FMO DATABASE

FMODB ID: 8782Y

Calculation Name: 2M1B-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2M1B

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-891959.143872
FMO2-HF: Nuclear repulsion	847592.531158
FMO2-HF: Total energy	-44366.612714
FMO2-MP2: Total energy	-44499.078787

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:HIS)

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

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.
58.535	62.087	5.603	-3.287	-5.871	0.013

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.884 / q_NPA : 0.935

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	VAL	0	0.022	0.026	3.313	2.113	4.359	0.021	-0.841	-1.426	-0.001
4	A	4	PRO	0	-0.052	-0.008	5.018	1.793	1.873	-0.001	-0.007	-0.072	0.000
43	A	43	ILE	0	-0.009	0.001	4.795	-1.834	-1.748	-0.001	-0.005	-0.080	0.000
44	A	44	ASN	0	-0.027	-0.014	2.916	-7.026	-6.055	0.066	-0.345	-0.693	-0.002
45	A	45	LYS	1	0.857	0.924	4.002	24.130	24.346	0.000	-0.014	-0.203	0.000
47	A	47	GLN	0	0.016	-0.008	2.124	-8.967	-9.365	5.518	-1.991	-3.129	0.016
104	A	104	LYS	1	0.768	0.904	4.179	38.823	39.174	0.000	-0.084	-0.268	0.000
5	A	5	GLU	-1	-0.885	-0.952	8.472	-21.596	-21.596	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.054	-0.039	11.490	2.027	2.027	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.026	-0.002	12.326	-1.473	-1.473	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.975	0.985	14.552	16.113	16.113	0.000	0.000	0.000	0.000
9	A	9	PHE	0	0.022	0.008	17.056	-0.426	-0.426	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.045	0.021	18.518	0.680	0.680	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.036	-0.018	21.776	-0.245	-0.245	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.045	0.029	21.835	0.658	0.658	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.009	-0.005	18.818	-0.860	-0.860	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.024	0.010	16.571	0.607	0.607	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.000	0.009	16.576	-1.369	-1.369	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.009	-0.018	11.541	0.683	0.683	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.023	-0.009	14.312	0.118	0.118	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.980	0.997	17.351	12.790	12.790	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.067	-0.021	17.874	0.524	0.524	0.000	0.000	0.000	0.000
20	A	20	THR	0	0.019	0.007	20.277	0.725	0.725	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.051	-0.027	21.158	-0.653	-0.653	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.858	-0.920	22.456	-11.418	-11.418	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.016	-0.030	24.151	-0.402	-0.402	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.003	-0.022	26.810	0.166	0.166	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.958	-0.959	29.732	-8.500	-8.500	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.049	0.023	30.061	0.275	0.275	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.027	-0.009	26.246	-0.449	-0.449	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.001	0.011	25.625	0.356	0.356	0.000	0.000	0.000	0.000
29	A	29	HIS	0	0.001	0.004	24.856	-0.213	-0.213	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.041	-0.032	20.354	0.152	0.152	0.000	0.000	0.000	0.000
31	A	31	THR	0	0.004	-0.028	23.978	-0.057	-0.057	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.053	0.038	21.037	-0.439	-0.439	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.019	0.002	19.707	-0.372	-0.372	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.775	-0.833	19.937	-10.743	-10.743	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.020	-0.016	18.031	-0.580	-0.580	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.034	0.014	15.939	-0.787	-0.787	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.036	-0.024	14.256	-0.855	-0.855	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.002	0.007	13.103	-0.773	-0.773	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.904	0.973	11.824	15.646	15.646	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.772	0.876	8.026	19.420	19.420	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.028	0.019	8.223	-1.608	-1.608	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.007	0.000	7.516	-1.718	-1.718	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.007	0.018	6.674	-1.820	-1.820	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.005	0.007	6.623	1.497	1.497	0.000	0.000	0.000	0.000
49	A	49	CYS	0	0.020	0.029	8.552	-0.815	-0.815	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.067	0.025	10.501	1.028	1.028	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.915	0.963	14.226	12.066	12.066	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.955	0.954	16.851	11.293	11.293	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.112	0.061	11.567	0.123	0.123	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.042	0.020	12.087	-0.337	-0.337	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.071	-0.031	14.395	0.152	0.152	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.913	-0.953	14.853	-14.386	-14.386	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.862	-0.916	9.133	-21.365	-21.365	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.023	-0.020	13.321	0.016	0.016	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.951	0.977	16.219	12.763	12.763	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.057	-0.026	14.636	0.346	0.346	0.000	0.000	0.000	0.000
61	A	61	HIS	0	-0.002	-0.001	14.298	-0.696	-0.696	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.041	0.033	17.050	0.334	0.334	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.954	0.988	20.220	10.215	10.215	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.031	-0.030	21.329	0.382	0.382	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.007	-0.001	23.178	0.240	0.240	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.034	0.018	26.242	0.287	0.287	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.018	-0.010	25.411	0.082	0.082	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.982	0.993	27.506	8.700	8.700	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.001	-0.001	23.974	-0.123	-0.123	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.073	0.035	17.416	0.114	0.114	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.786	-0.885	19.951	-12.229	-12.229	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.021	-0.021	21.701	0.095	0.095	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.019	0.003	21.302	0.099	0.099	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.028	0.012	17.055	-0.045	-0.045	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.009	-0.001	20.710	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.074	-0.060	24.159	0.272	0.272	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.021	0.015	17.721	0.058	0.058	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.943	0.967	22.182	10.963	10.963	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.936	0.979	23.000	9.271	9.271	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.854	0.923	23.840	10.409	10.409	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.001	0.016	17.073	-0.093	-0.093	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.053	0.036	21.556	-0.158	-0.158	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.003	-0.012	21.571	-0.196	-0.196	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.026	-0.045	12.327	-0.287	-0.287	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.003	-0.003	16.970	-0.478	-0.478	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.048	-0.033	19.212	0.318	0.318	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.871	0.965	13.635	15.755	15.755	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.001	-0.003	14.201	-0.788	-0.788	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.029	0.031	15.072	0.820	0.820	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.034	-0.021	15.972	-0.338	-0.338	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.060	0.032	15.083	0.692	0.692	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.957	0.969	18.583	10.424	10.424	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.015	-0.004	19.976	0.487	0.487	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.025	0.009	14.339	-0.163	-0.163	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.002	0.001	14.900	-0.527	-0.527	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.111	-0.088	13.372	0.835	0.835	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.050	0.033	10.297	-0.928	-0.928	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.003	-0.022	7.025	0.930	0.930	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.005	0.003	10.580	-1.105	-1.105	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.849	-0.922	11.640	-17.874	-17.874	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.895	-0.946	11.934	-18.242	-18.242	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.032	0.008	9.390	-0.365	-0.365	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.886	-0.941	8.437	-27.042	-27.042	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.965	0.964	8.758	23.585	23.585	0.000	0.000	0.000	0.000
106	A	106	PHE	0	0.039	0.027	7.164	-1.252	-1.252	0.000	0.000	0.000	0.000
107	A	107	SER	0	0.013	0.000	9.741	1.246	1.246	0.000	0.000	0.000	0.000
108	A	108	GLN	0	-0.044	-0.017	10.491	0.561	0.561	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.003	0.010	12.717	0.200	0.200	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.874	-0.933	16.542	-15.795	-15.795	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.016	-0.017	18.997	0.467	0.467	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.878	0.926	17.289	17.184	17.184	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.001	0.001	23.453	0.286	0.286	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.022	-0.009	27.038	0.141	0.141	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.048	-0.012	28.717	0.047	0.047	0.000	0.000	0.000	0.000
116	A	116	GLU	-2	-1.881	-1.932	25.814	-23.232	-23.232	0.000	0.000	0.000	0.000

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