FMO DATABASE

FMODB ID: 46RLN

Calculation Name: 2MOQ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2MOQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NX66

Base Structure: SolutionNMR

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	148
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1429789.919376
FMO2-HF: Nuclear repulsion	1370131.020175
FMO2-HF: Total energy	-59658.899201
FMO2-MP2: Total energy	-59835.751846

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:125:LEU)

Summations of interaction energy for fragment #1(A:125:LEU)

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.
-21.042	-10.462	13.219	-10.263	-13.532	-0.107

Interaction energy analysis for fragmet #1(A:125:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.774 / q_NPA : 0.880

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	127	GLN	0	0.074	0.049	2.742	-0.864	3.278	0.128	-1.878	-2.391	-0.007
4	A	128	GLU	-1	-0.877	-0.934	2.611	-35.417	-33.463	0.701	-1.140	-1.516	-0.016
5	A	129	LEU	0	-0.029	-0.017	4.372	-0.088	0.131	-0.001	-0.013	-0.205	0.000
6	A	130	ARG	1	0.900	0.925	5.160	19.790	19.820	-0.001	-0.001	-0.027	0.000
74	A	198	PHE	0	0.008	-0.007	4.529	3.368	3.471	-0.001	-0.005	-0.096	0.000
75	A	199	GLU	-1	-0.837	-0.891	4.585	-35.617	-35.507	-0.001	-0.010	-0.098	0.000
85	A	209	ILE	0	0.022	0.017	2.368	-1.558	-0.263	0.938	-0.543	-1.690	-0.003
86	A	210	LYS	1	0.850	0.924	1.850	-13.637	-11.095	8.125	-5.900	-4.767	-0.075
87	A	211	LEU	0	0.036	0.006	2.437	5.504	5.478	3.332	-0.745	-2.561	-0.006
88	A	212	VAL	0	-0.021	0.002	4.754	0.416	0.455	-0.001	-0.010	-0.028	0.000
99	A	223	ILE	0	-0.013	0.004	3.948	-2.766	-2.594	0.000	-0.018	-0.153	0.000
7	A	131	GLU	-1	-0.927	-0.960	7.470	-23.222	-23.222	0.000	0.000	0.000	0.000
8	A	132	ALA	0	-0.040	-0.005	4.898	1.234	1.234	0.000	0.000	0.000	0.000
9	A	133	ILE	0	0.000	-0.005	7.061	1.583	1.583	0.000	0.000	0.000	0.000
10	A	134	LYS	1	0.958	0.974	10.185	19.920	19.920	0.000	0.000	0.000	0.000
11	A	135	ASN	0	-0.034	-0.012	8.620	0.452	0.452	0.000	0.000	0.000	0.000
12	A	136	PRO	0	0.043	0.011	10.716	-0.408	-0.408	0.000	0.000	0.000	0.000
13	A	137	ALA	0	-0.011	0.006	10.439	0.683	0.683	0.000	0.000	0.000	0.000
14	A	138	ILE	0	0.015	0.009	7.743	0.473	0.473	0.000	0.000	0.000	0.000
15	A	139	LYS	1	0.837	0.910	11.191	17.036	17.036	0.000	0.000	0.000	0.000
16	A	140	ASP	-1	-0.860	-0.909	13.591	-15.732	-15.732	0.000	0.000	0.000	0.000
17	A	141	LYS	1	0.857	0.932	13.992	19.658	19.658	0.000	0.000	0.000	0.000
18	A	142	ASP	-1	-0.788	-0.899	14.844	-17.229	-17.229	0.000	0.000	0.000	0.000
19	A	143	HIS	0	-0.078	-0.039	13.785	0.491	0.491	0.000	0.000	0.000	0.000
20	A	144	SER	0	-0.018	-0.019	15.855	-0.475	-0.475	0.000	0.000	0.000	0.000
21	A	145	ALA	0	0.029	0.015	18.683	0.675	0.675	0.000	0.000	0.000	0.000
22	A	146	PRO	0	0.024	0.003	20.885	-0.247	-0.247	0.000	0.000	0.000	0.000
23	A	147	ASN	0	-0.035	-0.008	19.907	0.317	0.317	0.000	0.000	0.000	0.000
24	A	148	SER	0	-0.005	-0.010	18.429	-0.860	-0.860	0.000	0.000	0.000	0.000
25	A	149	ARG	1	0.959	0.979	19.952	13.032	13.032	0.000	0.000	0.000	0.000
26	A	150	PRO	0	0.011	0.013	19.618	-0.793	-0.793	0.000	0.000	0.000	0.000
27	A	151	ILE	0	-0.050	-0.020	17.743	0.395	0.395	0.000	0.000	0.000	0.000
28	A	152	ASP	-1	-0.816	-0.917	19.093	-14.050	-14.050	0.000	0.000	0.000	0.000
29	A	153	PHE	0	-0.079	-0.051	15.195	-0.197	-0.197	0.000	0.000	0.000	0.000
30	A	154	GLU	-1	-0.787	-0.865	20.285	-11.209	-11.209	0.000	0.000	0.000	0.000
31	A	155	MET	0	-0.047	-0.045	14.350	-1.046	-1.046	0.000	0.000	0.000	0.000
32	A	156	LYS	1	0.894	0.944	19.505	12.144	12.144	0.000	0.000	0.000	0.000
33	A	157	LYS	1	0.827	0.905	19.821	12.123	12.123	0.000	0.000	0.000	0.000
34	A	158	LYS	1	0.948	0.960	21.669	10.799	10.799	0.000	0.000	0.000	0.000
35	A	159	ASP	-1	-0.914	-0.956	24.061	-10.791	-10.791	0.000	0.000	0.000	0.000
36	A	160	GLY	0	0.039	0.032	25.793	0.189	0.189	0.000	0.000	0.000	0.000
37	A	161	THR	0	-0.029	-0.010	20.856	-0.032	-0.032	0.000	0.000	0.000	0.000
38	A	162	GLN	0	0.030	0.004	22.524	0.003	0.003	0.000	0.000	0.000	0.000
39	A	163	GLN	0	-0.005	-0.011	17.019	0.529	0.529	0.000	0.000	0.000	0.000
40	A	164	PHE	0	0.021	0.008	20.256	-0.122	-0.122	0.000	0.000	0.000	0.000
41	A	165	TYR	0	-0.021	0.008	21.683	0.243	0.243	0.000	0.000	0.000	0.000
42	A	166	HIS	0	-0.025	-0.021	17.878	0.526	0.526	0.000	0.000	0.000	0.000
43	A	167	TYR	0	0.046	0.011	17.901	-0.489	-0.489	0.000	0.000	0.000	0.000
44	A	168	ALA	0	-0.002	0.023	12.583	-0.377	-0.377	0.000	0.000	0.000	0.000
45	A	169	SER	0	-0.027	-0.030	13.439	-0.708	-0.708	0.000	0.000	0.000	0.000
46	A	170	SER	0	-0.029	-0.001	14.975	0.243	0.243	0.000	0.000	0.000	0.000
47	A	171	VAL	0	0.009	0.015	16.643	-0.949	-0.949	0.000	0.000	0.000	0.000
48	A	172	LYS	1	0.830	0.904	12.951	18.127	18.127	0.000	0.000	0.000	0.000
49	A	173	PRO	0	0.058	0.050	17.624	-0.255	-0.255	0.000	0.000	0.000	0.000
50	A	174	ALA	0	-0.051	-0.026	14.481	-1.058	-1.058	0.000	0.000	0.000	0.000
51	A	175	ARG	1	0.850	0.917	14.796	19.092	19.092	0.000	0.000	0.000	0.000
52	A	176	VAL	0	0.012	0.009	15.027	-1.495	-1.495	0.000	0.000	0.000	0.000
53	A	177	ILE	0	-0.024	-0.023	14.324	0.859	0.859	0.000	0.000	0.000	0.000
54	A	178	PHE	0	-0.033	-0.014	17.322	0.068	0.068	0.000	0.000	0.000	0.000
55	A	179	THR	0	0.013	0.003	15.319	-0.887	-0.887	0.000	0.000	0.000	0.000
56	A	180	ASP	-1	-0.761	-0.869	17.664	-16.433	-16.433	0.000	0.000	0.000	0.000
57	A	181	SER	0	-0.059	-0.033	19.497	0.125	0.125	0.000	0.000	0.000	0.000
58	A	182	LYS	1	0.933	0.977	15.284	18.779	18.779	0.000	0.000	0.000	0.000
59	A	183	PRO	0	0.036	0.036	16.001	-0.569	-0.569	0.000	0.000	0.000	0.000
60	A	184	GLU	-1	-0.761	-0.857	10.622	-28.256	-28.256	0.000	0.000	0.000	0.000
61	A	185	ILE	0	-0.019	-0.008	11.523	1.867	1.867	0.000	0.000	0.000	0.000
62	A	186	GLU	-1	-0.769	-0.848	10.472	-24.471	-24.471	0.000	0.000	0.000	0.000
63	A	187	LEU	0	0.007	-0.003	9.226	1.833	1.833	0.000	0.000	0.000	0.000
64	A	188	GLY	0	0.055	0.021	9.561	-1.846	-1.846	0.000	0.000	0.000	0.000
65	A	189	LEU	0	-0.046	-0.013	9.434	0.975	0.975	0.000	0.000	0.000	0.000
66	A	190	GLN	0	0.034	0.007	12.871	-0.136	-0.136	0.000	0.000	0.000	0.000
67	A	191	SER	0	0.010	-0.004	14.563	0.140	0.140	0.000	0.000	0.000	0.000
68	A	192	GLY	0	0.012	0.011	11.010	-0.767	-0.767	0.000	0.000	0.000	0.000
69	A	193	GLN	0	-0.075	-0.051	10.878	-0.866	-0.866	0.000	0.000	0.000	0.000
70	A	194	PHE	0	-0.013	0.000	13.196	0.297	0.297	0.000	0.000	0.000	0.000
71	A	195	TRP	0	0.049	0.011	8.089	-0.530	-0.530	0.000	0.000	0.000	0.000
72	A	196	ARG	1	0.836	0.937	8.609	19.729	19.729	0.000	0.000	0.000	0.000
73	A	197	LYS	1	0.890	0.926	5.163	25.933	25.933	0.000	0.000	0.000	0.000
76	A	200	VAL	0	0.025	0.019	7.141	2.985	2.985	0.000	0.000	0.000	0.000
77	A	201	TYR	0	-0.045	-0.042	9.595	-1.266	-1.266	0.000	0.000	0.000	0.000
78	A	202	GLU	-1	-0.749	-0.839	13.194	-15.570	-15.570	0.000	0.000	0.000	0.000
79	A	203	GLY	0	0.002	-0.005	16.441	0.282	0.282	0.000	0.000	0.000	0.000
80	A	204	ASP	-1	-0.931	-0.967	16.810	-18.724	-18.724	0.000	0.000	0.000	0.000
81	A	205	LYS	1	0.964	0.983	14.141	17.318	17.318	0.000	0.000	0.000	0.000
82	A	206	LYS	1	0.990	0.997	8.130	33.107	33.107	0.000	0.000	0.000	0.000
83	A	207	LEU	0	-0.001	0.008	9.757	-0.135	-0.135	0.000	0.000	0.000	0.000
84	A	208	PRO	0	-0.057	-0.022	5.620	-3.459	-3.459	0.000	0.000	0.000	0.000
89	A	213	SER	0	-0.049	-0.032	8.536	2.317	2.317	0.000	0.000	0.000	0.000
90	A	214	TYR	0	-0.004	0.010	5.373	-2.057	-2.057	0.000	0.000	0.000	0.000
91	A	215	ASP	-1	-0.805	-0.915	11.703	-14.543	-14.543	0.000	0.000	0.000	0.000
92	A	216	THR	0	-0.015	-0.020	14.017	0.234	0.234	0.000	0.000	0.000	0.000
93	A	217	VAL	0	-0.018	-0.001	15.882	0.526	0.526	0.000	0.000	0.000	0.000
94	A	218	LYS	1	0.952	0.983	17.345	14.609	14.609	0.000	0.000	0.000	0.000
95	A	219	ASP	-1	-0.808	-0.890	15.323	-16.511	-16.511	0.000	0.000	0.000	0.000
96	A	220	TYR	0	-0.011	-0.006	13.495	-0.500	-0.500	0.000	0.000	0.000	0.000
97	A	221	ALA	0	0.010	-0.017	8.223	-0.862	-0.862	0.000	0.000	0.000	0.000
98	A	222	TYR	0	-0.045	-0.041	8.858	0.713	0.713	0.000	0.000	0.000	0.000
100	A	224	ARG	1	0.803	0.858	6.109	27.767	27.767	0.000	0.000	0.000	0.000
101	A	225	PHE	0	0.019	-0.003	6.482	-6.515	-6.515	0.000	0.000	0.000	0.000
102	A	226	SER	0	0.031	0.021	8.275	2.208	2.208	0.000	0.000	0.000	0.000
103	A	227	VAL	0	-0.030	-0.018	10.735	-1.182	-1.182	0.000	0.000	0.000	0.000
104	A	228	SER	0	-0.038	-0.038	13.765	0.076	0.076	0.000	0.000	0.000	0.000
105	A	229	ASN	0	-0.027	-0.025	16.601	0.164	0.164	0.000	0.000	0.000	0.000
106	A	230	GLY	0	0.037	0.014	20.094	0.616	0.616	0.000	0.000	0.000	0.000
107	A	231	THR	0	-0.093	-0.058	16.566	0.205	0.205	0.000	0.000	0.000	0.000
108	A	232	LYS	1	0.973	0.974	19.702	12.287	12.287	0.000	0.000	0.000	0.000
109	A	233	ALA	0	0.032	0.022	19.730	0.264	0.264	0.000	0.000	0.000	0.000
110	A	234	VAL	0	-0.036	-0.019	13.563	-0.428	-0.428	0.000	0.000	0.000	0.000
111	A	235	LYS	1	0.917	0.971	14.826	18.343	18.343	0.000	0.000	0.000	0.000
112	A	236	ILE	0	-0.004	-0.010	11.020	-1.792	-1.792	0.000	0.000	0.000	0.000
113	A	237	VAL	0	0.001	0.026	9.021	1.348	1.348	0.000	0.000	0.000	0.000
114	A	238	SER	0	0.000	-0.005	9.113	-1.627	-1.627	0.000	0.000	0.000	0.000
115	A	239	SER	0	0.004	0.010	9.555	1.961	1.961	0.000	0.000	0.000	0.000
116	A	240	THR	0	0.044	0.015	10.561	-1.434	-1.434	0.000	0.000	0.000	0.000
117	A	241	HIS	0	-0.064	-0.046	13.379	0.435	0.435	0.000	0.000	0.000	0.000
118	A	242	PHE	0	0.026	0.013	15.109	-0.623	-0.623	0.000	0.000	0.000	0.000
119	A	243	ASN	0	0.002	0.018	17.680	0.698	0.698	0.000	0.000	0.000	0.000
120	A	244	ASN	0	-0.004	-0.015	20.840	-0.151	-0.151	0.000	0.000	0.000	0.000
121	A	245	LYS	1	0.912	0.964	20.259	13.125	13.125	0.000	0.000	0.000	0.000
122	A	246	GLU	-1	-0.828	-0.901	17.408	-15.821	-15.821	0.000	0.000	0.000	0.000
123	A	247	GLU	-1	-0.836	-0.918	16.663	-13.380	-13.380	0.000	0.000	0.000	0.000
124	A	248	LYS	1	0.833	0.901	13.374	16.197	16.197	0.000	0.000	0.000	0.000
125	A	249	TYR	0	0.010	0.007	10.867	-0.125	-0.125	0.000	0.000	0.000	0.000
126	A	250	ASP	-1	-0.778	-0.851	15.323	-13.749	-13.749	0.000	0.000	0.000	0.000
127	A	251	TYR	0	-0.052	-0.054	16.518	-0.499	-0.499	0.000	0.000	0.000	0.000
128	A	252	THR	0	-0.047	-0.038	14.453	0.533	0.533	0.000	0.000	0.000	0.000
129	A	253	LEU	0	-0.041	-0.005	16.419	-0.663	-0.663	0.000	0.000	0.000	0.000
130	A	254	MET	0	-0.029	-0.003	15.898	0.161	0.161	0.000	0.000	0.000	0.000
131	A	255	GLU	-1	-0.911	-0.968	17.867	-12.026	-12.026	0.000	0.000	0.000	0.000
132	A	256	PHE	0	-0.015	-0.011	20.710	-0.052	-0.052	0.000	0.000	0.000	0.000
133	A	257	ALA	0	0.062	0.046	21.609	0.517	0.517	0.000	0.000	0.000	0.000
134	A	258	GLN	0	-0.011	-0.017	22.856	0.371	0.371	0.000	0.000	0.000	0.000
135	A	259	PRO	0	-0.011	-0.015	22.252	-0.601	-0.601	0.000	0.000	0.000	0.000
136	A	260	ILE	0	-0.004	0.015	16.486	-0.013	-0.013	0.000	0.000	0.000	0.000
137	A	261	TYR	0	-0.007	-0.009	19.616	-0.449	-0.449	0.000	0.000	0.000	0.000
138	A	262	ASN	0	-0.038	-0.028	20.213	0.217	0.217	0.000	0.000	0.000	0.000
139	A	263	SER	0	-0.061	-0.024	21.728	0.505	0.505	0.000	0.000	0.000	0.000
140	A	264	ALA	0	0.050	0.013	24.854	0.263	0.263	0.000	0.000	0.000	0.000
141	A	265	ASP	-1	-0.888	-0.921	26.042	-9.659	-9.659	0.000	0.000	0.000	0.000
142	A	266	LYS	1	0.816	0.893	27.993	10.516	10.516	0.000	0.000	0.000	0.000
143	A	267	PHE	0	0.043	0.030	21.651	0.041	0.041	0.000	0.000	0.000	0.000
144	A	268	LYS	1	0.849	0.915	23.916	11.995	11.995	0.000	0.000	0.000	0.000
145	A	269	THR	0	-0.006	-0.022	23.189	-0.712	-0.712	0.000	0.000	0.000	0.000
146	A	270	GLU	-1	-0.961	-0.978	25.279	-10.107	-10.107	0.000	0.000	0.000	0.000
147	A	271	GLU	-1	-1.010	-0.998	26.393	-12.243	-12.243	0.000	0.000	0.000	0.000
148	A	272	ASP	-2	-1.899	-1.930	28.995	-19.666	-19.666	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:125:LEU)