FMO DATABASE

FMODB ID: JY639

Calculation Name: 2M0R-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2M0R

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HCY8

Base Structure: SolutionNMR

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	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-710752.100053
FMO2-HF: Nuclear repulsion	669115.769316
FMO2-HF: Total energy	-41636.330737
FMO2-MP2: Total energy	-41755.237192

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.
-99.26	-97.996	-0.013	-0.627	-0.624	-0.001

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 : 0.873 / q_NPA : 0.920

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

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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	GLN	0	-0.033	-0.028	3.851	-4.601	-3.337	-0.013	-0.627	-0.624	-0.001
4	A	4	CYS	-1	-0.797	-0.804	6.661	-26.399	-26.399	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.862	0.886	8.241	20.604	20.604	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.012	-0.033	10.607	2.527	2.527	0.000	0.000	0.000	0.000
7	A	7	ALA	0	-0.023	-0.002	11.247	-1.746	-1.746	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.009	-0.015	13.852	0.892	0.892	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.029	0.011	17.252	-0.100	-0.100	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.930	-0.976	16.530	-18.367	-18.367	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.959	-0.973	20.167	-11.795	-11.795	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.060	-0.025	23.492	0.503	0.503	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.027	-0.016	25.137	0.403	0.403	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.887	-0.942	25.975	-11.635	-11.635	0.000	0.000	0.000	0.000
15	A	15	PHE	0	-0.053	-0.011	23.622	0.246	0.246	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.014	-0.013	29.381	0.312	0.312	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.829	-0.924	30.505	-9.684	-9.684	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.038	-0.021	30.755	-0.170	-0.170	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.878	-0.931	27.327	-10.996	-10.996	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.957	0.959	25.893	9.826	9.826	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.028	0.007	25.540	-0.442	-0.442	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.021	-0.009	23.501	-0.284	-0.284	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.856	-0.926	20.076	-15.785	-15.785	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.050	-0.042	21.035	-0.621	-0.621	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.061	-0.026	22.445	-0.319	-0.319	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.001	0.003	18.426	-0.355	-0.355	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.923	0.961	16.055	16.933	16.933	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.035	-0.023	16.967	-0.974	-0.974	0.000	0.000	0.000	0.000
29	A	29	PHE	0	0.026	0.023	13.965	-0.192	-0.192	0.000	0.000	0.000	0.000
30	A	30	HIS	0	-0.010	0.002	12.595	0.103	0.103	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.069	-0.024	12.526	-1.475	-1.475	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.003	-0.019	14.156	-0.789	-0.789	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.028	-0.007	12.272	-0.404	-0.404	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.085	-0.042	10.431	-2.772	-2.772	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.986	-0.997	9.720	-22.162	-22.162	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.008	-0.002	10.885	-1.321	-1.321	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.015	0.000	7.626	-0.178	-0.178	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.914	0.949	5.121	39.905	39.905	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.916	-0.949	9.576	-27.122	-27.122	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.098	-0.059	11.894	2.429	2.429	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.016	-0.013	13.910	-0.350	-0.350	0.000	0.000	0.000	0.000
42	A	42	THR	0	0.031	0.015	14.712	0.810	0.810	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.053	-0.004	17.499	0.376	0.376	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.029	-0.016	18.795	0.976	0.976	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.685	-0.835	14.392	-20.247	-20.247	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.005	0.010	18.655	0.328	0.328	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.957	0.958	21.279	13.418	13.418	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.882	-0.934	20.571	-13.568	-13.568	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.028	0.016	19.476	0.452	0.452	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.026	-0.007	22.333	0.435	0.435	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.022	-0.020	25.694	0.548	0.548	0.000	0.000	0.000	0.000
52	A	52	GLN	0	-0.059	-0.021	23.221	0.930	0.930	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.035	-0.017	23.130	-0.213	-0.213	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.020	0.004	25.791	0.188	0.188	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.020	0.019	28.424	0.361	0.361	0.000	0.000	0.000	0.000
56	A	56	HIS	0	-0.022	-0.027	31.273	0.427	0.427	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.053	-0.029	30.808	0.236	0.236	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.037	-0.009	29.997	0.149	0.149	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.045	0.041	31.238	-0.209	-0.209	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.057	-0.004	31.594	0.077	0.077	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.069	-0.029	33.263	0.063	0.063	0.000	0.000	0.000	0.000
62	A	62	CYS	0	-0.036	-0.014	34.930	0.300	0.300	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.056	0.046	33.522	0.035	0.035	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.013	-0.022	27.521	-0.087	-0.087	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.963	-0.980	28.624	-9.940	-9.940	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.800	-0.877	29.602	-9.800	-9.800	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.850	0.882	27.131	9.880	9.880	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.045	-0.016	24.358	-0.444	-0.444	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.011	-0.018	26.488	-0.161	-0.161	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.099	-0.035	28.374	-0.191	-0.191	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.045	0.011	22.204	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.007	0.000	25.371	-0.281	-0.281	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.037	-0.009	26.556	0.056	0.056	0.000	0.000	0.000	0.000
74	A	74	CYS	0	-0.065	-0.024	23.102	0.099	0.099	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.002	-0.011	23.152	-0.597	-0.597	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.895	-0.944	22.116	-12.690	-12.690	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.018	-0.014	20.587	-0.391	-0.391	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.851	0.935	16.042	16.729	16.729	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.015	0.014	17.520	0.524	0.524	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.917	-0.969	16.527	-16.129	-16.129	0.000	0.000	0.000	0.000
81	A	81	PHE	0	0.040	0.034	15.607	0.858	0.858	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.841	0.904	17.309	13.452	13.452	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.048	-0.050	19.484	0.626	0.626	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.048	0.026	19.369	0.456	0.456	0.000	0.000	0.000	0.000
85	A	85	TRP	0	0.031	0.008	21.397	0.481	0.481	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.840	-0.903	23.765	-11.066	-11.066	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.019	0.013	24.434	0.491	0.491	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.016	-0.001	23.385	0.464	0.464	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.000	0.005	27.645	0.417	0.417	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.883	-0.933	30.062	-9.370	-9.370	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.051	0.024	29.395	0.323	0.323	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.011	0.004	31.418	0.331	0.331	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.852	0.923	33.580	9.374	9.374	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.024	0.004	34.440	0.294	0.294	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.030	-0.009	33.158	0.225	0.225	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.882	0.935	35.906	7.961	7.961	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.032	0.018	38.365	0.043	0.043	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.801	-0.892	40.751	-7.260	-7.260	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.920	0.960	43.859	6.729	6.729	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.014	-0.027	46.474	-0.046	-0.046	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.009	0.003	46.886	-0.063	-0.063	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.874	0.939	42.341	7.046	7.046	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.045	-0.024	42.389	-0.259	-0.259	0.000	0.000	0.000	0.000
104	A	104	HIS	-1	-0.922	-0.937	44.455	-6.842	-6.842	0.000	0.000	0.000	0.000

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