FMO DATABASE

FMODB ID: QV61Y

Calculation Name: 3F7E-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F7E

Chain ID: A

ChEMBL ID:

UniProt ID: A0QXP8

Base Structure: X-ray

Registration Date: 2023-09-23

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1116310.42054
FMO2-HF: Nuclear repulsion	1066200.6057
FMO2-HF: Total energy	-50109.81484
FMO2-MP2: Total energy	-50258.644109

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:2:VAL)

Summations of interaction energy for fragment #1(A:2:VAL)

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.
-6.948	-1.157	5.955	-2.963	-8.784	-0.027

Interaction energy analysis for fragmet #1(A:2:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.050 / q_NPA : -0.029

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

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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	4	VAL	0	0.035	0.023	2.866	-3.365	-0.699	0.301	-1.445	-1.522	-0.008
4	A	5	PRO	0	-0.048	-0.025	4.753	0.460	0.556	-0.001	-0.005	-0.090	0.000
5	A	6	GLU	-1	-0.875	-0.938	7.253	-0.071	-0.071	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.039	0.024	10.383	0.033	0.033	0.000	0.000	0.000	0.000
7	A	8	TYR	0	-0.022	-0.029	9.879	0.060	0.060	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.781	-0.879	9.356	-0.721	-0.721	0.000	0.000	0.000	0.000
9	A	10	SER	0	0.059	0.030	10.852	0.007	0.007	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.110	-0.057	12.779	0.046	0.046	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.057	-0.036	8.048	0.011	0.011	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.875	-0.937	12.718	-0.246	-0.246	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.863	0.916	15.391	0.269	0.269	0.000	0.000	0.000	0.000
14	A	15	PRO	0	0.028	0.040	17.515	-0.032	-0.032	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.026	-0.010	16.684	0.019	0.019	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.000	0.005	17.963	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.017	0.006	15.461	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	19	HIS	0	-0.036	-0.036	16.256	0.027	0.027	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.009	0.005	13.583	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.011	-0.016	14.426	0.050	0.050	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.012	-0.008	14.443	-0.025	-0.025	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.033	0.005	16.311	0.014	0.014	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.817	0.928	18.755	0.136	0.136	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.021	-0.007	22.234	0.001	0.001	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.818	-0.873	24.226	-0.120	-0.120	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.026	0.017	22.310	0.007	0.007	0.000	0.000	0.000	0.000
27	A	28	THR	0	-0.063	-0.052	22.040	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	29	PRO	0	0.022	0.005	19.210	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.026	-0.025	19.674	0.028	0.028	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.029	0.019	17.648	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	32	ASN	0	-0.058	-0.042	19.198	0.027	0.027	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.076	0.047	19.272	-0.023	-0.023	0.000	0.000	0.000	0.000
33	A	34	MET	0	-0.066	-0.016	17.558	0.031	0.031	0.000	0.000	0.000	0.000
34	A	35	TRP	0	0.047	0.045	18.922	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	36	PHE	0	-0.010	-0.016	13.010	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.025	0.008	15.210	0.030	0.030	0.000	0.000	0.000	0.000
37	A	38	TRP	0	-0.033	-0.046	5.579	-0.077	-0.077	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.779	-0.870	10.568	-0.315	-0.315	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.052	0.046	9.615	0.115	0.115	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.902	-0.929	6.148	0.199	0.199	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.071	-0.056	6.116	-0.577	-0.577	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.002	0.004	8.593	0.127	0.127	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.814	0.892	10.741	0.339	0.339	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.062	0.014	12.302	0.022	0.022	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.023	0.035	17.211	0.022	0.022	0.000	0.000	0.000	0.000
46	A	47	HIS	0	-0.021	-0.016	17.430	0.020	0.020	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.027	0.003	22.356	0.009	0.009	0.000	0.000	0.000	0.000
48	A	49	THR	0	0.011	0.001	25.179	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.865	0.916	26.186	0.080	0.080	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.914	0.968	25.721	0.124	0.124	0.000	0.000	0.000	0.000
51	A	52	GLN	0	0.048	0.008	24.413	0.006	0.006	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.883	0.945	20.442	0.202	0.202	0.000	0.000	0.000	0.000
53	A	54	TYR	0	0.098	0.064	20.283	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.858	0.901	21.442	0.111	0.111	0.000	0.000	0.000	0.000
55	A	56	ASN	0	0.000	0.013	19.638	0.022	0.022	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.061	0.035	16.081	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.857	0.928	17.827	0.126	0.126	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.035	-0.004	20.516	0.015	0.015	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.018	-0.002	15.833	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	61	PRO	0	0.036	0.031	13.587	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.008	0.009	11.356	-0.072	-0.072	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.040	-0.024	10.198	0.057	0.057	0.000	0.000	0.000	0.000
63	A	64	ALA	0	-0.012	-0.006	9.784	-0.082	-0.082	0.000	0.000	0.000	0.000
64	A	65	MET	0	-0.022	0.020	10.230	0.094	0.094	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.015	0.008	11.246	-0.044	-0.044	0.000	0.000	0.000	0.000
66	A	67	VAL	0	0.024	0.013	12.206	0.040	0.040	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.006	-0.006	14.738	-0.020	-0.020	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.757	-0.873	17.463	-0.223	-0.223	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.066	-0.020	19.586	0.012	0.012	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.876	-0.937	22.918	-0.138	-0.138	0.000	0.000	0.000	0.000
71	A	72	ASN	0	-0.053	-0.039	21.889	0.013	0.013	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.056	0.021	20.849	-0.018	-0.018	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.032	-0.011	20.009	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.822	0.926	14.931	0.285	0.285	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.006	-0.004	13.058	0.015	0.015	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.013	-0.017	7.641	-0.026	-0.026	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.888	-0.923	9.998	-0.375	-0.375	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.010	-0.011	5.565	-0.137	-0.137	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.965	0.981	6.214	0.641	0.641	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.091	0.032	5.001	-0.400	-0.342	-0.001	-0.006	-0.051	0.000
81	A	82	LEU	0	-0.030	-0.002	6.732	0.203	0.203	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.037	-0.031	9.280	-0.061	-0.061	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.854	-0.904	9.145	-0.374	-0.374	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.844	-0.919	12.241	-0.080	-0.080	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.099	-0.068	15.424	-0.033	-0.033	0.000	0.000	0.000	0.000
86	A	87	VAL	0	0.058	0.050	18.317	0.024	0.024	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.030	-0.020	20.844	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.789	-0.899	23.548	-0.119	-0.119	0.000	0.000	0.000	0.000
89	A	90	PRO	0	0.016	0.013	25.481	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.032	-0.028	28.845	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.007	-0.004	27.392	0.003	0.003	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.020	0.020	26.618	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.002	-0.019	17.637	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.007	-0.024	22.840	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.008	0.007	24.682	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.960	0.980	22.379	0.103	0.103	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.052	-0.017	18.106	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	99	ASN	0	0.024	0.005	22.080	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.962	-0.975	24.926	-0.110	-0.110	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.795	0.893	16.839	0.289	0.289	0.000	0.000	0.000	0.000
101	A	102	TYR	0	-0.073	-0.065	18.015	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.925	-0.942	23.957	-0.116	-0.116	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.003	0.010	27.107	0.006	0.006	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.016	-0.024	28.386	0.006	0.006	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.095	-0.042	27.908	0.005	0.005	0.000	0.000	0.000	0.000
106	A	107	THR	0	0.013	-0.023	29.956	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.886	-0.911	31.964	-0.073	-0.073	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.052	-0.022	30.962	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.000	0.015	28.759	0.005	0.005	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.021	-0.012	32.085	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.845	-0.892	29.326	-0.111	-0.111	0.000	0.000	0.000	0.000
112	A	113	LYS	1	1.001	0.992	29.335	0.064	0.064	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.006	0.006	29.459	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.845	-0.897	28.772	-0.083	-0.083	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.772	0.852	24.484	0.127	0.127	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.026	-0.014	21.264	0.008	0.008	0.000	0.000	0.000	0.000
117	A	118	ILE	0	0.019	0.007	17.218	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.055	-0.024	14.738	0.009	0.009	0.000	0.000	0.000	0.000
119	A	120	VAL	0	0.044	0.016	11.392	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.013	-0.017	8.386	0.039	0.039	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.829	0.893	4.439	0.109	0.218	-0.001	-0.005	-0.103	0.000
122	A	123	PRO	0	-0.011	-0.006	2.410	-0.340	-0.052	1.186	-0.366	-1.108	0.000
123	A	124	THR	0	-0.050	-0.037	2.675	-2.387	-1.249	1.887	-0.919	-2.107	-0.011
124	A	125	ALA	0	-0.048	-0.026	2.612	-0.367	0.021	1.067	0.187	-1.642	-0.005
125	A	126	PHE	0	0.039	0.019	2.313	-0.731	0.317	1.517	-0.404	-2.161	-0.003
126	A	127	SER	0	-0.069	-0.047	5.456	0.224	0.224	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.913	0.959	8.812	0.231	0.231	0.000	0.000	0.000	0.000
128	A	129	GLN	0	0.023	0.039	11.580	0.029	0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:VAL)