FMO DATABASE

FMODB ID: KR153

Calculation Name: 1WY6-A-Xray315

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WY6

Chain ID: A

ChEMBL ID:

UniProt ID: Q970G9

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	160
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1570451.592411
FMO2-HF: Nuclear repulsion	1505750.16154
FMO2-HF: Total energy	-64701.430871
FMO2-MP2: Total energy	-64887.588417

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:6:ACE )

Summations of interaction energy for fragment #1(A:6:ACE )

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.
0.9	2.004	0.022	-0.445	-0.68	0

Interaction energy analysis for fragmet #1(A:6:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.035 / q_NPA : -0.031

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].
3	A	8	ILE	0	0.074	0.046	3.848	1.334	2.053	-0.005	-0.308	-0.406
4	A	9	ILE	0	0.091	0.034	6.887	0.342	0.342	0.000	0.000	0.000
5	A	10	ARG	1	0.927	0.965	3.711	0.420	0.711	0.027	-0.125	-0.193
6	A	11	LYS	1	0.981	0.987	4.194	-1.460	-1.366	0.000	-0.012	-0.081
7	A	12	LEU	0	0.036	0.034	7.164	0.086	0.086	0.000	0.000	0.000
8	A	13	MET	0	-0.033	-0.017	9.867	0.078	0.078	0.000	0.000	0.000
9	A	14	ASP	-1	-0.983	-0.989	8.780	0.421	0.421	0.000	0.000	0.000
10	A	15	ALA	0	0.016	0.009	10.770	0.011	0.011	0.000	0.000	0.000
11	A	16	LYS	1	0.866	0.919	13.135	0.089	0.089	0.000	0.000	0.000
12	A	17	LYS	1	0.967	0.982	13.089	-0.135	-0.135	0.000	0.000	0.000
13	A	18	PHE	0	0.041	0.033	12.838	-0.003	-0.003	0.000	0.000	0.000
14	A	19	LEU	0	-0.026	-0.010	17.106	-0.010	-0.010	0.000	0.000	0.000
15	A	20	LEU	0	-0.058	-0.022	18.549	-0.006	-0.006	0.000	0.000	0.000
16	A	21	ASP	-1	-0.915	-0.955	19.523	0.065	0.065	0.000	0.000	0.000
17	A	22	GLY	0	-0.034	-0.022	21.673	0.004	0.004	0.000	0.000	0.000
18	A	23	TYR	0	-0.053	-0.002	18.981	0.007	0.007	0.000	0.000	0.000
19	A	24	ILE	0	-0.001	-0.029	19.219	0.006	0.006	0.000	0.000	0.000
20	A	25	ASP	-1	-0.895	-0.951	19.764	0.081	0.081	0.000	0.000	0.000
21	A	26	GLU	-1	-0.903	-0.954	16.135	0.147	0.147	0.000	0.000	0.000
22	A	27	GLY	0	0.031	0.006	14.992	0.021	0.021	0.000	0.000	0.000
23	A	28	VAL	0	-0.002	-0.010	15.347	-0.017	-0.017	0.000	0.000	0.000
24	A	29	LYS	1	0.944	0.982	14.426	-0.244	-0.244	0.000	0.000	0.000
25	A	30	ILE	0	0.013	0.010	10.061	0.003	0.003	0.000	0.000	0.000
26	A	31	VAL	0	0.003	-0.005	11.896	-0.037	-0.037	0.000	0.000	0.000
27	A	32	LEU	0	-0.032	-0.024	14.132	-0.037	-0.037	0.000	0.000	0.000
28	A	33	GLU	-1	-0.959	-0.973	9.727	0.397	0.397	0.000	0.000	0.000
29	A	34	ILE	0	-0.012	-0.009	8.101	-0.052	-0.052	0.000	0.000	0.000
30	A	35	THR	0	-0.049	-0.017	11.217	-0.050	-0.050	0.000	0.000	0.000
31	A	36	LYS	1	0.872	0.943	13.577	-0.039	-0.039	0.000	0.000	0.000
32	A	37	SER	0	-0.040	-0.009	9.938	-0.038	-0.038	0.000	0.000	0.000
33	A	38	SER	0	-0.021	0.003	11.229	-0.062	-0.062	0.000	0.000	0.000
34	A	39	THR	0	0.040	0.004	13.049	0.043	0.043	0.000	0.000	0.000
35	A	40	LYS	1	0.973	0.959	16.210	0.071	0.071	0.000	0.000	0.000
36	A	41	SER	0	-0.071	-0.026	18.200	-0.002	-0.002	0.000	0.000	0.000
37	A	42	GLU	-1	-1.002	-0.994	12.354	-0.567	-0.567	0.000	0.000	0.000
38	A	43	TYR	0	0.053	0.024	13.453	-0.030	-0.030	0.000	0.000	0.000
39	A	44	ASN	0	0.016	0.008	15.130	0.042	0.042	0.000	0.000	0.000
40	A	45	TRP	0	0.023	-0.001	12.776	0.051	0.051	0.000	0.000	0.000
41	A	46	PHE	0	-0.013	0.000	14.177	0.014	0.014	0.000	0.000	0.000
42	A	47	ILE	0	0.056	0.027	17.149	0.021	0.021	0.000	0.000	0.000
43	A	75	CYS	0	-0.068	-0.017	20.313	0.001	0.001	0.000	0.000	0.000
44	A	49	ASN	0	0.031	0.035	17.941	0.021	0.021	0.000	0.000	0.000
45	A	50	LEU	0	-0.001	0.006	18.548	0.011	0.011	0.000	0.000	0.000
46	A	51	LEU	0	0.000	-0.019	20.302	0.012	0.012	0.000	0.000	0.000
47	A	52	GLU	-1	-0.929	-0.952	23.079	-0.063	-0.063	0.000	0.000	0.000
48	A	53	SER	0	-0.060	-0.036	21.958	0.005	0.005	0.000	0.000	0.000
49	A	54	ILE	0	-0.043	-0.014	21.947	0.008	0.008	0.000	0.000	0.000
50	A	55	ASP	-1	-0.783	-0.880	23.995	0.006	0.006	0.000	0.000	0.000
51	A	84	CYS	0	0.050	0.026	26.984	0.004	0.004	0.000	0.000	0.000
52	A	57	ARG	1	0.895	0.952	28.822	-0.026	-0.026	0.000	0.000	0.000
53	A	58	TYR	0	-0.028	-0.019	24.375	0.005	0.005	0.000	0.000	0.000
54	A	59	MET	0	0.001	0.033	25.477	0.000	0.000	0.000	0.000	0.000
55	A	60	PHE	0	0.039	-0.004	26.172	-0.002	-0.002	0.000	0.000	0.000
56	A	61	GLN	0	0.035	0.033	26.188	0.005	0.005	0.000	0.000	0.000
57	A	62	VAL	0	-0.006	-0.003	21.245	0.003	0.003	0.000	0.000	0.000
58	A	63	LEU	0	-0.030	-0.020	23.613	-0.003	-0.003	0.000	0.000	0.000
59	A	64	ASP	-1	-0.843	-0.891	25.620	-0.001	-0.001	0.000	0.000	0.000
60	A	65	LYS	1	0.874	0.951	22.659	-0.038	-0.038	0.000	0.000	0.000
61	A	66	ILE	0	-0.005	-0.019	18.832	-0.001	-0.001	0.000	0.000	0.000
62	A	67	GLY	0	0.038	0.021	21.947	-0.013	-0.013	0.000	0.000	0.000
63	A	68	SER	0	-0.041	-0.023	24.323	-0.010	-0.010	0.000	0.000	0.000
64	A	69	TYR	0	0.026	0.025	19.541	-0.003	-0.003	0.000	0.000	0.000
65	A	70	PHE	0	-0.043	-0.009	17.426	-0.022	-0.022	0.000	0.000	0.000
66	A	71	ASP	-1	-0.914	-0.949	22.290	-0.087	-0.087	0.000	0.000	0.000
67	A	72	LEU	0	0.067	-0.003	25.107	-0.008	-0.008	0.000	0.000	0.000
68	A	73	ASP	-1	-0.873	-0.928	26.629	-0.079	-0.079	0.000	0.000	0.000
69	A	74	LYS	1	0.872	0.931	24.028	0.103	0.103	0.000	0.000	0.000
70	A	76	GLN	0	0.043	0.002	26.420	0.015	0.015	0.000	0.000	0.000
71	A	77	ASN	0	-0.073	-0.056	24.397	0.005	0.005	0.000	0.000	0.000
72	A	78	LEU	0	0.060	0.027	27.709	0.005	0.005	0.000	0.000	0.000
73	A	79	LYS	1	0.836	0.903	30.147	0.040	0.040	0.000	0.000	0.000
74	A	80	SER	0	0.038	0.005	27.658	0.004	0.004	0.000	0.000	0.000
75	A	81	VAL	0	0.000	-0.004	28.461	0.005	0.005	0.000	0.000	0.000
76	A	82	VAL	0	0.000	-0.005	30.756	0.005	0.005	0.000	0.000	0.000
77	A	83	GLU	-1	-0.781	-0.867	32.475	-0.021	-0.021	0.000	0.000	0.000
78	A	85	GLY	0	0.013	0.008	32.900	0.004	0.004	0.000	0.000	0.000
79	A	86	VAL	0	-0.012	-0.006	35.698	0.003	0.003	0.000	0.000	0.000
80	A	87	ILE	0	-0.006	-0.004	33.167	0.002	0.002	0.000	0.000	0.000
81	A	88	ASN	0	-0.078	-0.042	32.392	0.002	0.002	0.000	0.000	0.000
82	A	89	ASN	0	0.032	0.019	36.541	0.000	0.000	0.000	0.000	0.000
83	A	90	THR	0	-0.087	-0.041	35.729	0.001	0.001	0.000	0.000	0.000
84	A	91	LEU	0	0.022	0.009	37.425	-0.002	-0.002	0.000	0.000	0.000
85	A	92	ASN	0	0.024	0.015	33.287	-0.001	-0.001	0.000	0.000	0.000
86	A	93	GLU	-1	-0.881	-0.963	32.253	-0.014	-0.014	0.000	0.000	0.000
87	A	94	HIS	0	-0.034	-0.042	29.311	-0.009	-0.009	0.000	0.000	0.000
88	A	95	VAL	0	-0.019	-0.012	32.292	-0.004	-0.004	0.000	0.000	0.000
89	A	96	ASN	0	0.013	-0.004	34.654	-0.003	-0.003	0.000	0.000	0.000
90	A	97	LYS	1	1.002	1.006	31.470	0.024	0.024	0.000	0.000	0.000
91	A	98	ALA	0	-0.004	0.007	31.854	-0.004	-0.004	0.000	0.000	0.000
92	A	99	LEU	0	0.003	0.002	33.270	-0.003	-0.003	0.000	0.000	0.000
93	A	100	ASP	-1	-0.922	-0.962	36.526	-0.030	-0.030	0.000	0.000	0.000
94	A	101	ILE	0	-0.028	-0.022	30.624	-0.003	-0.003	0.000	0.000	0.000
95	A	102	LEU	0	-0.021	-0.006	33.231	-0.003	-0.003	0.000	0.000	0.000
96	A	103	VAL	0	-0.022	-0.012	35.833	-0.001	-0.001	0.000	0.000	0.000
97	A	104	ILE	0	-0.065	-0.025	36.210	0.000	0.000	0.000	0.000	0.000
98	A	105	GLN	0	-0.066	-0.032	30.607	0.001	0.001	0.000	0.000	0.000
99	A	106	GLY	0	0.011	0.011	36.082	-0.002	-0.002	0.000	0.000	0.000
100	A	107	LYS	1	0.847	0.945	31.913	0.066	0.066	0.000	0.000	0.000
101	A	108	ARG	1	0.952	0.953	37.835	0.032	0.032	0.000	0.000	0.000
102	A	109	ASP	-1	-0.821	-0.905	37.377	-0.046	-0.046	0.000	0.000	0.000
103	A	110	LYS	1	0.901	0.947	32.469	0.057	0.057	0.000	0.000	0.000
104	A	111	LEU	0	0.007	-0.001	37.637	0.003	0.003	0.000	0.000	0.000
105	A	112	GLU	-1	-0.836	-0.926	40.095	-0.027	-0.027	0.000	0.000	0.000
106	A	113	GLU	-1	-0.965	-0.966	37.153	-0.037	-0.037	0.000	0.000	0.000
107	A	114	ILE	0	0.015	0.019	36.281	0.002	0.002	0.000	0.000	0.000
108	A	115	GLY	0	0.033	0.011	40.149	0.003	0.003	0.000	0.000	0.000
109	A	116	ARG	1	0.896	0.948	42.367	0.029	0.029	0.000	0.000	0.000
110	A	117	GLH	0	-0.100	-0.068	37.251	0.001	0.001	0.000	0.000	0.000
111	A	118	ILE	0	-0.024	-0.005	41.760	0.002	0.002	0.000	0.000	0.000
112	A	119	LEU	0	-0.011	0.006	44.018	0.002	0.002	0.000	0.000	0.000
113	A	120	LYS	1	0.881	0.904	45.596	0.019	0.019	0.000	0.000	0.000
114	A	121	ASN	0	-0.006	0.004	44.783	0.001	0.001	0.000	0.000	0.000
115	A	122	ASN	0	-0.021	-0.001	45.637	0.001	0.001	0.000	0.000	0.000
116	A	123	GLU	-1	-0.921	-0.962	44.470	-0.001	-0.001	0.000	0.000	0.000
117	A	124	VAL	0	0.008	0.008	41.929	0.001	0.001	0.000	0.000	0.000
118	A	125	SER	0	-0.006	-0.006	44.059	0.000	0.000	0.000	0.000	0.000
119	A	126	ALA	0	0.072	0.018	46.173	-0.001	-0.001	0.000	0.000	0.000
120	A	127	SER	0	0.014	0.010	43.897	-0.001	-0.001	0.000	0.000	0.000
121	A	128	ILE	0	0.036	0.030	40.575	-0.002	-0.002	0.000	0.000	0.000
122	A	129	LEU	0	0.005	0.005	43.354	-0.002	-0.002	0.000	0.000	0.000
123	A	130	VAL	0	0.011	-0.004	46.176	-0.001	-0.001	0.000	0.000	0.000
124	A	131	ALA	0	-0.034	-0.008	41.597	-0.001	-0.001	0.000	0.000	0.000
125	A	132	ILE	0	0.030	0.004	40.464	-0.002	-0.002	0.000	0.000	0.000
126	A	133	ALA	0	-0.005	0.015	43.231	-0.002	-0.002	0.000	0.000	0.000
127	A	134	ASN	0	0.015	-0.008	45.856	-0.001	-0.001	0.000	0.000	0.000
128	A	135	ALA	0	-0.020	-0.001	41.364	-0.001	-0.001	0.000	0.000	0.000
129	A	136	LEU	0	0.008	-0.014	43.441	-0.002	-0.002	0.000	0.000	0.000
130	A	137	ARG	1	0.941	0.970	45.147	0.017	0.017	0.000	0.000	0.000
131	A	138	ARG	1	0.901	0.963	40.722	0.030	0.030	0.000	0.000	0.000
132	A	139	VAL	0	-0.059	-0.022	41.707	-0.002	-0.002	0.000	0.000	0.000
133	A	140	GLY	0	0.011	0.007	45.050	-0.001	-0.001	0.000	0.000	0.000
134	A	141	ASP	-1	-0.903	-0.939	46.591	-0.024	-0.024	0.000	0.000	0.000
135	A	142	GLU	-1	-0.831	-0.938	48.834	-0.022	-0.022	0.000	0.000	0.000
136	A	143	ARG	1	0.909	0.958	51.951	0.020	0.020	0.000	0.000	0.000
137	A	144	ASP	-1	-0.844	-0.909	47.979	-0.020	-0.020	0.000	0.000	0.000
138	A	145	ALA	0	-0.031	-0.008	48.768	0.001	0.001	0.000	0.000	0.000
139	A	146	THR	0	-0.033	-0.036	49.703	0.001	0.001	0.000	0.000	0.000
140	A	147	THR	0	-0.020	-0.016	51.290	0.001	0.001	0.000	0.000	0.000
141	A	148	LEU	0	-0.003	0.007	45.978	0.001	0.001	0.000	0.000	0.000
142	A	149	LEU	0	0.023	0.017	50.200	0.001	0.001	0.000	0.000	0.000
143	A	150	ILE	0	0.002	0.005	52.209	0.001	0.001	0.000	0.000	0.000
144	A	151	GLU	-1	-0.916	-0.951	50.450	-0.007	-0.007	0.000	0.000	0.000
145	A	152	ALA	0	-0.002	-0.014	50.222	0.001	0.001	0.000	0.000	0.000
146	A	161	CYS	0	-0.092	-0.029	51.911	0.001	0.001	0.000	0.000	0.000
147	A	154	LYS	1	0.953	0.980	55.104	0.008	0.008	0.000	0.000	0.000
148	A	155	LYS	1	0.831	0.927	48.537	0.007	0.007	0.000	0.000	0.000
149	A	156	GLY	0	-0.018	-0.001	53.781	0.001	0.001	0.000	0.000	0.000
150	A	157	GLU	-1	-0.970	-0.981	51.144	-0.007	-0.007	0.000	0.000	0.000
151	A	158	LYS	1	0.963	0.954	53.735	0.003	0.003	0.000	0.000	0.000
152	A	159	GLU	-1	-0.842	-0.922	52.900	-0.010	-0.010	0.000	0.000	0.000
153	A	160	ALA	0	0.017	0.007	52.323	-0.001	-0.001	0.000	0.000	0.000
154	A	162	ASN	0	-0.056	-0.034	57.684	0.000	0.000	0.000	0.000	0.000
155	A	163	ALA	0	0.006	0.010	54.929	0.000	0.000	0.000	0.000	0.000
156	A	164	VAL	0	-0.008	-0.018	55.843	-0.001	-0.001	0.000	0.000	0.000
157	A	165	ASN	0	-0.019	-0.021	58.058	0.000	0.000	0.000	0.000	0.000
158	A	166	THR	0	-0.048	-0.001	58.212	0.000	0.000	0.000	0.000	0.000
159	A	167	LEU	0	-0.091	-0.017	56.252	-0.001	-0.001	0.000	0.000	0.000
160	A	168	NME	0	-0.009	-0.006	60.403	0.001	0.001	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ACE )