FMO DATABASE

FMODB ID: RMN98

Calculation Name: 2M4N-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2M4N

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BIC1

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-823288.800146
FMO2-HF: Nuclear repulsion	780994.872935
FMO2-HF: Total energy	-42293.927211
FMO2-MP2: Total energy	-42416.219216

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:SER)

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

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.
-112.246	-110.798	-0.017	-0.669	-0.763	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.925

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	PHE	0	0.108	0.058	3.853	-0.129	1.319	-0.017	-0.669	-0.763	-0.003
4	A	4	GLY	0	0.004	0.004	6.382	2.658	2.658	0.000	0.000	0.000	0.000
5	A	5	GLY	0	-0.007	0.009	8.772	2.379	2.379	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.009	-0.011	10.829	2.821	2.821	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.006	0.007	10.908	-1.862	-1.862	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.918	0.958	12.513	20.438	20.438	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.040	0.032	14.316	-0.136	-0.136	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.053	-0.058	17.338	0.136	0.136	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.094	0.033	19.900	0.097	0.097	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.024	-0.009	23.618	0.471	0.471	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.895	-0.950	25.749	-10.264	-10.264	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.045	-0.007	26.013	0.383	0.383	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.018	-0.017	27.679	0.405	0.405	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.056	0.033	27.550	-0.351	-0.351	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.058	-0.032	28.141	-0.083	-0.083	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.835	0.918	23.897	11.513	11.513	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.053	0.046	23.294	-0.255	-0.255	0.000	0.000	0.000	0.000
20	A	20	TYR	0	0.026	0.005	17.603	-0.724	-0.724	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.029	-0.014	19.364	0.500	0.500	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.029	-0.002	16.648	-0.639	-0.639	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.023	-0.006	16.439	0.932	0.932	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.018	-0.013	15.529	-1.111	-1.111	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.016	0.010	14.640	0.978	0.978	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.931	-0.971	13.770	-19.561	-19.561	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.041	-0.030	10.666	0.658	0.658	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.043	-0.031	13.797	0.779	0.779	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.851	-0.921	17.186	-15.276	-15.276	0.000	0.000	0.000	0.000
30	A	30	ASN	0	-0.003	-0.016	18.672	-0.584	-0.584	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.063	0.016	20.494	-0.100	-0.100	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.862	-0.939	21.445	-11.275	-11.275	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.914	0.989	20.903	14.040	14.040	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.043	0.026	16.607	0.111	0.111	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.005	-0.002	19.936	0.006	0.006	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.003	-0.003	22.866	0.323	0.323	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.001	0.001	20.759	0.283	0.283	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.016	-0.003	20.594	0.033	0.033	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.004	0.002	22.436	0.288	0.288	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.856	-0.897	25.562	-11.584	-11.584	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.808	0.887	22.052	13.365	13.365	0.000	0.000	0.000	0.000
42	A	42	TYR	0	-0.059	-0.043	23.557	0.151	0.151	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.011	0.013	28.016	0.362	0.362	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.020	-0.020	29.826	0.378	0.378	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.847	-0.922	27.975	-10.848	-10.848	0.000	0.000	0.000	0.000
46	A	46	HIS	0	-0.013	-0.023	30.475	-0.037	-0.037	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.021	-0.009	32.831	0.328	0.328	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.787	0.887	26.427	11.182	11.182	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.848	-0.913	29.794	-9.334	-9.334	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.801	-0.864	32.250	-9.074	-9.074	0.000	0.000	0.000	0.000
51	A	51	PHE	0	0.001	-0.005	26.998	-0.106	-0.106	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.007	-0.007	25.536	0.087	0.087	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.004	0.001	19.253	-0.182	-0.182	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.031	0.003	20.795	0.432	0.432	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.811	-0.885	15.398	-17.873	-17.873	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.017	0.006	17.293	0.730	0.730	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.040	-0.034	15.515	-1.557	-1.557	0.000	0.000	0.000	0.000
58	A	58	ASN	0	-0.053	-0.035	14.005	0.900	0.900	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.882	-0.937	15.439	-16.796	-16.796	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.726	-0.856	18.255	-14.321	-14.321	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.867	-0.935	21.011	-12.753	-12.753	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.874	0.940	20.671	13.627	13.627	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.756	0.879	19.341	14.733	14.733	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.046	0.018	25.205	0.627	0.627	0.000	0.000	0.000	0.000
65	A	65	MET	0	0.003	0.011	26.111	-0.168	-0.168	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.007	-0.016	27.342	0.107	0.107	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.836	-0.913	23.869	-11.605	-11.605	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.040	-0.023	17.977	-0.031	-0.031	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.740	0.874	21.834	10.788	10.788	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.772	-0.870	24.982	-10.231	-10.231	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.060	-0.023	21.890	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.887	-0.941	23.017	-11.046	-11.046	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.063	0.020	21.510	-0.700	-0.700	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.697	0.814	17.741	15.880	15.880	0.000	0.000	0.000	0.000
75	A	75	PRO	0	0.014	-0.011	22.216	-0.347	-0.347	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.015	0.010	18.716	-0.114	-0.114	0.000	0.000	0.000	0.000
77	A	77	PRO	0	0.006	-0.002	23.052	0.141	0.141	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.045	0.009	24.236	-0.437	-0.437	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.025	-0.021	24.687	-0.302	-0.302	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.806	-0.866	20.465	-14.084	-14.084	0.000	0.000	0.000	0.000
81	A	81	CYS	0	0.008	0.005	18.567	0.033	0.033	0.000	0.000	0.000	0.000
82	A	82	PRO	0	0.049	0.033	16.493	-0.596	-0.596	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.012	0.000	12.164	-1.020	-1.020	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.015	0.009	12.139	-2.110	-2.110	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.874	-0.932	12.854	-18.781	-18.781	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.021	0.009	10.991	-0.999	-0.999	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.035	-0.060	7.120	-3.205	-3.205	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.041	-0.005	8.250	-2.770	-2.770	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.827	0.909	10.138	18.712	18.712	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.123	-0.060	5.083	-4.072	-4.072	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.029	0.008	5.604	-4.822	-4.822	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.037	-0.034	7.979	1.719	1.719	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.037	0.021	11.490	0.071	0.071	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.932	-0.955	13.979	-14.709	-14.709	0.000	0.000	0.000	0.000
95	A	95	ASN	0	-0.007	-0.004	14.678	0.277	0.277	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.025	0.010	11.064	-0.402	-0.402	0.000	0.000	0.000	0.000
97	A	97	PHE	0	-0.043	-0.015	6.226	0.195	0.195	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.861	-0.915	8.363	-30.197	-30.197	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.057	-0.026	10.098	1.548	1.548	0.000	0.000	0.000	0.000
100	A	100	PHE	0	-0.037	-0.013	12.041	-1.225	-1.225	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.003	0.002	13.817	1.052	1.052	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.026	-0.014	16.211	-0.070	-0.070	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.008	-0.014	19.475	0.163	0.163	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.841	0.929	23.063	11.055	11.055	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.838	0.873	26.067	9.063	9.063	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.803	0.907	29.639	9.276	9.276	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.082	-0.039	30.718	0.122	0.122	0.000	0.000	0.000	0.000
108	A	108	HIS	-1	-0.955	-0.972	29.997	-8.710	-8.710	0.000	0.000	0.000	0.000

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