FMO DATABASE

FMODB ID: LZ8Z9

Calculation Name: 1LJ9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1LJ9

Chain ID: A

ChEMBL ID:

UniProt ID: Q82ZP8

Base Structure: X-ray

Registration Date: 2023-09-20

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1304683.466553
FMO2-HF: Nuclear repulsion	1246856.89434
FMO2-HF: Total energy	-57826.572212
FMO2-MP2: Total energy	-57997.19224

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:THR)

Summations of interaction energy for fragment #1(A:2: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.
-0.929	2.437	1.194	-1.417	-3.141	-0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / 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

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	ILE	0	0.076	0.018	2.905	-1.776	0.634	0.260	-0.898	-1.772	-0.001
4	A	5	LEU	0	0.045	0.012	4.222	0.600	0.739	-0.001	0.000	-0.138	0.000
5	A	6	ARG	1	0.849	0.929	4.972	0.095	0.095	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.869	-0.941	2.559	-0.957	-0.157	0.936	-0.519	-1.216	-0.004
7	A	8	ILE	0	-0.017	-0.005	5.348	0.351	0.368	-0.001	0.000	-0.015	0.000
8	A	9	GLY	0	-0.012	-0.010	8.292	0.190	0.190	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.073	-0.040	6.201	0.171	0.171	0.000	0.000	0.000	0.000
10	A	11	ILE	0	0.050	0.030	7.641	0.087	0.087	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.011	0.006	11.150	0.061	0.061	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.951	0.971	10.705	0.206	0.206	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.007	0.028	13.742	0.037	0.037	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.052	0.018	15.087	0.023	0.023	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.899	-0.925	17.323	-0.073	-0.073	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.041	-0.047	18.183	0.023	0.023	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.011	0.015	17.770	0.015	0.015	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.023	0.006	21.168	0.003	0.003	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.064	-0.051	22.479	0.001	0.001	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.052	-0.024	23.323	0.008	0.008	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.869	-0.955	25.520	-0.057	-0.057	0.000	0.000	0.000	0.000
22	A	23	PHE	0	0.037	0.018	24.626	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.843	0.900	28.911	0.006	0.006	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.847	-0.917	30.808	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.020	-0.001	30.884	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.108	-0.052	33.094	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.007	-0.013	29.331	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	29	THR	0	0.021	0.038	26.755	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.946	0.954	24.694	0.040	0.040	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.084	0.049	23.833	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.086	-0.047	24.553	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	TYR	0	0.056	0.018	21.286	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.010	0.021	21.604	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.016	-0.012	25.680	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.001	0.010	28.842	0.001	0.001	0.000	0.000	0.000	0.000
36	A	37	VAL	0	0.046	0.021	26.355	0.003	0.003	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.899	0.936	23.385	0.184	0.184	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.045	-0.024	29.415	0.002	0.002	0.000	0.000	0.000	0.000
39	A	40	CYS	0	-0.095	-0.045	32.556	0.007	0.007	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.850	-0.898	27.445	-0.154	-0.154	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.100	-0.046	30.023	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.050	0.015	33.975	0.003	0.003	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.015	0.004	37.401	0.000	0.000	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.036	-0.002	31.378	0.000	0.000	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.028	0.015	35.329	0.006	0.006	0.000	0.000	0.000	0.000
46	A	47	GLN	0	0.023	-0.012	33.632	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.840	-0.903	32.129	-0.105	-0.105	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.998	0.999	30.651	0.128	0.128	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.018	-0.005	28.948	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.004	-0.002	27.473	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.916	-0.947	25.893	-0.172	-0.172	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.048	-0.029	24.938	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.044	-0.029	23.205	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.837	0.945	20.089	0.226	0.226	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.034	0.029	21.723	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.749	-0.857	24.267	-0.090	-0.090	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.890	0.896	27.155	0.109	0.109	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.030	-0.023	30.576	0.007	0.007	0.000	0.000	0.000	0.000
59	A	60	THR	0	-0.014	-0.024	25.513	0.009	0.009	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.013	0.009	28.708	0.004	0.004	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.032	-0.008	29.827	0.005	0.005	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.917	0.958	31.102	0.052	0.052	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.056	0.047	29.031	0.006	0.006	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.010	-0.006	31.154	0.004	0.004	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.872	0.926	33.817	0.045	0.045	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.892	0.940	33.213	0.039	0.039	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.013	-0.001	31.489	0.004	0.004	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.821	-0.872	35.245	-0.050	-0.050	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.843	-0.896	38.396	-0.034	-0.034	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.038	-0.012	35.084	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.059	0.035	38.644	0.001	0.001	0.000	0.000	0.000	0.000
72	A	73	PHE	0	0.007	0.017	35.202	0.000	0.000	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.018	-0.019	34.800	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.002	0.004	38.448	0.004	0.004	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.817	0.866	37.849	0.054	0.054	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.039	0.050	41.711	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.807	-0.899	43.741	-0.049	-0.049	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.776	-0.864	44.613	-0.059	-0.059	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.013	-0.001	46.428	0.002	0.002	0.000	0.000	0.000	0.000
80	A	81	SER	0	0.007	-0.005	48.113	0.002	0.002	0.000	0.000	0.000	0.000
81	A	82	ASN	0	0.008	-0.004	44.684	0.003	0.003	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.927	0.955	45.790	0.041	0.041	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.902	0.939	43.184	0.048	0.048	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.012	0.014	40.469	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.855	0.919	40.125	0.057	0.057	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.834	0.916	39.128	0.062	0.062	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.025	-0.027	34.530	0.005	0.005	0.000	0.000	0.000	0.000
88	A	89	TYR	0	0.009	0.003	37.702	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.065	0.034	36.512	0.003	0.003	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.029	-0.038	38.390	0.001	0.001	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.922	-0.971	40.242	-0.044	-0.044	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.909	0.959	37.577	0.040	0.040	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.022	0.005	36.324	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.912	0.949	35.835	0.054	0.054	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.015	0.005	37.303	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.009	0.010	32.908	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.033	0.017	30.050	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.001	-0.008	31.403	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.002	0.004	30.747	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	101	ILE	0	0.030	0.028	27.087	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.018	0.005	26.885	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.952	0.969	26.646	0.061	0.061	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.869	-0.925	25.696	-0.067	-0.067	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.076	-0.052	22.610	-0.017	-0.017	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.021	-0.010	21.705	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.040	0.027	22.334	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	108	SER	0	0.003	-0.004	19.041	0.004	0.004	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.082	-0.050	17.575	-0.034	-0.034	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.001	0.007	17.492	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.016	-0.006	16.958	0.006	0.006	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.029	-0.016	13.621	0.015	0.015	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.021	-0.011	13.214	-0.018	-0.018	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.043	-0.016	15.134	0.014	0.014	0.000	0.000	0.000	0.000
114	A	115	GLY	0	-0.030	-0.014	14.670	0.008	0.008	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.036	-0.001	11.216	-0.017	-0.017	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.027	-0.052	15.349	0.014	0.014	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.867	-0.947	17.673	-0.270	-0.270	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.044	0.020	18.579	-0.026	-0.026	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.834	-0.882	13.800	-0.348	-0.348	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.017	-0.010	14.586	-0.077	-0.077	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.022	-0.019	16.075	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	123	GLN	0	-0.001	0.005	14.504	-0.087	-0.087	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.008	0.015	10.041	-0.083	-0.083	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.011	-0.006	13.264	-0.047	-0.047	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.935	-0.965	16.244	-0.499	-0.499	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.002	-0.013	11.103	-0.046	-0.046	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.006	-0.004	10.721	-0.035	-0.035	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.042	-0.016	13.860	0.051	0.051	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.924	0.971	15.297	0.522	0.522	0.000	0.000	0.000	0.000
130	A	131	MET	0	0.031	0.014	9.537	-0.016	-0.016	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.995	1.003	14.311	0.397	0.397	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.902	0.962	16.616	0.394	0.394	0.000	0.000	0.000	0.000
133	A	134	ASN	0	0.023	0.007	14.785	0.086	0.086	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.056	0.023	14.019	0.037	0.037	0.000	0.000	0.000	0.000
135	A	136	SER	0	-0.091	-0.063	17.283	0.057	0.057	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.965	-0.985	20.483	-0.213	-0.213	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.849	-0.913	19.133	-0.258	-0.258	0.000	0.000	0.000	0.000
138	A	139	TRP	0	0.004	0.003	20.546	0.034	0.034	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.831	-0.910	22.129	-0.144	-0.144	0.000	0.000	0.000	0.000
140	A	141	PHE	0	0.006	0.005	24.314	0.023	0.023	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.002	-0.003	22.104	0.020	0.020	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.715	0.852	25.315	0.186	0.186	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.770	0.895	27.674	0.160	0.160	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.011	0.021	29.906	0.008	0.008	0.000	0.000	0.000	0.000

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