FMO DATABASE

FMODB ID: 5JJ1Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1567880.917213
FMO2-HF: Nuclear repulsion	1505287.145704
FMO2-HF: Total energy	-62593.771509
FMO2-MP2: Total energy	-62775.76943

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.
-3.68	0.153	1.721	-2.101	-3.453	-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 : 0.051 / q_NPA : 0.015

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	0.029	0.022	3.061	-2.038	-0.475	0.016	-0.671	-0.908	0.001
4	A	12	ILE	0	0.010	0.007	2.559	-0.566	0.222	1.472	-0.872	-1.389	-0.002
5	A	13	GLY	0	0.055	0.042	4.738	0.111	0.265	-0.001	-0.011	-0.143	0.000
6	A	14	ASP	-1	-0.801	-0.890	5.771	-0.648	-0.648	0.000	0.000	0.000	0.000
7	A	15	VAL	0	-0.020	-0.006	6.822	0.225	0.225	0.000	0.000	0.000	0.000
8	A	16	VAL	0	-0.014	-0.009	4.296	0.229	0.284	-0.001	-0.009	-0.045	0.000
9	A	17	ASP	-1	-0.841	-0.917	5.744	-0.945	-0.945	0.000	0.000	0.000	0.000
10	A	18	HIS	0	-0.016	-0.020	4.046	-0.890	-0.643	0.000	-0.039	-0.208	0.000
11	A	19	PHE	0	0.039	0.027	2.951	-0.434	0.480	0.237	-0.488	-0.662	-0.003
12	A	20	THR	0	-0.028	-0.017	4.833	0.356	0.432	-0.001	-0.004	-0.070	0.000
13	A	21	SER	0	-0.003	-0.016	5.712	-0.191	-0.191	0.000	0.000	0.000	0.000
14	A	22	THR	0	-0.016	0.003	7.816	0.052	0.052	0.000	0.000	0.000	0.000
15	A	23	VAL	0	-0.014	0.007	10.726	0.001	0.001	0.000	0.000	0.000	0.000
16	A	24	LYS	1	0.927	0.982	10.529	-0.131	-0.131	0.000	0.000	0.000	0.000
17	A	25	MET	0	0.005	-0.002	9.089	-0.011	-0.011	0.000	0.000	0.000	0.000
18	A	26	SER	0	-0.009	0.008	12.034	0.021	0.021	0.000	0.000	0.000	0.000
19	A	27	VAL	0	0.016	0.026	12.647	-0.016	-0.016	0.000	0.000	0.000	0.000
20	A	28	ILE	0	-0.025	-0.027	15.308	0.022	0.022	0.000	0.000	0.000	0.000
21	A	29	TYR	0	0.039	0.012	16.284	-0.023	-0.023	0.000	0.000	0.000	0.000
22	A	30	ASN	0	0.025	-0.021	20.671	0.017	0.017	0.000	0.000	0.000	0.000
23	A	32	SER	0	-0.007	0.021	24.427	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	32	ASN	0	-0.056	-0.056	27.079	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	32	ASN	0	0.050	0.011	27.604	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	32	SER	0	-0.008	0.007	27.295	0.005	0.005	0.000	0.000	0.000	0.000
27	A	32	ILE	0	0.028	0.049	23.255	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	33	LYS	1	0.929	0.966	19.313	0.025	0.025	0.000	0.000	0.000	0.000
29	A	34	HIS	0	0.028	0.032	13.912	-0.022	-0.022	0.000	0.000	0.000	0.000
30	A	35	VAL	0	-0.022	-0.012	11.539	0.020	0.020	0.000	0.000	0.000	0.000
31	A	36	TYR	0	-0.004	0.006	12.168	0.009	0.009	0.000	0.000	0.000	0.000
32	A	37	ASN	0	0.049	-0.010	6.485	-0.321	-0.321	0.000	0.000	0.000	0.000
33	A	38	GLY	0	-0.026	0.008	8.972	0.137	0.137	0.000	0.000	0.000	0.000
34	A	39	HIS	0	-0.028	-0.011	10.055	-0.031	-0.031	0.000	0.000	0.000	0.000
35	A	40	GLU	-1	-0.873	-0.930	13.510	-0.108	-0.108	0.000	0.000	0.000	0.000
36	A	41	LEU	0	-0.051	-0.029	16.114	0.026	0.026	0.000	0.000	0.000	0.000
37	A	42	PHE	0	0.037	0.019	18.277	-0.014	-0.014	0.000	0.000	0.000	0.000
38	A	43	PRO	0	0.026	-0.005	21.445	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	44	SER	0	-0.030	-0.009	22.426	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	45	ALA	0	-0.039	-0.012	21.363	0.005	0.005	0.000	0.000	0.000	0.000
41	A	46	VAL	0	-0.016	0.000	17.909	0.000	0.000	0.000	0.000	0.000	0.000
42	A	47	THR	0	-0.001	-0.012	21.234	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	48	SER	0	0.021	0.020	24.017	0.000	0.000	0.000	0.000	0.000	0.000
44	A	49	THR	0	-0.026	-0.014	21.692	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	50	PRO	0	-0.033	-0.004	17.647	0.015	0.015	0.000	0.000	0.000	0.000
46	A	52	ARG	1	0.968	0.998	20.149	0.050	0.050	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.032	-0.046	14.333	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.875	-0.938	16.974	-0.038	-0.038	0.000	0.000	0.000	0.000
49	A	55	VAL	0	-0.026	-0.032	15.460	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	56	HIS	0	0.018	0.000	14.785	0.019	0.019	0.000	0.000	0.000	0.000
51	A	57	GLY	0	-0.020	-0.009	16.173	0.019	0.019	0.000	0.000	0.000	0.000
52	A	58	GLY	0	0.035	0.004	17.200	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	59	ASP	-1	-0.878	-0.950	18.636	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	60	MET	0	0.056	0.058	22.063	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	61	DAR	1	0.889	0.939	25.403	0.019	0.019	0.000	0.000	0.000	0.000
56	A	62	SER	0	-0.051	-0.030	20.007	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	63	PHE	0	0.037	-0.008	21.087	0.004	0.004	0.000	0.000	0.000	0.000
58	A	64	PHE	0	-0.006	-0.002	15.110	0.002	0.002	0.000	0.000	0.000	0.000
59	A	65	THR	0	0.003	0.002	16.016	0.011	0.011	0.000	0.000	0.000	0.000
60	A	66	LEU	0	-0.029	-0.001	13.191	-0.030	-0.030	0.000	0.000	0.000	0.000
61	A	67	ILE	0	0.041	0.021	12.438	0.033	0.033	0.000	0.000	0.000	0.000
62	A	68	MET	0	-0.021	-0.001	12.345	-0.058	-0.058	0.000	0.000	0.000	0.000
63	A	69	THR	0	-0.051	-0.047	11.034	0.077	0.077	0.000	0.000	0.000	0.000
64	A	70	ASP	-1	-0.711	-0.834	12.439	-0.434	-0.434	0.000	0.000	0.000	0.000
65	A	71	PRO	0	-0.030	-0.015	10.172	0.046	0.046	0.000	0.000	0.000	0.000
66	A	72	ASP	-1	-0.806	-0.892	12.629	-0.497	-0.497	0.000	0.000	0.000	0.000
67	A	73	VAL	0	-0.051	0.008	15.431	0.057	0.057	0.000	0.000	0.000	0.000
68	A	74	PRO	0	0.076	0.017	18.966	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	75	GLY	0	0.051	-0.006	19.387	0.018	0.018	0.000	0.000	0.000	0.000
70	A	76	PRO	0	0.004	0.009	15.259	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	77	SER	0	-0.067	-0.025	16.879	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	78	ASP	-1	-0.917	-0.969	19.518	-0.177	-0.177	0.000	0.000	0.000	0.000
73	A	79	PRO	0	-0.024	0.015	16.039	0.010	0.010	0.000	0.000	0.000	0.000
74	A	80	TYR	0	0.006	-0.018	18.498	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	81	LEU	0	-0.032	-0.025	20.585	0.010	0.010	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.824	0.953	11.706	0.544	0.544	0.000	0.000	0.000	0.000
77	A	83	GLU	-1	-0.775	-0.877	12.751	-0.599	-0.599	0.000	0.000	0.000	0.000
78	A	84	HIS	1	0.838	0.899	16.067	0.271	0.271	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.044	-0.011	16.219	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	86	HIS	0	-0.028	-0.036	16.764	0.023	0.023	0.000	0.000	0.000	0.000
81	A	87	TRP	0	-0.001	-0.011	16.875	0.025	0.025	0.000	0.000	0.000	0.000
82	A	88	ILE	0	-0.004	-0.006	17.082	-0.037	-0.037	0.000	0.000	0.000	0.000
83	A	89	VAL	0	-0.011	0.014	18.157	0.025	0.025	0.000	0.000	0.000	0.000
84	A	90	THR	0	0.003	0.008	18.800	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	91	ASP	-1	-0.781	-0.890	21.024	-0.088	-0.088	0.000	0.000	0.000	0.000
86	A	92	ILE	0	0.038	0.013	17.805	0.011	0.011	0.000	0.000	0.000	0.000
87	A	93	PRO	0	-0.011	-0.005	20.410	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	94	GLY	0	0.049	0.025	19.356	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.110	-0.056	19.422	0.009	0.009	0.000	0.000	0.000	0.000
90	A	95	THR	0	-0.003	0.014	20.934	0.002	0.002	0.000	0.000	0.000	0.000
91	A	96	ASP	-1	-0.751	-0.872	19.591	-0.064	-0.064	0.000	0.000	0.000	0.000
92	A	97	SER	0	-0.001	0.002	18.753	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.133	-0.081	20.576	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	99	PHE	0	-0.007	-0.001	23.777	0.004	0.004	0.000	0.000	0.000	0.000
95	A	100	GLY	0	-0.031	0.001	22.794	0.003	0.003	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.820	0.894	23.826	0.094	0.094	0.000	0.000	0.000	0.000
97	A	102	GLU	-1	-0.920	-0.974	23.467	-0.133	-0.133	0.000	0.000	0.000	0.000
98	A	103	VAL	0	-0.028	-0.005	21.916	0.007	0.007	0.000	0.000	0.000	0.000
99	A	104	VAL	0	-0.005	-0.004	21.004	0.004	0.004	0.000	0.000	0.000	0.000
100	A	105	SER	0	0.049	0.016	22.020	-0.016	-0.016	0.000	0.000	0.000	0.000
101	A	106	TYR	0	0.021	0.011	18.230	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.852	-0.908	21.080	-0.169	-0.169	0.000	0.000	0.000	0.000
103	A	108	MET	0	-0.033	0.006	20.683	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	109	PRO	0	0.010	0.013	17.891	0.000	0.000	0.000	0.000	0.000	0.000
105	A	110	ARG	1	0.917	0.946	20.117	0.138	0.138	0.000	0.000	0.000	0.000
106	A	111	PRO	0	0.004	0.021	18.807	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	112	ASN	0	-0.032	-0.008	20.923	0.026	0.026	0.000	0.000	0.000	0.000
108	A	115	ILE	0	0.051	0.020	22.079	0.017	0.017	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.020	0.000	20.188	-0.021	-0.021	0.000	0.000	0.000	0.000
110	A	117	ILE	0	-0.003	0.000	15.087	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	118	HIS	1	0.767	0.876	14.736	0.241	0.241	0.000	0.000	0.000	0.000
112	A	119	ARG	1	0.777	0.866	7.731	0.913	0.913	0.000	0.000	0.000	0.000
113	A	120	PHE	0	0.021	0.005	11.485	-0.031	-0.031	0.000	0.000	0.000	0.000
114	A	121	VAL	0	-0.034	-0.034	6.860	-0.037	-0.037	0.000	0.000	0.000	0.000
115	A	122	PHE	0	0.024	0.014	9.028	0.093	0.093	0.000	0.000	0.000	0.000
116	A	123	LEU	0	-0.010	-0.012	6.053	-0.192	-0.192	0.000	0.000	0.000	0.000
117	A	124	LEU	0	0.026	0.013	9.413	0.100	0.100	0.000	0.000	0.000	0.000
118	A	125	PHE	0	0.059	0.026	9.788	-0.027	-0.027	0.000	0.000	0.000	0.000
119	A	126	LYS	1	0.953	0.973	13.075	0.070	0.070	0.000	0.000	0.000	0.000
120	A	127	GLN	0	0.005	0.004	16.050	-0.017	-0.017	0.000	0.000	0.000	0.000
121	A	128	LYS	1	0.906	0.956	19.160	0.132	0.132	0.000	0.000	0.000	0.000
122	A	129	LYS	1	0.930	0.937	21.761	0.077	0.077	0.000	0.000	0.000	0.000
123	A	129	ARG	1	0.913	0.998	23.803	0.044	0.044	0.000	0.000	0.000	0.000
124	A	130	GLY	0	-0.042	-0.017	25.199	0.006	0.006	0.000	0.000	0.000	0.000
125	A	143	VAL	0	0.008	-0.013	26.088	0.000	0.000	0.000	0.000	0.000	0.000
126	A	144	VAL	0	-0.015	0.004	20.553	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	145	CYS	0	-0.001	0.003	23.752	0.009	0.009	0.000	0.000	0.000	0.000
128	A	146	ARG	1	0.872	0.921	20.838	0.171	0.171	0.000	0.000	0.000	0.000
129	A	147	ASP	-1	-0.854	-0.926	20.223	-0.219	-0.219	0.000	0.000	0.000	0.000
130	A	148	GLY	0	0.012	0.017	19.851	0.013	0.013	0.000	0.000	0.000	0.000
131	A	149	PHE	0	-0.035	-0.006	14.250	0.006	0.006	0.000	0.000	0.000	0.000
132	A	150	ASN	0	0.038	0.009	14.869	-0.050	-0.050	0.000	0.000	0.000	0.000
133	A	151	THR	0	0.023	-0.013	10.110	0.043	0.043	0.000	0.000	0.000	0.000
134	A	152	ARG	1	0.816	0.910	8.894	0.833	0.833	0.000	0.000	0.000	0.000
135	A	153	LYS	1	0.961	0.978	12.969	0.308	0.308	0.000	0.000	0.000	0.000
136	A	154	PHE	0	0.077	0.048	15.818	0.031	0.031	0.000	0.000	0.000	0.000
137	A	155	THR	0	-0.026	-0.030	12.177	0.031	0.031	0.000	0.000	0.000	0.000
138	A	156	GLN	0	-0.021	-0.001	15.216	0.031	0.031	0.000	0.000	0.000	0.000
139	A	157	GLU	-1	-0.953	-0.978	17.127	-0.165	-0.165	0.000	0.000	0.000	0.000
140	A	158	ASN	0	-0.082	-0.031	18.647	0.037	0.037	0.000	0.000	0.000	0.000
141	A	159	GLU	-1	-0.939	-0.959	18.588	-0.098	-0.098	0.000	0.000	0.000	0.000
142	A	160	LEU	0	-0.019	-0.020	14.770	0.014	0.014	0.000	0.000	0.000	0.000
143	A	161	GLY	0	-0.022	-0.006	14.007	0.000	0.000	0.000	0.000	0.000	0.000
144	A	162	LEU	0	-0.002	0.000	8.439	-0.049	-0.049	0.000	0.000	0.000	0.000
145	A	163	PRO	0	0.015	0.004	5.937	0.049	0.049	0.000	0.000	0.000	0.000
146	A	164	VAL	0	-0.019	-0.006	8.521	0.105	0.105	0.000	0.000	0.000	0.000
147	A	165	ALA	0	-0.002	-0.013	7.134	0.115	0.115	0.000	0.000	0.000	0.000
148	A	166	ALA	0	-0.014	-0.019	4.502	-0.177	-0.141	-0.001	-0.007	-0.028	0.000
149	A	167	VAL	0	-0.064	-0.014	5.945	0.101	0.101	0.000	0.000	0.000	0.000
150	A	168	PHE	0	0.002	-0.001	5.536	-0.116	-0.116	0.000	0.000	0.000	0.000
151	A	169	PHE	0	0.047	0.026	8.456	0.154	0.154	0.000	0.000	0.000	0.000
152	A	170	ASN	0	0.006	0.001	11.420	-0.136	-0.136	0.000	0.000	0.000	0.000
153	A	171	CYS	0	-0.031	-0.013	13.514	0.038	0.038	0.000	0.000	0.000	0.000
154	A	172	GLN	0	0.012	-0.001	17.051	-0.026	-0.026	0.000	0.000	0.000	0.000
155	A	173	ARG	1	0.879	0.937	20.146	0.107	0.107	0.000	0.000	0.000	0.000
156	A	174	GLU	-1	-0.797	-0.909	23.744	-0.065	-0.065	0.000	0.000	0.000	0.000
157	A	175	THR	0	-0.040	-0.020	26.495	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:GLY)