FMO DATABASE

FMODB ID: 1485Z

Calculation Name: 1L3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1L3A

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LL85

Base Structure: X-ray

Registration Date: 2023-06-19

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	166
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1537740.370183
FMO2-HF: Nuclear repulsion	1473550.470482
FMO2-HF: Total energy	-64189.899702
FMO2-MP2: Total energy	-64379.099392

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:89:THR)

Summations of interaction energy for fragment #1(A:89:THR)

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.
-0.321	2.043	0.023	-1.2	-1.185	0.003

Interaction energy analysis for fragmet #1(A:89:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.020

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	91	LYS	1	0.891	0.940	3.375	-0.495	1.756	0.024	-1.195	-1.079	0.003
4	A	92	VAL	0	0.033	0.022	4.579	0.071	0.184	-0.001	-0.005	-0.106	0.000
5	A	93	PHE	0	-0.012	-0.013	7.052	0.282	0.282	0.000	0.000	0.000	0.000
6	A	94	VAL	0	0.026	0.010	9.712	-0.005	-0.005	0.000	0.000	0.000	0.000
7	A	95	GLY	0	0.048	0.010	12.335	0.026	0.026	0.000	0.000	0.000	0.000
8	A	96	TYR	0	-0.022	0.012	15.785	-0.017	-0.017	0.000	0.000	0.000	0.000
9	A	97	SER	0	0.002	-0.028	18.865	-0.010	-0.010	0.000	0.000	0.000	0.000
10	A	98	ILE	0	-0.029	0.001	22.074	0.003	0.003	0.000	0.000	0.000	0.000
11	A	99	TYR	0	0.034	0.010	22.060	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	100	LYS	1	0.788	0.873	28.439	-0.050	-0.050	0.000	0.000	0.000	0.000
13	A	101	GLY	0	-0.021	-0.004	32.189	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	102	LYS	1	0.956	0.980	35.180	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	103	ALA	0	0.017	0.013	31.062	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	104	ALA	0	-0.006	0.005	26.515	0.004	0.004	0.000	0.000	0.000	0.000
17	A	105	LEU	0	-0.012	-0.007	24.399	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	106	THR	0	0.002	0.017	19.000	0.004	0.004	0.000	0.000	0.000	0.000
19	A	107	VAL	0	0.015	0.015	19.305	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	108	GLU	-1	-0.827	-0.899	15.367	0.046	0.046	0.000	0.000	0.000	0.000
21	A	109	PRO	0	-0.020	0.007	12.046	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	110	ARG	1	0.849	0.900	13.176	-0.179	-0.179	0.000	0.000	0.000	0.000
23	A	111	SER	0	0.015	-0.017	10.447	0.096	0.096	0.000	0.000	0.000	0.000
24	A	112	PRO	0	0.016	0.011	11.839	-0.103	-0.103	0.000	0.000	0.000	0.000
25	A	113	GLU	-1	-0.830	-0.843	13.286	0.088	0.088	0.000	0.000	0.000	0.000
26	A	114	PHE	0	0.062	0.011	12.085	0.034	0.034	0.000	0.000	0.000	0.000
27	A	115	SER	0	0.005	0.015	15.900	-0.049	-0.049	0.000	0.000	0.000	0.000
28	A	116	PRO	0	0.041	0.019	17.455	0.033	0.033	0.000	0.000	0.000	0.000
29	A	117	LEU	0	-0.042	-0.032	18.581	0.001	0.001	0.000	0.000	0.000	0.000
30	A	118	ASP	-1	-0.845	-0.917	21.586	0.047	0.047	0.000	0.000	0.000	0.000
31	A	119	SER	0	-0.034	-0.030	21.390	0.001	0.001	0.000	0.000	0.000	0.000
32	A	120	GLY	0	0.003	0.016	18.153	0.015	0.015	0.000	0.000	0.000	0.000
33	A	121	ALA	0	-0.017	0.007	17.429	0.038	0.038	0.000	0.000	0.000	0.000
34	A	122	PHE	0	-0.007	-0.022	14.303	-0.025	-0.025	0.000	0.000	0.000	0.000
35	A	123	LYS	1	0.910	0.960	17.601	-0.083	-0.083	0.000	0.000	0.000	0.000
36	A	124	LEU	0	-0.027	0.005	16.170	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	125	SER	0	-0.084	-0.085	18.191	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	126	ARG	1	0.802	0.877	18.494	-0.106	-0.106	0.000	0.000	0.000	0.000
39	A	127	GLU	-1	-0.804	-0.904	17.670	0.239	0.239	0.000	0.000	0.000	0.000
40	A	128	GLY	0	-0.013	-0.006	15.549	-0.017	-0.017	0.000	0.000	0.000	0.000
41	A	129	MET	0	-0.028	-0.010	16.368	-0.046	-0.046	0.000	0.000	0.000	0.000
42	A	130	VAL	0	0.015	0.024	17.287	0.020	0.020	0.000	0.000	0.000	0.000
43	A	131	MET	0	-0.047	-0.018	17.833	-0.043	-0.043	0.000	0.000	0.000	0.000
44	A	132	LEU	0	0.018	0.008	20.109	0.009	0.009	0.000	0.000	0.000	0.000
45	A	133	GLN	0	-0.022	-0.033	19.179	-0.031	-0.031	0.000	0.000	0.000	0.000
46	A	134	PHE	0	0.055	0.024	23.762	0.002	0.002	0.000	0.000	0.000	0.000
47	A	135	ALA	0	0.032	0.007	26.907	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	136	PRO	0	0.068	0.029	28.789	0.004	0.004	0.000	0.000	0.000	0.000
49	A	137	ALA	0	-0.023	-0.017	31.805	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	138	ALA	0	-0.039	-0.007	33.390	0.000	0.000	0.000	0.000	0.000	0.000
51	A	139	GLY	0	0.053	0.011	34.854	0.001	0.001	0.000	0.000	0.000	0.000
52	A	140	VAL	0	-0.028	-0.015	34.418	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	141	ARG	1	0.934	0.966	32.700	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	142	GLN	0	0.051	0.051	29.699	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	143	TYR	0	-0.018	-0.044	28.061	0.005	0.005	0.000	0.000	0.000	0.000
56	A	144	ASP	-1	-0.769	-0.872	28.883	-0.055	-0.055	0.000	0.000	0.000	0.000
57	A	145	TRP	0	-0.019	-0.033	23.834	0.003	0.003	0.000	0.000	0.000	0.000
58	A	146	SER	0	-0.031	-0.005	26.335	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	147	ARG	1	0.844	0.907	28.854	0.036	0.036	0.000	0.000	0.000	0.000
60	A	148	LYS	1	0.867	0.950	22.341	0.065	0.065	0.000	0.000	0.000	0.000
61	A	149	GLN	0	0.037	0.017	28.410	0.001	0.001	0.000	0.000	0.000	0.000
62	A	150	VAL	0	0.006	0.009	23.362	0.006	0.006	0.000	0.000	0.000	0.000
63	A	151	PHE	0	0.013	-0.002	24.686	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	152	SER	0	-0.008	-0.014	22.343	0.000	0.000	0.000	0.000	0.000	0.000
65	A	153	LEU	0	-0.021	0.001	22.370	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	154	SER	0	0.006	-0.032	21.708	0.026	0.026	0.000	0.000	0.000	0.000
67	A	155	VAL	0	0.068	0.023	20.150	0.001	0.001	0.000	0.000	0.000	0.000
68	A	156	THR	0	0.025	0.011	22.678	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	157	GLU	-1	-0.807	-0.863	25.742	0.102	0.102	0.000	0.000	0.000	0.000
70	A	158	ILE	0	-0.012	-0.013	19.978	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	159	GLY	0	0.035	0.012	24.277	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	160	SER	0	-0.022	0.002	26.425	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	161	ILE	0	-0.028	-0.012	26.113	-0.007	-0.007	0.000	0.000	0.000	0.000
74	A	162	ILE	0	-0.089	-0.048	23.490	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	163	SER	0	-0.047	-0.030	26.899	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	164	LEU	0	-0.026	0.007	30.482	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	165	GLY	0	0.047	0.032	32.451	0.003	0.003	0.000	0.000	0.000	0.000
78	A	166	THR	0	-0.070	-0.065	35.197	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	167	LYS	1	0.914	0.943	36.792	-0.064	-0.064	0.000	0.000	0.000	0.000
80	A	168	ASP	-1	-0.846	-0.892	36.236	0.076	0.076	0.000	0.000	0.000	0.000
81	A	169	SER	0	0.030	-0.006	36.477	0.002	0.002	0.000	0.000	0.000	0.000
82	A	170	CYS	0	-0.073	-0.015	32.271	0.005	0.005	0.000	0.000	0.000	0.000
83	A	171	GLU	-1	-0.828	-0.922	34.308	0.045	0.045	0.000	0.000	0.000	0.000
84	A	172	PHE	0	-0.004	0.000	30.058	0.004	0.004	0.000	0.000	0.000	0.000
85	A	173	PHE	0	0.017	0.007	32.429	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	174	HIS	1	0.795	0.884	27.342	-0.072	-0.072	0.000	0.000	0.000	0.000
87	A	175	ASP	-1	-0.711	-0.871	32.224	0.012	0.012	0.000	0.000	0.000	0.000
88	A	176	PRO	0	-0.010	-0.001	30.780	0.004	0.004	0.000	0.000	0.000	0.000
89	A	177	ASN	0	-0.083	-0.029	32.455	0.001	0.001	0.000	0.000	0.000	0.000
90	A	178	LYS	1	0.957	0.984	31.713	-0.037	-0.037	0.000	0.000	0.000	0.000
91	A	179	GLY	0	0.054	0.021	35.974	0.003	0.003	0.000	0.000	0.000	0.000
92	A	180	ARG	1	0.876	0.933	35.864	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	181	SER	0	-0.022	-0.006	36.409	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	182	ASP	-1	-0.782	-0.894	39.353	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	183	GLU	-1	-0.894	-0.939	40.424	0.017	0.017	0.000	0.000	0.000	0.000
96	A	184	GLY	0	-0.003	0.012	39.066	0.003	0.003	0.000	0.000	0.000	0.000
97	A	185	ARG	1	0.858	0.936	39.097	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	186	VAL	0	-0.036	-0.040	34.003	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	187	ARG	1	0.890	0.951	34.497	-0.023	-0.023	0.000	0.000	0.000	0.000
100	A	188	LYS	1	0.828	0.907	28.533	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	189	VAL	0	0.005	-0.006	33.340	0.004	0.004	0.000	0.000	0.000	0.000
102	A	190	LEU	0	-0.024	0.020	27.819	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	191	LYS	1	0.805	0.892	31.899	-0.044	-0.044	0.000	0.000	0.000	0.000
104	A	192	VAL	0	-0.011	-0.013	29.957	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	193	GLU	-1	-0.787	-0.890	33.366	0.053	0.053	0.000	0.000	0.000	0.000
106	A	194	PRO	0	0.012	0.017	35.962	0.000	0.000	0.000	0.000	0.000	0.000
107	A	195	LEU	0	-0.060	-0.029	35.286	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	196	PRO	0	-0.001	-0.010	38.878	0.001	0.001	0.000	0.000	0.000	0.000
109	A	197	ASP	-1	-0.821	-0.886	39.744	0.047	0.047	0.000	0.000	0.000	0.000
110	A	198	GLY	0	-0.046	-0.019	39.790	0.001	0.001	0.000	0.000	0.000	0.000
111	A	199	SER	0	-0.073	-0.056	37.053	0.005	0.005	0.000	0.000	0.000	0.000
112	A	200	GLY	0	-0.014	-0.027	34.119	0.005	0.005	0.000	0.000	0.000	0.000
113	A	201	HIS	0	0.012	0.033	32.418	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	202	PHE	0	-0.034	-0.014	33.157	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	203	PHE	0	0.020	0.007	27.191	0.004	0.004	0.000	0.000	0.000	0.000
116	A	204	ASN	0	0.007	-0.010	31.689	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	205	LEU	0	-0.015	-0.002	28.558	0.005	0.005	0.000	0.000	0.000	0.000
118	A	206	SER	0	0.018	0.001	32.504	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	207	VAL	0	-0.071	-0.049	31.748	0.003	0.003	0.000	0.000	0.000	0.000
120	A	208	GLN	0	0.014	0.002	34.890	0.000	0.000	0.000	0.000	0.000	0.000
121	A	209	ASN	0	-0.055	-0.036	35.864	0.000	0.000	0.000	0.000	0.000	0.000
122	A	210	LYS	1	0.878	0.918	38.576	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	211	LEU	0	-0.015	0.003	37.080	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	212	ILE	0	-0.015	-0.007	37.309	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	213	ASN	0	-0.049	-0.020	40.604	0.002	0.002	0.000	0.000	0.000	0.000
126	A	214	LEU	0	-0.006	0.021	34.803	0.000	0.000	0.000	0.000	0.000	0.000
127	A	215	ASP	-1	-0.793	-0.912	39.337	0.010	0.010	0.000	0.000	0.000	0.000
128	A	216	GLU	-1	-0.883	-0.924	35.283	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	217	ASN	0	-0.041	-0.030	35.922	0.007	0.007	0.000	0.000	0.000	0.000
130	A	218	ILE	0	0.029	0.041	31.158	0.000	0.000	0.000	0.000	0.000	0.000
131	A	219	TYR	0	0.006	0.000	33.701	0.004	0.004	0.000	0.000	0.000	0.000
132	A	220	ILE	0	-0.033	-0.016	28.468	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	221	PRO	0	0.015	0.022	32.354	0.005	0.005	0.000	0.000	0.000	0.000
134	A	222	VAL	0	-0.036	-0.027	28.152	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	223	THR	0	0.037	-0.010	30.741	0.004	0.004	0.000	0.000	0.000	0.000
136	A	224	LYS	1	1.020	0.984	30.474	-0.081	-0.081	0.000	0.000	0.000	0.000
137	A	225	ALA	0	-0.014	0.006	29.065	0.009	0.009	0.000	0.000	0.000	0.000
138	A	226	GLU	-1	-0.736	-0.829	26.293	0.077	0.077	0.000	0.000	0.000	0.000
139	A	227	PHE	0	0.028	0.012	25.688	0.013	0.013	0.000	0.000	0.000	0.000
140	A	228	ALA	0	0.016	0.013	26.254	0.013	0.013	0.000	0.000	0.000	0.000
141	A	229	VAL	0	-0.010	0.000	21.223	0.020	0.020	0.000	0.000	0.000	0.000
142	A	230	LEU	0	-0.007	-0.006	21.585	0.024	0.024	0.000	0.000	0.000	0.000
143	A	231	VAL	0	0.037	0.017	21.867	0.026	0.026	0.000	0.000	0.000	0.000
144	A	232	SER	0	-0.014	0.010	20.972	0.029	0.029	0.000	0.000	0.000	0.000
145	A	233	ALA	0	0.016	0.000	17.575	0.034	0.034	0.000	0.000	0.000	0.000
146	A	234	PHE	0	-0.015	-0.022	17.536	0.045	0.045	0.000	0.000	0.000	0.000
147	A	235	ASN	0	-0.005	-0.022	19.396	0.025	0.025	0.000	0.000	0.000	0.000
148	A	236	PHE	0	-0.010	0.009	11.357	0.020	0.020	0.000	0.000	0.000	0.000
149	A	237	VAL	0	0.013	-0.007	13.356	0.065	0.065	0.000	0.000	0.000	0.000
150	A	238	MET	0	0.008	0.021	15.557	0.041	0.041	0.000	0.000	0.000	0.000
151	A	239	PRO	0	0.025	0.015	15.858	-0.004	-0.004	0.000	0.000	0.000	0.000
152	A	240	TYR	0	-0.018	-0.015	9.757	0.088	0.088	0.000	0.000	0.000	0.000
153	A	241	LEU	0	-0.088	-0.031	13.756	0.013	0.013	0.000	0.000	0.000	0.000
154	A	242	LEU	0	0.057	0.027	15.852	-0.037	-0.037	0.000	0.000	0.000	0.000
155	A	243	GLY	0	0.006	0.000	14.020	-0.029	-0.029	0.000	0.000	0.000	0.000
156	A	244	TRP	0	0.016	0.016	14.836	0.031	0.031	0.000	0.000	0.000	0.000
157	A	245	HIS	0	0.034	0.030	9.348	-0.158	-0.158	0.000	0.000	0.000	0.000
158	A	246	THR	0	-0.041	-0.032	10.848	0.040	0.040	0.000	0.000	0.000	0.000
159	A	247	ALA	0	0.038	0.029	13.034	-0.030	-0.030	0.000	0.000	0.000	0.000
160	A	248	VAL	0	0.030	0.018	14.860	-0.018	-0.018	0.000	0.000	0.000	0.000
161	A	249	ASN	0	-0.059	-0.029	10.535	-0.018	-0.018	0.000	0.000	0.000	0.000
162	A	250	SER	0	-0.041	-0.027	14.371	-0.019	-0.019	0.000	0.000	0.000	0.000
163	A	251	PHE	0	-0.037	-0.014	17.342	-0.037	-0.037	0.000	0.000	0.000	0.000
164	A	252	LYS	1	0.859	0.925	14.014	-0.538	-0.538	0.000	0.000	0.000	0.000
165	A	253	PRO	0	0.008	0.003	20.303	-0.014	-0.014	0.000	0.000	0.000	0.000
166	A	254	GLU	-1	-0.934	-0.952	21.250	0.239	0.239	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:89:THR)