FMO DATABASE

FMODB ID: 39Y9L

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1304272.113113
FMO2-HF: Nuclear repulsion	1246446.596474
FMO2-HF: Total energy	-57825.516639
FMO2-MP2: Total energy	-57996.205028

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.
-0.534	3.766	1.613	-2.039	-3.875	-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 : 0.053 / q_NPA : 0.024

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	0.074	0.015	2.759	-1.924	0.947	0.497	-1.176	-2.192	0.003
4	A	5	LEU	0	0.043	0.010	3.730	0.764	0.874	0.001	0.050	-0.161	0.000
5	A	6	ARG	1	0.929	0.977	5.069	1.174	1.174	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.889	-0.949	2.594	-3.499	-2.180	1.115	-0.913	-1.522	-0.008
7	A	8	ILE	0	-0.002	0.005	5.530	0.598	0.598	0.000	0.000	0.000	0.000
8	A	9	GLY	0	-0.022	-0.019	8.221	0.317	0.317	0.000	0.000	0.000	0.000
9	A	10	MET	0	-0.060	-0.035	6.096	0.346	0.346	0.000	0.000	0.000	0.000
10	A	11	ILE	0	0.053	0.032	7.640	0.203	0.203	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.005	0.001	11.260	0.149	0.149	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.948	0.969	11.032	0.827	0.827	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.013	0.025	13.631	0.086	0.086	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.032	0.005	14.991	0.068	0.068	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.939	-0.960	17.362	-0.288	-0.288	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.031	-0.036	18.431	0.055	0.055	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.004	0.013	17.819	0.037	0.037	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.031	0.019	21.325	0.032	0.032	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.035	-0.026	23.073	0.027	0.027	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.061	-0.026	23.402	0.023	0.023	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.847	-0.948	25.523	-0.180	-0.180	0.000	0.000	0.000	0.000
22	A	23	PHE	0	0.026	0.020	24.967	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.858	0.921	28.940	0.122	0.122	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.888	-0.954	30.871	-0.101	-0.101	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.016	0.006	30.742	0.005	0.005	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.121	-0.056	33.336	0.000	0.000	0.000	0.000	0.000	0.000
27	A	28	LEU	0	0.010	-0.004	29.334	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	29	THR	0	0.024	0.033	26.925	-0.018	-0.018	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.935	0.948	24.883	0.201	0.201	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.079	0.045	23.888	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.066	-0.036	24.610	-0.014	-0.014	0.000	0.000	0.000	0.000
32	A	33	TYR	0	0.085	0.032	21.025	0.008	0.008	0.000	0.000	0.000	0.000
33	A	34	LEU	0	-0.009	0.011	21.532	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.015	-0.009	25.625	0.002	0.002	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.001	0.012	28.753	0.009	0.009	0.000	0.000	0.000	0.000
36	A	37	VAL	0	0.036	0.016	26.419	0.011	0.011	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.967	0.985	22.726	0.352	0.352	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.025	-0.007	29.239	0.009	0.009	0.000	0.000	0.000	0.000
39	A	40	CYS	0	-0.078	-0.034	32.429	0.015	0.015	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.915	-0.951	27.596	-0.272	-0.272	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.144	-0.066	29.735	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.037	0.009	33.730	0.003	0.003	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.017	0.000	37.184	0.003	0.003	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.024	0.001	31.185	0.001	0.001	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.016	0.015	34.997	0.006	0.006	0.000	0.000	0.000	0.000
46	A	47	GLN	0	0.030	-0.012	33.306	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.897	-0.955	31.894	-0.213	-0.213	0.000	0.000	0.000	0.000
48	A	49	LYS	1	1.045	1.022	30.622	0.215	0.215	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.020	-0.006	28.970	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.006	-0.006	27.256	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.917	-0.943	25.633	-0.305	-0.305	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.068	-0.051	24.607	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.040	-0.027	22.860	-0.030	-0.030	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.861	0.958	19.569	0.406	0.406	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.034	0.031	21.498	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.738	-0.812	24.071	-0.253	-0.253	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.932	0.925	26.954	0.225	0.225	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.015	-0.003	30.355	0.015	0.015	0.000	0.000	0.000	0.000
59	A	60	THR	0	-0.033	-0.076	25.506	0.015	0.015	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.028	0.014	28.583	0.007	0.007	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.033	-0.008	29.703	0.012	0.012	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.894	0.948	30.990	0.175	0.175	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.063	0.049	28.993	0.011	0.011	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.016	-0.004	31.128	0.010	0.010	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.933	0.967	33.747	0.147	0.147	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.934	0.982	33.242	0.146	0.146	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.016	-0.002	31.514	0.008	0.008	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.904	-0.949	35.252	-0.125	-0.125	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.925	-0.964	38.520	-0.122	-0.122	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.062	-0.030	34.636	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.058	0.031	38.718	0.002	0.002	0.000	0.000	0.000	0.000
72	A	73	PHE	0	0.001	0.019	35.184	0.002	0.002	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.023	-0.021	34.854	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.015	0.011	38.388	0.005	0.005	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.883	0.934	37.917	0.137	0.137	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.059	0.038	41.571	0.004	0.004	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.898	-0.971	43.534	-0.113	-0.113	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.838	-0.912	44.312	-0.115	-0.115	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.005	0.005	46.169	0.002	0.002	0.000	0.000	0.000	0.000
80	A	81	SER	0	0.016	0.020	48.052	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	ASN	0	0.009	-0.001	43.957	0.004	0.004	0.000	0.000	0.000	0.000
82	A	83	LYS	1	1.013	1.029	45.525	0.102	0.102	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.869	0.910	42.976	0.112	0.112	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.003	0.019	40.254	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.884	0.938	39.894	0.133	0.133	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.840	0.924	38.904	0.119	0.119	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.020	-0.022	34.667	0.008	0.008	0.000	0.000	0.000	0.000
88	A	89	TYR	0	0.005	0.020	37.517	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.055	0.031	36.465	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.035	-0.043	38.296	0.005	0.005	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.923	-0.971	40.197	-0.101	-0.101	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.920	0.967	37.813	0.120	0.120	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.019	0.004	36.323	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.926	0.956	35.817	0.113	0.113	0.000	0.000	0.000	0.000
95	A	96	ASN	0	0.030	0.010	37.155	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.008	0.013	32.829	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.023	0.009	30.061	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	99	PRO	0	-0.014	-0.014	31.266	-0.012	-0.012	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.009	0.011	30.549	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	101	ILE	0	0.019	0.018	26.957	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.044	-0.015	26.768	-0.018	-0.018	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.944	0.959	26.531	0.138	0.138	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.866	-0.919	25.577	-0.195	-0.195	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.023	-0.020	22.513	-0.028	-0.028	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.030	-0.020	21.608	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.050	0.032	22.272	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.005	-0.009	18.964	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.080	-0.042	17.499	-0.079	-0.079	0.000	0.000	0.000	0.000
109	A	110	GLN	0	0.010	0.014	17.450	-0.026	-0.026	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.018	-0.009	16.925	0.005	0.005	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.033	-0.019	13.541	0.000	0.000	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.018	-0.010	13.231	-0.070	-0.070	0.000	0.000	0.000	0.000
113	A	114	GLN	0	-0.055	-0.023	15.132	0.085	0.085	0.000	0.000	0.000	0.000
114	A	115	GLY	0	-0.027	-0.013	14.768	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.021	0.005	11.262	0.012	0.012	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.019	-0.012	15.390	0.024	0.024	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.877	-0.957	17.645	-0.278	-0.278	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.052	0.023	18.230	-0.033	-0.033	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.852	-0.928	13.745	-0.297	-0.297	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.008	-0.003	14.483	-0.110	-0.110	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.018	-0.010	15.977	-0.060	-0.060	0.000	0.000	0.000	0.000
122	A	123	GLN	0	-0.028	-0.011	14.565	-0.049	-0.049	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.010	0.017	9.963	-0.099	-0.099	0.000	0.000	0.000	0.000
124	A	125	ALA	0	-0.012	-0.007	13.080	-0.084	-0.084	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.932	-0.967	16.027	-0.546	-0.546	0.000	0.000	0.000	0.000
126	A	127	TYR	0	0.024	0.006	11.289	-0.033	-0.033	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.002	-0.011	10.139	-0.075	-0.075	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.043	-0.014	13.394	0.041	0.041	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.953	0.977	14.984	0.586	0.586	0.000	0.000	0.000	0.000
130	A	131	MET	0	0.013	0.011	9.492	-0.045	-0.045	0.000	0.000	0.000	0.000
131	A	132	ARG	1	1.000	1.007	13.756	0.569	0.569	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.888	0.949	16.145	0.495	0.495	0.000	0.000	0.000	0.000
133	A	134	ASN	0	0.023	0.017	14.486	0.126	0.126	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.042	0.018	13.563	0.039	0.039	0.000	0.000	0.000	0.000
135	A	136	SER	0	-0.113	-0.079	16.803	0.065	0.065	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.932	-0.971	20.033	-0.370	-0.370	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.828	-0.901	18.738	-0.515	-0.515	0.000	0.000	0.000	0.000
138	A	139	TRP	0	-0.051	-0.021	20.242	0.043	0.043	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.901	-0.961	21.730	-0.283	-0.283	0.000	0.000	0.000	0.000
140	A	141	PHE	0	-0.003	0.005	23.879	0.039	0.039	0.000	0.000	0.000	0.000
141	A	142	VAL	0	-0.003	-0.006	21.762	0.029	0.029	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.754	0.879	24.925	0.349	0.349	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.844	0.939	27.315	0.262	0.262	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.009	0.020	29.538	0.018	0.018	0.000	0.000	0.000	0.000

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