FMO DATABASE

FMODB ID: RMYJ8

Calculation Name: 3Q1H-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3Q1H

Chain ID: A

ChEMBL ID:

UniProt ID: A0A384

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	161
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1616674.034604
FMO2-HF: Nuclear repulsion	1552216.478187
FMO2-HF: Total energy	-64457.556416
FMO2-MP2: Total energy	-64642.763804

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-149.685	-148.565	-0.011	-0.365	-0.743	0

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.838 / q_NPA : 0.902

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	2	ILE	0	0.039	0.032	3.837	2.680	3.696	-0.010	-0.329	-0.677
91	A	90	GLU	-1	-0.912	-0.959	4.340	-64.832	-64.728	-0.001	-0.036	-0.066
4	A	3	ILE	0	-0.038	-0.024	6.569	3.884	3.884	0.000	0.000	0.000
5	A	4	SER	0	0.033	-0.007	8.877	0.808	0.808	0.000	0.000	0.000
6	A	5	LEU	0	-0.021	-0.001	12.134	1.231	1.231	0.000	0.000	0.000
7	A	6	ILE	0	-0.029	-0.015	15.320	0.023	0.023	0.000	0.000	0.000
8	A	7	ALA	0	0.023	0.017	18.403	0.486	0.486	0.000	0.000	0.000
9	A	8	ALA	0	0.054	0.042	21.932	-0.092	-0.092	0.000	0.000	0.000
10	A	9	LEU	0	-0.023	-0.012	23.021	0.019	0.019	0.000	0.000	0.000
11	A	10	ALA	0	0.048	0.030	27.042	0.138	0.138	0.000	0.000	0.000
12	A	11	ALA	0	-0.001	-0.009	30.135	0.098	0.098	0.000	0.000	0.000
13	A	12	ASP	-1	-0.835	-0.893	26.759	-11.020	-11.020	0.000	0.000	0.000
14	A	13	ARG	1	0.851	0.937	26.922	9.238	9.238	0.000	0.000	0.000
15	A	14	VAL	0	-0.018	-0.018	24.679	-0.176	-0.176	0.000	0.000	0.000
16	A	15	ILE	0	0.015	0.011	27.203	0.379	0.379	0.000	0.000	0.000
17	A	16	GLY	0	-0.052	-0.019	27.877	-0.422	-0.422	0.000	0.000	0.000
18	A	17	MET	0	-0.027	-0.008	26.688	0.362	0.362	0.000	0.000	0.000
19	A	18	GLU	-1	-0.907	-0.943	29.316	-9.490	-9.490	0.000	0.000	0.000
20	A	19	ASN	0	-0.092	-0.051	25.260	0.099	0.099	0.000	0.000	0.000
21	A	20	ALA	0	0.023	-0.001	25.318	-0.292	-0.292	0.000	0.000	0.000
22	A	21	MET	0	-0.037	-0.008	18.640	-0.672	-0.672	0.000	0.000	0.000
23	A	22	PRO	0	0.009	0.011	21.347	0.408	0.408	0.000	0.000	0.000
24	A	23	TRP	0	0.004	-0.024	18.448	-0.653	-0.653	0.000	0.000	0.000
25	A	24	HIS	0	0.027	0.011	24.257	0.037	0.037	0.000	0.000	0.000
26	A	25	LEU	0	-0.021	-0.001	20.789	-0.259	-0.259	0.000	0.000	0.000
27	A	26	PRO	0	0.021	0.018	23.565	0.415	0.415	0.000	0.000	0.000
28	A	27	ALA	0	0.040	0.011	25.080	-0.386	-0.386	0.000	0.000	0.000
29	A	28	ASP	-1	-0.849	-0.895	25.526	-12.754	-12.754	0.000	0.000	0.000
30	A	29	LEU	0	0.033	0.024	19.635	-0.653	-0.653	0.000	0.000	0.000
31	A	30	ALA	0	0.002	0.006	21.331	-0.633	-0.633	0.000	0.000	0.000
32	A	31	TRP	0	-0.060	-0.044	16.932	-0.398	-0.398	0.000	0.000	0.000
33	A	32	PHE	0	0.052	0.032	13.280	-0.176	-0.176	0.000	0.000	0.000
34	A	33	LYS	1	1.003	1.004	17.823	13.001	13.001	0.000	0.000	0.000
35	A	34	ARG	1	0.896	0.946	19.824	14.080	14.080	0.000	0.000	0.000
36	A	35	ASN	0	0.016	0.010	14.351	0.599	0.599	0.000	0.000	0.000
37	A	36	THR	0	0.022	0.019	14.624	-1.214	-1.214	0.000	0.000	0.000
38	A	37	LEU	0	-0.060	-0.024	16.073	0.010	0.010	0.000	0.000	0.000
39	A	38	ASN	0	0.047	0.014	12.822	-0.202	-0.202	0.000	0.000	0.000
40	A	39	LYS	1	0.832	0.941	10.097	25.814	25.814	0.000	0.000	0.000
41	A	40	PRO	0	0.041	0.020	11.426	1.763	1.763	0.000	0.000	0.000
42	A	41	VAL	0	-0.021	0.008	14.246	-0.817	-0.817	0.000	0.000	0.000
43	A	42	ILE	0	0.019	0.011	12.874	0.661	0.661	0.000	0.000	0.000
44	A	43	MET	0	0.002	0.020	16.971	0.396	0.396	0.000	0.000	0.000
45	A	44	GLY	0	0.019	0.006	20.488	0.081	0.081	0.000	0.000	0.000
46	A	45	ARG	1	0.851	0.893	23.271	10.643	10.643	0.000	0.000	0.000
47	A	46	LYS	1	0.962	0.972	26.303	10.542	10.542	0.000	0.000	0.000
48	A	47	THR	0	0.032	0.028	23.591	0.494	0.494	0.000	0.000	0.000
49	A	48	PHE	0	0.044	0.021	24.817	0.144	0.144	0.000	0.000	0.000
50	A	49	GLU	-1	-0.889	-0.932	26.471	-9.945	-9.945	0.000	0.000	0.000
51	A	50	SER	0	-0.075	-0.041	28.491	0.256	0.256	0.000	0.000	0.000
52	A	51	ILE	0	0.020	0.016	25.127	0.088	0.088	0.000	0.000	0.000
53	A	52	GLY	0	-0.003	0.005	29.283	0.196	0.196	0.000	0.000	0.000
54	A	53	ARG	1	0.878	0.933	28.348	11.278	11.278	0.000	0.000	0.000
55	A	54	PRO	0	0.017	0.016	23.906	-0.260	-0.260	0.000	0.000	0.000
56	A	55	LEU	0	0.011	0.014	21.105	0.433	0.433	0.000	0.000	0.000
57	A	56	PRO	0	-0.029	-0.032	22.359	-0.420	-0.420	0.000	0.000	0.000
58	A	57	GLY	0	0.003	0.003	21.292	-0.404	-0.404	0.000	0.000	0.000
59	A	58	ARG	1	0.836	0.929	16.025	17.664	17.664	0.000	0.000	0.000
60	A	59	LEU	0	0.023	0.025	14.544	0.959	0.959	0.000	0.000	0.000
61	A	60	ASN	0	-0.014	-0.018	17.274	-0.264	-0.264	0.000	0.000	0.000
62	A	61	ILE	0	0.024	0.016	14.678	0.424	0.424	0.000	0.000	0.000
63	A	62	VAL	0	0.014	0.015	18.899	-0.046	-0.046	0.000	0.000	0.000
64	A	63	ILE	0	0.003	0.001	17.366	0.293	0.293	0.000	0.000	0.000
65	A	64	SER	0	-0.065	-0.065	21.732	0.677	0.677	0.000	0.000	0.000
66	A	65	SER	0	0.013	-0.004	25.126	-0.247	-0.247	0.000	0.000	0.000
67	A	66	GLN	0	-0.053	-0.006	27.515	0.196	0.196	0.000	0.000	0.000
68	A	67	PRO	0	0.050	0.017	28.110	-0.396	-0.396	0.000	0.000	0.000
69	A	68	GLY	0	0.039	0.019	27.627	0.044	0.044	0.000	0.000	0.000
70	A	69	THR	0	-0.028	-0.025	28.307	0.201	0.201	0.000	0.000	0.000
71	A	70	ASP	-1	-0.765	-0.868	27.817	-10.884	-10.884	0.000	0.000	0.000
72	A	71	GLU	-1	-0.880	-0.931	27.161	-11.374	-11.374	0.000	0.000	0.000
73	A	72	ARG	1	0.758	0.852	25.972	10.504	10.504	0.000	0.000	0.000
74	A	73	VAL	0	-0.052	-0.018	22.574	-0.552	-0.552	0.000	0.000	0.000
75	A	74	THR	0	0.001	0.010	18.651	0.229	0.229	0.000	0.000	0.000
76	A	75	TRP	0	-0.032	-0.014	21.083	-0.153	-0.153	0.000	0.000	0.000
77	A	76	ALA	0	0.020	0.013	18.750	-0.200	-0.200	0.000	0.000	0.000
78	A	77	ALA	0	0.002	0.002	20.712	0.439	0.439	0.000	0.000	0.000
79	A	78	SER	0	-0.063	-0.051	17.687	0.197	0.197	0.000	0.000	0.000
80	A	79	ILE	0	0.026	0.004	13.747	-0.333	-0.333	0.000	0.000	0.000
81	A	80	GLU	-1	-0.801	-0.886	13.265	-19.396	-19.396	0.000	0.000	0.000
82	A	81	GLU	-1	-0.849	-0.912	13.442	-16.249	-16.249	0.000	0.000	0.000
83	A	82	ALA	0	0.003	-0.009	15.111	-0.465	-0.465	0.000	0.000	0.000
84	A	83	LEU	0	-0.007	-0.008	8.749	-0.821	-0.821	0.000	0.000	0.000
85	A	84	ALA	0	-0.025	-0.009	10.419	-1.881	-1.881	0.000	0.000	0.000
86	A	85	PHE	0	-0.014	-0.019	12.250	-0.414	-0.414	0.000	0.000	0.000
87	A	86	ALA	0	-0.016	-0.001	10.286	0.310	0.310	0.000	0.000	0.000
88	A	87	GLY	0	0.009	0.011	10.098	-1.684	-1.684	0.000	0.000	0.000
89	A	88	ASN	0	-0.060	-0.044	6.635	-1.165	-1.165	0.000	0.000	0.000
90	A	89	ALA	0	-0.023	0.000	6.406	-2.731	-2.731	0.000	0.000	0.000
92	A	91	GLU	-1	-0.768	-0.870	5.904	-30.898	-30.898	0.000	0.000	0.000
93	A	92	VAL	0	-0.039	-0.019	8.520	2.810	2.810	0.000	0.000	0.000
94	A	93	MET	0	-0.029	-0.002	11.067	-0.006	-0.006	0.000	0.000	0.000
95	A	94	VAL	0	0.002	0.004	13.079	1.278	1.278	0.000	0.000	0.000
96	A	95	MET	0	0.020	0.003	15.829	0.308	0.308	0.000	0.000	0.000
97	A	96	GLY	0	0.065	0.053	19.307	0.855	0.855	0.000	0.000	0.000
98	A	97	GLY	0	0.003	-0.013	21.299	0.019	0.019	0.000	0.000	0.000
99	A	98	GLY	0	0.104	0.037	22.253	-0.566	-0.566	0.000	0.000	0.000
100	A	99	ARG	1	0.863	0.930	22.183	13.043	13.043	0.000	0.000	0.000
101	A	100	VAL	0	-0.035	-0.011	18.008	-0.232	-0.232	0.000	0.000	0.000
102	A	101	TYR	0	0.021	-0.003	17.614	-0.458	-0.458	0.000	0.000	0.000
103	A	102	LYS	1	0.982	0.990	17.341	12.300	12.300	0.000	0.000	0.000
104	A	103	GLN	0	-0.041	-0.022	18.060	-0.221	-0.221	0.000	0.000	0.000
105	A	104	PHE	0	0.029	-0.001	12.040	-0.543	-0.543	0.000	0.000	0.000
106	A	105	LEU	0	0.005	0.021	12.817	-1.693	-1.693	0.000	0.000	0.000
107	A	106	ASP	-1	-0.867	-0.925	13.104	-18.530	-18.530	0.000	0.000	0.000
108	A	107	ARG	1	0.803	0.886	9.192	20.444	20.444	0.000	0.000	0.000
109	A	108	ALA	0	-0.033	-0.016	8.166	-3.328	-3.328	0.000	0.000	0.000
110	A	109	ASN	0	-0.009	-0.005	5.078	2.150	2.150	0.000	0.000	0.000
111	A	110	ARG	1	0.828	0.908	9.006	28.959	28.959	0.000	0.000	0.000
112	A	111	MET	0	-0.054	-0.014	11.541	0.902	0.902	0.000	0.000	0.000
113	A	112	TYR	0	-0.070	-0.062	12.975	0.201	0.201	0.000	0.000	0.000
114	A	113	LEU	0	0.020	0.008	17.943	0.390	0.390	0.000	0.000	0.000
115	A	114	THR	0	-0.002	-0.007	21.316	0.282	0.282	0.000	0.000	0.000
116	A	115	HIS	1	0.861	0.923	23.550	12.811	12.811	0.000	0.000	0.000
117	A	116	ILE	0	0.066	0.008	27.395	0.088	0.088	0.000	0.000	0.000
118	A	117	ASP	-1	-0.879	-0.954	30.803	-10.119	-10.119	0.000	0.000	0.000
119	A	118	ALA	0	-0.032	0.003	33.033	0.243	0.243	0.000	0.000	0.000
120	A	119	GLU	-1	-0.893	-0.941	32.917	-9.502	-9.502	0.000	0.000	0.000
121	A	120	VAL	0	-0.042	-0.023	34.621	0.002	0.002	0.000	0.000	0.000
122	A	121	GLY	0	0.027	0.015	31.537	-0.224	-0.224	0.000	0.000	0.000
123	A	122	GLY	0	-0.008	-0.009	30.922	0.331	0.331	0.000	0.000	0.000
124	A	123	ASP	-1	-0.911	-0.964	31.705	-9.827	-9.827	0.000	0.000	0.000
125	A	124	THR	0	-0.093	-0.050	27.301	-0.218	-0.218	0.000	0.000	0.000
126	A	125	HIS	0	-0.025	-0.030	27.293	0.316	0.316	0.000	0.000	0.000
127	A	126	PHE	0	-0.014	-0.018	18.281	-0.392	-0.392	0.000	0.000	0.000
128	A	127	PRO	0	-0.108	-0.049	19.368	0.404	0.404	0.000	0.000	0.000
129	A	128	ASP	-1	-0.862	-0.928	21.639	-12.053	-12.053	0.000	0.000	0.000
130	A	129	TYR	0	-0.043	-0.041	17.965	-0.533	-0.533	0.000	0.000	0.000
131	A	130	GLU	-1	-0.866	-0.926	18.912	-12.595	-12.595	0.000	0.000	0.000
132	A	131	PRO	0	-0.035	-0.042	19.061	-0.651	-0.651	0.000	0.000	0.000
133	A	132	ASP	-1	-0.891	-0.918	20.026	-14.615	-14.615	0.000	0.000	0.000
134	A	133	GLU	-1	-0.833	-0.892	15.025	-18.141	-18.141	0.000	0.000	0.000
135	A	134	TRP	0	-0.038	-0.023	12.150	-2.025	-2.025	0.000	0.000	0.000
136	A	135	GLU	-1	-0.907	-0.948	15.415	-16.274	-16.274	0.000	0.000	0.000
137	A	136	SER	0	-0.061	-0.076	16.496	-0.862	-0.862	0.000	0.000	0.000
138	A	137	VAL	0	0.006	0.009	14.367	0.653	0.653	0.000	0.000	0.000
139	A	138	PHE	0	-0.039	-0.026	17.613	0.324	0.324	0.000	0.000	0.000
140	A	139	SER	0	0.007	0.004	20.009	-0.016	-0.016	0.000	0.000	0.000
141	A	140	GLU	0	-0.066	-0.062	23.215	0.526	0.526	0.000	0.000	0.000
142	A	141	PHE	0	0.027	0.003	26.245	-0.061	-0.061	0.000	0.000	0.000
143	A	142	HIS	1	0.804	0.897	29.555	9.733	9.733	0.000	0.000	0.000
144	A	143	ASP	-1	-0.824	-0.915	32.039	-8.582	-8.582	0.000	0.000	0.000
145	A	144	ALA	0	-0.020	-0.008	35.376	-0.198	-0.198	0.000	0.000	0.000
146	A	145	ASP	-1	-0.824	-0.906	37.085	-8.746	-8.746	0.000	0.000	0.000
147	A	146	GLU	-1	-0.951	-0.980	39.392	-8.050	-8.050	0.000	0.000	0.000
148	A	147	ALA	0	-0.062	-0.025	35.763	0.016	0.016	0.000	0.000	0.000
149	A	148	ASN	0	-0.112	-0.061	32.939	-0.622	-0.622	0.000	0.000	0.000
150	A	149	SER	0	0.033	0.007	35.893	0.088	0.088	0.000	0.000	0.000
151	A	150	HIS	0	-0.033	-0.020	34.040	0.294	0.294	0.000	0.000	0.000
152	A	151	SER	0	-0.028	0.007	34.212	-0.224	-0.224	0.000	0.000	0.000
153	A	152	TYR	0	-0.032	-0.022	27.105	-0.006	-0.006	0.000	0.000	0.000
154	A	153	CYS	0	-0.025	-0.010	26.702	0.005	0.005	0.000	0.000	0.000
155	A	154	PHE	0	-0.023	-0.004	19.588	-0.398	-0.398	0.000	0.000	0.000
156	A	155	GLU	-1	-0.786	-0.862	20.168	-13.665	-13.665	0.000	0.000	0.000
157	A	156	ILE	0	-0.046	-0.024	14.952	-0.457	-0.457	0.000	0.000	0.000
158	A	157	LEU	0	-0.001	0.010	16.034	0.353	0.353	0.000	0.000	0.000
159	A	158	GLU	-1	-0.835	-0.908	10.378	-29.701	-29.701	0.000	0.000	0.000
160	A	159	ARG	1	0.764	0.861	9.465	23.258	23.258	0.000	0.000	0.000
161	A	160	ARG	0	-0.116	-0.052	11.146	-5.335	-5.335	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)