FMO DATABASE

FMODB ID: QMVNY

Calculation Name: 3HPC-X-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3HPC

Chain ID: X

ChEMBL ID:

UniProt ID: B1H267

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	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1407764.00868
FMO2-HF: Nuclear repulsion	1346116.04235
FMO2-HF: Total energy	-61647.96633
FMO2-MP2: Total energy	-61829.578528

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:20:SER)

Summations of interaction energy for fragment #1(A:20:SER)

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.
-69.786	-68.698	-0.006	-0.453	-0.629	0

Interaction energy analysis for fragmet #1(A:20:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / q_NPA : 0.907

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].
3	A	22	SER	0	0.040	0.012	3.871	-3.244	-2.156	-0.006	-0.453	-0.629
4	A	23	VAL	0	-0.030	-0.016	6.364	1.480	1.480	0.000	0.000	0.000
5	A	24	ASP	-1	-0.862	-0.915	9.863	-22.996	-22.996	0.000	0.000	0.000
6	A	25	LEU	0	-0.067	-0.035	11.901	0.952	0.952	0.000	0.000	0.000
7	A	26	ASN	0	-0.030	-0.013	14.870	1.623	1.623	0.000	0.000	0.000
8	A	27	VAL	0	-0.016	-0.020	18.436	-0.168	-0.168	0.000	0.000	0.000
9	A	28	ASP	-1	-0.918	-0.950	20.990	-12.558	-12.558	0.000	0.000	0.000
10	A	29	PRO	0	-0.025	0.000	23.028	0.350	0.350	0.000	0.000	0.000
11	A	30	SER	0	0.019	0.001	25.506	0.204	0.204	0.000	0.000	0.000
12	A	31	LEU	0	-0.002	0.009	28.534	0.507	0.507	0.000	0.000	0.000
13	A	32	GLN	0	-0.019	-0.007	24.770	-0.212	-0.212	0.000	0.000	0.000
14	A	33	ILE	0	0.022	0.008	28.285	0.399	0.399	0.000	0.000	0.000
15	A	34	ASP	-1	-0.838	-0.896	27.656	-11.301	-11.301	0.000	0.000	0.000
16	A	35	ILE	0	-0.033	-0.022	29.458	0.472	0.472	0.000	0.000	0.000
17	A	36	PRO	0	-0.052	0.002	29.846	-0.142	-0.142	0.000	0.000	0.000
18	A	37	ASP	-1	-0.885	-0.923	30.883	-8.883	-8.883	0.000	0.000	0.000
19	A	38	ALA	0	0.047	0.006	33.976	0.054	0.054	0.000	0.000	0.000
20	A	39	LEU	0	-0.015	0.009	36.276	-0.017	-0.017	0.000	0.000	0.000
21	A	40	SER	0	-0.022	-0.018	39.177	0.072	0.072	0.000	0.000	0.000
22	A	41	GLU	-1	-0.828	-0.908	40.971	-6.830	-6.830	0.000	0.000	0.000
23	A	42	ARG	1	0.908	0.933	44.801	6.293	6.293	0.000	0.000	0.000
24	A	43	ASP	-1	-0.733	-0.816	42.477	-7.213	-7.213	0.000	0.000	0.000
25	A	44	LYS	1	0.899	0.964	42.903	6.680	6.680	0.000	0.000	0.000
26	A	45	VAL	0	0.001	0.000	37.038	0.008	0.008	0.000	0.000	0.000
27	A	46	LYS	1	0.871	0.941	40.506	7.055	7.055	0.000	0.000	0.000
28	A	47	PHE	0	-0.013	-0.030	34.769	-0.175	-0.175	0.000	0.000	0.000
29	A	48	THR	0	-0.004	-0.017	35.939	0.278	0.278	0.000	0.000	0.000
30	A	49	VAL	0	-0.030	-0.016	34.474	-0.360	-0.360	0.000	0.000	0.000
31	A	50	HIS	1	0.762	0.848	30.703	10.366	10.366	0.000	0.000	0.000
32	A	51	THR	0	0.043	0.013	32.500	-0.341	-0.341	0.000	0.000	0.000
33	A	52	LYS	1	0.903	0.959	28.098	11.423	11.423	0.000	0.000	0.000
34	A	53	THR	0	-0.019	-0.030	31.431	-0.144	-0.144	0.000	0.000	0.000
35	A	54	THR	0	0.009	-0.002	30.350	0.176	0.176	0.000	0.000	0.000
36	A	55	LEU	0	-0.031	-0.006	32.607	0.193	0.193	0.000	0.000	0.000
37	A	56	PRO	0	-0.004	-0.008	35.235	0.119	0.119	0.000	0.000	0.000
38	A	57	THR	0	-0.070	-0.040	37.605	0.195	0.195	0.000	0.000	0.000
39	A	58	PHE	0	0.040	0.026	35.372	0.060	0.060	0.000	0.000	0.000
40	A	59	GLN	0	-0.023	-0.019	39.946	-0.030	-0.030	0.000	0.000	0.000
41	A	60	SER	0	-0.040	-0.016	40.200	0.092	0.092	0.000	0.000	0.000
42	A	61	PRO	0	0.026	0.002	35.332	-0.102	-0.102	0.000	0.000	0.000
43	A	62	GLU	-1	-0.858	-0.921	33.063	-10.301	-10.301	0.000	0.000	0.000
44	A	63	PHE	0	-0.044	-0.002	35.926	0.252	0.252	0.000	0.000	0.000
45	A	64	SER	0	0.001	-0.022	36.304	-0.421	-0.421	0.000	0.000	0.000
46	A	65	VAL	0	0.006	0.036	38.085	0.208	0.208	0.000	0.000	0.000
47	A	66	THR	0	-0.012	0.005	39.194	-0.211	-0.211	0.000	0.000	0.000
48	A	67	ARG	1	0.760	0.871	38.940	7.772	7.772	0.000	0.000	0.000
49	A	68	GLN	0	-0.008	-0.006	40.463	-0.078	-0.078	0.000	0.000	0.000
50	A	69	HIS	0	0.026	0.015	38.663	-0.248	-0.248	0.000	0.000	0.000
51	A	70	GLU	-1	-0.816	-0.930	40.663	-7.398	-7.398	0.000	0.000	0.000
52	A	71	ASP	-1	-0.773	-0.869	41.420	-7.354	-7.354	0.000	0.000	0.000
53	A	72	PHE	0	-0.033	-0.040	34.754	-0.123	-0.123	0.000	0.000	0.000
54	A	73	VAL	0	-0.071	-0.018	39.421	-0.131	-0.131	0.000	0.000	0.000
55	A	74	TRP	0	0.075	0.044	41.581	-0.077	-0.077	0.000	0.000	0.000
56	A	75	LEU	0	-0.005	0.003	37.224	0.003	0.003	0.000	0.000	0.000
57	A	76	HIS	0	-0.043	-0.036	36.800	0.011	0.011	0.000	0.000	0.000
58	A	77	ASP	-1	-0.845	-0.925	39.741	-7.363	-7.363	0.000	0.000	0.000
59	A	78	THR	0	0.010	0.012	42.923	0.057	0.057	0.000	0.000	0.000
60	A	79	LEU	0	-0.040	-0.009	37.494	-0.018	-0.018	0.000	0.000	0.000
61	A	80	THR	0	-0.093	-0.062	40.050	-0.028	-0.028	0.000	0.000	0.000
62	A	81	GLU	-1	-0.955	-0.972	42.233	-6.652	-6.652	0.000	0.000	0.000
63	A	82	THR	0	-0.072	-0.034	43.087	0.184	0.184	0.000	0.000	0.000
64	A	83	THR	0	0.013	-0.008	43.761	-0.123	-0.123	0.000	0.000	0.000
65	A	84	ASP	-1	-0.927	-0.954	44.024	-7.051	-7.051	0.000	0.000	0.000
66	A	85	TYR	0	-0.121	-0.093	39.354	-0.236	-0.236	0.000	0.000	0.000
67	A	86	ALA	0	0.028	0.019	39.646	-0.193	-0.193	0.000	0.000	0.000
68	A	87	GLY	0	-0.056	-0.020	39.351	-0.037	-0.037	0.000	0.000	0.000
69	A	88	LEU	0	-0.077	-0.043	35.176	-0.319	-0.319	0.000	0.000	0.000
70	A	89	ILE	0	-0.018	-0.007	30.805	0.098	0.098	0.000	0.000	0.000
71	A	90	ILE	0	0.047	0.031	33.666	-0.243	-0.243	0.000	0.000	0.000
72	A	91	PRO	0	-0.048	-0.015	31.168	-0.120	-0.120	0.000	0.000	0.000
73	A	92	PRO	0	-0.005	-0.019	31.517	0.228	0.228	0.000	0.000	0.000
74	A	93	ALA	0	0.061	0.035	33.719	-0.211	-0.211	0.000	0.000	0.000
75	A	94	PRO	0	-0.025	0.005	33.693	-0.139	-0.139	0.000	0.000	0.000
76	A	95	THR	0	-0.018	-0.019	34.458	0.240	0.240	0.000	0.000	0.000
77	A	96	LYS	1	0.886	0.939	36.437	7.123	7.123	0.000	0.000	0.000
78	A	97	PRO	0	-0.060	-0.032	37.715	-0.095	-0.095	0.000	0.000	0.000
79	A	98	ASP	-1	-0.877	-0.927	38.212	-7.497	-7.497	0.000	0.000	0.000
80	A	99	PHE	0	-0.019	-0.024	36.587	-0.252	-0.252	0.000	0.000	0.000
81	A	100	ASP	-1	-0.861	-0.923	40.303	-7.003	-7.003	0.000	0.000	0.000
82	A	101	GLY	0	-0.010	-0.001	40.052	0.096	0.096	0.000	0.000	0.000
83	A	102	PRO	0	-0.001	-0.010	37.544	0.104	0.104	0.000	0.000	0.000
84	A	103	ARG	1	0.843	0.885	40.089	7.379	7.379	0.000	0.000	0.000
85	A	104	GLU	-1	-0.814	-0.909	43.436	-6.600	-6.600	0.000	0.000	0.000
86	A	105	LYS	1	0.800	0.882	37.805	8.255	8.255	0.000	0.000	0.000
87	A	106	MET	0	-0.037	-0.020	39.860	0.126	0.126	0.000	0.000	0.000
88	A	107	GLN	0	-0.105	-0.038	44.506	0.060	0.060	0.000	0.000	0.000
89	A	108	LYS	1	0.860	0.924	46.591	6.748	6.748	0.000	0.000	0.000
90	A	109	LEU	0	-0.026	-0.003	43.020	0.080	0.080	0.000	0.000	0.000
91	A	110	GLY	0	-0.028	-0.015	46.884	0.067	0.067	0.000	0.000	0.000
92	A	111	GLU	-1	-0.901	-0.955	49.342	-5.958	-5.958	0.000	0.000	0.000
93	A	112	GLY	0	0.012	0.013	49.955	0.118	0.118	0.000	0.000	0.000
94	A	113	GLU	-1	-0.947	-0.973	49.657	-6.224	-6.224	0.000	0.000	0.000
95	A	114	GLY	0	-0.042	-0.029	50.780	0.008	0.008	0.000	0.000	0.000
96	A	115	SER	0	-0.054	-0.021	52.430	0.134	0.134	0.000	0.000	0.000
97	A	116	MET	0	-0.044	-0.004	45.248	-0.058	-0.058	0.000	0.000	0.000
98	A	117	THR	0	0.028	0.013	46.382	0.052	0.052	0.000	0.000	0.000
99	A	118	LYS	1	0.987	0.972	47.251	6.032	6.032	0.000	0.000	0.000
100	A	119	GLU	-1	-0.944	-0.959	42.534	-7.216	-7.216	0.000	0.000	0.000
101	A	120	GLU	-1	-0.837	-0.932	41.749	-7.664	-7.664	0.000	0.000	0.000
102	A	121	PHE	0	0.007	-0.003	42.881	-0.159	-0.159	0.000	0.000	0.000
103	A	122	ALA	0	-0.001	-0.009	42.281	-0.110	-0.110	0.000	0.000	0.000
104	A	123	LYS	1	0.817	0.914	37.471	7.883	7.883	0.000	0.000	0.000
105	A	124	MET	0	0.032	0.011	38.608	-0.138	-0.138	0.000	0.000	0.000
106	A	125	LYS	1	0.886	0.933	39.840	7.115	7.115	0.000	0.000	0.000
107	A	126	GLN	0	0.005	0.001	35.111	-0.307	-0.307	0.000	0.000	0.000
108	A	127	GLU	-1	-0.866	-0.920	34.975	-8.675	-8.675	0.000	0.000	0.000
109	A	128	LEU	0	-0.003	-0.004	35.536	-0.186	-0.186	0.000	0.000	0.000
110	A	129	GLU	-1	-0.878	-0.928	37.436	-7.781	-7.781	0.000	0.000	0.000
111	A	130	ALA	0	-0.003	0.000	31.941	-0.186	-0.186	0.000	0.000	0.000
112	A	131	GLU	-1	-0.844	-0.906	32.650	-8.622	-8.622	0.000	0.000	0.000
113	A	132	TYR	0	-0.029	-0.038	34.137	-0.169	-0.169	0.000	0.000	0.000
114	A	133	LEU	0	0.024	0.004	32.298	-0.090	-0.090	0.000	0.000	0.000
115	A	134	ALA	0	-0.034	-0.006	29.831	-0.296	-0.296	0.000	0.000	0.000
116	A	135	VAL	0	-0.027	-0.012	30.617	-0.266	-0.266	0.000	0.000	0.000
117	A	136	PHE	0	-0.001	0.003	33.240	-0.071	-0.071	0.000	0.000	0.000
118	A	137	LYS	1	0.998	0.994	23.561	12.249	12.249	0.000	0.000	0.000
119	A	138	LYS	1	0.941	0.978	28.944	9.995	9.995	0.000	0.000	0.000
120	A	139	THR	0	0.026	0.012	30.004	-0.087	-0.087	0.000	0.000	0.000
121	A	140	VAL	0	0.056	0.037	30.071	0.029	0.029	0.000	0.000	0.000
122	A	141	SER	0	0.002	0.006	25.928	-0.154	-0.154	0.000	0.000	0.000
123	A	142	SER	0	-0.039	-0.023	28.426	-0.021	-0.021	0.000	0.000	0.000
124	A	143	HIS	1	0.820	0.881	30.512	8.938	8.938	0.000	0.000	0.000
125	A	144	GLU	-1	-0.803	-0.886	26.328	-11.617	-11.617	0.000	0.000	0.000
126	A	145	VAL	0	0.022	0.002	25.225	-0.048	-0.048	0.000	0.000	0.000
127	A	146	PHE	0	-0.036	-0.018	27.880	-0.148	-0.148	0.000	0.000	0.000
128	A	147	LEU	0	0.054	0.030	31.202	0.043	0.043	0.000	0.000	0.000
129	A	148	GLN	0	-0.034	-0.017	25.369	-0.299	-0.299	0.000	0.000	0.000
130	A	149	ARG	1	0.926	0.977	25.643	11.357	11.357	0.000	0.000	0.000
131	A	150	LEU	0	0.014	0.024	28.797	-0.033	-0.033	0.000	0.000	0.000
132	A	151	SER	0	-0.054	-0.046	28.574	0.024	0.024	0.000	0.000	0.000
133	A	152	SER	0	-0.046	-0.032	26.024	-0.130	-0.130	0.000	0.000	0.000
134	A	153	HIS	0	0.079	0.057	27.936	-0.138	-0.138	0.000	0.000	0.000
135	A	154	PRO	0	0.008	0.009	29.775	0.264	0.264	0.000	0.000	0.000
136	A	155	VAL	0	-0.052	-0.032	32.342	0.272	0.272	0.000	0.000	0.000
137	A	156	LEU	0	0.032	0.008	33.981	0.146	0.146	0.000	0.000	0.000
138	A	157	SER	0	-0.009	-0.005	32.284	0.226	0.226	0.000	0.000	0.000
139	A	158	LYS	1	0.897	0.932	34.419	9.052	9.052	0.000	0.000	0.000
140	A	159	ASP	-1	-0.749	-0.835	37.734	-7.558	-7.558	0.000	0.000	0.000
141	A	160	ARG	1	0.977	0.989	39.987	6.785	6.785	0.000	0.000	0.000
142	A	161	ASN	0	-0.014	-0.009	42.593	0.238	0.238	0.000	0.000	0.000
143	A	162	PHE	0	0.027	0.011	33.284	-0.028	-0.028	0.000	0.000	0.000
144	A	163	HIS	1	0.817	0.917	37.846	8.280	8.280	0.000	0.000	0.000
145	A	164	VAL	0	0.023	0.008	40.570	0.008	0.008	0.000	0.000	0.000
146	A	165	PHE	0	0.024	-0.005	36.711	0.035	0.035	0.000	0.000	0.000
147	A	166	LEU	0	-0.007	0.002	35.265	-0.030	-0.030	0.000	0.000	0.000
148	A	167	GLU	-1	-0.832	-0.923	38.907	-7.926	-7.926	0.000	0.000	0.000
149	A	168	TYR	0	-0.045	-0.016	41.731	0.164	0.164	0.000	0.000	0.000
150	A	169	ASP	-1	-0.854	-0.921	43.724	-7.415	-7.415	0.000	0.000	0.000
151	A	170	GLN	0	-0.093	-0.049	45.119	0.318	0.318	0.000	0.000	0.000
152	A	171	ASP	-1	-0.823	-0.892	46.148	-6.913	-6.913	0.000	0.000	0.000
153	A	172	LEU	0	-0.032	-0.021	43.482	0.093	0.093	0.000	0.000	0.000
154	A	173	SER	0	-0.109	-0.071	47.473	0.094	0.094	0.000	0.000	0.000
155	A	174	VAL	-1	-0.977	-0.971	49.331	-5.921	-5.921	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:SER)