FMO DATABASE

FMODB ID: 97LM2

Calculation Name: 3S02-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3S02

Chain ID: A

ChEMBL ID:

UniProt ID: P56427

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1322262.599573
FMO2-HF: Nuclear repulsion	1263936.61946
FMO2-HF: Total energy	-58325.980113
FMO2-MP2: Total energy	-58496.803095

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:106:SER)

Summations of interaction energy for fragment #1(A:106: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.
-3.818	-0.18599999999999	10.359	-7.115	-6.875	-0.053

Interaction energy analysis for fragmet #1(A:106:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.816 / q_NPA : 0.893

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	108	LEU	0	0.008	0.017	2.303	3.048	5.390	2.386	-2.026	-2.701	0.012
4	A	109	GLU	-1	-0.859	-0.915	1.899	-79.861	-78.759	7.975	-5.065	-4.012	-0.065
5	A	110	GLN	0	0.005	-0.008	4.788	4.220	4.291	-0.001	-0.012	-0.058	0.000
13	A	118	LYS	1	0.840	0.910	4.773	53.330	53.447	-0.001	-0.012	-0.104	0.000
6	A	111	ILE	0	0.009	0.008	8.032	-0.400	-0.400	0.000	0.000	0.000	0.000
7	A	112	ASP	-1	-0.870	-0.938	11.580	-19.116	-19.116	0.000	0.000	0.000	0.000
8	A	113	GLN	0	-0.029	-0.013	14.658	1.374	1.374	0.000	0.000	0.000	0.000
9	A	114	GLY	0	-0.006	-0.005	13.123	0.816	0.816	0.000	0.000	0.000	0.000
10	A	115	SER	0	-0.055	-0.015	8.236	-1.904	-1.904	0.000	0.000	0.000	0.000
11	A	116	ILE	0	0.002	-0.002	7.396	2.384	2.384	0.000	0.000	0.000	0.000
12	A	117	LEU	0	0.000	0.004	6.172	-5.514	-5.514	0.000	0.000	0.000	0.000
14	A	119	LEU	0	0.016	0.000	7.411	-3.493	-3.493	0.000	0.000	0.000	0.000
15	A	120	PRO	0	0.054	0.020	8.412	2.051	2.051	0.000	0.000	0.000	0.000
16	A	121	SER	0	0.035	0.009	11.124	1.270	1.270	0.000	0.000	0.000	0.000
17	A	122	ASN	0	-0.028	-0.023	13.410	0.923	0.923	0.000	0.000	0.000	0.000
18	A	123	LEU	0	-0.005	0.003	10.515	-0.080	-0.080	0.000	0.000	0.000	0.000
19	A	124	LEU	0	-0.009	0.003	14.011	1.135	1.135	0.000	0.000	0.000	0.000
20	A	125	PHE	0	-0.019	-0.008	16.288	0.916	0.916	0.000	0.000	0.000	0.000
21	A	126	GLU	-1	-0.832	-0.900	19.329	-12.644	-12.644	0.000	0.000	0.000	0.000
22	A	127	ASN	0	-0.013	-0.020	21.492	0.201	0.201	0.000	0.000	0.000	0.000
23	A	128	ALA	0	0.026	0.005	20.574	-0.370	-0.370	0.000	0.000	0.000	0.000
24	A	129	THR	0	-0.009	-0.006	21.643	-0.183	-0.183	0.000	0.000	0.000	0.000
25	A	130	SER	0	-0.045	-0.006	23.377	0.389	0.389	0.000	0.000	0.000	0.000
26	A	131	ASP	-1	-0.814	-0.908	22.430	-13.047	-13.047	0.000	0.000	0.000	0.000
27	A	132	ALA	0	-0.008	0.009	23.488	-0.141	-0.141	0.000	0.000	0.000	0.000
28	A	133	ILE	0	-0.025	-0.027	19.059	-0.479	-0.479	0.000	0.000	0.000	0.000
29	A	134	ASN	0	0.005	-0.004	18.047	1.463	1.463	0.000	0.000	0.000	0.000
30	A	135	GLN	0	0.032	-0.013	20.027	-0.605	-0.605	0.000	0.000	0.000	0.000
31	A	136	ASP	-1	-0.895	-0.944	17.797	-16.670	-16.670	0.000	0.000	0.000	0.000
32	A	137	MET	0	-0.017	-0.009	13.808	-1.643	-1.643	0.000	0.000	0.000	0.000
33	A	138	MET	0	-0.006	0.015	16.945	-0.653	-0.653	0.000	0.000	0.000	0.000
34	A	139	LEU	0	0.035	0.009	19.027	-0.158	-0.158	0.000	0.000	0.000	0.000
35	A	140	TYR	0	-0.017	-0.005	8.583	-1.012	-1.012	0.000	0.000	0.000	0.000
36	A	141	ILE	0	0.015	0.000	14.477	-0.885	-0.885	0.000	0.000	0.000	0.000
37	A	142	GLU	-1	-0.808	-0.896	16.548	-13.579	-13.579	0.000	0.000	0.000	0.000
38	A	143	ARG	1	0.903	0.955	10.982	22.550	22.550	0.000	0.000	0.000	0.000
39	A	144	ILE	0	-0.006	-0.002	11.657	-0.347	-0.347	0.000	0.000	0.000	0.000
40	A	145	ALA	0	0.034	0.016	14.247	0.191	0.191	0.000	0.000	0.000	0.000
41	A	146	LYS	1	0.816	0.895	17.681	14.152	14.152	0.000	0.000	0.000	0.000
42	A	147	ILE	0	-0.044	-0.015	12.123	0.473	0.473	0.000	0.000	0.000	0.000
43	A	148	ILE	0	0.052	0.026	14.970	0.109	0.109	0.000	0.000	0.000	0.000
44	A	149	GLN	0	0.005	-0.005	16.751	0.353	0.353	0.000	0.000	0.000	0.000
45	A	150	LYS	1	0.855	0.933	17.039	14.512	14.512	0.000	0.000	0.000	0.000
46	A	151	LEU	0	0.009	0.029	13.314	-0.280	-0.280	0.000	0.000	0.000	0.000
47	A	152	PRO	0	-0.009	-0.014	17.147	0.875	0.875	0.000	0.000	0.000	0.000
48	A	153	LYS	1	0.967	0.954	20.115	10.838	10.838	0.000	0.000	0.000	0.000
49	A	154	ARG	1	0.988	1.013	21.994	12.499	12.499	0.000	0.000	0.000	0.000
50	A	155	VAL	0	-0.027	0.005	16.080	-0.203	-0.203	0.000	0.000	0.000	0.000
51	A	156	HIS	0	0.033	0.009	18.655	0.843	0.843	0.000	0.000	0.000	0.000
52	A	157	ILE	0	-0.015	-0.014	14.899	-1.069	-1.069	0.000	0.000	0.000	0.000
53	A	158	ASN	0	-0.033	-0.027	16.203	0.225	0.225	0.000	0.000	0.000	0.000
54	A	159	VAL	0	0.015	0.009	15.622	-1.474	-1.474	0.000	0.000	0.000	0.000
55	A	160	ARG	1	0.906	0.955	13.851	21.744	21.744	0.000	0.000	0.000	0.000
56	A	161	GLY	0	0.028	0.019	15.549	-1.310	-1.310	0.000	0.000	0.000	0.000
57	A	162	PHE	0	-0.014	-0.017	13.964	0.565	0.565	0.000	0.000	0.000	0.000
58	A	163	THR	0	-0.049	-0.050	16.586	-0.043	-0.043	0.000	0.000	0.000	0.000
59	A	164	ASP	-1	-0.773	-0.845	17.687	-16.672	-16.672	0.000	0.000	0.000	0.000
60	A	165	ASP	-1	-0.829	-0.922	18.819	-14.074	-14.074	0.000	0.000	0.000	0.000
61	A	166	THR	0	-0.046	-0.036	21.522	0.809	0.809	0.000	0.000	0.000	0.000
62	A	167	PRO	0	-0.017	-0.013	24.018	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	168	LEU	0	-0.010	0.007	24.476	-0.066	-0.066	0.000	0.000	0.000	0.000
64	A	169	VAL	0	0.029	0.004	27.900	0.494	0.494	0.000	0.000	0.000	0.000
65	A	170	LYS	1	0.918	0.958	29.506	10.328	10.328	0.000	0.000	0.000	0.000
66	A	171	THR	0	0.042	0.022	27.836	-0.088	-0.088	0.000	0.000	0.000	0.000
67	A	172	ARG	1	0.954	0.984	29.194	10.981	10.981	0.000	0.000	0.000	0.000
68	A	173	PHE	0	-0.093	-0.034	26.048	0.136	0.136	0.000	0.000	0.000	0.000
69	A	174	LYS	1	0.937	0.944	29.761	9.838	9.838	0.000	0.000	0.000	0.000
70	A	175	SER	0	0.024	0.010	27.877	-0.033	-0.033	0.000	0.000	0.000	0.000
71	A	176	HIS	0	0.049	0.013	22.553	0.115	0.115	0.000	0.000	0.000	0.000
72	A	177	TYR	0	0.042	0.029	23.237	-0.333	-0.333	0.000	0.000	0.000	0.000
73	A	178	GLU	-1	-0.825	-0.879	24.558	-10.748	-10.748	0.000	0.000	0.000	0.000
74	A	179	LEU	0	0.021	0.024	22.100	-0.077	-0.077	0.000	0.000	0.000	0.000
75	A	180	ALA	0	0.012	0.008	20.076	-0.354	-0.354	0.000	0.000	0.000	0.000
76	A	181	ALA	0	0.011	0.008	20.971	-0.488	-0.488	0.000	0.000	0.000	0.000
77	A	182	ASN	0	-0.056	-0.042	23.528	0.294	0.294	0.000	0.000	0.000	0.000
78	A	183	ARG	1	0.874	0.936	18.458	16.089	16.089	0.000	0.000	0.000	0.000
79	A	184	ALA	0	0.004	0.008	19.199	-0.432	-0.432	0.000	0.000	0.000	0.000
80	A	185	TYR	0	-0.003	-0.001	20.176	0.097	0.097	0.000	0.000	0.000	0.000
81	A	186	ARG	1	0.849	0.916	22.187	12.430	12.430	0.000	0.000	0.000	0.000
82	A	187	VAL	0	0.057	0.025	16.162	0.157	0.157	0.000	0.000	0.000	0.000
83	A	188	MET	0	-0.017	0.011	19.611	0.037	0.037	0.000	0.000	0.000	0.000
84	A	189	LYS	1	0.923	0.951	20.835	11.669	11.669	0.000	0.000	0.000	0.000
85	A	190	VAL	0	0.019	0.012	20.494	0.354	0.354	0.000	0.000	0.000	0.000
86	A	191	LEU	0	-0.003	-0.008	16.158	0.036	0.036	0.000	0.000	0.000	0.000
87	A	192	ILE	0	-0.012	0.004	20.317	0.343	0.343	0.000	0.000	0.000	0.000
88	A	193	GLN	0	-0.059	-0.027	23.942	0.400	0.400	0.000	0.000	0.000	0.000
89	A	194	TYR	0	-0.013	-0.008	20.498	0.245	0.245	0.000	0.000	0.000	0.000
90	A	195	GLY	0	0.015	0.007	22.465	-0.208	-0.208	0.000	0.000	0.000	0.000
91	A	196	VAL	0	-0.052	-0.015	18.861	0.051	0.051	0.000	0.000	0.000	0.000
92	A	197	ASN	0	0.042	0.014	22.178	0.632	0.632	0.000	0.000	0.000	0.000
93	A	198	PRO	0	0.031	-0.003	23.627	-0.398	-0.398	0.000	0.000	0.000	0.000
94	A	199	ASN	0	-0.060	-0.025	25.202	-0.036	-0.036	0.000	0.000	0.000	0.000
95	A	200	GLN	0	-0.028	0.000	20.991	0.373	0.373	0.000	0.000	0.000	0.000
96	A	201	LEU	0	0.002	0.005	18.763	-0.869	-0.869	0.000	0.000	0.000	0.000
97	A	202	SER	0	0.025	0.018	20.535	0.400	0.400	0.000	0.000	0.000	0.000
98	A	203	PHE	0	-0.011	-0.013	20.153	-0.788	-0.788	0.000	0.000	0.000	0.000
99	A	204	SER	0	0.029	0.025	19.218	0.880	0.880	0.000	0.000	0.000	0.000
100	A	205	SER	0	-0.076	-0.061	20.228	-0.789	-0.789	0.000	0.000	0.000	0.000
101	A	206	TYR	0	0.074	0.042	17.406	0.324	0.324	0.000	0.000	0.000	0.000
102	A	207	GLY	0	0.000	0.012	20.185	0.491	0.491	0.000	0.000	0.000	0.000
103	A	208	SER	0	-0.016	0.004	19.276	-0.826	-0.826	0.000	0.000	0.000	0.000
104	A	209	THR	0	-0.066	-0.043	20.319	-0.085	-0.085	0.000	0.000	0.000	0.000
105	A	210	ASN	0	-0.032	-0.025	15.814	0.005	0.005	0.000	0.000	0.000	0.000
106	A	211	PRO	0	0.009	0.014	15.275	-1.128	-1.128	0.000	0.000	0.000	0.000
107	A	212	ILE	0	-0.035	-0.012	8.248	-1.054	-1.054	0.000	0.000	0.000	0.000
108	A	213	ALA	0	-0.018	-0.007	12.202	-0.485	-0.485	0.000	0.000	0.000	0.000
109	A	214	PRO	0	0.051	0.037	14.226	0.622	0.622	0.000	0.000	0.000	0.000
110	A	215	ASN	0	0.002	-0.006	17.502	-1.542	-1.542	0.000	0.000	0.000	0.000
111	A	216	ASP	-1	-0.824	-0.908	18.716	-15.916	-15.916	0.000	0.000	0.000	0.000
112	A	217	SER	0	-0.013	-0.032	16.366	0.366	0.366	0.000	0.000	0.000	0.000
113	A	218	LEU	0	0.005	0.003	17.410	0.061	0.061	0.000	0.000	0.000	0.000
114	A	219	GLU	-1	-0.825	-0.907	12.634	-19.251	-19.251	0.000	0.000	0.000	0.000
115	A	220	ASN	0	-0.050	-0.043	12.656	-3.623	-3.623	0.000	0.000	0.000	0.000
116	A	221	ARG	1	0.877	0.949	14.047	14.433	14.433	0.000	0.000	0.000	0.000
117	A	222	MET	0	-0.006	0.004	11.169	0.029	0.029	0.000	0.000	0.000	0.000
118	A	223	LYS	1	0.898	0.955	8.311	30.592	30.592	0.000	0.000	0.000	0.000
119	A	224	ASN	0	-0.023	-0.024	10.945	-2.731	-2.731	0.000	0.000	0.000	0.000
120	A	225	ASN	0	-0.029	-0.035	13.744	0.542	0.542	0.000	0.000	0.000	0.000
121	A	226	ARG	1	0.808	0.910	9.639	25.423	25.423	0.000	0.000	0.000	0.000
122	A	227	VAL	0	0.030	0.013	12.822	1.906	1.906	0.000	0.000	0.000	0.000
123	A	228	GLU	-1	-0.847	-0.907	10.152	-30.460	-30.460	0.000	0.000	0.000	0.000
124	A	229	ILE	0	-0.016	-0.013	11.000	2.494	2.494	0.000	0.000	0.000	0.000
125	A	230	PHE	0	0.004	0.002	10.882	-2.044	-2.044	0.000	0.000	0.000	0.000
126	A	231	PHE	0	-0.009	-0.007	9.908	1.938	1.938	0.000	0.000	0.000	0.000
127	A	232	SER	0	0.028	0.018	13.551	-0.465	-0.465	0.000	0.000	0.000	0.000
128	A	233	THR	0	-0.010	-0.022	16.375	0.437	0.437	0.000	0.000	0.000	0.000
129	A	234	ASP	-1	-0.888	-0.939	19.908	-12.245	-12.245	0.000	0.000	0.000	0.000
130	A	235	ALA	0	-0.034	-0.009	22.632	0.541	0.541	0.000	0.000	0.000	0.000
131	A	236	ASN	0	0.072	0.027	24.317	-0.036	-0.036	0.000	0.000	0.000	0.000
132	A	237	ASP	-1	-0.857	-0.921	27.277	-10.107	-10.107	0.000	0.000	0.000	0.000
133	A	238	LEU	0	0.018	0.004	24.924	0.321	0.321	0.000	0.000	0.000	0.000
134	A	239	SER	0	0.025	0.009	28.472	0.182	0.182	0.000	0.000	0.000	0.000
135	A	240	LYS	1	0.833	0.917	30.408	10.148	10.148	0.000	0.000	0.000	0.000
136	A	241	ILE	0	0.014	0.006	30.603	0.252	0.252	0.000	0.000	0.000	0.000
137	A	242	HIS	0	0.020	0.014	32.560	0.077	0.077	0.000	0.000	0.000	0.000
138	A	243	SER	0	-0.004	-0.004	34.373	0.303	0.303	0.000	0.000	0.000	0.000
139	A	244	ILE	0	-0.015	-0.004	36.412	0.210	0.210	0.000	0.000	0.000	0.000
140	A	245	LEU	0	-0.004	-0.006	35.688	0.173	0.173	0.000	0.000	0.000	0.000
141	A	246	ASP	-1	-0.926	-0.951	37.935	-7.888	-7.888	0.000	0.000	0.000	0.000
142	A	247	ASN	0	-0.060	-0.056	39.899	0.279	0.279	0.000	0.000	0.000	0.000
143	A	248	GLU	-1	-0.960	-0.949	42.236	-6.697	-6.697	0.000	0.000	0.000	0.000
144	A	249	PHE	0	-0.097	-0.061	41.382	0.142	0.142	0.000	0.000	0.000	0.000
145	A	250	ASN	0	-0.121	-0.062	40.863	0.171	0.171	0.000	0.000	0.000	0.000
146	A	251	PRO	-1	-0.949	-0.960	44.616	-6.704	-6.704	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:106:SER)