FMO DATABASE

FMODB ID: J3GK9

Calculation Name: 2QLC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QLC

Chain ID: A

ChEMBL ID:

UniProt ID: Q8KES1

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1131826.59863
FMO2-HF: Nuclear repulsion	1082578.999723
FMO2-HF: Total energy	-49247.598907
FMO2-MP2: Total energy	-49394.117001

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:1:MET)

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

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.
-1.539	3.648	1.823	-2.503	-4.508	-0.006

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / 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	3	LEU	0	0.035	0.019	2.760	-2.570	1.562	0.497	-1.775	-2.855	0.003
4	A	4	LYS	1	0.939	0.996	4.439	1.774	2.074	-0.001	-0.029	-0.270	0.000
5	A	5	VAL	0	0.000	0.000	5.749	0.298	0.298	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.745	0.850	7.478	1.463	1.463	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.055	0.022	11.718	0.110	0.110	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.071	0.035	13.804	-0.064	-0.064	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.993	1.002	11.231	0.211	0.211	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.778	-0.881	9.450	-0.778	-0.778	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.013	0.006	10.367	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.011	0.006	12.834	0.045	0.045	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.848	-0.912	9.538	0.193	0.193	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.040	-0.032	7.733	0.072	0.072	0.000	0.000	0.000	0.000
15	A	15	MET	0	-0.006	0.000	9.799	0.042	0.042	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.846	0.930	12.165	-0.083	-0.083	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.013	-0.003	12.574	0.033	0.033	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.835	0.913	8.543	0.114	0.114	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.027	0.000	15.517	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.011	-0.003	19.057	0.019	0.019	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.757	-0.839	21.435	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.888	-0.945	19.733	0.005	0.005	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.048	-0.051	23.984	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.775	0.871	26.514	0.011	0.011	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.832	-0.907	25.636	-0.068	-0.068	0.000	0.000	0.000	0.000
26	A	26	HIS	0	-0.020	-0.024	22.405	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.038	-0.006	22.060	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.001	-0.007	17.827	0.004	0.004	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.001	0.007	17.476	-0.006	-0.006	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.002	-0.001	11.895	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.024	0.006	12.906	0.018	0.018	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.011	0.002	10.371	-0.146	-0.146	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.078	0.040	7.690	0.128	0.128	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.067	0.028	10.669	-0.042	-0.042	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.839	0.909	8.041	0.621	0.621	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.008	0.007	8.293	-0.146	-0.146	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.020	-0.010	2.646	-2.538	-1.783	1.327	-0.699	-1.383	-0.009
38	A	38	ILE	0	0.039	0.010	6.392	0.382	0.382	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.053	-0.014	6.837	-0.153	-0.153	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.775	0.850	9.009	0.347	0.347	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.049	0.033	11.355	-0.089	-0.089	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.837	-0.893	14.281	-0.155	-0.155	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.006	-0.007	17.969	-0.015	-0.015	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.036	-0.019	20.963	0.008	0.008	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.016	-0.009	23.625	0.010	0.010	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.016	0.011	24.346	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.023	-0.013	27.174	0.006	0.006	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.028	-0.006	29.308	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.003	0.008	27.985	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.025	0.009	30.810	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.041	-0.007	31.694	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.015	-0.001	32.364	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.000	-0.003	30.475	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.011	0.012	26.987	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.877	0.949	28.372	0.095	0.095	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.063	0.017	26.731	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.860	0.924	26.273	0.080	0.080	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.815	-0.906	25.793	-0.102	-0.102	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.029	0.013	21.391	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.064	0.018	21.316	-0.017	-0.017	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.944	0.996	22.573	0.114	0.114	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.005	-0.009	19.174	0.000	0.000	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.045	0.023	17.791	-0.019	-0.019	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.000	-0.002	18.030	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.811	0.915	18.614	0.188	0.188	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.829	-0.897	14.429	-0.289	-0.289	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.061	-0.024	14.540	-0.038	-0.038	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.034	-0.017	14.040	-0.046	-0.046	0.000	0.000	0.000	0.000
69	A	69	HIS	0	-0.010	-0.005	13.976	0.047	0.047	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.001	-0.005	14.755	0.025	0.025	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.001	0.006	15.263	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.020	-0.006	13.507	0.003	0.003	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.015	0.012	17.005	0.007	0.007	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.018	-0.002	16.098	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	75	HIS	0	0.035	0.008	19.596	0.022	0.022	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.001	0.002	21.059	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	77	HIS	1	0.836	0.899	22.717	0.083	0.083	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.006	0.011	25.636	0.004	0.004	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.059	-0.033	27.126	0.005	0.005	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.032	0.023	26.878	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.867	-0.934	26.550	-0.058	-0.058	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.019	0.013	22.819	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	83	GLN	0	0.014	0.007	25.897	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.017	0.006	27.819	0.003	0.003	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.024	-0.049	29.233	0.008	0.008	0.000	0.000	0.000	0.000
86	A	86	ASN	0	0.030	-0.021	31.697	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.048	0.038	32.362	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.714	-0.851	27.678	-0.102	-0.102	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.895	0.961	28.601	0.076	0.076	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.027	-0.001	30.629	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.021	0.004	27.038	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.004	-0.002	25.258	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.053	-0.020	27.171	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.047	-0.030	28.817	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.023	0.005	23.917	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.901	0.961	24.903	0.151	0.151	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.978	0.984	25.970	0.115	0.115	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.032	-0.004	26.972	0.005	0.005	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.043	0.013	23.641	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.905	-0.958	24.264	-0.194	-0.194	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.101	-0.043	26.236	0.004	0.004	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.051	-0.041	24.814	0.005	0.005	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.043	-0.006	23.447	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.033	0.003	18.420	-0.017	-0.017	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.848	-0.923	19.224	-0.311	-0.311	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.016	-0.010	19.019	-0.031	-0.031	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.028	0.013	14.439	0.009	0.009	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.764	-0.860	18.025	-0.260	-0.260	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.053	-0.022	19.585	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	110	VAL	0	0.001	-0.002	17.328	0.009	0.009	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.026	0.007	20.284	0.002	0.002	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.004	-0.015	17.171	0.000	0.000	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.078	0.030	20.558	0.004	0.004	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.003	-0.002	20.762	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.043	-0.034	20.074	0.025	0.025	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.872	-0.934	20.526	-0.057	-0.057	0.000	0.000	0.000	0.000
117	A	117	TRP	0	-0.040	-0.035	17.669	-0.029	-0.029	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.035	0.035	20.703	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.027	-0.032	20.208	-0.008	-0.008	0.000	0.000	0.000	0.000
120	A	120	PHE	0	0.051	-0.003	22.055	0.019	0.019	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.785	0.870	19.989	0.306	0.306	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.885	-0.949	20.711	-0.235	-0.235	0.000	0.000	0.000	0.000
123	A	123	HIS	0	-0.087	-0.043	23.723	0.028	0.028	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.037	-0.018	26.479	0.010	0.010	0.000	0.000	0.000	0.000
125	A	125	LEU	0	0.010	0.007	26.917	0.010	0.010	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.031	0.008	22.564	0.019	0.019	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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