FMO DATABASE

FMODB ID: 94J42

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:

Apendix: None

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1307864.769519
FMO2-HF: Nuclear repulsion	1250037.973484
FMO2-HF: Total energy	-57826.796035
FMO2-MP2: Total energy	-57997.344817

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.
-2.043	0.944	0.82	-0.981	-2.827	-0.002

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 : 0.022 / q_NPA : -0.004

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	0.055	0.012	2.749	-1.739	0.383	0.357	-0.683	-1.797	0.000
4	A	5	LEU	0	0.022	0.011	4.036	0.555	0.693	0.000	0.003	-0.141	0.000
5	A	6	ARG	1	0.824	0.906	5.034	0.013	0.013	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.856	-0.932	2.758	-2.421	-1.694	0.463	-0.301	-0.889	-0.002
7	A	8	ILE	0	0.003	0.005	5.625	0.423	0.423	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.005	0.002	8.404	0.244	0.244	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.095	-0.055	6.529	0.322	0.322	0.000	0.000	0.000	0.000
10	A	11	ILE	0	0.052	0.029	7.931	0.148	0.148	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.005	0.006	11.374	0.124	0.124	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.942	0.969	10.962	0.510	0.510	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.006	0.029	13.975	0.074	0.074	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.033	0.014	15.121	0.052	0.052	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.820	-0.920	17.499	-0.218	-0.218	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.065	-0.057	18.255	0.053	0.053	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.028	0.023	18.219	0.033	0.033	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.036	0.020	21.645	0.028	0.028	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.061	-0.061	22.222	0.041	0.041	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.057	-0.021	23.470	0.024	0.024	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.879	-0.942	25.857	-0.209	-0.209	0.000	0.000	0.000	0.000
22	A	23	PHE	0	0.014	-0.010	24.495	0.014	0.014	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.842	0.903	28.932	0.131	0.131	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.808	-0.895	30.820	-0.110	-0.110	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.022	-0.003	30.605	0.006	0.006	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.086	-0.039	33.010	0.005	0.005	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.040	-0.027	29.483	0.001	0.001	0.000	0.000	0.000	0.000
28	A	29	THR	0	0.031	0.034	26.773	-0.015	-0.015	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.956	0.965	24.435	0.139	0.139	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.037	0.026	23.681	0.006	0.006	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.086	-0.044	24.380	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	33	TYR	0	0.048	0.021	21.150	0.000	0.000	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.016	0.023	21.487	0.001	0.001	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.020	-0.001	25.640	0.003	0.003	0.000	0.000	0.000	0.000
35	A	36	LEU	0	0.002	0.011	28.836	0.008	0.008	0.000	0.000	0.000	0.000
36	A	37	VAL	0	0.029	0.013	26.131	0.009	0.009	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.853	0.905	23.599	0.307	0.307	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.052	-0.032	29.355	0.008	0.008	0.000	0.000	0.000	0.000
39	A	40	CYS	0	-0.083	-0.037	32.401	0.013	0.013	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.830	-0.894	27.049	-0.270	-0.270	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.081	-0.029	29.896	0.004	0.004	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.044	0.014	33.878	0.007	0.007	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.039	0.020	37.353	0.004	0.004	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.052	-0.016	31.229	0.004	0.004	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.026	0.016	35.203	0.005	0.005	0.000	0.000	0.000	0.000
46	A	47	GLN	0	0.023	-0.014	33.898	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.843	-0.899	32.438	-0.129	-0.129	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.965	0.979	30.413	0.184	0.184	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.028	-0.012	28.916	-0.015	-0.015	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.018	0.004	27.406	-0.015	-0.015	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.933	-0.959	25.689	-0.214	-0.214	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.021	-0.020	24.851	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.034	-0.012	22.837	-0.026	-0.026	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.843	0.946	20.098	0.271	0.271	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.037	0.038	21.493	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.704	-0.832	24.081	-0.122	-0.122	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.878	0.901	27.031	0.131	0.131	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.043	-0.034	30.569	0.006	0.006	0.000	0.000	0.000	0.000
59	A	60	THR	0	-0.038	-0.041	25.477	0.005	0.005	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.014	0.015	28.672	0.000	0.000	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.032	-0.014	29.830	0.004	0.004	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.916	0.957	31.284	0.092	0.092	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.062	0.047	29.025	0.005	0.005	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.017	0.003	31.133	0.003	0.003	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.825	0.902	33.927	0.092	0.092	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.893	0.932	33.276	0.105	0.105	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.005	-0.003	31.358	0.003	0.003	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.829	-0.879	35.179	-0.094	-0.094	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.847	-0.899	38.159	-0.085	-0.085	0.000	0.000	0.000	0.000
70	A	71	GLN	0	0.016	0.022	35.417	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.040	0.030	38.640	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	73	PHE	0	0.008	0.009	34.814	0.000	0.000	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.031	-0.018	34.893	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.004	0.009	38.473	0.006	0.006	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.807	0.857	37.787	0.097	0.097	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.060	0.059	41.567	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.782	-0.882	43.425	-0.076	-0.076	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.793	-0.864	44.618	-0.084	-0.084	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.001	-0.003	46.488	0.003	0.003	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.001	-0.009	47.979	0.004	0.004	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.002	-0.014	44.722	0.004	0.004	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.917	0.946	45.785	0.063	0.063	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.910	0.953	43.038	0.064	0.064	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.008	0.007	40.631	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.863	0.917	39.983	0.087	0.087	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.836	0.910	38.939	0.093	0.093	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.019	-0.016	34.425	0.006	0.006	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.007	-0.001	37.814	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.067	0.034	36.432	0.003	0.003	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.022	-0.043	38.344	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.907	-0.939	40.391	-0.103	-0.103	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.918	0.971	37.355	0.111	0.111	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.031	0.004	36.219	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.859	0.907	35.818	0.110	0.110	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.008	0.006	37.346	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.009	0.009	33.019	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.036	0.016	29.800	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.005	-0.014	31.307	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.032	-0.004	30.737	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	101	ILE	0	0.017	0.018	26.968	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.006	0.007	26.703	-0.023	-0.023	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.963	0.992	26.387	0.168	0.168	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.835	-0.914	25.589	-0.256	-0.256	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.072	-0.035	22.441	-0.050	-0.050	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.016	-0.005	21.561	-0.031	-0.031	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.043	0.027	22.049	-0.045	-0.045	0.000	0.000	0.000	0.000
107	A	108	SER	0	0.000	-0.018	19.139	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.083	-0.053	17.492	-0.093	-0.093	0.000	0.000	0.000	0.000
109	A	110	GLN	0	-0.016	-0.005	17.459	-0.039	-0.039	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.024	-0.015	16.962	-0.023	-0.023	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.029	-0.013	13.615	-0.031	-0.031	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.019	-0.003	13.020	-0.130	-0.130	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.066	-0.036	15.070	0.073	0.073	0.000	0.000	0.000	0.000
114	A	115	GLY	0	-0.008	0.000	14.970	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.034	0.001	11.365	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.030	-0.052	15.504	0.082	0.082	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.844	-0.922	17.464	-0.470	-0.470	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.049	0.031	18.451	-0.038	-0.038	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.838	-0.874	13.575	-0.798	-0.798	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.006	0.000	14.345	-0.104	-0.104	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.036	-0.054	15.981	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	123	GLN	0	-0.024	-0.004	14.367	-0.032	-0.032	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.007	0.011	9.861	-0.056	-0.056	0.000	0.000	0.000	0.000
124	A	125	ALA	0	0.003	0.003	13.146	-0.032	-0.032	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.922	-0.959	16.233	-0.548	-0.548	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.008	-0.018	11.083	0.007	0.007	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.005	0.003	10.652	-0.017	-0.017	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.040	-0.021	13.499	0.087	0.087	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.900	0.944	15.265	0.514	0.514	0.000	0.000	0.000	0.000
130	A	131	MET	0	0.008	0.000	9.067	0.017	0.017	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.990	0.998	13.843	0.543	0.543	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.909	0.962	16.209	0.471	0.471	0.000	0.000	0.000	0.000
133	A	134	ASN	0	0.036	0.022	14.745	0.098	0.098	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.050	0.022	13.912	0.049	0.049	0.000	0.000	0.000	0.000
135	A	136	SER	0	-0.090	-0.061	17.178	0.049	0.049	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.965	-0.976	20.408	-0.173	-0.173	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.858	-0.918	18.984	-0.204	-0.204	0.000	0.000	0.000	0.000
138	A	139	TRP	0	0.021	0.012	20.334	0.031	0.031	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.815	-0.909	22.000	-0.174	-0.174	0.000	0.000	0.000	0.000
140	A	141	PHE	0	0.027	0.011	24.186	0.023	0.023	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.026	0.012	22.046	0.020	0.020	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.700	0.836	25.242	0.209	0.209	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.780	0.898	27.629	0.160	0.160	0.000	0.000	0.000	0.000
144	A	145	GLY	0	-0.007	0.019	29.407	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:2:THR)