FMO DATABASE

FMODB ID: JQVY9

Calculation Name: 2QGO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QGO

Chain ID: A

ChEMBL ID:

UniProt ID: Q5FLQ3

Base Structure: X-ray

Registration Date: 2023-09-23

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	114
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-906956.745189
FMO2-HF: Nuclear repulsion	862756.264399
FMO2-HF: Total energy	-44200.48079
FMO2-MP2: Total energy	-44329.902685

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:4:LEU)

Summations of interaction energy for fragment #1(A:4: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.
-9.183	-0.2	2.896	-3.223	-8.655	-0.008

Interaction energy analysis for fragmet #1(A:4:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.011 / q_NPA : -0.014

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	6	ILE	0	0.007	0.003	3.769	-1.040	0.806	-0.031	-0.842	-0.972	0.001
4	A	7	LYS	1	0.970	0.988	6.296	0.114	0.114	0.000	0.000	0.000	0.000
5	A	8	PHE	0	-0.010	-0.009	9.787	-0.020	-0.020	0.000	0.000	0.000	0.000
6	A	9	THR	0	0.021	-0.016	12.774	0.034	0.034	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.854	-0.935	16.084	-0.094	-0.094	0.000	0.000	0.000	0.000
8	A	11	ASN	0	0.012	0.005	19.321	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	12	ALA	0	-0.006	0.011	15.114	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	13	VAL	0	-0.005	-0.010	15.866	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	14	ASP	-1	-0.908	-0.959	17.674	-0.110	-0.110	0.000	0.000	0.000	0.000
12	A	15	TYR	0	-0.054	-0.041	18.430	0.003	0.003	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.013	-0.008	14.165	0.001	0.001	0.000	0.000	0.000	0.000
14	A	17	LYS	1	0.947	0.976	18.744	0.132	0.132	0.000	0.000	0.000	0.000
15	A	18	ARG	1	0.913	0.990	21.547	0.133	0.133	0.000	0.000	0.000	0.000
16	A	19	ARG	1	0.871	0.940	20.881	0.192	0.192	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.949	-0.965	22.687	-0.141	-0.141	0.000	0.000	0.000	0.000
18	A	21	ILE	0	-0.015	-0.022	16.685	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.036	-0.017	15.238	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	23	ASP	-1	-0.942	-0.966	16.261	-0.218	-0.218	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.812	0.913	17.315	0.198	0.198	0.000	0.000	0.000	0.000
22	A	25	ILE	0	-0.083	-0.027	13.411	-0.029	-0.029	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.018	-0.008	11.404	0.015	0.015	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.019	-0.002	9.829	-0.075	-0.075	0.000	0.000	0.000	0.000
25	A	28	LEU	0	0.008	0.016	5.893	0.088	0.088	0.000	0.000	0.000	0.000
26	A	29	ILE	0	-0.033	-0.019	7.752	-0.168	-0.168	0.000	0.000	0.000	0.000
27	A	30	THR	0	-0.027	-0.005	9.133	0.068	0.068	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.810	-0.901	11.520	-0.278	-0.278	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.865	-0.935	15.249	-0.283	-0.283	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.047	-0.021	17.042	0.030	0.030	0.000	0.000	0.000	0.000
31	A	34	GLY	0	-0.028	-0.009	18.058	0.020	0.020	0.000	0.000	0.000	0.000
32	A	35	GLY	0	-0.002	0.005	16.127	0.003	0.003	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.833	0.892	16.262	0.312	0.312	0.000	0.000	0.000	0.000
34	A	37	TYR	0	-0.109	-0.084	14.655	0.036	0.036	0.000	0.000	0.000	0.000
35	A	38	SER	0	-0.044	0.000	17.779	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.034	-0.036	18.805	0.021	0.021	0.000	0.000	0.000	0.000
37	A	49	HIS	1	0.811	0.890	13.653	0.314	0.314	0.000	0.000	0.000	0.000
38	A	50	PHE	0	-0.021	-0.037	8.065	-0.052	-0.052	0.000	0.000	0.000	0.000
39	A	51	SER	0	0.007	-0.005	12.345	0.046	0.046	0.000	0.000	0.000	0.000
40	A	52	ILE	0	-0.021	-0.011	10.498	-0.075	-0.075	0.000	0.000	0.000	0.000
41	A	53	ILE	0	0.012	0.006	13.089	0.071	0.071	0.000	0.000	0.000	0.000
42	A	54	TRP	0	-0.003	0.004	14.173	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	55	LEU	0	-0.017	-0.013	15.678	0.032	0.032	0.000	0.000	0.000	0.000
44	A	56	ASP	-1	-0.796	-0.901	18.198	-0.197	-0.197	0.000	0.000	0.000	0.000
45	A	57	LYS	1	0.877	0.929	18.726	0.206	0.206	0.000	0.000	0.000	0.000
46	A	58	VAL	0	0.009	0.005	14.076	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	59	ASP	-1	-0.736	-0.843	14.093	-0.284	-0.284	0.000	0.000	0.000	0.000
48	A	60	PRO	0	-0.029	-0.029	13.647	-0.040	-0.040	0.000	0.000	0.000	0.000
49	A	61	ASP	-1	-0.856	-0.917	13.916	-0.286	-0.286	0.000	0.000	0.000	0.000
50	A	62	TYR	0	-0.113	-0.060	9.480	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	63	PRO	0	0.006	0.000	9.306	-0.025	-0.025	0.000	0.000	0.000	0.000
52	A	64	VAL	0	-0.013	-0.003	3.534	-0.296	0.047	0.020	-0.060	-0.303	0.000
53	A	65	LYS	1	0.926	0.963	5.901	0.370	0.370	0.000	0.000	0.000	0.000
54	A	66	ILE	0	0.009	0.025	2.415	-2.220	-0.741	1.068	-0.634	-1.914	0.001
55	A	67	ALA	0	0.005	-0.002	3.614	0.325	0.638	0.003	0.016	-0.332	0.000
56	A	68	ASN	0	0.038	0.012	5.708	0.042	0.042	0.000	0.000	0.000	0.000
57	A	69	GLU	-1	-0.932	-0.967	8.747	0.165	0.165	0.000	0.000	0.000	0.000
58	A	70	GLN	0	-0.026	-0.024	11.930	0.013	0.013	0.000	0.000	0.000	0.000
59	A	71	ASN	0	-0.071	-0.025	13.051	0.015	0.015	0.000	0.000	0.000	0.000
60	A	72	VAL	0	0.047	0.036	10.872	0.019	0.019	0.000	0.000	0.000	0.000
61	A	73	LYS	1	0.917	0.960	10.505	0.178	0.178	0.000	0.000	0.000	0.000
62	A	74	ILE	0	0.025	0.022	7.036	0.058	0.058	0.000	0.000	0.000	0.000
63	A	75	TYR	0	-0.055	-0.041	7.047	-0.067	-0.067	0.000	0.000	0.000	0.000
64	A	76	THR	0	0.065	0.025	3.174	-0.412	-0.041	0.025	-0.075	-0.321	0.000
65	A	77	SER	0	0.001	-0.012	6.480	0.149	0.149	0.000	0.000	0.000	0.000
66	A	78	ASP	-1	-0.876	-0.959	5.960	-0.703	-0.703	0.000	0.000	0.000	0.000
67	A	79	PHE	0	0.014	0.006	6.976	-0.070	-0.070	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.714	-0.860	7.371	-0.723	-0.723	0.000	0.000	0.000	0.000
69	A	81	LYS	1	0.838	0.928	2.472	-0.905	0.194	1.042	-0.424	-1.716	0.000
70	A	82	THR	0	-0.083	-0.045	3.196	-1.606	-0.401	0.073	-0.606	-0.673	-0.006
71	A	83	MET	0	0.006	0.012	5.828	0.224	0.224	0.000	0.000	0.000	0.000
72	A	84	LEU	0	-0.062	-0.015	2.807	-0.879	-0.068	0.365	-0.236	-0.939	-0.001
73	A	85	GLY	0	0.078	0.032	4.349	0.009	0.163	0.000	-0.029	-0.125	0.000
74	A	86	PRO	0	-0.064	-0.037	3.811	-0.648	-0.114	0.008	-0.141	-0.401	-0.001
75	A	87	ASN	0	-0.006	-0.026	4.228	-0.167	-0.128	-0.001	-0.007	-0.031	0.000
76	A	88	MET	0	-0.009	0.020	2.684	-1.022	-0.233	0.324	-0.185	-0.928	-0.002
77	A	89	VAL	0	0.009	0.003	7.129	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	90	MET	0	-0.024	0.001	9.991	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	91	ASP	-1	-0.811	-0.900	11.922	-0.089	-0.089	0.000	0.000	0.000	0.000
80	A	92	TYR	0	-0.030	-0.029	15.682	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	93	ASN	0	-0.046	-0.029	18.890	0.026	0.026	0.000	0.000	0.000	0.000
82	A	94	ALA	0	0.032	0.018	22.040	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	95	GLY	0	-0.031	-0.007	24.338	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	96	SER	0	-0.009	-0.001	19.866	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	97	LEU	0	-0.001	-0.007	14.985	0.011	0.011	0.000	0.000	0.000	0.000
86	A	98	SER	0	-0.025	0.007	15.138	0.010	0.010	0.000	0.000	0.000	0.000
87	A	99	LEU	0	0.052	0.010	7.354	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	100	SER	0	-0.010	-0.004	10.493	0.050	0.050	0.000	0.000	0.000	0.000
89	A	101	SER	0	0.011	0.011	7.392	-0.075	-0.075	0.000	0.000	0.000	0.000
90	A	102	ASP	-1	-0.811	-0.888	8.920	0.659	0.659	0.000	0.000	0.000	0.000
91	A	103	GLU	-1	-0.993	-0.995	9.179	0.127	0.127	0.000	0.000	0.000	0.000
92	A	104	GLY	0	-0.017	0.006	12.005	-0.028	-0.028	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.076	-0.055	11.877	-0.040	-0.040	0.000	0.000	0.000	0.000
94	A	106	LEU	0	-0.012	0.001	7.264	0.002	0.002	0.000	0.000	0.000	0.000
95	A	107	ASP	-1	-0.757	-0.870	11.643	-0.308	-0.308	0.000	0.000	0.000	0.000
96	A	108	GLY	0	-0.005	0.005	14.044	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	109	SER	0	-0.055	-0.026	16.873	0.024	0.024	0.000	0.000	0.000	0.000
98	A	110	VAL	0	-0.033	0.003	12.690	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	111	ASP	-1	-0.836	-0.901	15.645	-0.222	-0.222	0.000	0.000	0.000	0.000
100	A	112	ILE	0	-0.018	-0.018	16.189	-0.036	-0.036	0.000	0.000	0.000	0.000
101	A	113	GLY	0	0.009	0.004	17.568	0.030	0.030	0.000	0.000	0.000	0.000
102	A	114	ASN	0	-0.020	0.000	18.402	-0.025	-0.025	0.000	0.000	0.000	0.000
103	A	115	GLY	0	0.133	0.039	18.716	0.010	0.010	0.000	0.000	0.000	0.000
104	A	116	ALA	0	0.022	0.011	19.482	0.012	0.012	0.000	0.000	0.000	0.000
105	A	117	ALA	0	-0.086	-0.054	22.689	0.014	0.014	0.000	0.000	0.000	0.000
106	A	118	LEU	0	0.053	0.039	19.216	0.015	0.015	0.000	0.000	0.000	0.000
107	A	119	LEU	0	0.025	0.017	19.790	0.015	0.015	0.000	0.000	0.000	0.000
108	A	120	LYS	1	0.898	0.957	23.549	0.148	0.148	0.000	0.000	0.000	0.000
109	A	121	ALA	0	-0.001	-0.003	26.606	0.011	0.011	0.000	0.000	0.000	0.000
110	A	122	ASN	0	0.023	0.016	22.390	0.014	0.014	0.000	0.000	0.000	0.000
111	A	123	LYS	1	0.957	0.973	26.567	0.125	0.125	0.000	0.000	0.000	0.000
112	A	124	ASN	0	-0.074	-0.052	28.802	0.010	0.010	0.000	0.000	0.000	0.000
113	A	125	VAL	0	-0.031	0.007	29.262	0.007	0.007	0.000	0.000	0.000	0.000
114	A	126	GLN	0	-0.044	-0.009	28.149	0.003	0.003	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:4:LEU)