11.593	0.000	0.000	0.000	0.000
135	A	232	ARG	1	0.780	0.868	27.859	8.868	8.868	0.000	0.000	0.000	0.000
136	A	233	ILE	0	-0.027	-0.012	27.269	-0.058	-0.058	0.000	0.000	0.000	0.000
137	A	234	PRO	0	0.003	0.001	31.368	0.181	0.181	0.000	0.000	0.000	0.000
138	A	235	LYS	1	0.890	0.943	34.120	8.551	8.551	0.000	0.000	0.000	0.000
139	A	236	ALA	0	0.026	0.027	36.763	0.134	0.134	0.000	0.000	0.000	0.000
140	A	237	GLU	-1	-0.882	-0.938	39.478	-7.162	-7.162	0.000	0.000	0.000	0.000
141	A	238	VAL	0	-0.030	-0.016	42.103	-0.088	-0.088	0.000	0.000	0.000	0.000
142	A	239	GLU	-1	-0.899	-0.965	43.107	-6.705	-6.705	0.000	0.000	0.000	0.000
143	A	240	ASP	-1	-0.927	-0.961	42.909	-6.951	-6.951	0.000	0.000	0.000	0.000
144	A	241	LEU	0	-0.020	-0.017	37.709	-0.071	-0.071	0.000	0.000	0.000	0.000
145	A	242	VAL	0	-0.011	-0.006	41.296	-0.026	-0.026	0.000	0.000	0.000	0.000
146	A	243	LEU	0	-0.074	-0.036	43.867	0.110	0.110	0.000	0.000	0.000	0.000
147	A	244	GLU	-1	-0.987	-0.998	38.630	-8.001	-8.001	0.000	0.000	0.000	0.000
148	A	245	GLU	-1	-1.009	-0.992	40.985	-7.590	-7.590	0.000	0.000	0.000	0.000
149	A	246	LEU	0	-0.110	-0.065	42.064	0.078	0.078	0.000	0.000	0.000	0.000
150	A	247	VAL	-1	-1.007	-0.977	44.039	-6.838	-6.838	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:98:PRO)