FMO DATABASE

FMODB ID: 3QL5L

Calculation Name: 3LRX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3LRX

Chain ID: A

ChEMBL ID:

UniProt ID: Q8TZS3

Base Structure: X-ray

Registration Date: 2023-06-19

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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1187269.807653
FMO2-HF: Nuclear repulsion	1135273.919589
FMO2-HF: Total energy	-51995.888064
FMO2-MP2: Total energy	-52147.827906

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:88:GLY)

Summations of interaction energy for fragment #1(A:88:GLY)

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.
0.877	1.768	-0.003	-0.368	-0.52	0

Interaction energy analysis for fragmet #1(A:88:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.003 / q_NPA : -0.013

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].
3	A	90	LEU	0	0.001	-0.003	3.654	1.310	2.201	-0.003	-0.368	-0.520
4	A	91	GLY	0	0.022	0.020	6.300	0.189	0.189	0.000	0.000	0.000
5	A	92	THR	0	-0.038	-0.031	9.839	-0.174	-0.174	0.000	0.000	0.000
6	A	93	PRO	0	-0.054	0.001	10.478	0.124	0.124	0.000	0.000	0.000
7	A	94	VAL	0	-0.016	-0.029	12.567	0.041	0.041	0.000	0.000	0.000
8	A	95	PRO	0	0.002	0.020	16.199	0.003	0.003	0.000	0.000	0.000
9	A	96	MET	0	-0.006	-0.012	17.628	0.028	0.028	0.000	0.000	0.000
10	A	97	GLU	-1	-0.927	-0.952	20.600	-0.165	-0.165	0.000	0.000	0.000
11	A	98	LYS	1	0.900	0.948	24.221	0.082	0.082	0.000	0.000	0.000
12	A	99	PHE	0	-0.003	-0.015	22.592	-0.003	-0.003	0.000	0.000	0.000
13	A	100	GLY	0	0.046	0.035	27.974	0.006	0.006	0.000	0.000	0.000
14	A	101	LYS	1	0.853	0.955	29.663	0.068	0.068	0.000	0.000	0.000
15	A	102	ILE	0	-0.016	-0.005	24.451	-0.007	-0.007	0.000	0.000	0.000
16	A	103	LEU	0	0.024	0.025	27.731	0.009	0.009	0.000	0.000	0.000
17	A	104	ALA	0	-0.019	-0.015	23.005	-0.015	-0.015	0.000	0.000	0.000
18	A	105	ILE	0	0.010	-0.003	23.983	0.018	0.018	0.000	0.000	0.000
19	A	106	GLY	0	0.033	0.001	21.571	-0.023	-0.023	0.000	0.000	0.000
20	A	107	ALA	0	-0.014	0.004	21.913	0.020	0.020	0.000	0.000	0.000
21	A	108	TYR	0	-0.012	-0.024	21.277	-0.012	-0.012	0.000	0.000	0.000
22	A	109	THR	0	0.040	-0.002	17.393	-0.003	-0.003	0.000	0.000	0.000
23	A	110	GLY	0	0.036	0.038	17.249	0.002	0.002	0.000	0.000	0.000
24	A	111	ILE	0	0.014	-0.023	18.036	-0.021	-0.021	0.000	0.000	0.000
25	A	112	VAL	0	-0.037	-0.019	15.027	0.007	0.007	0.000	0.000	0.000
26	A	113	GLU	-1	-0.824	-0.904	12.874	-0.496	-0.496	0.000	0.000	0.000
27	A	114	VAL	0	0.026	0.029	15.282	-0.019	-0.019	0.000	0.000	0.000
28	A	115	TYR	0	0.035	0.026	18.512	0.005	0.005	0.000	0.000	0.000
29	A	116	PRO	0	-0.035	-0.013	14.903	0.009	0.009	0.000	0.000	0.000
30	A	117	ILE	0	0.028	0.022	15.081	-0.001	-0.001	0.000	0.000	0.000
31	A	118	ALA	0	0.035	0.010	18.036	0.007	0.007	0.000	0.000	0.000
32	A	119	LYS	1	0.911	0.958	20.338	-0.013	-0.013	0.000	0.000	0.000
33	A	120	ALA	0	-0.016	-0.005	18.745	0.008	0.008	0.000	0.000	0.000
34	A	121	TRP	0	0.030	-0.015	20.497	0.004	0.004	0.000	0.000	0.000
35	A	122	GLN	0	0.074	0.040	22.936	-0.004	-0.004	0.000	0.000	0.000
36	A	123	GLU	-1	-0.990	-0.986	23.319	-0.024	-0.024	0.000	0.000	0.000
37	A	124	ILE	0	-0.054	-0.021	22.213	0.003	0.003	0.000	0.000	0.000
38	A	125	GLY	0	-0.056	-0.039	25.344	-0.001	-0.001	0.000	0.000	0.000
39	A	126	ASN	0	-0.072	-0.029	24.945	-0.001	-0.001	0.000	0.000	0.000
40	A	127	ASP	-1	-0.872	-0.951	28.164	-0.054	-0.054	0.000	0.000	0.000
41	A	128	VAL	0	-0.012	-0.013	24.748	-0.004	-0.004	0.000	0.000	0.000
42	A	129	THR	0	-0.024	-0.019	28.003	0.012	0.012	0.000	0.000	0.000
43	A	130	THR	0	0.018	0.019	24.194	-0.007	-0.007	0.000	0.000	0.000
44	A	131	LEU	0	0.025	0.015	26.198	0.010	0.010	0.000	0.000	0.000
45	A	132	HIS	0	-0.031	-0.013	23.571	0.000	0.000	0.000	0.000	0.000
46	A	133	VAL	0	0.024	0.016	25.989	0.009	0.009	0.000	0.000	0.000
47	A	134	THR	0	0.010	0.003	25.080	-0.010	-0.010	0.000	0.000	0.000
48	A	135	PHE	0	0.023	0.008	27.053	0.001	0.001	0.000	0.000	0.000
49	A	136	GLU	-1	-0.906	-0.971	28.840	-0.002	-0.002	0.000	0.000	0.000
50	A	137	PRO	0	-0.048	-0.021	29.320	0.003	0.003	0.000	0.000	0.000
51	A	138	MET	0	-0.084	-0.050	24.051	0.009	0.009	0.000	0.000	0.000
52	A	139	VAL	0	0.008	0.031	24.988	-0.006	-0.006	0.000	0.000	0.000
53	A	140	ILE	0	0.006	-0.018	21.382	0.012	0.012	0.000	0.000	0.000
54	A	141	LEU	0	-0.031	-0.026	19.441	-0.010	-0.010	0.000	0.000	0.000
55	A	142	LYS	1	0.955	0.992	23.950	-0.006	-0.006	0.000	0.000	0.000
56	A	143	GLU	-1	-0.856	-0.935	27.400	0.014	0.014	0.000	0.000	0.000
57	A	144	GLU	-1	-0.941	-0.975	22.817	0.049	0.049	0.000	0.000	0.000
58	A	145	LEU	0	-0.063	-0.044	23.239	-0.006	-0.006	0.000	0.000	0.000
59	A	146	GLU	-1	-0.905	-0.952	25.544	-0.012	-0.012	0.000	0.000	0.000
60	A	147	LYS	1	0.915	0.973	28.233	-0.029	-0.029	0.000	0.000	0.000
61	A	148	ALA	0	-0.103	-0.046	24.358	0.000	0.000	0.000	0.000	0.000
62	A	149	VAL	0	-0.025	-0.009	25.376	-0.009	-0.009	0.000	0.000	0.000
63	A	150	THR	0	-0.054	0.009	27.945	0.010	0.010	0.000	0.000	0.000
64	A	151	ARG	1	0.919	0.941	30.710	0.058	0.058	0.000	0.000	0.000
65	A	152	HIS	0	-0.005	-0.020	26.122	-0.001	-0.001	0.000	0.000	0.000
66	A	153	ILE	0	0.009	0.009	29.882	0.007	0.007	0.000	0.000	0.000
67	A	154	VAL	0	-0.005	-0.005	28.707	-0.005	-0.005	0.000	0.000	0.000
68	A	155	GLU	-1	-0.860	-0.935	30.104	-0.036	-0.036	0.000	0.000	0.000
69	A	156	PRO	0	-0.043	-0.010	30.858	-0.004	-0.004	0.000	0.000	0.000
70	A	157	VAL	0	0.012	-0.005	31.148	0.000	0.000	0.000	0.000	0.000
71	A	158	PRO	0	0.027	0.024	32.408	0.004	0.004	0.000	0.000	0.000
72	A	159	LEU	0	0.002	-0.003	29.934	-0.003	-0.003	0.000	0.000	0.000
73	A	160	ASN	0	0.037	0.000	32.953	0.009	0.009	0.000	0.000	0.000
74	A	161	PRO	0	-0.037	-0.019	33.390	-0.003	-0.003	0.000	0.000	0.000
75	A	162	ASN	0	-0.034	-0.015	34.451	0.004	0.004	0.000	0.000	0.000
76	A	163	GLN	0	0.000	0.019	35.709	0.000	0.000	0.000	0.000	0.000
77	A	164	ASP	-1	-0.835	-0.925	33.508	-0.030	-0.030	0.000	0.000	0.000
78	A	165	PHE	0	0.026	-0.013	25.246	-0.001	-0.001	0.000	0.000	0.000
79	A	166	LEU	0	0.005	0.013	30.634	-0.006	-0.006	0.000	0.000	0.000
80	A	167	ALA	0	-0.026	-0.001	31.619	-0.005	-0.005	0.000	0.000	0.000
81	A	168	ASN	0	0.024	-0.003	31.262	-0.003	-0.003	0.000	0.000	0.000
82	A	169	MET	0	-0.027	-0.013	24.889	-0.002	-0.002	0.000	0.000	0.000
83	A	170	LYS	1	0.968	1.002	29.819	0.057	0.057	0.000	0.000	0.000
84	A	171	ASN	0	-0.014	-0.014	32.740	0.000	0.000	0.000	0.000	0.000
85	A	172	VAL	0	0.040	0.034	27.048	0.000	0.000	0.000	0.000	0.000
86	A	173	SER	0	-0.013	0.002	29.215	-0.002	-0.002	0.000	0.000	0.000
87	A	174	GLN	0	-0.085	-0.055	30.630	-0.006	-0.006	0.000	0.000	0.000
88	A	175	ARG	1	0.906	0.960	32.131	0.036	0.036	0.000	0.000	0.000
89	A	176	LEU	0	0.017	0.007	26.420	-0.001	-0.001	0.000	0.000	0.000
90	A	177	LYS	1	0.894	0.946	30.888	0.081	0.081	0.000	0.000	0.000
91	A	178	GLU	-1	-0.933	-0.970	33.174	-0.046	-0.046	0.000	0.000	0.000
92	A	179	LYS	1	0.867	0.947	32.525	0.047	0.047	0.000	0.000	0.000
93	A	180	VAL	0	0.001	0.007	29.604	-0.001	-0.001	0.000	0.000	0.000
94	A	181	ARG	1	0.892	0.938	32.714	0.070	0.070	0.000	0.000	0.000
95	A	182	GLU	-1	-0.880	-0.957	36.072	-0.045	-0.045	0.000	0.000	0.000
96	A	183	LEU	0	-0.021	-0.026	31.948	0.003	0.003	0.000	0.000	0.000
97	A	184	LEU	0	-0.072	-0.035	32.086	-0.001	-0.001	0.000	0.000	0.000
98	A	185	GLU	-1	-0.938	-0.965	35.937	-0.058	-0.058	0.000	0.000	0.000
99	A	186	SER	0	-0.092	-0.020	39.111	0.004	0.004	0.000	0.000	0.000
100	A	187	GLU	-1	-0.892	-0.939	35.950	-0.055	-0.055	0.000	0.000	0.000
101	A	188	ASP	-1	-0.925	-0.957	36.995	-0.073	-0.073	0.000	0.000	0.000
102	A	189	TRP	0	-0.015	-0.045	30.831	-0.003	-0.003	0.000	0.000	0.000
103	A	190	ASP	-1	-0.833	-0.900	30.691	-0.098	-0.098	0.000	0.000	0.000
104	A	191	LEU	0	-0.079	-0.047	23.610	-0.011	-0.011	0.000	0.000	0.000
105	A	192	VAL	0	-0.009	0.018	26.245	0.008	0.008	0.000	0.000	0.000
106	A	193	PHE	0	0.002	-0.005	16.999	-0.018	-0.018	0.000	0.000	0.000
107	A	194	MET	0	-0.031	-0.002	21.668	0.026	0.026	0.000	0.000	0.000
108	A	195	VAL	0	0.066	0.047	15.993	-0.028	-0.028	0.000	0.000	0.000
109	A	196	GLY	0	0.029	0.005	19.040	0.040	0.040	0.000	0.000	0.000
110	A	197	PRO	0	-0.008	0.008	19.550	-0.028	-0.028	0.000	0.000	0.000
111	A	198	VAL	0	0.077	0.022	20.206	0.007	0.007	0.000	0.000	0.000
112	A	199	GLY	0	-0.030	-0.019	21.745	0.007	0.007	0.000	0.000	0.000
113	A	200	ASP	-1	-0.812	-0.937	24.489	-0.099	-0.099	0.000	0.000	0.000
114	A	201	GLN	0	0.015	-0.006	19.015	0.010	0.010	0.000	0.000	0.000
115	A	202	LYS	1	0.911	0.966	24.347	0.165	0.165	0.000	0.000	0.000
116	A	203	GLN	0	-0.021	-0.019	26.935	0.013	0.013	0.000	0.000	0.000
117	A	204	VAL	0	0.072	0.039	27.037	0.005	0.005	0.000	0.000	0.000
118	A	205	PHE	0	0.045	0.023	25.824	0.006	0.006	0.000	0.000	0.000
119	A	206	GLU	-1	-0.993	-1.006	28.484	-0.119	-0.119	0.000	0.000	0.000
120	A	207	VAL	0	-0.064	-0.020	31.661	0.008	0.008	0.000	0.000	0.000
121	A	208	VAL	0	0.067	0.016	28.634	0.004	0.004	0.000	0.000	0.000
122	A	209	LYS	1	0.849	0.931	31.125	0.132	0.132	0.000	0.000	0.000
123	A	210	GLU	-1	-0.950	-0.974	32.803	-0.078	-0.078	0.000	0.000	0.000
124	A	211	TYR	0	-0.036	-0.002	35.048	0.005	0.005	0.000	0.000	0.000
125	A	212	GLY	0	-0.027	-0.009	35.050	0.000	0.000	0.000	0.000	0.000
126	A	213	VAL	0	0.012	0.028	30.144	-0.001	-0.001	0.000	0.000	0.000
127	A	214	PRO	0	-0.037	-0.012	27.600	-0.007	-0.007	0.000	0.000	0.000
128	A	215	MET	0	0.035	0.008	24.234	0.007	0.007	0.000	0.000	0.000
129	A	216	LYS	1	0.816	0.936	16.457	0.423	0.423	0.000	0.000	0.000
130	A	217	VAL	0	-0.026	-0.012	18.592	0.022	0.022	0.000	0.000	0.000
131	A	218	ASP	-1	-0.792	-0.927	14.513	-0.442	-0.442	0.000	0.000	0.000
132	A	219	LEU	0	-0.061	-0.030	10.644	-0.007	-0.007	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:88:GLY)