FMO DATABASE

FMODB ID: QYVQY

Calculation Name: 2IEL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2IEL

Chain ID: A

ChEMBL ID:

UniProt ID: Q72LM7

Base Structure: X-ray

Registration Date: 2023-06-22

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1135541.79528
FMO2-HF: Nuclear repulsion	1085645.135359
FMO2-HF: Total energy	-49896.659922
FMO2-MP2: Total energy	-50047.272675

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:ALA)

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

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.
-5.935	-1.915	4.81	-3.501	-5.327	-0.012

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.035 / q_NPA : 0.009

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	4	TYR	0	0.022	-0.002	2.790	1.217	3.337	0.220	-0.965	-1.375	-0.001
4	A	5	LEU	0	0.006	0.016	6.098	-0.389	-0.389	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.000	-0.007	9.555	0.053	0.053	0.000	0.000	0.000	0.000
6	A	7	VAL	0	0.025	0.018	11.684	-0.026	-0.026	0.000	0.000	0.000	0.000
7	A	8	ALA	0	-0.005	-0.023	15.150	-0.010	-0.010	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.011	-0.007	17.831	0.006	0.006	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.947	0.959	21.187	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.032	-0.025	18.883	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.046	0.040	18.514	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.970	0.980	19.209	0.050	0.050	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.066	-0.028	19.319	0.000	0.000	0.000	0.000	0.000	0.000
14	A	15	PRO	0	0.104	0.041	19.241	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.864	-0.938	18.722	-0.130	-0.130	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.050	-0.011	13.678	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.040	0.016	14.195	-0.051	-0.051	0.000	0.000	0.000	0.000
18	A	19	ALA	0	-0.010	-0.007	14.410	-0.070	-0.070	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.958	0.996	10.981	0.115	0.115	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.014	-0.010	9.254	-0.063	-0.063	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.960	0.970	10.000	0.182	0.182	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.940	-0.969	11.822	-0.306	-0.306	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.053	-0.040	6.017	0.026	0.026	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.000	0.002	6.933	-0.313	-0.313	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.055	-0.014	8.956	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.078	-0.039	6.757	0.263	0.263	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.900	-0.950	3.437	-5.406	-4.330	0.028	-0.521	-0.584	-0.004
28	A	29	PRO	0	-0.013	-0.003	6.629	-0.298	-0.298	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.955	-0.974	4.874	-1.145	-1.145	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.058	-0.011	3.396	-0.792	-0.542	0.014	-0.074	-0.189	0.000
31	A	32	ARG	1	0.849	0.922	4.182	2.327	2.774	-0.001	-0.169	-0.277	0.000
32	A	33	PHE	0	0.003	-0.004	6.037	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.012	0.012	8.754	0.066	0.066	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.029	-0.007	11.124	0.092	0.092	0.000	0.000	0.000	0.000
35	A	36	LEU	0	0.034	0.017	14.166	0.013	0.013	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.009	-0.023	16.087	0.004	0.004	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.069	-0.026	19.000	0.004	0.004	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.036	-0.026	21.846	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.010	0.007	24.426	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.063	-0.018	26.839	0.010	0.010	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.038	0.016	30.051	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.026	0.014	31.607	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.021	-0.017	34.461	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	TRP	0	-0.001	-0.007	37.813	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.055	-0.015	40.517	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.011	0.005	37.064	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.922	-0.978	35.193	0.037	0.037	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.759	-0.871	30.284	0.037	0.037	0.000	0.000	0.000	0.000
49	A	50	ASN	0	0.017	0.004	31.589	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.885	-0.950	31.715	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.028	-0.009	30.360	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.905	0.955	26.209	-0.019	-0.019	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.889	0.949	27.538	0.012	0.012	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.929	0.967	28.858	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.009	0.014	25.716	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.888	-0.968	24.063	-0.021	-0.021	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.952	-0.982	24.522	-0.048	-0.048	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.909	-0.946	25.245	-0.045	-0.045	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.017	0.013	20.679	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	61	ALA	0	-0.008	-0.001	20.999	-0.025	-0.025	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.051	-0.030	22.685	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.007	-0.006	20.127	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.881	0.929	16.430	0.244	0.244	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.975	0.989	19.041	0.082	0.082	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.050	-0.018	21.599	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.006	0.003	13.778	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.822	-0.915	17.123	-0.311	-0.311	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.056	-0.019	18.518	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.082	-0.044	18.450	0.016	0.016	0.000	0.000	0.000	0.000
70	A	71	GLY	0	-0.065	-0.029	18.031	-0.010	-0.010	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.070	-0.016	12.162	-0.057	-0.057	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.031	0.026	10.854	0.079	0.079	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.001	-0.017	11.916	-0.083	-0.083	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.863	-0.924	8.377	-0.688	-0.688	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.918	-0.980	12.133	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	ALA	0	-0.044	-0.017	14.130	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.865	0.944	13.448	-0.088	-0.088	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.008	0.005	18.069	0.002	0.002	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.035	0.015	20.561	0.013	0.013	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.761	-0.888	21.410	0.086	0.086	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.038	-0.019	23.099	0.002	0.002	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.077	-0.038	24.434	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.044	0.000	19.912	0.010	0.010	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.030	-0.021	19.477	0.026	0.026	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.012	0.011	20.335	0.027	0.027	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.018	0.017	19.553	0.012	0.012	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.032	-0.016	14.536	0.016	0.016	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.966	-0.980	16.076	0.282	0.282	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.910	-0.963	17.812	0.177	0.177	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.778	-0.853	13.329	0.198	0.198	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.076	-0.053	11.420	0.054	0.054	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.033	-0.010	14.140	0.029	0.029	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.019	0.003	16.457	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.084	-0.050	11.601	-0.077	-0.077	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.055	0.043	11.324	0.129	0.129	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.024	-0.024	8.589	-0.050	-0.050	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.053	-0.018	6.877	0.266	0.266	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.038	-0.062	5.517	0.007	0.007	0.000	0.000	0.000	0.000
99	A	100	GLN	0	0.041	0.011	2.339	-0.511	-0.493	4.550	-1.765	-2.802	-0.007
100	A	101	GLY	0	0.003	0.003	4.918	-0.722	-0.613	-0.001	-0.007	-0.100	0.000
101	A	102	ILE	0	0.016	0.021	7.108	-0.280	-0.280	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.019	-0.004	8.355	-0.055	-0.055	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.019	0.024	10.995	-0.055	-0.055	0.000	0.000	0.000	0.000
104	A	105	SER	0	0.014	0.016	14.750	-0.031	-0.031	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.001	0.014	16.881	0.012	0.012	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.008	-0.009	20.531	-0.017	-0.017	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.049	0.020	23.699	0.012	0.012	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.080	0.033	24.607	0.004	0.004	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.005	0.009	27.421	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.035	-0.025	28.193	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.046	-0.013	23.679	0.002	0.002	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.969	0.964	26.648	-0.044	-0.044	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.049	0.022	18.717	0.007	0.007	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.023	0.017	21.836	0.010	0.010	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.922	0.961	24.850	-0.037	-0.037	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.060	-0.024	25.870	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.827	-0.902	24.852	0.152	0.152	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.018	-0.016	19.382	0.015	0.015	0.000	0.000	0.000	0.000
119	A	120	HIS	0	-0.002	-0.012	18.801	0.031	0.031	0.000	0.000	0.000	0.000
120	A	121	THR	0	0.030	0.017	18.706	0.026	0.026	0.000	0.000	0.000	0.000
121	A	122	GLN	0	-0.036	-0.024	20.417	0.042	0.042	0.000	0.000	0.000	0.000
122	A	123	ALA	0	-0.022	-0.017	16.160	0.021	0.021	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.927	-0.963	16.192	0.365	0.365	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.889	0.957	17.240	-0.208	-0.208	0.000	0.000	0.000	0.000
125	A	126	PHE	0	-0.043	-0.028	15.016	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.018	0.024	14.658	0.021	0.021	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.050	-0.016	8.254	0.103	0.103	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.005	0.000	8.531	-0.230	-0.230	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.036	0.025	10.166	0.096	0.096	0.000	0.000	0.000	0.000
130	A	131	ILE	0	-0.025	-0.008	8.186	-0.098	-0.098	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.036	-0.038	12.028	-0.022	-0.022	0.000	0.000	0.000	0.000
132	A	133	VAL	0	-0.001	-0.003	13.821	-0.031	-0.031	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.031	-0.013	16.573	0.011	0.011	0.000	0.000	0.000	0.000
134	A	135	ALA	0	0.020	0.002	19.790	-0.015	-0.015	0.000	0.000	0.000	0.000

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