FMO DATABASE

FMODB ID: 4JYNN

Calculation Name: 2FI9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FI9

Chain ID: A

ChEMBL ID:

UniProt ID: Q8RIU4

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-954103.878307
FMO2-HF: Nuclear repulsion	908893.585364
FMO2-HF: Total energy	-45210.292943
FMO2-MP2: Total energy	-45341.969268

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:11:HIS)

Summations of interaction energy for fragment #1(A:11:HIS)

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.
-10.413	-0.156	6.561	-5.876	-10.945	-0.028

Interaction energy analysis for fragmet #1(A:11:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : 0.003

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	13	PRO	0	-0.013	0.006	3.780	-1.267	1.565	0.025	-1.248	-1.609	0.004
4	A	14	GLY	0	0.064	0.028	4.754	-0.583	-0.462	-0.001	-0.006	-0.114	0.000
5	A	15	ARG	1	0.801	0.898	7.034	0.632	0.632	0.000	0.000	0.000	0.000
6	A	16	ALA	0	0.015	0.001	8.597	-0.139	-0.139	0.000	0.000	0.000	0.000
7	A	17	PRO	0	0.015	-0.001	10.491	0.132	0.132	0.000	0.000	0.000	0.000
8	A	18	ILE	0	-0.017	-0.012	8.453	0.046	0.046	0.000	0.000	0.000	0.000
9	A	19	ASP	-1	-0.862	-0.939	10.838	0.295	0.295	0.000	0.000	0.000	0.000
10	A	20	ALA	0	-0.054	-0.031	11.779	-0.055	-0.055	0.000	0.000	0.000	0.000
11	A	21	TYR	0	0.026	0.021	11.728	0.091	0.091	0.000	0.000	0.000	0.000
12	A	22	GLY	0	-0.004	0.004	13.762	-0.125	-0.125	0.000	0.000	0.000	0.000
13	A	23	ASN	0	-0.064	-0.039	13.894	0.023	0.023	0.000	0.000	0.000	0.000
14	A	24	GLY	0	0.096	0.060	14.023	0.091	0.091	0.000	0.000	0.000	0.000
15	A	25	GLY	0	-0.039	-0.029	10.604	0.272	0.272	0.000	0.000	0.000	0.000
16	A	26	PHE	0	-0.015	-0.002	7.925	-0.277	-0.277	0.000	0.000	0.000	0.000
17	A	27	ARG	1	0.808	0.895	8.117	-0.336	-0.336	0.000	0.000	0.000	0.000
18	A	28	PHE	0	0.055	0.017	2.688	-0.516	0.310	0.184	-0.261	-0.749	0.000
19	A	29	ALA	0	0.022	0.025	6.873	-0.180	-0.180	0.000	0.000	0.000	0.000
20	A	30	ASP	-1	-0.846	-0.910	8.705	0.055	0.055	0.000	0.000	0.000	0.000
21	A	31	MET	0	-0.067	-0.010	2.431	-0.489	0.133	0.510	-0.355	-0.778	-0.001
22	A	32	SER	0	-0.037	-0.034	6.379	0.109	0.109	0.000	0.000	0.000	0.000
23	A	33	HIS	0	-0.028	-0.010	3.329	1.449	2.081	0.031	-0.245	-0.418	0.002
24	A	34	ARG	1	0.909	0.959	4.983	-5.547	-5.505	-0.001	-0.007	-0.034	0.000
25	A	35	GLY	0	0.052	0.026	8.533	0.611	0.611	0.000	0.000	0.000	0.000
26	A	36	SER	0	0.023	0.001	9.078	0.165	0.165	0.000	0.000	0.000	0.000
27	A	37	ILE	0	-0.013	0.005	5.977	0.619	0.619	0.000	0.000	0.000	0.000
28	A	38	ILE	0	0.002	0.007	7.090	-0.694	-0.694	0.000	0.000	0.000	0.000
29	A	39	CYS	0	-0.043	-0.010	6.924	0.726	0.726	0.000	0.000	0.000	0.000
30	A	40	ILE	0	0.028	0.015	6.411	-0.171	-0.171	0.000	0.000	0.000	0.000
31	A	41	PRO	0	0.027	0.001	7.822	-0.060	-0.060	0.000	0.000	0.000	0.000
32	A	42	SER	0	-0.066	-0.057	5.524	-0.499	-0.499	0.000	0.000	0.000	0.000
33	A	43	GLY	0	-0.029	-0.020	3.312	-1.780	-1.589	0.008	-0.057	-0.142	0.000
34	A	44	ILE	0	-0.050	-0.011	4.213	-0.706	-0.233	0.000	-0.124	-0.350	0.000
35	A	45	TYR	0	-0.018	-0.027	2.364	-0.777	3.550	5.803	-3.530	-6.600	-0.033
36	A	46	GLY	0	0.006	0.000	4.004	-1.939	-1.748	0.002	-0.043	-0.151	0.000
37	A	47	ILE	0	-0.042	-0.031	5.944	-0.634	-0.634	0.000	0.000	0.000	0.000
38	A	48	ASP	-1	-0.920	-0.959	9.513	1.227	1.227	0.000	0.000	0.000	0.000
39	A	49	MET	0	-0.038	-0.003	12.466	-0.193	-0.193	0.000	0.000	0.000	0.000
40	A	50	THR	0	0.014	0.003	15.018	0.012	0.012	0.000	0.000	0.000	0.000
41	A	51	GLY	0	-0.001	-0.007	18.053	-0.062	-0.062	0.000	0.000	0.000	0.000
42	A	52	PRO	0	-0.037	-0.018	18.377	0.042	0.042	0.000	0.000	0.000	0.000
43	A	53	VAL	0	-0.024	-0.015	19.705	-0.030	-0.030	0.000	0.000	0.000	0.000
44	A	54	PRO	0	-0.023	0.006	16.616	0.015	0.015	0.000	0.000	0.000	0.000
45	A	55	THR	0	0.015	-0.031	17.632	-0.107	-0.107	0.000	0.000	0.000	0.000
46	A	56	GLN	0	0.018	-0.026	18.131	0.015	0.015	0.000	0.000	0.000	0.000
47	A	57	GLU	-1	-0.913	-0.944	15.466	0.216	0.216	0.000	0.000	0.000	0.000
48	A	58	ASP	-1	-0.828	-0.869	13.731	0.777	0.777	0.000	0.000	0.000	0.000
49	A	59	ILE	0	-0.005	-0.007	13.228	0.068	0.068	0.000	0.000	0.000	0.000
50	A	60	SER	0	-0.016	-0.009	12.506	-0.119	-0.119	0.000	0.000	0.000	0.000
51	A	61	ARG	1	0.955	0.965	6.258	1.736	1.736	0.000	0.000	0.000	0.000
52	A	62	VAL	0	-0.015	-0.004	10.528	-0.123	-0.123	0.000	0.000	0.000	0.000
53	A	63	LEU	0	-0.007	-0.007	12.762	-0.048	-0.048	0.000	0.000	0.000	0.000
54	A	64	GLU	-1	-0.962	-0.979	10.751	-0.753	-0.753	0.000	0.000	0.000	0.000
55	A	65	GLU	-1	-0.764	-0.851	7.510	-1.755	-1.755	0.000	0.000	0.000	0.000
56	A	66	SER	0	0.031	-0.009	12.368	0.047	0.047	0.000	0.000	0.000	0.000
57	A	67	ASP	-1	-0.924	-0.933	15.873	-0.326	-0.326	0.000	0.000	0.000	0.000
58	A	68	GLN	0	-0.097	-0.053	13.441	-0.102	-0.102	0.000	0.000	0.000	0.000
59	A	69	ILE	0	-0.050	-0.024	11.934	0.032	0.032	0.000	0.000	0.000	0.000
60	A	70	GLU	-1	-0.809	-0.888	16.137	-0.046	-0.046	0.000	0.000	0.000	0.000
61	A	71	VAL	0	-0.042	-0.007	18.025	0.022	0.022	0.000	0.000	0.000	0.000
62	A	72	LEU	0	0.001	0.010	14.437	0.008	0.008	0.000	0.000	0.000	0.000
63	A	73	LEU	0	-0.022	-0.013	16.468	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	74	ILE	0	0.012	-0.002	15.996	0.091	0.091	0.000	0.000	0.000	0.000
65	A	75	GLY	0	0.052	0.004	16.134	-0.050	-0.050	0.000	0.000	0.000	0.000
66	A	76	THR	0	-0.017	-0.011	16.909	0.075	0.075	0.000	0.000	0.000	0.000
67	A	77	GLY	0	0.032	0.006	18.115	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	78	VAL	0	-0.046	-0.035	19.114	-0.021	-0.021	0.000	0.000	0.000	0.000
69	A	79	GLU	-1	-0.890	-0.946	21.833	0.268	0.268	0.000	0.000	0.000	0.000
70	A	80	LEU	0	-0.050	0.008	23.206	0.030	0.030	0.000	0.000	0.000	0.000
71	A	81	LEU	0	-0.013	0.004	22.692	-0.029	-0.029	0.000	0.000	0.000	0.000
72	A	82	ARG	1	0.939	0.957	24.972	-0.190	-0.190	0.000	0.000	0.000	0.000
73	A	83	LEU	0	0.057	0.037	21.124	0.019	0.019	0.000	0.000	0.000	0.000
74	A	84	PRO	0	0.036	0.014	23.121	-0.032	-0.032	0.000	0.000	0.000	0.000
75	A	85	GLU	-1	-0.821	-0.893	25.427	0.100	0.100	0.000	0.000	0.000	0.000
76	A	86	GLU	-1	-0.882	-0.956	24.464	0.135	0.135	0.000	0.000	0.000	0.000
77	A	87	LEU	0	0.001	-0.001	19.542	-0.024	-0.024	0.000	0.000	0.000	0.000
78	A	88	ARG	1	0.763	0.869	22.302	-0.144	-0.144	0.000	0.000	0.000	0.000
79	A	89	VAL	0	-0.014	0.005	24.831	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.037	0.019	20.355	-0.016	-0.016	0.000	0.000	0.000	0.000
81	A	91	LEU	0	0.011	0.001	17.516	-0.030	-0.030	0.000	0.000	0.000	0.000
82	A	92	TRP	0	0.058	0.036	21.080	-0.034	-0.034	0.000	0.000	0.000	0.000
83	A	93	GLU	-1	-0.970	-0.987	23.590	-0.063	-0.063	0.000	0.000	0.000	0.000
84	A	94	LYS	1	0.829	0.908	17.389	0.285	0.285	0.000	0.000	0.000	0.000
85	A	95	ARG	1	0.791	0.887	20.832	0.050	0.050	0.000	0.000	0.000	0.000
86	A	96	ILE	0	0.006	0.033	16.362	0.001	0.001	0.000	0.000	0.000	0.000
87	A	97	SER	0	-0.045	-0.032	20.572	0.032	0.032	0.000	0.000	0.000	0.000
88	A	98	SER	0	-0.002	-0.022	20.493	0.008	0.008	0.000	0.000	0.000	0.000
89	A	99	ASP	-1	-0.900	-0.945	21.392	0.189	0.189	0.000	0.000	0.000	0.000
90	A	100	THR	0	-0.064	-0.044	20.969	0.029	0.029	0.000	0.000	0.000	0.000
91	A	101	MET	0	-0.025	0.003	20.456	-0.025	-0.025	0.000	0.000	0.000	0.000
92	A	102	SER	0	0.043	0.038	20.510	0.045	0.045	0.000	0.000	0.000	0.000
93	A	103	THR	0	0.010	-0.032	14.575	-0.051	-0.051	0.000	0.000	0.000	0.000
94	A	104	GLY	0	0.015	0.004	16.651	0.016	0.016	0.000	0.000	0.000	0.000
95	A	105	ALA	0	-0.041	-0.021	18.460	-0.032	-0.032	0.000	0.000	0.000	0.000
96	A	106	ALA	0	0.045	0.030	16.672	-0.034	-0.034	0.000	0.000	0.000	0.000
97	A	107	VAL	0	0.022	0.008	13.016	-0.015	-0.015	0.000	0.000	0.000	0.000
98	A	108	ARG	1	0.885	0.938	15.529	-0.406	-0.406	0.000	0.000	0.000	0.000
99	A	109	THR	0	0.018	-0.004	18.643	-0.047	-0.047	0.000	0.000	0.000	0.000
100	A	110	PHE	0	0.004	-0.003	11.249	-0.026	-0.026	0.000	0.000	0.000	0.000
101	A	111	ASN	0	-0.002	-0.009	14.022	-0.022	-0.022	0.000	0.000	0.000	0.000
102	A	112	VAL	0	-0.026	-0.005	16.501	-0.046	-0.046	0.000	0.000	0.000	0.000
103	A	113	LEU	0	0.022	-0.001	18.764	-0.031	-0.031	0.000	0.000	0.000	0.000
104	A	114	LEU	0	-0.032	-0.009	13.021	-0.041	-0.041	0.000	0.000	0.000	0.000
105	A	115	ALA	0	-0.027	-0.011	17.129	-0.044	-0.044	0.000	0.000	0.000	0.000
106	A	116	GLU	-1	-0.939	-0.962	19.875	0.029	0.029	0.000	0.000	0.000	0.000
107	A	117	ASP	-1	-0.947	-0.972	18.186	-0.145	-0.145	0.000	0.000	0.000	0.000
108	A	118	ARG	1	0.783	0.905	18.846	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	119	ALA	0	0.041	0.034	16.238	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	120	VAL	0	-0.032	-0.026	15.164	0.011	0.011	0.000	0.000	0.000	0.000
111	A	121	ALA	0	0.030	0.023	12.429	-0.038	-0.038	0.000	0.000	0.000	0.000
112	A	122	ALA	0	-0.028	-0.022	12.234	-0.015	-0.015	0.000	0.000	0.000	0.000
113	A	123	LEU	0	0.007	0.010	11.620	0.132	0.132	0.000	0.000	0.000	0.000
114	A	124	LEU	0	-0.038	-0.012	10.801	-0.174	-0.174	0.000	0.000	0.000	0.000
115	A	125	PHE	0	0.070	0.038	12.119	0.244	0.244	0.000	0.000	0.000	0.000
116	A	126	ALA	0	0.011	0.009	11.668	-0.081	-0.081	0.000	0.000	0.000	0.000
117	A	127	VAL	0	-0.031	-0.017	13.503	-0.138	-0.138	0.000	0.000	0.000	0.000
118	A	128	GLU	-1	-0.917	-0.949	15.995	0.831	0.831	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:HIS)