FMO DATABASE

FMODB ID: 984R2

Calculation Name: 2QSJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QSJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q5LQW4

Base Structure: X-ray

Registration Date: 2023-09-21

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1080799.028743
FMO2-HF: Nuclear repulsion	1032603.891909
FMO2-HF: Total energy	-48195.136835
FMO2-MP2: Total energy	-48338.932619

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:LEU)

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

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.
-19.293	-11.431	4.976	-4.723	-8.114	-0.037

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.081 / q_NPA : -0.041

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	VAL	0	-0.022	-0.024	2.896	-3.518	0.042	0.374	-1.721	-2.213	-0.007
4	A	4	VAL	0	0.015	0.008	4.744	0.599	0.665	-0.001	-0.009	-0.056	0.000
5	A	5	LEU	0	-0.004	0.008	8.247	0.180	0.180	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.040	-0.026	11.193	0.076	0.076	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.003	0.006	14.158	0.066	0.066	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.764	-0.900	17.414	-0.325	-0.325	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.757	-0.851	19.693	-0.227	-0.227	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.092	-0.051	22.144	0.046	0.046	0.000	0.000	0.000	0.000
11	A	11	HIS	0	0.029	0.001	16.212	-0.043	-0.043	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.038	-0.021	18.353	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.020	0.011	18.530	0.001	0.001	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.789	0.878	15.034	0.265	0.265	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.009	-0.006	14.070	-0.047	-0.047	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.014	-0.006	14.357	0.005	0.005	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.030	0.009	14.048	0.001	0.001	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.854	0.914	8.329	0.234	0.234	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.042	-0.032	10.036	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.054	-0.011	12.037	0.057	0.057	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.016	0.008	9.603	0.042	0.042	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.777	-0.884	5.692	-0.563	-0.563	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.046	-0.010	7.761	0.208	0.208	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.066	-0.033	10.536	0.099	0.099	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.003	0.003	7.061	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.037	-0.032	6.363	-0.139	-0.139	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.008	0.002	3.090	0.763	1.202	0.079	-0.085	-0.433	0.000
28	A	28	MET	0	-0.013	0.018	2.613	-5.986	-4.099	2.618	-2.000	-2.505	-0.025
29	A	29	ARG	1	0.792	0.877	2.373	-0.722	1.087	1.904	-0.879	-2.833	-0.005
30	A	30	VAL	0	-0.011	-0.003	4.050	-0.387	-0.286	0.002	-0.029	-0.074	0.000
31	A	31	GLU	-1	-0.817	-0.886	6.598	-0.474	-0.474	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.005	-0.013	9.456	-0.056	-0.056	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.025	-0.001	13.242	0.039	0.039	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.859	-0.919	16.494	-0.221	-0.221	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.010	-0.024	20.027	0.017	0.017	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.048	0.016	20.212	-0.036	-0.036	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.002	0.002	20.853	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.903	-0.924	18.683	-0.284	-0.284	0.000	0.000	0.000	0.000
39	A	39	ALA	0	-0.009	-0.009	16.250	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.008	0.000	16.320	-0.048	-0.048	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.002	0.001	17.971	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.032	-0.018	8.931	0.038	0.038	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.008	0.005	12.849	-0.021	-0.021	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.938	-0.974	14.760	-0.337	-0.337	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.112	-0.040	14.707	0.041	0.041	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.947	-0.975	13.237	-0.380	-0.380	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.111	-0.053	9.652	-0.090	-0.090	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.018	-0.010	7.644	0.017	0.017	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.041	-0.029	7.757	-0.357	-0.357	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.839	-0.909	6.436	-4.700	-4.700	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.039	-0.028	9.449	0.403	0.403	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.008	0.008	10.903	-0.083	-0.083	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.034	-0.012	13.389	0.099	0.099	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.015	0.002	15.535	0.015	0.015	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.772	-0.887	18.884	-0.281	-0.281	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.026	-0.020	21.729	0.000	0.000	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.061	-0.031	25.345	0.019	0.019	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.082	-0.043	28.404	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	PRO	0	-0.054	-0.008	25.135	0.017	0.017	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.785	-0.903	23.440	-0.298	-0.298	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.005	-0.007	25.940	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.842	-0.877	25.745	-0.254	-0.254	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.026	-0.021	26.457	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.026	0.011	26.136	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.798	-0.899	26.586	-0.284	-0.284	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.062	0.034	24.243	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.010	0.007	21.472	-0.030	-0.030	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.024	-0.014	22.458	-0.024	-0.024	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.690	0.783	23.555	0.276	0.276	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.016	0.012	17.361	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.829	0.906	18.359	0.639	0.639	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.795	0.896	21.373	0.304	0.304	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.057	-0.015	16.414	0.031	0.031	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.793	-0.879	16.324	-0.750	-0.750	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.039	-0.022	18.473	-0.057	-0.057	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.128	-0.075	15.727	-0.045	-0.045	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.002	0.005	13.543	-0.222	-0.222	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.046	0.039	13.918	0.151	0.151	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.019	-0.030	14.810	-0.062	-0.062	0.000	0.000	0.000	0.000
80	A	80	ALA	0	-0.013	0.005	16.981	0.073	0.073	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.006	-0.002	18.329	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.023	-0.014	17.595	0.007	0.007	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.005	-0.025	21.102	0.024	0.024	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.001	0.007	24.861	0.008	0.008	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.860	-0.914	27.695	-0.204	-0.204	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.077	-0.055	28.473	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.837	-0.900	30.583	-0.186	-0.186	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.022	-0.001	31.718	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.807	-0.883	32.758	-0.203	-0.203	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.014	0.019	28.232	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.004	0.000	27.533	-0.017	-0.017	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.714	0.817	28.761	0.192	0.192	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.027	0.008	30.740	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.010	0.005	25.366	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.012	-0.005	25.674	-0.023	-0.023	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.899	-0.929	27.438	-0.226	-0.226	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.073	-0.034	26.414	0.001	0.001	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.018	-0.001	24.461	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.016	-0.013	21.680	-0.045	-0.045	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.779	-0.871	18.127	-0.661	-0.661	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.041	0.006	20.073	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	102	PHE	0	-0.048	-0.024	21.044	0.002	0.002	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.014	-0.001	17.873	0.024	0.024	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.007	-0.001	22.258	0.004	0.004	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.818	0.873	21.432	0.319	0.319	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.054	-0.021	23.757	0.008	0.008	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.035	-0.013	22.663	0.021	0.021	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.822	-0.909	22.597	-0.232	-0.232	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.021	-0.006	18.439	-0.029	-0.029	0.000	0.000	0.000	0.000
110	A	110	GLN	0	0.003	0.001	17.707	-0.040	-0.040	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.023	-0.013	18.859	-0.036	-0.036	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.006	0.012	15.998	-0.033	-0.033	0.000	0.000	0.000	0.000
113	A	113	ILE	0	0.023	0.009	13.753	-0.072	-0.072	0.000	0.000	0.000	0.000
114	A	114	HIS	0	-0.011	-0.010	14.855	-0.112	-0.112	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.017	0.001	17.334	-0.026	-0.026	0.000	0.000	0.000	0.000
116	A	116	VAL	0	0.009	-0.002	11.633	-0.039	-0.039	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.036	-0.031	12.692	-0.142	-0.142	0.000	0.000	0.000	0.000
118	A	118	LEU	0	0.004	0.001	13.765	-0.057	-0.057	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.009	0.001	15.073	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.046	-0.021	8.928	-0.093	-0.093	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-1.013	-0.997	11.736	-0.677	-0.677	0.000	0.000	0.000	0.000
122	A	122	GLY	0	-0.044	-0.010	13.721	0.075	0.075	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.966	-0.994	16.348	-0.320	-0.320	0.000	0.000	0.000	0.000
124	A	124	ILE	0	-0.009	0.002	18.912	-0.041	-0.041	0.000	0.000	0.000	0.000
125	A	125	PHE	0	-0.032	-0.007	20.350	0.056	0.056	0.000	0.000	0.000	0.000
126	A	126	LEU	0	0.033	0.006	22.066	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	127	PRO	0	0.001	0.022	25.214	0.016	0.016	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.992	0.965	27.409	0.192	0.192	0.000	0.000	0.000	0.000
129	A	129	SER	0	-0.050	-0.017	30.557	0.008	0.008	0.000	0.000	0.000	0.000
130	A	130	TYR	0	-0.001	0.001	30.134	0.008	0.008	0.000	0.000	0.000	0.000
131	A	131	LEU	0	-0.071	-0.018	28.154	0.010	0.010	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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