FMO DATABASE

FMODB ID: MN2GZ

Calculation Name: 2HY5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HY5

Chain ID: A

ChEMBL ID:

UniProt ID: O87896

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1142428.288955
FMO2-HF: Nuclear repulsion	1091433.631793
FMO2-HF: Total energy	-50994.657161
FMO2-MP2: Total energy	-51144.709788

3D Structure

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:MET)

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

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.
-27.586	-31.103	31.484	-12.182	-15.785	-0.069

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.056 / q_NPA : -0.035

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	PHE	0	-0.025	-0.022	3.712	0.435	3.206	0.014	-1.239	-1.546	0.003
4	A	4	ALA	0	0.034	0.027	5.899	-0.042	-0.042	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.025	-0.015	9.053	0.351	0.351	0.000	0.000	0.000	0.000
6	A	6	GLN	0	-0.023	-0.015	11.866	-0.036	-0.036	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.015	-0.003	15.259	0.084	0.084	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.039	0.007	18.206	-0.059	-0.059	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.856	-0.920	21.464	-0.033	-0.033	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.003	0.001	23.324	-0.030	-0.030	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.018	-0.009	24.958	0.015	0.015	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.018	-0.007	25.882	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.031	0.000	27.815	0.011	0.011	0.000	0.000	0.000	0.000
14	A	14	HIS	1	0.889	0.944	24.646	0.032	0.032	0.000	0.000	0.000	0.000
15	A	15	GLN	0	0.016	0.006	21.645	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.035	0.032	19.866	-0.014	-0.014	0.000	0.000	0.000	0.000
17	A	17	SER	0	0.032	-0.001	18.684	-0.033	-0.033	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.786	-0.880	18.885	-0.169	-0.169	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.029	-0.027	17.160	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.020	0.016	14.472	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.017	0.010	14.022	-0.080	-0.080	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.003	-0.015	15.045	-0.096	-0.096	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.037	-0.004	7.495	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.026	-0.003	10.489	-0.132	-0.132	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.963	0.986	10.532	0.112	0.112	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.025	0.014	11.414	-0.068	-0.068	0.000	0.000	0.000	0.000
27	A	27	ALA	0	-0.054	-0.031	6.471	0.003	0.003	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.005	-0.009	6.728	-0.538	-0.538	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.950	-0.964	8.846	-0.475	-0.475	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.850	0.923	6.488	-0.129	-0.129	0.000	0.000	0.000	0.000
31	A	31	GLY	0	-0.005	0.008	6.613	0.291	0.291	0.000	0.000	0.000	0.000
32	A	32	HIS	0	-0.035	-0.001	1.877	-7.743	-15.163	17.844	-5.809	-4.615	-0.034
33	A	33	GLU	-1	-0.865	-0.936	3.579	-2.082	-1.442	0.002	-0.170	-0.472	0.000
34	A	34	ILE	0	-0.046	-0.014	5.633	-0.649	-0.649	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.012	0.014	8.149	0.431	0.431	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.834	0.895	9.687	1.281	1.281	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.013	0.017	11.976	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	38	PHE	0	-0.002	-0.017	14.497	0.072	0.072	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.019	0.005	16.833	0.065	0.065	0.000	0.000	0.000	0.000
40	A	40	TYR	0	0.014	-0.027	20.064	0.004	0.004	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.007	0.006	21.982	0.011	0.011	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.767	-0.889	25.195	-0.112	-0.112	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.004	0.019	22.398	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.035	-0.025	23.328	-0.031	-0.031	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.014	0.008	24.928	-0.025	-0.025	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.063	-0.028	22.568	0.016	0.016	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.027	0.008	24.095	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.012	0.011	25.500	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.882	0.916	28.899	0.202	0.202	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.032	-0.021	30.711	0.007	0.007	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.022	0.010	29.498	0.012	0.012	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.017	-0.016	32.620	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	53	PRO	0	-0.035	-0.016	30.052	0.012	0.012	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.030	0.010	33.097	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	55	GLN	0	0.010	-0.012	32.949	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.960	-0.954	33.038	-0.074	-0.074	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.813	-0.890	29.005	-0.076	-0.076	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.705	0.830	24.586	0.081	0.081	0.000	0.000	0.000	0.000
59	A	59	HIS	0	0.073	0.037	26.843	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.012	-0.020	22.575	-0.027	-0.027	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.016	-0.002	23.187	-0.032	-0.032	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.002	-0.012	23.814	-0.046	-0.046	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.978	1.018	20.523	0.194	0.194	0.000	0.000	0.000	0.000
64	A	64	TRP	0	-0.024	-0.025	14.997	-0.074	-0.074	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.032	-0.015	19.240	-0.070	-0.070	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.916	-0.965	21.001	-0.348	-0.348	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.037	-0.010	13.946	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.011	-0.028	16.273	-0.102	-0.102	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.907	-0.951	17.418	-0.562	-0.562	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.019	-0.004	15.896	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	TYR	0	-0.042	-0.035	11.566	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.946	-0.955	13.232	-1.041	-1.041	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.036	-0.012	11.786	-0.109	-0.109	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.710	-0.809	14.365	-0.677	-0.677	0.000	0.000	0.000	0.000
75	A	75	MET	0	-0.033	-0.012	15.774	-0.037	-0.037	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.023	-0.021	17.492	0.064	0.064	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.029	0.017	19.698	0.021	0.021	0.000	0.000	0.000	0.000
78	A	78	CYS	0	-0.068	0.001	22.491	0.019	0.019	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.105	0.034	23.684	0.023	0.023	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.023	0.013	26.917	0.020	0.020	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.064	-0.052	25.720	0.020	0.020	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.066	0.032	27.386	0.015	0.015	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.061	-0.028	28.867	0.024	0.024	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.860	0.932	29.923	0.125	0.125	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.818	0.883	28.544	0.130	0.130	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.026	0.051	32.361	0.006	0.006	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.057	-0.012	27.584	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.004	-0.022	30.890	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.809	-0.913	29.648	-0.267	-0.267	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.821	-0.944	31.830	-0.198	-0.198	0.000	0.000	0.000	0.000
91	A	91	GLY	0	-0.030	-0.004	32.819	0.013	0.013	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.868	-0.944	31.152	-0.190	-0.190	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.010	0.007	34.124	0.015	0.015	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.028	0.002	37.163	0.015	0.015	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.926	0.953	32.669	0.204	0.204	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.046	-0.023	34.519	0.012	0.012	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.024	0.002	38.787	0.008	0.008	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.860	0.931	37.377	0.131	0.131	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.919	-0.951	40.656	-0.120	-0.120	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.017	0.001	39.182	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.000	0.013	33.957	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.018	-0.028	32.572	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.002	0.022	26.077	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.042	0.026	25.606	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.010	-0.016	26.655	-0.019	-0.019	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.882	0.949	21.203	0.469	0.469	0.000	0.000	0.000	0.000
107	A	107	PHE	0	-0.026	0.001	21.288	-0.055	-0.055	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.825	0.891	18.171	0.681	0.681	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.037	0.023	22.949	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.003	-0.008	21.828	-0.013	-0.013	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.031	0.011	23.589	0.028	0.028	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.043	-0.001	20.715	-0.039	-0.039	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.009	0.008	19.770	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	114	GLN	0	0.019	0.014	17.856	-0.089	-0.089	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.006	0.024	14.744	-0.105	-0.105	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.009	-0.016	14.526	-0.040	-0.040	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.904	-0.969	14.568	-0.892	-0.892	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.045	0.017	11.422	-0.105	-0.105	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.061	-0.028	10.052	-0.204	-0.204	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.070	-0.025	10.127	0.057	0.057	0.000	0.000	0.000	0.000
121	A	121	GLN	0	-0.039	-0.010	9.939	-0.171	-0.171	0.000	0.000	0.000	0.000
122	A	122	ALA	0	-0.057	-0.012	6.137	-0.559	-0.559	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.820	-0.902	2.039	-11.214	-8.382	5.855	-3.633	-5.053	-0.030
124	A	124	ARG	1	0.836	0.903	2.028	-2.474	-4.814	7.769	-1.331	-4.099	-0.008
125	A	125	LEU	0	0.045	0.031	5.923	-0.781	-0.781	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.038	-0.017	8.221	0.302	0.302	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.003	-0.008	10.992	-0.207	-0.207	0.000	0.000	0.000	0.000
128	A	128	PHE	0	-0.006	-0.001	12.155	0.087	0.087	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.003	-0.021	17.061	-0.056	-0.056	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.842	-0.916	20.728	0.021	0.021	0.000	0.000	0.000	0.000

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