FMO DATABASE

FMODB ID: R8258

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	OptHSide
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	-1114142.798464
FMO2-HF: Nuclear repulsion	1064033.287218
FMO2-HF: Total energy	-50109.511246
FMO2-MP2: Total energy	-50258.419816

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.
-6.114	-1.416	8.356	-3.376	-9.677	-0.031

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 : -0.051 / q_NPA : -0.030

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	0.041	0.020	3.250	-2.558	-0.128	0.043	-1.191	-1.283	-0.002
4	A	5	PRO	0	-0.038	-0.026	4.859	0.479	0.479	0.000	0.000	0.000	0.000
5	A	6	GLU	-1	-0.885	-0.900	7.588	0.004	0.004	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.049	-0.010	10.576	0.011	0.011	0.000	0.000	0.000	0.000
7	A	8	TYR	0	-0.051	-0.039	9.937	0.052	0.052	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.802	-0.886	9.454	-0.686	-0.686	0.000	0.000	0.000	0.000
9	A	10	SER	0	0.072	0.030	10.662	0.000	0.000	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.100	-0.048	12.523	0.032	0.032	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.042	-0.022	7.614	0.015	0.015	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.863	-0.936	12.250	-0.262	-0.262	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.838	0.914	14.996	0.267	0.267	0.000	0.000	0.000	0.000
14	A	15	PRO	0	-0.002	0.027	17.111	-0.039	-0.039	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.001	0.003	16.812	0.024	0.024	0.000	0.000	0.000	0.000
16	A	17	TYR	0	-0.007	0.000	17.876	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.022	0.014	15.241	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	19	HIS	0	-0.038	-0.029	16.061	0.026	0.026	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.015	-0.009	13.141	-0.024	-0.024	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.005	-0.018	14.470	0.049	0.049	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.013	-0.008	14.504	-0.029	-0.029	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.041	0.007	16.333	0.018	0.018	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.861	0.946	18.926	0.152	0.152	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.021	-0.007	22.261	0.000	0.000	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.859	-0.898	23.973	-0.134	-0.134	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.011	0.008	22.059	0.007	0.007	0.000	0.000	0.000	0.000
27	A	28	THR	0	-0.057	-0.042	22.428	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	29	PRO	0	0.015	0.003	19.399	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.042	-0.028	19.780	0.029	0.029	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.049	0.027	17.735	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	32	ASN	0	-0.049	-0.034	19.163	0.025	0.025	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.078	0.059	19.180	-0.026	-0.026	0.000	0.000	0.000	0.000
33	A	34	MET	0	-0.054	-0.022	17.544	0.035	0.035	0.000	0.000	0.000	0.000
34	A	35	TRP	0	0.043	0.037	18.716	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	36	PHE	0	-0.008	-0.012	12.770	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.017	0.003	15.109	0.037	0.037	0.000	0.000	0.000	0.000
37	A	38	TRP	0	-0.032	-0.035	5.491	-0.080	-0.080	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.782	-0.869	10.661	-0.437	-0.437	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.043	0.033	9.680	0.117	0.117	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.924	-0.942	6.245	-0.166	-0.166	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.071	-0.051	6.119	-0.582	-0.582	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.015	-0.005	8.466	0.146	0.146	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.812	0.893	10.636	0.416	0.416	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.034	0.003	12.044	0.033	0.033	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.037	0.039	16.942	0.022	0.022	0.000	0.000	0.000	0.000
46	A	47	HIS	0	-0.014	-0.017	17.284	0.022	0.022	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.017	0.014	22.148	0.009	0.009	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.009	-0.011	24.469	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.873	0.917	25.925	0.105	0.105	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.911	0.960	25.219	0.147	0.147	0.000	0.000	0.000	0.000
51	A	52	GLN	0	0.048	0.008	24.388	0.005	0.005	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.888	0.952	20.216	0.222	0.222	0.000	0.000	0.000	0.000
53	A	54	TYR	0	0.091	0.060	20.160	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.877	0.921	21.246	0.129	0.129	0.000	0.000	0.000	0.000
55	A	56	ASN	0	0.006	0.004	19.605	0.021	0.021	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.040	0.024	15.993	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.850	0.930	17.736	0.161	0.161	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.026	0.000	20.403	0.010	0.010	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.018	0.001	15.642	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	61	PRO	0	0.048	0.035	13.246	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.011	0.010	11.163	-0.083	-0.083	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.028	-0.021	10.164	0.072	0.072	0.000	0.000	0.000	0.000
63	A	64	ALA	0	-0.017	-0.009	9.826	-0.090	-0.090	0.000	0.000	0.000	0.000
64	A	65	MET	0	-0.018	0.013	10.243	0.094	0.094	0.000	0.000	0.000	0.000
65	A	66	SER	0	0.008	0.019	11.267	-0.043	-0.043	0.000	0.000	0.000	0.000
66	A	67	VAL	0	0.017	0.010	12.173	0.032	0.032	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.020	-0.008	14.788	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.792	-0.891	17.483	-0.188	-0.188	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.057	-0.025	19.376	0.007	0.007	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.885	-0.935	22.743	-0.125	-0.125	0.000	0.000	0.000	0.000
71	A	72	ASN	0	-0.050	-0.033	22.112	0.014	0.014	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.050	0.018	20.979	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.011	-0.011	19.994	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.830	0.924	14.914	0.240	0.240	0.000	0.000	0.000	0.000
75	A	76	TYR	0	0.000	-0.005	13.574	0.006	0.006	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.023	-0.019	7.863	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.947	-0.963	10.353	-0.354	-0.354	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.007	-0.005	5.335	-0.087	-0.087	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.959	0.973	6.045	0.667	0.667	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.091	0.038	4.994	-0.466	-0.403	-0.001	-0.007	-0.054	0.000
81	A	82	LEU	0	-0.035	-0.004	6.558	0.240	0.240	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.051	-0.037	9.252	-0.070	-0.070	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.852	-0.906	9.234	-0.616	-0.616	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.840	-0.920	12.340	-0.161	-0.161	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.103	-0.064	15.333	-0.029	-0.029	0.000	0.000	0.000	0.000
86	A	87	VAL	0	0.038	0.029	17.875	0.027	0.027	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.034	-0.019	20.527	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.799	-0.917	23.106	-0.153	-0.153	0.000	0.000	0.000	0.000
89	A	90	PRO	0	0.023	0.017	25.065	0.003	0.003	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.037	-0.032	28.420	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.003	-0.002	26.946	0.005	0.005	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.035	0.026	26.149	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.005	-0.017	17.361	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.004	-0.018	22.619	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.005	0.003	24.268	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.959	0.984	22.145	0.135	0.135	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.049	-0.012	18.040	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	ASN	0	0.037	-0.001	21.939	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.954	-0.970	25.080	-0.123	-0.123	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.844	0.929	16.406	0.315	0.315	0.000	0.000	0.000	0.000
101	A	102	TYR	0	-0.083	-0.071	17.875	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.941	-0.946	23.745	-0.121	-0.121	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.022	-0.007	26.973	0.006	0.006	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.007	-0.021	28.259	0.006	0.006	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.100	-0.037	27.372	0.006	0.006	0.000	0.000	0.000	0.000
106	A	107	THR	0	0.018	-0.024	29.506	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.894	-0.913	31.675	-0.085	-0.085	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.059	-0.032	30.640	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.008	0.018	28.278	0.005	0.005	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.042	0.001	31.575	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.857	-0.893	29.350	-0.131	-0.131	0.000	0.000	0.000	0.000
112	A	113	LYS	1	1.001	0.992	29.242	0.080	0.080	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.016	0.012	29.141	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.845	-0.902	28.791	-0.106	-0.106	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.784	0.858	24.382	0.149	0.149	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.022	-0.011	21.171	0.008	0.008	0.000	0.000	0.000	0.000
117	A	118	ILE	0	0.006	0.002	16.836	-0.009	-0.009	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.052	-0.024	14.485	0.010	0.010	0.000	0.000	0.000	0.000
119	A	120	VAL	0	0.060	0.022	11.197	-0.024	-0.024	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.019	-0.012	8.015	0.030	0.030	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.867	0.905	4.549	0.597	0.688	-0.001	-0.004	-0.086	0.000
122	A	123	PRO	0	-0.017	-0.007	2.528	-0.499	-0.107	1.225	-0.413	-1.203	0.000
123	A	124	THR	0	-0.030	-0.036	2.564	-1.639	-1.586	3.655	-1.027	-2.681	-0.013
124	A	125	ALA	0	-0.051	-0.027	2.475	-1.006	-0.125	1.649	-0.436	-2.094	-0.010
125	A	126	PHE	0	0.039	0.023	2.244	-0.599	0.189	1.786	-0.298	-2.276	-0.006
126	A	127	SER	0	-0.023	-0.006	5.443	0.242	0.242	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.955	0.982	8.748	0.143	0.143	0.000	0.000	0.000	0.000
128	A	129	GLN	0	0.010	0.029	11.527	0.034	0.034	0.000	0.000	0.000	0.000

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