FMO DATABASE

FMODB ID: 1646Z

Calculation Name: 3ASD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ASD

Chain ID: A

ChEMBL ID:

UniProt ID: Q2W8Q0

Base Structure: X-ray

Registration Date: 2023-09-26

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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1166519.602287
FMO2-HF: Nuclear repulsion	1114547.440118
FMO2-HF: Total energy	-51972.162169
FMO2-MP2: Total energy	-52127.854188

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:78:PHE)

Summations of interaction energy for fragment #1(A:78:PHE)

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.
-25.982	-16.299	12.901	-7.221	-15.366	0.038

Interaction energy analysis for fragmet #1(A:78:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.017 / q_NPA : 0.002

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	80	VAL	0	0.065	0.012	2.855	-0.209	2.833	0.155	-1.174	-2.024	0.004
4	A	81	ASP	-1	-0.884	-0.925	4.585	-1.444	-1.161	0.000	-0.021	-0.262	0.000
5	A	82	VAL	0	-0.032	-0.037	6.168	0.393	0.393	0.000	0.000	0.000	0.000
6	A	83	ALA	0	-0.026	0.000	2.663	-0.782	-0.146	1.142	-0.525	-1.253	0.001
7	A	84	LEU	0	0.037	0.032	4.433	-0.056	0.088	-0.001	-0.018	-0.126	0.000
8	A	85	HIS	0	0.028	0.006	7.444	0.271	0.271	0.000	0.000	0.000	0.000
9	A	86	LEU	0	-0.040	-0.022	5.443	0.123	0.123	0.000	0.000	0.000	0.000
10	A	87	GLY	0	0.024	0.001	7.166	0.114	0.114	0.000	0.000	0.000	0.000
11	A	88	ILE	0	-0.024	-0.023	8.052	0.109	0.109	0.000	0.000	0.000	0.000
12	A	89	ALA	0	-0.019	-0.001	11.364	0.055	0.055	0.000	0.000	0.000	0.000
13	A	90	TYR	0	0.034	0.019	8.214	0.096	0.096	0.000	0.000	0.000	0.000
14	A	91	VAL	0	0.014	0.009	11.736	0.028	0.028	0.000	0.000	0.000	0.000
15	A	92	LYS	1	0.857	0.940	14.109	0.085	0.085	0.000	0.000	0.000	0.000
16	A	93	THR	0	-0.057	-0.038	15.362	0.016	0.016	0.000	0.000	0.000	0.000
17	A	94	GLY	0	0.018	0.022	16.795	0.018	0.018	0.000	0.000	0.000	0.000
18	A	95	ALA	0	-0.049	-0.004	13.802	0.013	0.013	0.000	0.000	0.000	0.000
19	A	96	VAL	0	0.030	-0.016	12.994	0.005	0.005	0.000	0.000	0.000	0.000
20	A	97	ASP	-1	-0.922	-0.935	12.975	0.340	0.340	0.000	0.000	0.000	0.000
21	A	98	ARG	1	1.015	0.999	8.926	-0.583	-0.583	0.000	0.000	0.000	0.000
22	A	99	GLY	0	-0.007	-0.011	8.117	0.043	0.043	0.000	0.000	0.000	0.000
23	A	100	THR	0	-0.002	-0.015	7.674	-0.198	-0.198	0.000	0.000	0.000	0.000
24	A	101	GLU	-1	-0.874	-0.922	6.941	0.866	0.866	0.000	0.000	0.000	0.000
25	A	102	LEU	0	-0.062	-0.031	2.867	-0.915	-0.098	0.135	-0.201	-0.751	-0.002
26	A	103	LEU	0	-0.022	-0.023	4.154	-1.111	-0.884	-0.001	-0.061	-0.166	0.000
27	A	104	GLU	-1	-0.852	-0.902	6.873	-0.172	-0.172	0.000	0.000	0.000	0.000
28	A	105	ARG	1	0.887	0.936	2.392	-20.089	-17.691	11.088	-3.988	-9.498	0.051
29	A	106	SER	0	-0.114	-0.044	2.801	-4.748	-2.688	0.383	-1.213	-1.230	-0.016
30	A	107	LEU	0	-0.016	-0.044	4.175	0.236	0.312	0.000	-0.020	-0.056	0.000
31	A	108	ALA	0	0.029	-0.008	6.504	0.131	0.131	0.000	0.000	0.000	0.000
32	A	109	ASP	-1	-0.882	-0.901	8.181	-0.473	-0.473	0.000	0.000	0.000	0.000
33	A	110	ALA	0	-0.073	-0.027	6.485	-0.015	-0.015	0.000	0.000	0.000	0.000
34	A	111	PRO	0	-0.054	-0.035	7.128	0.016	0.016	0.000	0.000	0.000	0.000
35	A	112	ASP	-1	-0.797	-0.877	10.124	-0.633	-0.633	0.000	0.000	0.000	0.000
36	A	113	ASN	0	0.084	0.025	6.509	0.393	0.393	0.000	0.000	0.000	0.000
37	A	114	VAL	0	0.016	0.029	10.269	0.128	0.128	0.000	0.000	0.000	0.000
38	A	115	LYS	1	0.809	0.883	12.098	0.853	0.853	0.000	0.000	0.000	0.000
39	A	116	VAL	0	0.033	0.034	12.311	0.102	0.102	0.000	0.000	0.000	0.000
40	A	117	ALA	0	0.056	0.020	11.266	0.101	0.101	0.000	0.000	0.000	0.000
41	A	118	THR	0	-0.037	-0.022	13.373	0.114	0.114	0.000	0.000	0.000	0.000
42	A	119	VAL	0	-0.014	-0.008	16.652	0.060	0.060	0.000	0.000	0.000	0.000
43	A	120	LEU	0	0.009	0.029	13.722	0.059	0.059	0.000	0.000	0.000	0.000
44	A	121	GLY	0	0.035	0.019	16.784	0.050	0.050	0.000	0.000	0.000	0.000
45	A	122	LEU	0	0.000	-0.015	18.018	0.044	0.044	0.000	0.000	0.000	0.000
46	A	123	THR	0	-0.010	-0.023	20.899	0.036	0.036	0.000	0.000	0.000	0.000
47	A	124	TYR	0	-0.024	-0.022	15.938	0.043	0.043	0.000	0.000	0.000	0.000
48	A	125	VAL	0	0.005	0.007	21.399	0.027	0.027	0.000	0.000	0.000	0.000
49	A	126	GLN	0	-0.070	-0.020	23.819	0.008	0.008	0.000	0.000	0.000	0.000
50	A	127	VAL	0	-0.067	-0.033	23.338	0.015	0.015	0.000	0.000	0.000	0.000
51	A	128	GLN	0	-0.005	0.007	26.153	0.015	0.015	0.000	0.000	0.000	0.000
52	A	129	LYS	1	0.933	0.985	21.355	0.152	0.152	0.000	0.000	0.000	0.000
53	A	130	TYR	0	0.060	-0.002	21.156	-0.021	-0.021	0.000	0.000	0.000	0.000
54	A	131	ASP	-1	-0.865	-0.951	20.626	-0.113	-0.113	0.000	0.000	0.000	0.000
55	A	132	LEU	0	-0.038	-0.009	15.486	0.003	0.003	0.000	0.000	0.000	0.000
56	A	133	ALA	0	-0.020	-0.020	16.515	-0.031	-0.031	0.000	0.000	0.000	0.000
57	A	134	VAL	0	0.031	0.025	17.739	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	135	PRO	0	0.045	0.013	13.428	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	136	LEU	0	0.005	0.011	11.903	-0.043	-0.043	0.000	0.000	0.000	0.000
60	A	137	LEU	0	-0.003	-0.001	14.129	-0.048	-0.048	0.000	0.000	0.000	0.000
61	A	138	ILE	0	-0.021	-0.011	15.383	0.000	0.000	0.000	0.000	0.000	0.000
62	A	139	LYS	1	0.812	0.880	10.633	0.118	0.118	0.000	0.000	0.000	0.000
63	A	140	VAL	0	-0.033	-0.018	12.845	-0.054	-0.054	0.000	0.000	0.000	0.000
64	A	141	ALA	0	-0.041	-0.025	14.397	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	142	GLU	-1	-0.876	-0.914	13.175	-0.150	-0.150	0.000	0.000	0.000	0.000
66	A	143	ALA	0	0.033	0.033	11.823	0.013	0.013	0.000	0.000	0.000	0.000
67	A	144	ASN	0	-0.048	-0.034	13.823	0.030	0.030	0.000	0.000	0.000	0.000
68	A	145	PRO	0	0.006	0.009	17.236	0.037	0.037	0.000	0.000	0.000	0.000
69	A	146	ILE	0	0.028	0.009	19.695	0.036	0.036	0.000	0.000	0.000	0.000
70	A	147	ASN	0	0.004	0.010	19.993	0.033	0.033	0.000	0.000	0.000	0.000
71	A	148	PHE	0	0.036	0.011	22.464	0.006	0.006	0.000	0.000	0.000	0.000
72	A	149	ASN	0	0.019	-0.012	24.280	0.021	0.021	0.000	0.000	0.000	0.000
73	A	150	VAL	0	0.032	0.020	18.573	0.010	0.010	0.000	0.000	0.000	0.000
74	A	151	ARG	1	0.931	0.979	20.442	0.197	0.197	0.000	0.000	0.000	0.000
75	A	152	PHE	0	0.022	0.011	23.616	0.016	0.016	0.000	0.000	0.000	0.000
76	A	153	ARG	1	0.904	0.945	23.431	0.192	0.192	0.000	0.000	0.000	0.000
77	A	154	LEU	0	0.035	0.036	19.754	0.006	0.006	0.000	0.000	0.000	0.000
78	A	155	GLY	0	0.053	0.024	22.867	0.017	0.017	0.000	0.000	0.000	0.000
79	A	156	VAL	0	-0.076	-0.038	26.286	0.010	0.010	0.000	0.000	0.000	0.000
80	A	157	ALA	0	0.024	0.002	22.958	0.009	0.009	0.000	0.000	0.000	0.000
81	A	158	LEU	0	-0.011	-0.004	21.884	0.011	0.011	0.000	0.000	0.000	0.000
82	A	159	ASP	-1	-0.799	-0.880	25.128	-0.054	-0.054	0.000	0.000	0.000	0.000
83	A	160	ASN	0	-0.009	-0.006	27.240	0.000	0.000	0.000	0.000	0.000	0.000
84	A	161	LEU	0	-0.090	-0.050	22.062	0.007	0.007	0.000	0.000	0.000	0.000
85	A	162	GLY	0	0.012	0.028	26.726	0.010	0.010	0.000	0.000	0.000	0.000
86	A	163	ARG	1	0.743	0.838	20.234	0.051	0.051	0.000	0.000	0.000	0.000
87	A	164	PHE	0	0.069	0.012	27.463	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	165	ASP	-1	-0.809	-0.916	29.536	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	166	GLU	-1	-0.791	-0.854	22.588	-0.040	-0.040	0.000	0.000	0.000	0.000
90	A	167	ALA	0	0.004	0.005	26.263	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	168	ILE	0	0.008	0.004	27.690	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	169	ASP	-1	-0.822	-0.892	27.018	-0.048	-0.048	0.000	0.000	0.000	0.000
93	A	170	SER	0	-0.044	-0.033	24.281	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	171	PHE	0	-0.007	-0.026	26.098	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	172	LYS	1	0.843	0.914	29.261	0.043	0.043	0.000	0.000	0.000	0.000
96	A	173	ILE	0	-0.007	-0.001	24.181	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	174	ALA	0	-0.024	-0.011	27.293	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	175	LEU	0	-0.012	-0.022	28.342	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	176	GLY	0	-0.018	-0.002	30.579	0.004	0.004	0.000	0.000	0.000	0.000
100	A	177	LEU	0	-0.063	-0.015	25.066	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	178	ARG	1	0.853	0.908	29.031	0.164	0.164	0.000	0.000	0.000	0.000
102	A	179	PRO	0	0.033	0.026	32.554	0.003	0.003	0.000	0.000	0.000	0.000
103	A	180	ASN	0	0.004	-0.019	35.569	0.009	0.009	0.000	0.000	0.000	0.000
104	A	181	GLU	-1	-0.746	-0.833	32.318	-0.143	-0.143	0.000	0.000	0.000	0.000
105	A	182	GLY	0	0.114	0.050	35.615	0.003	0.003	0.000	0.000	0.000	0.000
106	A	183	LYS	1	0.778	0.879	31.340	0.145	0.145	0.000	0.000	0.000	0.000
107	A	184	VAL	0	0.004	-0.009	31.253	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	185	HIS	0	0.042	0.040	33.801	0.008	0.008	0.000	0.000	0.000	0.000
109	A	186	ARG	1	0.967	0.978	36.875	0.083	0.083	0.000	0.000	0.000	0.000
110	A	187	ALA	0	0.015	0.012	32.490	0.004	0.004	0.000	0.000	0.000	0.000
111	A	188	ILE	0	0.005	0.018	32.599	0.004	0.004	0.000	0.000	0.000	0.000
112	A	189	ALA	0	-0.037	-0.018	34.604	0.007	0.007	0.000	0.000	0.000	0.000
113	A	190	PHE	0	0.015	-0.002	35.904	0.004	0.004	0.000	0.000	0.000	0.000
114	A	191	SER	0	0.017	-0.014	32.187	0.002	0.002	0.000	0.000	0.000	0.000
115	A	192	TYR	0	-0.086	-0.055	34.388	0.003	0.003	0.000	0.000	0.000	0.000
116	A	193	GLU	-1	-0.847	-0.918	37.007	-0.030	-0.030	0.000	0.000	0.000	0.000
117	A	194	GLN	0	-0.091	-0.039	33.522	0.006	0.006	0.000	0.000	0.000	0.000
118	A	195	MET	0	-0.060	0.010	33.783	0.002	0.002	0.000	0.000	0.000	0.000
119	A	196	GLY	0	-0.009	0.012	37.251	0.004	0.004	0.000	0.000	0.000	0.000
120	A	197	ARG	1	0.751	0.845	34.470	0.025	0.025	0.000	0.000	0.000	0.000
121	A	198	HIS	0	0.025	-0.020	41.129	0.000	0.000	0.000	0.000	0.000	0.000
122	A	199	GLU	-1	-0.987	-0.988	43.718	-0.024	-0.024	0.000	0.000	0.000	0.000
123	A	200	GLU	-1	-0.812	-0.904	38.624	-0.028	-0.028	0.000	0.000	0.000	0.000
124	A	201	ALA	0	0.007	0.010	40.142	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	202	LEU	0	0.006	0.017	41.155	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	203	PRO	0	0.022	0.006	42.201	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	204	HIS	1	0.858	0.942	37.297	0.054	0.054	0.000	0.000	0.000	0.000
128	A	205	PHE	0	0.065	0.029	40.567	-0.006	-0.006	0.000	0.000	0.000	0.000
129	A	206	LYS	1	0.914	0.952	42.816	0.036	0.036	0.000	0.000	0.000	0.000
130	A	207	LYS	1	0.920	0.962	40.333	0.070	0.070	0.000	0.000	0.000	0.000
131	A	208	ALA	0	-0.024	-0.036	39.995	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	209	ASN	0	-0.069	-0.031	41.330	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	210	GLU	-1	-0.920	-0.951	44.504	-0.058	-0.058	0.000	0.000	0.000	0.000
134	A	211	LEU	0	-0.120	-0.054	39.120	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	212	ASP	-1	-0.932	-0.964	41.931	-0.093	-0.093	0.000	0.000	0.000	0.000
136	A	213	GLU	-1	-0.958	-0.987	44.316	-0.071	-0.071	0.000	0.000	0.000	0.000
137	A	214	GLY	0	-0.071	-0.007	47.493	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:78:PHE)