FMO DATABASE

FMODB ID: QVL8Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-951760.4673
FMO2-HF: Nuclear repulsion	906551.000883
FMO2-HF: Total energy	-45209.466417
FMO2-MP2: Total energy	-45341.177999

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.
-6.964	0.656	13.393	-7.988	-13.025	-0.031

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 : -0.010 / q_NPA : -0.016

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	-0.001	0.010	3.406	1.841	4.133	0.361	-0.765	-1.888	0.003
4	A	14	GLY	0	0.069	0.043	4.736	-1.507	-1.407	-0.001	-0.006	-0.093	0.000
5	A	15	ARG	1	0.867	0.944	6.812	0.293	0.293	0.000	0.000	0.000	0.000
6	A	16	ALA	0	0.021	0.004	8.321	-0.137	-0.137	0.000	0.000	0.000	0.000
7	A	17	PRO	0	0.005	0.007	10.107	0.089	0.089	0.000	0.000	0.000	0.000
8	A	18	ILE	0	-0.043	-0.018	8.804	0.287	0.287	0.000	0.000	0.000	0.000
9	A	19	ASP	-1	-0.868	-0.940	11.632	1.161	1.161	0.000	0.000	0.000	0.000
10	A	20	ALA	0	-0.086	-0.054	12.602	-0.211	-0.211	0.000	0.000	0.000	0.000
11	A	21	TYR	0	0.035	0.017	12.436	0.187	0.187	0.000	0.000	0.000	0.000
12	A	22	GLY	0	-0.007	0.008	14.271	-0.115	-0.115	0.000	0.000	0.000	0.000
13	A	23	ASN	0	-0.028	-0.037	14.262	0.041	0.041	0.000	0.000	0.000	0.000
14	A	24	GLY	0	0.057	0.042	14.040	0.022	0.022	0.000	0.000	0.000	0.000
15	A	25	GLY	0	-0.036	-0.027	10.414	0.038	0.038	0.000	0.000	0.000	0.000
16	A	26	PHE	0	-0.028	-0.005	8.117	-0.184	-0.184	0.000	0.000	0.000	0.000
17	A	27	ARG	1	0.927	0.964	8.706	-0.966	-0.966	0.000	0.000	0.000	0.000
18	A	28	PHE	0	0.065	0.023	3.248	-2.190	-0.891	0.183	-0.615	-0.867	0.006
19	A	29	ALA	0	0.044	0.039	6.942	0.330	0.330	0.000	0.000	0.000	0.000
20	A	30	ASP	-1	-0.942	-0.964	8.400	1.058	1.058	0.000	0.000	0.000	0.000
21	A	31	MET	0	-0.060	-0.018	1.793	0.185	-0.917	3.717	-1.130	-1.486	-0.003
22	A	32	SER	0	-0.053	-0.036	6.858	0.039	0.039	0.000	0.000	0.000	0.000
23	A	33	HIS	0	-0.044	-0.032	3.662	-0.759	-0.408	0.004	-0.080	-0.275	0.000
24	A	34	ARG	1	0.945	0.987	4.935	-1.248	-1.248	0.000	0.000	0.000	0.000
25	A	35	GLY	0	0.072	0.022	8.163	-0.125	-0.125	0.000	0.000	0.000	0.000
26	A	36	SER	0	0.017	-0.004	8.957	0.341	0.341	0.000	0.000	0.000	0.000
27	A	37	ILE	0	-0.019	0.003	5.613	0.131	0.131	0.000	0.000	0.000	0.000
28	A	38	ILE	0	0.015	0.019	7.300	-0.456	-0.456	0.000	0.000	0.000	0.000
29	A	39	CYS	0	-0.051	-0.022	6.795	0.892	0.892	0.000	0.000	0.000	0.000
30	A	40	ILE	0	0.045	0.014	6.730	-0.332	-0.332	0.000	0.000	0.000	0.000
31	A	41	PRO	0	0.000	-0.009	7.900	0.300	0.300	0.000	0.000	0.000	0.000
32	A	42	SER	0	-0.056	-0.083	5.705	-0.046	-0.046	0.000	0.000	0.000	0.000
33	A	43	GLY	0	-0.021	-0.006	3.555	-1.551	-1.266	0.004	-0.090	-0.199	0.000
34	A	44	ILE	0	-0.054	-0.015	3.169	-2.690	-1.649	0.039	-0.354	-0.725	0.001
35	A	45	TYR	0	-0.045	-0.042	2.098	-2.118	1.006	9.086	-4.909	-7.301	-0.038
36	A	46	GLY	0	-0.003	-0.006	4.200	-0.570	-0.340	0.000	-0.039	-0.191	0.000
37	A	47	ILE	0	-0.032	-0.027	5.727	-0.677	-0.677	0.000	0.000	0.000	0.000
38	A	48	ASP	-1	-0.923	-0.963	9.500	0.185	0.185	0.000	0.000	0.000	0.000
39	A	49	MET	0	-0.064	-0.002	12.122	0.012	0.012	0.000	0.000	0.000	0.000
40	A	50	THR	0	0.023	0.003	14.601	0.056	0.056	0.000	0.000	0.000	0.000
41	A	51	GLY	0	-0.014	-0.017	17.650	0.013	0.013	0.000	0.000	0.000	0.000
42	A	52	PRO	0	-0.016	-0.006	17.873	0.008	0.008	0.000	0.000	0.000	0.000
43	A	53	VAL	0	-0.037	-0.020	19.131	0.023	0.023	0.000	0.000	0.000	0.000
44	A	54	PRO	0	-0.003	0.018	17.294	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	55	THR	0	0.015	-0.004	17.463	-0.053	-0.053	0.000	0.000	0.000	0.000
46	A	56	GLN	0	0.027	-0.026	17.898	0.033	0.033	0.000	0.000	0.000	0.000
47	A	57	GLU	-1	-0.897	-0.946	14.784	-0.568	-0.568	0.000	0.000	0.000	0.000
48	A	58	ASP	-1	-0.825	-0.887	13.573	-0.132	-0.132	0.000	0.000	0.000	0.000
49	A	59	ILE	0	-0.031	-0.020	13.033	0.050	0.050	0.000	0.000	0.000	0.000
50	A	60	SER	0	-0.030	-0.030	12.556	-0.079	-0.079	0.000	0.000	0.000	0.000
51	A	61	ARG	1	1.019	1.005	4.941	3.828	3.828	0.000	0.000	0.000	0.000
52	A	62	VAL	0	-0.002	0.003	10.719	0.013	0.013	0.000	0.000	0.000	0.000
53	A	63	LEU	0	-0.033	-0.025	12.800	0.013	0.013	0.000	0.000	0.000	0.000
54	A	64	GLU	-1	-0.983	-0.998	11.341	-1.278	-1.278	0.000	0.000	0.000	0.000
55	A	65	GLU	-1	-0.797	-0.826	7.850	-1.468	-1.468	0.000	0.000	0.000	0.000
56	A	66	SER	0	-0.033	-0.022	12.717	0.138	0.138	0.000	0.000	0.000	0.000
57	A	67	ASP	-1	-0.889	-0.932	16.123	-0.248	-0.248	0.000	0.000	0.000	0.000
58	A	68	GLN	0	-0.097	-0.051	13.310	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	69	ILE	0	-0.077	-0.033	11.814	0.109	0.109	0.000	0.000	0.000	0.000
60	A	70	GLU	-1	-0.914	-0.952	15.996	0.043	0.043	0.000	0.000	0.000	0.000
61	A	71	VAL	0	-0.064	-0.034	18.257	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	72	LEU	0	-0.007	0.001	14.641	0.042	0.042	0.000	0.000	0.000	0.000
63	A	73	LEU	0	-0.038	-0.015	16.443	-0.029	-0.029	0.000	0.000	0.000	0.000
64	A	74	ILE	0	0.023	0.000	15.966	0.060	0.060	0.000	0.000	0.000	0.000
65	A	75	GLY	0	0.027	-0.001	16.199	-0.031	-0.031	0.000	0.000	0.000	0.000
66	A	76	THR	0	-0.024	-0.015	16.795	0.022	0.022	0.000	0.000	0.000	0.000
67	A	77	GLY	0	0.040	0.004	18.152	-0.047	-0.047	0.000	0.000	0.000	0.000
68	A	78	VAL	0	-0.043	-0.029	19.185	0.025	0.025	0.000	0.000	0.000	0.000
69	A	79	GLU	-1	-0.912	-0.945	22.182	0.234	0.234	0.000	0.000	0.000	0.000
70	A	80	LEU	0	-0.025	0.012	23.252	0.018	0.018	0.000	0.000	0.000	0.000
71	A	81	LEU	0	-0.003	-0.002	22.515	-0.036	-0.036	0.000	0.000	0.000	0.000
72	A	82	ARG	1	0.944	0.962	24.591	-0.086	-0.086	0.000	0.000	0.000	0.000
73	A	83	LEU	0	0.074	0.050	21.370	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	84	PRO	0	0.033	0.022	23.261	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	85	GLU	-1	-0.948	-0.983	25.686	-0.033	-0.033	0.000	0.000	0.000	0.000
76	A	86	GLU	-1	-0.850	-0.934	24.840	-0.058	-0.058	0.000	0.000	0.000	0.000
77	A	87	LEU	0	0.003	-0.010	19.774	-0.020	-0.020	0.000	0.000	0.000	0.000
78	A	88	ARG	1	0.837	0.918	22.593	-0.022	-0.022	0.000	0.000	0.000	0.000
79	A	89	VAL	0	0.001	0.009	25.054	0.001	0.001	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.027	0.016	20.435	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	91	LEU	0	0.017	-0.001	17.909	-0.019	-0.019	0.000	0.000	0.000	0.000
82	A	92	TRP	0	0.006	0.008	21.447	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	93	GLU	-1	-0.990	-1.008	23.520	-0.186	-0.186	0.000	0.000	0.000	0.000
84	A	94	LYS	1	0.882	0.953	18.839	0.330	0.330	0.000	0.000	0.000	0.000
85	A	95	ARG	1	0.856	0.935	21.052	0.091	0.091	0.000	0.000	0.000	0.000
86	A	96	ILE	0	0.034	0.037	16.860	0.013	0.013	0.000	0.000	0.000	0.000
87	A	97	SER	0	-0.068	-0.022	20.879	0.009	0.009	0.000	0.000	0.000	0.000
88	A	98	SER	0	0.006	-0.017	20.504	0.023	0.023	0.000	0.000	0.000	0.000
89	A	99	ASP	-1	-0.879	-0.945	21.126	0.186	0.186	0.000	0.000	0.000	0.000
90	A	100	THR	0	-0.074	-0.026	20.834	0.036	0.036	0.000	0.000	0.000	0.000
91	A	101	MET	0	-0.011	0.006	20.411	0.007	0.007	0.000	0.000	0.000	0.000
92	A	102	SER	0	0.035	0.024	20.751	0.040	0.040	0.000	0.000	0.000	0.000
93	A	103	THR	0	0.019	-0.046	14.857	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	104	GLY	0	-0.001	0.002	17.117	0.071	0.071	0.000	0.000	0.000	0.000
95	A	105	ALA	0	-0.033	-0.023	19.075	0.029	0.029	0.000	0.000	0.000	0.000
96	A	106	ALA	0	0.059	0.029	16.697	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	107	VAL	0	0.003	0.012	13.719	0.036	0.036	0.000	0.000	0.000	0.000
98	A	108	ARG	1	0.900	0.949	15.881	-0.521	-0.521	0.000	0.000	0.000	0.000
99	A	109	THR	0	0.017	0.004	18.941	-0.030	-0.030	0.000	0.000	0.000	0.000
100	A	110	PHE	0	0.005	-0.012	11.103	-0.033	-0.033	0.000	0.000	0.000	0.000
101	A	111	ASN	0	-0.008	-0.008	14.365	0.094	0.094	0.000	0.000	0.000	0.000
102	A	112	VAL	0	-0.011	0.003	16.446	-0.029	-0.029	0.000	0.000	0.000	0.000
103	A	113	LEU	0	0.018	-0.002	18.403	-0.034	-0.034	0.000	0.000	0.000	0.000
104	A	114	LEU	0	-0.023	-0.011	12.628	-0.035	-0.035	0.000	0.000	0.000	0.000
105	A	115	ALA	0	-0.032	-0.014	16.625	-0.032	-0.032	0.000	0.000	0.000	0.000
106	A	116	GLU	-1	-0.978	-0.986	19.081	0.283	0.283	0.000	0.000	0.000	0.000
107	A	117	ASP	-1	-0.953	-0.962	18.584	0.337	0.337	0.000	0.000	0.000	0.000
108	A	118	ARG	1	0.891	0.953	19.522	-0.313	-0.313	0.000	0.000	0.000	0.000
109	A	119	ALA	0	0.028	0.026	16.427	0.067	0.067	0.000	0.000	0.000	0.000
110	A	120	VAL	0	-0.026	-0.015	14.991	-0.045	-0.045	0.000	0.000	0.000	0.000
111	A	121	ALA	0	0.035	0.016	12.718	0.082	0.082	0.000	0.000	0.000	0.000
112	A	122	ALA	0	-0.015	-0.015	11.958	-0.058	-0.058	0.000	0.000	0.000	0.000
113	A	123	LEU	0	0.007	0.019	11.305	0.131	0.131	0.000	0.000	0.000	0.000
114	A	124	LEU	0	-0.032	-0.029	10.621	-0.107	-0.107	0.000	0.000	0.000	0.000
115	A	125	PHE	0	0.069	0.028	11.803	0.135	0.135	0.000	0.000	0.000	0.000
116	A	126	ALA	0	0.000	0.026	11.314	0.029	0.029	0.000	0.000	0.000	0.000
117	A	127	VAL	0	-0.021	0.010	13.320	-0.126	-0.126	0.000	0.000	0.000	0.000
118	A	128	GLU	-1	-0.931	-0.958	16.015	0.547	0.547	0.000	0.000	0.000	0.000

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