FMO DATABASE

FMODB ID: 9GZ62

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1185684.701051
FMO2-HF: Nuclear repulsion	1133687.139248
FMO2-HF: Total energy	-51997.561803
FMO2-MP2: Total energy	-52149.303405

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.
-1.184	0.0030000000000002	-0.001	-0.602	-0.584	0.002

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 : 0.034 / q_NPA : 0.016

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	90	LEU	0	-0.021	-0.017	3.862	-0.233	0.954	-0.001	-0.602	-0.584	0.002
4	A	91	GLY	0	0.019	0.017	6.454	0.422	0.422	0.000	0.000	0.000	0.000
5	A	92	THR	0	-0.038	-0.043	10.128	-0.140	-0.140	0.000	0.000	0.000	0.000
6	A	93	PRO	0	-0.034	0.006	11.030	0.120	0.120	0.000	0.000	0.000	0.000
7	A	94	VAL	0	-0.005	-0.024	13.146	0.096	0.096	0.000	0.000	0.000	0.000
8	A	95	PRO	0	0.001	0.025	16.787	-0.018	-0.018	0.000	0.000	0.000	0.000
9	A	96	MET	0	-0.014	-0.008	17.807	0.023	0.023	0.000	0.000	0.000	0.000
10	A	97	GLU	-1	-0.888	-0.943	20.925	-0.296	-0.296	0.000	0.000	0.000	0.000
11	A	98	LYS	1	0.901	0.956	24.635	0.180	0.180	0.000	0.000	0.000	0.000
12	A	99	PHE	0	-0.017	-0.013	22.884	0.010	0.010	0.000	0.000	0.000	0.000
13	A	100	GLY	0	0.038	0.034	28.420	0.013	0.013	0.000	0.000	0.000	0.000
14	A	101	LYS	1	0.807	0.901	30.085	0.153	0.153	0.000	0.000	0.000	0.000
15	A	102	ILE	0	-0.034	-0.021	24.848	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	103	LEU	0	-0.004	0.018	28.106	0.002	0.002	0.000	0.000	0.000	0.000
17	A	104	ALA	0	-0.002	-0.016	23.238	-0.025	-0.025	0.000	0.000	0.000	0.000
18	A	105	ILE	0	0.003	-0.009	24.181	0.014	0.014	0.000	0.000	0.000	0.000
19	A	106	GLY	0	0.052	0.005	21.456	-0.044	-0.044	0.000	0.000	0.000	0.000
20	A	107	ALA	0	0.003	0.008	22.388	0.031	0.031	0.000	0.000	0.000	0.000
21	A	108	TYR	0	-0.054	-0.057	21.546	-0.025	-0.025	0.000	0.000	0.000	0.000
22	A	109	THR	0	0.022	-0.004	17.737	0.000	0.000	0.000	0.000	0.000	0.000
23	A	110	GLY	0	0.022	0.028	17.525	-0.030	-0.030	0.000	0.000	0.000	0.000
24	A	111	ILE	0	-0.004	-0.006	18.172	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	112	VAL	0	-0.019	-0.007	15.212	0.000	0.000	0.000	0.000	0.000	0.000
26	A	113	GLU	-1	-0.839	-0.896	12.818	-1.101	-1.101	0.000	0.000	0.000	0.000
27	A	114	VAL	0	0.014	-0.002	15.442	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	115	TYR	0	0.030	0.028	18.538	0.022	0.022	0.000	0.000	0.000	0.000
29	A	116	PRO	0	-0.030	-0.014	14.978	0.031	0.031	0.000	0.000	0.000	0.000
30	A	117	ILE	0	0.017	0.017	14.871	0.017	0.017	0.000	0.000	0.000	0.000
31	A	118	ALA	0	0.040	0.014	18.159	0.035	0.035	0.000	0.000	0.000	0.000
32	A	119	LYS	1	0.931	0.971	20.437	0.265	0.265	0.000	0.000	0.000	0.000
33	A	120	ALA	0	-0.009	0.000	18.606	0.028	0.028	0.000	0.000	0.000	0.000
34	A	121	TRP	0	0.014	-0.027	20.724	0.021	0.021	0.000	0.000	0.000	0.000
35	A	122	GLN	0	0.021	0.022	23.206	0.023	0.023	0.000	0.000	0.000	0.000
36	A	123	GLU	-1	-0.988	-0.989	23.361	-0.172	-0.172	0.000	0.000	0.000	0.000
37	A	124	ILE	0	-0.072	-0.034	21.881	0.015	0.015	0.000	0.000	0.000	0.000
38	A	125	GLY	0	-0.042	-0.021	25.366	0.015	0.015	0.000	0.000	0.000	0.000
39	A	126	ASN	0	-0.069	-0.048	25.569	0.015	0.015	0.000	0.000	0.000	0.000
40	A	127	ASP	-1	-0.839	-0.919	28.764	-0.163	-0.163	0.000	0.000	0.000	0.000
41	A	128	VAL	0	-0.018	-0.007	24.657	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	129	THR	0	-0.022	-0.012	28.098	0.019	0.019	0.000	0.000	0.000	0.000
43	A	130	THR	0	0.035	0.020	24.181	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	131	LEU	0	0.010	0.005	26.190	0.020	0.020	0.000	0.000	0.000	0.000
45	A	132	HIS	0	0.008	0.007	23.760	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	133	VAL	0	0.014	0.010	25.872	0.020	0.020	0.000	0.000	0.000	0.000
47	A	134	THR	0	-0.033	-0.024	25.486	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	135	PHE	0	0.046	0.008	26.885	0.011	0.011	0.000	0.000	0.000	0.000
49	A	136	GLU	-1	-0.865	-0.949	28.915	-0.096	-0.096	0.000	0.000	0.000	0.000
50	A	137	PRO	0	-0.066	-0.031	29.477	0.000	0.000	0.000	0.000	0.000	0.000
51	A	138	MET	0	-0.070	-0.036	23.473	0.006	0.006	0.000	0.000	0.000	0.000
52	A	139	VAL	0	0.031	0.041	25.239	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	140	ILE	0	-0.028	-0.029	21.387	0.011	0.011	0.000	0.000	0.000	0.000
54	A	141	LEU	0	-0.012	-0.017	19.315	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	142	LYS	1	0.831	0.909	23.688	0.113	0.113	0.000	0.000	0.000	0.000
56	A	143	GLU	-1	-0.792	-0.894	27.230	-0.119	-0.119	0.000	0.000	0.000	0.000
57	A	144	GLU	-1	-0.951	-0.981	23.294	-0.155	-0.155	0.000	0.000	0.000	0.000
58	A	145	LEU	0	-0.050	-0.034	22.950	-0.014	-0.014	0.000	0.000	0.000	0.000
59	A	146	GLU	-1	-0.816	-0.895	25.490	-0.134	-0.134	0.000	0.000	0.000	0.000
60	A	147	LYS	1	0.870	0.950	27.827	0.117	0.117	0.000	0.000	0.000	0.000
61	A	148	ALA	0	-0.071	-0.043	24.318	0.001	0.001	0.000	0.000	0.000	0.000
62	A	149	VAL	0	-0.026	-0.011	25.324	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	150	THR	0	-0.032	0.011	28.002	0.017	0.017	0.000	0.000	0.000	0.000
64	A	151	ARG	1	0.836	0.876	30.747	0.173	0.173	0.000	0.000	0.000	0.000
65	A	152	HIS	0	-0.033	-0.024	26.475	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	153	ILE	0	0.018	0.009	29.503	0.016	0.016	0.000	0.000	0.000	0.000
67	A	154	VAL	0	0.002	0.001	28.539	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	155	GLU	-1	-0.818	-0.903	30.002	-0.124	-0.124	0.000	0.000	0.000	0.000
69	A	156	PRO	0	-0.029	0.000	30.621	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	157	VAL	0	-0.011	-0.012	31.357	0.006	0.006	0.000	0.000	0.000	0.000
71	A	158	PRO	0	0.033	0.026	32.587	0.000	0.000	0.000	0.000	0.000	0.000
72	A	159	LEU	0	-0.032	-0.010	30.224	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	160	ASN	0	0.039	0.000	33.222	0.012	0.012	0.000	0.000	0.000	0.000
74	A	161	PRO	0	0.001	-0.004	33.558	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	162	ASN	0	-0.073	-0.035	34.855	0.007	0.007	0.000	0.000	0.000	0.000
76	A	163	GLN	0	-0.009	0.008	36.379	0.003	0.003	0.000	0.000	0.000	0.000
77	A	164	ASP	-1	-0.780	-0.888	33.105	-0.098	-0.098	0.000	0.000	0.000	0.000
78	A	165	PHE	0	0.023	0.011	25.393	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	166	LEU	0	0.006	0.006	30.418	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	167	ALA	0	-0.031	-0.025	31.600	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	168	ASN	0	-0.015	-0.016	31.364	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	169	MET	0	-0.007	-0.007	24.891	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	170	LYS	1	0.920	0.977	29.803	0.135	0.135	0.000	0.000	0.000	0.000
84	A	171	ASN	0	-0.005	-0.011	32.713	0.001	0.001	0.000	0.000	0.000	0.000
85	A	172	VAL	0	0.033	0.027	27.261	0.000	0.000	0.000	0.000	0.000	0.000
86	A	173	SER	0	-0.043	-0.053	29.250	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	174	GLN	0	-0.146	-0.073	30.740	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	175	ARG	1	0.900	0.951	32.418	0.124	0.124	0.000	0.000	0.000	0.000
89	A	176	LEU	0	0.005	0.002	26.850	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	177	LYS	1	0.897	0.948	30.869	0.163	0.163	0.000	0.000	0.000	0.000
91	A	178	GLU	-1	-0.853	-0.911	33.324	-0.122	-0.122	0.000	0.000	0.000	0.000
92	A	179	LYS	1	0.834	0.893	32.619	0.138	0.138	0.000	0.000	0.000	0.000
93	A	180	VAL	0	-0.019	-0.008	29.789	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	181	ARG	1	0.787	0.876	32.911	0.139	0.139	0.000	0.000	0.000	0.000
95	A	182	GLU	-1	-0.850	-0.914	36.552	-0.126	-0.126	0.000	0.000	0.000	0.000
96	A	183	LEU	0	0.004	-0.013	32.326	0.004	0.004	0.000	0.000	0.000	0.000
97	A	184	LEU	0	-0.055	-0.011	32.444	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	185	GLU	-1	-0.881	-0.911	36.498	-0.117	-0.117	0.000	0.000	0.000	0.000
99	A	186	SER	0	-0.080	-0.032	39.230	0.008	0.008	0.000	0.000	0.000	0.000
100	A	187	GLU	-1	-0.842	-0.881	35.931	-0.145	-0.145	0.000	0.000	0.000	0.000
101	A	188	ASP	-1	-0.914	-0.944	37.630	-0.148	-0.148	0.000	0.000	0.000	0.000
102	A	189	TRP	0	0.009	-0.043	30.910	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	190	ASP	-1	-0.828	-0.887	31.040	-0.183	-0.183	0.000	0.000	0.000	0.000
104	A	191	LEU	0	-0.074	-0.042	24.154	-0.014	-0.014	0.000	0.000	0.000	0.000
105	A	192	VAL	0	0.016	0.011	26.615	0.009	0.009	0.000	0.000	0.000	0.000
106	A	193	PHE	0	-0.038	-0.024	17.248	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	194	MET	0	-0.043	0.006	21.821	0.040	0.040	0.000	0.000	0.000	0.000
108	A	195	VAL	0	0.064	0.047	15.961	-0.042	-0.042	0.000	0.000	0.000	0.000
109	A	196	GLY	0	0.018	0.006	19.056	0.052	0.052	0.000	0.000	0.000	0.000
110	A	197	PRO	0	0.005	0.017	19.733	-0.034	-0.034	0.000	0.000	0.000	0.000
111	A	198	VAL	0	0.058	0.007	20.642	0.025	0.025	0.000	0.000	0.000	0.000
112	A	199	GLY	0	-0.014	-0.008	22.289	0.015	0.015	0.000	0.000	0.000	0.000
113	A	200	ASP	-1	-0.750	-0.856	24.928	-0.206	-0.206	0.000	0.000	0.000	0.000
114	A	201	GLN	0	-0.008	-0.033	19.200	0.026	0.026	0.000	0.000	0.000	0.000
115	A	202	LYS	1	0.926	0.967	24.809	0.269	0.269	0.000	0.000	0.000	0.000
116	A	203	GLN	0	-0.060	-0.034	27.357	0.030	0.030	0.000	0.000	0.000	0.000
117	A	204	VAL	0	0.047	0.026	27.216	0.015	0.015	0.000	0.000	0.000	0.000
118	A	205	PHE	0	0.003	-0.003	26.875	0.011	0.011	0.000	0.000	0.000	0.000
119	A	206	GLU	-1	-0.847	-0.914	28.873	-0.186	-0.186	0.000	0.000	0.000	0.000
120	A	207	VAL	0	-0.021	-0.008	32.338	0.011	0.011	0.000	0.000	0.000	0.000
121	A	208	VAL	0	0.043	0.008	29.031	0.006	0.006	0.000	0.000	0.000	0.000
122	A	209	LYS	1	0.793	0.878	31.811	0.197	0.197	0.000	0.000	0.000	0.000
123	A	210	GLU	-1	-0.905	-0.925	33.212	-0.132	-0.132	0.000	0.000	0.000	0.000
124	A	211	TYR	0	-0.018	-0.034	35.336	0.007	0.007	0.000	0.000	0.000	0.000
125	A	212	GLY	0	-0.059	-0.021	35.142	0.002	0.002	0.000	0.000	0.000	0.000
126	A	213	VAL	0	0.004	0.022	30.572	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	214	PRO	0	-0.028	-0.004	27.971	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	215	MET	0	0.007	-0.001	24.355	0.006	0.006	0.000	0.000	0.000	0.000
129	A	216	LYS	1	0.823	0.930	16.314	0.716	0.716	0.000	0.000	0.000	0.000
130	A	217	VAL	0	0.010	0.000	18.803	0.028	0.028	0.000	0.000	0.000	0.000
131	A	218	ASP	-1	-0.783	-0.906	14.655	-0.702	-0.702	0.000	0.000	0.000	0.000
132	A	219	LEU	0	-0.039	-0.019	10.929	-0.003	-0.003	0.000	0.000	0.000	0.000

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