FMO DATABASE

FMODB ID: VQQL1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1580376.768612
FMO2-HF: Nuclear repulsion	1517781.874253
FMO2-HF: Total energy	-62594.894359
FMO2-MP2: Total energy	-62776.964781

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.
-1.903	1.959	2.815	-2.787	-3.887	-0.013

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 : 0.067 / q_NPA : 0.022

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	0.008	0.016	3.441	-1.092	0.116	-0.001	-0.519	-0.688	0.000
4	A	12	ILE	0	0.033	0.017	2.468	-0.010	0.414	1.457	-0.793	-1.087	-0.002
5	A	13	GLY	0	0.060	0.045	4.838	0.195	0.331	-0.001	-0.010	-0.124	0.000
6	A	14	ASP	-1	-0.764	-0.834	5.943	-0.631	-0.631	0.000	0.000	0.000	0.000
7	A	15	VAL	0	-0.039	-0.011	6.879	0.191	0.191	0.000	0.000	0.000	0.000
8	A	16	VAL	0	0.004	-0.011	4.368	0.191	0.241	-0.001	-0.009	-0.040	0.000
9	A	17	ASP	-1	-0.802	-0.872	5.832	-0.780	-0.780	0.000	0.000	0.000	0.000
10	A	18	HIS	0	-0.008	-0.001	3.764	-0.499	-0.094	0.005	-0.083	-0.327	0.000
11	A	19	PHE	0	0.056	0.033	2.648	-1.191	0.316	1.358	-1.348	-1.517	-0.011
12	A	20	THR	0	-0.010	-0.016	4.510	0.852	0.915	-0.001	-0.011	-0.050	0.000
13	A	21	SER	0	-0.013	-0.014	5.251	-0.291	-0.291	0.000	0.000	0.000	0.000
14	A	22	THR	0	-0.018	-0.008	7.050	0.072	0.072	0.000	0.000	0.000	0.000
15	A	23	VAL	0	-0.017	0.004	10.141	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.887	0.959	10.090	-0.083	-0.083	0.000	0.000	0.000	0.000
17	A	25	MET	0	-0.004	-0.004	8.982	0.002	0.002	0.000	0.000	0.000	0.000
18	A	26	SER	0	-0.036	-0.011	11.972	0.019	0.019	0.000	0.000	0.000	0.000
19	A	27	VAL	0	-0.002	0.008	12.649	-0.013	-0.013	0.000	0.000	0.000	0.000
20	A	28	ILE	0	-0.024	-0.008	15.222	0.015	0.015	0.000	0.000	0.000	0.000
21	A	29	TYR	0	0.050	0.015	16.273	-0.017	-0.017	0.000	0.000	0.000	0.000
22	A	30	ASN	0	-0.019	-0.029	20.604	0.011	0.011	0.000	0.000	0.000	0.000
23	A	32	SER	0	0.025	0.044	24.419	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	32	ASN	0	-0.027	-0.033	27.194	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	32	ASN	0	0.023	0.013	27.929	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	32	SER	0	-0.003	-0.008	27.301	0.008	0.008	0.000	0.000	0.000	0.000
27	A	32	ILE	0	0.041	0.037	23.008	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	33	LYS	1	0.952	0.966	19.047	0.091	0.091	0.000	0.000	0.000	0.000
29	A	34	HIS	0	0.030	0.029	13.722	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	35	VAL	0	-0.009	0.002	11.760	0.009	0.009	0.000	0.000	0.000	0.000
31	A	36	TYR	0	-0.017	-0.011	11.696	0.020	0.020	0.000	0.000	0.000	0.000
32	A	37	ASN	0	0.045	0.003	6.031	-0.285	-0.285	0.000	0.000	0.000	0.000
33	A	38	GLY	0	-0.006	0.014	8.801	0.109	0.109	0.000	0.000	0.000	0.000
34	A	39	HIS	0	-0.018	0.001	10.400	0.025	0.025	0.000	0.000	0.000	0.000
35	A	40	GLU	-1	-0.872	-0.920	13.822	-0.209	-0.209	0.000	0.000	0.000	0.000
36	A	41	LEU	0	-0.067	-0.035	16.296	0.031	0.031	0.000	0.000	0.000	0.000
37	A	42	PHE	0	0.069	0.036	18.744	-0.015	-0.015	0.000	0.000	0.000	0.000
38	A	43	PRO	0	0.010	-0.002	21.937	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	44	SER	0	-0.042	-0.038	22.847	0.000	0.000	0.000	0.000	0.000	0.000
40	A	45	ALA	0	-0.083	-0.034	21.892	0.007	0.007	0.000	0.000	0.000	0.000
41	A	46	VAL	0	-0.024	-0.010	18.309	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	47	THR	0	0.007	-0.004	21.493	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	48	SER	0	0.012	-0.005	24.152	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	49	THR	0	0.015	0.003	21.623	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	50	PRO	0	-0.057	-0.004	17.650	0.014	0.014	0.000	0.000	0.000	0.000
46	A	52	ARG	1	0.852	0.925	20.235	0.072	0.072	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.032	-0.033	14.264	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.840	-0.924	16.678	-0.063	-0.063	0.000	0.000	0.000	0.000
49	A	55	VAL	0	-0.012	-0.020	15.165	-0.015	-0.015	0.000	0.000	0.000	0.000
50	A	56	HIS	0	0.018	-0.004	15.213	0.038	0.038	0.000	0.000	0.000	0.000
51	A	57	GLY	0	-0.009	-0.006	16.286	0.024	0.024	0.000	0.000	0.000	0.000
52	A	58	GLY	0	0.049	0.021	17.124	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	59	ASP	-1	-0.820	-0.893	18.303	0.015	0.015	0.000	0.000	0.000	0.000
54	A	60	MET	0	0.052	0.019	21.524	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	61	DAR	1	0.900	0.960	24.165	0.003	0.003	0.000	0.000	0.000	0.000
56	A	62	SER	0	-0.048	-0.028	19.147	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	63	PHE	0	0.041	0.003	20.431	0.002	0.002	0.000	0.000	0.000	0.000
58	A	64	PHE	0	0.013	0.006	14.611	0.007	0.007	0.000	0.000	0.000	0.000
59	A	65	THR	0	0.012	0.013	15.781	0.008	0.008	0.000	0.000	0.000	0.000
60	A	66	LEU	0	-0.022	-0.006	12.805	-0.020	-0.020	0.000	0.000	0.000	0.000
61	A	67	ILE	0	0.018	0.009	11.906	0.028	0.028	0.000	0.000	0.000	0.000
62	A	68	MET	0	-0.015	0.006	11.955	-0.049	-0.049	0.000	0.000	0.000	0.000
63	A	69	THR	0	-0.030	-0.044	10.434	0.072	0.072	0.000	0.000	0.000	0.000
64	A	70	ASP	-1	-0.738	-0.837	12.221	-0.438	-0.438	0.000	0.000	0.000	0.000
65	A	71	PRO	0	-0.024	-0.009	9.777	0.049	0.049	0.000	0.000	0.000	0.000
66	A	72	ASP	-1	-0.753	-0.865	12.727	-0.585	-0.585	0.000	0.000	0.000	0.000
67	A	73	VAL	0	-0.026	0.021	15.205	0.049	0.049	0.000	0.000	0.000	0.000
68	A	74	PRO	0	0.030	0.008	18.656	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	75	GLY	0	0.045	-0.012	19.307	0.011	0.011	0.000	0.000	0.000	0.000
70	A	76	PRO	0	-0.003	0.009	15.276	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	77	SER	0	-0.055	-0.034	16.785	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.882	-0.941	19.464	-0.173	-0.173	0.000	0.000	0.000	0.000
73	A	79	PRO	0	-0.035	0.008	15.799	0.009	0.009	0.000	0.000	0.000	0.000
74	A	80	TYR	0	-0.006	-0.019	18.275	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	81	LEU	0	-0.024	-0.016	20.102	0.015	0.015	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.756	0.891	11.486	0.557	0.557	0.000	0.000	0.000	0.000
77	A	83	GLU	-1	-0.779	-0.865	12.263	-0.537	-0.537	0.000	0.000	0.000	0.000
78	A	84	HIS	1	0.781	0.835	15.705	0.277	0.277	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.030	-0.008	15.578	-0.028	-0.028	0.000	0.000	0.000	0.000
80	A	86	HIS	0	-0.016	-0.031	16.221	0.020	0.020	0.000	0.000	0.000	0.000
81	A	87	TRP	0	-0.060	-0.051	16.733	0.020	0.020	0.000	0.000	0.000	0.000
82	A	88	ILE	0	0.003	0.006	16.383	-0.034	-0.034	0.000	0.000	0.000	0.000
83	A	89	VAL	0	0.021	0.024	17.708	0.025	0.025	0.000	0.000	0.000	0.000
84	A	90	THR	0	0.003	-0.010	18.195	-0.010	-0.010	0.000	0.000	0.000	0.000
85	A	91	ASP	-1	-0.773	-0.864	20.480	-0.071	-0.071	0.000	0.000	0.000	0.000
86	A	92	ILE	0	0.048	0.029	17.507	0.010	0.010	0.000	0.000	0.000	0.000
87	A	93	PRO	0	-0.004	-0.003	20.147	0.002	0.002	0.000	0.000	0.000	0.000
88	A	94	GLY	0	0.037	0.024	18.937	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.130	-0.063	18.992	0.009	0.009	0.000	0.000	0.000	0.000
90	A	95	THR	0	-0.002	0.001	20.263	0.001	0.001	0.000	0.000	0.000	0.000
91	A	96	ASP	-1	-0.657	-0.800	19.332	-0.090	-0.090	0.000	0.000	0.000	0.000
92	A	97	SER	0	-0.023	-0.019	18.690	0.000	0.000	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.063	-0.056	20.248	0.002	0.002	0.000	0.000	0.000	0.000
94	A	99	PHE	0	-0.011	-0.002	23.345	0.008	0.008	0.000	0.000	0.000	0.000
95	A	100	GLY	0	-0.029	-0.007	22.454	0.005	0.005	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.834	0.908	23.392	0.081	0.081	0.000	0.000	0.000	0.000
97	A	102	GLU	-1	-0.805	-0.912	22.512	-0.150	-0.150	0.000	0.000	0.000	0.000
98	A	103	VAL	0	-0.058	-0.028	21.245	0.011	0.011	0.000	0.000	0.000	0.000
99	A	104	VAL	0	0.003	0.000	20.296	0.005	0.005	0.000	0.000	0.000	0.000
100	A	105	SER	0	0.049	0.025	21.132	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.001	0.019	18.528	-0.024	-0.024	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.831	-0.887	20.675	-0.185	-0.185	0.000	0.000	0.000	0.000
103	A	108	MET	0	-0.026	0.025	20.402	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	109	PRO	0	0.005	0.017	17.699	0.005	0.005	0.000	0.000	0.000	0.000
105	A	110	ARG	1	0.868	0.903	20.077	0.176	0.176	0.000	0.000	0.000	0.000
106	A	111	PRO	0	0.034	0.049	18.888	0.004	0.004	0.000	0.000	0.000	0.000
107	A	112	ASN	0	0.019	0.009	20.937	0.025	0.025	0.000	0.000	0.000	0.000
108	A	115	ILE	0	0.019	0.009	22.163	0.017	0.017	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.050	0.021	20.581	-0.022	-0.022	0.000	0.000	0.000	0.000
110	A	117	ILE	0	0.002	-0.002	15.616	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	118	HIS	1	0.738	0.846	15.066	0.287	0.287	0.000	0.000	0.000	0.000
112	A	119	ARG	1	0.713	0.798	7.965	0.979	0.979	0.000	0.000	0.000	0.000
113	A	120	PHE	0	0.041	0.010	11.782	-0.025	-0.025	0.000	0.000	0.000	0.000
114	A	121	VAL	0	-0.024	-0.020	6.479	-0.055	-0.055	0.000	0.000	0.000	0.000
115	A	122	PHE	0	0.009	0.001	8.832	0.133	0.133	0.000	0.000	0.000	0.000
116	A	123	LEU	0	-0.023	-0.022	5.354	-0.196	-0.196	0.000	0.000	0.000	0.000
117	A	124	LEU	0	0.034	0.018	8.953	0.097	0.097	0.000	0.000	0.000	0.000
118	A	125	PHE	0	0.044	0.017	9.311	-0.014	-0.014	0.000	0.000	0.000	0.000
119	A	126	LYS	1	0.885	0.937	12.907	0.021	0.021	0.000	0.000	0.000	0.000
120	A	127	GLN	0	0.014	0.002	15.870	-0.011	-0.011	0.000	0.000	0.000	0.000
121	A	128	LYS	1	0.843	0.902	19.046	0.088	0.088	0.000	0.000	0.000	0.000
122	A	129	LYS	1	0.881	0.929	21.367	0.063	0.063	0.000	0.000	0.000	0.000
123	A	129	ARG	1	0.903	0.986	23.432	0.033	0.033	0.000	0.000	0.000	0.000
124	A	130	GLY	0	-0.064	-0.040	24.493	0.008	0.008	0.000	0.000	0.000	0.000
125	A	143	VAL	0	-0.011	-0.018	25.421	0.000	0.000	0.000	0.000	0.000	0.000
126	A	144	VAL	0	0.005	0.003	20.257	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	145	CYS	0	-0.016	0.001	23.329	0.005	0.005	0.000	0.000	0.000	0.000
128	A	146	ARG	1	0.861	0.912	20.426	0.179	0.179	0.000	0.000	0.000	0.000
129	A	147	ASP	-1	-0.840	-0.899	19.432	-0.231	-0.231	0.000	0.000	0.000	0.000
130	A	148	GLY	0	0.022	0.024	19.766	0.016	0.016	0.000	0.000	0.000	0.000
131	A	149	PHE	0	-0.026	0.000	14.028	0.008	0.008	0.000	0.000	0.000	0.000
132	A	150	ASN	0	0.010	-0.006	14.384	-0.020	-0.020	0.000	0.000	0.000	0.000
133	A	151	THR	0	0.018	-0.019	9.806	0.043	0.043	0.000	0.000	0.000	0.000
134	A	152	ARG	1	0.761	0.871	8.704	0.722	0.722	0.000	0.000	0.000	0.000
135	A	153	LYS	1	0.972	0.995	12.583	0.243	0.243	0.000	0.000	0.000	0.000
136	A	154	PHE	0	0.069	0.042	15.204	0.026	0.026	0.000	0.000	0.000	0.000
137	A	155	THR	0	-0.019	-0.037	11.468	0.029	0.029	0.000	0.000	0.000	0.000
138	A	156	GLN	0	-0.030	-0.011	14.700	0.023	0.023	0.000	0.000	0.000	0.000
139	A	157	GLU	-1	-0.950	-0.987	16.818	-0.153	-0.153	0.000	0.000	0.000	0.000
140	A	158	ASN	0	-0.077	-0.037	18.139	0.027	0.027	0.000	0.000	0.000	0.000
141	A	159	GLU	-1	-0.867	-0.919	18.142	-0.065	-0.065	0.000	0.000	0.000	0.000
142	A	160	LEU	0	-0.035	-0.014	14.430	0.014	0.014	0.000	0.000	0.000	0.000
143	A	161	GLY	0	-0.002	0.007	13.414	0.006	0.006	0.000	0.000	0.000	0.000
144	A	162	LEU	0	0.004	-0.006	7.830	-0.045	-0.045	0.000	0.000	0.000	0.000
145	A	163	PRO	0	-0.009	-0.001	5.544	0.036	0.036	0.000	0.000	0.000	0.000
146	A	164	VAL	0	-0.009	-0.001	7.813	0.103	0.103	0.000	0.000	0.000	0.000
147	A	165	ALA	0	0.000	-0.007	7.028	0.101	0.101	0.000	0.000	0.000	0.000
148	A	166	ALA	0	0.014	-0.006	4.107	-0.168	-0.099	-0.001	-0.014	-0.054	0.000
149	A	167	VAL	0	-0.071	-0.019	6.247	0.086	0.086	0.000	0.000	0.000	0.000
150	A	168	PHE	0	0.011	0.007	5.915	-0.069	-0.069	0.000	0.000	0.000	0.000
151	A	169	PHE	0	0.025	0.013	8.679	0.107	0.107	0.000	0.000	0.000	0.000
152	A	170	ASN	0	-0.002	-0.003	11.816	-0.102	-0.102	0.000	0.000	0.000	0.000
153	A	171	CYS	0	-0.016	-0.017	14.015	0.038	0.038	0.000	0.000	0.000	0.000
154	A	172	GLN	0	0.012	-0.011	17.539	-0.020	-0.020	0.000	0.000	0.000	0.000
155	A	173	ARG	1	0.879	0.935	20.628	0.132	0.132	0.000	0.000	0.000	0.000
156	A	174	GLU	-1	-0.736	-0.863	24.223	-0.104	-0.104	0.000	0.000	0.000	0.000
157	A	175	THR	0	-0.059	-0.022	26.744	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:9:GLY)