FMO DATABASE

FMODB ID: 49Z1N

Calculation Name: 1EP7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1EP7

Chain ID: A

ChEMBL ID:

UniProt ID: P80028

Base Structure: X-ray

Registration Date: 2023-09-20

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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-813551.461697
FMO2-HF: Nuclear repulsion	772447.914093
FMO2-HF: Total energy	-41103.547604
FMO2-MP2: Total energy	-41223.1326

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:1:GLY)

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

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.
-1.205	0.683	-0.009	-0.823	-1.055	-0.001

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : -0.006

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	3	SER	0	-0.004	0.004	3.457	-1.831	0.057	-0.009	-0.823	-1.055	-0.001
4	A	4	VAL	0	-0.030	-0.011	5.467	-0.064	-0.064	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.034	-0.011	5.914	1.031	1.031	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.032	-0.027	7.618	-0.436	-0.436	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.035	-0.005	9.774	-0.059	-0.059	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.867	-0.941	12.998	0.333	0.333	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.018	0.004	14.807	-0.070	-0.070	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.958	0.979	17.215	-0.123	-0.123	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.022	0.023	18.362	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.018	0.014	13.387	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.007	-0.016	15.127	0.036	0.036	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.840	-0.941	16.919	0.164	0.164	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.043	-0.015	15.106	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	16	GLN	0	0.011	-0.009	11.113	0.032	0.032	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.030	0.016	14.688	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.022	-0.004	18.020	-0.024	-0.024	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.940	0.982	9.469	-0.449	-0.449	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.018	0.009	16.225	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.943	0.975	17.291	-0.084	-0.084	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.967	-0.983	18.507	0.027	0.027	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.963	-1.001	13.910	0.012	0.012	0.000	0.000	0.000	0.000
24	A	24	HIS	0	-0.080	-0.024	18.377	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.876	0.956	13.486	0.033	0.033	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.038	-0.006	17.998	0.022	0.022	0.000	0.000	0.000	0.000
27	A	27	ILE	0	0.033	0.016	14.932	0.017	0.017	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.007	-0.005	15.173	-0.036	-0.036	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.042	-0.028	14.712	0.080	0.080	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.898	-0.948	14.768	0.315	0.315	0.000	0.000	0.000	0.000
31	A	31	PHE	0	-0.021	-0.010	16.291	0.047	0.047	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.061	-0.008	15.717	-0.042	-0.042	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.092	0.036	18.948	0.000	0.000	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.030	-0.010	17.883	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.055	-0.041	20.180	-0.013	-0.013	0.000	0.000	0.000	0.000
36	A	36	CYS	0	-0.002	0.038	19.396	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.019	0.002	22.130	0.011	0.011	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.028	-0.013	22.875	0.007	0.007	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.944	0.975	18.353	-0.172	-0.172	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.017	-0.014	18.600	0.001	0.001	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.024	0.006	18.411	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.036	0.021	14.261	0.009	0.009	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.040	0.018	13.587	0.038	0.038	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.017	-0.002	13.538	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.007	0.004	12.018	-0.030	-0.030	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.905	-0.953	9.126	0.572	0.572	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.025	0.026	9.801	-0.050	-0.050	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.032	-0.019	11.997	-0.058	-0.058	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.020	-0.044	8.515	0.032	0.032	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.002	-0.007	7.074	-0.160	-0.160	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.923	-0.964	9.462	-0.108	-0.108	0.000	0.000	0.000	0.000
52	A	53	TYR	0	-0.083	-0.050	12.455	-0.029	-0.029	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.090	0.059	8.979	0.030	0.030	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.061	-0.035	10.719	-0.042	-0.042	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.880	0.935	12.644	0.086	0.086	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.000	0.002	13.923	0.012	0.012	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.022	0.012	10.882	0.024	0.024	0.000	0.000	0.000	0.000
58	A	59	PHE	0	0.027	0.011	10.053	-0.048	-0.048	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.004	-0.002	9.941	0.265	0.265	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.985	0.995	11.145	-0.700	-0.700	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.008	-0.003	12.935	0.037	0.037	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.907	-0.948	15.753	0.262	0.262	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.021	-0.030	17.277	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.849	-0.904	20.892	0.157	0.157	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.067	-0.023	17.584	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.040	-0.018	16.939	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.086	0.038	20.229	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.001	-0.001	23.269	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.005	-0.002	19.219	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.018	-0.001	22.331	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.950	-0.979	23.487	0.103	0.103	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.026	-0.010	25.054	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.053	-0.020	23.051	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	GLY	0	-0.008	-0.001	25.190	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.045	-0.017	23.137	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.014	-0.010	26.556	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.010	0.014	27.798	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	79	MET	0	-0.026	0.020	22.031	0.018	0.018	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.021	-0.039	20.675	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	81	THR	0	0.003	-0.012	21.556	-0.027	-0.027	0.000	0.000	0.000	0.000
81	A	82	PHE	0	-0.018	-0.012	17.454	0.025	0.025	0.000	0.000	0.000	0.000
82	A	83	HIS	0	0.017	0.024	19.726	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.012	0.005	19.448	0.028	0.028	0.000	0.000	0.000	0.000
84	A	85	TYR	0	-0.043	-0.040	19.281	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.952	0.962	20.252	-0.076	-0.076	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.887	-0.938	22.455	0.063	0.063	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.015	-0.007	22.109	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.020	0.003	23.093	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.863	0.918	24.022	-0.121	-0.121	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.038	-0.025	24.316	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.832	-0.919	24.509	0.087	0.087	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.909	-0.938	23.998	0.136	0.136	0.000	0.000	0.000	0.000
93	A	94	LEU	0	0.012	0.022	22.623	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.025	0.021	24.044	0.016	0.016	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.014	0.011	25.132	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.002	-0.013	23.187	0.011	0.011	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.037	-0.007	24.155	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	GLN	0	0.069	0.007	20.995	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.933	-0.973	22.373	0.077	0.077	0.000	0.000	0.000	0.000
100	A	101	LYS	1	1.010	1.002	24.917	-0.083	-0.083	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.019	0.019	17.406	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.948	0.967	19.993	-0.073	-0.073	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.004	0.009	21.109	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.009	0.017	20.987	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	106	VAL	0	0.019	0.003	16.530	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.008	0.007	19.724	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.899	0.951	21.588	-0.079	-0.079	0.000	0.000	0.000	0.000
108	A	109	HIS	0	-0.091	-0.080	21.173	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	110	ALA	0	-0.027	0.010	19.028	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	111	ALA	0	-0.051	-0.012	20.396	-0.016	-0.016	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.010	0.001	23.905	0.004	0.004	0.000	0.000	0.000	0.000

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