FMO DATABASE

FMODB ID: 92NJ2

Calculation Name: 2MCF-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2MCF

Chain ID: A

ChEMBL ID:

UniProt ID: C5A217

Base Structure: SolutionNMR

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1394805.436603
FMO2-HF: Nuclear repulsion	1334615.178173
FMO2-HF: Total energy	-60190.258431
FMO2-MP2: Total energy	-60360.243424

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:MET)

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

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.
-173.184	-165.73	3.846	-4.142	-7.158	-0.033

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.836 / q_NPA : 0.911

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	TYR	0	0.026	-0.002	2.668	-9.098	-5.229	0.736	-1.805	-2.800	-0.011
88	A	88	LYS	1	0.835	0.911	2.295	26.107	26.607	0.759	-0.260	-0.999	-0.001
89	A	89	ILE	0	-0.019	0.016	4.242	-1.174	-0.831	-0.001	-0.034	-0.308	0.000
90	A	90	THR	0	-0.069	-0.071	2.217	-20.778	-18.093	2.353	-2.016	-3.022	-0.021
91	A	91	GLU	-1	-0.919	-0.964	4.526	-31.887	-31.830	-0.001	-0.027	-0.029	0.000
4	A	4	ASP	-1	-0.791	-0.882	5.916	-24.958	-24.958	0.000	0.000	0.000	0.000
5	A	5	VAL	0	0.008	0.016	9.078	1.106	1.106	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.040	-0.012	12.274	0.543	0.543	0.000	0.000	0.000	0.000
7	A	7	ILE	0	0.010	0.009	15.162	0.269	0.269	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.006	-0.010	18.271	0.213	0.213	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.011	0.011	21.009	0.208	0.208	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.801	-0.927	24.342	-11.584	-11.584	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.063	0.011	27.316	-0.051	-0.051	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.046	-0.011	29.089	0.223	0.223	0.000	0.000	0.000	0.000
13	A	13	HIS	0	0.011	-0.006	31.160	0.378	0.378	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.902	0.954	33.817	8.385	8.385	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.037	0.023	35.969	0.124	0.124	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.855	-0.912	37.922	-7.043	-7.043	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.874	0.922	41.485	6.522	6.522	0.000	0.000	0.000	0.000
18	A	18	HIS	0	-0.007	-0.023	42.969	0.124	0.124	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.062	-0.024	40.903	-0.159	-0.159	0.000	0.000	0.000	0.000
20	A	20	MET	0	-0.004	0.002	37.424	0.021	0.021	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.854	-0.917	34.556	-8.524	-8.524	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.012	-0.015	31.351	-0.198	-0.198	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.001	-0.003	27.015	-0.260	-0.260	0.000	0.000	0.000	0.000
24	A	24	CYS	0	-0.059	-0.009	26.672	0.616	0.616	0.000	0.000	0.000	0.000
25	A	25	PRO	0	0.002	-0.001	24.605	-0.373	-0.373	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.020	0.021	19.329	-0.089	-0.089	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.035	-0.025	19.439	-0.066	-0.066	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.011	0.005	13.458	-0.530	-0.530	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.067	-0.028	12.821	0.645	0.645	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.063	0.039	9.424	-1.137	-1.137	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.855	-0.925	8.496	-28.872	-28.872	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.835	0.911	8.998	20.151	20.151	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.031	0.006	5.874	-5.562	-5.562	0.000	0.000	0.000	0.000
34	A	34	TYR	0	0.056	0.015	4.883	2.920	2.920	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.873	-0.936	6.717	-27.014	-27.014	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.024	0.013	10.241	1.995	1.995	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.031	-0.009	8.784	1.861	1.861	0.000	0.000	0.000	0.000
38	A	38	MET	0	0.014	-0.003	9.082	1.335	1.335	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.963	-0.965	12.212	-16.441	-16.441	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.017	-0.010	13.626	1.291	1.291	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.006	0.005	13.278	1.179	1.179	0.000	0.000	0.000	0.000
42	A	42	ASN	0	0.005	0.004	15.834	1.438	1.438	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.002	-0.008	17.999	0.934	0.934	0.000	0.000	0.000	0.000
44	A	44	VAL	0	0.007	-0.007	18.713	0.856	0.856	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.778	-0.853	19.284	-13.018	-13.018	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.841	0.905	21.200	12.600	12.600	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.032	0.024	23.659	0.558	0.558	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.015	-0.009	21.941	0.568	0.568	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.778	0.889	23.061	12.650	12.650	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.011	0.006	27.300	0.379	0.379	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.059	-0.030	28.939	0.354	0.354	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.020	-0.017	27.462	0.155	0.155	0.000	0.000	0.000	0.000
53	A	53	ASN	0	-0.051	-0.031	30.768	-0.169	-0.169	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.013	-0.003	26.839	0.019	0.019	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.021	-0.011	27.866	0.049	0.049	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.044	-0.028	21.416	-0.167	-0.167	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.816	-0.888	22.124	-11.413	-11.413	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.918	-0.960	17.046	-13.899	-13.899	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.037	-0.015	17.091	0.561	0.561	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.918	-0.956	12.021	-18.744	-18.744	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.060	-0.035	12.048	0.717	0.717	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.877	-0.940	12.935	-16.426	-16.426	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.814	-0.911	8.938	-26.347	-26.347	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.079	-0.003	6.798	0.531	0.531	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.851	-0.929	7.332	-23.985	-23.985	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.013	-0.008	5.237	0.188	0.188	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.013	0.007	8.695	1.426	1.426	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.021	-0.024	11.565	-0.521	-0.521	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.826	0.896	14.962	15.225	15.225	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.824	0.907	17.467	12.001	12.001	0.000	0.000	0.000	0.000
71	A	71	TYR	0	-0.004	-0.038	19.178	0.040	0.040	0.000	0.000	0.000	0.000
72	A	72	THR	0	0.000	-0.002	23.812	0.038	0.038	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.017	0.000	25.201	0.102	0.102	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.812	-0.886	28.966	-8.290	-8.290	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.842	0.894	32.168	9.065	9.065	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.820	-0.887	34.460	-8.594	-8.594	0.000	0.000	0.000	0.000
77	A	77	GLY	0	-0.008	-0.005	38.137	0.002	0.002	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.795	0.898	34.586	8.962	8.962	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.864	0.905	32.716	8.666	8.666	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.014	0.013	29.859	0.089	0.089	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.090	-0.023	24.670	0.008	0.008	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.028	0.006	21.344	-0.126	-0.126	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.018	0.019	19.179	-0.355	-0.355	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.023	0.010	15.101	-0.382	-0.382	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.827	0.918	13.302	18.850	18.850	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.016	0.009	8.749	-0.652	-0.652	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.846	0.898	7.977	24.957	24.957	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.046	-0.017	6.981	1.935	1.935	0.000	0.000	0.000	0.000
93	A	94	PRO	0	0.068	0.029	7.537	-3.818	-3.818	0.000	0.000	0.000	0.000
94	A	95	PRO	0	0.006	-0.001	8.870	0.113	0.113	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.048	-0.022	10.776	1.392	1.392	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.909	-0.950	14.197	-16.998	-16.998	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.004	-0.012	17.624	0.307	0.307	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.050	-0.016	19.714	0.259	0.259	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.972	0.980	16.500	17.114	17.114	0.000	0.000	0.000	0.000
100	A	101	CYS	0	-0.075	-0.022	18.449	1.150	1.150	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.027	-0.033	19.686	-0.360	-0.360	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.013	-0.009	16.051	0.301	0.301	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.053	-0.027	19.434	0.338	0.338	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.861	-0.918	19.308	-14.684	-14.684	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.042	0.022	18.955	0.132	0.132	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.909	-0.968	20.663	-11.840	-11.840	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.889	0.945	22.810	12.141	12.141	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.757	-0.872	17.620	-17.848	-17.848	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.001	-0.002	20.558	0.096	0.096	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.885	-0.929	22.822	-10.867	-10.867	0.000	0.000	0.000	0.000
111	A	113	ILE	0	0.031	0.009	18.827	0.210	0.210	0.000	0.000	0.000	0.000
112	A	114	VAL	0	0.007	0.002	22.919	0.382	0.382	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.965	0.981	25.457	12.620	12.620	0.000	0.000	0.000	0.000
114	A	116	ALA	0	-0.028	-0.009	23.918	0.290	0.290	0.000	0.000	0.000	0.000
115	A	117	ILE	0	0.008	0.004	23.811	0.230	0.230	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.768	-0.875	27.268	-9.101	-9.101	0.000	0.000	0.000	0.000
117	A	119	GLU	-1	-0.915	-0.933	29.443	-10.332	-10.332	0.000	0.000	0.000	0.000
118	A	121	LEU	0	0.000	-0.007	29.489	0.298	0.298	0.000	0.000	0.000	0.000
119	A	122	ALA	0	-0.042	-0.033	32.535	0.311	0.311	0.000	0.000	0.000	0.000
120	A	123	LYS	1	0.797	0.891	31.782	10.090	10.090	0.000	0.000	0.000	0.000
121	A	124	GLY	0	0.008	0.024	35.458	0.186	0.186	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.901	-0.955	36.422	-8.045	-8.045	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.059	-0.005	35.717	0.152	0.152	0.000	0.000	0.000	0.000
124	A	127	ASN	0	-0.039	-0.042	37.665	0.184	0.184	0.000	0.000	0.000	0.000
125	A	128	SER	0	-0.004	-0.008	32.080	-0.169	-0.169	0.000	0.000	0.000	0.000
126	A	129	LYS	1	0.817	0.906	26.078	11.705	11.705	0.000	0.000	0.000	0.000
127	A	130	LEU	0	0.007	0.011	32.025	-0.085	-0.085	0.000	0.000	0.000	0.000
128	A	131	GLU	-1	-0.885	-0.945	25.809	-11.995	-11.995	0.000	0.000	0.000	0.000
129	A	132	GLY	0	0.077	0.044	28.543	0.268	0.268	0.000	0.000	0.000	0.000
130	A	133	LYS	1	0.866	0.945	21.868	13.018	13.018	0.000	0.000	0.000	0.000
131	A	134	PRO	0	0.000	-0.005	28.155	-0.126	-0.126	0.000	0.000	0.000	0.000
132	A	135	ILE	0	-0.033	-0.030	25.335	0.238	0.238	0.000	0.000	0.000	0.000
133	A	136	PRO	0	-0.023	-0.007	28.710	0.022	0.022	0.000	0.000	0.000	0.000
134	A	137	ASN	0	0.065	0.013	27.266	-0.073	-0.073	0.000	0.000	0.000	0.000
135	A	138	PRO	0	-0.020	-0.016	29.968	0.230	0.230	0.000	0.000	0.000	0.000
136	A	139	LEU	0	-0.032	0.001	28.032	0.266	0.266	0.000	0.000	0.000	0.000
137	A	140	LEU	0	-0.021	-0.018	31.468	-0.112	-0.112	0.000	0.000	0.000	0.000
138	A	141	GLY	0	-0.008	-0.005	31.965	0.312	0.312	0.000	0.000	0.000	0.000
139	A	142	LEU	0	-0.013	0.034	29.930	-0.269	-0.269	0.000	0.000	0.000	0.000
140	A	143	ASP	-1	-0.852	-0.927	26.296	-10.853	-10.853	0.000	0.000	0.000	0.000
141	A	144	SER	0	0.010	0.001	28.708	-0.219	-0.219	0.000	0.000	0.000	0.000
142	A	145	THR	0	-0.026	-0.017	26.494	-0.211	-0.211	0.000	0.000	0.000	0.000
143	A	146	ARG	1	0.887	0.945	28.804	8.954	8.954	0.000	0.000	0.000	0.000
144	A	147	THR	0	0.039	0.020	27.443	0.013	0.013	0.000	0.000	0.000	0.000
145	A	148	GLY	-1	-0.903	-0.930	29.725	-9.754	-9.754	0.000	0.000	0.000	0.000

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