FMO DATABASE

FMODB ID: KR6M3

Calculation Name: 1WS6-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WS6

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SJT0

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	171
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1735621.690137
FMO2-HF: Nuclear repulsion	1671997.1038
FMO2-HF: Total energy	-63624.586337
FMO2-MP2: Total energy	-63815.138781

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:15:VAL )

Summations of interaction energy for fragment #1(A:15:VAL )

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.
-2.092	1.097	0.8	-1.342	-2.645	-0.002

Interaction energy analysis for fragmet #1(A:15:VAL )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / q_NPA : 0.008

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	17	ARG	1	0.912	0.943	3.806	0.087	1.700	-0.018	-0.704	-0.890	0.002
4	A	18	ILE	0	0.010	0.028	6.801	-0.493	-0.493	0.000	0.000	0.000	0.000
5	A	19	LEU	0	-0.069	-0.063	9.555	-0.050	-0.050	0.000	0.000	0.000	0.000
6	A	20	GLY	0	-0.027	-0.017	12.365	-0.036	-0.036	0.000	0.000	0.000	0.000
7	A	21	GLY	0	0.045	0.034	15.700	0.052	0.052	0.000	0.000	0.000	0.000
8	A	22	LYS	1	0.958	0.964	17.286	-0.249	-0.249	0.000	0.000	0.000	0.000
9	A	23	ALA	0	0.037	0.030	13.306	0.022	0.022	0.000	0.000	0.000	0.000
10	A	24	ARG	1	0.929	0.975	12.683	-0.129	-0.129	0.000	0.000	0.000	0.000
11	A	25	GLY	0	0.004	0.001	10.093	-0.023	-0.023	0.000	0.000	0.000	0.000
12	A	26	VAL	0	0.012	0.007	8.785	0.349	0.349	0.000	0.000	0.000	0.000
13	A	27	ALA	0	-0.052	-0.030	4.640	-0.214	-0.153	0.000	-0.018	-0.043	0.000
14	A	28	LEU	0	-0.028	-0.022	4.617	-1.236	-1.102	0.000	-0.028	-0.106	0.000
15	A	29	LYS	1	0.905	0.956	3.642	1.614	2.112	0.053	-0.169	-0.382	0.000
16	A	30	VAL	0	0.004	-0.014	2.391	-1.536	-0.863	0.765	-0.412	-1.026	-0.004
17	A	31	PRO	0	0.048	0.043	4.982	-0.734	-0.636	0.000	-0.002	-0.095	0.000
18	A	32	ALA	0	0.000	-0.013	6.581	-0.192	-0.192	0.000	0.000	0.000	0.000
19	A	33	SER	0	0.013	0.007	7.499	0.020	0.020	0.000	0.000	0.000	0.000
20	A	34	ALA	0	-0.008	0.018	7.215	0.127	0.127	0.000	0.000	0.000	0.000
21	A	35	ARG	1	0.894	0.994	8.522	0.365	0.365	0.000	0.000	0.000	0.000
22	A	36	PRO	0	0.019	-0.010	4.371	-0.106	0.006	0.000	-0.009	-0.103	0.000
23	A	37	SER	0	0.035	-0.039	7.376	0.307	0.307	0.000	0.000	0.000	0.000
24	A	38	PRO	0	0.004	0.017	8.558	-0.093	-0.093	0.000	0.000	0.000	0.000
25	A	39	VAL	0	0.087	0.030	6.843	0.123	0.123	0.000	0.000	0.000	0.000
26	A	40	ARG	1	0.977	0.983	9.621	0.361	0.361	0.000	0.000	0.000	0.000
27	A	41	LEU	0	-0.003	0.026	12.642	0.043	0.043	0.000	0.000	0.000	0.000
28	A	42	ARG	1	0.947	0.968	7.909	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	43	LYS	1	0.933	0.966	13.151	0.072	0.072	0.000	0.000	0.000	0.000
30	A	44	ALA	0	-0.011	0.008	14.768	0.025	0.025	0.000	0.000	0.000	0.000
31	A	45	LEU	0	-0.010	-0.006	17.177	0.016	0.016	0.000	0.000	0.000	0.000
32	A	46	PHE	0	0.058	0.005	15.132	0.012	0.012	0.000	0.000	0.000	0.000
33	A	47	ASP	-1	-0.860	-0.925	19.016	0.030	0.030	0.000	0.000	0.000	0.000
34	A	48	TYR	0	-0.035	-0.003	20.793	0.004	0.004	0.000	0.000	0.000	0.000
35	A	49	LEU	0	0.046	0.017	20.344	0.005	0.005	0.000	0.000	0.000	0.000
36	A	50	ARG	1	0.792	0.915	18.424	-0.101	-0.101	0.000	0.000	0.000	0.000
37	A	51	LEU	0	-0.048	-0.013	24.348	0.001	0.001	0.000	0.000	0.000	0.000
38	A	52	ARG	1	0.802	0.879	26.527	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	53	TYR	0	-0.013	-0.024	25.776	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	54	PRO	0	0.013	0.008	26.907	0.016	0.016	0.000	0.000	0.000	0.000
41	A	55	ARG	1	0.940	0.965	28.737	-0.079	-0.079	0.000	0.000	0.000	0.000
42	A	56	ARG	1	0.796	0.896	22.939	-0.128	-0.128	0.000	0.000	0.000	0.000
43	A	57	GLY	0	0.117	0.065	26.137	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	58	ARG	1	0.831	0.928	25.101	-0.083	-0.083	0.000	0.000	0.000	0.000
45	A	59	PHE	0	-0.008	-0.008	17.852	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	60	LEU	0	0.005	0.002	21.801	0.018	0.018	0.000	0.000	0.000	0.000
47	A	61	ASP	-1	-0.850	-0.968	15.255	0.107	0.107	0.000	0.000	0.000	0.000
48	A	62	PRO	0	0.010	0.007	18.224	0.017	0.017	0.000	0.000	0.000	0.000
49	A	63	PHE	0	-0.014	-0.028	17.157	-0.023	-0.023	0.000	0.000	0.000	0.000
50	A	64	ALA	0	0.017	0.043	14.277	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	65	GLY	0	0.086	0.028	11.226	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	66	SER	0	-0.047	-0.039	7.534	-0.034	-0.034	0.000	0.000	0.000	0.000
53	A	67	GLY	0	0.074	0.029	9.485	0.176	0.176	0.000	0.000	0.000	0.000
54	A	68	ALA	0	-0.061	-0.025	7.851	0.033	0.033	0.000	0.000	0.000	0.000
55	A	69	VAL	0	0.016	0.020	9.538	0.027	0.027	0.000	0.000	0.000	0.000
56	A	70	GLY	0	0.098	0.043	13.090	0.015	0.015	0.000	0.000	0.000	0.000
57	A	71	LEU	0	-0.028	-0.027	10.457	0.016	0.016	0.000	0.000	0.000	0.000
58	A	72	GLU	-1	-0.785	-0.861	12.475	0.439	0.439	0.000	0.000	0.000	0.000
59	A	73	ALA	0	0.038	0.022	14.035	-0.026	-0.026	0.000	0.000	0.000	0.000
60	A	74	ALA	0	0.020	0.015	16.534	-0.012	-0.012	0.000	0.000	0.000	0.000
61	A	75	SER	0	-0.048	-0.053	14.985	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	76	GLU	-1	-0.888	-0.949	16.997	0.164	0.164	0.000	0.000	0.000	0.000
63	A	77	GLY	0	-0.069	-0.026	19.558	-0.036	-0.036	0.000	0.000	0.000	0.000
64	A	78	TRP	0	-0.018	0.004	20.446	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	79	GLU	-1	-0.905	-0.953	21.727	0.161	0.161	0.000	0.000	0.000	0.000
66	A	80	ALA	0	-0.024	-0.019	18.726	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	81	VAL	0	-0.005	0.002	20.741	0.015	0.015	0.000	0.000	0.000	0.000
68	A	82	LEU	0	-0.036	-0.011	14.602	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	83	VAL	0	0.013	0.019	18.590	0.008	0.008	0.000	0.000	0.000	0.000
70	A	84	GLU	-1	-0.863	-0.938	15.009	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	85	LYS	1	0.970	0.973	18.174	0.060	0.060	0.000	0.000	0.000	0.000
72	A	86	ASP	-1	-0.858	-0.921	15.557	-0.025	-0.025	0.000	0.000	0.000	0.000
73	A	87	PRO	0	0.023	0.002	16.683	0.034	0.034	0.000	0.000	0.000	0.000
74	A	88	GLU	-1	-0.921	-0.959	13.878	0.000	0.000	0.000	0.000	0.000	0.000
75	A	89	ALA	0	0.003	0.008	12.145	0.069	0.069	0.000	0.000	0.000	0.000
76	A	90	VAL	0	0.023	0.007	12.872	0.106	0.106	0.000	0.000	0.000	0.000
77	A	91	ARG	1	0.937	0.978	14.507	-0.132	-0.132	0.000	0.000	0.000	0.000
78	A	92	LEU	0	0.036	-0.008	8.219	0.099	0.099	0.000	0.000	0.000	0.000
79	A	93	LEU	0	-0.021	-0.002	10.978	0.199	0.199	0.000	0.000	0.000	0.000
80	A	94	LYS	1	0.957	0.978	12.554	-0.156	-0.156	0.000	0.000	0.000	0.000
81	A	95	GLU	-1	-0.932	-0.965	11.446	0.681	0.681	0.000	0.000	0.000	0.000
82	A	96	ASN	0	-0.060	-0.043	7.577	0.503	0.503	0.000	0.000	0.000	0.000
83	A	97	VAL	0	0.025	0.022	11.065	0.043	0.043	0.000	0.000	0.000	0.000
84	A	98	ARG	1	0.945	0.968	14.505	-0.444	-0.444	0.000	0.000	0.000	0.000
85	A	99	ARG	1	0.849	0.936	8.307	-2.013	-2.013	0.000	0.000	0.000	0.000
86	A	100	THR	0	-0.049	-0.031	11.208	-0.035	-0.035	0.000	0.000	0.000	0.000
87	A	101	GLY	0	0.017	0.029	13.524	-0.077	-0.077	0.000	0.000	0.000	0.000
88	A	102	LEU	0	-0.054	-0.011	14.762	-0.073	-0.073	0.000	0.000	0.000	0.000
89	A	103	GLY	0	0.001	0.003	17.832	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	104	ALA	0	-0.003	-0.012	17.706	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	105	ARG	1	0.973	1.001	19.760	-0.126	-0.126	0.000	0.000	0.000	0.000
92	A	106	VAL	0	-0.014	-0.007	17.310	0.003	0.003	0.000	0.000	0.000	0.000
93	A	107	VAL	0	-0.031	-0.023	19.870	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	108	ALA	0	-0.016	-0.011	20.561	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	109	LEU	0	0.048	0.025	21.508	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	110	PRO	0	0.016	0.008	22.453	0.001	0.001	0.000	0.000	0.000	0.000
97	A	111	VAL	0	0.062	0.012	21.453	0.007	0.007	0.000	0.000	0.000	0.000
98	A	112	GLU	-1	-0.937	-0.973	24.167	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	113	VAL	0	0.009	0.023	27.013	0.000	0.000	0.000	0.000	0.000	0.000
100	A	114	PHE	0	0.018	-0.007	25.129	0.006	0.006	0.000	0.000	0.000	0.000
101	A	115	LEU	0	-0.005	0.013	25.835	0.004	0.004	0.000	0.000	0.000	0.000
102	A	116	PRO	0	-0.048	-0.025	28.764	0.002	0.002	0.000	0.000	0.000	0.000
103	A	117	GLU	-1	-0.872	-0.951	30.378	0.047	0.047	0.000	0.000	0.000	0.000
104	A	118	ALA	0	-0.005	-0.005	28.356	0.004	0.004	0.000	0.000	0.000	0.000
105	A	119	LYS	1	0.892	0.940	30.465	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	120	ALA	0	-0.002	0.013	33.371	0.001	0.001	0.000	0.000	0.000	0.000
107	A	121	GLN	0	-0.084	-0.029	30.664	0.000	0.000	0.000	0.000	0.000	0.000
108	A	122	GLY	0	-0.009	-0.001	34.678	0.003	0.003	0.000	0.000	0.000	0.000
109	A	123	GLU	-1	-0.911	-0.943	29.456	0.090	0.090	0.000	0.000	0.000	0.000
110	A	124	ARG	1	0.917	0.943	30.616	-0.048	-0.048	0.000	0.000	0.000	0.000
111	A	125	PHE	0	-0.044	-0.029	24.887	0.013	0.013	0.000	0.000	0.000	0.000
112	A	126	THR	0	0.021	0.015	26.912	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	127	VAL	0	-0.029	-0.009	22.288	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	128	ALA	0	0.005	0.019	22.983	0.014	0.014	0.000	0.000	0.000	0.000
115	A	129	PHE	0	-0.030	-0.011	15.510	-0.020	-0.020	0.000	0.000	0.000	0.000
116	A	130	MET	0	0.037	0.028	19.346	0.007	0.007	0.000	0.000	0.000	0.000
117	A	131	ALA	0	-0.025	-0.019	15.294	-0.023	-0.023	0.000	0.000	0.000	0.000
118	A	132	PRO	0	0.015	0.026	15.890	-0.015	-0.015	0.000	0.000	0.000	0.000
119	A	133	PRO	0	0.016	-0.004	16.223	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	134	TYR	0	-0.024	-0.075	15.996	0.013	0.013	0.000	0.000	0.000	0.000
121	A	135	ALA	0	0.011	0.033	19.121	0.006	0.006	0.000	0.000	0.000	0.000
122	A	136	MET	0	-0.028	-0.010	21.117	0.016	0.016	0.000	0.000	0.000	0.000
123	A	137	ASP	-1	-0.814	-0.906	23.218	-0.087	-0.087	0.000	0.000	0.000	0.000
124	A	138	LEU	0	-0.063	-0.039	20.138	0.009	0.009	0.000	0.000	0.000	0.000
125	A	139	ALA	0	0.023	-0.007	24.462	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	140	ALA	0	0.041	0.053	27.832	0.010	0.010	0.000	0.000	0.000	0.000
127	A	141	LEU	0	0.000	-0.008	22.769	0.007	0.007	0.000	0.000	0.000	0.000
128	A	142	PHE	0	-0.019	-0.025	21.835	0.007	0.007	0.000	0.000	0.000	0.000
129	A	143	GLY	0	0.022	0.013	26.728	0.008	0.008	0.000	0.000	0.000	0.000
130	A	144	GLU	-1	-0.896	-0.950	28.361	-0.011	-0.011	0.000	0.000	0.000	0.000
131	A	145	LEU	0	-0.068	-0.039	24.190	0.008	0.008	0.000	0.000	0.000	0.000
132	A	146	LEU	0	-0.035	-0.022	27.903	0.007	0.007	0.000	0.000	0.000	0.000
133	A	147	ALA	0	0.027	0.027	30.441	0.004	0.004	0.000	0.000	0.000	0.000
134	A	148	SER	0	-0.130	-0.061	29.687	0.007	0.007	0.000	0.000	0.000	0.000
135	A	149	GLY	0	0.067	0.024	32.058	0.004	0.004	0.000	0.000	0.000	0.000
136	A	150	LEU	0	-0.042	-0.026	27.791	0.005	0.005	0.000	0.000	0.000	0.000
137	A	151	VAL	0	-0.067	-0.022	27.489	0.009	0.009	0.000	0.000	0.000	0.000
138	A	152	GLU	-1	-0.895	-0.925	30.197	0.053	0.053	0.000	0.000	0.000	0.000
139	A	153	ALA	0	0.036	0.009	32.573	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	154	GLY	0	-0.002	-0.006	33.653	0.005	0.005	0.000	0.000	0.000	0.000
141	A	155	GLY	0	-0.003	-0.001	29.628	0.002	0.002	0.000	0.000	0.000	0.000
142	A	156	LEU	0	-0.028	-0.031	25.738	-0.009	-0.009	0.000	0.000	0.000	0.000
143	A	157	TYR	0	0.072	0.055	25.561	0.009	0.009	0.000	0.000	0.000	0.000
144	A	158	VAL	0	-0.051	-0.035	20.750	-0.010	-0.010	0.000	0.000	0.000	0.000
145	A	159	LEU	0	0.022	0.011	21.806	0.001	0.001	0.000	0.000	0.000	0.000
146	A	160	GLN	0	-0.028	-0.031	13.637	0.015	0.015	0.000	0.000	0.000	0.000
147	A	161	HIS	1	0.841	0.916	19.245	0.130	0.130	0.000	0.000	0.000	0.000
148	A	162	PRO	0	0.040	0.023	19.347	-0.013	-0.013	0.000	0.000	0.000	0.000
149	A	163	LYS	1	0.891	0.945	20.264	0.226	0.226	0.000	0.000	0.000	0.000
150	A	164	ASP	-1	-0.825	-0.922	22.242	-0.161	-0.161	0.000	0.000	0.000	0.000
151	A	165	LEU	0	-0.014	0.025	24.079	0.012	0.012	0.000	0.000	0.000	0.000
152	A	166	TYR	0	0.005	-0.033	25.741	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	167	LEU	0	-0.005	-0.002	26.130	0.004	0.004	0.000	0.000	0.000	0.000
154	A	168	PRO	0	0.002	0.002	29.764	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	169	LEU	0	-0.010	-0.013	30.145	0.003	0.003	0.000	0.000	0.000	0.000
156	A	170	GLY	0	0.050	0.037	30.396	0.007	0.007	0.000	0.000	0.000	0.000
157	A	171	GLU	-1	-0.880	-0.918	29.099	-0.055	-0.055	0.000	0.000	0.000	0.000
158	A	172	ARG	1	0.848	0.921	25.080	0.106	0.106	0.000	0.000	0.000	0.000
159	A	173	ARG	1	0.916	0.968	21.717	0.053	0.053	0.000	0.000	0.000	0.000
160	A	174	VAL	0	0.015	0.007	20.664	-0.010	-0.010	0.000	0.000	0.000	0.000
161	A	175	TYR	0	-0.045	-0.043	15.804	0.003	0.003	0.000	0.000	0.000	0.000
162	A	176	GLY	0	-0.022	-0.010	16.232	-0.041	-0.041	0.000	0.000	0.000	0.000
163	A	177	GLU	-1	-0.821	-0.919	16.105	-0.262	-0.262	0.000	0.000	0.000	0.000
164	A	178	ASN	0	-0.016	0.021	13.952	0.024	0.024	0.000	0.000	0.000	0.000
165	A	179	ALA	0	0.001	0.008	17.624	0.009	0.009	0.000	0.000	0.000	0.000
166	A	180	LEU	0	-0.016	-0.003	17.989	-0.006	-0.006	0.000	0.000	0.000	0.000
167	A	181	THR	0	0.012	0.002	21.366	-0.003	-0.003	0.000	0.000	0.000	0.000
168	A	182	LEU	0	-0.054	-0.032	23.400	0.005	0.005	0.000	0.000	0.000	0.000
169	A	183	VAL	0	0.033	0.010	26.480	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	184	GLU	-1	-0.841	-0.923	29.334	0.002	0.002	0.000	0.000	0.000	0.000
171	A	185	VAL	-1	-0.842	-0.890	31.397	0.011	0.011	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:15:VAL )