FMO DATABASE

FMODB ID: KG5N3

Calculation Name: 4GA2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GA2

Chain ID: A

ChEMBL ID:

UniProt ID: H2QII6

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	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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1323431.486336
FMO2-HF: Nuclear repulsion	1265017.376611
FMO2-HF: Total energy	-58414.109726
FMO2-MP2: Total energy	-58585.544591

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:2:ARG)

Summations of interaction energy for fragment #1(A:2:ARG)

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.
22.155	23.571	-0.026	-0.583	-0.807	0.002

Interaction energy analysis for fragmet #1(A:2:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.951 / q_NPA : 0.953

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	4	SER	0	0.004	0.003	3.804	1.570	2.986	-0.026	-0.583	-0.807	0.002
4	A	5	LYS	1	0.998	0.980	6.251	22.616	22.616	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.063	0.037	9.517	1.294	1.294	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.827	-0.905	6.076	-30.471	-30.471	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.047	-0.024	9.070	1.388	1.388	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.909	-0.958	11.324	-16.091	-16.091	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.903	0.950	9.449	23.188	23.188	0.000	0.000	0.000	0.000
10	A	11	TYR	0	-0.014	-0.004	13.220	1.192	1.192	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.031	0.027	15.039	1.024	1.024	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.008	0.004	17.471	0.838	0.838	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.068	-0.046	17.705	0.669	0.669	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.019	-0.015	18.631	0.618	0.618	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.003	-0.007	21.123	0.526	0.526	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.003	0.000	22.876	0.467	0.467	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.016	-0.004	23.573	0.405	0.405	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.115	-0.056	24.460	0.261	0.261	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.081	0.052	25.770	-0.226	-0.226	0.000	0.000	0.000	0.000
20	A	21	SER	0	0.006	0.010	27.599	0.031	0.031	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.079	0.014	28.021	-0.341	-0.341	0.000	0.000	0.000	0.000
22	A	23	ARG	1	1.013	1.004	27.643	8.872	8.872	0.000	0.000	0.000	0.000
23	A	24	GLN	0	0.000	0.000	26.466	-0.256	-0.256	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.956	0.990	23.540	10.115	10.115	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.018	0.011	22.822	-0.454	-0.454	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.044	-0.016	23.700	-0.267	-0.267	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.926	0.963	19.439	12.113	12.113	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.048	0.030	18.815	-0.702	-0.702	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.036	0.005	17.844	-0.607	-0.607	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.033	-0.013	15.445	-0.537	-0.537	0.000	0.000	0.000	0.000
31	A	32	PHE	0	0.021	0.003	14.113	-0.986	-0.986	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.015	0.020	13.754	-0.892	-0.892	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.934	0.966	12.669	14.444	14.444	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.002	0.008	9.335	-1.163	-1.163	0.000	0.000	0.000	0.000
35	A	36	TYR	0	0.067	0.010	8.806	-1.747	-1.747	0.000	0.000	0.000	0.000
36	A	37	TYR	0	-0.004	0.008	9.706	-1.064	-1.064	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.907	-0.944	6.071	-25.914	-25.914	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.062	-0.029	5.356	-2.502	-2.502	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.882	0.954	6.058	30.756	30.756	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.858	-0.927	9.015	-19.532	-19.532	0.000	0.000	0.000	0.000
41	A	42	TYR	0	0.063	0.009	11.012	0.411	0.411	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.886	-0.935	14.421	-12.777	-12.777	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.033	0.010	14.208	0.706	0.706	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.023	-0.012	13.666	0.522	0.522	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.941	0.968	15.630	13.760	13.760	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.991	1.011	19.081	13.215	13.215	0.000	0.000	0.000	0.000
47	A	48	TYR	0	-0.023	-0.030	16.964	0.486	0.486	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.023	0.019	19.001	0.400	0.400	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.013	-0.004	20.573	0.587	0.587	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.052	-0.021	22.128	0.324	0.324	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.072	-0.065	22.279	0.333	0.333	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.009	-0.014	24.028	0.378	0.378	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.058	-0.029	26.460	0.169	0.169	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.025	-0.006	26.926	0.297	0.297	0.000	0.000	0.000	0.000
55	A	56	GLN	0	-0.027	-0.018	26.507	0.464	0.464	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.906	-0.940	28.330	-8.549	-8.549	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.927	0.949	30.476	8.131	8.131	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.809	-0.876	24.711	-10.931	-10.931	0.000	0.000	0.000	0.000
59	A	60	PRO	0	0.023	0.013	26.768	-0.228	-0.228	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.969	0.972	21.742	11.535	11.535	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.011	0.022	21.964	-0.463	-0.463	0.000	0.000	0.000	0.000
62	A	63	HIS	0	0.043	0.010	22.632	-0.380	-0.380	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.835	0.908	22.238	11.465	11.465	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.025	-0.014	14.123	-0.270	-0.270	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.037	0.008	19.298	-0.428	-0.428	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.041	0.004	21.245	-0.066	-0.066	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.009	0.015	15.800	-0.077	-0.077	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.048	-0.038	15.065	-0.486	-0.486	0.000	0.000	0.000	0.000
69	A	70	TYR	0	0.025	0.001	18.356	-0.078	-0.078	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.787	-0.864	21.256	-12.431	-12.431	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.074	-0.040	15.100	-0.203	-0.203	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.940	-0.961	18.787	-14.205	-14.205	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.941	-0.960	20.602	-12.050	-12.050	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.018	0.000	23.613	0.817	0.817	0.000	0.000	0.000	0.000
75	A	76	THR	0	0.063	0.009	25.547	-0.076	-0.076	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.816	-0.898	28.076	-9.027	-9.027	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.856	0.931	25.960	9.812	9.812	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.033	0.017	24.549	-0.030	-0.030	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.016	0.009	25.941	0.079	0.079	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.905	-0.943	29.386	-9.126	-9.126	0.000	0.000	0.000	0.000
81	A	82	CYS	0	-0.058	-0.018	25.446	0.067	0.067	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.044	-0.063	22.659	0.032	0.032	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.978	0.993	28.016	8.287	8.287	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.954	0.994	29.712	8.772	8.772	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.006	-0.024	26.718	0.132	0.132	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.043	-0.021	29.174	0.137	0.137	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.925	-0.978	31.777	-8.026	-8.026	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.092	-0.031	30.115	0.205	0.205	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.000	0.017	28.705	0.335	0.335	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.052	0.023	31.532	-0.232	-0.232	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.071	-0.045	31.600	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	93	GLN	0	-0.045	-0.009	26.600	-0.505	-0.505	0.000	0.000	0.000	0.000
93	A	94	LYS	1	1.005	0.986	30.297	8.187	8.187	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.771	-0.876	26.051	-10.744	-10.744	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.006	-0.006	25.473	-0.121	-0.121	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.045	-0.013	29.092	0.076	0.076	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.019	0.017	30.422	0.160	0.160	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.875	0.944	23.761	12.027	12.027	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.019	-0.018	28.799	-0.070	-0.070	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.004	0.000	30.748	0.079	0.079	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.910	-0.970	28.687	-10.348	-10.348	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.073	-0.036	25.437	-0.070	-0.070	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.019	-0.015	29.408	0.034	0.034	0.000	0.000	0.000	0.000
104	A	105	CYS	0	-0.028	-0.002	32.807	0.213	0.213	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.892	0.953	25.864	11.399	11.399	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.080	-0.037	30.305	0.199	0.199	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.791	-0.889	31.811	-8.128	-8.128	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.062	-0.021	35.563	0.008	0.008	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.024	-0.028	38.497	0.256	0.256	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.801	-0.883	37.835	-7.827	-7.827	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.018	0.014	40.663	0.129	0.129	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.774	0.862	33.692	8.511	8.511	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.043	0.018	36.776	-0.043	-0.043	0.000	0.000	0.000	0.000
114	A	115	LYS	1	1.042	1.018	37.737	6.686	6.686	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.019	-0.006	38.443	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	117	TRP	0	-0.004	-0.021	34.851	-0.016	-0.016	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.037	0.030	37.001	-0.095	-0.095	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.931	-0.957	38.390	-6.821	-6.821	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.896	0.952	36.429	8.068	8.068	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.013	-0.010	35.520	-0.021	-0.021	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.015	0.007	37.091	-0.036	-0.036	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.926	0.959	40.029	6.973	6.973	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.074	-0.036	35.493	0.035	0.035	0.000	0.000	0.000	0.000
124	A	125	PHE	0	-0.062	-0.020	32.011	-0.164	-0.164	0.000	0.000	0.000	0.000
125	A	126	PRO	0	0.038	0.013	37.451	-0.007	-0.007	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.027	0.017	39.998	-0.069	-0.069	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.020	-0.003	34.683	-0.129	-0.129	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.076	0.024	35.014	0.058	0.058	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.002	0.010	32.389	-0.028	-0.028	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.005	-0.016	34.227	-0.023	-0.023	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.002	-0.005	36.860	0.121	0.121	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.954	0.988	32.210	9.558	9.558	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.041	-0.027	33.281	0.025	0.025	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.925	0.957	37.319	7.056	7.056	0.000	0.000	0.000	0.000
135	A	136	GLU	-1	-0.900	-0.954	40.337	-7.630	-7.630	0.000	0.000	0.000	0.000
136	A	137	GLN	0	0.070	0.043	34.722	-0.136	-0.136	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.060	-0.037	39.735	0.084	0.084	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.044	-0.024	41.897	0.119	0.119	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.910	-0.942	42.311	-7.281	-7.281	0.000	0.000	0.000	0.000
140	A	141	CYS	0	-0.125	-0.055	41.668	0.045	0.045	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.973	-0.980	44.433	-6.486	-6.486	0.000	0.000	0.000	0.000
142	A	143	GLY	0	-0.034	-0.012	47.393	0.035	0.035	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.958	-0.978	50.232	-5.930	-5.930	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-1.015	-1.006	53.715	-5.583	-5.583	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ARG)