FMO DATABASE

FMODB ID: K9GN3

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:

Apendix: None

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1136843.589963
FMO2-HF: Nuclear repulsion	1086946.469716
FMO2-HF: Total energy	-49897.120247
FMO2-MP2: Total energy	-50047.769709

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.
-7.997	-1.562	3.513	-4.228	-5.72	-0.017

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 : 0.008 / q_NPA : -0.002

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	0.011	-0.004	2.703	2.340	4.895	0.499	-1.230	-1.823	-0.001
4	A	5	LEU	0	0.001	0.015	6.125	-0.403	-0.403	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.000	-0.006	9.669	0.043	0.043	0.000	0.000	0.000	0.000
6	A	7	VAL	0	0.022	0.016	11.709	-0.027	-0.027	0.000	0.000	0.000	0.000
7	A	8	ALA	0	-0.004	-0.021	15.175	-0.013	-0.013	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.019	-0.012	17.855	0.005	0.005	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.935	0.960	21.211	-0.019	-0.019	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.024	-0.014	18.957	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.046	0.052	18.533	-0.017	-0.017	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.972	0.980	19.226	0.044	0.044	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.060	-0.037	19.517	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	15	PRO	0	0.088	0.037	19.254	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.860	-0.935	18.730	-0.132	-0.132	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.040	-0.008	13.647	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.037	0.010	14.207	-0.052	-0.052	0.000	0.000	0.000	0.000
18	A	19	ALA	0	-0.010	-0.004	14.416	-0.070	-0.070	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.893	0.944	11.052	0.142	0.142	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.006	-0.010	9.340	-0.067	-0.067	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.894	0.940	10.002	0.181	0.181	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.882	-0.923	11.818	-0.309	-0.309	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.045	-0.036	5.896	0.018	0.018	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.002	0.003	6.923	-0.335	-0.335	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.055	-0.016	8.948	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.083	-0.038	6.370	0.312	0.312	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.922	-0.964	3.234	-7.603	-5.812	0.103	-0.987	-0.907	-0.008
28	A	29	PRO	0	0.009	0.005	6.578	-0.304	-0.304	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.946	-0.969	4.973	-1.131	-1.131	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.053	-0.005	3.354	-0.701	-0.455	0.014	-0.076	-0.185	0.000
31	A	32	ARG	1	0.848	0.915	4.159	2.267	2.714	-0.001	-0.164	-0.283	0.000
32	A	33	PHE	0	0.014	0.003	6.037	0.033	0.033	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.015	0.016	8.774	0.067	0.067	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.036	-0.011	11.124	0.091	0.091	0.000	0.000	0.000	0.000
35	A	36	LEU	0	0.040	0.018	14.191	0.012	0.012	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.018	-0.025	16.114	0.001	0.001	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.059	-0.019	19.065	0.003	0.003	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.047	-0.033	21.873	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.008	0.007	24.710	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.064	-0.020	26.954	0.010	0.010	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.037	0.017	30.078	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.023	0.012	31.573	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.017	-0.013	34.517	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	TRP	0	-0.005	-0.009	37.855	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.052	-0.014	40.625	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.006	0.002	37.362	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.924	-0.977	35.358	0.042	0.042	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.734	-0.871	30.666	0.044	0.044	0.000	0.000	0.000	0.000
49	A	50	ASN	0	-0.001	0.007	31.998	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.830	-0.897	32.113	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.032	-0.014	30.675	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	53	ARG	1	0.859	0.918	26.583	-0.027	-0.027	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.786	0.868	27.913	0.007	0.007	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.917	0.961	29.121	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.008	0.011	25.902	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.862	-0.943	24.319	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.871	-0.929	24.650	-0.038	-0.038	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.906	-0.941	25.280	-0.036	-0.036	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.015	0.011	20.687	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.001	0.001	21.021	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.057	-0.037	22.687	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.007	-0.005	20.177	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.842	0.908	16.156	0.245	0.245	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.972	0.992	19.057	0.072	0.072	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.052	-0.019	21.620	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.021	0.009	13.854	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.800	-0.899	16.896	-0.311	-0.311	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.052	-0.014	18.530	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.075	-0.039	18.309	0.012	0.012	0.000	0.000	0.000	0.000
70	A	71	GLY	0	-0.039	-0.021	18.036	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	72	ILE	0	-0.061	-0.012	12.259	-0.055	-0.055	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.040	0.031	10.774	0.080	0.080	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.004	-0.019	11.883	-0.078	-0.078	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.804	-0.865	8.305	-0.596	-0.596	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.899	-0.969	12.304	0.037	0.037	0.000	0.000	0.000	0.000
76	A	77	ALA	0	-0.037	-0.018	14.199	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.827	0.923	14.064	-0.137	-0.137	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.003	0.002	18.390	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.038	0.015	20.612	0.013	0.013	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.751	-0.881	21.512	0.091	0.091	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.036	-0.021	23.127	0.002	0.002	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.077	-0.041	24.606	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.023	0.001	19.758	0.011	0.011	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.007	-0.012	19.504	0.026	0.026	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.013	0.008	20.357	0.027	0.027	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.021	0.016	19.532	0.013	0.013	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.024	-0.010	14.625	0.018	0.018	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.881	-0.931	16.069	0.299	0.299	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.909	-0.963	17.796	0.183	0.183	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.782	-0.855	13.226	0.239	0.239	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.058	-0.043	11.444	0.053	0.053	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.038	-0.013	14.111	0.027	0.027	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.023	0.001	16.556	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.054	-0.031	11.840	-0.075	-0.075	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.048	0.036	11.249	0.132	0.132	0.000	0.000	0.000	0.000
96	A	97	GLY	0	-0.023	-0.020	8.562	-0.050	-0.050	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.045	-0.016	6.800	0.264	0.264	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.031	-0.059	5.648	0.025	0.025	0.000	0.000	0.000	0.000
99	A	100	GLN	0	0.034	0.011	2.435	-1.767	-0.477	2.899	-1.765	-2.424	-0.008
100	A	101	GLY	0	0.011	0.009	5.014	-0.708	-0.602	-0.001	-0.006	-0.098	0.000
101	A	102	ILE	0	0.008	0.016	7.131	-0.271	-0.271	0.000	0.000	0.000	0.000
102	A	103	VAL	0	-0.015	-0.003	8.326	-0.062	-0.062	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.021	0.027	11.017	-0.056	-0.056	0.000	0.000	0.000	0.000
104	A	105	SER	0	0.013	0.014	14.772	-0.032	-0.032	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.004	-0.001	16.901	0.011	0.011	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.007	-0.004	20.551	-0.017	-0.017	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.051	0.028	23.718	0.011	0.011	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.089	0.031	24.693	0.004	0.004	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.007	0.006	27.438	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.039	-0.028	28.287	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.047	-0.017	23.644	0.002	0.002	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.970	0.968	26.670	-0.048	-0.048	0.000	0.000	0.000	0.000
113	A	114	TRP	0	0.046	0.015	18.967	0.007	0.007	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.029	0.027	21.780	0.009	0.009	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.910	0.954	24.871	-0.039	-0.039	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.056	-0.021	25.866	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.822	-0.877	24.810	0.158	0.158	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.003	-0.010	19.433	0.015	0.015	0.000	0.000	0.000	0.000
119	A	120	HIS	0	0.007	-0.008	18.820	0.029	0.029	0.000	0.000	0.000	0.000
120	A	121	THR	0	-0.003	-0.016	18.725	0.028	0.028	0.000	0.000	0.000	0.000
121	A	122	GLN	0	-0.036	-0.030	20.437	0.039	0.039	0.000	0.000	0.000	0.000
122	A	123	ALA	0	-0.016	-0.016	16.179	0.021	0.021	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.932	-0.964	16.211	0.377	0.377	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.813	0.912	17.240	-0.216	-0.216	0.000	0.000	0.000	0.000
125	A	126	PHE	0	-0.066	-0.040	15.144	-0.010	-0.010	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.017	0.023	14.764	0.020	0.020	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.050	-0.015	8.422	0.098	0.098	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.011	0.001	8.345	-0.224	-0.224	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.027	0.019	10.186	0.103	0.103	0.000	0.000	0.000	0.000
130	A	131	ILE	0	-0.016	-0.002	8.092	-0.105	-0.105	0.000	0.000	0.000	0.000
131	A	132	HIS	0	-0.029	-0.029	12.043	-0.021	-0.021	0.000	0.000	0.000	0.000
132	A	133	VAL	0	-0.003	-0.004	13.801	-0.034	-0.034	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.030	-0.012	16.588	0.012	0.012	0.000	0.000	0.000	0.000
134	A	135	ALA	0	0.011	0.000	19.747	-0.016	-0.016	0.000	0.000	0.000	0.000

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