FMO DATABASE

FMODB ID: YR132

Calculation Name: 2M5T-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2M5T

Chain ID: A

ChEMBL ID:

UniProt ID: I2CMJ2

Base Structure: SolutionNMR

Registration Date: 2025-10-05

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	142
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1221010.692715
FMO2-HF: Nuclear repulsion	1165475.291597
FMO2-HF: Total energy	-55535.401119
FMO2-MP2: Total energy	-55694.056311

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:GLY)

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

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.
-232.658	-225.575	6.942	-7.818	-6.21	-0.095

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.822 / q_NPA : 0.906

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	SER	0	-0.024	-0.030	3.462	2.809	3.662	-0.001	-0.338	-0.515	0.000
59	A	59	TYR	0	-0.029	-0.013	3.109	-4.732	-3.843	0.022	-0.450	-0.462	-0.004
61	A	61	ARG	1	0.884	0.897	4.785	42.133	42.182	-0.001	-0.008	-0.040	0.000
64	A	64	ASP	-1	-0.895	-0.940	2.164	-135.080	-129.885	6.923	-7.014	-5.104	-0.091
65	A	65	ARG	1	0.901	0.953	4.537	23.409	23.506	-0.001	-0.008	-0.089	0.000
4	A	4	ASP	-1	-0.846	-0.908	6.123	-39.352	-39.352	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.010	0.002	9.359	1.888	1.888	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.019	-0.009	12.013	0.248	0.248	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.010	-0.001	15.034	-0.912	-0.912	0.000	0.000	0.000	0.000
8	A	8	HIS	0	0.049	0.023	15.388	1.523	1.523	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.024	0.013	19.671	-0.040	-0.040	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.893	-0.947	22.404	-12.304	-12.304	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.056	-0.032	24.989	0.227	0.227	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.001	0.008	24.871	0.195	0.195	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.042	-0.029	19.724	-0.629	-0.629	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.018	0.009	20.377	0.483	0.483	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.868	0.930	18.769	13.227	13.227	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.042	0.019	18.412	0.035	0.035	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.025	0.030	20.446	-0.287	-0.287	0.000	0.000	0.000	0.000
18	A	18	HIS	0	0.025	0.005	21.186	0.052	0.052	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.037	-0.023	15.455	-0.438	-0.438	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.100	-0.066	18.307	-0.499	-0.499	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.042	-0.016	20.707	0.453	0.453	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.013	0.015	23.575	0.178	0.178	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.021	-0.027	25.234	0.659	0.659	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.913	-0.945	28.633	-9.996	-9.996	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.054	-0.039	28.520	0.558	0.558	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.056	-0.016	25.836	-0.139	-0.139	0.000	0.000	0.000	0.000
27	A	27	ILE	0	0.015	0.015	28.544	0.327	0.327	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.009	-0.003	29.587	0.403	0.403	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.000	-0.007	27.808	-0.567	-0.567	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.006	0.019	27.982	0.467	0.467	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.011	-0.010	28.010	-0.370	-0.370	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.009	-0.001	29.352	-0.041	-0.041	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.022	-0.022	25.677	0.019	0.019	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.855	-0.922	23.470	-13.528	-13.528	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.026	0.009	21.633	-0.780	-0.780	0.000	0.000	0.000	0.000
36	A	36	GLN	0	0.022	-0.010	23.451	0.233	0.233	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.006	0.001	23.550	-0.656	-0.656	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.831	-0.938	24.192	-12.075	-12.075	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.030	0.030	25.569	-0.188	-0.188	0.000	0.000	0.000	0.000
40	A	40	CYS	0	-0.070	-0.040	22.246	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.903	-0.940	25.158	-11.340	-11.340	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.077	-0.050	20.230	-0.515	-0.515	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.004	0.019	21.021	-0.537	-0.537	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.017	0.009	18.290	-0.474	-0.474	0.000	0.000	0.000	0.000
45	A	45	PRO	0	-0.058	-0.036	16.049	0.703	0.703	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.924	-0.970	15.593	-20.120	-20.120	0.000	0.000	0.000	0.000
47	A	47	ASN	0	0.035	0.011	18.539	0.668	0.668	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.051	-0.012	20.474	-0.320	-0.320	0.000	0.000	0.000	0.000
49	A	49	PRO	0	-0.021	-0.009	21.565	0.602	0.602	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.866	-0.950	24.620	-11.009	-11.009	0.000	0.000	0.000	0.000
51	A	51	CYS	-1	-0.748	-0.783	26.355	-11.517	-11.517	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.793	-0.912	24.242	-12.247	-12.247	0.000	0.000	0.000	0.000
53	A	53	CYS	0	-0.084	-0.060	23.519	0.139	0.139	0.000	0.000	0.000	0.000
54	A	54	THR	0	0.060	0.036	23.531	-0.386	-0.386	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.016	0.002	22.145	-0.538	-0.538	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.030	-0.019	19.033	0.267	0.267	0.000	0.000	0.000	0.000
57	A	57	CYS	0	-0.082	-0.024	14.017	-0.501	-0.501	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.038	0.024	12.150	0.393	0.393	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.037	-0.008	9.344	0.501	0.501	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.022	-0.016	7.663	-1.535	-1.535	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.067	-0.030	8.858	1.986	1.986	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.007	0.006	6.819	2.317	2.317	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.046	-0.013	9.810	0.989	0.989	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.026	-0.012	13.124	0.223	0.223	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.000	-0.006	16.355	-0.072	-0.072	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.919	-0.970	18.824	-12.076	-12.076	0.000	0.000	0.000	0.000
71	A	71	CYS	0	-0.052	-0.021	20.074	-0.183	-0.183	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.832	-0.898	23.406	-10.584	-10.584	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.038	0.030	26.885	-0.146	-0.146	0.000	0.000	0.000	0.000
74	A	74	HIS	1	0.728	0.843	27.773	11.240	11.240	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.856	-0.920	29.593	-9.708	-9.708	0.000	0.000	0.000	0.000
76	A	76	TRP	0	-0.003	-0.001	31.493	-0.139	-0.139	0.000	0.000	0.000	0.000
77	A	77	TYR	0	0.015	-0.004	29.399	0.179	0.179	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.058	-0.026	31.115	-0.070	-0.070	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.019	0.015	27.125	-0.289	-0.289	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.951	-0.988	28.059	-10.753	-10.753	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.952	-0.975	29.248	-9.575	-9.575	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.012	-0.011	25.727	-0.266	-0.266	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.072	-0.049	23.194	-0.248	-0.248	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.014	0.018	18.841	-0.131	-0.131	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.060	0.022	25.527	0.392	0.392	0.000	0.000	0.000	0.000
86	A	86	PRO	0	0.015	0.005	29.020	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.943	0.981	31.840	9.334	9.334	0.000	0.000	0.000	0.000
88	A	88	HIS	0	-0.037	-0.025	32.451	0.387	0.387	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.058	-0.013	32.764	-0.074	-0.074	0.000	0.000	0.000	0.000
90	A	90	GLN	0	0.049	0.031	24.834	-0.240	-0.240	0.000	0.000	0.000	0.000
91	A	91	TYR	0	0.005	-0.016	29.292	0.360	0.360	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.016	-0.008	27.089	-0.177	-0.177	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.006	0.012	24.746	-0.574	-0.574	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.008	0.002	22.246	0.390	0.390	0.000	0.000	0.000	0.000
95	A	95	ILE	0	-0.014	-0.008	22.764	-0.716	-0.716	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.052	0.014	21.998	0.385	0.385	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.996	-0.990	22.681	-12.447	-12.447	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.024	-0.024	18.875	-0.600	-0.600	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.033	-0.012	15.267	0.651	0.651	0.000	0.000	0.000	0.000
100	A	100	CYS	0	-0.001	0.004	16.520	-0.378	-0.378	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.022	0.010	12.819	0.518	0.518	0.000	0.000	0.000	0.000
102	A	102	PRO	0	0.005	0.001	15.319	-0.590	-0.590	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.010	-0.008	12.208	-0.328	-0.328	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.783	-0.908	11.220	-29.912	-29.912	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.005	0.012	12.281	0.031	0.031	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.032	0.016	13.002	-1.487	-1.487	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.001	0.007	10.911	-1.131	-1.131	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.934	0.963	11.379	23.687	23.687	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.038	0.017	12.769	-1.595	-1.595	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.031	-0.014	12.848	0.844	0.844	0.000	0.000	0.000	0.000
111	A	111	CYS	0	0.008	0.027	16.404	0.160	0.160	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.943	0.950	19.509	12.317	12.317	0.000	0.000	0.000	0.000
113	A	113	HIS	1	0.683	0.771	21.836	12.848	12.848	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.092	0.040	17.806	-0.201	-0.201	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.046	-0.019	14.741	0.045	0.045	0.000	0.000	0.000	0.000
116	A	116	ILE	0	0.020	0.022	17.496	0.648	0.648	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.099	0.046	18.477	0.739	0.739	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.060	-0.021	15.359	-1.419	-1.419	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.050	0.001	13.638	1.151	1.151	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.019	-0.015	17.048	-0.322	-0.322	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.015	0.006	20.307	0.422	0.422	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.001	-0.009	20.359	-0.756	-0.756	0.000	0.000	0.000	0.000
123	A	123	GLY	0	0.041	0.023	21.339	0.533	0.533	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.899	-0.946	22.655	-12.762	-12.762	0.000	0.000	0.000	0.000
125	A	125	GLY	0	-0.011	0.009	22.470	0.409	0.409	0.000	0.000	0.000	0.000
126	A	126	HIS	1	0.856	0.913	22.821	12.606	12.606	0.000	0.000	0.000	0.000
127	A	127	VAL	0	0.015	0.025	17.076	-0.242	-0.242	0.000	0.000	0.000	0.000
128	A	128	ALA	0	0.013	0.008	20.465	0.567	0.567	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.006	-0.015	15.253	-0.975	-0.975	0.000	0.000	0.000	0.000
130	A	130	THR	0	-0.006	0.005	20.110	0.974	0.974	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.807	-0.932	21.039	-13.926	-13.926	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.007	-0.022	18.543	0.369	0.369	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.879	0.936	23.102	11.477	11.477	0.000	0.000	0.000	0.000
134	A	134	PRO	0	-0.157	-0.080	25.598	0.493	0.493	0.000	0.000	0.000	0.000
135	A	135	TYR	0	0.007	-0.008	25.823	0.219	0.219	0.000	0.000	0.000	0.000
136	A	136	ASN	0	0.007	0.020	24.644	0.193	0.193	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.001	0.009	26.664	0.481	0.481	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.927	0.969	29.015	10.401	10.401	0.000	0.000	0.000	0.000
139	A	139	ALA	0	-0.015	-0.018	30.400	0.237	0.237	0.000	0.000	0.000	0.000
140	A	140	THR	0	-0.025	-0.015	33.286	0.002	0.002	0.000	0.000	0.000	0.000
141	A	141	SER	0	-0.056	-0.030	34.922	0.235	0.235	0.000	0.000	0.000	0.000
142	A	142	GLN	-1	-0.930	-0.945	38.087	-8.136	-8.136	0.000	0.000	0.000	0.000

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