FMO DATABASE

FMODB ID: 98452

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	OptHSide
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	-1154779.078738
FMO2-HF: Nuclear repulsion	1105245.588172
FMO2-HF: Total energy	-49533.490566
FMO2-MP2: Total energy	-49682.025219

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.
-20.538	-12.015	9.554	-7.7	-10.376	-0.055

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 : -0.026 / 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

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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	0.037	0.007	1.988	-1.738	0.818	2.381	-2.249	-2.688	0.001
4	A	4	THR	0	0.024	0.023	2.927	-1.444	-0.081	0.532	-0.549	-1.346	-0.006
5	A	5	VAL	0	-0.053	-0.043	4.415	0.085	0.135	-0.001	-0.010	-0.039	0.000
6	A	6	LEU	0	-0.022	-0.007	7.981	0.027	0.027	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.008	0.002	10.871	0.013	0.013	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.038	-0.012	13.681	0.027	0.027	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.772	-0.914	17.010	-0.186	-0.186	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.063	0.028	19.584	0.000	0.000	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.091	-0.029	22.148	0.009	0.009	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.812	-0.900	19.009	-0.184	-0.184	0.000	0.000	0.000	0.000
13	A	13	TYR	0	0.037	0.011	19.283	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.861	-0.913	20.488	-0.219	-0.219	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.785	0.879	15.619	0.189	0.189	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.804	-0.905	15.121	-0.381	-0.381	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.785	0.880	16.149	0.183	0.183	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.071	-0.059	13.689	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.814	0.887	11.197	0.341	0.341	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.037	0.034	12.115	-0.072	-0.072	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.066	-0.023	13.915	-0.024	-0.024	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.032	-0.047	8.687	0.065	0.065	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.871	-0.917	9.911	-0.881	-0.881	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.118	-0.064	11.562	-0.025	-0.025	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.140	-0.072	9.984	0.043	0.043	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.035	0.007	7.652	0.098	0.098	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.931	-0.942	2.065	-12.965	-11.159	4.708	-3.106	-3.408	-0.039
28	A	28	TYR	0	-0.062	-0.027	3.189	-2.028	-0.866	0.129	-0.757	-0.534	-0.006
29	A	29	ASP	-1	-0.897	-0.949	2.273	-2.519	-1.048	1.804	-0.999	-2.275	-0.005
30	A	30	PHE	0	0.010	-0.004	4.196	0.077	0.192	0.001	-0.030	-0.086	0.000
31	A	31	ILE	0	0.014	0.012	7.334	0.094	0.094	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.783	-0.864	9.752	-0.307	-0.307	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.053	-0.038	13.319	0.039	0.039	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.772	-0.880	16.390	-0.123	-0.123	0.000	0.000	0.000	0.000
35	A	35	ASN	0	0.015	-0.001	19.573	0.014	0.014	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.073	0.025	21.202	0.001	0.001	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.863	0.930	22.638	0.048	0.048	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.914	0.953	15.596	0.127	0.127	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.075	0.026	17.389	0.004	0.004	0.000	0.000	0.000	0.000
40	A	40	TYR	0	-0.031	-0.029	18.879	0.007	0.007	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.092	-0.038	19.952	0.010	0.010	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.070	0.043	13.713	0.006	0.006	0.000	0.000	0.000	0.000
43	A	43	PHE	0	0.017	0.024	16.004	0.008	0.008	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.814	0.894	16.851	0.013	0.013	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.886	-0.943	14.672	0.040	0.040	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.084	-0.029	11.769	0.012	0.012	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.870	-0.957	10.868	0.103	0.103	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.080	-0.027	8.430	0.020	0.020	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.025	0.031	7.529	-0.030	-0.030	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.007	0.003	6.113	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.019	-0.020	8.920	0.020	0.020	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.016	0.021	10.600	-0.018	-0.018	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.008	0.010	12.727	0.017	0.017	0.000	0.000	0.000	0.000
54	A	54	MET	0	0.000	0.000	15.400	0.008	0.008	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.686	-0.807	18.424	-0.148	-0.148	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.012	-0.028	21.882	0.009	0.009	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.009	0.019	24.367	0.012	0.012	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.030	0.007	20.239	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.007	-0.010	24.921	0.006	0.006	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.040	0.005	27.198	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.787	-0.880	28.148	-0.086	-0.086	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.774	0.872	28.461	0.052	0.052	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.864	-0.921	27.186	-0.057	-0.057	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.051	0.023	24.182	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.058	-0.036	24.152	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.874	-0.912	25.893	-0.051	-0.051	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.000	0.008	20.491	0.004	0.004	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.002	-0.006	21.397	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.005	-0.001	22.175	0.003	0.003	0.000	0.000	0.000	0.000
70	A	70	ALA	0	-0.005	-0.001	22.373	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.000	-0.009	17.131	0.006	0.006	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.758	0.866	17.849	0.122	0.122	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.061	-0.036	21.648	0.011	0.011	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.007	0.020	17.343	0.024	0.024	0.000	0.000	0.000	0.000
75	A	75	SER	0	0.046	-0.006	19.486	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.880	0.933	14.590	-0.052	-0.052	0.000	0.000	0.000	0.000
77	A	77	THR	0	0.003	0.017	13.782	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.019	0.018	16.094	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.039	-0.031	17.647	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.018	0.031	12.393	0.001	0.001	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.018	0.024	13.219	0.017	0.017	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.038	0.011	14.627	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.013	-0.009	15.049	0.017	0.017	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.014	0.009	18.036	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.011	0.011	19.718	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.043	-0.065	21.491	0.005	0.005	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.897	0.942	24.615	0.120	0.120	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.062	-0.047	27.631	0.008	0.008	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.913	-0.970	29.122	-0.102	-0.102	0.000	0.000	0.000	0.000
90	A	90	ASN	0	0.026	0.029	31.762	0.006	0.006	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.029	-0.007	32.600	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.022	0.009	33.720	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	TYR	0	0.029	0.006	30.404	0.002	0.002	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.971	1.007	27.669	0.115	0.115	0.000	0.000	0.000	0.000
95	A	95	HIS	0	0.024	0.009	29.306	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.014	-0.021	31.168	0.001	0.001	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.004	0.006	25.729	0.002	0.002	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.039	-0.025	26.114	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.848	0.945	27.712	0.063	0.063	0.000	0.000	0.000	0.000
100	A	100	PHE	0	-0.004	0.017	24.349	0.005	0.005	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.968	0.979	23.184	0.062	0.062	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.036	0.010	20.831	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.027	-0.018	18.443	0.005	0.005	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.735	-0.810	20.317	-0.200	-0.200	0.000	0.000	0.000	0.000
105	A	105	TYR	0	0.005	0.000	21.942	0.004	0.004	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.078	-0.040	19.952	0.007	0.007	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.025	0.021	23.978	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.791	0.911	21.465	0.181	0.181	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.010	-0.027	26.086	0.012	0.012	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.064	0.027	19.624	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	PRO	0	0.030	0.031	24.017	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	112	THR	0	0.065	0.034	20.143	0.004	0.004	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.957	0.965	20.120	0.204	0.204	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.777	0.850	21.064	0.185	0.185	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.039	0.013	15.888	0.011	0.011	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.734	-0.835	15.842	-0.441	-0.441	0.000	0.000	0.000	0.000
117	A	117	ASN	0	-0.023	-0.013	16.515	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.034	-0.032	18.164	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.052	0.022	11.728	0.022	0.022	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.877	0.921	13.960	0.512	0.512	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.041	-0.007	15.456	0.031	0.031	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.036	-0.036	14.957	0.015	0.015	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.028	-0.018	9.613	0.046	0.046	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.793	0.925	13.278	0.247	0.247	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.020	0.016	11.993	-0.020	-0.020	0.000	0.000	0.000	0.000

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