FMO DATABASE

FMODB ID: K9KN3

Calculation Name: 1LCL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1LCL

Chain ID: A

ChEMBL ID:

UniProt ID: Q05315

Base Structure: X-ray

Registration Date: 2023-06-22

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1407882.029565
FMO2-HF: Nuclear repulsion	1349995.772558
FMO2-HF: Total energy	-57886.257007
FMO2-MP2: Total energy	-58053.25412

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-22.366	-20.453	21.684	-11.662	-11.936	-0.033

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.005 / 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	4	LEU	0	-0.024	0.003	2.499	-0.811	2.047	0.185	-1.481	-1.562	0.006
4	A	5	PRO	0	0.005	0.004	2.234	-6.802	-5.996	2.455	-1.553	-1.708	-0.021
5	A	6	VAL	0	0.014	-0.004	3.400	0.379	0.614	0.007	-0.054	-0.189	0.000
6	A	7	PRO	0	-0.012	-0.023	5.945	0.177	0.177	0.000	0.000	0.000	0.000
7	A	8	TYR	0	-0.062	-0.022	7.007	-0.277	-0.277	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.001	-0.032	8.713	0.282	0.282	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.854	-0.906	12.368	-0.619	-0.619	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.020	0.001	14.361	0.071	0.071	0.000	0.000	0.000	0.000
11	A	12	ALA	0	-0.002	0.000	17.484	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.028	-0.024	19.493	0.022	0.022	0.000	0.000	0.000	0.000
13	A	14	LEU	0	-0.017	-0.003	19.870	0.003	0.003	0.000	0.000	0.000	0.000
14	A	15	SER	0	0.010	0.008	23.786	0.006	0.006	0.000	0.000	0.000	0.000
15	A	16	THR	0	0.062	0.035	26.140	0.004	0.004	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.035	-0.016	26.701	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.009	0.003	22.132	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.000	-0.016	18.275	0.012	0.012	0.000	0.000	0.000	0.000
19	A	20	VAL	0	0.007	0.019	14.401	-0.023	-0.023	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.039	-0.028	13.050	0.035	0.035	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.011	-0.007	9.057	-0.081	-0.081	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.833	0.917	7.785	-0.482	-0.482	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.096	0.051	4.745	-0.387	-0.368	-0.001	-0.004	-0.014	0.000
24	A	25	ARG	1	0.881	0.949	5.017	-1.243	-1.243	0.000	0.000	0.000	0.000
25	A	26	PRO	0	0.026	0.021	6.179	0.429	0.429	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.020	-0.002	5.358	0.124	0.124	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.035	-0.012	8.364	-0.156	-0.156	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.012	0.003	11.978	0.014	0.014	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.053	-0.009	13.623	-0.033	-0.033	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.014	0.004	17.067	-0.035	-0.035	0.000	0.000	0.000	0.000
31	A	32	ASN	0	-0.028	-0.018	15.975	-0.058	-0.058	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.886	-0.932	17.998	0.187	0.187	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.002	0.026	13.162	-0.015	-0.015	0.000	0.000	0.000	0.000
34	A	35	TYR	0	-0.014	-0.035	14.260	-0.050	-0.050	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.020	-0.008	9.997	0.095	0.095	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.026	-0.027	12.576	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	38	VAL	0	0.003	0.003	12.794	-0.034	-0.034	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.762	-0.857	14.946	-0.028	-0.028	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.031	-0.005	16.548	-0.041	-0.041	0.000	0.000	0.000	0.000
40	A	41	HIS	1	0.845	0.922	17.617	0.181	0.181	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.055	0.015	21.083	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.844	-0.907	23.218	-0.135	-0.135	0.000	0.000	0.000	0.000
43	A	44	MET	0	-0.003	-0.005	17.812	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.877	0.943	19.444	0.124	0.124	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.832	-0.886	16.352	-0.204	-0.204	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.791	-0.909	19.618	-0.132	-0.132	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.072	-0.039	22.058	0.019	0.019	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.764	-0.868	23.293	-0.065	-0.065	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.090	-0.038	20.596	-0.016	-0.016	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.019	0.014	23.315	0.015	0.015	0.000	0.000	0.000	0.000
51	A	52	PHE	0	-0.012	-0.013	20.218	0.016	0.016	0.000	0.000	0.000	0.000
52	A	53	HIS	0	-0.090	-0.034	19.434	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	PHE	0	0.027	0.004	15.853	0.015	0.015	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.004	-0.018	17.099	0.006	0.006	0.000	0.000	0.000	0.000
55	A	56	VAL	0	-0.004	0.011	15.475	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	57	CYS	0	-0.002	0.015	16.794	0.015	0.015	0.000	0.000	0.000	0.000
57	A	58	PHE	0	0.055	0.006	11.703	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.024	-0.006	17.164	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.745	0.855	19.991	-0.256	-0.256	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.818	0.890	21.437	-0.130	-0.130	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.009	0.017	19.472	0.020	0.020	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.009	0.001	21.248	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	64	MET	0	-0.034	-0.007	21.445	0.001	0.001	0.000	0.000	0.000	0.000
64	A	65	ASN	0	0.004	-0.010	23.542	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	66	SER	0	0.017	-0.016	24.395	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.810	0.904	22.059	0.084	0.084	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.792	-0.860	26.616	-0.033	-0.033	0.000	0.000	0.000	0.000
68	A	69	TYR	0	-0.004	-0.023	29.637	0.005	0.005	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.015	0.000	28.027	0.002	0.002	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.006	0.003	28.575	0.004	0.004	0.000	0.000	0.000	0.000
71	A	72	TRP	0	0.010	-0.012	21.501	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.842	0.922	28.466	0.024	0.024	0.000	0.000	0.000	0.000
73	A	74	GLN	0	0.029	0.015	29.909	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	GLN	0	0.011	0.020	26.381	0.000	0.000	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.017	0.015	27.134	0.001	0.001	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.794	-0.886	25.563	0.100	0.100	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.003	-0.003	24.608	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.915	0.936	24.808	-0.108	-0.108	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.018	0.006	23.175	0.019	0.019	0.000	0.000	0.000	0.000
80	A	81	MET	0	-0.007	0.044	18.737	0.018	0.018	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.042	0.035	18.483	0.013	0.013	0.000	0.000	0.000	0.000
82	A	83	PHE	0	-0.001	-0.002	13.484	0.025	0.025	0.000	0.000	0.000	0.000
83	A	84	GLN	0	-0.022	-0.019	14.898	-0.027	-0.027	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.759	-0.884	14.142	0.542	0.542	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.014	0.005	12.176	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	87	GLN	0	-0.032	-0.013	11.202	0.209	0.209	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.912	-0.942	6.510	1.651	1.651	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.019	-0.012	8.643	-0.152	-0.152	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.834	-0.921	9.615	0.348	0.348	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.026	-0.002	12.166	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.010	0.002	14.120	-0.055	-0.055	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.001	0.016	16.375	0.013	0.013	0.000	0.000	0.000	0.000
93	A	94	SER	0	0.012	-0.002	18.966	-0.025	-0.025	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.015	-0.002	22.122	0.006	0.006	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.017	0.018	24.813	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.000	-0.019	28.190	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.831	-0.892	31.016	0.011	0.011	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.911	0.948	27.903	-0.028	-0.028	0.000	0.000	0.000	0.000
99	A	100	TYR	0	0.020	0.013	22.499	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	101	GLN	0	0.022	0.009	23.912	0.013	0.013	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.038	-0.013	18.358	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.012	0.001	18.997	0.008	0.008	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.031	0.001	15.292	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	ASN	0	0.008	-0.003	14.104	0.014	0.014	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.037	0.025	16.580	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	107	GLN	0	0.011	0.015	19.848	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.030	-0.028	21.151	0.003	0.003	0.000	0.000	0.000	0.000
108	A	109	SER	0	-0.038	-0.029	20.822	0.010	0.010	0.000	0.000	0.000	0.000
109	A	110	TYR	0	0.007	-0.036	19.218	0.005	0.005	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.008	0.003	23.878	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.036	-0.018	24.693	0.004	0.004	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.848	-0.932	26.584	0.014	0.014	0.000	0.000	0.000	0.000
113	A	114	HIS	0	-0.059	-0.040	26.223	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.802	0.899	28.752	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.000	0.001	28.652	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.879	0.941	28.641	0.068	0.068	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.074	0.033	25.342	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.810	-0.919	25.631	-0.067	-0.067	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.066	-0.030	27.086	0.000	0.000	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.049	-0.011	20.749	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.825	0.897	22.585	0.130	0.130	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.048	0.004	16.896	-0.030	-0.030	0.000	0.000	0.000	0.000
123	A	124	VAL	0	-0.039	-0.007	14.065	0.047	0.047	0.000	0.000	0.000	0.000
124	A	125	GLN	0	0.037	0.010	13.033	-0.032	-0.032	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.023	-0.016	9.159	0.087	0.087	0.000	0.000	0.000	0.000
126	A	127	TRP	0	-0.017	-0.025	9.240	-0.105	-0.105	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.885	0.957	10.294	-0.069	-0.069	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.792	-0.879	9.291	0.545	0.545	0.000	0.000	0.000	0.000
129	A	130	ILE	0	-0.060	-0.033	5.998	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.007	-0.002	2.309	-2.265	-1.062	2.617	-1.659	-2.162	0.012
131	A	132	LEU	0	-0.008	-0.022	1.908	-4.689	-6.820	7.855	-2.988	-2.736	0.008
132	A	133	THR	0	-0.035	-0.043	1.950	-8.551	-9.722	8.566	-3.881	-3.514	-0.038
133	A	134	LYS	1	0.905	0.950	4.288	-0.328	-0.234	0.000	-0.042	-0.051	0.000
134	A	135	PHE	0	0.038	0.019	7.606	0.025	0.025	0.000	0.000	0.000	0.000
135	A	136	ASN	0	0.000	-0.007	9.876	0.031	0.031	0.000	0.000	0.000	0.000
136	A	137	VAL	0	0.049	0.037	13.591	0.050	0.050	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.007	-0.008	17.112	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	139	TYR	0	0.014	0.015	17.798	0.032	0.032	0.000	0.000	0.000	0.000
139	A	140	LEU	0	-0.007	-0.008	22.052	0.002	0.002	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.888	0.939	25.062	0.033	0.033	0.000	0.000	0.000	0.000
141	A	142	ARG	1	0.921	0.969	26.425	0.072	0.072	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)