FMO DATABASE

FMODB ID: G5LY1

Calculation Name: 2A4D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2A4D

Chain ID: A

ChEMBL ID:

UniProt ID: Q13404

Base Structure: X-ray

Registration Date: 2023-09-20

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	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. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1288817.569969
FMO2-HF: Nuclear repulsion	1232620.53865
FMO2-HF: Total energy	-56197.031319
FMO2-MP2: Total energy	-56357.650672

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:82:GLY)

Summations of interaction energy for fragment #1(A:82: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.
1.916	3.009	-0.008	-0.477	-0.608	0.002

Interaction energy analysis for fragmet #1(A:82:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.009 / q_NPA : -0.005

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	84	LYS	1	0.947	0.974	3.796	2.048	3.141	-0.008	-0.477	-0.608	0.002
4	A	85	VAL	0	0.059	0.020	5.868	-0.150	-0.150	0.000	0.000	0.000	0.000
5	A	86	PRO	0	0.026	0.017	9.247	-0.065	-0.065	0.000	0.000	0.000	0.000
6	A	87	ARG	1	0.798	0.902	7.547	1.225	1.225	0.000	0.000	0.000	0.000
7	A	88	ASN	0	0.026	-0.005	7.067	-0.119	-0.119	0.000	0.000	0.000	0.000
8	A	89	PHE	0	0.030	0.015	10.448	0.071	0.071	0.000	0.000	0.000	0.000
9	A	90	ARG	1	0.822	0.918	13.663	0.263	0.263	0.000	0.000	0.000	0.000
10	A	91	LEU	0	-0.036	-0.026	10.954	0.029	0.029	0.000	0.000	0.000	0.000
11	A	92	LEU	0	0.025	0.006	13.158	0.033	0.033	0.000	0.000	0.000	0.000
12	A	93	GLU	-1	-0.868	-0.926	15.939	-0.140	-0.140	0.000	0.000	0.000	0.000
13	A	94	GLU	-1	-0.761	-0.859	17.768	-0.274	-0.274	0.000	0.000	0.000	0.000
14	A	95	LEU	0	-0.012	0.009	16.735	0.018	0.018	0.000	0.000	0.000	0.000
15	A	96	GLU	-1	-0.931	-0.966	19.305	-0.111	-0.111	0.000	0.000	0.000	0.000
16	A	97	GLU	-1	-0.861	-0.923	21.897	-0.129	-0.129	0.000	0.000	0.000	0.000
17	A	98	GLY	0	-0.032	-0.015	22.656	0.014	0.014	0.000	0.000	0.000	0.000
18	A	99	GLN	0	-0.019	-0.004	21.498	0.019	0.019	0.000	0.000	0.000	0.000
19	A	100	LYS	1	0.897	0.963	25.447	0.108	0.108	0.000	0.000	0.000	0.000
20	A	101	GLY	0	-0.001	0.005	28.425	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	102	VAL	0	0.062	0.020	26.862	0.001	0.001	0.000	0.000	0.000	0.000
22	A	103	GLY	0	-0.035	-0.017	29.950	0.002	0.002	0.000	0.000	0.000	0.000
23	A	104	ASP	-1	-0.864	-0.923	31.945	-0.083	-0.083	0.000	0.000	0.000	0.000
24	A	105	GLY	0	-0.001	0.006	32.844	0.005	0.005	0.000	0.000	0.000	0.000
25	A	106	THR	0	-0.099	-0.071	33.476	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	107	VAL	0	-0.020	-0.014	28.369	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	108	SER	0	-0.020	-0.004	27.179	0.006	0.006	0.000	0.000	0.000	0.000
28	A	109	TRP	0	-0.029	-0.041	20.847	0.007	0.007	0.000	0.000	0.000	0.000
29	A	110	GLY	0	0.055	0.033	21.036	0.012	0.012	0.000	0.000	0.000	0.000
30	A	111	LEU	0	0.031	0.016	15.020	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	112	GLU	-1	-0.863	-0.908	17.868	-0.245	-0.245	0.000	0.000	0.000	0.000
32	A	113	ASP	-1	-0.814	-0.905	16.519	-0.278	-0.278	0.000	0.000	0.000	0.000
33	A	114	ASP	-1	-0.922	-0.965	16.575	-0.262	-0.262	0.000	0.000	0.000	0.000
34	A	115	GLU	-1	-0.927	-0.948	15.990	-0.203	-0.203	0.000	0.000	0.000	0.000
35	A	116	ASP	-1	-0.811	-0.878	11.018	-0.761	-0.761	0.000	0.000	0.000	0.000
36	A	117	MET	0	-0.006	-0.015	9.994	-0.041	-0.041	0.000	0.000	0.000	0.000
37	A	118	THR	0	-0.144	-0.081	6.712	-0.192	-0.192	0.000	0.000	0.000	0.000
38	A	119	LEU	0	0.019	0.017	8.489	-0.126	-0.126	0.000	0.000	0.000	0.000
39	A	120	THR	0	-0.041	-0.030	9.354	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	121	ARG	1	0.820	0.893	11.918	0.449	0.449	0.000	0.000	0.000	0.000
41	A	122	TRP	0	-0.015	-0.004	14.280	0.053	0.053	0.000	0.000	0.000	0.000
42	A	123	THR	0	-0.006	-0.009	18.389	0.019	0.019	0.000	0.000	0.000	0.000
43	A	124	GLY	0	-0.014	-0.009	22.127	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	125	MET	0	0.005	-0.012	24.529	0.009	0.009	0.000	0.000	0.000	0.000
45	A	126	ILE	0	-0.021	-0.016	28.241	0.000	0.000	0.000	0.000	0.000	0.000
46	A	127	ILE	0	0.030	0.018	31.205	0.003	0.003	0.000	0.000	0.000	0.000
47	A	128	GLY	0	0.042	0.023	34.732	0.001	0.001	0.000	0.000	0.000	0.000
48	A	129	PRO	0	-0.046	-0.043	36.360	0.004	0.004	0.000	0.000	0.000	0.000
49	A	130	PRO	0	0.062	0.029	39.180	0.002	0.002	0.000	0.000	0.000	0.000
50	A	131	ARG	1	0.836	0.907	42.858	0.049	0.049	0.000	0.000	0.000	0.000
51	A	132	THR	0	-0.044	-0.026	40.750	0.000	0.000	0.000	0.000	0.000	0.000
52	A	133	ILE	0	-0.027	-0.014	41.068	0.001	0.001	0.000	0.000	0.000	0.000
53	A	134	TYR	0	-0.017	-0.033	37.331	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	135	GLU	-1	-0.881	-0.915	39.331	-0.059	-0.059	0.000	0.000	0.000	0.000
55	A	136	ASN	0	-0.044	-0.033	41.026	0.000	0.000	0.000	0.000	0.000	0.000
56	A	137	ARG	1	0.887	0.976	37.450	0.074	0.074	0.000	0.000	0.000	0.000
57	A	138	ILE	0	-0.003	-0.006	32.141	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	139	TYR	0	-0.018	-0.013	31.265	0.002	0.002	0.000	0.000	0.000	0.000
59	A	140	SER	0	0.050	0.025	27.326	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	141	LEU	0	-0.037	-0.022	24.805	0.005	0.005	0.000	0.000	0.000	0.000
61	A	142	LYS	1	0.873	0.929	20.498	0.217	0.217	0.000	0.000	0.000	0.000
62	A	143	ILE	0	-0.014	-0.015	18.295	0.013	0.013	0.000	0.000	0.000	0.000
63	A	144	GLU	-1	-0.928	-0.955	14.841	-0.394	-0.394	0.000	0.000	0.000	0.000
64	A	145	CYS	0	-0.001	0.009	13.427	0.047	0.047	0.000	0.000	0.000	0.000
65	A	146	GLY	0	0.096	0.044	10.905	-0.115	-0.115	0.000	0.000	0.000	0.000
66	A	147	PRO	0	0.008	-0.019	6.469	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.933	0.953	7.937	0.364	0.364	0.000	0.000	0.000	0.000
68	A	149	TYR	0	-0.043	0.005	10.495	0.122	0.122	0.000	0.000	0.000	0.000
69	A	150	PRO	0	0.020	0.001	11.306	-0.100	-0.100	0.000	0.000	0.000	0.000
70	A	151	GLU	-1	-0.811	-0.914	13.083	-0.136	-0.136	0.000	0.000	0.000	0.000
71	A	152	ALA	0	-0.081	-0.034	14.097	0.039	0.039	0.000	0.000	0.000	0.000
72	A	153	PRO	0	0.003	0.002	15.863	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	154	PRO	0	-0.012	0.001	16.717	-0.026	-0.026	0.000	0.000	0.000	0.000
74	A	155	PHE	0	-0.018	-0.001	17.380	0.048	0.048	0.000	0.000	0.000	0.000
75	A	156	VAL	0	0.037	0.012	19.209	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	157	ARG	1	0.886	0.941	22.231	0.193	0.193	0.000	0.000	0.000	0.000
77	A	158	PHE	0	0.058	0.017	24.676	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	159	VAL	0	-0.031	-0.013	25.462	0.000	0.000	0.000	0.000	0.000	0.000
79	A	160	THR	0	0.028	0.020	27.976	0.005	0.005	0.000	0.000	0.000	0.000
80	A	161	LYS	1	0.891	0.945	31.572	0.090	0.090	0.000	0.000	0.000	0.000
81	A	162	ILE	0	0.003	0.004	32.218	0.004	0.004	0.000	0.000	0.000	0.000
82	A	163	ASN	0	-0.069	-0.023	35.100	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	164	MET	0	0.024	0.009	32.555	0.001	0.001	0.000	0.000	0.000	0.000
84	A	165	ASN	0	0.000	0.000	34.820	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	166	GLY	0	0.036	0.009	32.221	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	167	VAL	0	-0.025	-0.001	29.630	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	168	ASN	0	-0.001	0.020	30.142	0.010	0.010	0.000	0.000	0.000	0.000
88	A	169	SER	0	0.058	0.020	31.882	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	170	SER	0	-0.045	-0.027	32.848	0.001	0.001	0.000	0.000	0.000	0.000
90	A	171	ASN	0	0.009	-0.019	28.254	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	172	GLY	0	0.089	0.055	27.962	-0.010	-0.010	0.000	0.000	0.000	0.000
92	A	173	VAL	0	-0.033	-0.011	24.521	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	174	VAL	0	-0.002	0.003	25.567	0.014	0.014	0.000	0.000	0.000	0.000
94	A	175	ASP	-1	-0.815	-0.882	25.627	-0.125	-0.125	0.000	0.000	0.000	0.000
95	A	176	PRO	0	0.059	0.012	23.318	0.007	0.007	0.000	0.000	0.000	0.000
96	A	177	ARG	1	0.829	0.873	25.764	0.107	0.107	0.000	0.000	0.000	0.000
97	A	178	ALA	0	-0.028	-0.003	28.646	0.008	0.008	0.000	0.000	0.000	0.000
98	A	179	ILE	0	0.009	0.021	27.526	0.005	0.005	0.000	0.000	0.000	0.000
99	A	180	SER	0	0.011	0.014	27.897	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	181	VAL	0	0.021	0.003	25.638	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	182	LEU	0	-0.001	-0.001	22.279	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	183	ALA	0	-0.011	0.000	23.625	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	184	LYS	1	0.866	0.924	25.505	0.091	0.091	0.000	0.000	0.000	0.000
104	A	185	TRP	0	0.011	0.001	17.865	0.009	0.009	0.000	0.000	0.000	0.000
105	A	186	GLN	0	-0.043	-0.019	22.195	0.022	0.022	0.000	0.000	0.000	0.000
106	A	187	ASN	0	-0.016	-0.018	17.507	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	188	SER	0	-0.004	-0.001	19.033	-0.016	-0.016	0.000	0.000	0.000	0.000
108	A	189	TYR	0	-0.068	-0.025	21.443	0.009	0.009	0.000	0.000	0.000	0.000
109	A	190	SER	0	0.061	0.020	19.959	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	191	ILE	0	0.046	0.015	17.397	0.019	0.019	0.000	0.000	0.000	0.000
111	A	192	LYS	1	0.795	0.901	21.475	0.158	0.158	0.000	0.000	0.000	0.000
112	A	193	VAL	0	0.010	0.006	24.424	0.012	0.012	0.000	0.000	0.000	0.000
113	A	194	VAL	0	-0.003	0.003	22.315	0.012	0.012	0.000	0.000	0.000	0.000
114	A	195	LEU	0	-0.003	0.007	24.374	0.011	0.011	0.000	0.000	0.000	0.000
115	A	196	GLN	0	0.018	-0.001	27.257	0.008	0.008	0.000	0.000	0.000	0.000
116	A	197	GLU	-1	-0.782	-0.858	28.754	-0.085	-0.085	0.000	0.000	0.000	0.000
117	A	198	LEU	0	-0.013	-0.013	26.864	0.008	0.008	0.000	0.000	0.000	0.000
118	A	199	ARG	1	0.924	0.960	30.802	0.095	0.095	0.000	0.000	0.000	0.000
119	A	200	ARG	1	0.803	0.865	33.248	0.091	0.091	0.000	0.000	0.000	0.000
120	A	201	LEU	0	-0.010	-0.008	31.826	0.007	0.007	0.000	0.000	0.000	0.000
121	A	202	MET	0	-0.005	0.029	32.200	0.006	0.006	0.000	0.000	0.000	0.000
122	A	203	MET	0	0.006	0.004	36.768	0.006	0.006	0.000	0.000	0.000	0.000
123	A	204	SER	0	-0.077	-0.027	38.350	0.006	0.006	0.000	0.000	0.000	0.000
124	A	205	LYS	1	0.974	0.949	40.498	0.048	0.048	0.000	0.000	0.000	0.000
125	A	206	GLU	-1	-0.923	-0.960	38.633	-0.068	-0.068	0.000	0.000	0.000	0.000
126	A	207	ASN	0	0.058	0.022	37.321	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	208	MET	0	-0.005	0.020	40.224	0.001	0.001	0.000	0.000	0.000	0.000
128	A	209	LYS	1	0.939	0.957	42.201	0.050	0.050	0.000	0.000	0.000	0.000
129	A	210	LEU	0	0.000	0.033	39.294	0.003	0.003	0.000	0.000	0.000	0.000
130	A	211	PRO	0	0.060	0.025	42.502	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	212	GLN	0	0.012	-0.003	38.291	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	213	PRO	0	-0.026	0.010	37.210	0.004	0.004	0.000	0.000	0.000	0.000
133	A	214	PRO	0	0.046	0.000	40.370	0.000	0.000	0.000	0.000	0.000	0.000
134	A	215	GLU	-1	-0.842	-0.918	38.642	-0.080	-0.080	0.000	0.000	0.000	0.000
135	A	216	GLY	0	0.012	0.006	36.378	0.002	0.002	0.000	0.000	0.000	0.000
136	A	217	GLN	0	-0.037	-0.001	35.888	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	218	CYS	0	0.015	0.005	30.302	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	219	TYR	0	-0.086	-0.036	28.591	0.006	0.006	0.000	0.000	0.000	0.000
139	A	220	SER	0	0.000	0.001	25.068	-0.009	-0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:82:GLY)