FMO DATABASE

FMODB ID: 4JZ7N

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:

Apendix: None

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1324408.900565
FMO2-HF: Nuclear repulsion	1265994.041007
FMO2-HF: Total energy	-58414.859558
FMO2-MP2: Total energy	-58586.371106

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.
19.394	21.576	-0.03	-1.069	-1.082	0.005

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 : 0.976 / q_NPA : 0.985

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	0.003	-0.025	3.804	0.865	3.047	-0.030	-1.069	-1.082	0.005
4	A	5	LYS	1	0.915	0.932	6.429	21.736	21.736	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.073	0.042	9.732	1.252	1.252	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.808	-0.870	6.494	-29.681	-29.681	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.047	-0.020	9.087	1.350	1.350	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.896	-0.961	11.324	-16.539	-16.539	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.886	0.939	9.455	23.760	23.760	0.000	0.000	0.000	0.000
10	A	11	TYR	0	0.001	0.005	13.232	1.237	1.237	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.036	0.028	15.061	1.071	1.071	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.008	0.004	17.459	0.870	0.870	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.055	-0.038	17.717	0.659	0.659	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.018	-0.015	18.507	0.646	0.646	0.000	0.000	0.000	0.000
15	A	16	GLN	0	0.003	0.003	21.048	0.613	0.613	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.014	0.013	22.941	0.498	0.498	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.018	0.002	23.399	0.402	0.402	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.102	-0.055	24.220	0.289	0.289	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.075	0.043	25.558	-0.249	-0.249	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.007	-0.017	27.421	0.099	0.099	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.062	0.007	27.623	-0.337	-0.337	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.957	0.971	27.170	9.010	9.010	0.000	0.000	0.000	0.000
23	A	24	GLN	0	0.036	0.034	26.060	-0.205	-0.205	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.889	0.949	23.114	10.207	10.207	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.040	0.016	22.258	-0.525	-0.525	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.039	-0.011	22.973	-0.291	-0.291	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.912	0.956	19.038	12.584	12.584	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.054	0.029	18.182	-0.740	-0.740	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.026	0.005	16.983	-0.643	-0.643	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.034	-0.011	14.839	-0.586	-0.586	0.000	0.000	0.000	0.000
31	A	32	PHE	0	0.018	0.002	13.363	-1.108	-1.108	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.015	0.020	13.344	-0.973	-0.973	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.935	0.968	11.668	14.459	14.459	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.014	0.004	8.765	-1.338	-1.338	0.000	0.000	0.000	0.000
35	A	36	TYR	0	0.065	0.004	8.496	-1.569	-1.569	0.000	0.000	0.000	0.000
36	A	37	TYR	0	-0.005	0.011	9.705	-1.181	-1.181	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.871	-0.916	5.109	-29.180	-29.180	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.061	-0.029	5.343	-3.220	-3.220	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.885	0.961	5.566	32.125	32.125	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.825	-0.895	9.016	-20.072	-20.072	0.000	0.000	0.000	0.000
41	A	42	TYR	0	0.072	0.010	11.028	0.391	0.391	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.834	-0.920	14.421	-12.871	-12.871	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.007	0.005	13.871	0.686	0.686	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.018	-0.011	13.647	0.511	0.511	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.858	0.919	15.627	14.230	14.230	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.961	0.994	19.075	13.568	13.568	0.000	0.000	0.000	0.000
47	A	48	TYR	0	0.006	-0.010	16.665	0.829	0.829	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.030	0.024	18.503	0.403	0.403	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.011	-0.003	20.111	0.603	0.603	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.062	-0.032	21.787	0.340	0.340	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.070	-0.063	21.523	0.355	0.355	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.000	-0.007	23.357	0.391	0.391	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.051	-0.023	25.775	0.247	0.247	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.032	-0.008	26.157	0.322	0.322	0.000	0.000	0.000	0.000
55	A	56	GLN	0	-0.014	-0.004	25.590	0.466	0.466	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.887	-0.931	27.354	-8.593	-8.593	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.965	0.968	29.593	8.159	8.159	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.801	-0.878	23.596	-11.133	-11.133	0.000	0.000	0.000	0.000
59	A	60	PRO	0	0.022	0.013	25.762	-0.235	-0.235	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.968	0.976	20.960	11.419	11.419	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.009	0.021	20.968	-0.482	-0.482	0.000	0.000	0.000	0.000
62	A	63	HIS	0	0.015	-0.004	21.837	-0.403	-0.403	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.834	0.900	21.264	11.537	11.537	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.024	-0.017	13.325	-0.323	-0.323	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.031	0.007	18.744	-0.447	-0.447	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.041	0.009	20.811	-0.060	-0.060	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.006	0.014	15.226	-0.095	-0.095	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.053	-0.036	14.848	-0.526	-0.526	0.000	0.000	0.000	0.000
69	A	70	TYR	0	0.023	0.002	18.264	-0.080	-0.080	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.775	-0.864	21.005	-12.321	-12.321	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.070	-0.040	14.935	-0.226	-0.226	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.888	-0.922	18.873	-14.083	-14.083	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.817	-0.883	20.594	-11.682	-11.682	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.004	0.006	23.605	0.829	0.829	0.000	0.000	0.000	0.000
75	A	76	THR	0	0.037	-0.017	25.538	-0.180	-0.180	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.787	-0.874	28.063	-9.021	-9.021	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.802	0.889	25.950	9.803	9.803	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.041	0.025	24.467	-0.036	-0.036	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.027	0.012	25.741	0.073	0.073	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.843	-0.890	29.091	-9.164	-9.164	0.000	0.000	0.000	0.000
81	A	82	CYS	0	-0.081	-0.033	24.913	0.079	0.079	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.036	-0.059	21.991	0.034	0.034	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.944	0.967	27.305	8.297	8.297	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.909	0.960	29.004	8.761	8.761	0.000	0.000	0.000	0.000
85	A	86	SER	0	0.002	-0.025	25.714	0.139	0.139	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.046	-0.025	28.177	0.153	0.153	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.874	-0.931	30.788	-8.104	-8.104	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.084	-0.025	29.093	0.202	0.202	0.000	0.000	0.000	0.000
89	A	90	ASN	0	-0.003	0.014	27.713	0.327	0.327	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.047	0.023	30.537	-0.227	-0.227	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.063	-0.044	30.591	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	93	GLN	0	-0.043	-0.008	25.551	-0.506	-0.506	0.000	0.000	0.000	0.000
93	A	94	LYS	1	1.005	0.985	29.333	8.182	8.182	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.777	-0.877	25.117	-10.817	-10.817	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.005	0.004	24.451	-0.106	-0.106	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.049	-0.015	28.165	0.083	0.083	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.017	0.014	29.741	0.159	0.159	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.868	0.948	23.631	11.892	11.892	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.005	-0.013	28.058	-0.064	-0.064	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.003	0.001	30.172	0.083	0.083	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.895	-0.958	27.442	-10.554	-10.554	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.068	-0.032	25.059	-0.039	-0.039	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.014	-0.011	29.168	0.038	0.038	0.000	0.000	0.000	0.000
104	A	105	CYS	0	-0.045	-0.017	32.649	0.223	0.223	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.763	0.873	25.926	11.503	11.503	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.034	-0.006	30.319	-0.103	-0.103	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.812	-0.879	31.797	-8.128	-8.128	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.053	-0.020	35.549	0.002	0.002	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.020	-0.037	38.481	0.256	0.256	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.784	-0.857	37.461	-7.921	-7.921	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.026	0.017	40.616	0.128	0.128	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.695	0.799	33.639	8.551	8.551	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.038	0.013	36.431	-0.045	-0.045	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.969	0.962	37.432	6.730	6.730	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.019	-0.004	37.695	-0.015	-0.015	0.000	0.000	0.000	0.000
116	A	117	TRP	0	0.011	-0.019	33.588	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.046	0.036	36.465	-0.095	-0.095	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.843	-0.900	37.732	-6.844	-6.844	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.876	0.947	35.112	8.171	8.171	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.024	-0.002	34.655	-0.018	-0.018	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.010	0.008	36.222	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.903	0.949	39.198	7.097	7.097	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.070	-0.033	34.588	0.033	0.033	0.000	0.000	0.000	0.000
124	A	125	PHE	0	-0.058	-0.022	30.994	-0.163	-0.163	0.000	0.000	0.000	0.000
125	A	126	PRO	0	0.039	0.014	36.656	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.030	0.020	39.347	-0.068	-0.068	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.018	-0.005	34.000	-0.137	-0.137	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.071	0.025	34.530	0.064	0.064	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.002	0.008	31.791	-0.029	-0.029	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.006	-0.017	33.714	-0.027	-0.027	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.002	-0.005	36.222	0.115	0.115	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.970	1.002	32.359	9.480	9.480	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.037	-0.026	32.766	0.025	0.025	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.869	0.938	36.855	7.067	7.067	0.000	0.000	0.000	0.000
135	A	136	GLU	-1	-0.886	-0.951	39.988	-7.621	-7.621	0.000	0.000	0.000	0.000
136	A	137	GLN	0	0.056	0.034	34.602	-0.133	-0.133	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.059	-0.038	39.052	0.084	0.084	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.035	-0.024	41.656	0.120	0.120	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.920	-0.947	42.273	-7.273	-7.273	0.000	0.000	0.000	0.000
140	A	141	CYS	0	-0.149	-0.067	41.993	0.021	0.021	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.921	-0.961	44.415	-6.639	-6.639	0.000	0.000	0.000	0.000
142	A	143	GLY	0	-0.016	-0.002	47.321	0.036	0.036	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.963	-0.980	50.215	-5.893	-5.893	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-1.011	-1.004	53.697	-5.587	-5.587	0.000	0.000	0.000	0.000

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