FMO DATABASE

FMODB ID: YYJ92

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	OptH
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	-1535362.098364
FMO2-HF: Nuclear repulsion	1471173.580765
FMO2-HF: Total energy	-64188.517598
FMO2-MP2: Total energy	-64377.774555

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.
-0.336	1.985	-0.001	-1.368	-0.953	0.006

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 : 0.012 / q_NPA : 0.007

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	0.970	0.991	3.607	-0.077	2.244	-0.001	-1.368	-0.953	0.006
4	A	92	VAL	0	0.017	-0.002	5.073	-0.155	-0.155	0.000	0.000	0.000	0.000
5	A	93	PHE	0	-0.041	-0.023	7.746	0.196	0.196	0.000	0.000	0.000	0.000
6	A	94	VAL	0	0.022	0.022	10.120	-0.028	-0.028	0.000	0.000	0.000	0.000
7	A	95	GLY	0	0.064	0.008	12.759	-0.031	-0.031	0.000	0.000	0.000	0.000
8	A	96	TYR	0	-0.054	-0.005	16.287	-0.025	-0.025	0.000	0.000	0.000	0.000
9	A	97	SER	0	0.046	0.025	19.116	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	98	ILE	0	-0.020	0.016	22.298	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	99	TYR	0	0.031	0.010	23.251	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	100	LYS	1	0.841	0.917	28.517	-0.085	-0.085	0.000	0.000	0.000	0.000
13	A	101	GLY	0	-0.046	-0.031	32.201	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	102	LYS	1	0.978	0.986	35.506	-0.045	-0.045	0.000	0.000	0.000	0.000
15	A	103	ALA	0	0.038	0.022	31.245	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	104	ALA	0	-0.023	0.006	26.759	0.004	0.004	0.000	0.000	0.000	0.000
17	A	105	LEU	0	-0.012	-0.012	24.781	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	106	THR	0	-0.004	-0.010	19.372	0.002	0.002	0.000	0.000	0.000	0.000
19	A	107	VAL	0	-0.016	-0.011	19.337	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	108	GLU	-1	-0.899	-0.953	15.179	0.191	0.191	0.000	0.000	0.000	0.000
21	A	109	PRO	0	-0.016	0.007	12.389	-0.039	-0.039	0.000	0.000	0.000	0.000
22	A	110	ARG	1	0.904	0.935	13.564	-0.139	-0.139	0.000	0.000	0.000	0.000
23	A	111	SER	0	-0.019	-0.028	10.350	0.047	0.047	0.000	0.000	0.000	0.000
24	A	112	PRO	0	0.014	0.025	11.980	-0.080	-0.080	0.000	0.000	0.000	0.000
25	A	113	GLU	-1	-0.948	-0.972	13.374	0.016	0.016	0.000	0.000	0.000	0.000
26	A	114	PHE	0	0.038	0.012	11.671	0.025	0.025	0.000	0.000	0.000	0.000
27	A	115	SER	0	-0.024	-0.020	15.836	-0.044	-0.044	0.000	0.000	0.000	0.000
28	A	116	PRO	0	0.008	-0.002	17.740	0.024	0.024	0.000	0.000	0.000	0.000
29	A	117	LEU	0	-0.035	-0.029	18.826	0.009	0.009	0.000	0.000	0.000	0.000
30	A	118	ASP	-1	-0.860	-0.920	21.588	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	119	SER	0	-0.026	-0.026	21.707	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	120	GLY	0	-0.015	0.003	18.341	0.015	0.015	0.000	0.000	0.000	0.000
33	A	121	ALA	0	0.010	0.024	17.885	0.029	0.029	0.000	0.000	0.000	0.000
34	A	122	PHE	0	-0.011	-0.015	14.214	-0.031	-0.031	0.000	0.000	0.000	0.000
35	A	123	LYS	1	0.953	0.989	17.618	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	124	LEU	0	-0.018	0.005	16.088	-0.021	-0.021	0.000	0.000	0.000	0.000
37	A	125	SER	0	-0.059	-0.044	18.148	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	126	ARG	1	0.917	0.957	18.552	-0.080	-0.080	0.000	0.000	0.000	0.000
39	A	127	GLU	-1	-0.888	-0.926	17.646	0.204	0.204	0.000	0.000	0.000	0.000
40	A	128	GLY	0	0.008	0.002	15.775	-0.018	-0.018	0.000	0.000	0.000	0.000
41	A	129	MET	0	-0.049	-0.029	16.656	-0.045	-0.045	0.000	0.000	0.000	0.000
42	A	130	VAL	0	0.022	0.019	16.992	0.044	0.044	0.000	0.000	0.000	0.000
43	A	131	MET	0	-0.097	-0.022	17.973	-0.053	-0.053	0.000	0.000	0.000	0.000
44	A	132	LEU	0	0.033	0.022	20.210	0.012	0.012	0.000	0.000	0.000	0.000
45	A	133	GLN	0	-0.019	-0.015	19.851	-0.032	-0.032	0.000	0.000	0.000	0.000
46	A	134	PHE	0	0.055	0.022	24.303	0.006	0.006	0.000	0.000	0.000	0.000
47	A	135	ALA	0	0.009	0.004	27.435	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	136	PRO	0	0.067	0.030	29.274	0.005	0.005	0.000	0.000	0.000	0.000
49	A	137	ALA	0	-0.017	-0.021	32.219	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	138	ALA	0	-0.017	0.001	33.427	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	139	GLY	0	0.055	0.019	35.302	0.001	0.001	0.000	0.000	0.000	0.000
52	A	140	VAL	0	-0.044	-0.032	34.327	0.001	0.001	0.000	0.000	0.000	0.000
53	A	141	ARG	1	0.934	0.963	33.321	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	142	GLN	0	0.051	0.059	30.111	0.000	0.000	0.000	0.000	0.000	0.000
55	A	143	TYR	0	-0.025	-0.041	28.351	0.004	0.004	0.000	0.000	0.000	0.000
56	A	144	ASP	-1	-0.760	-0.863	29.237	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	145	TRP	0	-0.047	-0.033	24.209	0.002	0.002	0.000	0.000	0.000	0.000
58	A	146	SER	0	-0.021	-0.005	27.256	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	147	ARG	1	0.881	0.927	29.708	0.005	0.005	0.000	0.000	0.000	0.000
60	A	148	LYS	1	0.933	0.991	22.696	0.000	0.000	0.000	0.000	0.000	0.000
61	A	149	GLN	0	0.012	0.006	28.564	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	150	VAL	0	0.006	0.000	23.172	0.008	0.008	0.000	0.000	0.000	0.000
63	A	151	PHE	0	0.006	-0.012	24.941	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	152	SER	0	-0.007	-0.034	21.836	0.009	0.009	0.000	0.000	0.000	0.000
65	A	153	LEU	0	0.011	0.015	22.372	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	154	SER	0	0.016	-0.001	21.838	0.026	0.026	0.000	0.000	0.000	0.000
67	A	155	VAL	0	0.134	0.045	20.375	0.004	0.004	0.000	0.000	0.000	0.000
68	A	156	THR	0	0.018	0.001	22.851	0.007	0.007	0.000	0.000	0.000	0.000
69	A	157	GLU	-1	-0.822	-0.891	25.983	0.107	0.107	0.000	0.000	0.000	0.000
70	A	158	ILE	0	-0.004	0.000	20.399	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	159	GLY	0	0.032	0.011	24.730	0.002	0.002	0.000	0.000	0.000	0.000
72	A	160	SER	0	-0.017	-0.007	26.922	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	161	ILE	0	-0.037	-0.014	26.324	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	162	ILE	0	-0.060	-0.035	24.181	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	163	SER	0	-0.072	-0.021	27.562	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	164	LEU	0	-0.003	0.017	30.913	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	165	GLY	0	0.053	0.030	32.947	0.004	0.004	0.000	0.000	0.000	0.000
78	A	166	THR	0	-0.088	-0.079	35.648	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	167	LYS	1	0.933	0.953	37.385	-0.075	-0.075	0.000	0.000	0.000	0.000
80	A	168	ASP	-1	-0.846	-0.883	36.339	0.086	0.086	0.000	0.000	0.000	0.000
81	A	169	SER	0	0.028	-0.012	36.285	0.000	0.000	0.000	0.000	0.000	0.000
82	A	170	CYS	0	-0.036	-0.002	32.183	0.004	0.004	0.000	0.000	0.000	0.000
83	A	171	GLU	-1	-0.909	-0.967	34.438	0.056	0.056	0.000	0.000	0.000	0.000
84	A	172	PHE	0	-0.004	-0.005	29.471	0.002	0.002	0.000	0.000	0.000	0.000
85	A	173	PHE	0	0.028	0.014	32.611	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	174	HIS	1	0.728	0.831	26.760	-0.085	-0.085	0.000	0.000	0.000	0.000
87	A	175	ASP	-1	-0.818	-0.927	31.997	0.024	0.024	0.000	0.000	0.000	0.000
88	A	176	PRO	0	-0.066	-0.034	31.047	0.001	0.001	0.000	0.000	0.000	0.000
89	A	177	ASN	0	-0.078	-0.031	32.604	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	178	LYS	1	0.970	0.993	32.854	-0.024	-0.024	0.000	0.000	0.000	0.000
91	A	179	GLY	0	0.117	0.063	35.958	0.002	0.002	0.000	0.000	0.000	0.000
92	A	180	ARG	1	0.820	0.913	35.695	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	181	SER	0	-0.010	-0.006	36.518	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	182	ASP	-1	-0.848	-0.926	39.226	0.003	0.003	0.000	0.000	0.000	0.000
95	A	183	GLU	-1	-0.914	-0.966	40.218	0.020	0.020	0.000	0.000	0.000	0.000
96	A	184	GLY	0	-0.017	0.013	38.884	0.002	0.002	0.000	0.000	0.000	0.000
97	A	185	ARG	1	0.935	0.957	39.766	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	186	VAL	0	-0.056	-0.040	34.110	0.000	0.000	0.000	0.000	0.000	0.000
99	A	187	ARG	1	0.992	1.008	35.013	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	188	LYS	1	0.880	0.939	27.869	-0.040	-0.040	0.000	0.000	0.000	0.000
101	A	189	VAL	0	0.000	0.003	33.257	0.003	0.003	0.000	0.000	0.000	0.000
102	A	190	LEU	0	-0.008	0.024	28.146	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	191	LYS	1	0.897	0.965	32.246	-0.056	-0.056	0.000	0.000	0.000	0.000
104	A	192	VAL	0	0.002	-0.001	30.438	0.001	0.001	0.000	0.000	0.000	0.000
105	A	193	GLU	-1	-0.859	-0.953	33.782	0.061	0.061	0.000	0.000	0.000	0.000
106	A	194	PRO	0	-0.011	0.009	36.617	0.002	0.002	0.000	0.000	0.000	0.000
107	A	195	LEU	0	-0.044	-0.023	35.607	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	196	PRO	0	0.013	-0.004	39.239	0.000	0.000	0.000	0.000	0.000	0.000
109	A	197	ASP	-1	-0.879	-0.932	40.514	0.063	0.063	0.000	0.000	0.000	0.000
110	A	198	GLY	0	-0.022	0.000	40.249	0.001	0.001	0.000	0.000	0.000	0.000
111	A	199	SER	0	-0.067	-0.036	37.507	0.005	0.005	0.000	0.000	0.000	0.000
112	A	200	GLY	0	-0.027	-0.037	34.502	0.006	0.006	0.000	0.000	0.000	0.000
113	A	201	HIS	0	0.027	0.039	32.750	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	202	PHE	0	-0.029	-0.011	33.653	0.001	0.001	0.000	0.000	0.000	0.000
115	A	203	PHE	0	0.000	-0.007	27.238	0.003	0.003	0.000	0.000	0.000	0.000
116	A	204	ASN	0	0.003	-0.015	32.161	-0.007	-0.007	0.000	0.000	0.000	0.000
117	A	205	LEU	0	-0.011	0.005	29.229	0.003	0.003	0.000	0.000	0.000	0.000
118	A	206	SER	0	-0.006	-0.003	32.984	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	207	VAL	0	-0.049	-0.033	31.982	0.003	0.003	0.000	0.000	0.000	0.000
120	A	208	GLN	0	0.061	0.032	34.986	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	209	ASN	0	0.011	0.006	36.072	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	210	LYS	1	0.994	0.994	38.487	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	211	LEU	0	-0.005	-0.003	37.138	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	212	ILE	0	-0.003	0.012	37.262	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	213	ASN	0	-0.059	-0.031	40.479	0.001	0.001	0.000	0.000	0.000	0.000
126	A	214	LEU	0	-0.017	0.001	34.933	0.000	0.000	0.000	0.000	0.000	0.000
127	A	215	ASP	-1	-0.960	-1.000	39.480	0.022	0.022	0.000	0.000	0.000	0.000
128	A	216	GLU	-1	-0.857	-0.929	35.584	0.021	0.021	0.000	0.000	0.000	0.000
129	A	217	ASN	0	0.000	-0.003	36.396	0.005	0.005	0.000	0.000	0.000	0.000
130	A	218	ILE	0	-0.018	0.016	31.736	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	219	TYR	0	0.016	0.006	33.824	0.005	0.005	0.000	0.000	0.000	0.000
132	A	220	ILE	0	-0.030	-0.026	28.960	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	221	PRO	0	-0.028	0.010	32.837	0.005	0.005	0.000	0.000	0.000	0.000
134	A	222	VAL	0	-0.025	-0.017	28.656	0.001	0.001	0.000	0.000	0.000	0.000
135	A	223	THR	0	0.026	-0.031	30.564	0.001	0.001	0.000	0.000	0.000	0.000
136	A	224	LYS	1	1.040	1.000	30.870	-0.097	-0.097	0.000	0.000	0.000	0.000
137	A	225	ALA	0	-0.023	-0.010	29.439	0.008	0.008	0.000	0.000	0.000	0.000
138	A	226	GLU	-1	-0.745	-0.844	26.587	0.115	0.115	0.000	0.000	0.000	0.000
139	A	227	PHE	0	0.014	0.012	26.044	0.015	0.015	0.000	0.000	0.000	0.000
140	A	228	ALA	0	0.010	0.006	26.578	0.013	0.013	0.000	0.000	0.000	0.000
141	A	229	VAL	0	-0.009	0.007	21.475	0.019	0.019	0.000	0.000	0.000	0.000
142	A	230	LEU	0	0.012	0.005	21.884	0.029	0.029	0.000	0.000	0.000	0.000
143	A	231	VAL	0	0.025	0.023	22.279	0.025	0.025	0.000	0.000	0.000	0.000
144	A	232	SER	0	-0.024	-0.009	21.104	0.028	0.028	0.000	0.000	0.000	0.000
145	A	233	ALA	0	0.017	0.002	18.209	0.034	0.034	0.000	0.000	0.000	0.000
146	A	234	PHE	0	-0.026	-0.036	17.950	0.044	0.044	0.000	0.000	0.000	0.000
147	A	235	ASN	0	0.033	0.000	19.902	0.015	0.015	0.000	0.000	0.000	0.000
148	A	236	PHE	0	-0.025	0.006	11.278	0.009	0.009	0.000	0.000	0.000	0.000
149	A	237	VAL	0	-0.007	-0.016	13.896	0.056	0.056	0.000	0.000	0.000	0.000
150	A	238	MET	0	0.014	0.009	15.847	0.028	0.028	0.000	0.000	0.000	0.000
151	A	239	PRO	0	0.029	0.023	16.047	-0.009	-0.009	0.000	0.000	0.000	0.000
152	A	240	TYR	0	-0.001	-0.008	10.353	0.055	0.055	0.000	0.000	0.000	0.000
153	A	241	LEU	0	-0.109	-0.037	13.882	0.007	0.007	0.000	0.000	0.000	0.000
154	A	242	LEU	0	0.052	0.019	15.896	-0.042	-0.042	0.000	0.000	0.000	0.000
155	A	243	GLY	0	0.013	0.009	14.114	-0.032	-0.032	0.000	0.000	0.000	0.000
156	A	244	TRP	0	0.021	0.008	15.182	0.000	0.000	0.000	0.000	0.000	0.000
157	A	245	HIS	0	0.037	0.028	9.683	-0.107	-0.107	0.000	0.000	0.000	0.000
158	A	246	THR	0	-0.068	-0.047	10.756	0.010	0.010	0.000	0.000	0.000	0.000
159	A	247	ALA	0	0.028	0.020	13.135	-0.036	-0.036	0.000	0.000	0.000	0.000
160	A	248	VAL	0	0.022	0.011	14.907	-0.017	-0.017	0.000	0.000	0.000	0.000
161	A	249	ASN	0	-0.043	-0.011	10.506	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	250	SER	0	-0.050	-0.028	14.293	-0.019	-0.019	0.000	0.000	0.000	0.000
163	A	251	PHE	0	-0.035	-0.009	17.068	-0.037	-0.037	0.000	0.000	0.000	0.000
164	A	252	LYS	1	0.914	0.949	14.131	-0.414	-0.414	0.000	0.000	0.000	0.000
165	A	253	PRO	0	-0.013	-0.005	19.993	-0.013	-0.013	0.000	0.000	0.000	0.000
166	A	254	GLU	-1	-0.929	-0.949	20.946	0.190	0.190	0.000	0.000	0.000	0.000

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