FMO DATABASE

FMODB ID: YR1K2

Calculation Name: 2N2M-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2N2M

Chain ID: A

ChEMBL ID:

UniProt ID: Q8D0Z7

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	156
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1367358.470774
FMO2-HF: Nuclear repulsion	1307135.221987
FMO2-HF: Total energy	-60223.248787
FMO2-MP2: Total energy	-60402.572697

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:GLU)

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

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.
-12.516	-9.45	0.834	-1.389	-2.512	-0.006

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.121 / q_NPA : -0.075

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	GLU	-1	-0.923	-0.955	3.519	-4.668	-3.013	0.007	-0.813	-0.850	-0.002
4	A	4	SER	0	-0.041	-0.026	4.482	2.563	2.690	-0.001	-0.003	-0.123	0.000
35	A	35	TYR	0	0.032	0.014	2.437	-1.912	-0.628	0.828	-0.573	-1.539	-0.004
5	A	5	SER	0	-0.101	-0.052	7.014	-0.090	-0.090	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.012	0.006	9.356	0.565	0.565	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.011	-0.044	12.595	-0.280	-0.280	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.001	0.001	16.176	0.232	0.232	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.057	0.025	19.173	-0.149	-0.149	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.038	-0.010	22.700	0.107	0.107	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.012	-0.012	24.537	-0.033	-0.033	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.018	-0.006	26.593	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.017	-0.025	29.755	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.979	1.003	31.424	-0.243	-0.243	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.015	0.006	34.897	0.001	0.001	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.910	0.950	37.234	-0.255	-0.255	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.838	-0.933	40.554	0.385	0.385	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.895	-0.946	43.044	0.253	0.253	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.001	-0.017	45.789	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.022	-0.003	38.456	0.004	0.004	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.916	0.958	37.285	-0.353	-0.353	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.042	0.022	42.347	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.842	-0.939	37.655	0.305	0.305	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.855	0.951	38.968	-0.263	-0.263	0.000	0.000	0.000	0.000
25	A	25	ASN	0	0.010	0.004	34.191	0.024	0.024	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.036	-0.003	31.897	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	27	ARG	1	1.013	0.995	30.026	-0.550	-0.550	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.038	0.025	27.583	0.041	0.041	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.034	0.001	22.979	-0.053	-0.053	0.000	0.000	0.000	0.000
30	A	30	ASN	0	-0.031	-0.055	19.694	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.002	0.012	14.400	-0.075	-0.075	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.864	0.934	15.471	-0.381	-0.381	0.000	0.000	0.000	0.000
33	A	33	TYR	0	0.009	0.002	5.198	0.624	0.624	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.876	0.925	10.063	0.502	0.502	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.849	-0.926	4.968	-6.957	-6.957	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.043	-0.024	6.964	1.017	1.017	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.042	-0.035	7.491	1.028	1.028	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.027	-0.020	10.842	0.220	0.220	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.850	-0.919	14.619	-1.416	-1.416	0.000	0.000	0.000	0.000
41	A	41	TRP	0	-0.068	-0.023	8.960	0.366	0.366	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.105	0.062	10.951	-0.373	-0.373	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.058	-0.028	9.288	0.328	0.328	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.018	-0.011	10.989	0.041	0.041	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.017	0.018	12.881	0.044	0.044	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.004	0.003	14.357	0.031	0.031	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.043	0.018	13.436	0.033	0.033	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.008	0.000	18.786	-0.070	-0.070	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.031	-0.016	20.969	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.033	-0.045	24.598	-0.066	-0.066	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.845	0.906	28.277	-0.581	-0.581	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.842	0.950	31.218	-0.451	-0.451	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.010	-0.019	34.750	0.032	0.032	0.000	0.000	0.000	0.000
54	A	54	PHE	0	-0.074	-0.023	36.655	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.885	-0.937	39.846	0.387	0.387	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.965	-0.979	42.563	0.329	0.329	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.042	-0.035	45.633	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.050	-0.028	48.410	0.006	0.006	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.814	-0.895	48.468	0.238	0.238	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.036	-0.010	51.957	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	61	PHE	0	-0.042	-0.039	50.797	0.002	0.002	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.925	0.966	48.531	-0.256	-0.256	0.000	0.000	0.000	0.000
63	A	63	LEU	0	0.038	0.040	43.790	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.010	-0.009	41.678	0.006	0.006	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.876	-0.950	39.654	0.412	0.412	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.022	0.003	38.532	0.020	0.020	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.917	-0.939	35.012	0.619	0.619	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.025	0.007	32.883	0.036	0.036	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.899	0.934	26.509	-0.980	-0.980	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.007	-0.009	28.080	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	71	TYR	0	0.034	0.015	22.748	0.004	0.004	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.002	0.001	23.424	-0.055	-0.055	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.005	0.017	17.267	0.096	0.096	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.066	-0.045	19.160	-0.041	-0.041	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.021	0.002	15.190	0.140	0.140	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.016	0.013	16.004	-0.072	-0.072	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.006	0.006	15.092	0.016	0.016	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.040	-0.030	14.395	0.077	0.077	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.031	0.016	16.018	-0.147	-0.147	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.881	0.935	15.240	1.472	1.472	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.051	-0.014	19.746	0.017	0.017	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.002	-0.009	23.072	0.045	0.045	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.858	-0.938	21.985	-0.791	-0.791	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.044	-0.022	20.843	-0.097	-0.097	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.013	-0.003	21.723	0.067	0.067	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.008	-0.001	18.297	-0.063	-0.063	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.016	0.009	20.468	0.092	0.092	0.000	0.000	0.000	0.000
88	A	88	TYR	0	0.026	0.004	18.129	-0.065	-0.065	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.010	0.016	20.136	0.038	0.038	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.063	-0.026	18.232	0.036	0.036	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.037	0.003	20.740	-0.041	-0.041	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.030	0.010	20.612	0.112	0.112	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.049	-0.018	22.385	-0.085	-0.085	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.036	0.031	23.852	0.079	0.079	0.000	0.000	0.000	0.000
95	A	95	HIS	0	-0.014	-0.024	24.602	0.000	0.000	0.000	0.000	0.000	0.000
96	A	96	GLY	0	-0.026	0.000	27.698	0.019	0.019	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.882	0.920	27.395	-0.909	-0.909	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.083	0.038	30.756	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.962	0.981	31.987	-0.729	-0.729	0.000	0.000	0.000	0.000
100	A	100	PHE	0	0.029	0.030	35.714	-0.011	-0.011	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.003	0.000	39.275	0.018	0.018	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.013	-0.002	40.881	-0.020	-0.020	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.024	0.013	41.990	0.023	0.023	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.010	0.001	42.849	-0.023	-0.023	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.007	0.005	42.318	0.016	0.016	0.000	0.000	0.000	0.000
106	A	106	GLN	0	0.015	0.011	38.989	0.030	0.030	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.033	-0.013	35.484	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.881	-0.938	37.235	0.494	0.494	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.084	-0.075	32.752	0.031	0.031	0.000	0.000	0.000	0.000
110	A	110	ARG	1	0.965	0.992	34.809	-0.478	-0.478	0.000	0.000	0.000	0.000
111	A	111	SER	0	0.008	0.000	30.102	0.055	0.055	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.947	0.980	31.419	-0.557	-0.557	0.000	0.000	0.000	0.000
113	A	113	THR	0	0.070	0.025	28.369	0.067	0.067	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.034	-0.015	29.106	-0.063	-0.063	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.056	0.033	28.049	0.051	0.051	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.007	0.012	24.711	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	117	TYR	0	-0.017	-0.005	25.350	0.001	0.001	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.079	0.036	25.065	-0.013	-0.013	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.042	-0.008	23.304	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	120	GLY	0	-0.001	-0.015	21.880	0.056	0.056	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.012	0.011	21.777	-0.057	-0.057	0.000	0.000	0.000	0.000
122	A	122	GLN	0	0.019	0.033	15.507	-0.110	-0.110	0.000	0.000	0.000	0.000
123	A	123	PHE	0	0.000	-0.015	20.477	-0.073	-0.073	0.000	0.000	0.000	0.000
124	A	124	ASN	0	0.035	0.014	17.818	0.132	0.132	0.000	0.000	0.000	0.000
125	A	125	PRO	0	-0.030	-0.003	21.798	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	126	HIS	0	0.037	0.010	23.330	-0.040	-0.040	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.015	-0.010	20.397	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.011	-0.003	18.655	-0.206	-0.206	0.000	0.000	0.000	0.000
129	A	129	PHE	0	-0.004	-0.014	20.019	0.114	0.114	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.008	0.025	16.561	-0.054	-0.054	0.000	0.000	0.000	0.000
131	A	131	ILE	0	-0.010	-0.007	19.848	0.115	0.115	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.772	-0.854	17.568	-0.021	-0.021	0.000	0.000	0.000	0.000
133	A	133	ALA	0	-0.008	0.000	20.914	0.090	0.090	0.000	0.000	0.000	0.000
134	A	134	SER	0	-0.033	-0.030	21.311	0.011	0.011	0.000	0.000	0.000	0.000
135	A	135	TYR	0	-0.014	0.000	23.714	0.014	0.014	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.780	-0.891	22.767	0.580	0.580	0.000	0.000	0.000	0.000
137	A	137	TYR	0	-0.030	-0.018	26.792	-0.013	-0.013	0.000	0.000	0.000	0.000
138	A	138	SER	0	-0.009	-0.021	29.118	0.038	0.038	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.925	0.960	31.200	-0.301	-0.301	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.000	0.000	34.141	0.014	0.014	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.955	-0.962	36.587	0.247	0.247	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.871	-0.920	40.227	0.270	0.270	0.000	0.000	0.000	0.000
143	A	143	VAL	0	-0.001	-0.012	36.954	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.812	0.893	36.738	-0.260	-0.260	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.009	0.007	31.562	0.002	0.002	0.000	0.000	0.000	0.000
146	A	146	GLY	0	0.016	0.011	32.323	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.030	-0.009	26.995	0.014	0.014	0.000	0.000	0.000	0.000
148	A	148	TRP	0	0.003	0.015	27.878	-0.016	-0.016	0.000	0.000	0.000	0.000
149	A	149	MET	0	-0.007	-0.015	22.779	0.065	0.065	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.008	0.001	24.786	-0.050	-0.050	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.027	-0.001	21.909	0.066	0.066	0.000	0.000	0.000	0.000
152	A	152	ALA	0	-0.020	0.002	20.753	-0.087	-0.087	0.000	0.000	0.000	0.000
153	A	153	GLY	0	0.032	0.014	16.738	0.167	0.167	0.000	0.000	0.000	0.000
154	A	154	TYR	0	-0.020	0.002	15.093	-0.093	-0.093	0.000	0.000	0.000	0.000
155	A	155	ARG	1	0.923	0.975	11.557	2.056	2.056	0.000	0.000	0.000	0.000
156	A	156	PHE	-1	-0.847	-0.909	6.544	-4.112	-4.112	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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