FMO DATABASE

FMODB ID: YVV82

Calculation Name: 1QOU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1QOU

Chain ID: A

ChEMBL ID:

UniProt ID: Q41261

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	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	157
LigandResidueName
LigandFragmentNumber	0
LigandCharge	DAR=1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1570819.008835
FMO2-HF: Nuclear repulsion	1508224.562747
FMO2-HF: Total energy	-62594.446088
FMO2-MP2: Total energy	-62776.475361

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:9:GLY)

Summations of interaction energy for fragment #1(A:9: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.
-3.304	0.623	1.218	-1.874	-3.271	-0.004

Interaction energy analysis for fragmet #1(A:9:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.054 / 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	11	VAL	0	0.023	0.018	2.996	-1.857	-0.322	0.019	-0.652	-0.902	0.001
4	A	12	ILE	0	0.017	0.010	2.591	-0.520	0.398	1.037	-0.714	-1.242	-0.002
5	A	13	GLY	0	0.048	0.042	4.740	0.141	0.299	-0.001	-0.011	-0.146	0.000
6	A	14	ASP	-1	-0.782	-0.858	5.772	-0.662	-0.662	0.000	0.000	0.000	0.000
7	A	15	VAL	0	-0.032	-0.012	6.900	0.223	0.223	0.000	0.000	0.000	0.000
8	A	16	VAL	0	-0.001	-0.005	4.311	0.227	0.284	-0.001	-0.009	-0.047	0.000
9	A	17	ASP	-1	-0.819	-0.883	5.743	-1.020	-1.020	0.000	0.000	0.000	0.000
10	A	18	HIS	0	0.000	0.001	4.030	-0.930	-0.570	0.003	-0.078	-0.285	0.000
11	A	19	PHE	0	0.040	0.023	2.976	-0.342	0.442	0.163	-0.398	-0.549	-0.003
12	A	20	THR	0	-0.022	-0.012	4.835	0.383	0.459	-0.001	-0.004	-0.070	0.000
13	A	21	SER	0	-0.009	-0.023	5.642	-0.177	-0.177	0.000	0.000	0.000	0.000
14	A	22	THR	0	-0.013	0.005	7.834	0.043	0.043	0.000	0.000	0.000	0.000
15	A	23	VAL	0	-0.018	0.012	10.729	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.933	0.976	10.525	-0.130	-0.130	0.000	0.000	0.000	0.000
17	A	25	MET	0	-0.010	-0.009	8.945	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	26	SER	0	-0.014	0.006	12.012	0.025	0.025	0.000	0.000	0.000	0.000
19	A	27	VAL	0	0.015	0.022	12.687	-0.017	-0.017	0.000	0.000	0.000	0.000
20	A	28	ILE	0	-0.023	-0.024	15.267	0.021	0.021	0.000	0.000	0.000	0.000
21	A	29	TYR	0	0.023	-0.005	16.192	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	30	ASN	0	0.026	-0.012	20.708	0.016	0.016	0.000	0.000	0.000	0.000
23	A	32	SER	0	-0.013	0.012	24.463	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	32	ASN	0	-0.050	-0.045	27.113	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	32	ASN	0	0.031	0.012	27.837	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	32	SER	0	0.007	0.008	27.264	0.007	0.007	0.000	0.000	0.000	0.000
27	A	32	ILE	0	0.037	0.050	23.276	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	33	LYS	1	0.937	0.964	19.405	0.021	0.021	0.000	0.000	0.000	0.000
29	A	34	HIS	0	0.039	0.037	13.695	-0.018	-0.018	0.000	0.000	0.000	0.000
30	A	35	VAL	0	-0.015	-0.008	11.542	0.018	0.018	0.000	0.000	0.000	0.000
31	A	36	TYR	0	-0.017	-0.003	12.149	0.014	0.014	0.000	0.000	0.000	0.000
32	A	37	ASN	0	0.056	-0.001	6.240	-0.306	-0.306	0.000	0.000	0.000	0.000
33	A	38	GLY	0	-0.014	0.015	8.975	0.135	0.135	0.000	0.000	0.000	0.000
34	A	39	HIS	0	-0.030	-0.011	10.036	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	40	GLU	-1	-0.855	-0.910	13.505	-0.125	-0.125	0.000	0.000	0.000	0.000
36	A	41	LEU	0	-0.057	-0.027	16.047	0.028	0.028	0.000	0.000	0.000	0.000
37	A	42	PHE	0	0.063	0.033	18.281	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	43	PRO	0	0.027	-0.004	21.457	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	44	SER	0	-0.031	-0.018	22.438	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	45	ALA	0	-0.070	-0.021	21.461	0.005	0.005	0.000	0.000	0.000	0.000
41	A	46	VAL	0	-0.014	-0.001	17.995	0.000	0.000	0.000	0.000	0.000	0.000
42	A	47	THR	0	0.022	0.005	21.262	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	48	SER	0	-0.007	-0.003	24.092	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	49	THR	0	-0.002	-0.001	21.612	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	50	PRO	0	-0.042	0.000	17.599	0.015	0.015	0.000	0.000	0.000	0.000
46	A	52	ARG	1	0.877	0.934	20.189	0.044	0.044	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.046	-0.041	14.222	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.834	-0.923	16.972	-0.034	-0.034	0.000	0.000	0.000	0.000
49	A	55	VAL	0	-0.027	-0.033	15.372	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	56	HIS	0	0.005	-0.003	14.756	0.022	0.022	0.000	0.000	0.000	0.000
51	A	57	GLY	0	-0.015	-0.002	16.146	0.018	0.018	0.000	0.000	0.000	0.000
52	A	58	GLY	0	0.037	0.007	17.195	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	59	ASP	-1	-0.884	-0.950	18.629	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	60	MET	0	0.069	0.032	22.060	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	61	DAR	1	0.916	0.962	25.305	0.013	0.013	0.000	0.000	0.000	0.000
56	A	62	SER	0	-0.028	-0.003	20.031	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	63	PHE	0	0.037	-0.009	21.060	0.004	0.004	0.000	0.000	0.000	0.000
58	A	64	PHE	0	0.007	0.004	15.006	0.003	0.003	0.000	0.000	0.000	0.000
59	A	65	THR	0	0.008	0.008	15.988	0.010	0.010	0.000	0.000	0.000	0.000
60	A	66	LEU	0	-0.021	-0.003	12.981	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	67	ILE	0	0.034	0.022	12.453	0.031	0.031	0.000	0.000	0.000	0.000
62	A	68	MET	0	-0.019	0.004	12.345	-0.055	-0.055	0.000	0.000	0.000	0.000
63	A	69	THR	0	-0.041	-0.048	10.975	0.076	0.076	0.000	0.000	0.000	0.000
64	A	70	ASP	-1	-0.738	-0.842	12.470	-0.433	-0.433	0.000	0.000	0.000	0.000
65	A	71	PRO	0	-0.018	-0.012	10.102	0.050	0.050	0.000	0.000	0.000	0.000
66	A	72	ASP	-1	-0.787	-0.874	12.608	-0.543	-0.543	0.000	0.000	0.000	0.000
67	A	73	VAL	0	-0.039	0.015	15.425	0.058	0.058	0.000	0.000	0.000	0.000
68	A	74	PRO	0	0.069	0.015	18.968	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	75	GLY	0	0.047	-0.009	19.375	0.018	0.018	0.000	0.000	0.000	0.000
70	A	76	PRO	0	-0.006	0.002	15.195	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	77	SER	0	-0.061	-0.027	16.856	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.898	-0.959	19.486	-0.188	-0.188	0.000	0.000	0.000	0.000
73	A	79	PRO	0	-0.045	0.006	15.962	0.009	0.009	0.000	0.000	0.000	0.000
74	A	80	TYR	0	0.031	-0.005	18.500	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	81	LEU	0	-0.041	-0.027	20.611	0.010	0.010	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.779	0.917	11.517	0.585	0.585	0.000	0.000	0.000	0.000
77	A	83	GLU	-1	-0.757	-0.855	12.794	-0.593	-0.593	0.000	0.000	0.000	0.000
78	A	84	HIS	1	0.800	0.859	16.068	0.271	0.271	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.040	-0.009	16.197	-0.030	-0.030	0.000	0.000	0.000	0.000
80	A	86	HIS	0	-0.018	-0.038	16.825	0.022	0.022	0.000	0.000	0.000	0.000
81	A	87	TRP	0	-0.025	-0.020	17.085	0.023	0.023	0.000	0.000	0.000	0.000
82	A	88	ILE	0	-0.009	-0.006	17.081	-0.036	-0.036	0.000	0.000	0.000	0.000
83	A	89	VAL	0	0.001	0.024	18.156	0.025	0.025	0.000	0.000	0.000	0.000
84	A	90	THR	0	0.001	-0.009	18.799	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	91	ASP	-1	-0.785	-0.883	21.023	-0.080	-0.080	0.000	0.000	0.000	0.000
86	A	92	ILE	0	0.048	0.018	17.922	0.011	0.011	0.000	0.000	0.000	0.000
87	A	93	PRO	0	-0.007	0.002	20.379	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	94	GLY	0	0.043	0.030	19.336	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.111	-0.057	19.405	0.008	0.008	0.000	0.000	0.000	0.000
90	A	95	THR	0	-0.014	-0.001	20.917	0.002	0.002	0.000	0.000	0.000	0.000
91	A	96	ASP	-1	-0.713	-0.830	19.555	-0.061	-0.061	0.000	0.000	0.000	0.000
92	A	97	SER	0	0.027	0.002	18.662	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.094	-0.062	20.531	0.000	0.000	0.000	0.000	0.000	0.000
94	A	99	PHE	0	-0.024	-0.010	23.708	0.004	0.004	0.000	0.000	0.000	0.000
95	A	100	GLY	0	-0.029	0.004	22.746	0.003	0.003	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.831	0.899	23.785	0.089	0.089	0.000	0.000	0.000	0.000
97	A	102	GLU	-1	-0.848	-0.949	23.449	-0.141	-0.141	0.000	0.000	0.000	0.000
98	A	103	VAL	0	-0.033	-0.011	21.921	0.008	0.008	0.000	0.000	0.000	0.000
99	A	104	VAL	0	-0.008	-0.003	20.951	0.004	0.004	0.000	0.000	0.000	0.000
100	A	105	SER	0	0.045	0.015	22.020	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.008	0.014	18.372	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.836	-0.894	21.119	-0.175	-0.175	0.000	0.000	0.000	0.000
103	A	108	MET	0	-0.018	0.021	20.720	-0.014	-0.014	0.000	0.000	0.000	0.000
104	A	109	PRO	0	0.023	0.021	17.799	0.001	0.001	0.000	0.000	0.000	0.000
105	A	110	ARG	1	0.881	0.917	20.140	0.148	0.148	0.000	0.000	0.000	0.000
106	A	111	PRO	0	0.020	0.031	18.823	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	112	ASN	0	-0.004	0.003	20.927	0.027	0.027	0.000	0.000	0.000	0.000
108	A	115	ILE	0	0.036	0.018	22.218	0.018	0.018	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.028	0.008	20.166	-0.022	-0.022	0.000	0.000	0.000	0.000
110	A	117	ILE	0	0.009	0.004	15.249	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	118	HIS	1	0.758	0.872	14.730	0.250	0.250	0.000	0.000	0.000	0.000
112	A	119	ARG	1	0.756	0.827	7.788	0.975	0.975	0.000	0.000	0.000	0.000
113	A	120	PHE	0	0.018	0.004	11.485	-0.029	-0.029	0.000	0.000	0.000	0.000
114	A	121	VAL	0	-0.031	-0.032	6.878	-0.037	-0.037	0.000	0.000	0.000	0.000
115	A	122	PHE	0	0.020	0.014	9.070	0.092	0.092	0.000	0.000	0.000	0.000
116	A	123	LEU	0	-0.015	-0.014	5.725	-0.173	-0.173	0.000	0.000	0.000	0.000
117	A	124	LEU	0	0.022	0.013	9.412	0.097	0.097	0.000	0.000	0.000	0.000
118	A	125	PHE	0	0.063	0.023	9.651	-0.023	-0.023	0.000	0.000	0.000	0.000
119	A	126	LYS	1	0.907	0.957	13.073	0.055	0.055	0.000	0.000	0.000	0.000
120	A	127	GLN	0	0.015	0.007	16.048	-0.017	-0.017	0.000	0.000	0.000	0.000
121	A	128	LYS	1	0.904	0.957	19.158	0.124	0.124	0.000	0.000	0.000	0.000
122	A	129	LYS	1	0.885	0.920	21.759	0.077	0.077	0.000	0.000	0.000	0.000
123	A	129	ARG	1	0.911	0.985	23.801	0.039	0.039	0.000	0.000	0.000	0.000
124	A	130	GLY	0	-0.060	-0.022	24.718	0.004	0.004	0.000	0.000	0.000	0.000
125	A	143	VAL	0	0.001	-0.018	25.801	0.000	0.000	0.000	0.000	0.000	0.000
126	A	144	VAL	0	-0.008	0.007	20.515	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	145	CYS	0	-0.008	0.006	23.761	0.009	0.009	0.000	0.000	0.000	0.000
128	A	146	ARG	1	0.862	0.912	20.840	0.174	0.174	0.000	0.000	0.000	0.000
129	A	147	ASP	-1	-0.863	-0.921	20.224	-0.227	-0.227	0.000	0.000	0.000	0.000
130	A	148	GLY	0	0.035	0.030	19.852	0.013	0.013	0.000	0.000	0.000	0.000
131	A	149	PHE	0	-0.036	-0.005	14.223	0.007	0.007	0.000	0.000	0.000	0.000
132	A	150	ASN	0	0.028	-0.002	15.053	-0.034	-0.034	0.000	0.000	0.000	0.000
133	A	151	THR	0	0.013	-0.018	9.973	0.039	0.039	0.000	0.000	0.000	0.000
134	A	152	ARG	1	0.788	0.876	8.554	0.883	0.883	0.000	0.000	0.000	0.000
135	A	153	LYS	1	0.979	0.989	12.968	0.297	0.297	0.000	0.000	0.000	0.000
136	A	154	PHE	0	0.078	0.049	15.685	0.031	0.031	0.000	0.000	0.000	0.000
137	A	155	THR	0	-0.017	-0.031	11.986	0.032	0.032	0.000	0.000	0.000	0.000
138	A	156	GLN	0	-0.032	-0.003	15.215	0.028	0.028	0.000	0.000	0.000	0.000
139	A	157	GLU	-1	-0.946	-0.978	17.126	-0.175	-0.175	0.000	0.000	0.000	0.000
140	A	158	ASN	0	-0.091	-0.038	18.636	0.036	0.036	0.000	0.000	0.000	0.000
141	A	159	GLU	-1	-0.921	-0.954	18.558	-0.097	-0.097	0.000	0.000	0.000	0.000
142	A	160	LEU	0	-0.022	-0.018	14.808	0.014	0.014	0.000	0.000	0.000	0.000
143	A	161	GLY	0	-0.025	-0.007	14.004	0.002	0.002	0.000	0.000	0.000	0.000
144	A	162	LEU	0	0.000	-0.001	8.546	-0.048	-0.048	0.000	0.000	0.000	0.000
145	A	163	PRO	0	0.017	0.009	5.893	0.049	0.049	0.000	0.000	0.000	0.000
146	A	164	VAL	0	-0.031	-0.015	8.527	0.111	0.111	0.000	0.000	0.000	0.000
147	A	165	ALA	0	0.001	-0.015	7.120	0.124	0.124	0.000	0.000	0.000	0.000
148	A	166	ALA	0	0.006	-0.005	4.337	-0.177	-0.138	-0.001	-0.008	-0.030	0.000
149	A	167	VAL	0	-0.077	-0.024	5.907	0.109	0.109	0.000	0.000	0.000	0.000
150	A	168	PHE	0	0.006	-0.004	5.562	-0.118	-0.118	0.000	0.000	0.000	0.000
151	A	169	PHE	0	0.040	0.019	8.480	0.149	0.149	0.000	0.000	0.000	0.000
152	A	170	ASN	0	0.000	0.000	11.328	-0.135	-0.135	0.000	0.000	0.000	0.000
153	A	171	CYS	0	-0.045	-0.029	13.508	0.040	0.040	0.000	0.000	0.000	0.000
154	A	172	GLN	0	-0.005	-0.024	17.049	-0.027	-0.027	0.000	0.000	0.000	0.000
155	A	173	ARG	1	0.853	0.920	20.138	0.114	0.114	0.000	0.000	0.000	0.000
156	A	174	GLU	-1	-0.776	-0.892	23.740	-0.067	-0.067	0.000	0.000	0.000	0.000
157	A	175	THR	0	-0.040	-0.019	26.491	0.000	0.000	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:9:GLY)