FMO DATABASE

FMODB ID: Y1MZ2

Calculation Name: 4S1J-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4S1J

Chain ID: A

ChEMBL ID:

UniProt ID: E9B8M3

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	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1686722.082157
FMO2-HF: Nuclear repulsion	1623030.946459
FMO2-HF: Total energy	-63691.135697
FMO2-MP2: Total energy	-63877.622661

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:22:GLU)

Summations of interaction energy for fragment #1(A:22:GLU)

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.
-17.98	-14.363	1.888	-2.212	-3.294	0.005

Interaction energy analysis for fragmet #1(A:22:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.104 / q_NPA : -0.062

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	24	GLU	-1	-0.840	-0.915	3.205	-5.991	-4.099	0.067	-1.003	-0.957	-0.004
27	A	48	PHE	0	-0.012	-0.015	4.621	-1.067	-0.937	-0.001	-0.015	-0.114	0.000
95	A	116	PHE	0	-0.059	-0.028	3.992	0.334	1.133	0.026	-0.208	-0.618	-0.002
132	A	153	LYS	1	0.891	0.955	1.903	-12.787	-11.991	1.796	-0.986	-1.605	0.011
4	A	25	VAL	0	-0.062	-0.020	5.720	1.077	1.077	0.000	0.000	0.000	0.000
5	A	26	THR	0	0.001	0.003	7.810	0.235	0.235	0.000	0.000	0.000	0.000
6	A	27	ALA	0	0.024	0.024	11.416	0.326	0.326	0.000	0.000	0.000	0.000
7	A	28	LYS	1	0.945	0.963	11.555	0.055	0.055	0.000	0.000	0.000	0.000
8	A	29	VAL	0	0.055	0.033	13.918	-0.030	-0.030	0.000	0.000	0.000	0.000
9	A	30	TYR	0	-0.039	-0.011	15.400	0.176	0.176	0.000	0.000	0.000	0.000
10	A	31	PHE	0	0.003	-0.007	17.230	-0.099	-0.099	0.000	0.000	0.000	0.000
11	A	32	ASP	-1	-0.785	-0.849	19.922	0.506	0.506	0.000	0.000	0.000	0.000
12	A	33	ALA	0	0.014	0.000	21.619	-0.057	-0.057	0.000	0.000	0.000	0.000
13	A	34	MET	0	-0.036	-0.012	23.590	0.008	0.008	0.000	0.000	0.000	0.000
14	A	35	ILE	0	-0.019	-0.010	25.158	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	36	ASP	-1	-0.847	-0.918	28.854	0.329	0.329	0.000	0.000	0.000	0.000
16	A	37	SER	0	-0.041	-0.023	32.675	0.008	0.008	0.000	0.000	0.000	0.000
17	A	38	GLU	-1	-0.769	-0.859	28.074	0.622	0.622	0.000	0.000	0.000	0.000
18	A	39	PRO	0	-0.036	-0.020	27.669	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	40	LEU	0	-0.028	-0.030	22.455	0.050	0.050	0.000	0.000	0.000	0.000
20	A	41	GLY	0	0.040	0.020	21.831	0.100	0.100	0.000	0.000	0.000	0.000
21	A	42	ARG	1	0.822	0.879	18.323	-0.486	-0.486	0.000	0.000	0.000	0.000
22	A	43	ILE	0	-0.015	-0.002	14.556	0.160	0.160	0.000	0.000	0.000	0.000
23	A	44	THR	0	0.014	0.001	13.362	-0.306	-0.306	0.000	0.000	0.000	0.000
24	A	45	ILE	0	-0.002	-0.005	11.167	0.405	0.405	0.000	0.000	0.000	0.000
25	A	46	GLY	0	0.005	-0.007	8.816	-0.150	-0.150	0.000	0.000	0.000	0.000
26	A	47	LEU	0	-0.006	-0.009	8.747	-0.137	-0.137	0.000	0.000	0.000	0.000
28	A	49	GLY	0	0.041	0.019	8.637	-0.057	-0.057	0.000	0.000	0.000	0.000
29	A	50	LYS	1	0.815	0.903	9.845	6.014	6.014	0.000	0.000	0.000	0.000
30	A	51	ASP	-1	-0.917	-0.962	7.546	-8.947	-8.947	0.000	0.000	0.000	0.000
31	A	52	ALA	0	0.013	0.000	10.355	0.329	0.329	0.000	0.000	0.000	0.000
32	A	53	PRO	0	0.042	0.049	12.810	0.288	0.288	0.000	0.000	0.000	0.000
33	A	54	LEU	0	0.004	0.004	15.572	0.238	0.238	0.000	0.000	0.000	0.000
34	A	55	THR	0	-0.022	-0.048	14.419	0.264	0.264	0.000	0.000	0.000	0.000
35	A	56	THR	0	-0.059	-0.043	11.560	0.233	0.233	0.000	0.000	0.000	0.000
36	A	57	GLU	-1	-0.771	-0.871	14.756	-0.885	-0.885	0.000	0.000	0.000	0.000
37	A	58	ASN	0	0.002	-0.003	18.231	0.223	0.223	0.000	0.000	0.000	0.000
38	A	59	PHE	0	0.019	-0.007	15.197	0.136	0.136	0.000	0.000	0.000	0.000
39	A	60	ARG	1	0.770	0.851	16.786	0.925	0.925	0.000	0.000	0.000	0.000
40	A	61	GLN	0	0.006	-0.001	18.308	0.183	0.183	0.000	0.000	0.000	0.000
41	A	62	LEU	0	-0.032	0.001	21.017	0.099	0.099	0.000	0.000	0.000	0.000
42	A	63	CYS	0	-0.074	-0.025	18.439	0.129	0.129	0.000	0.000	0.000	0.000
43	A	64	THR	0	-0.037	-0.036	21.013	0.090	0.090	0.000	0.000	0.000	0.000
44	A	65	GLY	0	-0.007	0.011	23.541	0.048	0.048	0.000	0.000	0.000	0.000
45	A	66	GLU	-1	-0.831	-0.897	23.691	-0.542	-0.542	0.000	0.000	0.000	0.000
46	A	67	HIS	0	-0.037	-0.027	25.524	0.042	0.042	0.000	0.000	0.000	0.000
47	A	68	GLY	0	-0.014	-0.003	29.330	0.018	0.018	0.000	0.000	0.000	0.000
48	A	69	PHE	0	-0.037	-0.036	26.954	0.036	0.036	0.000	0.000	0.000	0.000
49	A	70	GLY	0	0.047	0.011	24.985	-0.051	-0.051	0.000	0.000	0.000	0.000
50	A	71	TYR	0	-0.056	-0.045	19.100	0.031	0.031	0.000	0.000	0.000	0.000
51	A	72	LYS	1	0.879	0.949	23.969	0.003	0.003	0.000	0.000	0.000	0.000
52	A	73	ASP	-1	-0.832	-0.908	26.368	0.074	0.074	0.000	0.000	0.000	0.000
53	A	74	SER	0	-0.027	-0.013	24.722	0.011	0.011	0.000	0.000	0.000	0.000
54	A	75	ILE	0	-0.010	-0.025	25.548	0.045	0.045	0.000	0.000	0.000	0.000
55	A	76	PHE	0	0.008	-0.003	18.202	-0.026	-0.026	0.000	0.000	0.000	0.000
56	A	77	HIS	0	-0.008	0.012	23.428	0.060	0.060	0.000	0.000	0.000	0.000
57	A	78	ARG	1	0.819	0.894	23.500	-0.338	-0.338	0.000	0.000	0.000	0.000
58	A	79	VAL	0	-0.001	0.003	21.704	0.038	0.038	0.000	0.000	0.000	0.000
59	A	80	ILE	0	0.003	0.003	20.764	-0.046	-0.046	0.000	0.000	0.000	0.000
60	A	81	PRO	0	0.022	0.006	20.007	0.111	0.111	0.000	0.000	0.000	0.000
61	A	82	ASN	0	-0.060	-0.041	18.127	0.055	0.055	0.000	0.000	0.000	0.000
62	A	83	PHE	0	-0.009	-0.008	16.236	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	84	MET	0	-0.016	0.005	15.330	0.099	0.099	0.000	0.000	0.000	0.000
64	A	85	ILE	0	-0.008	0.013	16.684	-0.072	-0.072	0.000	0.000	0.000	0.000
65	A	86	GLN	0	0.023	-0.005	17.527	0.020	0.020	0.000	0.000	0.000	0.000
66	A	87	GLY	0	0.037	0.009	19.999	0.043	0.043	0.000	0.000	0.000	0.000
67	A	88	GLY	0	0.050	0.018	21.471	-0.070	-0.070	0.000	0.000	0.000	0.000
68	A	89	ASP	-1	-0.749	-0.860	22.836	-0.109	-0.109	0.000	0.000	0.000	0.000
69	A	90	PHE	0	0.013	-0.005	24.384	0.040	0.040	0.000	0.000	0.000	0.000
70	A	91	THR	0	-0.065	-0.044	28.563	-0.020	-0.020	0.000	0.000	0.000	0.000
71	A	92	ASN	0	-0.028	0.000	30.588	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	93	PHE	0	-0.048	-0.018	29.001	0.024	0.024	0.000	0.000	0.000	0.000
73	A	94	ASP	-1	-0.815	-0.888	29.674	0.063	0.063	0.000	0.000	0.000	0.000
74	A	95	GLY	0	-0.033	-0.016	26.426	0.032	0.032	0.000	0.000	0.000	0.000
75	A	96	THR	0	-0.112	-0.078	27.227	-0.041	-0.041	0.000	0.000	0.000	0.000
76	A	97	GLY	0	0.009	0.015	29.176	-0.035	-0.035	0.000	0.000	0.000	0.000
77	A	98	GLY	0	-0.017	-0.013	26.218	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	99	LYS	1	0.823	0.927	26.357	0.262	0.262	0.000	0.000	0.000	0.000
79	A	100	SER	0	-0.026	-0.018	23.443	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	101	ILE	0	0.007	0.002	22.463	0.053	0.053	0.000	0.000	0.000	0.000
81	A	102	TYR	0	-0.055	-0.040	20.124	0.019	0.019	0.000	0.000	0.000	0.000
82	A	103	GLY	0	0.017	0.016	26.729	0.018	0.018	0.000	0.000	0.000	0.000
83	A	104	GLU	-1	-0.938	-0.962	27.770	-0.350	-0.350	0.000	0.000	0.000	0.000
84	A	105	LYS	1	0.891	0.949	25.267	0.363	0.363	0.000	0.000	0.000	0.000
85	A	106	PHE	0	-0.008	-0.002	18.119	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	107	ALA	0	0.039	0.004	21.316	0.022	0.022	0.000	0.000	0.000	0.000
87	A	108	ASP	-1	-0.814	-0.897	17.082	-1.086	-1.086	0.000	0.000	0.000	0.000
88	A	109	GLU	-1	-0.769	-0.844	14.827	-2.089	-2.089	0.000	0.000	0.000	0.000
89	A	110	ASN	0	-0.014	-0.026	9.506	0.085	0.085	0.000	0.000	0.000	0.000
90	A	111	LEU	0	0.005	0.010	12.061	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	112	LYS	1	0.931	0.955	10.570	3.173	3.173	0.000	0.000	0.000	0.000
92	A	113	VAL	0	-0.012	0.012	4.967	-0.597	-0.597	0.000	0.000	0.000	0.000
93	A	114	LYS	1	0.931	0.974	6.709	0.463	0.463	0.000	0.000	0.000	0.000
94	A	115	HIS	0	0.017	-0.009	6.651	-0.282	-0.282	0.000	0.000	0.000	0.000
96	A	117	VAL	0	0.008	0.013	7.273	-0.778	-0.778	0.000	0.000	0.000	0.000
97	A	118	GLY	0	0.064	0.024	7.401	1.413	1.413	0.000	0.000	0.000	0.000
98	A	119	ALA	0	-0.052	-0.007	6.662	-0.499	-0.499	0.000	0.000	0.000	0.000
99	A	120	LEU	0	-0.005	0.004	8.038	0.068	0.068	0.000	0.000	0.000	0.000
100	A	121	SER	0	-0.018	-0.033	10.468	-0.660	-0.660	0.000	0.000	0.000	0.000
101	A	122	MET	0	0.014	0.029	12.851	0.206	0.206	0.000	0.000	0.000	0.000
102	A	123	ALA	0	-0.030	-0.016	16.437	0.045	0.045	0.000	0.000	0.000	0.000
103	A	124	ASN	0	-0.057	-0.032	18.765	0.028	0.028	0.000	0.000	0.000	0.000
104	A	125	ALA	0	0.018	0.003	21.742	0.080	0.080	0.000	0.000	0.000	0.000
105	A	126	GLY	0	0.021	0.017	23.156	0.014	0.014	0.000	0.000	0.000	0.000
106	A	127	PRO	0	-0.008	-0.001	21.392	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	128	ASN	0	-0.035	-0.032	21.260	-0.038	-0.038	0.000	0.000	0.000	0.000
108	A	129	THR	0	0.002	0.003	22.574	0.058	0.058	0.000	0.000	0.000	0.000
109	A	130	ASN	0	-0.032	-0.020	18.468	0.148	0.148	0.000	0.000	0.000	0.000
110	A	131	GLY	0	0.070	0.023	21.345	0.003	0.003	0.000	0.000	0.000	0.000
111	A	132	SER	0	0.022	0.012	21.658	-0.075	-0.075	0.000	0.000	0.000	0.000
112	A	133	GLN	0	-0.059	-0.036	21.055	0.078	0.078	0.000	0.000	0.000	0.000
113	A	134	PHE	0	0.000	0.007	15.915	-0.104	-0.104	0.000	0.000	0.000	0.000
114	A	135	PHE	0	-0.019	-0.016	13.812	0.112	0.112	0.000	0.000	0.000	0.000
115	A	136	ILE	0	0.012	0.010	11.850	-0.120	-0.120	0.000	0.000	0.000	0.000
116	A	137	THR	0	-0.009	-0.010	9.942	-0.216	-0.216	0.000	0.000	0.000	0.000
117	A	138	THR	0	-0.050	-0.064	11.536	0.493	0.493	0.000	0.000	0.000	0.000
118	A	139	ALA	0	0.014	0.019	13.320	0.323	0.323	0.000	0.000	0.000	0.000
119	A	140	PRO	0	-0.007	-0.019	11.016	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	141	THR	0	0.038	0.021	11.727	-0.243	-0.243	0.000	0.000	0.000	0.000
121	A	142	PRO	0	0.012	0.014	13.498	-0.297	-0.297	0.000	0.000	0.000	0.000
122	A	143	TRP	0	-0.015	-0.017	14.367	-0.236	-0.236	0.000	0.000	0.000	0.000
123	A	144	LEU	0	-0.017	-0.004	14.192	-0.127	-0.127	0.000	0.000	0.000	0.000
124	A	145	ASP	-1	-0.752	-0.873	11.163	-0.264	-0.264	0.000	0.000	0.000	0.000
125	A	146	GLY	0	0.005	0.009	12.928	0.138	0.138	0.000	0.000	0.000	0.000
126	A	147	ARG	1	0.834	0.907	14.872	0.316	0.316	0.000	0.000	0.000	0.000
127	A	148	HIS	1	0.857	0.938	14.567	0.569	0.569	0.000	0.000	0.000	0.000
128	A	149	VAL	0	0.016	0.031	12.499	-0.159	-0.159	0.000	0.000	0.000	0.000
129	A	150	VAL	0	0.010	0.008	7.224	0.270	0.270	0.000	0.000	0.000	0.000
130	A	151	PHE	0	-0.003	-0.006	9.084	-0.857	-0.857	0.000	0.000	0.000	0.000
131	A	152	GLY	0	0.066	0.016	7.851	-0.303	-0.303	0.000	0.000	0.000	0.000
133	A	154	VAL	0	0.017	0.006	7.545	-0.392	-0.392	0.000	0.000	0.000	0.000
134	A	155	LEU	0	-0.119	-0.057	7.103	0.917	0.917	0.000	0.000	0.000	0.000
135	A	156	ASP	-1	-0.867	-0.944	9.525	2.010	2.010	0.000	0.000	0.000	0.000
136	A	157	GLY	0	0.092	0.060	12.940	-0.218	-0.218	0.000	0.000	0.000	0.000
137	A	158	MET	0	-0.057	-0.025	11.389	-0.129	-0.129	0.000	0.000	0.000	0.000
138	A	159	ASP	-1	-0.862	-0.944	13.769	1.608	1.608	0.000	0.000	0.000	0.000
139	A	160	VAL	0	0.022	0.021	17.201	-0.140	-0.140	0.000	0.000	0.000	0.000
140	A	161	VAL	0	0.013	0.002	14.077	-0.132	-0.132	0.000	0.000	0.000	0.000
141	A	162	LEU	0	-0.018	-0.013	14.759	-0.120	-0.120	0.000	0.000	0.000	0.000
142	A	163	ARG	1	0.834	0.910	17.972	-0.926	-0.926	0.000	0.000	0.000	0.000
143	A	164	ILE	0	-0.006	-0.003	19.281	-0.111	-0.111	0.000	0.000	0.000	0.000
144	A	165	GLU	-1	-0.790	-0.857	18.314	1.527	1.527	0.000	0.000	0.000	0.000
145	A	166	LYS	1	0.770	0.873	19.622	-1.507	-1.507	0.000	0.000	0.000	0.000
146	A	167	THR	0	-0.002	0.017	24.126	-0.077	-0.077	0.000	0.000	0.000	0.000
147	A	168	LYS	1	0.964	0.981	26.437	-0.458	-0.458	0.000	0.000	0.000	0.000
148	A	169	THR	0	0.011	0.025	26.312	-0.041	-0.041	0.000	0.000	0.000	0.000
149	A	170	ASN	0	-0.008	-0.005	29.576	-0.022	-0.022	0.000	0.000	0.000	0.000
150	A	171	SER	0	0.025	-0.016	31.158	0.015	0.015	0.000	0.000	0.000	0.000
151	A	172	HIS	0	0.001	0.006	30.043	0.003	0.003	0.000	0.000	0.000	0.000
152	A	173	ASP	-1	-0.824	-0.886	25.755	0.417	0.417	0.000	0.000	0.000	0.000
153	A	174	ARG	1	0.974	0.997	26.270	-0.205	-0.205	0.000	0.000	0.000	0.000
154	A	175	PRO	0	0.000	-0.013	26.163	0.009	0.009	0.000	0.000	0.000	0.000
155	A	176	VAL	0	-0.060	-0.030	28.933	-0.043	-0.043	0.000	0.000	0.000	0.000
156	A	177	LYS	1	0.823	0.905	30.828	-0.365	-0.365	0.000	0.000	0.000	0.000
157	A	178	PRO	0	0.011	-0.001	29.333	0.036	0.036	0.000	0.000	0.000	0.000
158	A	179	VAL	0	0.047	0.025	23.049	0.009	0.009	0.000	0.000	0.000	0.000
159	A	180	LYS	1	0.840	0.935	25.252	-0.186	-0.186	0.000	0.000	0.000	0.000
160	A	181	ILE	0	0.027	0.026	21.107	0.060	0.060	0.000	0.000	0.000	0.000
161	A	182	VAL	0	-0.019	-0.020	24.570	-0.061	-0.061	0.000	0.000	0.000	0.000
162	A	183	ALA	0	-0.034	-0.021	25.308	-0.052	-0.052	0.000	0.000	0.000	0.000
163	A	184	SER	0	-0.022	-0.027	21.488	0.070	0.070	0.000	0.000	0.000	0.000
164	A	185	GLY	0	0.020	0.019	20.768	-0.019	-0.019	0.000	0.000	0.000	0.000
165	A	186	GLU	-1	-0.847	-0.908	18.294	-0.705	-0.705	0.000	0.000	0.000	0.000
166	A	187	LEU	-1	-0.958	-0.973	16.348	-0.141	-0.141	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:GLU)