FMO DATABASE

FMODB ID: QV5NY

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:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1295402.874172
FMO2-HF: Nuclear repulsion	1241876.560236
FMO2-HF: Total energy	-53526.313936
FMO2-MP2: Total energy	-53686.067696

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.
-21.649	-16.366	11.289	-7.024	-9.548	-0.013

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 : 0.063 / q_NPA : 0.017

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	-0.825	-0.920	1.939	-13.015	-12.970	7.892	-3.663	-4.275	-0.040
4	A	25	THR	0	-0.080	-0.045	2.328	-5.203	-2.720	2.775	-2.072	-3.185	0.014
5	A	26	THR	0	0.042	0.007	2.659	-4.257	-1.670	0.624	-1.268	-1.943	0.013
6	A	27	VAL	0	0.045	0.029	4.932	-1.176	-1.074	-0.001	-0.015	-0.086	0.000
7	A	28	PRO	0	-0.013	-0.006	6.660	-0.095	-0.095	0.000	0.000	0.000	0.000
8	A	29	TYR	0	0.009	0.001	6.277	-0.653	-0.653	0.000	0.000	0.000	0.000
9	A	30	ILE	0	0.055	0.041	9.776	-0.263	-0.263	0.000	0.000	0.000	0.000
10	A	31	PHE	0	0.000	-0.016	11.798	-0.188	-0.188	0.000	0.000	0.000	0.000
11	A	32	ARG	1	0.887	0.948	8.035	-0.537	-0.537	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.015	0.029	14.237	-0.086	-0.086	0.000	0.000	0.000	0.000
13	A	34	LEU	0	0.039	0.012	15.913	-0.089	-0.089	0.000	0.000	0.000	0.000
14	A	35	LYS	1	0.870	0.932	16.911	-0.098	-0.098	0.000	0.000	0.000	0.000
15	A	36	LYS	1	0.866	0.938	16.830	-0.438	-0.438	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.011	0.003	19.374	-0.023	-0.023	0.000	0.000	0.000	0.000
17	A	38	MET	0	0.009	0.013	21.629	0.005	0.005	0.000	0.000	0.000	0.000
18	A	39	GLY	0	0.030	0.030	23.075	-0.026	-0.026	0.000	0.000	0.000	0.000
19	A	40	PHE	0	-0.002	0.000	20.248	-0.028	-0.028	0.000	0.000	0.000	0.000
20	A	41	GLU	-1	-0.772	-0.884	20.962	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	42	ARG	1	0.752	0.855	18.484	0.080	0.080	0.000	0.000	0.000	0.000
22	A	43	LEU	0	0.015	0.031	15.374	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	44	THR	0	-0.010	-0.016	13.789	-0.117	-0.117	0.000	0.000	0.000	0.000
24	A	45	LEU	0	0.012	0.020	7.779	0.091	0.091	0.000	0.000	0.000	0.000
25	A	46	THR	0	-0.043	-0.037	11.108	-0.208	-0.208	0.000	0.000	0.000	0.000
26	A	47	ILE	0	-0.008	-0.022	7.963	0.125	0.125	0.000	0.000	0.000	0.000
27	A	48	TYR	0	-0.075	-0.052	11.089	-0.124	-0.124	0.000	0.000	0.000	0.000
28	A	49	ASP	-1	-0.801	-0.880	11.715	-0.647	-0.647	0.000	0.000	0.000	0.000
29	A	50	PRO	0	-0.001	-0.016	13.590	0.037	0.037	0.000	0.000	0.000	0.000
30	A	51	SER	0	-0.026	0.003	15.625	0.022	0.022	0.000	0.000	0.000	0.000
31	A	52	THR	0	-0.093	-0.067	16.453	0.025	0.025	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.823	-0.889	18.560	-0.140	-0.140	0.000	0.000	0.000	0.000
33	A	54	GLN	0	-0.068	-0.041	17.276	0.034	0.034	0.000	0.000	0.000	0.000
34	A	55	ILE	0	-0.031	-0.002	14.457	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	56	VAL	0	0.048	0.011	11.945	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	57	VAL	0	-0.023	-0.022	11.600	0.011	0.011	0.000	0.000	0.000	0.000
37	A	58	ARG	1	0.853	0.940	4.452	1.842	1.908	-0.001	-0.006	-0.059	0.000
38	A	59	ALA	0	0.025	0.001	7.148	-0.531	-0.531	0.000	0.000	0.000	0.000
39	A	60	THR	0	-0.004	0.000	9.152	0.306	0.306	0.000	0.000	0.000	0.000
40	A	61	SER	0	0.003	0.011	11.630	0.000	0.000	0.000	0.000	0.000	0.000
41	A	62	SER	0	-0.085	-0.059	13.357	0.066	0.066	0.000	0.000	0.000	0.000
42	A	63	GLY	0	0.052	0.026	12.705	-0.060	-0.060	0.000	0.000	0.000	0.000
43	A	64	LYS	1	0.981	0.989	13.791	0.396	0.396	0.000	0.000	0.000	0.000
44	A	65	PHE	0	0.001	0.009	6.883	0.165	0.165	0.000	0.000	0.000	0.000
45	A	66	PRO	0	0.019	0.019	12.551	-0.108	-0.108	0.000	0.000	0.000	0.000
46	A	67	LYS	1	0.903	0.941	8.552	1.797	1.797	0.000	0.000	0.000	0.000
47	A	68	GLU	-1	-0.795	-0.900	14.150	-0.349	-0.349	0.000	0.000	0.000	0.000
48	A	69	GLY	0	0.041	0.020	15.256	-0.062	-0.062	0.000	0.000	0.000	0.000
49	A	70	PHE	0	-0.045	-0.004	17.190	0.036	0.036	0.000	0.000	0.000	0.000
50	A	71	LYS	1	1.053	1.028	19.197	0.223	0.223	0.000	0.000	0.000	0.000
51	A	72	LYS	1	0.900	0.949	20.497	0.049	0.049	0.000	0.000	0.000	0.000
52	A	73	GLY	0	-0.004	-0.007	23.555	0.005	0.005	0.000	0.000	0.000	0.000
53	A	74	GLU	-1	-0.865	-0.914	22.842	-0.225	-0.225	0.000	0.000	0.000	0.000
54	A	75	GLY	0	0.083	0.028	23.535	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	76	ILE	0	0.014	0.005	23.905	0.007	0.007	0.000	0.000	0.000	0.000
56	A	77	THR	0	0.017	0.001	18.009	0.030	0.030	0.000	0.000	0.000	0.000
57	A	78	GLY	0	0.060	0.034	20.758	0.014	0.014	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.748	0.875	22.152	0.061	0.061	0.000	0.000	0.000	0.000
59	A	80	VAL	0	0.015	0.020	20.495	0.012	0.012	0.000	0.000	0.000	0.000
60	A	81	TRP	0	-0.030	-0.022	17.559	0.014	0.014	0.000	0.000	0.000	0.000
61	A	82	LYS	1	0.875	0.946	20.774	0.041	0.041	0.000	0.000	0.000	0.000
62	A	83	HIS	0	0.043	0.010	24.282	0.006	0.006	0.000	0.000	0.000	0.000
63	A	84	GLY	0	0.008	0.020	22.453	0.014	0.014	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.018	-0.009	23.531	0.034	0.034	0.000	0.000	0.000	0.000
65	A	86	PRO	0	0.009	-0.010	23.109	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	87	ILE	0	0.000	0.010	24.233	-0.013	-0.013	0.000	0.000	0.000	0.000
67	A	88	VAL	0	-0.004	0.002	25.061	0.005	0.005	0.000	0.000	0.000	0.000
68	A	89	ILE	0	0.007	0.004	27.346	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	90	PRO	0	0.019	-0.008	29.196	0.000	0.000	0.000	0.000	0.000	0.000
70	A	91	ASP	-1	-0.818	-0.891	31.580	0.003	0.003	0.000	0.000	0.000	0.000
71	A	92	ILE	0	-0.027	-0.016	25.971	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	93	SER	0	-0.118	-0.075	30.128	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	94	GLN	0	-0.035	-0.026	33.392	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.848	-0.917	30.089	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.036	0.019	31.246	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	97	GLU	-1	-0.805	-0.889	29.335	-0.057	-0.057	0.000	0.000	0.000	0.000
77	A	98	PHE	0	-0.049	-0.035	23.932	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	99	LEU	0	0.025	0.004	24.790	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	100	ASN	0	-0.035	-0.015	24.661	-0.022	-0.022	0.000	0.000	0.000	0.000
80	A	101	LYS	1	0.841	0.921	20.925	0.282	0.282	0.000	0.000	0.000	0.000
81	A	102	VAL	0	0.012	0.012	16.411	-0.022	-0.022	0.000	0.000	0.000	0.000
82	A	103	TRP	0	-0.050	-0.042	16.236	-0.046	-0.046	0.000	0.000	0.000	0.000
83	A	104	LYS	1	0.814	0.908	21.336	0.346	0.346	0.000	0.000	0.000	0.000
84	A	105	ARG	1	0.819	0.885	21.523	0.103	0.103	0.000	0.000	0.000	0.000
85	A	106	LYS	1	1.021	0.990	26.527	0.140	0.140	0.000	0.000	0.000	0.000
86	A	107	LYS	1	0.955	0.981	30.189	0.078	0.078	0.000	0.000	0.000	0.000
87	A	108	SER	0	-0.001	0.008	28.488	0.001	0.001	0.000	0.000	0.000	0.000
88	A	109	LYS	1	0.772	0.838	26.822	0.003	0.003	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.847	0.916	30.925	-0.023	-0.023	0.000	0.000	0.000	0.000
90	A	111	LYS	1	1.021	1.030	32.776	-0.033	-0.033	0.000	0.000	0.000	0.000
91	A	112	ILE	0	-0.042	-0.020	26.382	0.009	0.009	0.000	0.000	0.000	0.000
92	A	113	ALA	0	0.060	0.052	28.352	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	114	PHE	0	-0.015	-0.027	20.847	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	115	ILE	0	0.006	0.011	22.406	0.008	0.008	0.000	0.000	0.000	0.000
95	A	116	ALA	0	-0.011	-0.007	20.227	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	117	VAL	0	0.037	0.009	17.966	0.003	0.003	0.000	0.000	0.000	0.000
97	A	118	PRO	0	-0.012	-0.001	18.043	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	119	ILE	0	-0.023	-0.010	12.162	0.044	0.044	0.000	0.000	0.000	0.000
99	A	120	LYS	1	0.870	0.919	15.879	-0.272	-0.272	0.000	0.000	0.000	0.000
100	A	121	SER	0	0.065	0.029	13.811	0.045	0.045	0.000	0.000	0.000	0.000
101	A	122	GLY	0	0.051	0.033	16.257	-0.069	-0.069	0.000	0.000	0.000	0.000
102	A	123	GLY	0	-0.004	0.002	18.488	-0.047	-0.047	0.000	0.000	0.000	0.000
103	A	124	LYS	1	0.931	0.964	18.927	-0.146	-0.146	0.000	0.000	0.000	0.000
104	A	125	VAL	0	0.003	-0.006	17.770	0.049	0.049	0.000	0.000	0.000	0.000
105	A	126	ILE	0	0.024	0.029	11.817	-0.064	-0.064	0.000	0.000	0.000	0.000
106	A	127	GLY	0	0.038	0.004	13.101	-0.080	-0.080	0.000	0.000	0.000	0.000
107	A	128	VAL	0	-0.046	0.000	14.124	0.051	0.051	0.000	0.000	0.000	0.000
108	A	129	LEU	0	0.020	0.038	13.637	-0.069	-0.069	0.000	0.000	0.000	0.000
109	A	130	SER	0	-0.032	-0.018	15.462	-0.019	-0.019	0.000	0.000	0.000	0.000
110	A	131	ALA	0	0.008	-0.002	17.336	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.702	-0.802	20.024	-0.058	-0.058	0.000	0.000	0.000	0.000
112	A	133	LYS	1	0.825	0.897	23.105	-0.128	-0.128	0.000	0.000	0.000	0.000
113	A	134	GLU	-1	-0.716	-0.817	25.888	0.021	0.021	0.000	0.000	0.000	0.000
114	A	135	ILE	0	-0.022	0.002	29.244	0.019	0.019	0.000	0.000	0.000	0.000
115	A	136	ASN	0	-0.036	-0.023	30.606	-0.022	-0.022	0.000	0.000	0.000	0.000
116	A	137	GLU	-1	-0.824	-0.908	33.536	0.098	0.098	0.000	0.000	0.000	0.000
117	A	138	LYS	1	0.844	0.905	35.423	-0.103	-0.103	0.000	0.000	0.000	0.000
118	A	139	ASP	-1	-0.742	-0.823	29.891	0.179	0.179	0.000	0.000	0.000	0.000
119	A	140	SER	0	0.006	-0.039	31.124	-0.013	-0.013	0.000	0.000	0.000	0.000
120	A	141	LEU	0	0.030	-0.002	28.156	0.015	0.015	0.000	0.000	0.000	0.000
121	A	142	ASP	-1	-0.816	-0.877	27.768	0.195	0.195	0.000	0.000	0.000	0.000
122	A	143	GLU	-1	-0.805	-0.871	27.763	0.223	0.223	0.000	0.000	0.000	0.000
123	A	144	TYR	0	-0.043	-0.048	24.444	0.037	0.037	0.000	0.000	0.000	0.000
124	A	145	THR	0	0.000	-0.016	23.353	0.020	0.020	0.000	0.000	0.000	0.000
125	A	146	ARG	1	0.827	0.908	23.308	-0.198	-0.198	0.000	0.000	0.000	0.000
126	A	147	PHE	0	0.040	0.017	19.190	0.042	0.042	0.000	0.000	0.000	0.000
127	A	148	LEU	0	0.007	-0.011	18.415	0.064	0.064	0.000	0.000	0.000	0.000
128	A	149	SER	0	-0.006	-0.014	18.477	0.030	0.030	0.000	0.000	0.000	0.000
129	A	150	MET	0	0.006	0.023	19.193	0.051	0.051	0.000	0.000	0.000	0.000
130	A	151	ILE	0	-0.013	-0.008	14.475	0.104	0.104	0.000	0.000	0.000	0.000
131	A	152	ALA	0	-0.008	-0.015	14.443	0.117	0.117	0.000	0.000	0.000	0.000
132	A	153	THR	0	-0.004	-0.007	14.587	0.041	0.041	0.000	0.000	0.000	0.000
133	A	154	LEU	0	-0.010	0.005	11.828	0.068	0.068	0.000	0.000	0.000	0.000
134	A	155	ILE	0	-0.017	-0.021	9.200	0.242	0.242	0.000	0.000	0.000	0.000
135	A	156	ALA	0	-0.015	-0.016	10.333	0.163	0.163	0.000	0.000	0.000	0.000
136	A	157	ASN	0	-0.015	-0.008	12.353	-0.050	-0.050	0.000	0.000	0.000	0.000
137	A	158	SER	0	-0.042	-0.018	6.699	0.230	0.230	0.000	0.000	0.000	0.000
138	A	159	PHE	0	-0.074	-0.032	7.537	0.437	0.437	0.000	0.000	0.000	0.000
139	A	160	SER	0	0.007	0.016	9.478	-0.251	-0.251	0.000	0.000	0.000	0.000

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