FMO DATABASE

FMODB ID: 94J62

Calculation Name: 2O5F-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O5F

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RY71

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1544866.464053
FMO2-HF: Nuclear repulsion	1483492.944806
FMO2-HF: Total energy	-61373.519247
FMO2-MP2: Total energy	-61554.652184

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:7:GLU)

Summations of interaction energy for fragment #1(A:7:GLU)

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.
63.59	70.009	1.556	-3.371	-4.604	0.029

Interaction energy analysis for fragmet #1(A:7:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.806 / q_NPA : -0.894

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	9	LEU	0	0.030	0.013	3.818	-6.793	-4.818	-0.014	-0.922	-1.038	0.003
4	A	10	ASP	-1	-0.741	-0.842	6.673	29.105	29.105	0.000	0.000	0.000	0.000
5	A	11	LEU	0	-0.060	-0.027	10.332	-0.830	-0.830	0.000	0.000	0.000	0.000
6	A	12	VAL	0	-0.033	-0.015	12.907	-0.681	-0.681	0.000	0.000	0.000	0.000
7	A	13	ASN	0	-0.010	-0.016	16.133	-0.066	-0.066	0.000	0.000	0.000	0.000
8	A	14	GLU	-1	-0.892	-0.972	19.675	14.156	14.156	0.000	0.000	0.000	0.000
9	A	15	ARG	1	0.837	0.926	22.277	-12.287	-12.287	0.000	0.000	0.000	0.000
10	A	16	ASP	-1	-0.765	-0.846	17.252	16.832	16.832	0.000	0.000	0.000	0.000
11	A	17	GLU	-1	-0.880	-0.927	19.104	13.782	13.782	0.000	0.000	0.000	0.000
12	A	18	VAL	0	-0.004	-0.016	13.978	0.250	0.250	0.000	0.000	0.000	0.000
13	A	19	VAL	0	-0.057	-0.032	15.843	-0.850	-0.850	0.000	0.000	0.000	0.000
14	A	20	GLY	0	0.003	0.007	13.211	-0.461	-0.461	0.000	0.000	0.000	0.000
15	A	21	GLN	0	-0.050	-0.027	7.597	-0.240	-0.240	0.000	0.000	0.000	0.000
16	A	22	ILE	0	-0.017	-0.003	8.008	-1.372	-1.372	0.000	0.000	0.000	0.000
17	A	23	LEU	0	0.009	0.018	2.595	-2.183	0.702	1.379	-1.868	-2.397	0.025
18	A	24	ARG	1	0.988	0.979	2.898	-39.633	-38.506	0.191	-0.529	-0.789	0.001
19	A	25	THR	0	-0.041	-0.032	4.504	-4.225	-4.050	-0.001	-0.015	-0.158	0.000
20	A	26	ASP	-1	-0.852	-0.910	6.329	28.965	28.965	0.000	0.000	0.000	0.000
21	A	27	PRO	0	0.011	0.002	8.664	-2.229	-2.229	0.000	0.000	0.000	0.000
22	A	28	ALA	0	-0.058	-0.033	12.045	-2.306	-2.306	0.000	0.000	0.000	0.000
23	A	29	LEU	0	-0.023	-0.010	7.885	-1.285	-1.285	0.000	0.000	0.000	0.000
24	A	30	ARG	1	0.839	0.925	11.785	-20.623	-20.623	0.000	0.000	0.000	0.000
25	A	31	TRP	0	0.054	0.019	8.549	1.190	1.190	0.000	0.000	0.000	0.000
26	A	32	GLU	-1	-0.753	-0.843	13.707	17.203	17.203	0.000	0.000	0.000	0.000
27	A	33	ARG	1	0.819	0.894	14.343	-17.804	-17.804	0.000	0.000	0.000	0.000
28	A	34	VAL	0	-0.001	0.012	9.523	1.344	1.344	0.000	0.000	0.000	0.000
29	A	35	ARG	1	0.886	0.945	11.421	-21.262	-21.262	0.000	0.000	0.000	0.000
30	A	36	VAL	0	-0.022	-0.008	10.897	1.861	1.861	0.000	0.000	0.000	0.000
31	A	37	VAL	0	-0.004	0.002	12.711	-1.220	-1.220	0.000	0.000	0.000	0.000
32	A	38	ASN	0	-0.002	-0.023	14.805	0.450	0.450	0.000	0.000	0.000	0.000
33	A	39	ALA	0	0.006	0.011	17.569	-0.419	-0.419	0.000	0.000	0.000	0.000
34	A	40	PHE	0	0.001	0.002	20.416	0.028	0.028	0.000	0.000	0.000	0.000
35	A	41	LEU	0	0.019	0.027	23.594	-0.112	-0.112	0.000	0.000	0.000	0.000
36	A	42	ARG	1	0.834	0.879	25.311	-9.378	-9.378	0.000	0.000	0.000	0.000
37	A	43	ASN	0	0.068	0.052	29.041	-0.071	-0.071	0.000	0.000	0.000	0.000
38	A	44	SER	0	-0.091	-0.087	31.949	-0.106	-0.106	0.000	0.000	0.000	0.000
39	A	45	GLN	0	-0.047	-0.022	35.044	-0.268	-0.268	0.000	0.000	0.000	0.000
40	A	46	GLY	0	-0.048	-0.011	34.066	-0.096	-0.096	0.000	0.000	0.000	0.000
41	A	47	GLN	0	-0.023	-0.010	32.268	0.120	0.120	0.000	0.000	0.000	0.000
42	A	48	LEU	0	0.015	-0.008	26.859	0.101	0.101	0.000	0.000	0.000	0.000
43	A	49	TRP	0	0.032	0.020	21.939	-0.050	-0.050	0.000	0.000	0.000	0.000
44	A	50	ILE	0	-0.027	-0.008	24.254	0.441	0.441	0.000	0.000	0.000	0.000
45	A	51	PRO	0	0.031	0.029	20.397	-0.399	-0.399	0.000	0.000	0.000	0.000
46	A	52	ARG	1	0.859	0.929	22.732	-10.311	-10.311	0.000	0.000	0.000	0.000
47	A	53	ARG	1	0.821	0.926	16.450	-15.304	-15.304	0.000	0.000	0.000	0.000
48	A	61	PRO	0	0.022	-0.005	18.682	0.107	0.107	0.000	0.000	0.000	0.000
49	A	62	ASN	0	-0.014	-0.010	20.304	-0.285	-0.285	0.000	0.000	0.000	0.000
50	A	63	ALA	0	-0.029	-0.015	20.506	-0.444	-0.444	0.000	0.000	0.000	0.000
51	A	64	LEU	0	-0.004	0.003	21.584	0.273	0.273	0.000	0.000	0.000	0.000
52	A	65	ASP	-1	-0.767	-0.876	17.080	15.375	15.375	0.000	0.000	0.000	0.000
53	A	66	VAL	0	-0.016	-0.019	17.811	-0.672	-0.672	0.000	0.000	0.000	0.000
54	A	67	SER	0	-0.061	-0.051	19.618	0.109	0.109	0.000	0.000	0.000	0.000
55	A	68	VAL	0	-0.015	-0.003	15.723	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	69	GLY	0	-0.018	-0.024	14.803	-0.559	-0.559	0.000	0.000	0.000	0.000
57	A	70	GLY	0	0.042	0.049	10.746	0.331	0.331	0.000	0.000	0.000	0.000
58	A	71	ALA	0	-0.038	-0.028	6.889	-0.803	-0.803	0.000	0.000	0.000	0.000
59	A	72	VAL	0	-0.010	0.004	8.418	0.464	0.464	0.000	0.000	0.000	0.000
60	A	73	GLN	0	-0.094	-0.058	4.130	6.057	6.314	0.001	-0.037	-0.222	0.000
61	A	74	SER	0	-0.079	-0.080	5.954	-3.160	-3.160	0.000	0.000	0.000	0.000
62	A	75	GLY	0	-0.022	-0.015	7.891	0.819	0.819	0.000	0.000	0.000	0.000
63	A	76	GLU	-1	-0.781	-0.850	8.886	25.043	25.043	0.000	0.000	0.000	0.000
64	A	77	THR	0	-0.017	-0.021	11.167	-0.585	-0.585	0.000	0.000	0.000	0.000
65	A	78	TYR	0	-0.030	-0.063	13.550	0.706	0.706	0.000	0.000	0.000	0.000
66	A	79	GLU	-1	-0.828	-0.910	15.312	13.791	13.791	0.000	0.000	0.000	0.000
67	A	80	GLU	-1	-0.884	-0.940	13.035	18.698	18.698	0.000	0.000	0.000	0.000
68	A	81	ALA	0	0.031	0.030	11.147	0.249	0.249	0.000	0.000	0.000	0.000
69	A	82	PHE	0	-0.040	-0.020	12.057	-0.363	-0.363	0.000	0.000	0.000	0.000
70	A	83	ARG	1	0.749	0.811	15.206	-14.551	-14.551	0.000	0.000	0.000	0.000
71	A	84	ARG	1	0.722	0.840	8.004	-25.584	-25.584	0.000	0.000	0.000	0.000
72	A	85	GLU	-1	-0.760	-0.881	9.601	22.746	22.746	0.000	0.000	0.000	0.000
73	A	86	ALA	0	-0.024	-0.019	12.815	-0.756	-0.756	0.000	0.000	0.000	0.000
74	A	87	ARG	1	0.783	0.864	14.349	-15.769	-15.769	0.000	0.000	0.000	0.000
75	A	88	GLU	-1	-0.875	-0.923	9.452	22.267	22.267	0.000	0.000	0.000	0.000
76	A	89	GLU	-1	-0.754	-0.879	13.496	16.307	16.307	0.000	0.000	0.000	0.000
77	A	90	LEU	0	-0.061	-0.056	15.753	-0.890	-0.890	0.000	0.000	0.000	0.000
78	A	91	ASN	0	-0.081	-0.027	17.909	-0.263	-0.263	0.000	0.000	0.000	0.000
79	A	92	VAL	0	-0.047	-0.030	19.086	-0.690	-0.690	0.000	0.000	0.000	0.000
80	A	93	GLU	-1	-0.778	-0.849	19.179	14.116	14.116	0.000	0.000	0.000	0.000
81	A	94	ILE	0	0.034	0.000	18.599	-0.584	-0.584	0.000	0.000	0.000	0.000
82	A	95	ASP	-1	-0.849	-0.884	20.921	12.560	12.560	0.000	0.000	0.000	0.000
83	A	96	ALA	0	-0.062	-0.022	23.703	-0.436	-0.436	0.000	0.000	0.000	0.000
84	A	97	LEU	0	-0.036	-0.017	24.546	-0.426	-0.426	0.000	0.000	0.000	0.000
85	A	98	SER	0	-0.024	0.004	26.504	0.075	0.075	0.000	0.000	0.000	0.000
86	A	99	TRP	0	0.013	-0.008	22.233	0.169	0.169	0.000	0.000	0.000	0.000
87	A	100	ARG	1	0.847	0.913	25.298	-10.046	-10.046	0.000	0.000	0.000	0.000
88	A	101	PRO	0	0.042	0.011	23.557	0.152	0.152	0.000	0.000	0.000	0.000
89	A	102	LEU	0	-0.093	-0.045	24.189	-0.489	-0.489	0.000	0.000	0.000	0.000
90	A	103	ALA	0	0.004	-0.009	24.194	-0.448	-0.448	0.000	0.000	0.000	0.000
91	A	104	SER	0	0.037	0.022	21.492	0.396	0.396	0.000	0.000	0.000	0.000
92	A	105	PHE	0	-0.040	-0.024	21.235	-0.686	-0.686	0.000	0.000	0.000	0.000
93	A	106	SER	0	0.052	0.034	20.519	0.592	0.592	0.000	0.000	0.000	0.000
94	A	107	PRO	0	-0.007	0.014	18.071	-0.593	-0.593	0.000	0.000	0.000	0.000
95	A	108	PHE	0	0.019	0.007	20.124	-0.384	-0.384	0.000	0.000	0.000	0.000
96	A	109	GLN	0	-0.072	-0.034	23.977	-0.321	-0.321	0.000	0.000	0.000	0.000
97	A	110	THR	0	-0.110	-0.056	23.380	-0.396	-0.396	0.000	0.000	0.000	0.000
98	A	111	THR	0	-0.054	-0.056	24.079	-0.041	-0.041	0.000	0.000	0.000	0.000
99	A	112	LEU	0	-0.037	-0.014	20.116	0.112	0.112	0.000	0.000	0.000	0.000
100	A	113	SER	0	-0.015	-0.048	16.108	0.422	0.422	0.000	0.000	0.000	0.000
101	A	114	SER	0	-0.055	-0.054	13.864	0.708	0.708	0.000	0.000	0.000	0.000
102	A	115	PHE	0	0.025	0.017	15.782	-1.143	-1.143	0.000	0.000	0.000	0.000
103	A	116	MET	0	0.007	0.026	15.629	0.633	0.633	0.000	0.000	0.000	0.000
104	A	117	CYS	0	-0.057	-0.009	17.425	-1.014	-1.014	0.000	0.000	0.000	0.000
105	A	118	VAL	0	0.036	0.008	18.449	0.469	0.469	0.000	0.000	0.000	0.000
106	A	119	TYR	0	0.061	0.026	17.767	-0.379	-0.379	0.000	0.000	0.000	0.000
107	A	120	GLU	-1	-0.726	-0.801	22.409	9.548	9.548	0.000	0.000	0.000	0.000
108	A	121	LEU	0	0.016	0.002	21.580	-0.117	-0.117	0.000	0.000	0.000	0.000
109	A	122	ARG	1	0.784	0.876	25.058	-9.384	-9.384	0.000	0.000	0.000	0.000
110	A	123	SER	0	0.065	0.019	27.556	-0.100	-0.100	0.000	0.000	0.000	0.000
111	A	124	ASP	-1	-0.783	-0.880	29.468	8.437	8.437	0.000	0.000	0.000	0.000
112	A	125	ALA	0	-0.032	0.004	29.104	-0.161	-0.161	0.000	0.000	0.000	0.000
113	A	126	THR	0	-0.005	-0.009	27.722	0.208	0.208	0.000	0.000	0.000	0.000
114	A	127	PRO	0	0.026	0.015	23.025	-0.106	-0.106	0.000	0.000	0.000	0.000
115	A	128	ILE	0	-0.018	0.009	23.821	-0.181	-0.181	0.000	0.000	0.000	0.000
116	A	129	PHE	0	0.013	0.004	20.667	0.241	0.241	0.000	0.000	0.000	0.000
117	A	130	ASN	0	0.038	0.024	14.825	-0.801	-0.801	0.000	0.000	0.000	0.000
118	A	131	PRO	0	-0.004	-0.031	18.601	0.298	0.298	0.000	0.000	0.000	0.000
119	A	132	ASN	0	-0.075	-0.020	14.210	-0.401	-0.401	0.000	0.000	0.000	0.000
120	A	133	ASP	-1	-0.874	-0.938	14.575	16.927	16.927	0.000	0.000	0.000	0.000
121	A	134	ILE	0	-0.058	-0.006	16.688	-0.317	-0.317	0.000	0.000	0.000	0.000
122	A	135	SER	0	-0.033	-0.026	20.017	-0.369	-0.369	0.000	0.000	0.000	0.000
123	A	136	GLY	0	-0.005	-0.007	23.325	-0.470	-0.470	0.000	0.000	0.000	0.000
124	A	137	GLY	0	0.013	-0.002	24.371	0.399	0.399	0.000	0.000	0.000	0.000
125	A	138	GLU	-1	-0.837	-0.875	26.216	9.012	9.012	0.000	0.000	0.000	0.000
126	A	139	TRP	0	-0.013	-0.006	28.536	0.264	0.264	0.000	0.000	0.000	0.000
127	A	140	LEU	0	-0.015	0.000	28.900	-0.298	-0.298	0.000	0.000	0.000	0.000
128	A	141	THR	0	0.044	0.021	31.178	0.197	0.197	0.000	0.000	0.000	0.000
129	A	142	PRO	0	0.065	0.008	30.814	0.074	0.074	0.000	0.000	0.000	0.000
130	A	143	GLU	-1	-0.962	-0.974	31.848	7.682	7.682	0.000	0.000	0.000	0.000
131	A	144	HIS	0	0.051	0.018	34.085	0.069	0.069	0.000	0.000	0.000	0.000
132	A	145	LEU	0	0.000	0.014	26.392	0.056	0.056	0.000	0.000	0.000	0.000
133	A	146	LEU	0	-0.022	-0.025	29.056	0.138	0.138	0.000	0.000	0.000	0.000
134	A	147	ALA	0	-0.026	0.000	31.276	0.004	0.004	0.000	0.000	0.000	0.000
135	A	148	ARG	1	0.818	0.884	29.739	-9.198	-9.198	0.000	0.000	0.000	0.000
136	A	149	ILE	0	-0.026	-0.015	26.640	0.077	0.077	0.000	0.000	0.000	0.000
137	A	150	ALA	0	-0.062	-0.028	29.581	0.027	0.027	0.000	0.000	0.000	0.000
138	A	151	ALA	0	-0.043	-0.017	32.655	-0.121	-0.121	0.000	0.000	0.000	0.000
139	A	152	GLY	0	0.003	0.010	30.537	-0.126	-0.126	0.000	0.000	0.000	0.000
140	A	153	GLU	-1	-0.917	-0.959	28.765	9.515	9.515	0.000	0.000	0.000	0.000
141	A	154	ALA	0	-0.025	-0.012	24.063	0.197	0.197	0.000	0.000	0.000	0.000
142	A	155	ALA	0	0.023	0.004	23.009	-0.046	-0.046	0.000	0.000	0.000	0.000
143	A	156	LYS	1	0.851	0.924	15.032	-15.807	-15.807	0.000	0.000	0.000	0.000
144	A	157	GLY	0	0.012	-0.002	19.503	-0.434	-0.434	0.000	0.000	0.000	0.000
145	A	158	ASP	-1	-0.757	-0.843	18.627	14.151	14.151	0.000	0.000	0.000	0.000
146	A	159	LEU	0	-0.022	0.001	21.172	-0.309	-0.309	0.000	0.000	0.000	0.000
147	A	160	ALA	0	0.040	0.004	22.740	-0.336	-0.336	0.000	0.000	0.000	0.000
148	A	161	GLU	-1	-0.717	-0.816	24.269	10.976	10.976	0.000	0.000	0.000	0.000
149	A	162	LEU	0	0.037	0.019	19.697	-0.321	-0.321	0.000	0.000	0.000	0.000
150	A	163	VAL	0	0.012	0.011	24.405	-0.289	-0.289	0.000	0.000	0.000	0.000
151	A	164	ARG	1	0.966	0.982	27.252	-9.554	-9.554	0.000	0.000	0.000	0.000
152	A	165	ARG	1	0.807	0.898	25.758	-10.978	-10.978	0.000	0.000	0.000	0.000
153	A	166	CYS	0	-0.063	-0.015	25.461	-0.033	-0.033	0.000	0.000	0.000	0.000
154	A	167	TYR	0	-0.085	-0.056	26.928	-0.169	-0.169	0.000	0.000	0.000	0.000
155	A	168	ARG	1	0.917	0.954	31.240	-8.425	-8.425	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLU)