FMO DATABASE

FMODB ID: 49J7N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1139530.845117
FMO2-HF: Nuclear repulsion	1089633.395968
FMO2-HF: Total energy	-49897.449149
FMO2-MP2: Total energy	-50048.050331

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.
-12.694	-4.016	6.442	-6.596	-8.528	-0.029

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 : 0.036 / q_NPA : 0.014

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	-0.067	-0.049	2.477	1.236	3.011	4.084	-2.172	-3.688	-0.006
4	A	5	LEU	0	0.012	0.011	5.536	-0.327	-0.327	0.000	0.000	0.000	0.000
5	A	6	VAL	0	-0.007	-0.003	9.266	0.000	0.000	0.000	0.000	0.000	0.000
6	A	7	VAL	0	0.006	0.010	11.264	0.027	0.027	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.004	-0.014	14.726	-0.015	-0.015	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.022	-0.016	17.483	0.012	0.012	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.904	0.960	20.879	0.016	0.016	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.017	-0.021	19.107	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.018	0.038	17.903	-0.023	-0.023	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.964	0.980	18.701	0.073	0.073	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.049	-0.032	19.028	0.002	0.002	0.000	0.000	0.000	0.000
14	A	15	PRO	0	0.077	0.035	18.785	-0.028	-0.028	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.854	-0.934	18.363	-0.201	-0.201	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.033	-0.006	12.833	-0.020	-0.020	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.028	0.011	13.814	-0.073	-0.073	0.000	0.000	0.000	0.000
18	A	19	ALA	0	-0.022	-0.008	14.518	-0.065	-0.065	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.886	0.929	10.797	0.301	0.301	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.006	-0.014	8.960	-0.103	-0.103	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.870	0.934	9.818	0.234	0.234	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.869	-0.918	11.746	-0.429	-0.429	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.014	-0.005	5.482	0.036	0.036	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.010	-0.004	7.522	-0.172	-0.172	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.059	-0.020	8.734	0.070	0.070	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.099	-0.048	6.804	0.319	0.319	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.828	-0.905	2.718	-10.039	-6.528	0.828	-2.245	-2.094	-0.023
28	A	29	PRO	0	0.007	0.011	5.772	-0.336	-0.336	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.944	-0.973	4.827	-0.997	-0.997	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.049	-0.004	2.875	-0.843	-0.503	0.117	-0.162	-0.296	0.001
31	A	32	ARG	1	0.835	0.909	3.908	2.138	2.600	0.001	-0.155	-0.309	0.000
32	A	33	PHE	0	0.013	-0.001	5.765	-0.102	-0.187	-0.001	-0.010	0.096	0.000
33	A	34	VAL	0	0.021	0.015	8.433	0.103	0.103	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.036	-0.015	11.062	0.053	0.053	0.000	0.000	0.000	0.000
35	A	36	LEU	0	0.039	0.022	13.941	0.020	0.020	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.036	-0.030	15.737	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.051	-0.027	18.499	0.006	0.006	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.044	-0.023	21.616	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.020	0.019	24.393	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.052	-0.018	26.548	0.008	0.008	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.043	0.016	29.549	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.018	0.005	31.204	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.021	0.003	34.371	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	TRP	0	-0.011	-0.020	37.670	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.059	-0.015	39.846	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	TYR	0	-0.018	-0.029	36.798	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.950	-0.970	35.328	0.038	0.038	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.718	-0.840	30.725	0.044	0.044	0.000	0.000	0.000	0.000
49	A	50	ASN	0	-0.038	-0.020	32.186	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.791	-0.859	32.175	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.014	-0.015	30.448	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.812	0.887	26.913	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.807	0.872	27.590	0.011	0.011	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.884	0.936	28.668	0.000	0.000	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.026	0.018	25.165	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.845	-0.916	24.069	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.867	-0.920	24.392	-0.044	-0.044	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.877	-0.930	24.699	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.000	0.003	20.268	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.007	0.000	20.398	-0.027	-0.027	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.073	-0.045	22.330	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.003	-0.006	19.590	-0.017	-0.017	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.835	0.906	15.720	0.252	0.252	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.966	0.990	18.675	0.079	0.079	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.045	-0.020	21.286	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.016	0.010	13.425	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.830	-0.910	16.084	-0.331	-0.331	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.020	-0.008	17.925	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.074	-0.033	17.999	0.012	0.012	0.000	0.000	0.000	0.000
70	A	71	GLY	0	-0.036	-0.009	17.835	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.039	-0.020	12.241	-0.054	-0.054	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.037	0.027	10.093	0.088	0.088	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.007	-0.013	11.130	-0.114	-0.114	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.794	-0.859	8.433	-0.439	-0.439	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.880	-0.957	12.106	0.114	0.114	0.000	0.000	0.000	0.000
76	A	77	ALA	0	-0.024	-0.023	14.007	-0.036	-0.036	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.820	0.922	14.274	-0.171	-0.171	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.015	0.010	18.357	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.045	0.021	20.446	0.019	0.019	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.759	-0.883	21.399	0.067	0.067	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.049	-0.024	22.763	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.063	-0.035	24.121	-0.009	-0.009	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.029	-0.007	18.986	0.012	0.012	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.007	-0.006	18.899	0.024	0.024	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.012	0.017	20.029	0.027	0.027	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.038	0.023	19.185	0.019	0.019	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.012	-0.009	14.248	0.017	0.017	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.859	-0.903	16.381	0.285	0.285	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.932	-0.972	18.728	0.171	0.171	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.773	-0.852	13.551	0.288	0.288	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.038	-0.034	11.653	0.067	0.067	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.038	-0.008	14.684	0.035	0.035	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.024	-0.008	17.070	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.055	-0.031	12.168	-0.066	-0.066	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.037	0.030	11.672	0.150	0.150	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.012	-0.013	9.072	-0.041	-0.041	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.062	-0.025	7.221	0.378	0.378	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.015	-0.057	5.997	-0.286	-0.286	0.000	0.000	0.000	0.000
99	A	100	GLN	0	0.015	0.001	2.662	-2.740	-0.169	1.414	-1.847	-2.139	-0.001
100	A	101	GLY	0	0.010	0.009	5.113	-1.033	-0.929	-0.001	-0.005	-0.098	0.000
101	A	102	ILE	0	-0.006	0.011	6.662	-0.169	-0.169	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.002	-0.008	7.947	-0.100	-0.100	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.016	0.035	10.679	-0.035	-0.035	0.000	0.000	0.000	0.000
104	A	105	SER	0	0.053	0.017	14.461	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.006	0.018	16.692	0.019	0.019	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.007	-0.015	20.345	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.059	0.025	23.626	0.009	0.009	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.072	0.025	24.633	0.008	0.008	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.008	0.010	27.351	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.024	-0.008	27.987	0.001	0.001	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.010	-0.007	23.305	0.007	0.007	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.931	0.958	26.186	-0.021	-0.021	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.054	0.021	18.487	0.008	0.008	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.025	0.022	21.647	0.010	0.010	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.832	0.910	24.540	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.036	-0.013	25.352	0.000	0.000	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.815	-0.885	24.244	0.109	0.109	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.006	0.010	18.811	0.012	0.012	0.000	0.000	0.000	0.000
119	A	120	HIS	0	-0.010	-0.013	18.292	0.019	0.019	0.000	0.000	0.000	0.000
120	A	121	THR	0	-0.009	-0.009	18.285	0.012	0.012	0.000	0.000	0.000	0.000
121	A	122	GLN	0	-0.032	-0.035	19.480	0.042	0.042	0.000	0.000	0.000	0.000
122	A	123	ALA	0	0.000	-0.008	15.353	0.022	0.022	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.920	-0.962	15.578	0.277	0.277	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.773	0.881	16.657	-0.175	-0.175	0.000	0.000	0.000	0.000
125	A	126	PHE	0	-0.036	-0.022	14.683	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	127	GLY	0	-0.018	0.002	14.888	0.065	0.065	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.032	-0.011	8.418	0.089	0.089	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.007	0.002	7.959	-0.208	-0.208	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.015	0.012	9.596	0.073	0.073	0.000	0.000	0.000	0.000
130	A	131	ILE	0	-0.014	-0.004	7.464	-0.083	-0.083	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.022	-0.030	11.521	-0.027	-0.027	0.000	0.000	0.000	0.000
132	A	133	VAL	0	-0.001	-0.001	13.556	-0.037	-0.037	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.038	-0.016	16.350	0.026	0.026	0.000	0.000	0.000	0.000
134	A	135	ALA	0	0.011	0.000	19.197	-0.010	-0.010	0.000	0.000	0.000	0.000

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