FMO DATABASE

FMODB ID: 43Q1N

Calculation Name: 1EVS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1EVS

Chain ID: A

ChEMBL ID:

UniProt ID: P13725

Base Structure: X-ray

Registration Date: 2023-03-13

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	161
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1677769.589268
FMO2-HF: Nuclear repulsion	1610821.671311
FMO2-HF: Total energy	-66947.917957
FMO2-MP2: Total energy	-67139.910964

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:4:GLY)

Summations of interaction energy for fragment #1(A:4: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.
-10.164	-9.98	6.581	-3.337	-3.428	0.013

Interaction energy analysis for fragmet #1(A:4:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.047 / q_NPA : 0.025

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	6	CYS	0	-0.010	-0.009	3.864	-0.708	0.569	-0.006	-0.680	-0.590	0.003
4	A	7	SER	0	0.036	0.017	5.905	1.042	1.042	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.775	0.878	8.364	1.369	1.369	0.000	0.000	0.000	0.000
6	A	9	GLU	-1	-0.839	-0.899	10.678	-0.457	-0.457	0.000	0.000	0.000	0.000
7	A	10	TYR	0	0.005	-0.018	12.968	-0.006	-0.006	0.000	0.000	0.000	0.000
8	A	11	ARG	1	0.972	0.963	14.387	0.253	0.253	0.000	0.000	0.000	0.000
9	A	12	VAL	0	0.053	0.048	11.125	0.065	0.065	0.000	0.000	0.000	0.000
10	A	13	LEU	0	0.038	0.026	7.201	0.058	0.058	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.050	-0.021	10.628	0.121	0.121	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.044	0.026	13.554	0.087	0.087	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.010	-0.013	7.509	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	17	LEU	0	0.003	0.000	9.477	0.170	0.170	0.000	0.000	0.000	0.000
15	A	18	GLN	0	-0.034	-0.020	11.727	0.088	0.088	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.935	0.973	13.631	-0.086	-0.086	0.000	0.000	0.000	0.000
17	A	20	GLN	0	0.011	0.017	7.973	-0.147	-0.147	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.013	-0.044	12.936	0.043	0.043	0.000	0.000	0.000	0.000
19	A	22	ASP	-1	-0.786	-0.882	15.069	0.092	0.092	0.000	0.000	0.000	0.000
20	A	23	LEU	0	-0.028	0.003	15.014	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	24	MET	0	-0.030	-0.020	12.572	0.062	0.062	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.026	0.008	17.462	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	26	ASP	-1	-0.854	-0.898	20.510	0.226	0.226	0.000	0.000	0.000	0.000
24	A	27	THR	0	0.012	-0.013	21.912	0.029	0.029	0.000	0.000	0.000	0.000
25	A	28	SER	0	-0.040	-0.036	24.004	0.017	0.017	0.000	0.000	0.000	0.000
26	A	29	ARG	1	0.830	0.903	14.995	-0.470	-0.470	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.012	-0.017	17.704	0.041	0.041	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.028	0.010	22.226	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.779	-0.879	25.477	0.178	0.178	0.000	0.000	0.000	0.000
30	A	33	PRO	0	-0.015	0.011	23.776	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	34	TYR	0	-0.042	-0.034	25.216	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	35	ILE	0	-0.009	-0.019	26.974	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.789	0.875	28.398	-0.219	-0.219	0.000	0.000	0.000	0.000
34	A	37	ILE	0	0.005	0.013	26.981	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	38	GLN	0	0.038	0.007	28.670	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	39	GLY	0	-0.004	0.016	31.823	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	40	LEU	0	-0.038	-0.034	31.761	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	41	ASP	-1	-0.813	-0.886	33.010	0.157	0.157	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.030	0.007	35.297	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.027	0.000	38.316	0.002	0.002	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.980	0.977	39.313	-0.080	-0.080	0.000	0.000	0.000	0.000
42	A	45	LEU	0	0.007	0.016	37.016	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.792	0.867	31.438	-0.154	-0.154	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.876	-0.921	34.621	0.098	0.098	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.065	-0.038	36.123	0.004	0.004	0.000	0.000	0.000	0.000
46	A	49	CYS	0	-0.067	-0.021	26.763	0.023	0.023	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.929	0.964	30.829	-0.116	-0.116	0.000	0.000	0.000	0.000
48	A	51	GLU	-1	-0.759	-0.858	27.383	0.150	0.150	0.000	0.000	0.000	0.000
49	A	52	ARG	1	0.845	0.902	29.318	-0.150	-0.150	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.011	0.000	29.889	0.004	0.004	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.028	0.017	30.140	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	ALA	0	-0.063	-0.021	26.774	0.003	0.003	0.000	0.000	0.000	0.000
53	A	56	PHE	0	-0.012	-0.001	20.963	0.023	0.023	0.000	0.000	0.000	0.000
54	A	57	PRO	0	0.019	0.019	22.317	-0.015	-0.015	0.000	0.000	0.000	0.000
55	A	58	SER	0	0.092	0.063	25.071	0.008	0.008	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.737	-0.874	24.660	0.056	0.056	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.951	-0.966	26.010	0.022	0.022	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.009	-0.010	25.184	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.057	-0.038	20.829	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	63	ARG	1	0.750	0.853	22.959	-0.032	-0.032	0.000	0.000	0.000	0.000
61	A	64	GLY	0	0.030	0.023	25.487	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.033	-0.012	21.672	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.045	0.037	23.521	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	67	ARG	1	0.875	0.944	17.921	0.214	0.214	0.000	0.000	0.000	0.000
65	A	68	ARG	1	0.904	0.929	15.231	0.331	0.331	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.075	0.045	18.021	0.018	0.018	0.000	0.000	0.000	0.000
67	A	70	PHE	0	0.014	0.016	16.500	0.035	0.035	0.000	0.000	0.000	0.000
68	A	71	LEU	0	0.003	0.004	12.929	0.038	0.038	0.000	0.000	0.000	0.000
69	A	72	GLN	0	-0.003	-0.009	14.770	0.026	0.026	0.000	0.000	0.000	0.000
70	A	73	THR	0	0.020	0.001	16.844	0.053	0.053	0.000	0.000	0.000	0.000
71	A	74	LEU	0	0.003	0.027	13.924	0.047	0.047	0.000	0.000	0.000	0.000
72	A	75	ASN	0	0.033	0.004	11.654	0.202	0.202	0.000	0.000	0.000	0.000
73	A	76	ALA	0	0.005	0.015	13.848	0.095	0.095	0.000	0.000	0.000	0.000
74	A	77	THR	0	-0.027	-0.021	17.132	0.032	0.032	0.000	0.000	0.000	0.000
75	A	78	LEU	0	0.014	-0.007	12.133	0.034	0.034	0.000	0.000	0.000	0.000
76	A	79	GLY	0	0.024	0.017	14.717	0.090	0.090	0.000	0.000	0.000	0.000
77	A	80	CYS	0	-0.028	-0.006	15.534	0.014	0.014	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.009	-0.001	17.071	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.005	-0.007	11.888	0.018	0.018	0.000	0.000	0.000	0.000
80	A	83	HIS	0	-0.045	-0.023	16.446	0.002	0.002	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.943	0.970	19.306	-0.279	-0.279	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.003	0.003	16.909	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.031	0.022	18.514	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.825	-0.881	20.396	0.242	0.242	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.045	-0.027	23.599	-0.031	-0.031	0.000	0.000	0.000	0.000
86	A	89	GLU	-1	-0.884	-0.934	19.378	0.579	0.579	0.000	0.000	0.000	0.000
87	A	90	GLN	0	-0.061	-0.034	23.428	-0.021	-0.021	0.000	0.000	0.000	0.000
88	A	91	ARG	1	0.734	0.845	25.564	-0.280	-0.280	0.000	0.000	0.000	0.000
89	A	92	LEU	0	-0.009	0.007	23.917	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	93	PRO	0	-0.023	-0.012	27.641	0.001	0.001	0.000	0.000	0.000	0.000
91	A	94	LYS	1	0.905	0.954	27.728	-0.228	-0.228	0.000	0.000	0.000	0.000
92	A	95	ALA	0	0.068	0.016	26.012	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	96	GLN	0	-0.038	-0.002	28.136	0.002	0.002	0.000	0.000	0.000	0.000
94	A	97	ASP	-1	-0.808	-0.917	31.295	0.188	0.188	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.049	-0.002	28.058	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.893	-0.936	32.754	0.145	0.145	0.000	0.000	0.000	0.000
97	A	100	ARG	1	0.944	0.965	35.519	-0.137	-0.137	0.000	0.000	0.000	0.000
98	A	101	SER	0	-0.060	-0.038	34.814	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	102	GLY	0	-0.016	0.005	36.963	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	103	LEU	0	-0.084	-0.038	31.710	0.002	0.002	0.000	0.000	0.000	0.000
101	A	104	ASN	0	-0.009	-0.028	28.471	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	105	ILE	0	0.047	0.013	25.879	0.014	0.014	0.000	0.000	0.000	0.000
103	A	106	GLU	-1	-0.757	-0.857	24.803	0.278	0.278	0.000	0.000	0.000	0.000
104	A	107	ASP	-1	-0.786	-0.872	24.334	0.258	0.258	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.002	-0.002	23.544	0.023	0.023	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.899	-0.957	21.083	0.393	0.393	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.767	0.880	19.482	-0.204	-0.204	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.030	-0.009	19.051	0.056	0.056	0.000	0.000	0.000	0.000
109	A	112	GLN	0	-0.026	-0.019	18.366	0.034	0.034	0.000	0.000	0.000	0.000
110	A	113	MET	0	0.000	0.005	13.421	0.169	0.169	0.000	0.000	0.000	0.000
111	A	114	ALA	0	0.000	0.012	14.128	0.143	0.143	0.000	0.000	0.000	0.000
112	A	115	ARG	1	0.985	0.990	13.016	-0.851	-0.851	0.000	0.000	0.000	0.000
113	A	116	PRO	0	0.048	0.012	9.941	0.253	0.253	0.000	0.000	0.000	0.000
114	A	117	ASN	0	-0.017	-0.007	9.154	0.322	0.322	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.017	0.005	10.026	0.045	0.045	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.020	-0.008	7.760	-0.107	-0.107	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.031	0.019	5.027	0.633	0.633	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.008	0.001	5.484	-0.594	-0.594	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.887	0.934	8.001	-1.201	-1.201	0.000	0.000	0.000	0.000
120	A	123	ASN	0	0.002	0.005	2.129	-9.912	-11.001	6.588	-2.652	-2.848	0.010
121	A	124	ASN	0	0.015	-0.001	4.674	-2.028	-2.032	-0.001	-0.005	0.010	0.000
122	A	125	ILE	0	0.006	-0.003	6.007	-0.226	-0.226	0.000	0.000	0.000	0.000
123	A	126	TYR	0	0.012	0.009	6.146	-0.103	-0.103	0.000	0.000	0.000	0.000
124	A	128	MET	0	0.033	0.027	7.538	0.112	0.112	0.000	0.000	0.000	0.000
125	A	129	ALA	0	0.008	0.001	10.778	0.087	0.087	0.000	0.000	0.000	0.000
126	A	130	GLN	0	-0.044	-0.014	10.069	0.186	0.186	0.000	0.000	0.000	0.000
127	A	131	LEU	0	-0.046	-0.026	12.175	-0.087	-0.087	0.000	0.000	0.000	0.000
128	A	132	LEU	0	-0.032	-0.007	14.109	0.076	0.076	0.000	0.000	0.000	0.000
129	A	133	ASP	-1	-0.844	-0.920	17.258	-0.356	-0.356	0.000	0.000	0.000	0.000
130	A	134	ASN	0	-0.009	0.015	19.514	0.025	0.025	0.000	0.000	0.000	0.000
131	A	156	ALA	0	0.050	0.016	35.760	0.003	0.003	0.000	0.000	0.000	0.000
132	A	157	SER	0	-0.031	-0.021	35.876	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	158	ASP	-1	-0.782	-0.869	37.219	0.136	0.136	0.000	0.000	0.000	0.000
134	A	159	ALA	0	0.005	-0.019	35.413	0.007	0.007	0.000	0.000	0.000	0.000
135	A	160	PHE	0	0.033	0.026	34.971	0.011	0.011	0.000	0.000	0.000	0.000
136	A	161	GLN	0	0.084	0.028	35.732	0.009	0.009	0.000	0.000	0.000	0.000
137	A	162	ARG	1	0.894	0.930	32.255	-0.164	-0.164	0.000	0.000	0.000	0.000
138	A	163	LYS	1	0.885	0.960	31.284	-0.168	-0.168	0.000	0.000	0.000	0.000
139	A	164	LEU	0	0.075	0.038	31.094	0.011	0.011	0.000	0.000	0.000	0.000
140	A	165	GLU	-1	-0.816	-0.866	30.825	0.157	0.157	0.000	0.000	0.000	0.000
141	A	166	GLY	0	0.020	0.005	27.303	0.008	0.008	0.000	0.000	0.000	0.000
142	A	168	ARG	1	0.795	0.887	28.054	-0.138	-0.138	0.000	0.000	0.000	0.000
143	A	169	PHE	0	-0.046	-0.026	20.767	-0.004	-0.004	0.000	0.000	0.000	0.000
144	A	170	LEU	0	0.027	0.007	21.990	0.010	0.010	0.000	0.000	0.000	0.000
145	A	171	HIS	0	0.014	0.014	23.942	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	172	GLY	0	0.013	-0.005	25.755	-0.009	-0.009	0.000	0.000	0.000	0.000
147	A	173	TYR	0	0.003	0.005	15.495	0.003	0.003	0.000	0.000	0.000	0.000
148	A	174	HIS	0	0.012	0.000	20.756	0.003	0.003	0.000	0.000	0.000	0.000
149	A	175	ARG	1	0.799	0.878	22.425	-0.146	-0.146	0.000	0.000	0.000	0.000
150	A	176	PHE	0	0.007	-0.014	17.533	-0.018	-0.018	0.000	0.000	0.000	0.000
151	A	177	MET	0	-0.016	-0.016	15.065	-0.005	-0.005	0.000	0.000	0.000	0.000
152	A	178	HIS	0	0.007	-0.005	19.431	-0.031	-0.031	0.000	0.000	0.000	0.000
153	A	179	SER	0	-0.027	-0.029	21.966	-0.019	-0.019	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.030	-0.008	15.909	-0.027	-0.027	0.000	0.000	0.000	0.000
155	A	181	GLY	0	0.058	0.047	18.336	-0.033	-0.033	0.000	0.000	0.000	0.000
156	A	182	ARG	1	0.859	0.924	19.257	-0.087	-0.087	0.000	0.000	0.000	0.000
157	A	183	VAL	0	-0.015	0.019	20.012	-0.020	-0.020	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.053	0.010	13.318	-0.033	-0.033	0.000	0.000	0.000	0.000
159	A	185	SER	0	-0.055	-0.039	18.320	-0.039	-0.039	0.000	0.000	0.000	0.000
160	A	186	LYS	1	0.930	0.968	20.874	0.023	0.023	0.000	0.000	0.000	0.000
161	A	187	TRP	0	0.017	0.014	15.325	-0.036	-0.036	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:GLY)