FMO DATABASE

FMODB ID: LGM29

Calculation Name: 2PCS-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2PCS

Chain ID: A

ChEMBL ID:

UniProt ID: Q5QL47

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	160
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1487008.928263
FMO2-HF: Nuclear repulsion	1425799.068298
FMO2-HF: Total energy	-61209.859965
FMO2-MP2: Total energy	-61387.53468

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:1:LEU)

Summations of interaction energy for fragment #1(A:1: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.
-154.466	-141.618	13.453	-10.862	-15.436	-0.107

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.773 / q_NPA : 0.878

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	3	GLY	0	0.055	0.031	3.373	-1.907	0.618	0.026	-1.224	-1.327	-0.005
4	A	4	ASN	0	-0.062	-0.020	5.355	2.953	2.990	-0.001	-0.002	-0.033	0.000
109	A	109	TYR	0	-0.006	-0.006	2.350	2.086	3.332	0.875	-0.442	-1.678	-0.002
111	A	111	ALA	0	0.031	0.005	2.426	7.783	9.363	0.481	-0.742	-1.319	-0.003
112	A	112	GLU	-1	-0.869	-0.911	1.789	-83.036	-82.392	9.267	-6.012	-3.899	-0.081
113	A	113	VAL	0	-0.024	-0.026	3.396	4.905	5.434	0.029	-0.099	-0.459	0.000
122	A	122	GLN	0	0.000	-0.014	3.040	-12.303	-10.343	0.224	-0.675	-1.509	-0.004
123	A	123	ARG	1	1.052	1.025	3.090	20.301	21.162	0.181	-0.374	-0.668	-0.004
125	A	125	LEU	0	0.013	0.005	2.266	-0.068	0.623	1.149	-0.364	-1.476	-0.001
126	A	126	GLY	0	0.026	0.018	2.849	-2.403	-1.033	0.392	-0.582	-1.181	-0.002
127	A	127	GLY	0	-0.002	0.003	3.386	2.609	2.530	0.037	0.200	-0.157	0.000
129	A	129	ALA	0	0.011	0.005	2.950	1.302	1.679	0.131	-0.119	-0.388	-0.001
130	A	130	LYS	1	0.950	0.987	4.924	21.858	21.877	-0.001	-0.003	-0.015	0.000
160	A	160	HIS	-1	-0.900	-0.956	2.922	-41.970	-40.882	0.663	-0.424	-1.327	-0.004
5	A	5	GLY	0	0.068	0.020	9.020	-0.554	-0.554	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.035	-0.014	11.602	0.926	0.926	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.020	0.004	13.558	-0.110	-0.110	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.956	-0.969	17.411	-12.210	-12.210	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.038	-0.026	19.309	-0.073	-0.073	0.000	0.000	0.000	0.000
10	A	10	LYS	0	0.002	0.003	22.864	0.222	0.222	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.039	0.002	26.507	-0.041	-0.041	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.001	-0.009	27.003	-0.344	-0.344	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.019	-0.006	24.974	-0.222	-0.222	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.885	-0.948	25.744	-10.734	-10.734	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.822	-0.860	27.554	-9.801	-9.801	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.004	-0.001	21.573	-0.258	-0.258	0.000	0.000	0.000	0.000
17	A	17	TRP	0	0.000	0.001	21.891	-0.544	-0.544	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.031	-0.026	23.663	-0.262	-0.262	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.885	0.942	23.257	10.505	10.505	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.041	-0.022	17.540	-0.467	-0.467	0.000	0.000	0.000	0.000
21	A	21	MET	0	0.015	0.019	20.042	-0.761	-0.761	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.815	-0.874	22.748	-10.754	-10.754	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.050	0.020	21.834	-0.363	-0.363	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.039	-0.048	22.578	-0.129	-0.129	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.088	-0.036	21.815	0.158	0.158	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.072	0.039	17.453	-0.396	-0.396	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.014	-0.020	18.507	-0.491	-0.491	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.886	0.950	20.445	10.831	10.831	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.056	-0.024	17.854	0.100	0.100	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.030	0.016	13.383	-0.653	-0.653	0.000	0.000	0.000	0.000
31	A	31	MET	0	-0.035	-0.020	13.412	0.777	0.777	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.005	-0.010	14.724	-0.705	-0.705	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.070	0.001	16.837	0.284	0.284	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.889	0.952	18.253	12.211	12.211	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.031	-0.023	20.890	0.591	0.591	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.011	0.007	17.763	-0.641	-0.641	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.957	-0.966	21.573	-11.114	-11.114	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.013	-0.004	22.703	-0.546	-0.546	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.041	-0.027	21.072	0.360	0.360	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.019	-0.021	25.128	0.062	0.062	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.947	-0.966	25.653	-11.144	-11.144	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.896	-0.947	21.857	-13.148	-13.148	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.862	0.923	20.142	14.366	14.366	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.017	-0.005	18.939	0.924	0.924	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.885	0.936	18.951	13.114	13.114	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.014	0.002	16.420	0.570	0.570	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.809	-0.879	17.538	-13.970	-13.970	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.023	0.013	12.840	0.129	0.129	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.049	-0.065	16.432	0.087	0.087	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.047	0.034	11.516	0.519	0.519	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.007	-0.021	15.413	0.105	0.105	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.033	0.007	11.129	0.658	0.658	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.007	-0.007	13.402	-0.684	-0.684	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.008	-0.005	10.871	0.191	0.191	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.044	0.019	7.695	-1.047	-1.047	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.903	0.997	11.037	14.290	14.290	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.001	-0.013	14.687	0.161	0.161	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.809	0.906	16.255	12.893	12.893	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.025	-0.031	11.491	-0.495	-0.495	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.827	-0.894	15.682	-13.916	-13.916	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.030	-0.022	13.313	-1.244	-1.244	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.012	-0.001	14.921	1.315	1.315	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.003	-0.009	13.529	-1.603	-1.603	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.858	-0.915	15.660	-14.672	-14.672	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.006	0.008	16.435	-1.221	-1.221	0.000	0.000	0.000	0.000
66	A	66	THR	0	0.046	0.015	17.463	0.540	0.540	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.815	-0.904	19.674	-15.588	-15.588	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.043	0.028	21.345	-0.089	-0.089	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.833	0.919	22.966	13.893	13.893	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.032	0.037	25.002	-0.203	-0.203	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.038	-0.013	26.408	0.226	0.226	0.000	0.000	0.000	0.000
72	A	72	TYR	0	0.072	0.002	23.504	-0.362	-0.362	0.000	0.000	0.000	0.000
73	A	73	HIS	1	0.803	0.876	18.465	15.349	15.349	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.003	-0.005	15.680	0.347	0.347	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.868	0.932	15.454	17.268	17.268	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.006	0.002	12.360	0.978	0.978	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.012	0.013	12.659	-1.873	-1.873	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.006	-0.011	9.849	1.525	1.525	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.027	-0.019	10.849	-1.335	-1.335	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.011	0.013	11.111	1.967	1.967	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.901	-0.969	12.066	-19.867	-19.867	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.079	0.030	14.355	0.836	0.836	0.000	0.000	0.000	0.000
83	A	83	GLY	0	-0.015	0.010	15.282	-0.551	-0.551	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.051	-0.033	12.432	0.159	0.159	0.000	0.000	0.000	0.000
85	A	85	GLY	0	-0.046	-0.029	11.671	-0.914	-0.914	0.000	0.000	0.000	0.000
86	A	86	PHE	0	0.019	0.026	9.438	1.171	1.171	0.000	0.000	0.000	0.000
87	A	87	VAL	0	-0.037	-0.030	5.802	-3.411	-3.411	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.025	0.004	7.392	5.699	5.699	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.011	-0.019	6.361	-6.925	-6.925	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.921	-0.941	7.794	-23.583	-23.583	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.005	-0.013	8.762	-4.113	-4.113	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.067	-0.028	11.022	2.075	2.075	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.007	0.003	13.086	-1.098	-1.098	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.837	-0.899	15.712	-15.446	-15.446	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.034	-0.010	18.670	-0.254	-0.254	0.000	0.000	0.000	0.000
96	A	96	THR	0	0.001	-0.004	21.485	0.450	0.450	0.000	0.000	0.000	0.000
97	A	97	PRO	0	-0.011	0.001	23.708	-0.087	-0.087	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.016	-0.023	24.018	0.049	0.049	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.050	-0.032	27.377	0.365	0.365	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.904	-0.952	30.352	-8.906	-8.906	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.960	-0.969	31.324	-8.751	-8.751	0.000	0.000	0.000	0.000
102	A	102	CYS	0	-0.055	-0.008	26.150	-0.356	-0.356	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.003	-0.028	22.485	0.045	0.045	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.003	0.007	19.510	-0.430	-0.430	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.007	0.006	15.139	-0.050	-0.050	0.000	0.000	0.000	0.000
106	A	106	THR	0	-0.018	-0.022	15.399	-0.499	-0.499	0.000	0.000	0.000	0.000
107	A	107	TYR	0	0.012	0.005	8.294	0.467	0.467	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.002	-0.008	9.497	-1.298	-1.298	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.015	-0.011	5.032	-5.110	-5.110	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.021	0.017	6.131	-0.542	-0.542	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.047	0.019	9.323	1.574	1.574	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.937	0.957	11.235	15.614	15.614	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.018	0.010	8.072	0.117	0.117	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.027	0.015	7.044	-1.367	-1.367	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.029	-0.016	7.768	-1.630	-1.630	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.049	-0.013	6.969	1.150	1.150	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.037	0.025	7.192	1.286	1.286	0.000	0.000	0.000	0.000
124	A	124	MET	0	-0.060	-0.016	5.719	1.963	1.963	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.031	-0.026	6.249	2.084	2.084	0.000	0.000	0.000	0.000
131	A	131	LEU	0	-0.019	-0.003	7.580	1.667	1.667	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.038	-0.034	7.580	1.574	1.574	0.000	0.000	0.000	0.000
133	A	133	ILE	0	0.018	0.024	7.010	1.049	1.049	0.000	0.000	0.000	0.000
134	A	134	SER	0	-0.004	-0.045	10.485	1.079	1.079	0.000	0.000	0.000	0.000
135	A	135	ASP	-1	-0.919	-0.969	13.032	-13.877	-13.877	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.002	0.013	13.333	0.997	0.997	0.000	0.000	0.000	0.000
137	A	137	PHE	0	0.076	0.016	12.639	0.934	0.934	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.961	0.998	16.573	14.050	14.050	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.764	0.890	17.242	15.372	15.372	0.000	0.000	0.000	0.000
140	A	140	ILE	0	0.047	0.019	18.245	0.676	0.676	0.000	0.000	0.000	0.000
141	A	141	GLN	0	0.061	0.037	20.650	0.334	0.334	0.000	0.000	0.000	0.000
142	A	142	LYS	1	0.920	0.966	22.662	11.391	11.391	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.874	-0.945	24.007	-10.050	-10.050	0.000	0.000	0.000	0.000
144	A	144	ILE	0	0.040	0.026	23.156	0.346	0.346	0.000	0.000	0.000	0.000
145	A	145	ALA	0	0.056	0.050	26.612	0.325	0.325	0.000	0.000	0.000	0.000
146	A	146	LYS	1	0.754	0.852	27.842	10.410	10.410	0.000	0.000	0.000	0.000
147	A	147	SER	0	-0.080	-0.040	28.824	0.307	0.307	0.000	0.000	0.000	0.000
148	A	148	LYS	1	0.807	0.908	30.858	8.627	8.627	0.000	0.000	0.000	0.000
149	A	149	GLN	0	0.060	0.020	28.992	0.059	0.059	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.909	-0.948	30.557	-8.564	-8.564	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.078	-0.053	26.157	-0.127	-0.127	0.000	0.000	0.000	0.000
152	A	152	SER	-1	-0.859	-0.918	27.959	-9.740	-9.740	0.000	0.000	0.000	0.000
153	A	153	GLU	-1	-0.962	-0.974	24.013	-11.523	-11.523	0.000	0.000	0.000	0.000
154	A	154	GLY	0	-0.030	-0.023	21.858	0.021	0.021	0.000	0.000	0.000	0.000
155	A	155	HIS	0	0.002	0.013	17.482	-0.170	-0.170	0.000	0.000	0.000	0.000
156	A	156	HIS	-1	-0.805	-0.899	11.297	-19.516	-19.516	0.000	0.000	0.000	0.000
157	A	157	HIS	0	-0.063	-0.013	12.285	0.006	0.006	0.000	0.000	0.000	0.000
158	A	158	HIS	0	0.021	0.000	5.239	1.552	1.552	0.000	0.000	0.000	0.000
159	A	159	HIS	0	-0.077	-0.034	8.444	2.624	2.624	0.000	0.000	0.000	0.000

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