FMO DATABASE

FMODB ID: LNZ59

Calculation Name: 3LUA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3LUA

Chain ID: A

ChEMBL ID:

UniProt ID: A3DK02

Base Structure: X-ray

Registration Date: 2023-09-21

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	125
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1154369.964029
FMO2-HF: Nuclear repulsion	1104837.604607
FMO2-HF: Total energy	-49532.359421
FMO2-MP2: Total energy	-49680.981381

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:-1:LEU)

Summations of interaction energy for fragment #1(A:-1:LEU)

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.
-15.758	-7.873	7.105	-6.219	-8.77	-0.024

Interaction energy analysis for fragmet #1(A:-1:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.006

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

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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	3	GLY	0	0.064	0.006	1.865	-1.448	-0.607	5.039	-2.764	-3.117	0.005
4	A	4	THR	0	0.027	0.021	3.023	-1.766	-0.610	0.453	-0.371	-1.237	-0.005
5	A	5	VAL	0	-0.032	-0.039	4.380	0.224	0.270	0.000	-0.011	-0.034	0.000
6	A	6	LEU	0	-0.034	-0.015	7.965	-0.023	-0.023	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.003	-0.003	10.948	0.046	0.046	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.029	-0.008	13.771	0.019	0.019	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.784	-0.927	17.116	-0.218	-0.218	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.070	0.048	19.744	-0.008	-0.008	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.084	-0.035	22.277	0.010	0.010	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.870	-0.938	19.170	-0.263	-0.263	0.000	0.000	0.000	0.000
13	A	13	TYR	0	0.017	0.006	19.517	-0.021	-0.021	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.927	-0.972	20.656	-0.240	-0.240	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.845	0.902	15.788	0.285	0.285	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.786	-0.904	15.607	-0.453	-0.453	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.836	0.927	16.401	0.205	0.205	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.062	-0.049	13.620	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.850	0.924	11.170	0.517	0.517	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.044	0.039	12.123	-0.056	-0.056	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.070	-0.024	13.943	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.051	-0.057	8.772	0.060	0.060	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.863	-0.913	9.955	-0.770	-0.770	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.104	-0.050	11.624	0.016	0.016	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.138	-0.068	10.169	0.055	0.055	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.033	0.005	7.637	0.113	0.113	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.949	-0.953	3.063	-3.980	-2.741	0.090	-0.522	-0.807	-0.002
28	A	28	TYR	0	-0.053	-0.009	3.236	-2.077	-0.845	0.118	-0.748	-0.601	-0.005
29	A	29	ASP	-1	-0.883	-0.938	2.336	-7.276	-3.972	1.406	-1.791	-2.919	-0.017
30	A	30	PHE	0	0.000	-0.015	4.371	0.472	0.539	-0.001	-0.012	-0.055	0.000
31	A	31	ILE	0	0.003	0.008	7.682	0.085	0.085	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.815	-0.893	9.995	-0.404	-0.404	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.050	-0.031	13.544	0.039	0.039	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.816	-0.921	16.604	-0.225	-0.225	0.000	0.000	0.000	0.000
35	A	35	ASN	0	0.033	-0.001	19.792	0.016	0.016	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.080	0.025	21.413	-0.006	-0.006	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.818	0.905	22.847	0.109	0.109	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.983	1.012	15.615	0.266	0.266	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.077	0.029	17.425	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	TYR	0	-0.021	-0.019	19.084	0.002	0.002	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.088	-0.051	19.702	0.009	0.009	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.073	0.053	14.016	0.002	0.002	0.000	0.000	0.000	0.000
43	A	43	PHE	0	0.047	0.023	16.021	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.763	0.853	16.991	0.072	0.072	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.870	-0.927	14.414	-0.072	-0.072	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.102	-0.011	12.169	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.882	-0.953	10.684	0.051	0.051	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.071	-0.029	8.233	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.011	0.027	7.482	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.029	-0.004	5.778	0.026	0.026	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.013	-0.026	8.714	0.045	0.045	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.010	0.026	10.530	-0.049	-0.049	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.008	0.010	12.991	0.035	0.035	0.000	0.000	0.000	0.000
54	A	54	MET	0	0.001	-0.004	15.355	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.751	-0.866	18.434	-0.165	-0.165	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.057	-0.042	21.906	0.006	0.006	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.023	0.006	24.386	0.012	0.012	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.027	0.004	20.391	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	59	PRO	0	-0.008	-0.018	25.026	0.004	0.004	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.043	0.013	27.325	0.002	0.002	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.832	-0.936	28.193	-0.109	-0.109	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.860	0.941	28.500	0.074	0.074	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.903	-0.948	27.160	-0.093	-0.093	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.040	0.014	24.252	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.055	-0.032	24.189	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.910	-0.946	25.912	-0.083	-0.083	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.008	0.015	20.562	0.002	0.002	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.002	-0.011	21.249	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.035	-0.012	22.165	0.004	0.004	0.000	0.000	0.000	0.000
70	A	70	ALA	0	0.011	-0.003	22.331	0.006	0.006	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.015	-0.013	17.011	0.004	0.004	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.762	0.870	17.848	0.143	0.143	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.057	-0.028	21.603	0.017	0.017	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.037	0.058	17.509	0.032	0.032	0.000	0.000	0.000	0.000
75	A	75	SER	0	0.035	-0.008	19.471	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.857	0.908	14.900	0.045	0.045	0.000	0.000	0.000	0.000
77	A	77	THR	0	0.012	0.002	13.983	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.031	0.014	16.059	-0.014	-0.014	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.052	-0.040	17.354	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.015	0.028	12.225	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.006	0.013	13.029	0.011	0.011	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.059	0.017	14.478	-0.029	-0.029	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.010	-0.007	15.135	0.025	0.025	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.009	0.005	18.048	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.009	0.012	19.819	0.008	0.008	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.004	-0.021	21.557	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.887	0.924	24.594	0.143	0.143	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.042	0.007	27.631	0.012	0.012	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.897	-0.971	29.086	-0.106	-0.106	0.000	0.000	0.000	0.000
90	A	90	ASN	0	0.034	0.030	31.748	0.007	0.007	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.034	-0.003	32.546	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.022	0.006	33.637	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	TYR	0	0.048	0.018	30.375	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.985	1.014	28.424	0.113	0.113	0.000	0.000	0.000	0.000
95	A	95	HIS	0	-0.032	-0.028	29.208	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.011	-0.019	31.062	0.002	0.002	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.008	0.004	25.672	0.001	0.001	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.034	-0.022	26.035	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.887	0.971	27.584	0.071	0.071	0.000	0.000	0.000	0.000
100	A	100	PHE	0	0.008	0.021	24.231	0.006	0.006	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.968	0.978	23.056	0.066	0.066	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.029	0.026	20.676	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.022	-0.015	17.893	0.016	0.016	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.768	-0.857	20.427	-0.181	-0.181	0.000	0.000	0.000	0.000
105	A	105	TYR	0	-0.019	-0.010	21.964	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.094	-0.049	20.026	0.010	0.010	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.033	0.019	24.010	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.886	0.988	20.981	0.225	0.225	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.004	-0.030	26.118	0.012	0.012	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.085	0.041	19.382	0.009	0.009	0.000	0.000	0.000	0.000
111	A	111	PRO	0	0.011	0.030	24.004	-0.010	-0.010	0.000	0.000	0.000	0.000
112	A	112	THR	0	0.119	0.038	20.208	0.006	0.006	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.922	0.959	20.103	0.173	0.173	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.815	0.884	20.979	0.172	0.172	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.034	0.014	16.040	0.014	0.014	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.778	-0.864	16.102	-0.337	-0.337	0.000	0.000	0.000	0.000
117	A	117	ASN	0	-0.004	0.006	16.415	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.025	-0.004	18.067	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.042	0.022	11.754	0.021	0.021	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.918	0.936	13.955	0.383	0.383	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.079	-0.049	15.333	0.035	0.035	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.080	-0.056	14.863	0.020	0.020	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.024	-0.007	9.483	0.030	0.030	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.883	0.966	13.158	0.155	0.155	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.014	0.012	11.994	-0.013	-0.013	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:LEU)