FMO DATABASE

FMODB ID: Q1K2Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1674040.543098
FMO2-HF: Nuclear repulsion	1607094.435542
FMO2-HF: Total energy	-66946.107556
FMO2-MP2: Total energy	-67138.311248

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.
-3.881	-1.404	0.305	-1.502	-1.278	0.002

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 : 0.029 / q_NPA : 0.017

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	-0.002	-0.008	3.625	-2.350	-1.079	0.000	-0.924	-0.347	0.003
4	A	7	SER	0	0.036	0.027	6.344	0.915	0.915	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.820	0.909	8.148	1.650	1.650	0.000	0.000	0.000	0.000
6	A	9	GLU	-1	-0.798	-0.870	10.780	-0.552	-0.552	0.000	0.000	0.000	0.000
7	A	10	TYR	0	0.000	-0.037	13.168	-0.012	-0.012	0.000	0.000	0.000	0.000
8	A	11	ARG	1	0.979	0.968	14.608	0.304	0.304	0.000	0.000	0.000	0.000
9	A	12	VAL	0	0.055	0.054	11.383	0.065	0.065	0.000	0.000	0.000	0.000
10	A	13	LEU	0	0.015	0.019	7.937	0.048	0.048	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.040	-0.021	11.062	0.088	0.088	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.048	0.034	14.058	0.076	0.076	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.018	-0.026	8.363	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.020	-0.005	10.057	0.137	0.137	0.000	0.000	0.000	0.000
15	A	18	GLN	0	-0.026	-0.023	12.215	0.088	0.088	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.990	1.010	13.624	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	20	GLN	0	-0.022	-0.018	9.243	-0.060	-0.060	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.044	-0.047	13.254	0.057	0.057	0.000	0.000	0.000	0.000
19	A	22	ASP	-1	-0.838	-0.920	15.580	0.010	0.010	0.000	0.000	0.000	0.000
20	A	23	LEU	0	-0.031	-0.007	15.220	0.013	0.013	0.000	0.000	0.000	0.000
21	A	24	MET	0	-0.095	-0.044	12.837	0.021	0.021	0.000	0.000	0.000	0.000
22	A	25	GLN	0	0.026	0.041	17.571	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	ASP	-1	-0.868	-0.907	20.759	0.152	0.152	0.000	0.000	0.000	0.000
24	A	27	THR	0	0.074	0.023	22.217	0.025	0.025	0.000	0.000	0.000	0.000
25	A	28	SER	0	-0.038	-0.019	24.485	0.016	0.016	0.000	0.000	0.000	0.000
26	A	29	ARG	1	0.835	0.902	15.019	-0.339	-0.339	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.027	-0.018	18.286	0.039	0.039	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.025	0.009	22.352	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.872	-0.943	25.595	0.150	0.150	0.000	0.000	0.000	0.000
30	A	33	PRO	0	-0.035	-0.008	23.628	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	34	TYR	0	-0.031	-0.014	25.562	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	35	ILE	0	-0.013	-0.021	27.265	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.849	0.907	27.464	-0.193	-0.193	0.000	0.000	0.000	0.000
34	A	37	ILE	0	-0.001	0.015	27.488	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	38	GLN	0	0.007	0.001	29.468	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	39	GLY	0	-0.024	-0.013	32.481	-0.011	-0.011	0.000	0.000	0.000	0.000
37	A	40	LEU	0	-0.058	-0.046	32.208	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	41	ASP	-1	-0.894	-0.943	34.160	0.115	0.115	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.029	0.021	35.798	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.023	-0.013	38.909	0.001	0.001	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.993	0.988	39.826	-0.065	-0.065	0.000	0.000	0.000	0.000
42	A	45	LEU	0	0.032	0.021	37.645	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.916	0.965	31.490	-0.116	-0.116	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.909	-0.942	35.325	0.069	0.069	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.045	-0.002	36.971	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	49	CYS	0	-0.072	-0.016	27.370	0.015	0.015	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.967	0.980	31.584	-0.078	-0.078	0.000	0.000	0.000	0.000
48	A	51	GLU	-1	-0.747	-0.846	28.259	0.079	0.079	0.000	0.000	0.000	0.000
49	A	52	ARG	1	0.960	0.977	29.936	-0.086	-0.086	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.008	-0.007	30.629	0.000	0.000	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.036	0.017	30.583	0.001	0.001	0.000	0.000	0.000	0.000
52	A	55	ALA	0	-0.062	-0.014	27.118	0.002	0.002	0.000	0.000	0.000	0.000
53	A	56	PHE	0	-0.003	-0.005	21.319	0.010	0.010	0.000	0.000	0.000	0.000
54	A	57	PRO	0	0.018	0.019	22.890	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	58	SER	0	0.086	0.057	25.496	0.004	0.004	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.785	-0.894	25.663	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.951	-0.970	26.716	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.021	0.001	26.207	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.063	-0.041	21.710	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	63	ARG	1	0.813	0.871	24.124	0.037	0.037	0.000	0.000	0.000	0.000
61	A	64	GLY	0	0.003	0.011	26.209	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.022	0.010	22.547	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.024	0.030	24.370	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	67	ARG	1	0.887	0.945	18.713	0.289	0.289	0.000	0.000	0.000	0.000
65	A	68	ARG	1	0.899	0.926	15.522	0.402	0.402	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.067	0.030	18.509	0.005	0.005	0.000	0.000	0.000	0.000
67	A	70	PHE	0	0.022	0.013	17.377	0.022	0.022	0.000	0.000	0.000	0.000
68	A	71	LEU	0	0.011	0.007	13.677	0.024	0.024	0.000	0.000	0.000	0.000
69	A	72	GLN	0	-0.020	-0.016	15.384	0.003	0.003	0.000	0.000	0.000	0.000
70	A	73	THR	0	0.024	0.015	17.195	0.042	0.042	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.006	0.009	14.429	0.040	0.040	0.000	0.000	0.000	0.000
72	A	75	ASN	0	0.043	0.004	11.725	0.128	0.128	0.000	0.000	0.000	0.000
73	A	76	ALA	0	0.002	0.008	14.415	0.069	0.069	0.000	0.000	0.000	0.000
74	A	77	THR	0	-0.015	-0.007	17.208	0.037	0.037	0.000	0.000	0.000	0.000
75	A	78	LEU	0	0.012	0.001	12.810	0.036	0.036	0.000	0.000	0.000	0.000
76	A	79	GLY	0	0.030	0.023	14.892	0.071	0.071	0.000	0.000	0.000	0.000
77	A	80	CYS	0	-0.017	0.005	15.744	0.036	0.036	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.015	-0.004	17.252	0.008	0.008	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.021	-0.007	11.934	0.031	0.031	0.000	0.000	0.000	0.000
80	A	83	HIS	0	-0.046	-0.036	16.504	0.018	0.018	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.930	0.971	19.360	-0.181	-0.181	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.013	0.000	17.383	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.000	0.017	18.583	0.003	0.003	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.803	-0.874	20.294	0.198	0.198	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.047	-0.045	23.515	-0.016	-0.016	0.000	0.000	0.000	0.000
86	A	89	GLU	-1	-0.936	-0.974	19.573	0.496	0.496	0.000	0.000	0.000	0.000
87	A	90	GLN	0	-0.064	-0.029	23.533	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	91	ARG	1	0.723	0.842	25.488	-0.221	-0.221	0.000	0.000	0.000	0.000
89	A	92	LEU	0	-0.023	0.007	24.512	-0.020	-0.020	0.000	0.000	0.000	0.000
90	A	93	PRO	0	-0.003	0.009	28.123	0.003	0.003	0.000	0.000	0.000	0.000
91	A	94	LYS	1	0.954	0.972	28.225	-0.234	-0.234	0.000	0.000	0.000	0.000
92	A	95	ALA	0	0.055	0.017	26.477	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	96	GLN	0	0.013	0.005	28.593	0.008	0.008	0.000	0.000	0.000	0.000
94	A	97	ASP	-1	-0.898	-0.954	31.723	0.171	0.171	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.057	-0.018	28.322	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.877	-0.926	32.951	0.143	0.143	0.000	0.000	0.000	0.000
97	A	100	ARG	1	0.941	0.972	35.594	-0.130	-0.130	0.000	0.000	0.000	0.000
98	A	101	SER	0	-0.067	-0.034	35.415	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	102	GLY	0	-0.014	0.000	37.252	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	103	LEU	0	-0.092	-0.041	31.993	0.001	0.001	0.000	0.000	0.000	0.000
101	A	104	ASN	0	0.065	0.021	30.077	0.008	0.008	0.000	0.000	0.000	0.000
102	A	105	ILE	0	0.067	0.026	26.072	0.011	0.011	0.000	0.000	0.000	0.000
103	A	106	GLU	-1	-0.863	-0.924	25.006	0.254	0.254	0.000	0.000	0.000	0.000
104	A	107	ASP	-1	-0.855	-0.928	24.612	0.227	0.227	0.000	0.000	0.000	0.000
105	A	108	LEU	0	-0.023	-0.024	23.800	0.018	0.018	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.865	-0.935	21.476	0.364	0.364	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.878	0.941	19.873	-0.188	-0.188	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.041	-0.018	19.349	0.044	0.044	0.000	0.000	0.000	0.000
109	A	112	GLN	0	0.019	0.018	18.377	0.035	0.035	0.000	0.000	0.000	0.000
110	A	113	MET	0	-0.012	0.003	13.822	0.121	0.121	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.038	-0.011	14.232	0.106	0.106	0.000	0.000	0.000	0.000
112	A	115	ARG	1	1.023	1.007	12.032	-0.863	-0.863	0.000	0.000	0.000	0.000
113	A	116	PRO	0	0.032	0.005	10.447	0.158	0.158	0.000	0.000	0.000	0.000
114	A	117	ASN	0	0.040	0.020	9.285	0.398	0.398	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.002	0.000	9.974	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.045	-0.023	7.421	-0.180	-0.180	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.034	0.023	5.384	0.253	0.253	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.001	0.003	5.975	-0.689	-0.689	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.881	0.924	8.079	-0.749	-0.749	0.000	0.000	0.000	0.000
120	A	123	ASN	0	0.019	0.015	3.075	-2.786	-1.533	0.306	-0.575	-0.983	-0.001
121	A	124	ASN	0	0.043	0.014	5.021	-1.588	-1.635	-0.001	-0.003	0.052	0.000
122	A	125	ILE	0	-0.023	-0.009	6.654	-0.048	-0.048	0.000	0.000	0.000	0.000
123	A	126	TYR	0	0.020	0.017	6.339	0.012	0.012	0.000	0.000	0.000	0.000
124	A	128	MET	0	0.030	0.003	8.390	0.193	0.193	0.000	0.000	0.000	0.000
125	A	129	ALA	0	-0.003	0.003	11.537	0.114	0.114	0.000	0.000	0.000	0.000
126	A	130	GLN	0	-0.058	-0.029	10.125	0.155	0.155	0.000	0.000	0.000	0.000
127	A	131	LEU	0	-0.048	-0.027	11.867	0.001	0.001	0.000	0.000	0.000	0.000
128	A	132	LEU	0	-0.088	-0.024	14.729	0.091	0.091	0.000	0.000	0.000	0.000
129	A	133	ASP	-1	-0.844	-0.909	17.524	-0.399	-0.399	0.000	0.000	0.000	0.000
130	A	134	ASN	0	0.026	0.022	19.581	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	156	ALA	0	-0.008	-0.002	35.918	0.000	0.000	0.000	0.000	0.000	0.000
132	A	157	SER	0	0.012	0.006	35.592	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	158	ASP	-1	-0.782	-0.892	37.002	0.105	0.105	0.000	0.000	0.000	0.000
134	A	159	ALA	0	-0.005	-0.031	35.414	0.005	0.005	0.000	0.000	0.000	0.000
135	A	160	PHE	0	0.026	0.023	35.258	0.008	0.008	0.000	0.000	0.000	0.000
136	A	161	GLN	0	0.041	0.010	36.178	0.006	0.006	0.000	0.000	0.000	0.000
137	A	162	ARG	1	0.921	0.940	31.860	-0.136	-0.136	0.000	0.000	0.000	0.000
138	A	163	LYS	1	0.960	1.008	31.439	-0.139	-0.139	0.000	0.000	0.000	0.000
139	A	164	LEU	0	0.066	0.025	31.496	0.006	0.006	0.000	0.000	0.000	0.000
140	A	165	GLU	-1	-0.905	-0.942	30.692	0.111	0.111	0.000	0.000	0.000	0.000
141	A	166	GLY	0	0.000	0.003	27.653	0.005	0.005	0.000	0.000	0.000	0.000
142	A	168	ARG	1	0.794	0.894	28.728	-0.102	-0.102	0.000	0.000	0.000	0.000
143	A	169	PHE	0	-0.030	-0.015	21.251	-0.007	-0.007	0.000	0.000	0.000	0.000
144	A	170	LEU	0	0.028	0.005	22.368	0.002	0.002	0.000	0.000	0.000	0.000
145	A	171	HIS	0	-0.015	-0.003	24.329	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	172	GLY	0	0.006	-0.004	26.204	-0.010	-0.010	0.000	0.000	0.000	0.000
147	A	173	TYR	0	-0.011	-0.002	15.783	0.000	0.000	0.000	0.000	0.000	0.000
148	A	174	HIS	0	0.044	0.010	20.745	0.001	0.001	0.000	0.000	0.000	0.000
149	A	175	ARG	1	0.802	0.875	22.707	-0.073	-0.073	0.000	0.000	0.000	0.000
150	A	176	PHE	0	0.000	-0.010	18.265	-0.020	-0.020	0.000	0.000	0.000	0.000
151	A	177	MET	0	-0.019	-0.026	15.353	-0.021	-0.021	0.000	0.000	0.000	0.000
152	A	178	HIS	0	0.012	0.005	19.868	-0.032	-0.032	0.000	0.000	0.000	0.000
153	A	179	SER	0	0.004	-0.008	22.572	-0.017	-0.017	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.044	-0.018	16.793	-0.026	-0.026	0.000	0.000	0.000	0.000
155	A	181	GLY	0	0.073	0.044	18.654	-0.031	-0.031	0.000	0.000	0.000	0.000
156	A	182	ARG	1	0.900	0.955	19.625	0.001	0.001	0.000	0.000	0.000	0.000
157	A	183	VAL	0	-0.025	0.003	20.756	-0.018	-0.018	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.038	0.007	14.215	-0.032	-0.032	0.000	0.000	0.000	0.000
159	A	185	SER	0	-0.075	-0.033	19.185	-0.028	-0.028	0.000	0.000	0.000	0.000
160	A	186	LYS	1	0.918	0.957	21.492	0.075	0.075	0.000	0.000	0.000	0.000
161	A	187	TRP	0	0.021	0.014	16.110	-0.031	-0.031	0.000	0.000	0.000	0.000

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