FMO DATABASE

FMODB ID: VQ771

Calculation Name: 5AP8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5AP8

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UWV6

Base Structure: X-ray

Registration Date: 2023-09-24

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	151
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1548388.275095
FMO2-HF: Nuclear repulsion	1488942.067888
FMO2-HF: Total energy	-59446.207208
FMO2-MP2: Total energy	-59624.743399

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.
-16.125	-9.996	10.35	-4.599	-11.882	-0.028

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 : -0.003 / q_NPA : 0.003

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	3	VAL	0	0.023	0.009	3.715	-1.736	0.103	0.002	-0.820	-1.022	0.003
4	A	4	TYR	0	-0.036	-0.024	5.783	0.453	0.453	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.023	0.013	9.338	-0.120	-0.120	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.021	-0.020	12.429	0.088	0.088	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.872	-0.952	15.721	-0.172	-0.172	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.025	-0.004	18.833	0.041	0.041	0.000	0.000	0.000	0.000
9	A	18	GLY	0	0.052	0.032	15.539	0.015	0.015	0.000	0.000	0.000	0.000
10	A	19	LYS	1	0.896	0.918	15.214	0.175	0.175	0.000	0.000	0.000	0.000
11	A	20	LYS	1	0.873	0.946	13.763	0.440	0.440	0.000	0.000	0.000	0.000
12	A	21	LEU	0	0.079	0.019	8.767	0.067	0.067	0.000	0.000	0.000	0.000
13	A	22	VAL	0	0.020	0.033	10.623	0.042	0.042	0.000	0.000	0.000	0.000
14	A	23	LYS	1	0.922	0.968	12.925	0.144	0.144	0.000	0.000	0.000	0.000
15	A	24	LEU	0	-0.075	-0.058	11.200	0.066	0.066	0.000	0.000	0.000	0.000
16	A	25	LYS	1	0.951	0.982	10.087	-0.650	-0.650	0.000	0.000	0.000	0.000
17	A	26	ILE	0	0.028	0.025	5.302	0.234	0.234	0.000	0.000	0.000	0.000
18	A	27	ALA	0	0.001	0.005	6.348	-0.334	-0.334	0.000	0.000	0.000	0.000
19	A	28	GLU	-1	-0.862	-0.933	8.934	0.606	0.606	0.000	0.000	0.000	0.000
20	A	29	PHE	0	0.000	-0.010	11.827	-0.078	-0.078	0.000	0.000	0.000	0.000
21	A	30	THR	0	-0.017	-0.023	12.654	0.095	0.095	0.000	0.000	0.000	0.000
22	A	31	ARG	1	0.950	0.975	15.170	-0.081	-0.081	0.000	0.000	0.000	0.000
23	A	32	VAL	0	-0.025	-0.002	15.586	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	33	GLY	0	0.030	0.030	13.251	0.013	0.013	0.000	0.000	0.000	0.000
25	A	34	LYS	1	0.825	0.914	9.342	-0.345	-0.345	0.000	0.000	0.000	0.000
26	A	35	GLY	0	0.018	0.026	7.588	-0.071	-0.071	0.000	0.000	0.000	0.000
27	A	36	VAL	0	0.013	0.003	7.564	-0.045	-0.045	0.000	0.000	0.000	0.000
28	A	37	VAL	0	-0.031	-0.020	9.067	-0.141	-0.141	0.000	0.000	0.000	0.000
29	A	38	LEU	0	0.002	0.000	8.758	0.020	0.020	0.000	0.000	0.000	0.000
30	A	39	ASP	-1	-0.790	-0.905	12.623	-0.118	-0.118	0.000	0.000	0.000	0.000
31	A	40	PRO	0	-0.009	0.002	16.393	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	41	PHE	0	-0.025	-0.021	19.093	0.015	0.015	0.000	0.000	0.000	0.000
33	A	42	ALA	0	-0.043	0.003	17.833	0.029	0.029	0.000	0.000	0.000	0.000
34	A	43	GLN	0	0.014	-0.010	19.819	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	44	ILE	0	-0.031	-0.002	16.485	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	45	THR	0	-0.039	-0.028	16.458	-0.024	-0.024	0.000	0.000	0.000	0.000
37	A	46	LEU	0	-0.026	-0.002	8.976	0.039	0.039	0.000	0.000	0.000	0.000
38	A	47	SER	0	0.028	0.008	12.133	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	48	ASN	0	0.012	0.010	10.846	0.021	0.021	0.000	0.000	0.000	0.000
40	A	49	LYS	1	0.876	0.917	11.860	0.193	0.193	0.000	0.000	0.000	0.000
41	A	50	ASP	-1	-0.786	-0.885	9.638	0.055	0.055	0.000	0.000	0.000	0.000
42	A	51	LYS	1	0.897	0.937	6.816	-0.033	-0.033	0.000	0.000	0.000	0.000
43	A	52	ASP	-1	-0.818	-0.907	5.887	1.346	1.346	0.000	0.000	0.000	0.000
44	A	53	ILE	0	-0.039	-0.013	7.534	0.678	0.678	0.000	0.000	0.000	0.000
45	A	54	VAL	0	0.033	0.020	2.267	-0.391	0.076	1.047	-0.325	-1.188	-0.002
46	A	55	ARG	1	0.858	0.914	2.742	-1.907	-0.019	5.464	-3.340	-4.012	-0.001
47	A	56	ARG	1	0.935	0.974	3.846	0.867	-0.507	-0.009	2.170	-0.788	-0.002
48	A	57	ILE	0	-0.047	-0.021	5.884	-0.223	-0.223	0.000	0.000	0.000	0.000
49	A	58	GLY	0	0.033	0.022	3.007	-0.246	0.001	0.058	-0.111	-0.194	0.000
50	A	59	ILE	0	0.014	0.014	3.480	-0.540	-0.120	0.009	-0.044	-0.385	0.000
51	A	60	THR	0	-0.009	-0.014	6.032	-0.040	-0.040	0.000	0.000	0.000	0.000
52	A	61	ILE	0	-0.015	-0.021	9.021	-0.038	-0.038	0.000	0.000	0.000	0.000
53	A	62	VAL	0	0.015	0.012	11.544	0.074	0.074	0.000	0.000	0.000	0.000
54	A	63	ASP	-1	-0.924	-0.955	15.323	-0.353	-0.353	0.000	0.000	0.000	0.000
55	A	64	THR	0	0.015	0.004	16.905	0.042	0.042	0.000	0.000	0.000	0.000
56	A	65	SER	0	-0.016	-0.005	19.121	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	66	TRP	0	0.056	0.014	19.479	0.009	0.009	0.000	0.000	0.000	0.000
58	A	67	ASN	0	-0.033	-0.030	22.377	0.006	0.006	0.000	0.000	0.000	0.000
59	A	68	ASN	0	0.002	-0.008	25.219	0.003	0.003	0.000	0.000	0.000	0.000
60	A	69	THR	0	-0.005	0.017	21.536	0.013	0.013	0.000	0.000	0.000	0.000
61	A	70	SER	0	0.004	0.004	24.110	0.013	0.013	0.000	0.000	0.000	0.000
62	A	71	GLN	0	0.042	0.001	23.222	0.008	0.008	0.000	0.000	0.000	0.000
63	A	72	SER	0	-0.066	-0.050	23.789	0.015	0.015	0.000	0.000	0.000	0.000
64	A	73	GLU	-1	-0.771	-0.851	20.845	-0.125	-0.125	0.000	0.000	0.000	0.000
65	A	74	PHE	0	0.026	0.001	15.867	0.000	0.000	0.000	0.000	0.000	0.000
66	A	75	LYS	1	0.887	0.950	19.725	0.022	0.022	0.000	0.000	0.000	0.000
67	A	76	ASN	0	-0.010	-0.008	21.699	0.000	0.000	0.000	0.000	0.000	0.000
68	A	77	ILE	0	0.011	0.028	15.412	0.028	0.028	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.957	0.986	15.905	-0.325	-0.325	0.000	0.000	0.000	0.000
70	A	79	GLY	0	0.040	0.011	13.171	0.003	0.003	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.845	-0.909	11.823	0.145	0.145	0.000	0.000	0.000	0.000
72	A	81	HIS	1	0.771	0.872	12.841	-0.025	-0.025	0.000	0.000	0.000	0.000
73	A	82	ARG	1	0.784	0.870	11.984	0.019	0.019	0.000	0.000	0.000	0.000
74	A	83	ARG	1	0.832	0.911	14.449	0.224	0.224	0.000	0.000	0.000	0.000
75	A	84	ILE	0	-0.016	-0.025	12.528	-0.032	-0.032	0.000	0.000	0.000	0.000
76	A	85	PRO	0	-0.010	0.007	14.752	0.044	0.044	0.000	0.000	0.000	0.000
77	A	86	ILE	0	-0.018	0.007	17.877	-0.042	-0.042	0.000	0.000	0.000	0.000
78	A	87	LEU	0	0.019	0.019	15.083	-0.047	-0.047	0.000	0.000	0.000	0.000
79	A	88	PHE	0	0.008	-0.004	19.610	0.042	0.042	0.000	0.000	0.000	0.000
80	A	89	ALA	0	0.022	0.023	19.668	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	90	GLY	0	0.043	0.007	19.618	0.033	0.033	0.000	0.000	0.000	0.000
82	A	91	ASN	0	-0.042	-0.030	19.523	0.053	0.053	0.000	0.000	0.000	0.000
83	A	92	PRO	0	-0.017	-0.028	21.425	0.018	0.018	0.000	0.000	0.000	0.000
84	A	93	ILE	0	-0.046	-0.017	23.644	0.025	0.025	0.000	0.000	0.000	0.000
85	A	94	HIS	0	0.004	-0.012	23.054	0.027	0.027	0.000	0.000	0.000	0.000
86	A	95	TYR	0	0.016	0.018	24.175	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	96	GLY	0	0.017	0.012	24.390	0.027	0.027	0.000	0.000	0.000	0.000
88	A	97	ILE	0	-0.037	-0.015	25.079	0.011	0.011	0.000	0.000	0.000	0.000
89	A	98	ALA	0	0.058	0.029	23.272	-0.030	-0.030	0.000	0.000	0.000	0.000
90	A	99	TYR	0	-0.030	-0.042	20.021	0.030	0.030	0.000	0.000	0.000	0.000
91	A	100	LYS	1	0.850	0.944	19.720	0.221	0.221	0.000	0.000	0.000	0.000
92	A	101	LEU	0	-0.033	-0.010	15.223	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	102	SER	0	-0.027	-0.053	16.344	0.008	0.008	0.000	0.000	0.000	0.000
94	A	103	SER	0	0.052	0.007	12.536	-0.074	-0.074	0.000	0.000	0.000	0.000
95	A	104	ILE	0	-0.010	-0.014	10.336	-0.121	-0.121	0.000	0.000	0.000	0.000
96	A	105	GLU	-1	-0.749	-0.819	11.278	-0.736	-0.736	0.000	0.000	0.000	0.000
97	A	106	ALA	0	0.054	0.035	12.032	-0.087	-0.087	0.000	0.000	0.000	0.000
98	A	107	LEU	0	-0.009	0.003	4.998	-0.096	-0.096	0.000	0.000	0.000	0.000
99	A	108	ILE	0	-0.021	-0.002	7.767	-0.401	-0.401	0.000	0.000	0.000	0.000
100	A	109	ALA	0	0.036	0.017	9.579	-0.139	-0.139	0.000	0.000	0.000	0.000
101	A	110	THR	0	-0.022	-0.035	6.235	0.112	0.112	0.000	0.000	0.000	0.000
102	A	111	LEU	0	-0.025	-0.022	2.701	-0.862	-0.045	0.322	-0.194	-0.945	-0.001
103	A	112	TYR	0	-0.024	-0.040	6.253	-0.130	-0.130	0.000	0.000	0.000	0.000
104	A	113	ILE	0	0.019	0.009	9.200	0.127	0.127	0.000	0.000	0.000	0.000
105	A	114	VAL	0	-0.083	-0.037	4.419	0.201	0.292	-0.001	-0.005	-0.085	0.000
106	A	115	ASP	-1	-0.868	-0.956	6.533	-1.102	-1.102	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.835	-0.884	2.434	-10.493	-9.300	3.369	-1.848	-2.715	-0.025
108	A	117	VAL	0	0.026	0.006	5.486	-0.342	-0.342	0.000	0.000	0.000	0.000
109	A	118	GLU	-1	-0.845	-0.917	5.872	-2.460	-2.460	0.000	0.000	0.000	0.000
110	A	119	GLU	-1	-0.815	-0.907	2.891	-2.443	-1.902	0.089	-0.082	-0.548	0.000
111	A	120	ALA	0	-0.056	-0.015	6.328	0.264	0.264	0.000	0.000	0.000	0.000
112	A	121	ILE	0	0.026	0.015	8.707	0.411	0.411	0.000	0.000	0.000	0.000
113	A	122	LYS	1	0.781	0.881	5.891	2.452	2.452	0.000	0.000	0.000	0.000
114	A	123	LEU	0	0.015	0.008	6.169	0.350	0.350	0.000	0.000	0.000	0.000
115	A	124	SER	0	-0.052	-0.043	9.038	0.267	0.267	0.000	0.000	0.000	0.000
116	A	125	ASN	0	0.057	0.037	12.271	0.136	0.136	0.000	0.000	0.000	0.000
117	A	126	VAL	0	-0.022	0.010	10.109	0.138	0.138	0.000	0.000	0.000	0.000
118	A	127	VAL	0	-0.063	-0.039	13.297	0.120	0.120	0.000	0.000	0.000	0.000
119	A	128	LYS	1	1.021	1.005	16.190	0.247	0.247	0.000	0.000	0.000	0.000
120	A	129	TRP	0	0.018	0.008	16.529	0.011	0.011	0.000	0.000	0.000	0.000
121	A	130	GLY	0	0.006	0.008	15.228	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	131	HIS	0	0.013	-0.014	16.107	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	132	THR	0	-0.004	-0.002	17.975	0.000	0.000	0.000	0.000	0.000	0.000
124	A	133	PHE	0	-0.003	0.000	13.564	0.006	0.006	0.000	0.000	0.000	0.000
125	A	134	ILE	0	0.019	0.020	12.901	0.001	0.001	0.000	0.000	0.000	0.000
126	A	135	GLU	-1	-0.833	-0.928	16.871	-0.518	-0.518	0.000	0.000	0.000	0.000
127	A	136	LEU	0	-0.083	-0.008	20.165	0.040	0.040	0.000	0.000	0.000	0.000
128	A	137	ASN	0	-0.019	-0.025	18.014	0.070	0.070	0.000	0.000	0.000	0.000
129	A	138	LYS	1	0.943	0.983	17.054	0.561	0.561	0.000	0.000	0.000	0.000
130	A	139	GLU	-1	-0.889	-0.955	17.346	-0.452	-0.452	0.000	0.000	0.000	0.000
131	A	140	LEU	0	0.027	0.018	19.356	0.013	0.013	0.000	0.000	0.000	0.000
132	A	141	LEU	0	-0.039	-0.023	13.440	-0.025	-0.025	0.000	0.000	0.000	0.000
133	A	142	GLU	-1	-0.783	-0.869	14.390	-0.931	-0.931	0.000	0.000	0.000	0.000
134	A	143	ALA	0	-0.060	-0.031	16.493	0.016	0.016	0.000	0.000	0.000	0.000
135	A	144	TYR	0	-0.055	-0.058	14.997	0.045	0.045	0.000	0.000	0.000	0.000
136	A	145	LYS	1	0.828	0.916	10.297	0.963	0.963	0.000	0.000	0.000	0.000
137	A	146	ASN	0	-0.073	-0.039	11.668	0.183	0.183	0.000	0.000	0.000	0.000
138	A	147	LYS	1	0.866	0.966	12.812	0.618	0.618	0.000	0.000	0.000	0.000
139	A	148	THR	0	-0.019	-0.036	15.166	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	149	GLU	-1	-0.719	-0.845	16.933	-0.164	-0.164	0.000	0.000	0.000	0.000
141	A	150	GLU	-1	-0.903	-0.959	17.827	-0.152	-0.152	0.000	0.000	0.000	0.000
142	A	151	ASP	-1	-0.830	-0.893	19.604	-0.230	-0.230	0.000	0.000	0.000	0.000
143	A	152	ILE	0	-0.053	-0.020	14.629	-0.016	-0.016	0.000	0.000	0.000	0.000
144	A	153	LYS	1	0.860	0.916	19.027	0.172	0.172	0.000	0.000	0.000	0.000
145	A	154	LYS	1	0.748	0.848	21.426	0.190	0.190	0.000	0.000	0.000	0.000
146	A	155	ILE	0	0.057	0.026	20.598	0.011	0.011	0.000	0.000	0.000	0.000
147	A	156	GLU	-1	-0.729	-0.815	20.977	-0.311	-0.311	0.000	0.000	0.000	0.000
148	A	157	ARG	1	0.868	0.918	23.065	0.191	0.191	0.000	0.000	0.000	0.000
149	A	158	GLU	-1	-0.798	-0.865	26.453	-0.177	-0.177	0.000	0.000	0.000	0.000
150	A	159	ILE	0	-0.045	-0.009	23.076	0.005	0.005	0.000	0.000	0.000	0.000
151	A	160	ILE	0	-0.032	0.003	25.167	0.012	0.012	0.000	0.000	0.000	0.000

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