FMO DATABASE

FMODB ID: R53L8

Calculation Name: 1WRJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WRJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q973C7

Base Structure: X-ray

Registration Date: 2023-06-21

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	149
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1508590.989703
FMO2-HF: Nuclear repulsion	1448267.542494
FMO2-HF: Total energy	-60323.447209
FMO2-MP2: Total energy	-60499.46907

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:1:MET)

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

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.
-11.633	-12.016	21.04	-8.913	-11.743	-0.05

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.022 / q_NPA : -0.010

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	3	VAL	0	0.002	0.021	2.614	-1.820	1.498	1.281	-1.604	-2.994	0.001
4	A	4	TYR	0	-0.015	-0.069	4.023	0.122	0.181	0.002	-0.004	-0.058	0.000
5	A	5	GLY	0	0.054	0.023	7.731	0.101	0.101	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.077	-0.039	10.081	0.016	0.016	0.000	0.000	0.000	0.000
7	A	7	TYR	0	-0.023	-0.038	13.880	0.047	0.047	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.951	0.962	16.294	0.293	0.293	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.033	0.014	20.068	0.025	0.025	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.034	0.009	22.013	0.010	0.010	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.048	-0.028	24.335	0.018	0.018	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.018	0.024	23.792	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.034	-0.006	19.173	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.005	-0.007	15.591	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.003	0.009	12.516	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.029	-0.012	9.738	0.032	0.032	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.039	0.010	7.501	-0.048	-0.048	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.904	0.980	3.700	1.780	2.044	0.003	-0.036	-0.230	0.000
19	A	19	ASN	0	0.059	0.022	2.407	-1.726	-0.367	0.825	-0.814	-1.370	-0.001
20	A	20	GLU	-1	-0.807	-0.894	1.737	-9.794	-16.863	18.785	-5.851	-5.864	-0.044
21	A	21	LYS	1	0.780	0.893	3.924	2.174	2.526	0.012	-0.047	-0.318	0.000
22	A	22	GLY	0	0.029	0.001	6.472	0.616	0.616	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.002	-0.014	6.653	-0.712	-0.712	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.042	-0.030	7.259	0.180	0.180	0.000	0.000	0.000	0.000
25	A	25	MET	0	-0.057	-0.035	9.918	0.234	0.234	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.010	0.011	11.374	-0.086	-0.086	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.763	-0.849	14.169	-0.488	-0.488	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.030	0.007	17.294	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.099	-0.081	16.257	0.069	0.069	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.917	-0.945	17.400	-0.534	-0.534	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.030	0.040	11.631	-0.080	-0.080	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.852	-0.890	10.257	-1.029	-1.029	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.982	0.961	10.601	0.257	0.257	0.000	0.000	0.000	0.000
34	A	35	SER	0	-0.004	0.013	10.283	0.050	0.050	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.052	-0.034	6.085	0.098	0.098	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.049	-0.005	6.732	-0.519	-0.519	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.828	-0.925	6.507	-0.172	-0.172	0.000	0.000	0.000	0.000
38	A	39	ASN	0	0.007	-0.022	7.418	-0.338	-0.338	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.856	-0.897	9.112	-0.210	-0.210	0.000	0.000	0.000	0.000
40	A	41	TYR	0	-0.090	-0.040	3.363	-1.463	-0.129	0.132	-0.557	-0.909	-0.006
41	A	42	PHE	0	-0.091	-0.064	6.316	-0.083	-0.083	0.000	0.000	0.000	0.000
42	A	43	THR	0	0.033	0.030	9.279	0.057	0.057	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.874	-0.939	12.112	-0.175	-0.175	0.000	0.000	0.000	0.000
44	A	45	PHE	0	-0.092	-0.050	11.734	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.030	-0.013	11.535	0.003	0.003	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.061	0.051	15.092	0.042	0.042	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.841	0.909	14.705	0.433	0.433	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.032	-0.014	15.850	0.018	0.018	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.807	-0.873	19.051	-0.271	-0.271	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.036	-0.011	21.395	0.022	0.022	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.062	-0.061	21.647	0.008	0.008	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.023	-0.032	19.913	0.009	0.009	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.860	-0.910	24.785	-0.149	-0.149	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.012	-0.002	27.084	0.017	0.017	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.779	0.890	26.178	0.169	0.169	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.935	0.959	26.016	0.136	0.136	0.000	0.000	0.000	0.000
57	A	58	VAL	0	-0.015	-0.010	20.791	0.007	0.007	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.866	-0.907	20.354	-0.322	-0.322	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.006	-0.019	18.118	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	61	THR	0	-0.077	-0.048	16.491	-0.076	-0.076	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.767	-0.888	11.659	-0.585	-0.585	0.000	0.000	0.000	0.000
62	A	63	PRO	0	-0.001	0.003	10.073	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.008	-0.006	10.483	-0.167	-0.167	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.826	-0.894	8.231	-1.763	-1.763	0.000	0.000	0.000	0.000
65	A	66	PHE	0	-0.004	-0.046	10.847	0.057	0.057	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.962	0.995	9.637	0.987	0.987	0.000	0.000	0.000	0.000
67	A	68	PRO	0	-0.002	-0.001	11.392	0.127	0.127	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.043	-0.008	13.954	0.116	0.116	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.029	0.013	17.400	0.016	0.016	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.849	-0.943	20.324	-0.252	-0.252	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.007	-0.003	22.301	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.951	0.974	20.705	0.399	0.399	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.018	0.036	17.497	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.902	0.954	20.801	0.227	0.227	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.004	-0.004	24.040	0.009	0.009	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.007	-0.022	18.014	0.016	0.016	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.927	0.967	17.259	0.454	0.454	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.850	-0.880	21.514	-0.201	-0.201	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.014	-0.014	22.744	0.017	0.017	0.000	0.000	0.000	0.000
80	A	81	MET	0	-0.052	-0.007	16.087	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.806	0.875	21.625	0.236	0.236	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.078	-0.007	24.792	0.025	0.025	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.908	0.940	25.258	0.149	0.149	0.000	0.000	0.000	0.000
84	A	85	TRP	0	0.048	0.032	24.521	0.004	0.004	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.028	0.003	26.682	0.016	0.016	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.858	-0.894	29.083	-0.168	-0.168	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.041	0.016	29.453	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.833	0.895	30.165	0.187	0.187	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.006	-0.001	31.651	-0.013	-0.013	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.038	-0.001	29.111	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.817	0.903	32.585	0.135	0.135	0.000	0.000	0.000	0.000
92	A	93	GLN	0	0.070	0.039	33.813	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.031	0.018	27.871	0.000	0.000	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.037	-0.038	30.991	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.774	-0.862	32.540	-0.140	-0.140	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.010	0.013	30.804	0.009	0.009	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.023	-0.014	27.284	0.004	0.004	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.826	0.921	30.624	0.152	0.152	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.009	0.008	30.360	0.002	0.002	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.024	0.023	33.665	0.006	0.006	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.085	0.010	33.051	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.982	0.986	32.482	0.152	0.152	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.018	-0.002	30.652	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.059	0.031	27.799	-0.020	-0.020	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.016	0.012	27.531	-0.023	-0.023	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.006	-0.007	27.708	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.039	-0.006	24.777	-0.028	-0.028	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.041	0.004	23.217	-0.040	-0.040	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.100	-0.043	23.230	-0.025	-0.025	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.866	0.923	18.350	0.593	0.593	0.000	0.000	0.000	0.000
111	A	112	ASN	0	0.017	-0.002	17.944	-0.107	-0.107	0.000	0.000	0.000	0.000
112	A	113	ASN	0	0.019	0.001	14.702	0.072	0.072	0.000	0.000	0.000	0.000
113	A	114	VAL	0	0.029	0.008	12.755	-0.063	-0.063	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.021	-0.012	15.306	0.079	0.079	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.036	0.029	17.311	0.046	0.046	0.000	0.000	0.000	0.000
116	A	117	ILE	0	0.027	0.026	12.333	0.043	0.043	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.031	-0.004	16.149	0.054	0.054	0.000	0.000	0.000	0.000
118	A	119	PRO	0	0.022	0.018	18.860	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	120	CYS	0	-0.045	-0.017	21.980	0.032	0.032	0.000	0.000	0.000	0.000
120	A	121	HIS	0	-0.001	-0.020	22.692	0.005	0.005	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.819	0.881	23.062	0.317	0.317	0.000	0.000	0.000	0.000
122	A	123	VAL	0	-0.035	-0.009	26.603	0.020	0.020	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.014	0.015	29.183	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	125	GLY	0	-0.033	-0.024	32.438	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.844	-0.933	35.525	-0.145	-0.145	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.968	0.986	38.889	0.144	0.144	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.024	-0.015	37.286	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	LEU	0	0.138	0.071	33.261	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	130	GLY	0	-0.002	0.011	32.548	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	131	GLY	0	-0.001	-0.002	30.723	0.000	0.000	0.000	0.000	0.000	0.000
131	A	132	TYR	0	0.058	0.004	22.253	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.006	0.013	21.776	0.026	0.026	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.851	0.896	20.494	0.474	0.474	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.034	0.024	25.446	0.016	0.016	0.000	0.000	0.000	0.000
135	A	136	VAL	0	-0.008	-0.025	28.850	-0.007	-0.007	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.858	-0.910	31.442	-0.201	-0.201	0.000	0.000	0.000	0.000
137	A	138	LEU	0	0.048	0.032	23.934	0.007	0.007	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.781	0.891	27.513	0.258	0.258	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.785	0.851	28.494	0.185	0.185	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.886	0.942	29.363	0.222	0.222	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.015	-0.003	23.950	0.005	0.005	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.029	-0.018	27.653	0.005	0.005	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.749	-0.841	30.157	-0.171	-0.171	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.020	0.008	25.664	0.010	0.010	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.770	-0.821	25.358	-0.278	-0.278	0.000	0.000	0.000	0.000
146	A	147	GLY	0	0.012	-0.001	29.697	0.007	0.007	0.000	0.000	0.000	0.000
147	A	148	ILE	0	-0.114	-0.042	30.250	0.009	0.009	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.915	-0.947	34.301	-0.131	-0.131	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.049	-0.027	34.829	0.000	0.000	0.000	0.000	0.000	0.000

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