FMO DATABASE

FMODB ID: 82LNY

Calculation Name: 4L9H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4L9H

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y3I1

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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1501447.679359
FMO2-HF: Nuclear repulsion	1440623.916638
FMO2-HF: Total energy	-60823.762721
FMO2-MP2: Total energy	-60999.628857

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:176:GLY)

Summations of interaction energy for fragment #1(A:176: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.
1.329	2.572	-0.004	-0.613	-0.626	0.003

Interaction energy analysis for fragmet #1(A:176:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.059 / q_NPA : 0.031

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	178	SER	0	0.021	0.005	3.871	0.472	1.715	-0.004	-0.613	-0.626	0.003
4	A	179	SER	0	0.009	0.010	6.256	0.515	0.515	0.000	0.000	0.000	0.000
5	A	180	PRO	0	0.001	0.000	8.854	0.005	0.005	0.000	0.000	0.000	0.000
6	A	181	HIS	0	0.058	0.013	11.111	0.145	0.145	0.000	0.000	0.000	0.000
7	A	182	SER	0	0.007	-0.006	14.564	0.062	0.062	0.000	0.000	0.000	0.000
8	A	183	LEU	0	-0.044	-0.006	13.915	0.054	0.054	0.000	0.000	0.000	0.000
9	A	184	GLU	-1	-0.901	-0.949	15.016	-0.310	-0.310	0.000	0.000	0.000	0.000
10	A	185	THR	0	-0.021	-0.012	16.992	0.046	0.046	0.000	0.000	0.000	0.000
11	A	186	LEU	0	-0.010	-0.004	19.914	0.043	0.043	0.000	0.000	0.000	0.000
12	A	187	TYR	0	0.045	0.008	19.388	0.032	0.032	0.000	0.000	0.000	0.000
13	A	188	GLN	0	-0.018	-0.011	20.846	0.036	0.036	0.000	0.000	0.000	0.000
14	A	189	SER	0	-0.026	-0.013	22.879	0.020	0.020	0.000	0.000	0.000	0.000
15	A	190	ALA	0	-0.060	-0.027	24.572	0.014	0.014	0.000	0.000	0.000	0.000
16	A	191	ASP	-1	-0.934	-0.958	26.159	-0.098	-0.098	0.000	0.000	0.000	0.000
17	A	192	CYS	0	-0.092	-0.054	22.664	0.006	0.006	0.000	0.000	0.000	0.000
18	A	193	SER	0	0.031	0.022	26.148	0.010	0.010	0.000	0.000	0.000	0.000
19	A	194	ASP	-1	-0.830	-0.908	27.636	-0.076	-0.076	0.000	0.000	0.000	0.000
20	A	195	ALA	0	0.040	0.004	24.428	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	196	ASN	0	-0.067	-0.047	24.788	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	197	ASP	-1	-0.721	-0.819	26.352	-0.129	-0.129	0.000	0.000	0.000	0.000
23	A	198	ALA	0	0.050	0.036	21.192	-0.021	-0.021	0.000	0.000	0.000	0.000
24	A	199	LEU	0	-0.013	0.005	21.429	-0.031	-0.031	0.000	0.000	0.000	0.000
25	A	200	ILE	0	-0.008	-0.013	22.775	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	201	VAL	0	0.054	0.023	20.197	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	202	LEU	0	-0.015	0.004	16.585	-0.033	-0.033	0.000	0.000	0.000	0.000
28	A	203	ILE	0	-0.046	-0.025	20.045	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	204	HIS	0	0.063	0.037	22.928	0.000	0.000	0.000	0.000	0.000	0.000
30	A	205	LEU	0	0.023	0.015	15.960	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	206	LEU	0	-0.022	-0.012	17.131	-0.021	-0.021	0.000	0.000	0.000	0.000
32	A	207	MET	0	-0.011	0.015	20.224	0.002	0.002	0.000	0.000	0.000	0.000
33	A	208	LEU	0	-0.038	-0.011	21.445	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	209	GLU	-1	-0.843	-0.915	15.837	-0.622	-0.622	0.000	0.000	0.000	0.000
35	A	210	SER	0	-0.075	-0.040	19.752	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	211	GLY	0	0.015	0.014	22.400	0.030	0.030	0.000	0.000	0.000	0.000
37	A	212	TYR	0	-0.010	-0.004	24.557	0.019	0.019	0.000	0.000	0.000	0.000
38	A	213	ILE	0	0.011	0.004	25.974	-0.027	-0.027	0.000	0.000	0.000	0.000
39	A	214	PRO	0	-0.001	-0.002	27.057	0.014	0.014	0.000	0.000	0.000	0.000
40	A	215	GLN	0	0.020	-0.007	29.807	0.002	0.002	0.000	0.000	0.000	0.000
41	A	216	GLY	0	0.002	-0.015	32.015	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	217	THR	0	-0.029	-0.007	28.246	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	218	GLU	-1	-0.833	-0.909	29.918	-0.202	-0.202	0.000	0.000	0.000	0.000
44	A	219	ALA	0	0.009	0.014	26.346	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	220	LYS	1	0.848	0.910	23.097	0.331	0.331	0.000	0.000	0.000	0.000
46	A	221	ALA	0	-0.016	-0.002	20.599	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	222	LEU	0	-0.027	-0.022	20.774	-0.042	-0.042	0.000	0.000	0.000	0.000
48	A	223	SER	0	0.087	0.032	23.207	0.001	0.001	0.000	0.000	0.000	0.000
49	A	224	MET	0	-0.019	-0.002	24.992	-0.020	-0.020	0.000	0.000	0.000	0.000
50	A	225	PRO	0	-0.055	-0.029	27.143	0.008	0.008	0.000	0.000	0.000	0.000
51	A	226	GLU	-1	-0.819	-0.923	30.394	-0.121	-0.121	0.000	0.000	0.000	0.000
52	A	227	LYS	1	0.829	0.909	33.604	0.100	0.100	0.000	0.000	0.000	0.000
53	A	228	TRP	0	0.019	0.017	27.509	0.003	0.003	0.000	0.000	0.000	0.000
54	A	229	LYS	1	0.889	0.937	30.264	0.108	0.108	0.000	0.000	0.000	0.000
55	A	230	LEU	0	-0.029	-0.023	33.059	0.004	0.004	0.000	0.000	0.000	0.000
56	A	231	SER	0	-0.019	-0.019	36.796	0.000	0.000	0.000	0.000	0.000	0.000
57	A	232	GLY	0	0.027	0.032	36.543	0.004	0.004	0.000	0.000	0.000	0.000
58	A	233	VAL	0	-0.057	-0.026	34.734	0.001	0.001	0.000	0.000	0.000	0.000
59	A	234	TYR	0	-0.007	-0.026	29.715	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	235	LYS	1	0.848	0.920	32.797	0.121	0.121	0.000	0.000	0.000	0.000
61	A	236	LEU	0	0.041	0.045	26.988	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	237	GLN	0	-0.010	-0.023	31.085	0.011	0.011	0.000	0.000	0.000	0.000
63	A	238	TYR	0	0.007	-0.009	26.308	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	239	MET	0	0.035	0.027	31.439	0.018	0.018	0.000	0.000	0.000	0.000
65	A	240	HIS	0	0.038	-0.006	26.269	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	241	PRO	0	0.030	0.027	28.306	0.014	0.014	0.000	0.000	0.000	0.000
67	A	242	LEU	0	-0.011	0.007	28.013	0.007	0.007	0.000	0.000	0.000	0.000
68	A	243	CYS	0	-0.056	-0.027	31.970	0.009	0.009	0.000	0.000	0.000	0.000
69	A	244	GLU	-1	-0.867	-0.917	34.460	-0.135	-0.135	0.000	0.000	0.000	0.000
70	A	245	GLY	0	0.027	0.018	37.008	0.005	0.005	0.000	0.000	0.000	0.000
71	A	246	SER	0	-0.082	-0.054	36.105	0.005	0.005	0.000	0.000	0.000	0.000
72	A	247	SER	0	-0.018	-0.011	35.332	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	248	ALA	0	0.029	0.028	31.900	0.008	0.008	0.000	0.000	0.000	0.000
74	A	249	THR	0	-0.057	-0.041	33.218	0.000	0.000	0.000	0.000	0.000	0.000
75	A	250	LEU	0	0.015	0.019	27.553	0.004	0.004	0.000	0.000	0.000	0.000
76	A	251	THR	0	0.026	0.010	31.888	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	252	CYS	0	-0.046	-0.018	30.250	0.000	0.000	0.000	0.000	0.000	0.000
78	A	253	VAL	0	0.041	0.012	32.423	0.001	0.001	0.000	0.000	0.000	0.000
79	A	254	PRO	0	0.040	0.020	32.239	0.001	0.001	0.000	0.000	0.000	0.000
80	A	255	LEU	0	-0.019	-0.008	33.873	0.004	0.004	0.000	0.000	0.000	0.000
81	A	256	GLY	0	0.013	0.012	34.911	0.002	0.002	0.000	0.000	0.000	0.000
82	A	257	ASN	0	-0.030	-0.025	30.957	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	258	LEU	0	-0.030	-0.014	30.200	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	259	ILE	0	0.028	0.017	27.775	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	260	VAL	0	-0.046	-0.017	30.367	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	261	VAL	0	0.035	0.006	27.570	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	262	ASN	0	-0.034	-0.037	31.004	0.006	0.006	0.000	0.000	0.000	0.000
88	A	263	ALA	0	0.030	0.018	31.267	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	264	THR	0	-0.038	-0.024	33.139	0.012	0.012	0.000	0.000	0.000	0.000
90	A	265	LEU	0	-0.002	0.001	35.093	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	266	LYS	1	0.890	0.967	37.346	0.105	0.105	0.000	0.000	0.000	0.000
92	A	267	ILE	0	0.092	0.034	38.972	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	268	ASN	0	0.016	0.009	42.016	0.003	0.003	0.000	0.000	0.000	0.000
94	A	269	ASN	0	-0.044	-0.038	44.563	0.001	0.001	0.000	0.000	0.000	0.000
95	A	270	GLU	-1	-0.756	-0.811	44.733	-0.079	-0.079	0.000	0.000	0.000	0.000
96	A	271	ILE	0	-0.038	-0.040	41.352	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	272	ARG	1	0.852	0.890	40.079	0.093	0.093	0.000	0.000	0.000	0.000
98	A	273	SER	0	-0.012	-0.003	38.237	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	274	VAL	0	-0.020	-0.002	33.906	0.001	0.001	0.000	0.000	0.000	0.000
100	A	275	LYS	1	0.843	0.906	30.196	0.112	0.112	0.000	0.000	0.000	0.000
101	A	276	ARG	1	0.926	0.972	33.580	0.065	0.065	0.000	0.000	0.000	0.000
102	A	277	LEU	0	-0.014	-0.016	26.221	0.004	0.004	0.000	0.000	0.000	0.000
103	A	278	GLN	0	0.020	0.027	30.459	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	279	LEU	0	0.001	0.005	24.570	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	280	LEU	0	0.049	0.024	26.088	0.005	0.005	0.000	0.000	0.000	0.000
106	A	281	PRO	0	0.030	0.018	24.142	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	282	GLU	-1	-0.783	-0.892	23.024	-0.025	-0.025	0.000	0.000	0.000	0.000
108	A	283	SER	0	-0.027	-0.010	22.496	0.019	0.019	0.000	0.000	0.000	0.000
109	A	284	PHE	0	-0.062	-0.037	18.661	0.006	0.006	0.000	0.000	0.000	0.000
110	A	285	ILE	0	-0.009	0.019	18.323	-0.024	-0.024	0.000	0.000	0.000	0.000
111	A	286	CYS	0	-0.040	-0.012	17.147	0.027	0.027	0.000	0.000	0.000	0.000
112	A	287	LYS	1	0.908	0.961	20.616	0.011	0.011	0.000	0.000	0.000	0.000
113	A	288	GLU	-1	-0.873	-0.958	24.139	0.001	0.001	0.000	0.000	0.000	0.000
114	A	289	LYS	1	0.758	0.856	17.205	-0.062	-0.062	0.000	0.000	0.000	0.000
115	A	290	LEU	0	-0.015	-0.013	20.365	-0.016	-0.016	0.000	0.000	0.000	0.000
116	A	291	GLY	0	-0.002	0.014	22.578	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	292	GLU	-1	-0.818	-0.882	18.026	0.067	0.067	0.000	0.000	0.000	0.000
118	A	293	ASN	0	0.029	0.005	14.603	-0.046	-0.046	0.000	0.000	0.000	0.000
119	A	294	VAL	0	0.098	0.047	13.662	0.024	0.024	0.000	0.000	0.000	0.000
120	A	295	ALA	0	-0.061	-0.040	10.365	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	296	ASN	0	-0.075	-0.033	12.108	0.074	0.074	0.000	0.000	0.000	0.000
122	A	297	ILE	0	0.041	0.047	15.080	0.025	0.025	0.000	0.000	0.000	0.000
123	A	298	TYR	0	-0.030	-0.034	14.491	0.003	0.003	0.000	0.000	0.000	0.000
124	A	299	LYS	1	0.870	0.914	14.136	0.031	0.031	0.000	0.000	0.000	0.000
125	A	300	ASP	-1	-0.873	-0.950	14.400	-0.015	-0.015	0.000	0.000	0.000	0.000
126	A	301	LEU	0	0.082	0.045	11.447	-0.016	-0.016	0.000	0.000	0.000	0.000
127	A	302	GLN	0	0.047	0.031	10.270	0.087	0.087	0.000	0.000	0.000	0.000
128	A	303	LYS	1	0.902	0.959	13.855	0.003	0.003	0.000	0.000	0.000	0.000
129	A	304	LEU	0	0.041	0.031	17.280	0.005	0.005	0.000	0.000	0.000	0.000
130	A	305	SER	0	-0.014	-0.028	15.430	-0.023	-0.023	0.000	0.000	0.000	0.000
131	A	306	ARG	1	0.895	0.952	14.095	0.239	0.239	0.000	0.000	0.000	0.000
132	A	307	LEU	0	-0.001	0.010	19.221	0.010	0.010	0.000	0.000	0.000	0.000
133	A	308	PHE	0	0.043	0.002	21.656	0.017	0.017	0.000	0.000	0.000	0.000
134	A	309	LYS	1	0.866	0.932	17.206	0.481	0.481	0.000	0.000	0.000	0.000
135	A	310	ASP	-1	-0.859	-0.938	21.679	-0.197	-0.197	0.000	0.000	0.000	0.000
136	A	311	GLN	0	-0.015	-0.005	24.261	0.020	0.020	0.000	0.000	0.000	0.000
137	A	312	LEU	0	-0.028	0.000	26.282	0.016	0.016	0.000	0.000	0.000	0.000
138	A	313	VAL	0	0.026	0.017	23.774	0.006	0.006	0.000	0.000	0.000	0.000
139	A	314	TYR	0	0.023	0.006	20.506	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	315	PRO	0	0.009	0.005	26.852	0.008	0.008	0.000	0.000	0.000	0.000
141	A	316	LEU	0	0.001	0.011	29.577	0.009	0.009	0.000	0.000	0.000	0.000
142	A	317	LEU	0	-0.005	0.013	26.229	0.007	0.007	0.000	0.000	0.000	0.000
143	A	318	ALA	0	0.025	0.015	30.489	0.006	0.006	0.000	0.000	0.000	0.000
144	A	319	PHE	0	0.019	0.003	32.475	0.008	0.008	0.000	0.000	0.000	0.000
145	A	320	THR	0	-0.033	-0.052	33.489	0.007	0.007	0.000	0.000	0.000	0.000
146	A	321	ARG	1	0.834	0.897	32.507	0.162	0.162	0.000	0.000	0.000	0.000
147	A	322	GLN	0	-0.004	0.001	35.643	0.010	0.010	0.000	0.000	0.000	0.000
148	A	323	ALA	0	-0.048	-0.016	38.300	0.007	0.007	0.000	0.000	0.000	0.000
149	A	324	LEU	0	-0.065	-0.032	36.587	0.005	0.005	0.000	0.000	0.000	0.000
150	A	325	ASN	0	-0.084	-0.033	40.228	0.005	0.005	0.000	0.000	0.000	0.000
151	A	326	LEU	0	-0.015	-0.002	36.586	0.000	0.000	0.000	0.000	0.000	0.000
152	A	327	PRO	0	0.020	0.002	35.448	0.000	0.000	0.000	0.000	0.000	0.000
153	A	328	ASP	-1	-0.843	-0.913	32.252	-0.132	-0.132	0.000	0.000	0.000	0.000
154	A	329	VAL	0	-0.039	-0.022	27.123	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	330	PHE	0	-0.010	0.008	24.340	-0.014	-0.014	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:176:GLY)