FMO DATABASE

FMODB ID: M82YZ

Calculation Name: 4XCH-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4XCH

Chain ID: A

ChEMBL ID:

UniProt ID: B2CMA5

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1414123.598273
FMO2-HF: Nuclear repulsion	1355277.536179
FMO2-HF: Total energy	-58846.062094
FMO2-MP2: Total energy	-59016.759744

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:12:LEU)

Summations of interaction energy for fragment #1(A:12: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.
-59.591	-48.729	6.807	-5.097	-12.574	-0.048

Interaction energy analysis for fragmet #1(A:12:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.829 / q_NPA : 0.909

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	14	HIS	0	0.024	-0.008	2.703	-0.716	4.241	2.014	-2.316	-4.655	-0.025
4	A	15	THR	0	-0.048	-0.041	3.923	5.888	6.124	0.003	-0.019	-0.220	0.000
5	A	16	ILE	0	0.003	0.006	4.757	2.782	2.909	-0.001	-0.005	-0.121	0.000
6	A	17	VAL	0	-0.049	-0.006	2.500	-0.034	0.935	0.637	-0.353	-1.253	-0.003
10	A	21	TYR	0	-0.066	-0.054	2.933	-2.802	-1.578	0.238	-0.558	-0.905	-0.006
12	A	23	ARG	1	0.852	0.914	2.549	42.810	44.133	2.373	-0.763	-2.933	-0.005
29	A	40	ASP	-1	-0.739	-0.831	3.231	-42.395	-41.449	0.088	-0.460	-0.574	-0.003
31	A	42	ARG	1	0.785	0.886	3.066	38.161	38.595	0.045	-0.119	-0.360	0.000
143	A	154	ALA	0	0.005	0.020	4.156	0.419	0.524	-0.001	-0.015	-0.090	0.000
144	A	155	PHE	0	-0.027	-0.025	2.431	-4.190	-3.649	1.411	-0.489	-1.463	-0.006
7	A	18	LYS	1	0.924	0.967	5.620	24.153	24.153	0.000	0.000	0.000	0.000
8	A	19	ALA	0	-0.019	0.015	7.767	0.444	0.444	0.000	0.000	0.000	0.000
9	A	20	PRO	0	0.000	0.006	9.011	0.803	0.803	0.000	0.000	0.000	0.000
11	A	22	ILE	0	-0.001	0.024	8.846	-0.547	-0.547	0.000	0.000	0.000	0.000
13	A	24	LEU	0	0.018	0.023	7.197	-0.319	-0.319	0.000	0.000	0.000	0.000
14	A	25	ILE	0	-0.116	-0.059	5.370	-4.553	-4.553	0.000	0.000	0.000	0.000
15	A	26	SER	0	0.001	-0.017	7.335	-1.579	-1.579	0.000	0.000	0.000	0.000
16	A	27	GLU	-1	-0.766	-0.857	10.581	-16.032	-16.032	0.000	0.000	0.000	0.000
17	A	28	GLU	-1	-0.924	-0.954	13.924	-21.179	-21.179	0.000	0.000	0.000	0.000
18	A	29	VAL	0	-0.017	-0.015	16.228	0.786	0.786	0.000	0.000	0.000	0.000
19	A	30	GLY	0	0.045	0.032	19.934	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	31	PRO	0	-0.024	-0.043	22.589	0.283	0.283	0.000	0.000	0.000	0.000
21	A	32	LYS	1	0.911	0.954	25.374	10.392	10.392	0.000	0.000	0.000	0.000
22	A	33	GLY	0	0.016	0.015	24.618	0.364	0.364	0.000	0.000	0.000	0.000
23	A	34	ASP	-1	-0.936	-0.956	24.077	-11.842	-11.842	0.000	0.000	0.000	0.000
24	A	35	ILE	0	-0.024	-0.010	18.364	-0.375	-0.375	0.000	0.000	0.000	0.000
25	A	36	ILE	0	0.005	0.013	15.967	0.572	0.572	0.000	0.000	0.000	0.000
26	A	37	THR	0	-0.010	-0.003	13.895	-0.868	-0.868	0.000	0.000	0.000	0.000
27	A	38	ASN	0	-0.016	0.001	10.368	1.016	1.016	0.000	0.000	0.000	0.000
28	A	39	PHE	0	0.024	-0.004	8.750	-1.748	-1.748	0.000	0.000	0.000	0.000
30	A	41	ILE	0	0.027	0.017	6.690	0.025	0.025	0.000	0.000	0.000	0.000
32	A	43	LEU	0	0.046	0.005	8.064	1.044	1.044	0.000	0.000	0.000	0.000
33	A	44	ILE	0	-0.012	0.000	10.021	1.127	1.127	0.000	0.000	0.000	0.000
34	A	45	GLN	0	0.057	0.023	8.456	-2.438	-2.438	0.000	0.000	0.000	0.000
35	A	46	PRO	0	-0.019	-0.025	5.135	0.939	0.939	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.063	-0.042	8.189	0.786	0.786	0.000	0.000	0.000	0.000
37	A	48	GLU	-1	-0.914	-0.938	11.226	-18.707	-18.707	0.000	0.000	0.000	0.000
38	A	49	ASN	0	-0.017	-0.017	12.895	1.556	1.556	0.000	0.000	0.000	0.000
39	A	50	ALA	0	-0.028	-0.022	12.695	-1.483	-1.483	0.000	0.000	0.000	0.000
40	A	51	MET	0	-0.011	0.031	14.366	1.041	1.041	0.000	0.000	0.000	0.000
41	A	52	ASP	-1	-0.805	-0.864	16.558	-13.154	-13.154	0.000	0.000	0.000	0.000
42	A	53	THR	0	-0.021	-0.045	19.628	-0.323	-0.323	0.000	0.000	0.000	0.000
43	A	54	ALA	0	0.055	0.040	20.857	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	55	GLY	0	0.035	0.018	21.382	0.210	0.210	0.000	0.000	0.000	0.000
45	A	56	LEU	0	-0.020	-0.009	14.911	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	57	HIS	1	0.824	0.880	18.838	11.987	11.987	0.000	0.000	0.000	0.000
47	A	58	THR	0	0.026	-0.004	21.467	0.433	0.433	0.000	0.000	0.000	0.000
48	A	59	ILE	0	-0.002	-0.010	17.634	0.178	0.178	0.000	0.000	0.000	0.000
49	A	60	GLU	-1	-0.856	-0.919	18.882	-13.736	-13.736	0.000	0.000	0.000	0.000
50	A	61	HIS	1	0.791	0.889	19.940	11.574	11.574	0.000	0.000	0.000	0.000
51	A	62	LEU	0	-0.004	0.016	22.801	0.334	0.334	0.000	0.000	0.000	0.000
52	A	63	LEU	0	0.051	0.012	16.338	0.234	0.234	0.000	0.000	0.000	0.000
53	A	64	ALA	0	-0.016	0.004	20.499	0.047	0.047	0.000	0.000	0.000	0.000
54	A	65	LYS	1	0.879	0.931	21.961	10.190	10.190	0.000	0.000	0.000	0.000
55	A	66	LEU	0	-0.037	-0.020	22.491	0.107	0.107	0.000	0.000	0.000	0.000
56	A	67	ILE	0	0.062	0.023	17.334	0.076	0.076	0.000	0.000	0.000	0.000
57	A	68	ARG	1	0.881	0.940	21.452	12.679	12.679	0.000	0.000	0.000	0.000
58	A	69	GLN	0	-0.036	-0.011	24.313	0.168	0.168	0.000	0.000	0.000	0.000
59	A	70	ARG	1	0.727	0.843	22.689	11.562	11.562	0.000	0.000	0.000	0.000
60	A	71	ILE	0	-0.031	-0.007	19.520	-0.055	-0.055	0.000	0.000	0.000	0.000
61	A	72	ASP	-1	-0.886	-0.930	23.279	-10.708	-10.708	0.000	0.000	0.000	0.000
62	A	73	GLY	0	-0.006	-0.021	22.177	-0.478	-0.478	0.000	0.000	0.000	0.000
63	A	74	LEU	0	-0.005	-0.002	17.519	-0.496	-0.496	0.000	0.000	0.000	0.000
64	A	75	ILE	0	-0.036	-0.009	18.700	0.587	0.587	0.000	0.000	0.000	0.000
65	A	76	ASP	-1	-0.835	-0.913	17.071	-15.407	-15.407	0.000	0.000	0.000	0.000
66	A	77	CYS	0	-0.062	-0.028	15.277	-0.980	-0.980	0.000	0.000	0.000	0.000
67	A	78	SER	0	0.054	0.023	14.975	0.708	0.708	0.000	0.000	0.000	0.000
68	A	79	PRO	0	-0.010	0.001	13.631	-1.345	-1.345	0.000	0.000	0.000	0.000
69	A	80	PHE	0	-0.045	-0.019	6.998	-0.617	-0.617	0.000	0.000	0.000	0.000
70	A	81	GLY	0	0.045	0.018	11.431	1.017	1.017	0.000	0.000	0.000	0.000
71	A	82	CYS	0	-0.079	-0.031	7.571	1.012	1.012	0.000	0.000	0.000	0.000
72	A	83	ARG	1	0.901	0.939	11.280	16.843	16.843	0.000	0.000	0.000	0.000
73	A	84	THR	0	0.054	0.015	8.105	-0.293	-0.293	0.000	0.000	0.000	0.000
74	A	85	GLY	0	0.019	0.001	9.749	-0.520	-0.520	0.000	0.000	0.000	0.000
75	A	86	PHE	0	-0.012	0.007	10.572	0.788	0.788	0.000	0.000	0.000	0.000
76	A	87	HIS	0	0.005	0.000	9.655	-3.247	-3.247	0.000	0.000	0.000	0.000
77	A	88	MET	0	-0.032	-0.009	10.892	1.686	1.686	0.000	0.000	0.000	0.000
78	A	89	ILE	0	-0.017	-0.003	12.478	-1.138	-1.138	0.000	0.000	0.000	0.000
79	A	90	MET	0	0.010	0.002	15.139	0.819	0.819	0.000	0.000	0.000	0.000
80	A	91	TRP	0	0.009	0.005	17.723	-0.487	-0.487	0.000	0.000	0.000	0.000
81	A	92	GLY	0	0.015	0.010	20.385	0.192	0.192	0.000	0.000	0.000	0.000
82	A	93	LYS	1	0.806	0.878	17.526	15.203	15.203	0.000	0.000	0.000	0.000
83	A	94	GLN	0	-0.015	-0.014	16.164	0.958	0.958	0.000	0.000	0.000	0.000
84	A	95	ASP	-1	-0.796	-0.906	15.494	-16.689	-16.689	0.000	0.000	0.000	0.000
85	A	96	SER	0	-0.010	-0.014	11.105	-0.142	-0.142	0.000	0.000	0.000	0.000
86	A	97	GLU	-1	-0.956	-0.977	13.523	-14.046	-14.046	0.000	0.000	0.000	0.000
87	A	98	LYS	0	0.018	-0.002	16.547	0.061	0.061	0.000	0.000	0.000	0.000
88	A	99	ILE	0	0.007	-0.001	13.272	0.385	0.385	0.000	0.000	0.000	0.000
89	A	100	ALA	0	0.001	0.003	14.235	0.006	0.006	0.000	0.000	0.000	0.000
90	A	101	GLN	0	0.016	0.006	15.608	0.582	0.582	0.000	0.000	0.000	0.000
91	A	102	VAL	0	-0.006	0.004	18.396	0.460	0.460	0.000	0.000	0.000	0.000
92	A	103	ILE	0	-0.002	0.003	14.084	0.353	0.353	0.000	0.000	0.000	0.000
93	A	104	LYS	1	0.824	0.907	17.290	12.984	12.984	0.000	0.000	0.000	0.000
94	A	105	SER	0	0.062	0.044	18.907	0.446	0.446	0.000	0.000	0.000	0.000
95	A	106	SER	0	-0.044	-0.034	19.735	0.585	0.585	0.000	0.000	0.000	0.000
96	A	107	LEU	0	-0.008	-0.015	15.953	0.334	0.334	0.000	0.000	0.000	0.000
97	A	108	GLU	-1	-0.870	-0.952	20.632	-11.468	-11.468	0.000	0.000	0.000	0.000
98	A	109	GLU	-1	-0.841	-0.903	23.698	-9.874	-9.874	0.000	0.000	0.000	0.000
99	A	110	ILE	0	-0.035	-0.025	20.787	0.290	0.290	0.000	0.000	0.000	0.000
100	A	111	ALA	0	-0.019	-0.007	23.228	0.334	0.334	0.000	0.000	0.000	0.000
101	A	112	GLU	-1	-0.942	-0.978	25.019	-9.698	-9.698	0.000	0.000	0.000	0.000
102	A	113	GLY	0	-0.028	-0.019	28.154	0.308	0.308	0.000	0.000	0.000	0.000
103	A	114	ILE	0	-0.056	-0.007	26.393	0.187	0.187	0.000	0.000	0.000	0.000
104	A	115	THR	0	-0.011	-0.027	29.423	0.072	0.072	0.000	0.000	0.000	0.000
105	A	116	TRP	0	-0.008	-0.028	29.082	-0.455	-0.455	0.000	0.000	0.000	0.000
106	A	117	GLU	-1	-0.874	-0.951	32.114	-8.410	-8.410	0.000	0.000	0.000	0.000
107	A	118	ASP	-1	-0.859	-0.881	30.262	-8.996	-8.996	0.000	0.000	0.000	0.000
108	A	119	VAL	0	-0.021	-0.013	26.837	-0.378	-0.378	0.000	0.000	0.000	0.000
109	A	120	PRO	0	-0.018	0.008	26.929	0.263	0.263	0.000	0.000	0.000	0.000
110	A	121	GLY	0	0.045	0.013	28.258	-0.327	-0.327	0.000	0.000	0.000	0.000
111	A	122	THR	0	0.024	0.007	28.938	-0.213	-0.213	0.000	0.000	0.000	0.000
112	A	123	THR	0	-0.004	-0.011	31.370	0.129	0.129	0.000	0.000	0.000	0.000
113	A	124	ILE	0	-0.009	-0.013	33.095	-0.248	-0.248	0.000	0.000	0.000	0.000
114	A	125	GLU	-1	-0.877	-0.923	34.543	-8.152	-8.152	0.000	0.000	0.000	0.000
115	A	126	SER	0	-0.067	-0.048	32.256	-0.179	-0.179	0.000	0.000	0.000	0.000
116	A	127	CYS	-1	-0.895	-0.879	27.361	-11.275	-11.275	0.000	0.000	0.000	0.000
117	A	128	GLY	0	0.002	0.008	28.137	0.248	0.248	0.000	0.000	0.000	0.000
118	A	129	ASN	0	-0.049	-0.057	25.809	0.430	0.430	0.000	0.000	0.000	0.000
119	A	130	TYR	0	0.021	0.017	27.937	-0.118	-0.118	0.000	0.000	0.000	0.000
120	A	131	LYS	1	0.944	0.970	30.181	9.366	9.366	0.000	0.000	0.000	0.000
121	A	132	ASP	-1	-0.884	-0.916	24.272	-11.847	-11.847	0.000	0.000	0.000	0.000
122	A	133	HIS	0	0.034	-0.002	25.192	-0.573	-0.573	0.000	0.000	0.000	0.000
123	A	134	SER	0	-0.034	-0.023	25.518	0.395	0.395	0.000	0.000	0.000	0.000
124	A	135	LEU	0	0.058	0.036	25.522	-0.390	-0.390	0.000	0.000	0.000	0.000
125	A	136	HIS	0	0.011	0.014	26.684	0.003	0.003	0.000	0.000	0.000	0.000
126	A	137	SER	0	-0.012	-0.032	22.512	-0.255	-0.255	0.000	0.000	0.000	0.000
127	A	138	ALA	0	0.021	0.003	21.977	-0.386	-0.386	0.000	0.000	0.000	0.000
128	A	139	LYS	1	0.818	0.906	22.313	9.627	9.627	0.000	0.000	0.000	0.000
129	A	140	GLU	-1	-0.881	-0.915	23.865	-10.565	-10.565	0.000	0.000	0.000	0.000
130	A	141	TRP	0	-0.018	-0.030	16.179	-0.663	-0.663	0.000	0.000	0.000	0.000
131	A	142	ALA	0	-0.006	0.004	18.969	-0.496	-0.496	0.000	0.000	0.000	0.000
132	A	143	LYS	1	0.885	0.922	20.102	10.387	10.387	0.000	0.000	0.000	0.000
133	A	144	LEU	0	-0.039	0.000	17.622	-0.087	-0.087	0.000	0.000	0.000	0.000
134	A	145	ILE	0	0.013	0.005	14.422	-0.331	-0.331	0.000	0.000	0.000	0.000
135	A	146	LEU	0	-0.009	-0.009	16.643	-0.405	-0.405	0.000	0.000	0.000	0.000
136	A	147	SER	0	-0.112	-0.060	19.175	0.119	0.119	0.000	0.000	0.000	0.000
137	A	148	GLN	0	-0.022	-0.010	14.775	-0.435	-0.435	0.000	0.000	0.000	0.000
138	A	149	GLY	0	0.029	0.027	16.153	-0.319	-0.319	0.000	0.000	0.000	0.000
139	A	150	ILE	0	-0.006	-0.003	12.756	-1.048	-1.048	0.000	0.000	0.000	0.000
140	A	151	SER	0	-0.013	-0.020	10.466	1.278	1.278	0.000	0.000	0.000	0.000
141	A	152	THR	0	0.047	0.005	11.413	-1.124	-1.124	0.000	0.000	0.000	0.000
142	A	153	ASP	-1	-0.835	-0.913	8.191	-27.213	-27.213	0.000	0.000	0.000	0.000
145	A	156	GLU	-1	-0.930	-0.966	6.979	-16.874	-16.874	0.000	0.000	0.000	0.000
146	A	157	ARG	1	0.779	0.874	10.683	18.726	18.726	0.000	0.000	0.000	0.000
147	A	158	LYS	1	0.908	0.954	12.325	18.960	18.960	0.000	0.000	0.000	0.000
148	A	159	PRO	0	-0.014	-0.014	14.447	-0.422	-0.422	0.000	0.000	0.000	0.000
149	A	160	ILE	-1	-0.805	-0.865	16.379	-12.887	-12.887	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:LEU)