FMO DATABASE

FMODB ID: 7G8YK

Calculation Name: 1Q6W-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1Q6W

Chain ID: A

ChEMBL ID:

UniProt ID: O28346

Base Structure: X-ray

Registration Date: 2023-06-21

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	151
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1348890.26364
FMO2-HF: Nuclear repulsion	1290917.966509
FMO2-HF: Total energy	-57972.297131
FMO2-MP2: Total energy	-58145.186638

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:ALA)

Summations of interaction energy for fragment #1(A:9:ALA)

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.
-4.825	1.368	2.798	-3.343	-5.647	-0.021

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.009 / q_NPA : -0.001

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	ASN	0	0.008	0.003	3.843	-1.167	-0.017	-0.013	-0.651	-0.486	0.003
4	A	12	PRO	0	-0.026	0.009	5.759	0.037	0.037	0.000	0.000	0.000	0.000
5	A	13	ILE	0	0.044	0.027	6.881	0.159	0.159	0.000	0.000	0.000	0.000
6	A	14	TYR	0	0.038	0.034	9.562	-0.006	-0.006	0.000	0.000	0.000	0.000
7	A	15	PHE	0	0.017	-0.017	12.885	0.039	0.039	0.000	0.000	0.000	0.000
8	A	16	GLU	-1	-0.845	-0.949	16.029	-0.158	-0.158	0.000	0.000	0.000	0.000
9	A	17	SER	0	-0.095	-0.043	13.036	0.000	0.000	0.000	0.000	0.000	0.000
10	A	18	ILE	0	0.003	0.030	12.138	0.031	0.031	0.000	0.000	0.000	0.000
11	A	19	GLN	0	-0.047	-0.023	15.655	0.017	0.017	0.000	0.000	0.000	0.000
12	A	20	ILE	0	-0.011	-0.029	18.419	0.015	0.015	0.000	0.000	0.000	0.000
13	A	21	GLY	0	0.004	0.010	20.564	0.002	0.002	0.000	0.000	0.000	0.000
14	A	22	GLU	-1	-0.881	-0.916	14.048	0.045	0.045	0.000	0.000	0.000	0.000
15	A	23	LYS	1	0.952	0.965	16.622	-0.140	-0.140	0.000	0.000	0.000	0.000
16	A	24	ILE	0	-0.054	-0.019	11.498	0.037	0.037	0.000	0.000	0.000	0.000
17	A	25	GLU	-1	-0.886	-0.957	14.086	0.178	0.178	0.000	0.000	0.000	0.000
18	A	26	GLY	0	0.003	0.006	14.096	0.071	0.071	0.000	0.000	0.000	0.000
19	A	27	LEU	0	-0.051	-0.024	14.405	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	28	PRO	0	0.008	-0.018	16.210	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	29	ARG	1	0.937	0.971	18.056	-0.118	-0.118	0.000	0.000	0.000	0.000
22	A	30	THR	0	-0.066	-0.045	21.246	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	31	VAL	0	-0.063	0.001	24.734	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	32	THR	0	0.057	0.012	25.351	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	33	GLU	-1	-0.896	-0.956	28.035	0.043	0.043	0.000	0.000	0.000	0.000
26	A	34	THR	0	0.032	0.008	25.952	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	35	ASP	-1	-0.826	-0.899	23.580	0.086	0.086	0.000	0.000	0.000	0.000
28	A	36	ILE	0	-0.046	-0.001	26.196	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	37	TRP	0	0.059	0.006	29.255	-0.006	-0.006	0.000	0.000	0.000	0.000
30	A	38	THR	0	-0.029	-0.004	24.182	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	39	PHE	0	-0.005	-0.013	24.323	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.016	0.005	27.087	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	41	TYR	0	-0.033	-0.026	28.958	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	42	LEU	0	-0.045	-0.015	23.381	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	43	THR	0	-0.047	-0.030	27.474	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	44	ALA	0	-0.033	-0.010	29.606	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	45	ASP	-1	-0.923	-0.945	32.289	0.004	0.004	0.000	0.000	0.000	0.000
38	A	46	PHE	0	-0.031	-0.029	33.609	0.004	0.004	0.000	0.000	0.000	0.000
39	A	47	PHE	0	0.020	0.016	35.628	0.001	0.001	0.000	0.000	0.000	0.000
40	A	48	PRO	0	0.063	0.016	37.072	0.003	0.003	0.000	0.000	0.000	0.000
41	A	49	LEU	0	-0.046	-0.018	36.707	0.002	0.002	0.000	0.000	0.000	0.000
42	A	50	HIS	0	-0.082	-0.072	33.408	0.000	0.000	0.000	0.000	0.000	0.000
43	A	51	THR	0	-0.028	-0.017	34.514	0.002	0.002	0.000	0.000	0.000	0.000
44	A	52	ASP	-1	-0.849	-0.893	37.019	0.018	0.018	0.000	0.000	0.000	0.000
45	A	53	VAL	0	0.018	-0.008	39.980	0.001	0.001	0.000	0.000	0.000	0.000
46	A	54	GLU	-1	-0.861	-0.940	41.801	0.025	0.025	0.000	0.000	0.000	0.000
47	A	55	PHE	0	-0.062	-0.028	41.781	0.000	0.000	0.000	0.000	0.000	0.000
48	A	56	ALA	0	0.032	0.010	40.215	0.000	0.000	0.000	0.000	0.000	0.000
49	A	57	LYS	1	0.859	0.950	42.151	-0.027	-0.027	0.000	0.000	0.000	0.000
50	A	58	LYS	1	0.902	0.956	45.109	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	59	THR	0	-0.035	-0.013	42.021	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	60	ILE	0	-0.004	-0.009	41.412	0.001	0.001	0.000	0.000	0.000	0.000
53	A	61	PHE	0	0.031	0.002	37.501	0.002	0.002	0.000	0.000	0.000	0.000
54	A	62	GLY	0	-0.016	0.027	40.943	0.003	0.003	0.000	0.000	0.000	0.000
55	A	63	LYS	1	0.908	0.938	38.388	-0.044	-0.044	0.000	0.000	0.000	0.000
56	A	64	PRO	0	0.046	0.023	36.257	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	65	ILE	0	-0.032	-0.015	33.654	0.004	0.004	0.000	0.000	0.000	0.000
58	A	66	ALA	0	0.046	0.011	28.514	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	67	GLN	0	0.042	0.025	28.731	0.003	0.003	0.000	0.000	0.000	0.000
60	A	68	GLY	0	0.049	0.021	28.127	0.004	0.004	0.000	0.000	0.000	0.000
61	A	69	MET	0	0.024	-0.007	25.334	0.004	0.004	0.000	0.000	0.000	0.000
62	A	70	LEU	0	0.001	0.029	23.493	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	71	VAL	0	0.001	-0.011	23.176	0.007	0.007	0.000	0.000	0.000	0.000
64	A	72	LEU	0	-0.002	0.000	22.068	0.010	0.010	0.000	0.000	0.000	0.000
65	A	73	SER	0	0.009	-0.001	20.084	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	74	ILE	0	-0.025	-0.015	18.482	0.004	0.004	0.000	0.000	0.000	0.000
67	A	75	ALA	0	-0.044	-0.008	17.924	0.022	0.022	0.000	0.000	0.000	0.000
68	A	76	LEU	0	0.027	-0.005	16.712	0.018	0.018	0.000	0.000	0.000	0.000
69	A	77	GLY	0	0.019	0.026	14.342	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	78	MET	0	-0.051	-0.009	13.114	0.026	0.026	0.000	0.000	0.000	0.000
71	A	79	VAL	0	-0.012	-0.005	13.284	0.072	0.072	0.000	0.000	0.000	0.000
72	A	80	ASP	-1	-0.869	-0.947	10.119	-0.091	-0.091	0.000	0.000	0.000	0.000
73	A	81	GLN	0	-0.017	-0.002	8.659	-0.080	-0.080	0.000	0.000	0.000	0.000
74	A	82	VAL	0	-0.008	0.006	7.820	0.251	0.251	0.000	0.000	0.000	0.000
75	A	83	ILE	0	0.004	0.001	6.544	0.361	0.361	0.000	0.000	0.000	0.000
76	A	84	LEU	0	0.032	0.004	4.640	-0.160	-0.012	-0.001	-0.015	-0.132	0.000
77	A	85	SER	0	-0.086	-0.034	2.889	-3.394	-1.531	0.259	-0.819	-1.303	-0.007
78	A	86	ASN	0	-0.059	-0.039	3.230	2.848	3.850	0.270	-0.429	-0.842	-0.003
79	A	87	TYR	0	-0.038	-0.020	3.107	-1.739	-0.835	0.394	-0.497	-0.801	-0.004
80	A	88	ASP	-1	-0.845	-0.896	2.597	-3.396	-2.255	1.871	-1.081	-1.931	-0.010
81	A	89	VAL	0	0.055	-0.008	3.407	0.547	0.532	0.018	0.149	-0.152	0.000
82	A	90	SER	0	-0.010	0.007	6.302	0.255	0.255	0.000	0.000	0.000	0.000
83	A	91	SER	0	-0.093	-0.084	8.476	0.089	0.089	0.000	0.000	0.000	0.000
84	A	92	VAL	0	0.002	0.005	9.063	0.100	0.100	0.000	0.000	0.000	0.000
85	A	93	ILE	0	-0.031	-0.004	11.468	-0.010	-0.010	0.000	0.000	0.000	0.000
86	A	94	ALA	0	0.001	-0.007	14.568	0.008	0.008	0.000	0.000	0.000	0.000
87	A	95	PHE	0	-0.023	0.002	16.669	0.007	0.007	0.000	0.000	0.000	0.000
88	A	96	PHE	0	-0.019	-0.005	17.921	0.005	0.005	0.000	0.000	0.000	0.000
89	A	97	GLY	0	0.042	0.018	21.099	0.005	0.005	0.000	0.000	0.000	0.000
90	A	98	ILE	0	-0.017	-0.020	21.901	0.003	0.003	0.000	0.000	0.000	0.000
91	A	99	LYS	1	0.925	0.974	24.195	0.023	0.023	0.000	0.000	0.000	0.000
92	A	100	ASP	-1	-0.911	-0.965	26.493	0.012	0.012	0.000	0.000	0.000	0.000
93	A	101	VAL	0	0.042	0.035	25.651	0.003	0.003	0.000	0.000	0.000	0.000
94	A	102	ARG	1	0.910	0.960	28.172	-0.020	-0.020	0.000	0.000	0.000	0.000
95	A	103	PHE	0	0.009	-0.010	27.663	0.006	0.006	0.000	0.000	0.000	0.000
96	A	104	LEU	0	-0.042	-0.014	30.308	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	105	ARG	1	0.921	0.965	31.850	-0.058	-0.058	0.000	0.000	0.000	0.000
98	A	106	PRO	0	-0.022	0.002	31.875	0.001	0.001	0.000	0.000	0.000	0.000
99	A	107	VAL	0	0.033	0.025	27.852	0.004	0.004	0.000	0.000	0.000	0.000
100	A	108	PHE	0	-0.024	-0.030	31.062	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	109	ILE	0	0.029	-0.010	30.911	0.006	0.006	0.000	0.000	0.000	0.000
102	A	110	GLY	0	0.026	0.031	30.414	0.003	0.003	0.000	0.000	0.000	0.000
103	A	111	ASP	-1	-0.868	-0.920	29.215	0.084	0.084	0.000	0.000	0.000	0.000
104	A	112	THR	0	-0.010	-0.008	23.907	0.005	0.005	0.000	0.000	0.000	0.000
105	A	113	ILE	0	-0.022	-0.008	22.451	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	114	ALA	0	0.036	0.004	20.600	0.018	0.018	0.000	0.000	0.000	0.000
107	A	115	ALA	0	-0.012	-0.013	18.411	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	116	SER	0	0.000	0.024	17.620	0.026	0.026	0.000	0.000	0.000	0.000
109	A	117	ALA	0	0.016	-0.004	15.795	-0.029	-0.029	0.000	0.000	0.000	0.000
110	A	118	GLU	-1	-0.921	-0.959	17.114	0.093	0.093	0.000	0.000	0.000	0.000
111	A	119	VAL	0	-0.008	0.017	16.423	-0.019	-0.019	0.000	0.000	0.000	0.000
112	A	120	VAL	0	0.004	-0.019	19.145	0.006	0.006	0.000	0.000	0.000	0.000
113	A	121	GLU	-1	-0.940	-0.977	21.904	-0.033	-0.033	0.000	0.000	0.000	0.000
114	A	122	LYS	1	0.809	0.905	18.402	0.087	0.087	0.000	0.000	0.000	0.000
115	A	123	GLN	0	-0.029	-0.003	22.347	0.006	0.006	0.000	0.000	0.000	0.000
116	A	124	ASP	-1	-0.861	-0.923	22.629	-0.118	-0.118	0.000	0.000	0.000	0.000
117	A	125	PHE	0	-0.072	-0.027	22.347	0.010	0.010	0.000	0.000	0.000	0.000
118	A	126	ASP	-1	-0.716	-0.836	22.325	-0.145	-0.145	0.000	0.000	0.000	0.000
119	A	127	GLU	-1	-0.902	-0.954	23.471	-0.132	-0.132	0.000	0.000	0.000	0.000
120	A	128	LYS	1	0.910	0.942	19.595	0.171	0.171	0.000	0.000	0.000	0.000
121	A	129	SER	0	-0.073	-0.086	18.228	-0.030	-0.030	0.000	0.000	0.000	0.000
122	A	130	GLY	0	0.106	0.051	18.504	0.017	0.017	0.000	0.000	0.000	0.000
123	A	131	VAL	0	-0.028	-0.004	18.585	-0.016	-0.016	0.000	0.000	0.000	0.000
124	A	132	VAL	0	0.005	0.001	16.328	0.012	0.012	0.000	0.000	0.000	0.000
125	A	133	THR	0	-0.006	-0.016	19.048	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	134	TYR	0	-0.001	-0.008	13.854	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	135	LYS	1	0.880	0.937	19.896	-0.053	-0.053	0.000	0.000	0.000	0.000
128	A	136	LEU	0	-0.028	-0.022	18.913	0.013	0.013	0.000	0.000	0.000	0.000
129	A	137	GLU	-1	-0.901	-0.959	21.291	0.070	0.070	0.000	0.000	0.000	0.000
130	A	138	VAL	0	0.022	0.016	21.888	0.016	0.016	0.000	0.000	0.000	0.000
131	A	139	LYS	1	0.946	0.965	23.838	-0.123	-0.123	0.000	0.000	0.000	0.000
132	A	140	ASN	0	-0.005	0.004	25.113	0.013	0.013	0.000	0.000	0.000	0.000
133	A	141	GLN	0	0.089	0.025	27.445	0.009	0.009	0.000	0.000	0.000	0.000
134	A	142	ARG	1	0.835	0.926	28.403	-0.073	-0.073	0.000	0.000	0.000	0.000
135	A	143	GLY	0	0.013	0.010	28.368	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	144	GLU	-1	-0.899	-0.941	29.425	0.064	0.064	0.000	0.000	0.000	0.000
137	A	145	LEU	0	0.008	0.001	26.599	0.006	0.006	0.000	0.000	0.000	0.000
138	A	146	VAL	0	-0.016	-0.018	26.962	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	147	LEU	0	0.001	0.009	24.265	-0.008	-0.008	0.000	0.000	0.000	0.000
140	A	148	THR	0	-0.006	-0.005	25.725	0.010	0.010	0.000	0.000	0.000	0.000
141	A	149	ALA	0	0.027	0.002	23.611	-0.006	-0.006	0.000	0.000	0.000	0.000
142	A	150	LEU	0	-0.015	0.015	23.649	0.006	0.006	0.000	0.000	0.000	0.000
143	A	151	TYR	0	0.015	0.007	15.486	0.004	0.004	0.000	0.000	0.000	0.000
144	A	152	SER	0	0.021	0.015	19.692	0.002	0.002	0.000	0.000	0.000	0.000
145	A	153	ALA	0	0.015	0.010	15.261	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	154	LEU	0	0.001	0.014	17.143	0.006	0.006	0.000	0.000	0.000	0.000
147	A	155	ILE	0	-0.009	0.002	13.193	-0.030	-0.030	0.000	0.000	0.000	0.000
148	A	156	ARG	1	0.942	0.958	12.489	0.392	0.392	0.000	0.000	0.000	0.000
149	A	157	LYS	1	0.757	0.913	14.662	0.124	0.124	0.000	0.000	0.000	0.000
150	A	158	THR	0	-0.027	-0.019	15.305	-0.040	-0.040	0.000	0.000	0.000	0.000
151	A	159	PRO	0	-0.039	-0.003	15.066	0.032	0.032	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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