FMO DATABASE

FMODB ID: R84Y8

Calculation Name: 4G3W-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4G3W

Chain ID: A

ChEMBL ID:

UniProt ID: O66591

Base Structure: X-ray

Registration Date: 2023-09-23

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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1290419.423157
FMO2-HF: Nuclear repulsion	1236893.595346
FMO2-HF: Total energy	-53525.827811
FMO2-MP2: Total energy	-53685.57234

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:22:ASN)

Summations of interaction energy for fragment #1(A:22:ASN)

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.
-21.639	-12.747	6.485	-6.216	-9.161	0.001

Interaction energy analysis for fragmet #1(A:22:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.051 / q_NPA : 0.014

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	24	GLU	-1	-0.842	-0.932	2.387	-12.960	-8.440	2.061	-2.796	-3.786	-0.023
4	A	25	THR	0	-0.086	-0.040	2.328	-6.503	-4.351	4.101	-2.507	-3.746	0.015
5	A	26	THR	0	0.043	0.009	2.816	-3.512	-1.432	0.325	-0.899	-1.505	0.009
6	A	27	VAL	0	0.041	0.034	5.175	-0.869	-0.794	-0.001	-0.010	-0.065	0.000
7	A	28	PRO	0	-0.022	-0.012	7.038	-0.036	-0.036	0.000	0.000	0.000	0.000
8	A	29	TYR	0	-0.011	-0.009	6.266	-0.630	-0.630	0.000	0.000	0.000	0.000
9	A	30	ILE	0	0.062	0.041	10.070	-0.228	-0.228	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.010	-0.020	11.973	-0.169	-0.169	0.000	0.000	0.000	0.000
11	A	32	ARG	1	0.909	0.962	8.892	-0.389	-0.389	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.031	0.026	14.568	-0.088	-0.088	0.000	0.000	0.000	0.000
13	A	34	LEU	0	0.044	0.023	16.220	-0.074	-0.074	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.884	0.940	17.076	-0.076	-0.076	0.000	0.000	0.000	0.000
15	A	36	LYS	1	0.899	0.947	17.326	-0.341	-0.341	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.010	0.002	19.776	-0.023	-0.023	0.000	0.000	0.000	0.000
17	A	38	MET	0	-0.004	0.010	21.901	0.004	0.004	0.000	0.000	0.000	0.000
18	A	39	GLY	0	0.021	0.029	23.151	-0.022	-0.022	0.000	0.000	0.000	0.000
19	A	40	PHE	0	0.011	0.003	20.455	-0.031	-0.031	0.000	0.000	0.000	0.000
20	A	41	GLU	-1	-0.818	-0.888	20.988	-0.016	-0.016	0.000	0.000	0.000	0.000
21	A	42	ARG	1	0.750	0.851	18.708	0.085	0.085	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.025	0.026	15.589	-0.023	-0.023	0.000	0.000	0.000	0.000
23	A	44	THR	0	-0.042	-0.030	14.398	-0.117	-0.117	0.000	0.000	0.000	0.000
24	A	45	LEU	0	0.054	0.048	8.342	0.087	0.087	0.000	0.000	0.000	0.000
25	A	46	THR	0	-0.041	-0.023	11.736	-0.180	-0.180	0.000	0.000	0.000	0.000
26	A	47	ILE	0	-0.010	-0.018	8.164	0.115	0.115	0.000	0.000	0.000	0.000
27	A	48	TYR	0	-0.068	-0.043	11.330	-0.117	-0.117	0.000	0.000	0.000	0.000
28	A	49	ASP	-1	-0.811	-0.895	12.111	-0.635	-0.635	0.000	0.000	0.000	0.000
29	A	50	PRO	0	0.010	-0.012	13.223	0.036	0.036	0.000	0.000	0.000	0.000
30	A	51	SER	0	-0.016	0.013	15.655	0.026	0.026	0.000	0.000	0.000	0.000
31	A	52	THR	0	-0.104	-0.078	16.339	0.036	0.036	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.833	-0.888	18.114	-0.138	-0.138	0.000	0.000	0.000	0.000
33	A	54	GLN	0	-0.060	-0.035	17.315	0.033	0.033	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.038	-0.002	14.698	-0.034	-0.034	0.000	0.000	0.000	0.000
35	A	56	VAL	0	0.039	0.002	12.418	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	57	VAL	0	-0.035	-0.014	11.792	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	58	ARG	1	0.826	0.916	4.504	1.965	2.030	-0.001	-0.004	-0.059	0.000
38	A	59	ALA	0	0.067	0.021	7.509	-0.504	-0.504	0.000	0.000	0.000	0.000
39	A	60	THR	0	-0.028	-0.007	9.485	0.274	0.274	0.000	0.000	0.000	0.000
40	A	61	SER	0	0.037	0.020	11.921	0.006	0.006	0.000	0.000	0.000	0.000
41	A	62	SER	0	-0.097	-0.059	14.114	0.070	0.070	0.000	0.000	0.000	0.000
42	A	63	GLY	0	0.037	0.014	13.107	-0.072	-0.072	0.000	0.000	0.000	0.000
43	A	64	LYS	1	0.984	0.995	13.876	0.389	0.389	0.000	0.000	0.000	0.000
44	A	65	PHE	0	0.001	0.005	7.486	0.164	0.164	0.000	0.000	0.000	0.000
45	A	66	PRO	0	0.015	0.024	13.171	-0.101	-0.101	0.000	0.000	0.000	0.000
46	A	67	LYS	1	0.922	0.941	9.110	1.637	1.637	0.000	0.000	0.000	0.000
47	A	68	GLU	-1	-0.823	-0.914	14.572	-0.359	-0.359	0.000	0.000	0.000	0.000
48	A	69	GLY	0	0.040	0.020	15.809	-0.044	-0.044	0.000	0.000	0.000	0.000
49	A	70	PHE	0	-0.045	-0.014	17.598	0.036	0.036	0.000	0.000	0.000	0.000
50	A	71	LYS	1	1.048	1.028	19.518	0.213	0.213	0.000	0.000	0.000	0.000
51	A	72	LYS	1	0.960	0.969	21.065	0.059	0.059	0.000	0.000	0.000	0.000
52	A	73	GLY	0	-0.046	-0.029	23.614	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	74	GLU	-1	-0.861	-0.903	23.484	-0.223	-0.223	0.000	0.000	0.000	0.000
54	A	75	GLY	0	0.078	0.024	23.948	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	76	ILE	0	0.043	0.016	24.632	0.007	0.007	0.000	0.000	0.000	0.000
56	A	77	THR	0	0.000	0.004	18.588	0.025	0.025	0.000	0.000	0.000	0.000
57	A	78	GLY	0	0.063	0.032	21.256	0.014	0.014	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.777	0.881	22.591	0.063	0.063	0.000	0.000	0.000	0.000
59	A	80	VAL	0	0.020	0.022	21.028	0.013	0.013	0.000	0.000	0.000	0.000
60	A	81	TRP	0	-0.044	-0.026	18.306	0.014	0.014	0.000	0.000	0.000	0.000
61	A	82	LYS	1	0.866	0.932	21.234	0.052	0.052	0.000	0.000	0.000	0.000
62	A	83	HIS	0	0.041	0.010	24.545	0.007	0.007	0.000	0.000	0.000	0.000
63	A	84	GLY	0	0.009	0.018	22.894	0.014	0.014	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.008	-0.004	23.947	0.031	0.031	0.000	0.000	0.000	0.000
65	A	86	PRO	0	0.018	-0.001	23.720	-0.016	-0.016	0.000	0.000	0.000	0.000
66	A	87	ILE	0	-0.011	0.005	24.914	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	88	VAL	0	0.002	0.005	25.991	0.000	0.000	0.000	0.000	0.000	0.000
68	A	89	ILE	0	-0.011	-0.012	27.593	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	90	PRO	0	0.023	-0.001	29.771	0.002	0.002	0.000	0.000	0.000	0.000
70	A	91	ASP	-1	-0.818	-0.898	32.199	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	92	ILE	0	-0.029	-0.012	26.458	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	93	SER	0	-0.125	-0.080	30.773	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	94	GLN	0	-0.032	-0.024	33.883	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.853	-0.912	30.972	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.023	0.007	31.865	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	97	GLU	-1	-0.836	-0.902	30.081	-0.056	-0.056	0.000	0.000	0.000	0.000
77	A	98	PHE	0	-0.077	-0.044	24.456	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	99	LEU	0	0.037	0.014	24.877	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.037	-0.007	24.901	-0.018	-0.018	0.000	0.000	0.000	0.000
80	A	101	LYS	1	0.877	0.931	21.308	0.284	0.284	0.000	0.000	0.000	0.000
81	A	102	VAL	0	0.011	0.007	17.014	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	103	TRP	0	-0.052	-0.042	16.629	-0.042	-0.042	0.000	0.000	0.000	0.000
83	A	104	LYS	1	0.816	0.923	21.815	0.354	0.354	0.000	0.000	0.000	0.000
84	A	105	ARG	1	0.839	0.889	22.367	0.108	0.108	0.000	0.000	0.000	0.000
85	A	106	LYS	1	1.007	0.973	26.844	0.138	0.138	0.000	0.000	0.000	0.000
86	A	107	LYS	1	0.997	1.003	30.468	0.090	0.090	0.000	0.000	0.000	0.000
87	A	108	SER	0	-0.031	-0.007	28.838	0.002	0.002	0.000	0.000	0.000	0.000
88	A	109	LYS	1	0.800	0.844	27.347	0.012	0.012	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.820	0.928	31.601	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	111	LYS	1	1.032	1.016	33.301	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	112	ILE	0	-0.055	-0.020	26.805	0.011	0.011	0.000	0.000	0.000	0.000
92	A	113	ALA	0	0.091	0.060	28.732	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	114	PHE	0	-0.034	-0.034	21.386	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	115	ILE	0	0.020	0.021	23.217	0.007	0.007	0.000	0.000	0.000	0.000
95	A	116	ALA	0	-0.005	-0.004	20.757	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	117	VAL	0	0.017	0.000	18.424	0.002	0.002	0.000	0.000	0.000	0.000
97	A	118	PRO	0	0.012	-0.002	18.642	-0.015	-0.015	0.000	0.000	0.000	0.000
98	A	119	ILE	0	-0.012	0.002	12.665	0.045	0.045	0.000	0.000	0.000	0.000
99	A	120	LYS	1	0.883	0.928	16.236	-0.244	-0.244	0.000	0.000	0.000	0.000
100	A	121	SER	0	0.061	0.024	14.009	0.047	0.047	0.000	0.000	0.000	0.000
101	A	122	GLY	0	0.049	0.037	16.561	-0.057	-0.057	0.000	0.000	0.000	0.000
102	A	123	GLY	0	-0.016	-0.008	18.742	-0.045	-0.045	0.000	0.000	0.000	0.000
103	A	124	LYS	1	0.942	0.976	19.107	-0.138	-0.138	0.000	0.000	0.000	0.000
104	A	125	VAL	0	-0.015	-0.013	18.003	0.046	0.046	0.000	0.000	0.000	0.000
105	A	126	ILE	0	0.020	0.027	12.154	-0.059	-0.059	0.000	0.000	0.000	0.000
106	A	127	GLY	0	0.033	-0.001	13.676	-0.087	-0.087	0.000	0.000	0.000	0.000
107	A	128	VAL	0	-0.051	-0.013	14.520	0.060	0.060	0.000	0.000	0.000	0.000
108	A	129	LEU	0	0.028	0.028	14.228	-0.063	-0.063	0.000	0.000	0.000	0.000
109	A	130	SER	0	0.025	0.014	16.056	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	131	ALA	0	-0.030	-0.014	17.871	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.713	-0.804	20.557	-0.070	-0.070	0.000	0.000	0.000	0.000
112	A	133	LYS	1	0.905	0.941	23.575	-0.106	-0.106	0.000	0.000	0.000	0.000
113	A	134	GLU	-1	-0.762	-0.847	26.335	0.010	0.010	0.000	0.000	0.000	0.000
114	A	135	ILE	0	-0.007	-0.001	29.723	0.016	0.016	0.000	0.000	0.000	0.000
115	A	136	ASN	0	-0.021	-0.018	30.765	-0.021	-0.021	0.000	0.000	0.000	0.000
116	A	137	GLU	-1	-0.854	-0.914	33.834	0.084	0.084	0.000	0.000	0.000	0.000
117	A	138	LYS	1	0.864	0.909	35.919	-0.093	-0.093	0.000	0.000	0.000	0.000
118	A	139	ASP	-1	-0.789	-0.844	30.537	0.165	0.165	0.000	0.000	0.000	0.000
119	A	140	SER	0	0.015	-0.035	32.123	-0.015	-0.015	0.000	0.000	0.000	0.000
120	A	141	LEU	0	0.022	-0.017	28.706	0.014	0.014	0.000	0.000	0.000	0.000
121	A	142	ASP	-1	-0.828	-0.874	28.524	0.172	0.172	0.000	0.000	0.000	0.000
122	A	143	GLU	-1	-0.837	-0.885	28.590	0.199	0.199	0.000	0.000	0.000	0.000
123	A	144	TYR	0	-0.074	-0.068	24.980	0.031	0.031	0.000	0.000	0.000	0.000
124	A	145	THR	0	-0.004	-0.025	24.022	0.023	0.023	0.000	0.000	0.000	0.000
125	A	146	ARG	1	0.890	0.939	23.769	-0.188	-0.188	0.000	0.000	0.000	0.000
126	A	147	PHE	0	0.065	0.024	19.777	0.039	0.039	0.000	0.000	0.000	0.000
127	A	148	LEU	0	0.016	0.006	18.722	0.061	0.061	0.000	0.000	0.000	0.000
128	A	149	SER	0	-0.023	-0.017	18.936	0.029	0.029	0.000	0.000	0.000	0.000
129	A	150	MET	0	0.002	0.013	19.775	0.043	0.043	0.000	0.000	0.000	0.000
130	A	151	ILE	0	-0.020	-0.015	15.013	0.092	0.092	0.000	0.000	0.000	0.000
131	A	152	ALA	0	-0.025	-0.027	15.005	0.102	0.102	0.000	0.000	0.000	0.000
132	A	153	THR	0	-0.028	-0.018	14.902	0.053	0.053	0.000	0.000	0.000	0.000
133	A	154	LEU	0	-0.011	0.003	12.391	0.064	0.064	0.000	0.000	0.000	0.000
134	A	155	ILE	0	-0.038	-0.020	9.629	0.235	0.235	0.000	0.000	0.000	0.000
135	A	156	ALA	0	-0.006	-0.019	10.500	0.187	0.187	0.000	0.000	0.000	0.000
136	A	157	ASN	0	-0.012	0.003	12.197	-0.071	-0.071	0.000	0.000	0.000	0.000
137	A	158	SER	0	-0.003	-0.009	6.522	0.234	0.234	0.000	0.000	0.000	0.000
138	A	159	PHE	0	-0.091	-0.015	7.950	0.259	0.259	0.000	0.000	0.000	0.000
139	A	160	SER	0	0.019	0.007	9.456	-0.287	-0.287	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ASN)