FMO DATABASE

FMODB ID: 7N6MK

Calculation Name: 3HPE-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3HPE

Chain ID: A

ChEMBL ID:

UniProt ID: Q1CRX8

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	164
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1637933.548043
FMO2-HF: Nuclear repulsion	1573460.690508
FMO2-HF: Total energy	-64472.857536
FMO2-MP2: Total energy	-64663.816095

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:18:LYS)

Summations of interaction energy for fragment #1(A:18: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.
-290.047	-284.49	27.096	-10.945	-21.705	-0.256

Interaction energy analysis for fragmet #1(A:18:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.628 / q_NPA : 1.854

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	20	TYR	0	-0.027	-0.048	2.130	-34.102	-37.597	4.839	3.643	-4.987	-0.069
4	A	21	THR	0	-0.028	-0.014	4.618	9.622	9.709	-0.001	-0.014	-0.071	0.000
36	A	53	ASP	-1	-0.856	-0.922	2.418	-141.075	-138.475	5.818	-3.649	-4.769	-0.049
37	A	54	ALA	0	0.073	0.027	2.466	11.697	13.112	0.634	-0.792	-1.256	-0.004
38	A	55	ASP	-1	-0.835	-0.931	1.913	-207.092	-203.241	15.773	-9.891	-9.732	-0.132
39	A	56	PRO	0	0.041	0.025	3.211	17.283	18.128	0.036	-0.200	-0.681	-0.002
40	A	57	ASN	0	0.005	0.002	4.797	23.562	23.634	-0.001	-0.001	-0.070	0.000
45	A	62	ASN	0	-0.065	-0.041	4.211	12.482	12.604	-0.001	-0.033	-0.088	0.000
164	A	181	ALA	-1	-0.925	-0.945	4.347	-70.975	-70.915	-0.001	-0.008	-0.051	0.000
5	A	22	ILE	0	-0.011	-0.006	8.378	0.562	0.562	0.000	0.000	0.000	0.000
6	A	23	ASP	-1	-0.811	-0.886	11.237	-32.406	-32.406	0.000	0.000	0.000	0.000
7	A	24	LYS	1	0.827	0.875	13.741	33.884	33.884	0.000	0.000	0.000	0.000
8	A	25	ALA	0	-0.021	0.007	17.105	1.534	1.534	0.000	0.000	0.000	0.000
9	A	26	ASN	0	-0.040	-0.032	16.156	2.397	2.397	0.000	0.000	0.000	0.000
10	A	27	SER	0	-0.038	-0.001	14.494	-1.042	-1.042	0.000	0.000	0.000	0.000
11	A	28	SER	0	-0.019	-0.014	16.832	1.839	1.839	0.000	0.000	0.000	0.000
12	A	29	VAL	0	-0.012	-0.003	18.150	-1.015	-1.015	0.000	0.000	0.000	0.000
13	A	30	TRP	0	-0.001	-0.022	20.648	2.024	2.024	0.000	0.000	0.000	0.000
14	A	31	PHE	0	-0.028	-0.010	23.843	-0.348	-0.348	0.000	0.000	0.000	0.000
15	A	32	GLU	-1	-0.829	-0.903	26.685	-19.880	-19.880	0.000	0.000	0.000	0.000
16	A	33	VAL	0	-0.001	0.008	29.717	-0.134	-0.134	0.000	0.000	0.000	0.000
17	A	34	LYS	1	0.881	0.937	32.836	17.532	17.532	0.000	0.000	0.000	0.000
18	A	35	HIS	0	-0.022	-0.008	36.347	-0.157	-0.157	0.000	0.000	0.000	0.000
19	A	36	PHE	0	-0.005	-0.023	39.216	0.144	0.144	0.000	0.000	0.000	0.000
20	A	37	LYS	1	0.968	1.000	40.348	14.114	14.114	0.000	0.000	0.000	0.000
21	A	38	PHE	0	-0.023	-0.025	39.722	-0.308	-0.308	0.000	0.000	0.000	0.000
22	A	39	ASN	0	0.019	0.031	38.716	-0.292	-0.292	0.000	0.000	0.000	0.000
23	A	40	GLU	-1	-0.783	-0.874	33.370	-17.358	-17.358	0.000	0.000	0.000	0.000
24	A	41	THR	0	-0.068	-0.036	33.850	0.147	0.147	0.000	0.000	0.000	0.000
25	A	42	ARG	1	0.871	0.920	28.880	19.969	19.969	0.000	0.000	0.000	0.000
26	A	43	GLY	0	-0.010	-0.004	29.227	0.665	0.665	0.000	0.000	0.000	0.000
27	A	44	VAL	0	0.022	0.020	24.498	-0.575	-0.575	0.000	0.000	0.000	0.000
28	A	45	PHE	0	-0.016	-0.016	23.114	0.998	0.998	0.000	0.000	0.000	0.000
29	A	46	ASP	-1	-0.801	-0.890	22.949	-22.754	-22.754	0.000	0.000	0.000	0.000
30	A	47	SER	0	-0.037	-0.015	22.124	-0.568	-0.568	0.000	0.000	0.000	0.000
31	A	48	PHE	0	-0.029	-0.013	15.860	0.289	0.289	0.000	0.000	0.000	0.000
32	A	49	ASP	-1	-0.850	-0.913	15.684	-32.427	-32.427	0.000	0.000	0.000	0.000
33	A	50	GLY	0	-0.010	-0.024	12.685	0.970	0.970	0.000	0.000	0.000	0.000
34	A	51	LYS	1	0.857	0.945	8.088	48.650	48.650	0.000	0.000	0.000	0.000
35	A	52	ILE	0	0.026	0.006	5.144	2.306	2.306	0.000	0.000	0.000	0.000
41	A	58	THR	0	-0.029	-0.024	5.088	-6.827	-6.827	0.000	0.000	0.000	0.000
42	A	59	LYS	1	0.835	0.921	6.695	61.599	61.599	0.000	0.000	0.000	0.000
43	A	60	ALA	0	0.035	0.029	5.710	6.118	6.118	0.000	0.000	0.000	0.000
44	A	61	LEU	0	-0.039	-0.022	5.734	-11.116	-11.116	0.000	0.000	0.000	0.000
46	A	63	VAL	0	-0.017	-0.022	6.068	7.394	7.394	0.000	0.000	0.000	0.000
47	A	64	PHE	0	0.053	0.018	7.415	-3.800	-3.800	0.000	0.000	0.000	0.000
48	A	65	GLU	-1	-0.837	-0.916	10.112	-37.516	-37.516	0.000	0.000	0.000	0.000
49	A	66	GLY	0	0.040	0.013	12.268	-1.876	-1.876	0.000	0.000	0.000	0.000
50	A	67	LYS	0	-0.027	-0.012	15.008	1.273	1.273	0.000	0.000	0.000	0.000
51	A	68	ILE	0	0.017	0.027	18.560	-0.614	-0.614	0.000	0.000	0.000	0.000
52	A	69	ASP	-1	-0.784	-0.884	21.463	-23.278	-23.278	0.000	0.000	0.000	0.000
53	A	70	ILE	0	0.002	0.016	24.434	0.343	0.343	0.000	0.000	0.000	0.000
54	A	71	LYS	1	0.880	0.923	26.762	21.887	21.887	0.000	0.000	0.000	0.000
55	A	72	SER	0	-0.060	-0.043	25.402	0.284	0.284	0.000	0.000	0.000	0.000
56	A	73	ILE	0	-0.021	0.013	27.491	-0.361	-0.361	0.000	0.000	0.000	0.000
57	A	74	ASN	0	-0.021	-0.027	28.701	1.205	1.205	0.000	0.000	0.000	0.000
58	A	75	THR	0	-0.006	-0.012	30.345	0.555	0.555	0.000	0.000	0.000	0.000
59	A	76	ARG	1	0.875	0.942	31.798	18.900	18.900	0.000	0.000	0.000	0.000
60	A	77	ASN	0	-0.057	-0.031	34.570	0.673	0.673	0.000	0.000	0.000	0.000
61	A	78	LYS	1	0.985	0.984	37.328	15.163	15.163	0.000	0.000	0.000	0.000
62	A	79	LYS	1	0.986	1.001	38.299	13.706	13.706	0.000	0.000	0.000	0.000
63	A	80	ARG	1	0.950	0.978	36.260	16.643	16.643	0.000	0.000	0.000	0.000
64	A	81	ASP	-1	-0.733	-0.896	33.396	-17.984	-17.984	0.000	0.000	0.000	0.000
65	A	82	ASP	-1	-0.838	-0.904	35.083	-16.239	-16.239	0.000	0.000	0.000	0.000
66	A	83	HIS	0	-0.085	-0.030	37.568	-0.115	-0.115	0.000	0.000	0.000	0.000
67	A	84	LEU	0	0.015	0.003	32.825	-0.073	-0.073	0.000	0.000	0.000	0.000
68	A	85	LYS	1	0.890	0.931	32.559	17.255	17.255	0.000	0.000	0.000	0.000
69	A	86	THR	0	-0.001	0.003	34.450	0.038	0.038	0.000	0.000	0.000	0.000
70	A	87	ALA	0	-0.001	-0.016	36.738	-0.334	-0.334	0.000	0.000	0.000	0.000
71	A	88	GLU	-1	-0.883	-0.931	38.280	-14.548	-14.548	0.000	0.000	0.000	0.000
72	A	89	PHE	0	-0.032	-0.016	34.696	-0.190	-0.190	0.000	0.000	0.000	0.000
73	A	90	PHE	0	0.044	0.005	28.060	-0.283	-0.283	0.000	0.000	0.000	0.000
74	A	91	ASP	-1	-0.857	-0.906	32.497	-16.751	-16.751	0.000	0.000	0.000	0.000
75	A	92	VAL	0	0.027	0.013	30.318	-0.252	-0.252	0.000	0.000	0.000	0.000
76	A	93	VAL	0	-0.021	-0.009	31.906	-0.337	-0.337	0.000	0.000	0.000	0.000
77	A	94	LYS	1	0.827	0.911	33.747	16.353	16.353	0.000	0.000	0.000	0.000
78	A	95	TYR	0	-0.005	0.002	29.194	-0.220	-0.220	0.000	0.000	0.000	0.000
79	A	96	PRO	0	0.035	0.019	27.623	-0.340	-0.340	0.000	0.000	0.000	0.000
80	A	97	LYS	1	0.863	0.921	21.044	25.220	25.220	0.000	0.000	0.000	0.000
81	A	98	GLY	0	0.022	0.025	23.599	0.759	0.759	0.000	0.000	0.000	0.000
82	A	99	SER	0	-0.078	-0.045	19.155	-0.983	-0.983	0.000	0.000	0.000	0.000
83	A	100	PHE	0	0.020	0.016	15.161	1.096	1.096	0.000	0.000	0.000	0.000
84	A	101	LYS	1	0.875	0.930	15.193	31.749	31.749	0.000	0.000	0.000	0.000
85	A	102	MET	0	-0.030	0.014	9.355	1.648	1.648	0.000	0.000	0.000	0.000
86	A	103	THR	0	-0.022	-0.019	13.939	-1.288	-1.288	0.000	0.000	0.000	0.000
87	A	104	LYS	1	0.841	0.919	14.295	32.154	32.154	0.000	0.000	0.000	0.000
88	A	105	TYR	0	0.029	0.003	10.275	0.860	0.860	0.000	0.000	0.000	0.000
89	A	106	GLU	-1	-0.802	-0.898	13.068	-32.073	-32.073	0.000	0.000	0.000	0.000
90	A	107	ASP	-1	-0.916	-0.951	14.015	-36.323	-36.323	0.000	0.000	0.000	0.000
91	A	108	GLY	0	0.026	0.031	14.394	1.866	1.866	0.000	0.000	0.000	0.000
92	A	109	LYS	1	0.842	0.905	15.866	29.291	29.291	0.000	0.000	0.000	0.000
93	A	110	ILE	0	-0.002	-0.010	13.019	-2.112	-2.112	0.000	0.000	0.000	0.000
94	A	111	HIS	0	-0.016	-0.020	15.410	3.010	3.010	0.000	0.000	0.000	0.000
95	A	112	GLY	0	0.024	-0.014	16.304	-2.285	-2.285	0.000	0.000	0.000	0.000
96	A	113	ASP	-1	-0.895	-0.922	18.172	-25.892	-25.892	0.000	0.000	0.000	0.000
97	A	114	LEU	0	-0.027	-0.010	19.935	-0.975	-0.975	0.000	0.000	0.000	0.000
98	A	115	THR	0	-0.014	-0.004	22.058	1.345	1.345	0.000	0.000	0.000	0.000
99	A	116	LEU	0	0.034	0.003	24.078	-0.438	-0.438	0.000	0.000	0.000	0.000
100	A	117	HIS	1	0.832	0.914	26.822	18.517	18.517	0.000	0.000	0.000	0.000
101	A	118	GLY	0	0.034	0.011	28.837	0.577	0.577	0.000	0.000	0.000	0.000
102	A	119	VAL	0	-0.050	-0.003	29.544	0.099	0.099	0.000	0.000	0.000	0.000
103	A	120	THR	0	0.034	-0.007	23.998	-0.312	-0.312	0.000	0.000	0.000	0.000
104	A	121	LYS	1	0.888	0.946	25.233	20.712	20.712	0.000	0.000	0.000	0.000
105	A	122	PRO	0	0.055	0.054	22.671	-0.843	-0.843	0.000	0.000	0.000	0.000
106	A	123	VAL	0	-0.054	-0.037	21.091	1.074	1.074	0.000	0.000	0.000	0.000
107	A	124	VAL	0	0.005	-0.005	19.454	-1.217	-1.217	0.000	0.000	0.000	0.000
108	A	125	LEU	0	-0.053	-0.014	17.367	1.222	1.222	0.000	0.000	0.000	0.000
109	A	126	GLU	-1	-0.821	-0.892	18.216	-31.495	-31.495	0.000	0.000	0.000	0.000
110	A	127	ALA	0	-0.034	-0.028	14.811	0.352	0.352	0.000	0.000	0.000	0.000
111	A	128	LYS	1	0.917	0.959	15.187	32.038	32.038	0.000	0.000	0.000	0.000
112	A	129	ILE	0	0.019	0.007	8.574	-0.205	-0.205	0.000	0.000	0.000	0.000
113	A	130	GLN	0	-0.018	-0.003	11.795	-0.068	-0.068	0.000	0.000	0.000	0.000
114	A	131	ALA	0	0.048	0.020	7.481	-2.706	-2.706	0.000	0.000	0.000	0.000
115	A	132	PRO	0	0.022	0.023	7.901	1.439	1.439	0.000	0.000	0.000	0.000
116	A	133	LEU	0	-0.022	-0.004	9.262	5.101	5.101	0.000	0.000	0.000	0.000
117	A	134	GLN	0	-0.009	-0.005	10.916	-1.517	-1.517	0.000	0.000	0.000	0.000
118	A	135	ASN	0	0.018	0.006	13.371	4.035	4.035	0.000	0.000	0.000	0.000
119	A	136	PRO	0	0.041	0.013	15.194	0.572	0.572	0.000	0.000	0.000	0.000
120	A	137	MET	0	0.015	0.015	18.691	1.087	1.087	0.000	0.000	0.000	0.000
121	A	138	ASN	0	0.005	-0.018	14.853	-1.244	-1.244	0.000	0.000	0.000	0.000
122	A	139	LYS	1	0.885	0.939	15.649	28.633	28.633	0.000	0.000	0.000	0.000
123	A	140	LYS	1	0.964	0.997	10.634	43.226	43.226	0.000	0.000	0.000	0.000
124	A	141	GLU	-1	-0.831	-0.906	5.882	-82.103	-82.103	0.000	0.000	0.000	0.000
125	A	142	PHE	0	-0.033	-0.021	7.836	-1.025	-1.025	0.000	0.000	0.000	0.000
126	A	143	MET	0	-0.004	0.014	6.204	-3.513	-3.513	0.000	0.000	0.000	0.000
127	A	144	VAL	0	0.006	-0.001	8.969	2.727	2.727	0.000	0.000	0.000	0.000
128	A	145	LEU	0	-0.020	0.002	9.723	-1.097	-1.097	0.000	0.000	0.000	0.000
129	A	146	GLN	0	0.005	-0.003	12.356	3.134	3.134	0.000	0.000	0.000	0.000
130	A	147	ALA	0	0.025	0.007	15.576	-0.966	-0.966	0.000	0.000	0.000	0.000
131	A	148	GLU	-1	-0.881	-0.935	17.496	-25.238	-25.238	0.000	0.000	0.000	0.000
132	A	149	GLY	0	0.060	0.023	21.245	-0.653	-0.653	0.000	0.000	0.000	0.000
133	A	150	LYS	1	0.841	0.914	23.474	20.669	20.669	0.000	0.000	0.000	0.000
134	A	151	ILE	0	-0.005	0.006	25.476	-0.302	-0.302	0.000	0.000	0.000	0.000
135	A	152	ASN	0	0.050	0.032	28.266	0.641	0.641	0.000	0.000	0.000	0.000
136	A	153	ARG	1	0.780	0.853	31.272	16.479	16.479	0.000	0.000	0.000	0.000
137	A	154	LYS	1	0.770	0.861	32.286	15.810	15.810	0.000	0.000	0.000	0.000
138	A	155	ASP	-1	-0.863	-0.921	31.117	-18.692	-18.692	0.000	0.000	0.000	0.000
139	A	156	PHE	0	-0.014	-0.021	25.887	-0.088	-0.088	0.000	0.000	0.000	0.000
140	A	157	GLY	0	-0.050	-0.034	31.430	0.230	0.230	0.000	0.000	0.000	0.000
141	A	158	ILE	0	0.003	0.010	29.999	0.489	0.489	0.000	0.000	0.000	0.000
142	A	159	GLY	0	0.092	0.046	34.536	0.024	0.024	0.000	0.000	0.000	0.000
143	A	160	LYS	1	0.829	0.917	37.283	16.455	16.455	0.000	0.000	0.000	0.000
144	A	161	THR	0	0.037	0.018	39.837	0.039	0.039	0.000	0.000	0.000	0.000
145	A	162	PHE	0	0.009	0.022	39.955	0.325	0.325	0.000	0.000	0.000	0.000
146	A	163	SER	0	0.040	0.013	40.938	-0.400	-0.400	0.000	0.000	0.000	0.000
147	A	164	ASP	-1	-0.784	-0.878	38.702	-16.011	-16.011	0.000	0.000	0.000	0.000
148	A	165	ALA	0	-0.040	-0.039	40.697	-0.076	-0.076	0.000	0.000	0.000	0.000
149	A	166	VAL	0	-0.064	-0.029	42.448	0.216	0.216	0.000	0.000	0.000	0.000
150	A	167	VAL	0	0.019	0.003	36.471	-0.119	-0.119	0.000	0.000	0.000	0.000
151	A	168	GLY	0	0.028	0.036	36.666	0.085	0.085	0.000	0.000	0.000	0.000
152	A	169	ASP	-1	-0.822	-0.905	35.693	-16.408	-16.408	0.000	0.000	0.000	0.000
153	A	170	GLU	-1	-0.883	-0.921	31.304	-19.980	-19.980	0.000	0.000	0.000	0.000
154	A	171	VAL	0	-0.034	-0.024	28.051	0.299	0.299	0.000	0.000	0.000	0.000
155	A	172	LYS	1	0.864	0.934	25.298	23.052	23.052	0.000	0.000	0.000	0.000
156	A	173	ILE	0	-0.019	-0.023	21.393	0.238	0.238	0.000	0.000	0.000	0.000
157	A	174	GLU	-1	-0.818	-0.910	21.356	-25.116	-25.116	0.000	0.000	0.000	0.000
158	A	175	LEU	0	-0.011	0.003	15.929	0.236	0.236	0.000	0.000	0.000	0.000
159	A	176	LYS	1	0.868	0.926	17.050	26.724	26.724	0.000	0.000	0.000	0.000
160	A	177	LEU	0	0.027	0.011	12.720	1.018	1.018	0.000	0.000	0.000	0.000
161	A	178	GLU	-1	-0.899	-0.946	12.108	-37.467	-37.467	0.000	0.000	0.000	0.000
162	A	179	ALA	0	-0.016	-0.020	7.903	1.095	1.095	0.000	0.000	0.000	0.000
163	A	180	TYR	0	0.008	0.008	7.780	-2.981	-2.981	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:LYS)