FMO DATABASE

FMODB ID: 3Q17L

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1438565.550142
FMO2-HF: Nuclear repulsion	1379432.405727
FMO2-HF: Total energy	-59133.144415
FMO2-MP2: Total energy	-59307.113292

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.
-5.98	-3.481	0.018	-0.863	-1.654	-0.001

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 : 0.024 / q_NPA : -0.002

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	-0.898	-0.962	3.897	0.446	1.603	-0.010	-0.506	-0.640	0.001
4	A	57	ILE	0	-0.029	-0.016	6.747	-0.102	-0.102	0.000	0.000	0.000	0.000
5	A	58	LYS	1	0.946	0.979	9.360	-0.995	-0.995	0.000	0.000	0.000	0.000
6	A	59	ILE	0	0.022	0.020	12.981	-0.021	-0.021	0.000	0.000	0.000	0.000
7	A	60	LYS	1	0.913	0.957	16.280	-0.444	-0.444	0.000	0.000	0.000	0.000
8	A	61	GLY	0	0.020	0.011	19.187	-0.021	-0.021	0.000	0.000	0.000	0.000
9	A	62	ASP	-1	-0.950	-0.984	21.974	0.215	0.215	0.000	0.000	0.000	0.000
10	A	63	THR	0	0.036	0.018	18.149	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	64	ILE	0	0.001	0.015	13.354	0.025	0.025	0.000	0.000	0.000	0.000
12	A	65	VAL	0	-0.041	-0.034	13.569	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	66	SER	0	0.055	0.022	9.141	0.103	0.103	0.000	0.000	0.000	0.000
14	A	67	ASP	-1	-0.923	-0.965	8.259	1.242	1.242	0.000	0.000	0.000	0.000
15	A	68	LYS	1	0.902	0.943	6.578	-1.105	-1.105	0.000	0.000	0.000	0.000
16	A	69	PHE	0	-0.020	-0.010	10.324	-0.122	-0.122	0.000	0.000	0.000	0.000
17	A	70	GLU	-1	-0.880	-0.939	13.741	0.441	0.441	0.000	0.000	0.000	0.000
18	A	71	ALA	0	0.024	0.020	16.470	-0.041	-0.041	0.000	0.000	0.000	0.000
19	A	72	LYS	1	0.990	1.017	18.240	-0.168	-0.168	0.000	0.000	0.000	0.000
20	A	73	ILE	0	-0.033	-0.026	18.801	-0.015	-0.015	0.000	0.000	0.000	0.000
21	A	74	LYS	1	0.905	0.960	22.208	-0.141	-0.141	0.000	0.000	0.000	0.000
22	A	75	GLU	-1	-0.916	-0.976	25.179	0.141	0.141	0.000	0.000	0.000	0.000
23	A	76	PRO	0	-0.020	0.008	25.129	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	77	PHE	0	-0.047	-0.032	27.283	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	78	ILE	0	-0.003	0.014	29.455	0.000	0.000	0.000	0.000	0.000	0.000
26	A	79	ILE	0	0.020	0.026	30.142	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	80	ASN	0	-0.093	-0.074	33.152	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	81	GLU	-1	-0.792	-0.909	34.694	0.029	0.029	0.000	0.000	0.000	0.000
29	A	82	LYS	1	0.957	0.966	36.667	-0.032	-0.032	0.000	0.000	0.000	0.000
30	A	83	ASP	-1	-0.860	-0.929	39.989	0.022	0.022	0.000	0.000	0.000	0.000
31	A	84	GLU	-1	-0.952	-0.975	35.190	0.020	0.020	0.000	0.000	0.000	0.000
32	A	85	LYS	1	0.807	0.904	37.818	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	86	LYS	1	0.988	1.000	32.352	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	87	LYS	1	0.921	0.965	32.754	-0.042	-0.042	0.000	0.000	0.000	0.000
35	A	88	TYR	0	0.030	0.028	28.182	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	89	ILE	0	-0.004	-0.002	24.864	0.001	0.001	0.000	0.000	0.000	0.000
37	A	90	ALA	0	-0.001	-0.005	25.966	0.001	0.001	0.000	0.000	0.000	0.000
38	A	91	PHE	0	0.019	-0.013	22.159	0.005	0.005	0.000	0.000	0.000	0.000
39	A	92	LYS	1	0.928	0.986	23.383	-0.091	-0.091	0.000	0.000	0.000	0.000
40	A	93	MET	0	-0.003	-0.012	18.295	0.020	0.020	0.000	0.000	0.000	0.000
41	A	94	GLU	-1	-0.963	-0.973	22.459	0.140	0.140	0.000	0.000	0.000	0.000
42	A	95	ILE	0	0.037	0.024	17.165	0.021	0.021	0.000	0.000	0.000	0.000
43	A	96	THR	0	-0.017	-0.019	18.919	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	97	ALA	0	-0.013	0.010	16.553	0.046	0.046	0.000	0.000	0.000	0.000
45	A	98	LYS	1	0.950	0.984	14.166	-0.509	-0.509	0.000	0.000	0.000	0.000
46	A	99	LYS	1	0.865	0.920	10.098	-0.296	-0.296	0.000	0.000	0.000	0.000
47	A	100	ASP	-1	-0.961	-0.989	14.550	0.038	0.038	0.000	0.000	0.000	0.000
48	A	101	ASP	-1	-0.865	-0.944	11.161	0.241	0.241	0.000	0.000	0.000	0.000
49	A	102	LYS	1	0.969	0.988	14.703	0.117	0.117	0.000	0.000	0.000	0.000
50	A	103	ASP	-1	-0.849	-0.921	12.334	0.064	0.064	0.000	0.000	0.000	0.000
51	A	104	LEU	0	-0.089	-0.032	12.332	0.055	0.055	0.000	0.000	0.000	0.000
52	A	105	ASN	0	-0.027	-0.009	15.273	-0.036	-0.036	0.000	0.000	0.000	0.000
53	A	106	PRO	0	0.002	-0.013	16.418	0.029	0.029	0.000	0.000	0.000	0.000
54	A	107	SER	0	0.030	-0.029	17.264	0.020	0.020	0.000	0.000	0.000	0.000
55	A	108	SER	0	0.009	0.018	14.451	0.010	0.010	0.000	0.000	0.000	0.000
56	A	109	ILE	0	0.011	0.024	12.542	0.046	0.046	0.000	0.000	0.000	0.000
57	A	110	SER	0	-0.098	-0.060	12.603	0.022	0.022	0.000	0.000	0.000	0.000
58	A	111	HIS	0	-0.013	-0.003	14.192	0.007	0.007	0.000	0.000	0.000	0.000
59	A	112	ASP	-1	-0.866	-0.939	9.169	0.308	0.308	0.000	0.000	0.000	0.000
60	A	113	TYR	0	-0.095	-0.052	6.046	0.313	0.313	0.000	0.000	0.000	0.000
61	A	114	ILE	0	-0.021	-0.012	10.253	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	115	ASN	0	0.034	0.036	12.834	-0.028	-0.028	0.000	0.000	0.000	0.000
63	A	116	ILE	0	-0.013	0.002	15.696	0.017	0.017	0.000	0.000	0.000	0.000
64	A	117	THR	0	-0.031	-0.023	18.961	-0.016	-0.016	0.000	0.000	0.000	0.000
65	A	118	GLN	0	-0.022	-0.025	21.527	0.006	0.006	0.000	0.000	0.000	0.000
66	A	119	ASP	-1	-0.870	-0.918	25.195	0.094	0.094	0.000	0.000	0.000	0.000
67	A	120	ASP	-1	-0.850	-0.920	27.217	0.040	0.040	0.000	0.000	0.000	0.000
68	A	121	LYS	1	0.907	0.936	30.135	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	122	ASN	0	-0.027	-0.019	31.480	0.002	0.002	0.000	0.000	0.000	0.000
70	A	123	THR	0	-0.028	-0.017	27.017	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	124	VAL	0	0.040	0.014	22.303	0.004	0.004	0.000	0.000	0.000	0.000
72	A	125	ASN	0	-0.063	-0.007	23.479	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	126	LYS	1	1.031	1.020	17.942	0.025	0.025	0.000	0.000	0.000	0.000
74	A	127	LEU	0	-0.032	-0.032	21.337	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	128	ARG	1	0.898	0.955	21.345	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	129	ASP	-1	-0.836	-0.894	19.990	0.077	0.077	0.000	0.000	0.000	0.000
77	A	130	GLY	0	-0.040	-0.052	23.011	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	131	TYR	0	-0.028	-0.021	23.377	0.003	0.003	0.000	0.000	0.000	0.000
79	A	132	LEU	0	0.003	0.002	28.536	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	133	LEU	0	0.009	0.018	31.710	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	134	SER	0	-0.037	-0.017	34.967	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	135	ASP	-1	-0.848	-0.938	31.535	0.042	0.042	0.000	0.000	0.000	0.000
83	A	136	LYS	1	0.977	0.977	33.997	-0.026	-0.026	0.000	0.000	0.000	0.000
84	A	137	LYS	1	0.842	0.932	35.104	-0.047	-0.047	0.000	0.000	0.000	0.000
85	A	138	TYR	0	0.063	0.007	30.468	0.002	0.002	0.000	0.000	0.000	0.000
86	A	139	LYS	1	1.003	1.032	30.741	-0.034	-0.034	0.000	0.000	0.000	0.000
87	A	140	ASP	-1	-0.921	-0.975	30.812	0.076	0.076	0.000	0.000	0.000	0.000
88	A	141	TRP	0	-0.033	-0.031	26.008	0.007	0.007	0.000	0.000	0.000	0.000
89	A	142	THR	0	0.012	0.001	26.176	0.008	0.008	0.000	0.000	0.000	0.000
90	A	143	GLU	-1	-0.940	-0.959	26.449	0.060	0.060	0.000	0.000	0.000	0.000
91	A	144	HIS	1	0.866	0.922	24.553	-0.078	-0.078	0.000	0.000	0.000	0.000
92	A	145	ASN	0	0.018	0.004	22.284	0.015	0.015	0.000	0.000	0.000	0.000
93	A	146	GLN	0	0.061	0.063	21.064	0.023	0.023	0.000	0.000	0.000	0.000
94	A	147	ASP	-1	-0.887	-0.927	21.842	0.047	0.047	0.000	0.000	0.000	0.000
95	A	148	GLN	0	-0.017	-0.019	18.210	0.018	0.018	0.000	0.000	0.000	0.000
96	A	149	ILE	0	0.000	-0.003	19.207	-0.014	-0.014	0.000	0.000	0.000	0.000
97	A	150	LYS	1	0.943	0.962	19.126	-0.045	-0.045	0.000	0.000	0.000	0.000
98	A	151	LYS	1	0.996	1.004	16.688	-0.119	-0.119	0.000	0.000	0.000	0.000
99	A	152	GLY	0	-0.021	-0.009	19.067	0.022	0.022	0.000	0.000	0.000	0.000
100	A	153	LYS	1	0.886	0.949	21.536	-0.109	-0.109	0.000	0.000	0.000	0.000
101	A	154	THR	0	0.094	0.036	21.513	0.022	0.022	0.000	0.000	0.000	0.000
102	A	155	ALA	0	-0.047	-0.013	22.633	-0.020	-0.020	0.000	0.000	0.000	0.000
103	A	156	GLN	0	-0.028	-0.011	23.157	0.020	0.020	0.000	0.000	0.000	0.000
104	A	157	ALA	0	0.003	0.020	21.358	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	158	MET	0	-0.031	-0.027	23.393	0.002	0.002	0.000	0.000	0.000	0.000
106	A	159	PHE	0	0.008	0.014	18.477	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	160	ILE	0	0.067	0.052	22.543	0.003	0.003	0.000	0.000	0.000	0.000
108	A	161	TYR	0	0.039	0.022	18.182	0.004	0.004	0.000	0.000	0.000	0.000
109	A	162	GLU	-1	-0.930	-0.965	24.533	0.025	0.025	0.000	0.000	0.000	0.000
110	A	163	LEU	0	-0.042	-0.035	26.845	0.001	0.001	0.000	0.000	0.000	0.000
111	A	164	ARG	1	0.849	0.927	25.212	-0.039	-0.039	0.000	0.000	0.000	0.000
112	A	165	GLY	0	0.040	0.030	29.788	0.001	0.001	0.000	0.000	0.000	0.000
113	A	166	ASP	-1	-0.954	-0.988	31.998	0.055	0.055	0.000	0.000	0.000	0.000
114	A	167	GLY	0	0.023	0.036	30.101	0.002	0.002	0.000	0.000	0.000	0.000
115	A	168	ASN	0	-0.027	-0.042	27.585	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	169	ILE	0	0.028	0.022	23.080	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	170	ASN	0	-0.043	-0.029	20.564	0.017	0.017	0.000	0.000	0.000	0.000
118	A	171	LEU	0	-0.015	0.000	16.128	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	172	ASN	0	0.000	-0.015	14.645	0.029	0.029	0.000	0.000	0.000	0.000
120	A	173	VAL	0	0.070	0.020	10.690	0.005	0.005	0.000	0.000	0.000	0.000
121	A	174	HIS	0	-0.035	0.001	7.840	0.036	0.036	0.000	0.000	0.000	0.000
122	A	175	LYS	1	0.938	0.964	3.169	-2.639	-2.184	0.018	-0.111	-0.362	-0.001
123	A	176	TYR	0	0.010	0.005	3.687	-0.316	0.074	0.010	-0.116	-0.285	0.000
124	A	177	SER	0	-0.016	0.013	3.888	-0.166	-0.057	-0.001	-0.015	-0.093	0.000
125	A	178	GLU	-1	-0.938	-0.976	3.884	-2.782	-2.394	0.001	-0.115	-0.274	-0.001
126	A	179	ASP	-1	-0.867	-0.939	7.031	0.002	0.002	0.000	0.000	0.000	0.000
127	A	180	LYS	1	0.892	0.944	9.481	-0.185	-0.185	0.000	0.000	0.000	0.000
128	A	181	THR	0	-0.039	-0.023	9.815	0.012	0.012	0.000	0.000	0.000	0.000
129	A	182	VAL	0	-0.097	-0.048	7.857	0.016	0.016	0.000	0.000	0.000	0.000
130	A	183	ASP	-1	-0.852	-0.942	11.292	0.481	0.481	0.000	0.000	0.000	0.000
131	A	184	SER	0	-0.037	-0.030	14.364	-0.036	-0.036	0.000	0.000	0.000	0.000
132	A	185	LYS	1	0.947	0.987	17.265	-0.195	-0.195	0.000	0.000	0.000	0.000
133	A	186	SER	0	0.024	0.016	20.570	-0.010	-0.010	0.000	0.000	0.000	0.000
134	A	187	PHE	0	-0.037	-0.019	22.103	0.003	0.003	0.000	0.000	0.000	0.000
135	A	188	LYS	1	0.925	0.955	26.695	-0.113	-0.113	0.000	0.000	0.000	0.000
136	A	189	PHE	0	0.115	0.061	29.882	0.000	0.000	0.000	0.000	0.000	0.000
137	A	190	SER	0	-0.018	-0.021	31.310	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	191	LYS	1	0.877	0.930	33.225	-0.089	-0.089	0.000	0.000	0.000	0.000
139	A	192	LEU	0	0.038	0.052	28.763	0.002	0.002	0.000	0.000	0.000	0.000
140	A	193	LYS	1	0.941	0.967	32.800	-0.086	-0.086	0.000	0.000	0.000	0.000
141	A	194	THR	0	0.012	0.001	33.554	0.002	0.002	0.000	0.000	0.000	0.000
142	A	195	GLU	-1	-0.946	-0.980	33.989	0.068	0.068	0.000	0.000	0.000	0.000
143	A	196	ASP	-1	-0.880	-0.924	36.151	0.043	0.043	0.000	0.000	0.000	0.000
144	A	197	PHE	0	-0.045	-0.038	35.681	0.004	0.004	0.000	0.000	0.000	0.000
145	A	198	SER	0	-0.039	0.005	38.887	-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:54:ASN)