FMO DATABASE

FMODB ID: 9G1M2

Calculation Name: 3QFG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3QFG

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G019

Base Structure: X-ray

Registration Date: 2023-06-20

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	145
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1446239.713975
FMO2-HF: Nuclear repulsion	1387103.646146
FMO2-HF: Total energy	-59136.067829
FMO2-MP2: Total energy	-59310.155018

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:54:ASN)

Summations of interaction energy for fragment #1(A:54:ASN)

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.
-10.649	-4.477	0.513	-2.95	-3.736	-0.011

Interaction energy analysis for fragmet #1(A:54:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.041 / q_NPA : 0.008

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	56	ASP	-1	-0.830	-0.889	3.899	-0.479	0.640	-0.005	-0.507	-0.607	0.002
4	A	57	ILE	0	-0.032	-0.024	6.555	-0.055	-0.055	0.000	0.000	0.000	0.000
5	A	58	LYS	1	0.870	0.936	9.247	-0.565	-0.565	0.000	0.000	0.000	0.000
6	A	59	ILE	0	0.019	0.008	12.787	-0.027	-0.027	0.000	0.000	0.000	0.000
7	A	60	LYS	1	0.952	0.985	16.149	-0.150	-0.150	0.000	0.000	0.000	0.000
8	A	61	GLY	0	0.007	0.010	19.107	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	62	ASP	-1	-0.825	-0.895	21.825	0.071	0.071	0.000	0.000	0.000	0.000
10	A	63	THR	0	-0.015	-0.027	18.355	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	64	ILE	0	0.029	0.024	12.890	0.016	0.016	0.000	0.000	0.000	0.000
12	A	65	VAL	0	-0.047	-0.035	13.759	-0.017	-0.017	0.000	0.000	0.000	0.000
13	A	66	SER	0	0.046	0.028	9.172	0.044	0.044	0.000	0.000	0.000	0.000
14	A	67	ASP	-1	-0.863	-0.937	7.497	0.038	0.038	0.000	0.000	0.000	0.000
15	A	68	LYS	1	0.836	0.890	7.617	-0.367	-0.367	0.000	0.000	0.000	0.000
16	A	69	PHE	0	-0.006	-0.003	10.167	-0.057	-0.057	0.000	0.000	0.000	0.000
17	A	70	GLU	-1	-0.844	-0.907	13.740	0.113	0.113	0.000	0.000	0.000	0.000
18	A	71	ALA	0	0.009	0.000	16.318	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	72	LYS	1	0.835	0.931	17.959	-0.053	-0.053	0.000	0.000	0.000	0.000
20	A	73	ILE	0	0.008	-0.005	18.293	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	74	LYS	1	0.762	0.863	22.132	-0.035	-0.035	0.000	0.000	0.000	0.000
22	A	75	GLU	-1	-0.816	-0.915	25.284	0.063	0.063	0.000	0.000	0.000	0.000
23	A	76	PRO	0	-0.020	0.005	24.682	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	77	PHE	0	-0.051	-0.037	26.941	0.000	0.000	0.000	0.000	0.000	0.000
25	A	78	ILE	0	0.027	0.009	29.059	0.000	0.000	0.000	0.000	0.000	0.000
26	A	79	ILE	0	0.025	0.019	29.466	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	80	ASN	0	-0.045	-0.043	32.480	0.001	0.001	0.000	0.000	0.000	0.000
28	A	81	GLU	-1	-0.810	-0.915	34.311	0.001	0.001	0.000	0.000	0.000	0.000
29	A	82	LYS	1	0.887	0.936	36.270	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	83	ASP	-1	-0.814	-0.884	39.542	0.001	0.001	0.000	0.000	0.000	0.000
31	A	84	GLU	-1	-0.810	-0.881	33.954	0.001	0.001	0.000	0.000	0.000	0.000
32	A	85	LYS	1	0.730	0.853	38.014	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	86	LYS	1	0.876	0.954	31.269	0.000	0.000	0.000	0.000	0.000	0.000
34	A	87	LYS	1	0.887	0.930	32.425	-0.015	-0.015	0.000	0.000	0.000	0.000
35	A	88	TYR	0	0.021	-0.008	27.670	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	89	ILE	0	-0.035	-0.001	24.170	0.001	0.001	0.000	0.000	0.000	0.000
37	A	90	ALA	0	0.020	0.000	25.378	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	91	PHE	0	0.032	-0.003	21.772	0.002	0.002	0.000	0.000	0.000	0.000
39	A	92	LYS	1	0.875	0.962	23.169	-0.021	-0.021	0.000	0.000	0.000	0.000
40	A	93	MET	0	-0.015	-0.004	18.166	0.009	0.009	0.000	0.000	0.000	0.000
41	A	94	GLU	-1	-0.789	-0.870	22.184	0.026	0.026	0.000	0.000	0.000	0.000
42	A	95	ILE	0	0.010	0.013	16.969	0.009	0.009	0.000	0.000	0.000	0.000
43	A	96	THR	0	0.014	0.005	18.700	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	97	ALA	0	0.000	0.020	16.435	0.017	0.017	0.000	0.000	0.000	0.000
45	A	98	LYS	1	0.814	0.894	13.856	-0.075	-0.075	0.000	0.000	0.000	0.000
46	A	99	LYS	1	0.860	0.925	10.497	0.308	0.308	0.000	0.000	0.000	0.000
47	A	100	ASP	-1	-0.902	-0.951	14.812	-0.113	-0.113	0.000	0.000	0.000	0.000
48	A	101	ASP	-1	-0.800	-0.901	11.196	-0.149	-0.149	0.000	0.000	0.000	0.000
49	A	102	LYS	1	0.984	0.984	14.627	0.226	0.226	0.000	0.000	0.000	0.000
50	A	103	ASP	-1	-0.850	-0.905	11.784	-0.044	-0.044	0.000	0.000	0.000	0.000
51	A	104	LEU	0	-0.080	-0.035	11.814	0.055	0.055	0.000	0.000	0.000	0.000
52	A	105	ASN	0	0.003	0.016	15.275	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	106	PRO	0	-0.022	-0.015	16.440	0.021	0.021	0.000	0.000	0.000	0.000
54	A	107	SER	0	0.023	-0.002	16.941	0.016	0.016	0.000	0.000	0.000	0.000
55	A	108	SER	0	0.036	0.015	13.593	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	109	ILE	0	-0.037	-0.005	12.346	0.039	0.039	0.000	0.000	0.000	0.000
57	A	110	SER	0	-0.078	-0.060	12.458	0.022	0.022	0.000	0.000	0.000	0.000
58	A	111	HIS	0	-0.006	-0.006	12.319	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	112	ASP	-1	-0.804	-0.903	8.570	0.304	0.304	0.000	0.000	0.000	0.000
60	A	113	TYR	0	-0.132	-0.086	6.155	0.131	0.131	0.000	0.000	0.000	0.000
61	A	114	ILE	0	-0.024	-0.006	9.629	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	115	ASN	0	0.054	0.022	12.427	-0.018	-0.018	0.000	0.000	0.000	0.000
63	A	116	ILE	0	-0.023	0.011	15.106	0.010	0.010	0.000	0.000	0.000	0.000
64	A	117	THR	0	0.009	-0.005	18.586	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	118	GLN	0	-0.030	-0.022	21.136	0.001	0.001	0.000	0.000	0.000	0.000
66	A	119	ASP	-1	-0.833	-0.909	24.834	0.060	0.060	0.000	0.000	0.000	0.000
67	A	120	ASP	-1	-0.809	-0.900	26.946	0.026	0.026	0.000	0.000	0.000	0.000
68	A	121	LYS	1	0.777	0.859	29.816	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	122	ASN	0	-0.023	-0.005	31.020	0.003	0.003	0.000	0.000	0.000	0.000
70	A	123	THR	0	-0.019	-0.012	26.524	0.001	0.001	0.000	0.000	0.000	0.000
71	A	124	VAL	0	0.006	0.007	21.682	0.002	0.002	0.000	0.000	0.000	0.000
72	A	125	ASN	0	-0.052	-0.034	22.808	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	126	LYS	1	0.960	0.975	15.544	0.019	0.019	0.000	0.000	0.000	0.000
74	A	127	LEU	0	-0.054	-0.023	21.100	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	128	ARG	1	0.855	0.902	20.886	0.001	0.001	0.000	0.000	0.000	0.000
76	A	129	ASP	-1	-0.841	-0.925	19.380	0.010	0.010	0.000	0.000	0.000	0.000
77	A	130	GLY	0	-0.047	-0.031	22.399	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	131	TYR	0	-0.025	-0.012	22.658	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	132	LEU	0	-0.002	0.000	28.291	0.001	0.001	0.000	0.000	0.000	0.000
80	A	133	LEU	0	0.022	0.011	31.701	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	134	SER	0	-0.037	-0.017	34.543	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	135	ASP	-1	-0.787	-0.881	30.922	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	136	LYS	1	0.968	0.981	33.174	0.009	0.009	0.000	0.000	0.000	0.000
84	A	137	LYS	1	0.797	0.905	35.182	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	138	TYR	0	0.001	-0.045	30.479	0.002	0.002	0.000	0.000	0.000	0.000
86	A	139	LYS	1	0.947	0.977	30.704	0.016	0.016	0.000	0.000	0.000	0.000
87	A	140	ASP	-1	-0.866	-0.934	30.585	0.001	0.001	0.000	0.000	0.000	0.000
88	A	141	TRP	0	-0.066	-0.029	25.870	0.003	0.003	0.000	0.000	0.000	0.000
89	A	142	THR	0	-0.018	-0.039	26.245	0.003	0.003	0.000	0.000	0.000	0.000
90	A	143	GLU	-1	-0.866	-0.913	26.570	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	144	HIS	1	0.819	0.880	24.840	0.017	0.017	0.000	0.000	0.000	0.000
92	A	145	ASN	0	0.035	0.002	22.190	0.002	0.002	0.000	0.000	0.000	0.000
93	A	146	GLN	0	0.026	0.034	20.799	0.012	0.012	0.000	0.000	0.000	0.000
94	A	147	ASP	-1	-0.846	-0.896	21.748	-0.041	-0.041	0.000	0.000	0.000	0.000
95	A	148	GLN	0	-0.076	-0.047	17.781	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	149	ILE	0	-0.015	-0.001	18.788	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	150	LYS	1	0.970	0.976	19.018	0.062	0.062	0.000	0.000	0.000	0.000
98	A	151	LYS	1	0.971	0.977	16.965	0.205	0.205	0.000	0.000	0.000	0.000
99	A	152	GLY	0	0.017	0.026	18.978	0.003	0.003	0.000	0.000	0.000	0.000
100	A	153	LYS	1	0.835	0.907	21.489	0.047	0.047	0.000	0.000	0.000	0.000
101	A	154	THR	0	0.044	0.002	21.553	0.001	0.001	0.000	0.000	0.000	0.000
102	A	155	ALA	0	-0.019	-0.006	22.692	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	156	GLN	0	-0.050	-0.022	23.185	0.010	0.010	0.000	0.000	0.000	0.000
104	A	157	ALA	0	-0.001	0.008	21.609	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	158	MET	0	-0.018	-0.008	23.686	0.005	0.005	0.000	0.000	0.000	0.000
106	A	159	PHE	0	0.017	0.025	17.673	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	160	ILE	0	0.012	0.003	21.978	0.002	0.002	0.000	0.000	0.000	0.000
108	A	161	TYR	0	0.063	0.029	17.841	0.001	0.001	0.000	0.000	0.000	0.000
109	A	162	GLU	-1	-0.847	-0.901	24.074	0.004	0.004	0.000	0.000	0.000	0.000
110	A	163	LEU	0	-0.041	-0.022	26.356	0.002	0.002	0.000	0.000	0.000	0.000
111	A	164	ARG	1	0.874	0.945	24.771	-0.020	-0.020	0.000	0.000	0.000	0.000
112	A	165	GLY	0	0.049	0.019	29.392	0.001	0.001	0.000	0.000	0.000	0.000
113	A	166	ASP	-1	-0.875	-0.919	31.067	0.029	0.029	0.000	0.000	0.000	0.000
114	A	167	GLY	0	0.043	0.036	29.888	0.002	0.002	0.000	0.000	0.000	0.000
115	A	168	ASN	0	-0.101	-0.076	26.940	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	169	ILE	0	0.032	0.028	22.950	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	170	ASN	0	-0.032	-0.012	20.231	0.011	0.011	0.000	0.000	0.000	0.000
118	A	171	LEU	0	-0.007	0.015	15.987	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	172	ASN	0	-0.021	-0.014	14.615	0.024	0.024	0.000	0.000	0.000	0.000
120	A	173	VAL	0	0.035	0.011	10.428	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	174	HIS	0	-0.020	0.013	7.581	0.056	0.056	0.000	0.000	0.000	0.000
122	A	175	LYS	1	0.822	0.888	2.586	-1.314	-0.035	0.296	-0.485	-1.089	0.000
123	A	176	TYR	0	-0.027	-0.007	3.330	-0.604	0.169	0.066	-0.316	-0.525	0.002
124	A	177	SER	0	0.016	0.014	3.806	-0.096	0.021	-0.001	-0.019	-0.097	0.000
125	A	178	GLU	-1	-0.918	-0.971	3.069	-8.040	-5.156	0.157	-1.623	-1.418	-0.015
126	A	179	ASP	-1	-0.908	-0.956	6.607	-0.042	-0.042	0.000	0.000	0.000	0.000
127	A	180	LYS	1	0.930	0.966	9.172	-0.247	-0.247	0.000	0.000	0.000	0.000
128	A	181	THR	0	-0.025	-0.021	9.403	-0.031	-0.031	0.000	0.000	0.000	0.000
129	A	182	VAL	0	-0.065	-0.022	7.401	0.042	0.042	0.000	0.000	0.000	0.000
130	A	183	ASP	-1	-0.817	-0.912	10.792	0.273	0.273	0.000	0.000	0.000	0.000
131	A	184	SER	0	-0.032	-0.041	13.772	-0.032	-0.032	0.000	0.000	0.000	0.000
132	A	185	LYS	1	0.843	0.940	16.781	-0.068	-0.068	0.000	0.000	0.000	0.000
133	A	186	SER	0	0.013	0.000	20.217	-0.006	-0.006	0.000	0.000	0.000	0.000
134	A	187	PHE	0	-0.044	-0.032	21.241	0.000	0.000	0.000	0.000	0.000	0.000
135	A	188	LYS	1	0.952	0.973	26.096	-0.066	-0.066	0.000	0.000	0.000	0.000
136	A	189	PHE	0	0.095	0.036	29.496	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	190	SER	0	-0.001	0.000	30.739	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	191	LYS	1	0.909	0.951	32.953	-0.043	-0.043	0.000	0.000	0.000	0.000
139	A	192	LEU	0	0.000	0.029	28.040	0.000	0.000	0.000	0.000	0.000	0.000
140	A	193	LYS	1	0.951	0.974	32.158	-0.031	-0.031	0.000	0.000	0.000	0.000
141	A	194	THR	0	0.034	0.010	33.009	0.001	0.001	0.000	0.000	0.000	0.000
142	A	195	GLU	-1	-0.843	-0.908	33.554	0.014	0.014	0.000	0.000	0.000	0.000
143	A	196	ASP	-1	-0.785	-0.865	35.714	0.010	0.010	0.000	0.000	0.000	0.000
144	A	197	PHE	0	-0.066	-0.027	34.970	0.000	0.000	0.000	0.000	0.000	0.000
145	A	198	SER	0	-0.026	-0.016	38.092	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:54:ASN)