FMO DATABASE

FMODB ID: M37MZ

Calculation Name: 4O2T-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4O2T

Chain ID: A

ChEMBL ID:

UniProt ID: A6LCN0

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	168
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1826258.638072
FMO2-HF: Nuclear repulsion	1757459.815638
FMO2-HF: Total energy	-68798.822434
FMO2-MP2: Total energy	-68997.996902

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
0.105	1.464	0.001	-0.756	-0.604	0.003

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.055 / q_NPA : 0.027

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	25	SER	0	0.010	-0.019	3.868	-0.438	0.921	0.001	-0.756	-0.604	0.003
4	A	26	TYR	0	0.084	0.022	6.466	0.424	0.424	0.000	0.000	0.000	0.000
5	A	27	THR	0	0.028	0.007	8.872	0.200	0.200	0.000	0.000	0.000	0.000
6	A	28	ASP	-1	-0.836	-0.884	7.574	-2.129	-2.129	0.000	0.000	0.000	0.000
7	A	29	MET	0	0.006	0.020	6.204	0.285	0.285	0.000	0.000	0.000	0.000
8	A	30	LEU	0	0.034	0.020	9.640	0.205	0.205	0.000	0.000	0.000	0.000
9	A	31	LYS	1	0.840	0.927	11.302	1.335	1.335	0.000	0.000	0.000	0.000
10	A	32	ASP	-1	-0.856	-0.915	10.291	-0.839	-0.839	0.000	0.000	0.000	0.000
11	A	33	GLU	-1	-0.731	-0.873	13.319	-0.215	-0.215	0.000	0.000	0.000	0.000
12	A	34	LYS	1	0.804	0.885	15.041	0.392	0.392	0.000	0.000	0.000	0.000
13	A	35	LYS	1	0.867	0.930	13.719	0.585	0.585	0.000	0.000	0.000	0.000
14	A	36	ALA	0	-0.005	-0.003	16.304	0.042	0.042	0.000	0.000	0.000	0.000
15	A	37	ILE	0	0.022	0.005	18.309	0.039	0.039	0.000	0.000	0.000	0.000
16	A	38	GLU	-1	-0.799	-0.883	20.901	-0.267	-0.267	0.000	0.000	0.000	0.000
17	A	39	ARG	1	0.953	0.978	19.690	0.172	0.172	0.000	0.000	0.000	0.000
18	A	40	PHE	0	0.021	0.010	22.131	0.026	0.026	0.000	0.000	0.000	0.000
19	A	41	ILE	0	-0.004	-0.004	23.966	0.015	0.015	0.000	0.000	0.000	0.000
20	A	42	ASP	-1	-0.959	-0.971	26.359	-0.118	-0.118	0.000	0.000	0.000	0.000
21	A	43	ASP	-1	-0.962	-0.992	25.775	-0.066	-0.066	0.000	0.000	0.000	0.000
22	A	44	LYS	1	0.831	0.926	25.628	0.070	0.070	0.000	0.000	0.000	0.000
23	A	45	GLY	0	-0.006	0.016	30.181	0.006	0.006	0.000	0.000	0.000	0.000
24	A	46	LEU	0	-0.062	-0.027	27.622	0.006	0.006	0.000	0.000	0.000	0.000
25	A	47	GLU	-1	-0.795	-0.875	31.365	-0.076	-0.076	0.000	0.000	0.000	0.000
26	A	48	ILE	0	-0.022	-0.020	27.967	0.004	0.004	0.000	0.000	0.000	0.000
27	A	49	LEU	0	-0.026	-0.009	31.357	0.001	0.001	0.000	0.000	0.000	0.000
28	A	50	ASP	-1	-0.929	-0.977	32.065	-0.122	-0.122	0.000	0.000	0.000	0.000
29	A	51	ASP	-1	-0.885	-0.928	33.345	-0.076	-0.076	0.000	0.000	0.000	0.000
30	A	52	PHE	0	-0.048	-0.048	33.531	0.002	0.002	0.000	0.000	0.000	0.000
31	A	53	PRO	0	-0.013	0.012	36.659	0.000	0.000	0.000	0.000	0.000	0.000
32	A	54	ALA	0	0.010	-0.010	39.645	0.002	0.002	0.000	0.000	0.000	0.000
33	A	55	ASP	-1	-0.930	-0.972	42.825	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	56	SER	0	-0.061	-0.024	38.597	0.002	0.002	0.000	0.000	0.000	0.000
35	A	57	VAL	0	-0.023	-0.006	39.402	0.003	0.003	0.000	0.000	0.000	0.000
36	A	58	PHE	0	0.006	-0.004	34.204	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	59	LYS	1	0.776	0.870	38.425	0.065	0.065	0.000	0.000	0.000	0.000
38	A	60	GLU	-1	-0.878	-0.938	34.938	-0.040	-0.040	0.000	0.000	0.000	0.000
39	A	61	ASN	0	0.043	0.012	33.720	0.004	0.004	0.000	0.000	0.000	0.000
40	A	62	GLN	0	-0.007	0.005	33.045	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	63	PHE	0	-0.013	-0.018	28.592	0.007	0.007	0.000	0.000	0.000	0.000
42	A	64	VAL	0	0.021	0.040	31.266	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	65	LEU	0	-0.034	-0.018	24.684	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	66	LEU	0	0.007	0.009	27.312	0.002	0.002	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.879	-0.939	26.493	-0.121	-0.121	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.090	-0.062	23.894	-0.021	-0.021	0.000	0.000	0.000	0.000
47	A	69	GLY	0	0.007	0.004	21.909	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	70	VAL	0	-0.048	-0.014	22.536	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	71	TYR	0	0.019	0.014	22.475	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	72	LEU	0	-0.013	-0.023	26.649	0.011	0.011	0.000	0.000	0.000	0.000
51	A	73	ASN	0	0.010	0.013	29.774	0.002	0.002	0.000	0.000	0.000	0.000
52	A	74	ILE	0	0.001	-0.005	32.753	0.006	0.006	0.000	0.000	0.000	0.000
53	A	75	ILE	0	-0.036	-0.012	33.723	0.000	0.000	0.000	0.000	0.000	0.000
54	A	76	ASP	-1	-0.852	-0.928	37.625	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	77	LYS	1	0.918	0.941	38.411	0.017	0.017	0.000	0.000	0.000	0.000
56	A	78	GLY	0	0.061	0.029	40.040	0.000	0.000	0.000	0.000	0.000	0.000
57	A	79	SER	0	-0.041	-0.020	41.520	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	80	ASP	-1	-0.815	-0.898	42.447	-0.018	-0.018	0.000	0.000	0.000	0.000
59	A	81	GLN	0	-0.055	-0.004	41.777	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	82	ARG	1	0.826	0.901	37.894	0.018	0.018	0.000	0.000	0.000	0.000
61	A	83	ALA	0	0.034	0.022	35.168	0.002	0.002	0.000	0.000	0.000	0.000
62	A	84	VAL	0	0.002	0.002	36.628	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	85	GLN	0	0.028	0.015	30.130	0.003	0.003	0.000	0.000	0.000	0.000
64	A	86	TYR	0	-0.078	-0.054	29.533	0.001	0.001	0.000	0.000	0.000	0.000
65	A	87	LYS	1	0.860	0.937	34.165	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	88	THR	0	0.002	0.012	36.447	0.002	0.002	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.818	0.900	35.181	-0.046	-0.046	0.000	0.000	0.000	0.000
68	A	90	MET	0	-0.031	0.001	32.896	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	91	LEU	0	0.008	0.004	33.525	0.008	0.008	0.000	0.000	0.000	0.000
70	A	92	TYR	0	-0.016	-0.034	25.642	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	93	ARG	1	0.852	0.910	32.007	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	94	CYS	0	-0.044	-0.016	27.788	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	95	LYS	1	0.831	0.915	28.376	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	96	MET	0	-0.006	0.000	20.616	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	97	SER	0	0.028	0.010	22.160	0.020	0.020	0.000	0.000	0.000	0.000
76	A	98	TYR	0	-0.047	-0.030	16.007	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	99	PHE	0	-0.005	-0.026	17.955	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	100	MET	0	-0.057	0.006	11.293	-0.049	-0.049	0.000	0.000	0.000	0.000
79	A	101	ASP	-1	-0.868	-0.936	11.739	-0.198	-0.198	0.000	0.000	0.000	0.000
80	A	102	SER	0	-0.055	-0.034	14.724	0.044	0.044	0.000	0.000	0.000	0.000
81	A	103	THR	0	0.016	0.005	17.887	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	104	ILE	0	-0.020	0.000	17.603	0.001	0.001	0.000	0.000	0.000	0.000
83	A	105	VAL	0	0.015	0.010	21.038	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	106	ALA	0	-0.028	-0.015	20.470	0.019	0.019	0.000	0.000	0.000	0.000
85	A	107	ILE	0	-0.017	-0.014	22.456	0.013	0.013	0.000	0.000	0.000	0.000
86	A	108	GLU	-1	-0.839	-0.941	25.756	0.037	0.037	0.000	0.000	0.000	0.000
87	A	109	ASN	0	-0.017	-0.015	29.364	0.000	0.000	0.000	0.000	0.000	0.000
88	A	110	TYR	0	0.035	0.026	31.828	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	111	GLY	0	0.060	0.043	33.471	0.001	0.001	0.000	0.000	0.000	0.000
90	A	112	PRO	0	-0.029	-0.006	36.125	0.004	0.004	0.000	0.000	0.000	0.000
91	A	113	HIS	0	0.010	-0.005	33.343	0.004	0.004	0.000	0.000	0.000	0.000
92	A	114	SER	0	-0.054	0.001	33.753	0.006	0.006	0.000	0.000	0.000	0.000
93	A	115	ASN	0	0.038	0.020	34.916	0.001	0.001	0.000	0.000	0.000	0.000
94	A	116	GLY	0	0.005	0.009	37.178	0.005	0.005	0.000	0.000	0.000	0.000
95	A	117	THR	0	-0.031	-0.025	32.677	0.003	0.003	0.000	0.000	0.000	0.000
96	A	118	SER	0	0.000	0.008	34.202	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	119	PRO	0	-0.006	-0.012	33.186	0.003	0.003	0.000	0.000	0.000	0.000
98	A	120	ILE	0	-0.027	0.005	26.746	0.008	0.008	0.000	0.000	0.000	0.000
99	A	121	ALA	0	-0.001	-0.005	30.721	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	122	PHE	0	-0.044	-0.029	28.803	0.008	0.008	0.000	0.000	0.000	0.000
101	A	123	THR	0	-0.002	-0.007	30.429	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	124	TYR	0	0.007	0.010	30.339	0.001	0.001	0.000	0.000	0.000	0.000
103	A	125	GLY	0	0.017	-0.006	29.079	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	126	ASP	-1	-0.874	-0.912	26.871	0.057	0.057	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.021	-0.015	21.629	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	128	SER	0	-0.008	-0.016	18.749	0.024	0.024	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.849	0.908	19.321	-0.131	-0.131	0.000	0.000	0.000	0.000
108	A	130	ASN	0	0.040	0.011	15.359	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	131	SER	0	-0.010	0.001	16.117	0.075	0.075	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.050	0.027	15.891	-0.037	-0.037	0.000	0.000	0.000	0.000
111	A	133	TYR	0	-0.019	-0.008	17.903	0.002	0.002	0.000	0.000	0.000	0.000
112	A	134	ASP	-1	-0.776	-0.843	21.153	0.124	0.124	0.000	0.000	0.000	0.000
113	A	135	PRO	0	0.043	0.016	21.716	0.011	0.011	0.000	0.000	0.000	0.000
114	A	136	SER	0	0.002	-0.029	22.571	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	137	TYR	0	-0.003	0.031	12.903	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.061	-0.052	17.314	0.021	0.021	0.000	0.000	0.000	0.000
117	A	139	TYR	0	0.003	0.007	19.888	-0.017	-0.017	0.000	0.000	0.000	0.000
118	A	140	VAL	0	0.009	0.022	22.257	-0.015	-0.015	0.000	0.000	0.000	0.000
119	A	141	SER	0	0.019	0.008	20.624	0.007	0.007	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.777	-0.853	21.495	-0.095	-0.095	0.000	0.000	0.000	0.000
121	A	143	GLY	0	0.035	0.002	22.200	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	144	MET	0	-0.040	0.003	23.754	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	145	GLN	0	0.014	-0.014	25.498	0.004	0.004	0.000	0.000	0.000	0.000
124	A	146	GLU	-1	-0.792	-0.868	26.552	-0.063	-0.063	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.043	0.008	28.486	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	148	LEU	0	-0.026	0.001	31.383	0.001	0.001	0.000	0.000	0.000	0.000
127	A	149	LYS	1	0.815	0.903	29.751	0.065	0.065	0.000	0.000	0.000	0.000
128	A	150	TYR	0	-0.013	-0.022	30.743	0.000	0.000	0.000	0.000	0.000	0.000
129	A	151	VAL	0	-0.037	-0.007	34.753	0.001	0.001	0.000	0.000	0.000	0.000
130	A	152	GLY	0	0.019	0.012	37.308	0.001	0.001	0.000	0.000	0.000	0.000
131	A	153	ASP	-1	-0.797	-0.875	38.398	0.015	0.015	0.000	0.000	0.000	0.000
132	A	154	ARG	1	0.810	0.866	39.233	-0.018	-0.018	0.000	0.000	0.000	0.000
133	A	155	ALA	0	0.028	0.048	36.901	0.000	0.000	0.000	0.000	0.000	0.000
134	A	156	LYS	1	0.798	0.886	35.224	0.001	0.001	0.000	0.000	0.000	0.000
135	A	157	VAL	0	0.002	0.002	30.574	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	158	LYS	1	0.860	0.927	29.970	0.045	0.045	0.000	0.000	0.000	0.000
137	A	159	MET	0	-0.051	-0.021	25.870	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	160	ILE	0	0.000	0.012	21.662	0.007	0.007	0.000	0.000	0.000	0.000
139	A	161	VAL	0	-0.009	0.001	19.793	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	162	PRO	0	0.040	0.032	17.191	0.009	0.009	0.000	0.000	0.000	0.000
141	A	163	PHE	0	0.045	0.011	11.146	0.011	0.011	0.000	0.000	0.000	0.000
142	A	164	LYS	1	0.837	0.912	14.842	0.356	0.356	0.000	0.000	0.000	0.000
143	A	165	ARG	1	0.761	0.858	15.910	0.157	0.157	0.000	0.000	0.000	0.000
144	A	166	GLY	0	0.064	0.042	17.248	0.020	0.020	0.000	0.000	0.000	0.000
145	A	167	ALA	0	0.004	0.005	17.949	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	168	TYR	0	0.034	0.000	12.154	-0.036	-0.036	0.000	0.000	0.000	0.000
147	A	169	ASN	0	-0.024	-0.009	13.062	0.109	0.109	0.000	0.000	0.000	0.000
148	A	170	ASP	-1	-0.767	-0.861	12.287	0.179	0.179	0.000	0.000	0.000	0.000
149	A	171	GLN	0	-0.085	-0.055	11.750	-0.039	-0.039	0.000	0.000	0.000	0.000
150	A	172	SER	0	-0.081	-0.049	8.916	-0.098	-0.098	0.000	0.000	0.000	0.000
151	A	173	ASN	0	-0.081	-0.045	7.277	0.403	0.403	0.000	0.000	0.000	0.000
152	A	174	GLY	0	0.000	-0.005	8.779	-0.131	-0.131	0.000	0.000	0.000	0.000
153	A	175	GLN	0	-0.089	-0.054	9.971	-0.049	-0.049	0.000	0.000	0.000	0.000
154	A	176	PRO	0	0.009	0.013	13.212	0.022	0.022	0.000	0.000	0.000	0.000
155	A	177	VAL	0	-0.030	-0.014	16.638	0.030	0.030	0.000	0.000	0.000	0.000
156	A	178	TYR	0	0.029	0.007	19.582	-0.022	-0.022	0.000	0.000	0.000	0.000
157	A	179	TYR	0	0.012	-0.008	23.166	0.017	0.017	0.000	0.000	0.000	0.000
158	A	180	GLU	-1	-0.816	-0.908	26.338	0.000	0.000	0.000	0.000	0.000	0.000
159	A	181	ILE	0	-0.010	-0.009	29.067	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	182	LEU	0	-0.040	-0.008	28.053	0.009	0.009	0.000	0.000	0.000	0.000
161	A	183	GLU	-1	-0.897	-0.954	31.415	0.010	0.010	0.000	0.000	0.000	0.000
162	A	184	TYR	0	-0.012	-0.030	29.437	0.005	0.005	0.000	0.000	0.000	0.000
163	A	185	ILE	0	-0.027	-0.021	35.049	-0.002	-0.002	0.000	0.000	0.000	0.000
164	A	186	PHE	0	0.073	0.014	36.902	0.003	0.003	0.000	0.000	0.000	0.000
165	A	187	GLU	-1	-0.839	-0.911	36.984	0.046	0.046	0.000	0.000	0.000	0.000
166	A	188	GLU	-1	-0.872	-0.934	39.645	0.013	0.013	0.000	0.000	0.000	0.000
167	A	189	ASN	0	-0.068	-0.046	42.319	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	190	LEU	0	-0.033	-0.005	40.185	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:0:GLY)