FMO DATABASE

FMODB ID: R5258

Calculation Name: 1WY6-A-Xray372

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: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1565623.117629
FMO2-HF: Nuclear repulsion	1501092.527918
FMO2-HF: Total energy	-64530.589711
FMO2-MP2: Total energy	-64716.236105

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.
-63.224	-59.483	7.43	-3.585	-7.586	0.01

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 : -0.922 / q_NPA : -0.971

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	ILE	0	0.085	0.031	2.035	-13.453	-11.565	3.827	-1.976	-3.738	-0.001
4	A	10	ARG	1	0.921	0.962	2.178	-52.422	-51.165	3.602	-1.458	-3.401	0.011
5	A	11	LYS	1	0.988	0.991	4.141	-40.900	-40.304	0.001	-0.151	-0.447	0.000
6	A	12	LEU	0	0.035	0.034	5.895	-4.039	-4.039	0.000	0.000	0.000	0.000
7	A	13	MET	0	-0.039	-0.019	6.962	-4.388	-4.388	0.000	0.000	0.000	0.000
8	A	14	ASP	-1	-0.978	-0.987	8.134	21.198	21.198	0.000	0.000	0.000	0.000
9	A	15	ALA	0	0.016	0.010	9.883	-2.028	-2.028	0.000	0.000	0.000	0.000
10	A	16	LYS	1	0.868	0.920	11.381	-21.713	-21.713	0.000	0.000	0.000	0.000
11	A	17	LYS	1	0.963	0.980	12.819	-20.779	-20.779	0.000	0.000	0.000	0.000
12	A	18	PHE	0	0.044	0.035	12.733	-1.104	-1.104	0.000	0.000	0.000	0.000
13	A	19	LEU	0	-0.027	-0.011	15.308	-1.008	-1.008	0.000	0.000	0.000	0.000
14	A	20	LEU	0	-0.061	-0.024	16.397	-0.755	-0.755	0.000	0.000	0.000	0.000
15	A	21	ASP	-1	-0.914	-0.955	18.968	14.142	14.142	0.000	0.000	0.000	0.000
16	A	22	GLY	0	-0.034	-0.021	20.905	-0.601	-0.601	0.000	0.000	0.000	0.000
17	A	23	TYR	0	-0.053	-0.002	18.505	-0.480	-0.480	0.000	0.000	0.000	0.000
18	A	24	ILE	0	0.002	-0.028	18.630	0.942	0.942	0.000	0.000	0.000	0.000
19	A	25	ASP	-1	-0.899	-0.952	19.042	13.593	13.593	0.000	0.000	0.000	0.000
20	A	26	GLU	-1	-0.903	-0.954	15.981	14.977	14.977	0.000	0.000	0.000	0.000
21	A	27	GLY	0	0.028	0.005	14.251	1.263	1.263	0.000	0.000	0.000	0.000
22	A	28	VAL	0	0.001	-0.009	14.416	1.261	1.261	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.943	0.981	14.727	-16.494	-16.494	0.000	0.000	0.000	0.000
24	A	30	ILE	0	0.012	0.010	9.442	0.926	0.926	0.000	0.000	0.000	0.000
25	A	31	VAL	0	0.001	-0.005	11.336	1.847	1.847	0.000	0.000	0.000	0.000
26	A	32	LEU	0	-0.032	-0.025	12.946	0.688	0.688	0.000	0.000	0.000	0.000
27	A	33	GLU	-1	-0.954	-0.971	10.256	24.134	24.134	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.010	-0.008	6.644	1.213	1.213	0.000	0.000	0.000	0.000
29	A	35	THR	0	-0.055	-0.020	9.967	0.238	0.238	0.000	0.000	0.000	0.000
30	A	36	LYS	1	0.878	0.944	12.882	-18.821	-18.821	0.000	0.000	0.000	0.000
31	A	37	SER	0	-0.039	-0.008	8.886	0.615	0.615	0.000	0.000	0.000	0.000
32	A	38	SER	0	-0.019	0.005	8.620	1.428	1.428	0.000	0.000	0.000	0.000
33	A	39	THR	0	0.038	0.004	10.688	-2.005	-2.005	0.000	0.000	0.000	0.000
34	A	40	LYS	1	0.976	0.960	11.805	-15.656	-15.656	0.000	0.000	0.000	0.000
35	A	41	SER	0	-0.075	-0.029	13.116	0.213	0.213	0.000	0.000	0.000	0.000
36	A	42	GLU	-1	-1.000	-0.994	6.232	45.476	45.476	0.000	0.000	0.000	0.000
37	A	43	TYR	0	0.056	0.026	8.565	2.078	2.078	0.000	0.000	0.000	0.000
38	A	44	ASN	0	0.014	0.008	10.372	-1.811	-1.811	0.000	0.000	0.000	0.000
39	A	45	TRP	0	0.024	-0.001	7.061	-2.965	-2.965	0.000	0.000	0.000	0.000
40	A	46	PHE	0	-0.011	0.001	10.072	-0.985	-0.985	0.000	0.000	0.000	0.000
41	A	47	ILE	0	0.055	0.027	12.165	-0.974	-0.974	0.000	0.000	0.000	0.000
42	A	48	CYS	0	-0.068	-0.017	15.796	-0.204	-0.204	0.000	0.000	0.000	0.000
43	A	49	ASN	0	0.030	0.034	13.071	-0.851	-0.851	0.000	0.000	0.000	0.000
44	A	50	LEU	0	0.001	0.007	15.062	-0.595	-0.595	0.000	0.000	0.000	0.000
45	A	51	LEU	0	0.000	-0.020	16.276	-0.856	-0.856	0.000	0.000	0.000	0.000
46	A	52	GLU	-1	-0.932	-0.955	18.409	13.283	13.283	0.000	0.000	0.000	0.000
47	A	53	SER	0	-0.061	-0.036	18.098	-0.278	-0.278	0.000	0.000	0.000	0.000
48	A	54	ILE	0	-0.041	-0.011	19.366	-0.251	-0.251	0.000	0.000	0.000	0.000
49	A	55	ASP	-1	-0.782	-0.879	20.925	10.775	10.775	0.000	0.000	0.000	0.000
50	A	56	CYS	0	0.057	0.028	24.396	0.037	0.037	0.000	0.000	0.000	0.000
51	A	57	ARG	1	0.895	0.952	26.934	-10.795	-10.795	0.000	0.000	0.000	0.000
52	A	58	TYR	0	-0.026	-0.018	22.652	-0.361	-0.361	0.000	0.000	0.000	0.000
53	A	59	MET	0	0.000	0.033	22.434	0.117	0.117	0.000	0.000	0.000	0.000
54	A	60	PHE	0	0.039	-0.004	23.343	0.368	0.368	0.000	0.000	0.000	0.000
55	A	61	GLN	0	0.033	0.033	24.573	0.201	0.201	0.000	0.000	0.000	0.000
56	A	62	VAL	0	-0.003	-0.002	18.621	0.281	0.281	0.000	0.000	0.000	0.000
57	A	63	LEU	0	-0.034	-0.022	20.994	0.470	0.470	0.000	0.000	0.000	0.000
58	A	64	ASP	-1	-0.839	-0.890	22.708	11.370	11.370	0.000	0.000	0.000	0.000
59	A	65	LYS	1	0.875	0.952	21.494	-12.618	-12.618	0.000	0.000	0.000	0.000
60	A	66	ILE	0	0.004	-0.015	16.170	0.377	0.377	0.000	0.000	0.000	0.000
61	A	67	GLY	0	0.034	0.020	19.154	0.627	0.627	0.000	0.000	0.000	0.000
62	A	68	SER	0	-0.019	-0.015	20.916	0.230	0.230	0.000	0.000	0.000	0.000
63	A	69	TYR	0	-0.006	0.011	16.956	0.021	0.021	0.000	0.000	0.000	0.000
64	A	70	PHE	0	-0.042	-0.008	13.324	1.293	1.293	0.000	0.000	0.000	0.000
65	A	71	ASP	-1	-0.910	-0.947	18.372	14.993	14.993	0.000	0.000	0.000	0.000
66	A	72	LEU	0	0.064	-0.003	20.011	0.374	0.374	0.000	0.000	0.000	0.000
67	A	73	ASP	-1	-0.871	-0.929	21.767	13.546	13.546	0.000	0.000	0.000	0.000
68	A	74	LYS	1	0.873	0.931	18.064	-15.657	-15.657	0.000	0.000	0.000	0.000
69	A	76	GLN	0	0.044	0.003	20.718	-1.341	-1.341	0.000	0.000	0.000	0.000
70	A	77	ASN	0	-0.069	-0.054	19.232	-0.738	-0.738	0.000	0.000	0.000	0.000
71	A	78	LEU	0	0.061	0.028	22.643	-0.117	-0.117	0.000	0.000	0.000	0.000
72	A	79	LYS	1	0.847	0.909	25.006	-10.311	-10.311	0.000	0.000	0.000	0.000
73	A	80	SER	0	0.027	-0.004	22.847	-0.507	-0.507	0.000	0.000	0.000	0.000
74	A	81	VAL	0	0.010	0.002	24.125	-0.129	-0.129	0.000	0.000	0.000	0.000
75	A	82	VAL	0	0.009	0.001	26.478	-0.303	-0.303	0.000	0.000	0.000	0.000
76	A	83	GLH	0	-0.036	-0.056	28.227	-0.333	-0.333	0.000	0.000	0.000	0.000
77	A	85	GLY	0	0.019	0.012	29.306	-0.196	-0.196	0.000	0.000	0.000	0.000
78	A	86	VAL	0	-0.012	-0.006	32.058	-0.314	-0.314	0.000	0.000	0.000	0.000
79	A	87	ILE	0	-0.010	-0.006	29.677	-0.230	-0.230	0.000	0.000	0.000	0.000
80	A	88	ASN	0	-0.074	-0.039	29.851	-0.192	-0.192	0.000	0.000	0.000	0.000
81	A	89	ASN	0	0.034	0.019	33.644	-0.194	-0.194	0.000	0.000	0.000	0.000
82	A	90	THR	0	-0.085	-0.040	32.871	-0.153	-0.153	0.000	0.000	0.000	0.000
83	A	91	LEU	0	0.024	0.011	34.014	0.218	0.218	0.000	0.000	0.000	0.000
84	A	92	ASN	0	0.026	0.016	30.033	0.076	0.076	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.881	-0.962	29.483	10.499	10.499	0.000	0.000	0.000	0.000
86	A	94	HIS	0	-0.037	-0.043	26.329	0.239	0.239	0.000	0.000	0.000	0.000
87	A	95	VAL	0	-0.019	-0.013	28.499	0.153	0.153	0.000	0.000	0.000	0.000
88	A	96	ASN	0	0.013	-0.004	30.572	-0.073	-0.073	0.000	0.000	0.000	0.000
89	A	97	LYS	1	1.003	1.007	28.027	-11.085	-11.085	0.000	0.000	0.000	0.000
90	A	98	ALA	0	-0.007	0.005	27.273	0.138	0.138	0.000	0.000	0.000	0.000
91	A	99	LEU	0	0.003	0.002	28.478	0.009	0.009	0.000	0.000	0.000	0.000
92	A	100	ASP	-1	-0.918	-0.961	31.757	9.238	9.238	0.000	0.000	0.000	0.000
93	A	101	ILE	0	-0.029	-0.022	25.595	0.002	0.002	0.000	0.000	0.000	0.000
94	A	102	LEU	0	-0.023	-0.008	27.828	0.049	0.049	0.000	0.000	0.000	0.000
95	A	103	VAL	0	-0.018	-0.010	30.309	-0.127	-0.127	0.000	0.000	0.000	0.000
96	A	104	ILE	0	-0.065	-0.025	30.218	-0.161	-0.161	0.000	0.000	0.000	0.000
97	A	105	GLN	0	-0.067	-0.032	24.796	-0.257	-0.257	0.000	0.000	0.000	0.000
98	A	106	GLY	0	0.011	0.012	29.830	0.022	0.022	0.000	0.000	0.000	0.000
99	A	107	LYS	1	0.847	0.945	25.968	-11.820	-11.820	0.000	0.000	0.000	0.000
100	A	108	ARG	1	0.955	0.953	31.918	-7.911	-7.911	0.000	0.000	0.000	0.000
101	A	109	ASP	-1	-0.817	-0.904	31.470	9.879	9.879	0.000	0.000	0.000	0.000
102	A	110	LYS	1	0.897	0.945	26.802	-11.244	-11.244	0.000	0.000	0.000	0.000
103	A	111	LEU	0	0.000	-0.005	32.129	-0.083	-0.083	0.000	0.000	0.000	0.000
104	A	112	GLU	-1	-0.825	-0.922	34.755	7.833	7.833	0.000	0.000	0.000	0.000
105	A	113	GLU	-1	-0.964	-0.962	31.818	9.630	9.630	0.000	0.000	0.000	0.000
106	A	114	ILE	0	0.007	0.013	31.588	-0.098	-0.098	0.000	0.000	0.000	0.000
107	A	115	GLY	0	0.033	0.011	35.305	-0.169	-0.169	0.000	0.000	0.000	0.000
108	A	116	ARG	1	0.929	0.966	36.978	-8.324	-8.324	0.000	0.000	0.000	0.000
109	A	117	GLU	-1	-0.912	-0.917	33.963	9.045	9.045	0.000	0.000	0.000	0.000
110	A	118	ILE	0	-0.003	-0.007	37.389	-0.101	-0.101	0.000	0.000	0.000	0.000
111	A	119	LEU	0	-0.017	0.002	39.741	-0.208	-0.208	0.000	0.000	0.000	0.000
112	A	120	LYS	1	0.841	0.921	36.877	-8.441	-8.441	0.000	0.000	0.000	0.000
113	A	121	ASN	0	-0.021	-0.028	38.788	-0.031	-0.031	0.000	0.000	0.000	0.000
114	A	122	ASN	0	-0.003	0.008	41.907	0.174	0.174	0.000	0.000	0.000	0.000
115	A	123	GLU	-1	-0.913	-0.955	41.085	6.971	6.971	0.000	0.000	0.000	0.000
116	A	124	VAL	0	0.003	0.006	38.268	0.041	0.041	0.000	0.000	0.000	0.000
117	A	125	SER	0	-0.009	-0.008	40.577	-0.219	-0.219	0.000	0.000	0.000	0.000
118	A	126	ALA	0	0.079	0.021	42.402	0.065	0.065	0.000	0.000	0.000	0.000
119	A	127	SER	0	0.014	0.011	40.528	0.035	0.035	0.000	0.000	0.000	0.000
120	A	128	ILE	0	0.033	0.027	36.936	0.101	0.101	0.000	0.000	0.000	0.000
121	A	129	LEU	0	0.002	0.004	39.371	0.089	0.089	0.000	0.000	0.000	0.000
122	A	130	VAL	0	0.012	-0.003	41.906	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	131	ALA	0	-0.032	-0.008	37.219	0.019	0.019	0.000	0.000	0.000	0.000
124	A	132	ILE	0	0.027	0.003	36.066	0.103	0.103	0.000	0.000	0.000	0.000
125	A	133	ALA	0	-0.003	0.017	38.485	0.009	0.009	0.000	0.000	0.000	0.000
126	A	134	ASN	0	0.012	-0.009	41.104	-0.163	-0.163	0.000	0.000	0.000	0.000
127	A	135	ALA	0	-0.020	-0.001	36.206	0.020	0.020	0.000	0.000	0.000	0.000
128	A	136	LEU	0	0.006	-0.014	38.282	0.071	0.071	0.000	0.000	0.000	0.000
129	A	137	ARG	1	0.945	0.970	39.811	-6.906	-6.906	0.000	0.000	0.000	0.000
130	A	138	ARG	1	0.901	0.962	35.689	-8.717	-8.717	0.000	0.000	0.000	0.000
131	A	139	VAL	0	-0.061	-0.022	35.966	0.114	0.114	0.000	0.000	0.000	0.000
132	A	140	GLY	0	0.014	0.007	39.273	0.022	0.022	0.000	0.000	0.000	0.000
133	A	141	ASP	-1	-0.904	-0.935	40.996	7.350	7.350	0.000	0.000	0.000	0.000
134	A	142	GLU	-1	-0.831	-0.939	43.215	7.008	7.008	0.000	0.000	0.000	0.000
135	A	143	ARG	1	0.908	0.958	46.474	-6.448	-6.448	0.000	0.000	0.000	0.000
136	A	144	ASP	-1	-0.838	-0.906	42.759	7.195	7.195	0.000	0.000	0.000	0.000
137	A	145	ALA	0	-0.035	-0.011	43.700	-0.015	-0.015	0.000	0.000	0.000	0.000
138	A	146	THR	0	-0.034	-0.036	44.580	-0.059	-0.059	0.000	0.000	0.000	0.000
139	A	147	THR	0	-0.013	-0.013	46.336	-0.128	-0.128	0.000	0.000	0.000	0.000
140	A	148	LEU	0	-0.007	0.006	41.143	-0.055	-0.055	0.000	0.000	0.000	0.000
141	A	149	LEU	0	0.020	0.015	45.542	-0.049	-0.049	0.000	0.000	0.000	0.000
142	A	150	ILE	0	0.004	0.005	47.624	-0.115	-0.115	0.000	0.000	0.000	0.000
143	A	151	GLU	-1	-0.914	-0.950	46.260	6.424	6.424	0.000	0.000	0.000	0.000
144	A	152	ALA	0	-0.004	-0.015	46.007	-0.034	-0.034	0.000	0.000	0.000	0.000
145	A	153	CYS	0	-0.093	-0.030	47.801	-0.158	-0.158	0.000	0.000	0.000	0.000
146	A	154	LYS	1	0.956	0.981	51.074	-6.123	-6.123	0.000	0.000	0.000	0.000
147	A	155	LYS	1	0.829	0.926	44.798	-6.950	-6.950	0.000	0.000	0.000	0.000
148	A	156	GLY	0	-0.018	-0.001	50.132	0.015	0.015	0.000	0.000	0.000	0.000
149	A	157	GLU	-1	-0.969	-0.979	47.147	6.721	6.721	0.000	0.000	0.000	0.000
150	A	158	LYS	1	0.960	0.953	49.944	-5.937	-5.937	0.000	0.000	0.000	0.000
151	A	159	GLU	-1	-0.841	-0.922	48.715	6.198	6.198	0.000	0.000	0.000	0.000
152	A	160	ALA	0	0.021	0.008	48.107	-0.007	-0.007	0.000	0.000	0.000	0.000
153	A	162	ASN	0	-0.058	-0.035	53.427	-0.168	-0.168	0.000	0.000	0.000	0.000
154	A	163	ALA	0	0.006	0.010	50.249	-0.056	-0.056	0.000	0.000	0.000	0.000
155	A	164	VAL	0	-0.005	-0.015	51.215	-0.027	-0.027	0.000	0.000	0.000	0.000
156	A	165	ASN	0	-0.020	-0.022	53.327	-0.093	-0.093	0.000	0.000	0.000	0.000
157	A	166	THR	0	-0.050	-0.001	53.357	-0.103	-0.103	0.000	0.000	0.000	0.000
158	A	167	LEU	0	-0.097	-0.022	51.175	-0.022	-0.022	0.000	0.000	0.000	0.000

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