FMO DATABASE

FMODB ID: LL5R9

Calculation Name: 1L3A-A-Xray315

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	168
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1541245.871714
FMO2-HF: Nuclear repulsion	1476886.483982
FMO2-HF: Total energy	-64359.387732
FMO2-MP2: Total energy	-64549.166624

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:88:ACE )

Summations of interaction energy for fragment #1(A:88:ACE )

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.
1.497	2.188	-0.005	-0.322	-0.363	0.001

Interaction energy analysis for fragmet #1(A:88:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.025 / q_NPA : 0.003

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	90	PRO	0	0.037	0.025	3.864	1.067	1.758	-0.005	-0.322	-0.363	0.001
4	A	91	LYS	1	0.969	0.992	7.002	0.201	0.201	0.000	0.000	0.000	0.000
5	A	92	VAL	0	0.018	-0.002	9.886	0.021	0.021	0.000	0.000	0.000	0.000
6	A	93	PHE	0	-0.042	-0.024	12.547	0.035	0.035	0.000	0.000	0.000	0.000
7	A	94	VAL	0	0.022	0.022	15.146	0.000	0.000	0.000	0.000	0.000	0.000
8	A	95	GLY	0	0.065	0.008	17.662	0.019	0.019	0.000	0.000	0.000	0.000
9	A	96	TYR	0	-0.054	-0.005	20.950	0.000	0.000	0.000	0.000	0.000	0.000
10	A	97	SER	0	0.044	0.025	23.951	0.013	0.013	0.000	0.000	0.000	0.000
11	A	98	ILE	0	-0.020	0.015	27.161	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	99	TYR	0	0.032	0.010	28.215	0.002	0.002	0.000	0.000	0.000	0.000
13	A	100	LYS	1	0.840	0.917	33.485	0.052	0.052	0.000	0.000	0.000	0.000
14	A	101	GLY	0	-0.047	-0.031	37.091	0.001	0.001	0.000	0.000	0.000	0.000
15	A	102	LYS	1	0.978	0.986	40.144	0.029	0.029	0.000	0.000	0.000	0.000
16	A	103	ALA	0	0.038	0.022	35.474	0.002	0.002	0.000	0.000	0.000	0.000
17	A	104	ALA	0	-0.026	0.004	31.419	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	105	LEU	0	-0.009	-0.011	28.737	0.004	0.004	0.000	0.000	0.000	0.000
19	A	106	THR	0	-0.009	-0.012	23.610	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	107	VAL	0	-0.014	-0.010	23.247	0.009	0.009	0.000	0.000	0.000	0.000
21	A	108	GLU	-1	-0.902	-0.955	18.991	-0.107	-0.107	0.000	0.000	0.000	0.000
22	A	109	PRO	0	-0.013	0.008	16.122	0.018	0.018	0.000	0.000	0.000	0.000
23	A	110	ARG	1	0.905	0.936	16.549	-0.021	-0.021	0.000	0.000	0.000	0.000
24	A	111	SER	0	-0.019	-0.029	12.667	0.003	0.003	0.000	0.000	0.000	0.000
25	A	112	PRO	0	0.013	0.025	13.601	0.007	0.007	0.000	0.000	0.000	0.000
26	A	113	GLU	-1	-0.946	-0.971	14.584	0.125	0.125	0.000	0.000	0.000	0.000
27	A	114	PHE	0	0.038	0.013	12.527	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	115	SER	0	-0.025	-0.021	15.862	0.001	0.001	0.000	0.000	0.000	0.000
29	A	116	PRO	0	0.007	-0.003	16.428	0.003	0.003	0.000	0.000	0.000	0.000
30	A	117	LEU	0	-0.033	-0.028	17.589	-0.030	-0.030	0.000	0.000	0.000	0.000
31	A	118	ASP	-1	-0.861	-0.921	20.152	0.145	0.145	0.000	0.000	0.000	0.000
32	A	119	SER	0	-0.025	-0.025	19.746	0.018	0.018	0.000	0.000	0.000	0.000
33	A	120	GLY	0	-0.016	0.002	16.229	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	121	ALA	0	0.010	0.025	15.947	0.009	0.009	0.000	0.000	0.000	0.000
35	A	122	PHE	0	-0.011	-0.015	12.359	0.014	0.014	0.000	0.000	0.000	0.000
36	A	123	LYS	1	0.953	0.989	16.596	-0.143	-0.143	0.000	0.000	0.000	0.000
37	A	124	LEU	0	-0.015	0.006	16.967	0.012	0.012	0.000	0.000	0.000	0.000
38	A	125	SER	0	-0.062	-0.044	18.412	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	126	ARG	1	0.917	0.957	19.282	-0.068	-0.068	0.000	0.000	0.000	0.000
40	A	127	GLU	-1	-0.888	-0.926	18.845	0.023	0.023	0.000	0.000	0.000	0.000
41	A	128	GLY	0	0.007	0.002	17.991	0.004	0.004	0.000	0.000	0.000	0.000
42	A	129	MET	0	-0.048	-0.029	18.803	0.001	0.001	0.000	0.000	0.000	0.000
43	A	130	VAL	0	0.019	0.018	20.010	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	131	MET	0	-0.094	-0.021	21.126	0.016	0.016	0.000	0.000	0.000	0.000
45	A	132	LEU	0	0.031	0.022	23.582	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	133	GLN	0	-0.015	-0.014	23.361	0.007	0.007	0.000	0.000	0.000	0.000
47	A	134	PHE	0	0.052	0.021	27.992	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	135	ALA	0	0.011	0.005	31.480	0.004	0.004	0.000	0.000	0.000	0.000
49	A	136	PRO	0	0.066	0.030	33.294	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	137	ALA	0	-0.014	-0.020	36.480	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	138	ALA	0	-0.021	0.000	37.926	0.002	0.002	0.000	0.000	0.000	0.000
52	A	139	GLY	0	0.056	0.018	39.731	0.002	0.002	0.000	0.000	0.000	0.000
53	A	140	VAL	0	-0.044	-0.032	39.274	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	141	ARG	1	0.933	0.964	38.398	0.038	0.038	0.000	0.000	0.000	0.000
55	A	142	GLN	0	0.053	0.060	34.804	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	143	TYR	0	-0.024	-0.041	32.865	0.001	0.001	0.000	0.000	0.000	0.000
57	A	144	ASP	-1	-0.759	-0.864	33.589	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	145	TRP	0	-0.046	-0.033	28.329	0.003	0.003	0.000	0.000	0.000	0.000
59	A	146	SER	0	-0.022	-0.005	30.765	0.002	0.002	0.000	0.000	0.000	0.000
60	A	147	ARG	1	0.881	0.927	33.131	0.024	0.024	0.000	0.000	0.000	0.000
61	A	148	LYS	1	0.931	0.990	26.138	0.042	0.042	0.000	0.000	0.000	0.000
62	A	149	GLN	0	0.014	0.006	31.834	0.005	0.005	0.000	0.000	0.000	0.000
63	A	150	VAL	0	0.005	0.000	26.428	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	151	PHE	0	0.005	-0.013	28.278	0.006	0.006	0.000	0.000	0.000	0.000
65	A	152	SER	0	-0.005	-0.033	24.669	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	153	LEU	0	0.009	0.014	25.433	0.003	0.003	0.000	0.000	0.000	0.000
67	A	154	SER	0	0.014	-0.002	24.698	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	155	VAL	0	0.139	0.046	22.634	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	156	THR	0	0.017	0.002	25.306	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	157	GLU	-1	-0.822	-0.891	28.699	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	158	ILE	0	-0.005	-0.001	23.513	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	159	GLY	0	0.033	0.011	27.789	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	160	SER	0	-0.013	-0.005	29.768	0.000	0.000	0.000	0.000	0.000	0.000
74	A	161	ILE	0	-0.040	-0.015	29.725	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	162	ILE	0	-0.060	-0.035	27.376	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	163	SER	0	-0.071	-0.021	30.925	0.000	0.000	0.000	0.000	0.000	0.000
77	A	164	LEU	0	-0.002	0.018	34.145	0.003	0.003	0.000	0.000	0.000	0.000
78	A	165	GLY	0	0.053	0.029	36.324	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	166	THR	0	-0.093	-0.081	39.263	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	167	LYS	1	0.935	0.954	41.251	0.025	0.025	0.000	0.000	0.000	0.000
81	A	168	ASP	-1	-0.847	-0.883	39.760	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	169	SER	0	0.027	-0.012	39.783	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	170	CYS	0	-0.036	-0.002	35.469	0.000	0.000	0.000	0.000	0.000	0.000
84	A	171	GLU	-1	-0.907	-0.965	37.668	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	172	PHE	0	-0.006	-0.007	32.811	0.002	0.002	0.000	0.000	0.000	0.000
86	A	173	PHE	0	0.030	0.015	35.563	0.000	0.000	0.000	0.000	0.000	0.000
87	A	174	HIS	1	0.728	0.831	29.456	0.007	0.007	0.000	0.000	0.000	0.000
88	A	175	ASP	-1	-0.816	-0.927	34.533	0.006	0.006	0.000	0.000	0.000	0.000
89	A	176	PRO	0	-0.069	-0.035	33.217	0.002	0.002	0.000	0.000	0.000	0.000
90	A	177	ASN	0	-0.078	-0.030	34.556	0.003	0.003	0.000	0.000	0.000	0.000
91	A	178	LYS	1	0.969	0.993	34.012	-0.026	-0.026	0.000	0.000	0.000	0.000
92	A	179	GLY	0	0.119	0.064	37.636	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	180	ARG	1	0.819	0.912	36.626	-0.030	-0.030	0.000	0.000	0.000	0.000
94	A	181	SER	0	-0.009	-0.006	37.723	0.001	0.001	0.000	0.000	0.000	0.000
95	A	182	ASP	-1	-0.848	-0.926	40.416	0.013	0.013	0.000	0.000	0.000	0.000
96	A	183	GLU	-1	-0.913	-0.966	41.815	0.009	0.009	0.000	0.000	0.000	0.000
97	A	184	GLY	0	-0.019	0.013	40.845	0.000	0.000	0.000	0.000	0.000	0.000
98	A	185	ARG	1	0.937	0.958	41.817	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	186	VAL	0	-0.057	-0.040	36.518	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	187	ARG	1	0.991	1.007	37.565	0.004	0.004	0.000	0.000	0.000	0.000
101	A	188	LYS	1	0.881	0.938	30.767	0.007	0.007	0.000	0.000	0.000	0.000
102	A	189	VAL	0	0.003	0.004	36.118	0.001	0.001	0.000	0.000	0.000	0.000
103	A	190	LEU	0	-0.013	0.022	31.581	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	191	LYS	1	0.901	0.966	35.577	0.016	0.016	0.000	0.000	0.000	0.000
105	A	192	VAL	0	-0.001	-0.002	34.023	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	193	GLU	-1	-0.857	-0.953	37.410	-0.016	-0.016	0.000	0.000	0.000	0.000
107	A	194	PRO	0	-0.015	0.007	40.458	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	195	LEU	0	-0.041	-0.021	40.055	0.001	0.001	0.000	0.000	0.000	0.000
109	A	196	PRO	0	0.012	-0.004	43.379	0.001	0.001	0.000	0.000	0.000	0.000
110	A	197	ASP	-1	-0.880	-0.932	45.033	-0.031	-0.031	0.000	0.000	0.000	0.000
111	A	198	GLY	0	-0.022	0.001	44.422	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	199	SER	0	-0.065	-0.035	42.184	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	200	GLY	0	-0.029	-0.037	38.862	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	201	HIS	0	0.026	0.038	36.683	0.001	0.001	0.000	0.000	0.000	0.000
115	A	202	PHE	0	-0.024	-0.009	37.815	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	203	PHE	0	-0.001	-0.008	30.993	0.001	0.001	0.000	0.000	0.000	0.000
117	A	204	ASN	0	0.003	-0.015	36.008	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	205	LEU	0	-0.008	0.006	32.684	0.002	0.002	0.000	0.000	0.000	0.000
119	A	206	SER	0	-0.009	-0.005	36.490	0.000	0.000	0.000	0.000	0.000	0.000
120	A	207	VAL	0	-0.048	-0.033	35.165	0.001	0.001	0.000	0.000	0.000	0.000
121	A	208	GLN	0	0.061	0.032	38.074	0.000	0.000	0.000	0.000	0.000	0.000
122	A	209	ASN	0	0.010	0.005	38.769	0.003	0.003	0.000	0.000	0.000	0.000
123	A	210	LYS	1	0.995	0.995	41.055	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	211	LEU	0	-0.009	-0.004	39.177	0.000	0.000	0.000	0.000	0.000	0.000
125	A	212	ILE	0	0.001	0.013	39.845	0.000	0.000	0.000	0.000	0.000	0.000
126	A	213	ASN	0	-0.062	-0.032	42.957	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	214	LEU	0	-0.014	0.003	37.915	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	215	ASP	-1	-0.957	-0.999	42.459	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	216	GLU	-1	-0.859	-0.930	38.966	-0.019	-0.019	0.000	0.000	0.000	0.000
130	A	217	ASN	0	0.002	-0.002	39.899	0.002	0.002	0.000	0.000	0.000	0.000
131	A	218	ILE	0	-0.023	0.014	35.633	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	219	TYR	0	0.020	0.007	37.572	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	220	ILE	0	-0.033	-0.027	33.361	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	221	PRO	0	-0.027	0.010	37.013	0.000	0.000	0.000	0.000	0.000	0.000
135	A	222	VAL	0	-0.027	-0.018	32.920	-0.004	-0.004	0.000	0.000	0.000	0.000
136	A	223	THR	0	0.024	-0.033	35.381	0.001	0.001	0.000	0.000	0.000	0.000
137	A	224	LYS	1	1.043	1.001	35.372	0.040	0.040	0.000	0.000	0.000	0.000
138	A	225	ALA	0	-0.023	-0.010	34.330	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	226	GLU	-1	-0.745	-0.844	31.340	-0.062	-0.062	0.000	0.000	0.000	0.000
140	A	227	PHE	0	0.016	0.013	30.515	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	228	ALA	0	0.009	0.006	30.699	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	229	VAL	0	-0.008	0.007	26.161	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	230	LEU	0	0.011	0.004	26.215	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	231	VAL	0	0.028	0.024	26.164	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	232	SER	0	-0.027	-0.009	25.665	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	233	ALA	0	0.019	0.003	22.269	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	234	PHE	0	-0.028	-0.037	21.742	-0.004	-0.004	0.000	0.000	0.000	0.000
148	A	235	ASN	0	0.033	0.000	23.151	0.008	0.008	0.000	0.000	0.000	0.000
149	A	236	PHE	0	-0.024	0.006	15.534	0.004	0.004	0.000	0.000	0.000	0.000
150	A	237	VAL	0	-0.008	-0.017	17.332	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	238	MET	0	0.016	0.010	18.633	0.011	0.011	0.000	0.000	0.000	0.000
152	A	239	PRO	0	0.028	0.023	18.838	0.013	0.013	0.000	0.000	0.000	0.000
153	A	240	TYR	0	-0.002	-0.009	13.217	0.003	0.003	0.000	0.000	0.000	0.000
154	A	241	LEU	0	-0.107	-0.037	15.805	0.020	0.020	0.000	0.000	0.000	0.000
155	A	242	LEU	0	0.052	0.020	18.110	0.017	0.017	0.000	0.000	0.000	0.000
156	A	243	GLY	0	0.012	0.008	15.306	0.017	0.017	0.000	0.000	0.000	0.000
157	A	244	TRP	0	0.021	0.008	16.112	0.012	0.012	0.000	0.000	0.000	0.000
158	A	245	HIS	0	0.038	0.028	11.052	0.001	0.001	0.000	0.000	0.000	0.000
159	A	246	THR	0	-0.070	-0.047	11.161	0.009	0.009	0.000	0.000	0.000	0.000
160	A	247	ALA	0	0.028	0.021	13.404	0.019	0.019	0.000	0.000	0.000	0.000
161	A	248	VAL	0	0.024	0.011	16.450	0.004	0.004	0.000	0.000	0.000	0.000
162	A	249	ASN	0	-0.044	-0.011	11.419	-0.039	-0.039	0.000	0.000	0.000	0.000
163	A	250	SER	0	-0.050	-0.028	14.804	0.009	0.009	0.000	0.000	0.000	0.000
164	A	251	PHE	0	-0.034	-0.008	16.884	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	252	LYS	1	0.915	0.949	13.957	-0.013	-0.013	0.000	0.000	0.000	0.000
166	A	253	PRO	0	-0.024	-0.014	20.039	0.009	0.009	0.000	0.000	0.000	0.000
167	A	254	GLU	-1	-0.907	-0.948	19.846	0.039	0.039	0.000	0.000	0.000	0.000
168	A	255	NME	0	-0.016	0.004	21.149	0.012	0.012	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:88:ACE )