FMO DATABASE

FMODB ID: KK613

Calculation Name: 2HE9-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HE9

Chain ID: A

ChEMBL ID:

UniProt ID: P30414

Base Structure: X-ray

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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1825973.368396
FMO2-HF: Nuclear repulsion	1758137.277807
FMO2-HF: Total energy	-67836.090589
FMO2-MP2: Total energy	-68030.004743

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:6:SER)

Summations of interaction energy for fragment #1(A:6: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.
-30.811	-32.812	19.212	-8.744	-8.466	-0.041

Interaction energy analysis for fragmet #1(A:6:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.792 / q_NPA : 0.878

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	8	GLN	0	0.062	0.023	3.847	4.829	6.082	-0.012	-0.455	-0.786	0.000
21	A	26	GLN	0	0.008	0.002	2.088	-3.480	-3.958	5.666	-1.958	-3.230	0.018
22	A	27	LEU	0	-0.007	-0.013	3.183	4.097	4.976	0.022	-0.404	-0.497	0.000
23	A	28	PHE	0	0.014	0.024	1.687	-34.451	-38.726	13.533	-5.725	-3.533	-0.058
24	A	29	SER	0	-0.008	-0.029	3.639	2.632	3.077	0.004	-0.186	-0.262	-0.001
25	A	30	ASP	-1	-0.898	-0.941	4.794	-47.679	-47.504	-0.001	-0.016	-0.158	0.000
4	A	9	CYS	0	-0.038	-0.007	6.618	2.224	2.224	0.000	0.000	0.000	0.000
5	A	10	HIS	0	-0.006	-0.013	9.881	-0.349	-0.349	0.000	0.000	0.000	0.000
6	A	11	PHE	0	-0.033	-0.024	12.952	0.454	0.454	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.759	-0.826	16.193	-16.681	-16.681	0.000	0.000	0.000	0.000
8	A	13	ILE	0	-0.022	-0.024	18.682	0.317	0.317	0.000	0.000	0.000	0.000
9	A	14	GLU	-1	-0.858	-0.933	21.764	-10.835	-10.835	0.000	0.000	0.000	0.000
10	A	15	ILE	0	-0.007	-0.012	24.609	-0.100	-0.100	0.000	0.000	0.000	0.000
11	A	16	ASN	0	-0.036	-0.025	27.633	0.163	0.163	0.000	0.000	0.000	0.000
12	A	17	ARG	1	0.937	0.963	29.620	9.683	9.683	0.000	0.000	0.000	0.000
13	A	18	GLU	-1	-0.886	-0.920	28.659	-10.007	-10.007	0.000	0.000	0.000	0.000
14	A	19	PRO	0	-0.039	-0.034	25.600	-0.343	-0.343	0.000	0.000	0.000	0.000
15	A	20	VAL	0	0.010	0.012	22.799	0.040	0.040	0.000	0.000	0.000	0.000
16	A	21	GLY	0	0.043	0.019	20.902	-0.106	-0.106	0.000	0.000	0.000	0.000
17	A	22	ARG	1	0.785	0.857	14.976	17.990	17.990	0.000	0.000	0.000	0.000
18	A	23	ILE	0	-0.003	0.012	13.181	-0.333	-0.333	0.000	0.000	0.000	0.000
19	A	24	MET	0	-0.004	0.003	9.461	-0.841	-0.841	0.000	0.000	0.000	0.000
20	A	25	PHE	0	0.019	-0.014	8.008	0.427	0.427	0.000	0.000	0.000	0.000
26	A	31	ILE	0	0.011	-0.007	6.403	5.277	5.277	0.000	0.000	0.000	0.000
27	A	32	CYS	0	-0.059	-0.020	7.894	4.015	4.015	0.000	0.000	0.000	0.000
28	A	33	PRO	0	0.081	0.053	8.080	-1.300	-1.300	0.000	0.000	0.000	0.000
29	A	34	LYS	1	0.881	0.943	9.116	17.161	17.161	0.000	0.000	0.000	0.000
30	A	35	THR	0	-0.002	-0.044	10.721	1.691	1.691	0.000	0.000	0.000	0.000
31	A	36	CYS	0	-0.041	0.008	6.687	-0.335	-0.335	0.000	0.000	0.000	0.000
32	A	37	LYS	1	0.958	0.987	8.733	21.964	21.964	0.000	0.000	0.000	0.000
33	A	38	ASN	0	-0.004	-0.010	10.692	1.932	1.932	0.000	0.000	0.000	0.000
34	A	39	PHE	0	0.062	0.026	9.897	0.819	0.819	0.000	0.000	0.000	0.000
35	A	40	LEU	0	0.057	0.022	6.687	0.706	0.706	0.000	0.000	0.000	0.000
36	A	41	CYS	0	-0.046	-0.023	11.226	1.608	1.608	0.000	0.000	0.000	0.000
37	A	42	LEU	0	-0.050	-0.003	14.527	1.534	1.534	0.000	0.000	0.000	0.000
38	A	43	CYS	0	0.001	-0.002	12.724	1.036	1.036	0.000	0.000	0.000	0.000
39	A	44	SER	0	-0.006	-0.026	14.599	0.885	0.885	0.000	0.000	0.000	0.000
40	A	45	GLY	0	-0.023	-0.024	16.205	1.145	1.145	0.000	0.000	0.000	0.000
41	A	46	GLU	-1	-0.798	-0.875	15.049	-19.612	-19.612	0.000	0.000	0.000	0.000
42	A	47	LYS	1	0.801	0.877	16.568	18.851	18.851	0.000	0.000	0.000	0.000
43	A	48	GLY	0	0.030	0.031	20.612	0.546	0.546	0.000	0.000	0.000	0.000
44	A	49	LEU	0	-0.015	-0.011	23.977	-0.205	-0.205	0.000	0.000	0.000	0.000
45	A	50	GLY	0	0.000	0.003	24.564	-0.243	-0.243	0.000	0.000	0.000	0.000
46	A	51	LYS	1	0.889	0.932	23.833	13.360	13.360	0.000	0.000	0.000	0.000
47	A	52	THR	0	-0.057	-0.055	26.734	0.398	0.398	0.000	0.000	0.000	0.000
48	A	53	THR	0	-0.038	-0.042	26.512	0.302	0.302	0.000	0.000	0.000	0.000
49	A	54	GLY	0	0.019	0.017	28.952	0.297	0.297	0.000	0.000	0.000	0.000
50	A	55	LYS	1	0.872	0.941	26.771	10.319	10.319	0.000	0.000	0.000	0.000
51	A	56	LYS	1	0.957	0.980	22.321	13.529	13.529	0.000	0.000	0.000	0.000
52	A	57	LEU	0	-0.015	0.006	20.208	-0.235	-0.235	0.000	0.000	0.000	0.000
53	A	58	CYS	0	-0.099	-0.022	19.019	-0.576	-0.576	0.000	0.000	0.000	0.000
54	A	59	TYR	0	0.011	-0.018	14.059	0.425	0.425	0.000	0.000	0.000	0.000
55	A	60	LYS	1	0.900	0.940	19.173	14.265	14.265	0.000	0.000	0.000	0.000
56	A	61	GLY	0	0.000	0.006	21.382	0.453	0.453	0.000	0.000	0.000	0.000
57	A	62	SER	0	-0.104	-0.056	20.648	0.475	0.475	0.000	0.000	0.000	0.000
58	A	63	THR	0	0.034	0.001	23.237	-0.029	-0.029	0.000	0.000	0.000	0.000
59	A	64	PHE	0	0.035	0.008	17.195	-0.486	-0.486	0.000	0.000	0.000	0.000
60	A	65	HIS	0	-0.036	-0.006	22.527	0.392	0.392	0.000	0.000	0.000	0.000
61	A	66	ARG	1	0.888	0.944	24.230	11.170	11.170	0.000	0.000	0.000	0.000
62	A	67	VAL	0	0.031	0.026	23.602	-0.601	-0.601	0.000	0.000	0.000	0.000
63	A	68	VAL	0	-0.044	-0.026	24.349	0.510	0.510	0.000	0.000	0.000	0.000
64	A	69	LYS	1	0.975	0.982	24.704	9.517	9.517	0.000	0.000	0.000	0.000
65	A	70	ASN	0	-0.063	-0.032	24.812	0.146	0.146	0.000	0.000	0.000	0.000
66	A	71	PHE	0	-0.053	-0.033	21.906	0.045	0.045	0.000	0.000	0.000	0.000
67	A	72	MET	0	-0.013	0.006	19.616	-0.740	-0.740	0.000	0.000	0.000	0.000
68	A	73	ILE	0	0.042	0.042	18.502	0.662	0.662	0.000	0.000	0.000	0.000
69	A	74	GLN	0	0.010	-0.026	18.852	-0.628	-0.628	0.000	0.000	0.000	0.000
70	A	75	GLY	0	0.017	0.014	19.445	0.617	0.617	0.000	0.000	0.000	0.000
71	A	76	GLY	0	0.043	0.022	18.850	-0.361	-0.361	0.000	0.000	0.000	0.000
72	A	77	ASP	-1	-0.733	-0.863	19.768	-11.609	-11.609	0.000	0.000	0.000	0.000
73	A	78	PHE	0	0.043	0.011	20.539	0.397	0.397	0.000	0.000	0.000	0.000
74	A	79	SER	0	-0.045	-0.020	24.037	0.215	0.215	0.000	0.000	0.000	0.000
75	A	80	GLU	-1	-0.943	-0.962	27.210	-9.364	-9.364	0.000	0.000	0.000	0.000
76	A	81	GLY	0	-0.012	0.021	26.541	0.289	0.289	0.000	0.000	0.000	0.000
77	A	82	ASN	0	-0.043	-0.045	27.592	0.078	0.078	0.000	0.000	0.000	0.000
78	A	83	GLY	0	0.026	0.023	25.476	0.160	0.160	0.000	0.000	0.000	0.000
79	A	84	LYS	1	0.904	0.952	26.551	9.110	9.110	0.000	0.000	0.000	0.000
80	A	85	GLY	0	0.012	0.013	26.614	0.070	0.070	0.000	0.000	0.000	0.000
81	A	86	GLY	0	0.020	0.016	22.697	-0.398	-0.398	0.000	0.000	0.000	0.000
82	A	87	GLU	-1	-0.782	-0.847	22.388	-11.720	-11.720	0.000	0.000	0.000	0.000
83	A	88	SER	0	-0.009	-0.016	18.350	-0.676	-0.676	0.000	0.000	0.000	0.000
84	A	89	ILE	0	0.025	-0.006	15.309	0.713	0.713	0.000	0.000	0.000	0.000
85	A	90	TYR	0	-0.086	-0.059	14.226	0.342	0.342	0.000	0.000	0.000	0.000
86	A	91	GLY	0	-0.014	0.010	20.886	0.612	0.612	0.000	0.000	0.000	0.000
87	A	92	GLY	0	0.040	0.023	24.158	0.090	0.090	0.000	0.000	0.000	0.000
88	A	93	TYR	0	-0.026	-0.005	21.909	-0.402	-0.402	0.000	0.000	0.000	0.000
89	A	94	PHE	0	-0.048	-0.022	14.912	0.181	0.181	0.000	0.000	0.000	0.000
90	A	95	LYS	1	0.973	0.963	20.146	12.779	12.779	0.000	0.000	0.000	0.000
91	A	96	ASP	-1	-0.806	-0.895	17.875	-14.952	-14.952	0.000	0.000	0.000	0.000
92	A	97	GLU	-1	-0.794	-0.855	12.225	-23.779	-23.779	0.000	0.000	0.000	0.000
93	A	98	ASN	0	0.011	-0.010	12.212	0.290	0.290	0.000	0.000	0.000	0.000
94	A	99	PHE	0	0.010	0.013	15.309	-0.096	-0.096	0.000	0.000	0.000	0.000
95	A	100	ILE	0	0.008	0.016	13.205	0.970	0.970	0.000	0.000	0.000	0.000
96	A	101	LEU	0	0.005	0.004	7.895	0.475	0.475	0.000	0.000	0.000	0.000
97	A	102	LYS	1	0.860	0.936	12.584	17.340	17.340	0.000	0.000	0.000	0.000
98	A	103	HIS	0	-0.002	-0.018	13.905	-1.263	-1.263	0.000	0.000	0.000	0.000
99	A	104	ASP	-1	-0.796	-0.878	14.173	-17.787	-17.787	0.000	0.000	0.000	0.000
100	A	105	ARG	1	0.821	0.880	11.800	20.639	20.639	0.000	0.000	0.000	0.000
101	A	106	ALA	0	0.029	0.018	15.855	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	107	PHE	0	0.046	0.004	13.502	-0.900	-0.900	0.000	0.000	0.000	0.000
103	A	108	LEU	0	-0.020	0.020	10.248	-1.549	-1.549	0.000	0.000	0.000	0.000
104	A	109	LEU	0	-0.034	0.000	9.031	1.408	1.408	0.000	0.000	0.000	0.000
105	A	110	SER	0	0.000	-0.025	10.914	-1.359	-1.359	0.000	0.000	0.000	0.000
106	A	111	MET	0	0.001	0.012	13.564	0.195	0.195	0.000	0.000	0.000	0.000
107	A	112	ALA	0	-0.009	0.002	15.749	0.749	0.749	0.000	0.000	0.000	0.000
108	A	113	ASN	0	-0.057	-0.042	19.351	0.258	0.258	0.000	0.000	0.000	0.000
109	A	114	ARG	1	0.963	0.974	21.946	10.993	10.993	0.000	0.000	0.000	0.000
110	A	115	GLY	0	0.064	0.038	24.569	0.518	0.518	0.000	0.000	0.000	0.000
111	A	116	LYS	1	0.946	0.977	23.176	11.950	11.950	0.000	0.000	0.000	0.000
112	A	117	HIS	0	-0.032	-0.019	21.662	0.022	0.022	0.000	0.000	0.000	0.000
113	A	118	THR	0	-0.018	-0.007	22.594	0.201	0.201	0.000	0.000	0.000	0.000
114	A	119	ASN	0	-0.016	-0.013	17.477	-0.026	-0.026	0.000	0.000	0.000	0.000
115	A	120	GLY	0	0.050	0.016	19.630	0.082	0.082	0.000	0.000	0.000	0.000
116	A	121	SER	0	0.015	-0.004	17.737	-0.686	-0.686	0.000	0.000	0.000	0.000
117	A	122	GLN	0	-0.049	-0.021	17.537	-0.656	-0.656	0.000	0.000	0.000	0.000
118	A	123	PHE	0	0.011	0.019	14.582	-0.567	-0.567	0.000	0.000	0.000	0.000
119	A	124	PHE	0	-0.051	-0.035	15.900	0.915	0.915	0.000	0.000	0.000	0.000
120	A	125	ILE	0	0.047	0.028	13.849	-1.175	-1.175	0.000	0.000	0.000	0.000
121	A	126	THR	0	-0.040	-0.019	15.278	0.805	0.805	0.000	0.000	0.000	0.000
122	A	127	THR	0	-0.008	-0.035	16.870	-0.608	-0.608	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.905	0.961	19.433	11.701	11.701	0.000	0.000	0.000	0.000
124	A	129	PRO	0	0.001	0.006	18.668	-0.323	-0.323	0.000	0.000	0.000	0.000
125	A	130	ALA	0	-0.022	-0.016	19.215	0.712	0.712	0.000	0.000	0.000	0.000
126	A	131	PRO	0	0.078	0.030	20.139	-0.196	-0.196	0.000	0.000	0.000	0.000
127	A	132	HIS	0	-0.001	0.005	21.160	-0.089	-0.089	0.000	0.000	0.000	0.000
128	A	133	LEU	0	-0.016	-0.004	19.478	0.291	0.291	0.000	0.000	0.000	0.000
129	A	134	ASP	-1	-0.760	-0.873	17.984	-15.939	-15.939	0.000	0.000	0.000	0.000
130	A	135	GLY	0	-0.033	-0.022	19.000	0.601	0.601	0.000	0.000	0.000	0.000
131	A	136	VAL	0	-0.085	-0.037	20.560	0.406	0.406	0.000	0.000	0.000	0.000
132	A	137	HIS	1	0.837	0.921	17.356	14.131	14.131	0.000	0.000	0.000	0.000
133	A	138	VAL	0	0.023	0.019	12.459	-0.114	-0.114	0.000	0.000	0.000	0.000
134	A	139	VAL	0	0.061	0.037	10.152	-0.462	-0.462	0.000	0.000	0.000	0.000
135	A	140	PHE	0	-0.019	-0.033	8.062	-0.570	-0.570	0.000	0.000	0.000	0.000
136	A	141	GLY	0	0.044	0.013	5.958	-5.028	-5.028	0.000	0.000	0.000	0.000
137	A	142	LEU	0	-0.025	-0.002	6.748	2.851	2.851	0.000	0.000	0.000	0.000
138	A	143	VAL	0	-0.008	0.006	7.946	-1.963	-1.963	0.000	0.000	0.000	0.000
139	A	144	ILE	0	-0.041	-0.030	6.880	0.451	0.451	0.000	0.000	0.000	0.000
140	A	145	SER	0	-0.003	-0.005	10.260	1.093	1.093	0.000	0.000	0.000	0.000
141	A	146	GLY	0	0.109	0.064	13.543	-0.577	-0.577	0.000	0.000	0.000	0.000
142	A	147	PHE	0	-0.051	-0.026	12.701	0.264	0.264	0.000	0.000	0.000	0.000
143	A	148	GLU	-1	-0.784	-0.904	17.697	-14.627	-14.627	0.000	0.000	0.000	0.000
144	A	149	VAL	0	0.000	0.012	18.835	0.523	0.523	0.000	0.000	0.000	0.000
145	A	150	ILE	0	-0.051	-0.028	15.804	0.333	0.333	0.000	0.000	0.000	0.000
146	A	151	GLU	-1	-0.911	-0.953	19.684	-11.204	-11.204	0.000	0.000	0.000	0.000
147	A	152	GLN	0	0.009	0.006	22.918	0.296	0.296	0.000	0.000	0.000	0.000
148	A	153	ILE	0	-0.024	-0.022	20.380	0.453	0.453	0.000	0.000	0.000	0.000
149	A	154	GLU	-1	-0.789	-0.882	22.698	-11.891	-11.891	0.000	0.000	0.000	0.000
150	A	155	ASN	0	-0.071	-0.044	24.558	0.763	0.763	0.000	0.000	0.000	0.000
151	A	156	LEU	0	0.000	0.022	26.500	0.454	0.454	0.000	0.000	0.000	0.000
152	A	157	LYS	1	0.903	0.960	29.431	8.294	8.294	0.000	0.000	0.000	0.000
153	A	158	THR	0	0.005	-0.003	29.204	-0.084	-0.084	0.000	0.000	0.000	0.000
154	A	159	ASP	-1	-0.823	-0.907	32.180	-8.716	-8.716	0.000	0.000	0.000	0.000
155	A	160	ALA	0	-0.001	-0.020	33.643	-0.160	-0.160	0.000	0.000	0.000	0.000
156	A	161	ALA	0	-0.043	-0.008	32.430	-0.015	-0.015	0.000	0.000	0.000	0.000
157	A	162	SER	0	-0.063	-0.037	28.653	-0.346	-0.346	0.000	0.000	0.000	0.000
158	A	163	ARG	1	0.926	0.961	28.287	9.367	9.367	0.000	0.000	0.000	0.000
159	A	164	PRO	0	-0.007	-0.003	26.579	0.377	0.377	0.000	0.000	0.000	0.000
160	A	165	TYR	0	-0.021	-0.020	29.867	0.114	0.114	0.000	0.000	0.000	0.000
161	A	166	ALA	0	-0.032	0.003	29.834	0.173	0.173	0.000	0.000	0.000	0.000
162	A	167	ASP	-1	-0.822	-0.895	29.269	-10.756	-10.756	0.000	0.000	0.000	0.000
163	A	168	VAL	0	0.027	0.016	23.082	-0.124	-0.124	0.000	0.000	0.000	0.000
164	A	169	ARG	1	0.784	0.858	24.396	10.702	10.702	0.000	0.000	0.000	0.000
165	A	170	VAL	0	0.036	0.015	18.691	-0.234	-0.234	0.000	0.000	0.000	0.000
166	A	171	ILE	0	-0.022	0.002	21.494	0.099	0.099	0.000	0.000	0.000	0.000
167	A	172	ASP	-1	-0.815	-0.911	20.435	-14.857	-14.857	0.000	0.000	0.000	0.000
168	A	173	CYS	0	-0.101	-0.040	15.941	-0.065	-0.065	0.000	0.000	0.000	0.000
169	A	174	GLY	0	0.065	0.056	14.912	0.736	0.736	0.000	0.000	0.000	0.000
170	A	175	VAL	0	-0.079	-0.045	9.545	-1.293	-1.293	0.000	0.000	0.000	0.000
171	A	176	LEU	0	-0.046	-0.025	9.107	2.231	2.231	0.000	0.000	0.000	0.000
172	A	177	ALA	-1	-0.925	-0.951	7.950	-40.206	-40.206	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:SER)