FMO DATABASE

FMODB ID: M2M1Z

Calculation Name: 2RH3-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2RH3

Chain ID: A

ChEMBL ID:

UniProt ID: P07166

Base Structure: X-ray

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-983588.510069
FMO2-HF: Nuclear repulsion	936816.897846
FMO2-HF: Total energy	-46771.612224
FMO2-MP2: Total energy	-46908.446018

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:82:ILE)

Summations of interaction energy for fragment #1(A:82:ILE)

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.
26.6	33.628	9.994	-6.954	-10.069	-0.068

Interaction energy analysis for fragmet #1(A:82:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / q_NPA : 0.921

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	84	VAL	0	-0.022	0.001	2.768	-2.719	0.411	0.238	-1.354	-2.015	-0.006
4	A	85	PHE	0	0.026	-0.001	5.006	2.114	2.177	-0.001	-0.005	-0.057	0.000
76	A	157	MET	0	-0.004	0.012	4.107	-11.786	-11.143	0.022	-0.269	-0.396	-0.002
77	A	158	PHE	0	0.082	0.033	2.948	10.801	12.109	0.022	-0.484	-0.846	0.000
78	A	159	PRO	0	0.032	0.013	1.925	-43.286	-43.440	7.370	-4.014	-3.202	-0.053
79	A	160	VAL	0	0.016	-0.002	2.295	-2.268	-1.215	1.758	-0.605	-2.206	-0.006
80	A	161	SER	0	0.058	0.037	3.895	4.519	4.676	0.002	-0.016	-0.143	0.000
82	A	163	ILE	0	-0.026	-0.018	2.390	1.658	2.406	0.584	-0.206	-1.126	-0.001
83	A	164	GLU	-1	-0.935	-0.957	5.238	-24.723	-24.643	-0.001	-0.001	-0.078	0.000
5	A	86	LEU	0	-0.023	-0.011	8.388	0.173	0.173	0.000	0.000	0.000	0.000
6	A	87	SER	0	-0.022	-0.012	11.148	0.821	0.821	0.000	0.000	0.000	0.000
7	A	88	ALA	0	0.053	0.024	14.909	-0.139	-0.139	0.000	0.000	0.000	0.000
8	A	89	ARG	1	0.900	0.949	17.772	12.762	12.762	0.000	0.000	0.000	0.000
9	A	90	PRO	0	0.029	0.023	21.626	-0.338	-0.338	0.000	0.000	0.000	0.000
10	A	91	PRO	0	0.010	0.017	23.570	0.069	0.069	0.000	0.000	0.000	0.000
11	A	92	ALA	0	-0.050	-0.024	25.819	0.186	0.186	0.000	0.000	0.000	0.000
12	A	93	PRO	0	0.047	0.011	29.520	-0.179	-0.179	0.000	0.000	0.000	0.000
13	A	94	GLU	-1	-0.946	-0.968	32.015	-8.726	-8.726	0.000	0.000	0.000	0.000
14	A	95	VAL	0	-0.141	-0.055	26.648	-0.095	-0.095	0.000	0.000	0.000	0.000
15	A	96	SER	0	-0.071	-0.079	26.079	-0.359	-0.359	0.000	0.000	0.000	0.000
16	A	97	LYS	1	1.002	1.006	28.194	9.428	9.428	0.000	0.000	0.000	0.000
17	A	98	ILE	0	-0.027	-0.016	25.107	0.027	0.027	0.000	0.000	0.000	0.000
18	A	99	TYR	0	0.003	-0.023	24.451	-0.374	-0.374	0.000	0.000	0.000	0.000
19	A	100	ASP	-1	-0.792	-0.909	26.866	-10.147	-10.147	0.000	0.000	0.000	0.000
20	A	101	ASN	0	-0.004	-0.001	30.503	0.503	0.503	0.000	0.000	0.000	0.000
21	A	102	LEU	0	-0.059	-0.028	24.623	-0.019	-0.019	0.000	0.000	0.000	0.000
22	A	103	ILE	0	-0.042	-0.022	27.837	0.001	0.001	0.000	0.000	0.000	0.000
23	A	104	LEU	0	0.004	0.019	30.023	0.282	0.282	0.000	0.000	0.000	0.000
24	A	105	GLN	0	-0.046	-0.022	30.235	-0.055	-0.055	0.000	0.000	0.000	0.000
25	A	106	TYR	0	-0.020	-0.016	26.639	-0.344	-0.344	0.000	0.000	0.000	0.000
26	A	107	SER	0	0.060	0.028	25.630	0.028	0.028	0.000	0.000	0.000	0.000
27	A	108	PRO	0	0.087	0.040	25.842	-0.441	-0.441	0.000	0.000	0.000	0.000
28	A	109	SER	0	-0.004	-0.002	21.515	-0.699	-0.699	0.000	0.000	0.000	0.000
29	A	110	LYS	1	0.946	0.987	21.155	12.055	12.055	0.000	0.000	0.000	0.000
30	A	111	SER	0	0.035	0.002	21.943	-0.431	-0.431	0.000	0.000	0.000	0.000
31	A	112	LEU	0	0.029	0.016	19.333	-0.289	-0.289	0.000	0.000	0.000	0.000
32	A	113	GLN	0	-0.041	-0.026	16.993	-0.360	-0.360	0.000	0.000	0.000	0.000
33	A	114	MET	0	-0.100	-0.043	17.625	-0.877	-0.877	0.000	0.000	0.000	0.000
34	A	115	ILE	0	0.037	0.040	19.521	-0.517	-0.517	0.000	0.000	0.000	0.000
35	A	116	LEU	0	0.011	0.006	13.688	-0.700	-0.700	0.000	0.000	0.000	0.000
36	A	117	ARG	1	0.938	0.967	14.323	17.692	17.692	0.000	0.000	0.000	0.000
37	A	118	ARG	1	0.825	0.900	14.670	14.790	14.790	0.000	0.000	0.000	0.000
38	A	119	ALA	0	0.037	0.018	16.329	-0.594	-0.594	0.000	0.000	0.000	0.000
39	A	120	LEU	0	-0.005	-0.018	10.505	-0.682	-0.682	0.000	0.000	0.000	0.000
40	A	121	GLY	0	-0.023	0.000	12.193	-1.615	-1.615	0.000	0.000	0.000	0.000
41	A	122	ASP	-1	-0.822	-0.890	13.548	-16.394	-16.394	0.000	0.000	0.000	0.000
42	A	123	PHE	0	0.014	-0.013	12.365	0.264	0.264	0.000	0.000	0.000	0.000
43	A	124	GLU	-1	-0.801	-0.903	7.617	-36.584	-36.584	0.000	0.000	0.000	0.000
44	A	125	ASN	0	-0.008	-0.007	11.615	-0.682	-0.682	0.000	0.000	0.000	0.000
45	A	126	MET	0	0.015	0.014	14.629	0.685	0.685	0.000	0.000	0.000	0.000
46	A	127	LEU	0	-0.078	-0.034	9.167	0.178	0.178	0.000	0.000	0.000	0.000
47	A	128	ALA	0	-0.036	-0.017	12.539	0.011	0.011	0.000	0.000	0.000	0.000
48	A	129	ASP	-1	-0.773	-0.851	13.636	-16.355	-16.355	0.000	0.000	0.000	0.000
49	A	130	GLY	0	-0.036	-0.018	15.589	0.764	0.764	0.000	0.000	0.000	0.000
50	A	131	SER	0	-0.043	-0.058	16.597	0.594	0.594	0.000	0.000	0.000	0.000
51	A	132	PHE	0	-0.069	-0.037	12.813	0.570	0.570	0.000	0.000	0.000	0.000
52	A	133	ARG	1	0.911	0.968	14.395	18.150	18.150	0.000	0.000	0.000	0.000
53	A	134	ALA	0	0.010	0.006	18.134	0.498	0.498	0.000	0.000	0.000	0.000
54	A	135	ALA	0	-0.009	0.012	18.572	0.537	0.537	0.000	0.000	0.000	0.000
55	A	136	PRO	0	-0.003	-0.015	20.324	-0.112	-0.112	0.000	0.000	0.000	0.000
56	A	137	LYS	1	0.894	0.952	17.365	14.803	14.803	0.000	0.000	0.000	0.000
57	A	138	SER	0	-0.028	-0.018	19.165	-0.465	-0.465	0.000	0.000	0.000	0.000
58	A	139	TYR	0	-0.048	-0.032	19.816	-0.058	-0.058	0.000	0.000	0.000	0.000
59	A	140	PRO	0	0.028	0.015	24.747	-0.095	-0.095	0.000	0.000	0.000	0.000
60	A	141	ILE	0	0.010	0.008	24.356	-0.325	-0.325	0.000	0.000	0.000	0.000
61	A	142	PRO	0	0.013	0.003	27.435	0.346	0.346	0.000	0.000	0.000	0.000
62	A	143	HIS	0	-0.040	-0.010	29.372	0.027	0.027	0.000	0.000	0.000	0.000
63	A	144	THR	0	0.044	0.016	33.123	0.382	0.382	0.000	0.000	0.000	0.000
64	A	145	ALA	0	0.030	0.014	34.879	-0.183	-0.183	0.000	0.000	0.000	0.000
65	A	146	PHE	0	-0.017	-0.003	36.721	0.036	0.036	0.000	0.000	0.000	0.000
66	A	147	GLU	-1	-0.914	-0.957	30.481	-10.260	-10.260	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.960	0.972	30.910	9.834	9.834	0.000	0.000	0.000	0.000
68	A	149	SER	0	0.026	0.013	25.969	-0.425	-0.425	0.000	0.000	0.000	0.000
69	A	150	ILE	0	0.009	0.010	23.194	-0.082	-0.082	0.000	0.000	0.000	0.000
70	A	151	ILE	0	-0.048	-0.031	18.178	-0.047	-0.047	0.000	0.000	0.000	0.000
71	A	152	VAL	0	0.002	0.015	17.797	-0.022	-0.022	0.000	0.000	0.000	0.000
72	A	153	GLN	0	0.025	0.001	15.339	-1.559	-1.559	0.000	0.000	0.000	0.000
73	A	154	THR	0	-0.012	-0.011	11.790	1.104	1.104	0.000	0.000	0.000	0.000
74	A	155	SER	0	-0.035	-0.016	8.361	0.045	0.045	0.000	0.000	0.000	0.000
75	A	156	ARG	1	0.856	0.913	7.588	35.569	35.569	0.000	0.000	0.000	0.000
81	A	162	LEU	0	0.046	0.026	6.783	2.457	2.457	0.000	0.000	0.000	0.000
84	A	165	ALA	0	0.000	0.000	7.156	2.782	2.782	0.000	0.000	0.000	0.000
85	A	166	ALA	0	0.007	0.000	7.677	2.174	2.174	0.000	0.000	0.000	0.000
86	A	167	ARG	1	0.888	0.933	4.952	31.130	31.130	0.000	0.000	0.000	0.000
87	A	168	ASN	0	0.025	0.015	9.050	1.939	1.939	0.000	0.000	0.000	0.000
88	A	169	HIS	0	-0.037	-0.014	12.029	1.653	1.653	0.000	0.000	0.000	0.000
89	A	170	PHE	0	-0.015	-0.029	10.750	1.032	1.032	0.000	0.000	0.000	0.000
90	A	171	ASP	-1	-0.795	-0.912	10.245	-20.516	-20.516	0.000	0.000	0.000	0.000
91	A	172	PRO	0	-0.001	0.012	12.373	-0.368	-0.368	0.000	0.000	0.000	0.000
92	A	173	LEU	0	-0.010	-0.008	14.714	0.722	0.722	0.000	0.000	0.000	0.000
93	A	174	GLY	0	-0.009	0.014	11.855	0.231	0.231	0.000	0.000	0.000	0.000
94	A	175	LEU	0	-0.021	-0.017	12.897	0.375	0.375	0.000	0.000	0.000	0.000
95	A	176	GLU	-1	-0.883	-0.930	11.886	-16.246	-16.246	0.000	0.000	0.000	0.000
96	A	177	THR	0	0.021	0.002	11.202	-1.527	-1.527	0.000	0.000	0.000	0.000
97	A	178	ALA	0	0.001	-0.012	7.138	-0.535	-0.535	0.000	0.000	0.000	0.000
98	A	179	ARG	1	1.003	1.008	8.720	16.166	16.166	0.000	0.000	0.000	0.000
99	A	180	ALA	0	-0.036	-0.006	11.473	0.332	0.332	0.000	0.000	0.000	0.000
100	A	181	PHE	0	0.070	0.028	5.520	0.161	0.161	0.000	0.000	0.000	0.000
101	A	182	GLY	0	0.038	0.016	9.293	-0.229	-0.229	0.000	0.000	0.000	0.000
102	A	183	HIS	0	-0.028	-0.009	9.958	0.087	0.087	0.000	0.000	0.000	0.000
103	A	184	LYS	1	0.830	0.923	12.916	17.431	17.431	0.000	0.000	0.000	0.000
104	A	185	LEU	0	0.007	0.018	7.797	0.565	0.565	0.000	0.000	0.000	0.000
105	A	186	ALA	0	-0.001	-0.008	11.853	0.363	0.363	0.000	0.000	0.000	0.000
106	A	187	THR	0	-0.036	-0.030	13.603	1.176	1.176	0.000	0.000	0.000	0.000
107	A	188	ALA	0	0.030	0.010	15.022	0.840	0.840	0.000	0.000	0.000	0.000
108	A	189	ALA	0	-0.009	0.011	13.884	0.606	0.606	0.000	0.000	0.000	0.000
109	A	190	LEU	0	-0.014	-0.012	16.008	0.690	0.690	0.000	0.000	0.000	0.000
110	A	191	ALA	0	-0.010	0.008	18.808	0.776	0.776	0.000	0.000	0.000	0.000
111	A	192	CYS	0	-0.068	-0.029	18.691	0.875	0.875	0.000	0.000	0.000	0.000
112	A	193	PHE	0	-0.004	-0.003	19.751	0.388	0.388	0.000	0.000	0.000	0.000
113	A	194	PHE	0	0.045	0.004	21.569	0.426	0.426	0.000	0.000	0.000	0.000
114	A	195	ALA	0	-0.003	0.003	24.028	0.584	0.584	0.000	0.000	0.000	0.000
115	A	196	ARG	1	0.949	0.979	20.602	14.677	14.677	0.000	0.000	0.000	0.000
116	A	197	GLU	-1	-0.700	-0.815	25.647	-11.520	-11.520	0.000	0.000	0.000	0.000
117	A	198	LYS	1	0.932	0.978	27.793	10.124	10.124	0.000	0.000	0.000	0.000
118	A	199	ALA	0	-0.046	-0.025	28.552	0.369	0.369	0.000	0.000	0.000	0.000
119	A	200	THR	0	-0.038	-0.042	28.568	0.179	0.179	0.000	0.000	0.000	0.000
120	A	201	ASN	0	-0.058	-0.018	31.409	0.152	0.152	0.000	0.000	0.000	0.000
121	A	202	SER	-1	-0.929	-0.958	30.288	-9.817	-9.817	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:82:ILE)