FMO DATABASE

FMODB ID: 2288R

Calculation Name: 1WS6-A-Xray372

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: 2023-06-19

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	171
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1736437.537276
FMO2-HF: Nuclear repulsion	1672811.372722
FMO2-HF: Total energy	-63626.164554
FMO2-MP2: Total energy	-63816.634666

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.
-2.093	0.78	1.637	-1.582	-2.926	0

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 : 0.001

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	0.921	0.948	3.806	0.289	1.849	-0.022	-0.666	-0.872	0.001
4	A	18	ILE	0	-0.004	0.029	6.787	-0.472	-0.472	0.000	0.000	0.000	0.000
5	A	19	LEU	0	-0.025	-0.036	9.873	-0.049	-0.049	0.000	0.000	0.000	0.000
6	A	20	GLY	0	-0.023	-0.020	12.365	-0.045	-0.045	0.000	0.000	0.000	0.000
7	A	21	GLY	0	0.035	0.027	15.690	0.053	0.053	0.000	0.000	0.000	0.000
8	A	22	LYS	1	0.899	0.942	17.240	-0.277	-0.277	0.000	0.000	0.000	0.000
9	A	23	ALA	0	0.046	0.033	13.382	0.017	0.017	0.000	0.000	0.000	0.000
10	A	24	ARG	1	0.924	0.973	12.630	-0.124	-0.124	0.000	0.000	0.000	0.000
11	A	25	GLY	0	0.010	0.004	10.059	-0.031	-0.031	0.000	0.000	0.000	0.000
12	A	26	VAL	0	-0.010	-0.001	8.741	0.298	0.298	0.000	0.000	0.000	0.000
13	A	27	ALA	0	-0.035	-0.016	4.575	-0.180	-0.122	-0.001	-0.018	-0.039	0.000
14	A	28	LEU	0	-0.015	-0.004	4.614	-1.310	-1.173	-0.001	-0.029	-0.107	0.000
15	A	29	LYS	1	0.893	0.925	3.669	1.891	2.384	0.053	-0.172	-0.374	0.000
16	A	30	VAL	0	-0.020	-0.004	2.231	-1.571	-1.173	1.610	-0.686	-1.321	-0.001
17	A	31	PRO	0	0.083	0.060	4.984	-0.760	-0.641	-0.001	-0.002	-0.115	0.000
18	A	32	ALA	0	-0.007	-0.017	6.311	-0.171	-0.171	0.000	0.000	0.000	0.000
19	A	33	SER	0	0.012	0.013	7.235	0.002	0.002	0.000	0.000	0.000	0.000
20	A	34	ALA	0	-0.014	0.007	7.194	0.128	0.128	0.000	0.000	0.000	0.000
21	A	35	ARG	1	0.902	0.979	8.671	0.312	0.312	0.000	0.000	0.000	0.000
22	A	36	PRO	0	0.027	-0.004	4.315	-0.114	-0.006	-0.001	-0.009	-0.098	0.000
23	A	37	SER	0	0.030	-0.029	7.517	0.281	0.281	0.000	0.000	0.000	0.000
24	A	38	PRO	0	0.000	0.007	8.741	-0.069	-0.069	0.000	0.000	0.000	0.000
25	A	39	VAL	0	0.082	0.035	7.170	0.110	0.110	0.000	0.000	0.000	0.000
26	A	40	ARG	1	0.977	0.986	10.196	0.315	0.315	0.000	0.000	0.000	0.000
27	A	41	LEU	0	0.002	0.023	13.312	0.041	0.041	0.000	0.000	0.000	0.000
28	A	42	ARG	1	0.911	0.946	8.234	-0.129	-0.129	0.000	0.000	0.000	0.000
29	A	43	LYS	1	0.859	0.913	13.520	0.035	0.035	0.000	0.000	0.000	0.000
30	A	44	ALA	0	-0.010	0.006	15.183	0.023	0.023	0.000	0.000	0.000	0.000
31	A	45	LEU	0	-0.016	-0.004	17.110	0.014	0.014	0.000	0.000	0.000	0.000
32	A	46	PHE	0	0.048	0.004	15.129	0.013	0.013	0.000	0.000	0.000	0.000
33	A	47	ASP	-1	-0.823	-0.879	19.337	0.043	0.043	0.000	0.000	0.000	0.000
34	A	48	TYR	0	0.019	0.005	21.150	0.002	0.002	0.000	0.000	0.000	0.000
35	A	49	LEU	0	0.034	0.013	20.479	0.004	0.004	0.000	0.000	0.000	0.000
36	A	50	ARG	1	0.763	0.862	18.455	-0.113	-0.113	0.000	0.000	0.000	0.000
37	A	51	LEU	0	-0.047	-0.014	24.348	0.000	0.000	0.000	0.000	0.000	0.000
38	A	52	ARG	1	0.773	0.851	26.688	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	53	TYR	0	-0.012	-0.026	26.034	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	54	PRO	0	0.031	0.017	26.949	0.015	0.015	0.000	0.000	0.000	0.000
41	A	55	ARG	1	0.922	0.960	28.780	-0.086	-0.086	0.000	0.000	0.000	0.000
42	A	56	ARG	1	0.795	0.894	22.300	-0.141	-0.141	0.000	0.000	0.000	0.000
43	A	57	GLY	0	0.105	0.063	26.188	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	58	ARG	1	0.774	0.879	25.127	-0.093	-0.093	0.000	0.000	0.000	0.000
45	A	59	PHE	0	-0.011	-0.012	17.833	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	60	LEU	0	0.007	0.003	21.838	0.018	0.018	0.000	0.000	0.000	0.000
47	A	61	ASP	-1	-0.825	-0.955	15.294	0.161	0.161	0.000	0.000	0.000	0.000
48	A	62	PRO	0	0.015	0.007	18.252	0.017	0.017	0.000	0.000	0.000	0.000
49	A	63	PHE	0	0.009	-0.012	17.282	-0.020	-0.020	0.000	0.000	0.000	0.000
50	A	64	ALA	0	0.023	0.045	14.314	-0.012	-0.012	0.000	0.000	0.000	0.000
51	A	65	GLY	0	0.047	0.006	11.241	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	66	SER	0	-0.023	-0.053	7.279	-0.104	-0.104	0.000	0.000	0.000	0.000
53	A	67	GLY	0	0.048	0.016	9.506	0.162	0.162	0.000	0.000	0.000	0.000
54	A	68	ALA	0	-0.052	-0.020	7.819	0.023	0.023	0.000	0.000	0.000	0.000
55	A	69	VAL	0	0.014	0.010	9.575	0.018	0.018	0.000	0.000	0.000	0.000
56	A	70	GLY	0	0.098	0.050	13.127	0.007	0.007	0.000	0.000	0.000	0.000
57	A	71	LEU	0	-0.030	-0.028	10.485	0.006	0.006	0.000	0.000	0.000	0.000
58	A	72	GLU	-1	-0.795	-0.867	12.052	0.478	0.478	0.000	0.000	0.000	0.000
59	A	73	ALA	0	0.036	0.019	14.078	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	74	ALA	0	0.043	0.028	16.611	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	75	SER	0	-0.031	-0.041	14.994	-0.013	-0.013	0.000	0.000	0.000	0.000
62	A	76	GLU	-1	-0.826	-0.902	17.152	0.149	0.149	0.000	0.000	0.000	0.000
63	A	77	GLY	0	-0.059	-0.019	19.601	-0.033	-0.033	0.000	0.000	0.000	0.000
64	A	78	TRP	0	-0.028	-0.001	20.307	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	79	GLU	-1	-0.860	-0.926	21.768	0.168	0.168	0.000	0.000	0.000	0.000
66	A	80	ALA	0	-0.029	-0.024	18.738	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	81	VAL	0	-0.001	0.006	20.778	0.013	0.013	0.000	0.000	0.000	0.000
68	A	82	LEU	0	-0.050	-0.012	14.583	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	83	VAL	0	0.008	0.016	18.620	0.007	0.007	0.000	0.000	0.000	0.000
70	A	84	GLU	-1	-0.769	-0.878	14.944	0.017	0.017	0.000	0.000	0.000	0.000
71	A	85	LYS	1	0.842	0.897	17.491	0.018	0.018	0.000	0.000	0.000	0.000
72	A	86	ASP	-1	-0.812	-0.909	15.247	0.010	0.010	0.000	0.000	0.000	0.000
73	A	87	PRO	0	0.015	0.005	16.690	0.035	0.035	0.000	0.000	0.000	0.000
74	A	88	GLU	-1	-0.956	-0.967	13.336	0.010	0.010	0.000	0.000	0.000	0.000
75	A	89	ALA	0	0.019	0.007	12.155	0.073	0.073	0.000	0.000	0.000	0.000
76	A	90	VAL	0	0.018	0.002	12.885	0.107	0.107	0.000	0.000	0.000	0.000
77	A	91	ARG	1	0.905	0.969	14.504	-0.183	-0.183	0.000	0.000	0.000	0.000
78	A	92	LEU	0	0.008	-0.016	8.559	0.103	0.103	0.000	0.000	0.000	0.000
79	A	93	LEU	0	-0.017	0.001	10.996	0.198	0.198	0.000	0.000	0.000	0.000
80	A	94	LYS	1	0.969	0.983	12.575	-0.172	-0.172	0.000	0.000	0.000	0.000
81	A	95	GLU	-1	-0.857	-0.911	11.737	0.625	0.625	0.000	0.000	0.000	0.000
82	A	96	ASN	0	-0.026	-0.021	7.591	0.464	0.464	0.000	0.000	0.000	0.000
83	A	97	VAL	0	0.015	0.025	11.092	0.042	0.042	0.000	0.000	0.000	0.000
84	A	98	ARG	1	0.939	0.968	14.536	-0.446	-0.446	0.000	0.000	0.000	0.000
85	A	99	ARG	1	0.854	0.930	8.509	-1.832	-1.832	0.000	0.000	0.000	0.000
86	A	100	THR	0	-0.056	-0.046	11.115	-0.043	-0.043	0.000	0.000	0.000	0.000
87	A	101	GLY	0	0.017	0.028	13.524	-0.075	-0.075	0.000	0.000	0.000	0.000
88	A	102	LEU	0	-0.059	-0.016	14.492	-0.071	-0.071	0.000	0.000	0.000	0.000
89	A	103	GLY	0	0.003	0.005	17.832	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	104	ALA	0	-0.013	-0.018	17.717	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	105	ARG	1	0.918	0.973	19.796	-0.128	-0.128	0.000	0.000	0.000	0.000
92	A	106	VAL	0	-0.019	-0.014	17.312	0.005	0.005	0.000	0.000	0.000	0.000
93	A	107	VAL	0	-0.016	-0.022	19.898	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	108	ALA	0	-0.021	-0.012	20.579	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	109	LEU	0	0.053	0.029	21.525	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	110	PRO	0	0.023	0.012	22.470	0.004	0.004	0.000	0.000	0.000	0.000
97	A	111	VAL	0	0.039	0.006	21.419	0.006	0.006	0.000	0.000	0.000	0.000
98	A	112	GLU	-1	-0.944	-0.974	24.186	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	113	VAL	0	-0.002	0.014	27.030	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	114	PHE	0	0.034	0.007	25.217	0.005	0.005	0.000	0.000	0.000	0.000
101	A	115	LEU	0	-0.002	0.004	25.880	0.003	0.003	0.000	0.000	0.000	0.000
102	A	116	PRO	0	-0.029	-0.016	28.788	0.002	0.002	0.000	0.000	0.000	0.000
103	A	117	GLU	-1	-0.871	-0.944	30.321	0.056	0.056	0.000	0.000	0.000	0.000
104	A	118	ALA	0	-0.013	-0.008	28.367	0.003	0.003	0.000	0.000	0.000	0.000
105	A	119	LYS	1	0.915	0.945	30.493	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	120	ALA	0	0.005	0.017	33.399	0.000	0.000	0.000	0.000	0.000	0.000
107	A	121	GLN	0	-0.079	-0.027	30.081	0.000	0.000	0.000	0.000	0.000	0.000
108	A	122	GLY	0	-0.002	0.003	34.707	0.003	0.003	0.000	0.000	0.000	0.000
109	A	123	GLU	-1	-0.859	-0.906	28.764	0.107	0.107	0.000	0.000	0.000	0.000
110	A	124	ARG	1	0.885	0.933	30.742	-0.055	-0.055	0.000	0.000	0.000	0.000
111	A	125	PHE	0	-0.032	-0.019	25.206	0.012	0.012	0.000	0.000	0.000	0.000
112	A	126	THR	0	0.020	0.002	26.802	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	127	VAL	0	-0.043	-0.020	22.414	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	128	ALA	0	0.005	0.020	23.001	0.014	0.014	0.000	0.000	0.000	0.000
115	A	129	PHE	0	-0.025	-0.008	15.556	-0.021	-0.021	0.000	0.000	0.000	0.000
116	A	130	MET	0	0.042	0.033	19.370	0.008	0.008	0.000	0.000	0.000	0.000
117	A	131	ALA	0	-0.032	-0.022	15.327	-0.022	-0.022	0.000	0.000	0.000	0.000
118	A	132	PRO	0	0.034	0.031	15.907	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	133	PRO	0	0.022	0.000	16.177	-0.032	-0.032	0.000	0.000	0.000	0.000
120	A	134	TYR	0	-0.029	-0.069	16.086	0.014	0.014	0.000	0.000	0.000	0.000
121	A	135	ALA	0	0.005	0.030	19.258	0.004	0.004	0.000	0.000	0.000	0.000
122	A	136	MET	0	-0.018	-0.002	21.217	0.013	0.013	0.000	0.000	0.000	0.000
123	A	137	ASP	-1	-0.808	-0.904	23.302	-0.073	-0.073	0.000	0.000	0.000	0.000
124	A	138	LEU	0	-0.071	-0.039	19.979	0.010	0.010	0.000	0.000	0.000	0.000
125	A	139	ALA	0	0.029	-0.007	24.606	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	140	ALA	0	0.034	0.047	27.971	0.009	0.009	0.000	0.000	0.000	0.000
127	A	141	LEU	0	-0.004	-0.010	22.758	0.008	0.008	0.000	0.000	0.000	0.000
128	A	142	PHE	0	-0.019	-0.029	21.925	0.007	0.007	0.000	0.000	0.000	0.000
129	A	143	GLY	0	0.014	0.014	26.747	0.008	0.008	0.000	0.000	0.000	0.000
130	A	144	GLU	-1	-0.888	-0.945	28.437	0.001	0.001	0.000	0.000	0.000	0.000
131	A	145	LEU	0	-0.062	-0.037	23.993	0.008	0.008	0.000	0.000	0.000	0.000
132	A	146	LEU	0	-0.034	-0.014	27.927	0.007	0.007	0.000	0.000	0.000	0.000
133	A	147	ALA	0	0.027	0.027	30.466	0.003	0.003	0.000	0.000	0.000	0.000
134	A	148	SER	0	-0.113	-0.068	29.679	0.006	0.006	0.000	0.000	0.000	0.000
135	A	149	GLY	0	0.053	0.022	32.084	0.004	0.004	0.000	0.000	0.000	0.000
136	A	150	LEU	0	-0.034	-0.025	27.976	0.004	0.004	0.000	0.000	0.000	0.000
137	A	151	VAL	0	-0.049	-0.011	27.507	0.008	0.008	0.000	0.000	0.000	0.000
138	A	152	GLU	-1	-0.847	-0.890	30.231	0.065	0.065	0.000	0.000	0.000	0.000
139	A	153	ALA	0	0.027	-0.001	32.609	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	154	GLY	0	-0.003	-0.013	33.690	0.004	0.004	0.000	0.000	0.000	0.000
141	A	155	GLY	0	0.014	0.019	29.661	0.002	0.002	0.000	0.000	0.000	0.000
142	A	156	LEU	0	-0.038	-0.036	25.799	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	157	TYR	0	0.085	0.051	25.575	0.011	0.011	0.000	0.000	0.000	0.000
144	A	158	VAL	0	-0.054	-0.037	20.969	-0.010	-0.010	0.000	0.000	0.000	0.000
145	A	159	LEU	0	0.033	0.023	21.845	0.003	0.003	0.000	0.000	0.000	0.000
146	A	160	GLN	0	-0.025	-0.025	13.967	0.001	0.001	0.000	0.000	0.000	0.000
147	A	161	HIS	1	0.853	0.918	19.345	0.108	0.108	0.000	0.000	0.000	0.000
148	A	162	PRO	0	0.050	0.026	19.405	-0.012	-0.012	0.000	0.000	0.000	0.000
149	A	163	LYS	1	0.810	0.865	20.326	0.215	0.215	0.000	0.000	0.000	0.000
150	A	164	ASP	-1	-0.807	-0.887	22.480	-0.156	-0.156	0.000	0.000	0.000	0.000
151	A	165	LEU	0	-0.014	0.025	24.021	0.011	0.011	0.000	0.000	0.000	0.000
152	A	166	TYR	0	0.000	-0.033	25.804	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	167	LEU	0	0.022	0.010	26.801	0.004	0.004	0.000	0.000	0.000	0.000
154	A	168	PRO	0	0.006	0.002	29.848	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	169	LEU	0	-0.019	-0.015	30.280	0.003	0.003	0.000	0.000	0.000	0.000
156	A	170	GLY	0	0.044	0.028	30.467	0.007	0.007	0.000	0.000	0.000	0.000
157	A	171	GLU	-1	-0.892	-0.923	29.473	-0.044	-0.044	0.000	0.000	0.000	0.000
158	A	172	ARG	1	0.830	0.906	25.394	0.096	0.096	0.000	0.000	0.000	0.000
159	A	173	ARG	1	0.910	0.969	22.597	0.035	0.035	0.000	0.000	0.000	0.000
160	A	174	VAL	0	0.015	0.003	21.347	-0.007	-0.007	0.000	0.000	0.000	0.000
161	A	175	TYR	0	-0.048	-0.047	16.619	0.003	0.003	0.000	0.000	0.000	0.000
162	A	176	GLY	0	-0.013	-0.006	17.007	-0.036	-0.036	0.000	0.000	0.000	0.000
163	A	177	GLU	-1	-0.764	-0.871	16.712	-0.230	-0.230	0.000	0.000	0.000	0.000
164	A	178	ASN	0	-0.030	0.017	14.139	0.008	0.008	0.000	0.000	0.000	0.000
165	A	179	ALA	0	0.003	0.010	17.905	0.007	0.007	0.000	0.000	0.000	0.000
166	A	180	LEU	0	-0.014	0.001	17.957	-0.003	-0.003	0.000	0.000	0.000	0.000
167	A	181	THR	0	-0.002	-0.002	21.521	-0.004	-0.004	0.000	0.000	0.000	0.000
168	A	182	LEU	0	-0.032	-0.020	23.321	0.006	0.006	0.000	0.000	0.000	0.000
169	A	183	VAL	0	0.032	0.012	26.554	-0.003	-0.003	0.000	0.000	0.000	0.000
170	A	184	GLU	-1	-0.810	-0.878	29.365	0.014	0.014	0.000	0.000	0.000	0.000
171	A	185	VAL	0	0.036	0.049	30.899	-0.002	-0.002	0.000	0.000	0.000	0.000

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