FMO DATABASE

FMODB ID: K3K43

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1673785.683429
FMO2-HF: Nuclear repulsion	1606838.261388
FMO2-HF: Total energy	-66947.422041
FMO2-MP2: Total energy	-67139.481384

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.
-6.675	-3.762	1.329	-2.297	-1.944	0.001

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 : 0.022 / q_NPA : 0.012

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	0.002	3.583	-2.575	-1.274	0.000	-0.935	-0.366	0.002
4	A	7	SER	0	0.029	0.026	6.308	0.928	0.928	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.803	0.894	8.467	1.407	1.407	0.000	0.000	0.000	0.000
6	A	9	GLU	-1	-0.805	-0.872	10.742	-0.542	-0.542	0.000	0.000	0.000	0.000
7	A	10	TYR	0	0.025	-0.031	13.140	-0.024	-0.024	0.000	0.000	0.000	0.000
8	A	11	ARG	1	0.979	0.970	14.591	0.293	0.293	0.000	0.000	0.000	0.000
9	A	12	VAL	0	0.053	0.044	11.050	0.063	0.063	0.000	0.000	0.000	0.000
10	A	13	LEU	0	0.024	0.024	7.802	0.063	0.063	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.047	-0.022	11.046	0.097	0.097	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.042	0.030	14.053	0.080	0.080	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.012	-0.025	7.817	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.004	0.006	10.016	0.146	0.146	0.000	0.000	0.000	0.000
15	A	18	GLN	0	-0.039	-0.030	12.227	0.088	0.088	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.992	1.007	13.640	-0.028	-0.028	0.000	0.000	0.000	0.000
17	A	20	GLN	0	-0.006	-0.007	8.580	-0.114	-0.114	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.027	-0.046	13.276	0.054	0.054	0.000	0.000	0.000	0.000
19	A	22	ASP	-1	-0.817	-0.894	15.608	0.024	0.024	0.000	0.000	0.000	0.000
20	A	23	LEU	0	0.003	0.015	15.362	0.010	0.010	0.000	0.000	0.000	0.000
21	A	24	MET	0	-0.090	-0.055	13.127	0.033	0.033	0.000	0.000	0.000	0.000
22	A	25	GLN	0	0.018	0.038	17.607	0.003	0.003	0.000	0.000	0.000	0.000
23	A	26	ASP	-1	-0.856	-0.905	20.795	0.176	0.176	0.000	0.000	0.000	0.000
24	A	27	THR	0	0.041	0.015	22.255	0.025	0.025	0.000	0.000	0.000	0.000
25	A	28	SER	0	-0.051	-0.033	24.324	0.016	0.016	0.000	0.000	0.000	0.000
26	A	29	ARG	1	0.856	0.914	15.385	-0.340	-0.340	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.020	-0.015	18.102	0.040	0.040	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.031	0.009	22.397	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.815	-0.911	25.641	0.152	0.152	0.000	0.000	0.000	0.000
30	A	33	PRO	0	-0.014	0.006	23.833	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	34	TYR	0	-0.037	-0.022	25.570	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	35	ILE	0	-0.005	-0.018	27.313	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.834	0.899	28.094	-0.198	-0.198	0.000	0.000	0.000	0.000
34	A	37	ILE	0	0.006	0.016	27.515	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	38	GLN	0	0.045	0.016	29.229	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	39	GLY	0	0.001	0.007	32.531	-0.011	-0.011	0.000	0.000	0.000	0.000
37	A	40	LEU	0	-0.052	-0.036	32.189	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	41	ASP	-1	-0.847	-0.897	33.403	0.129	0.129	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.045	0.023	35.843	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.018	-0.010	38.955	0.001	0.001	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.984	0.990	39.871	-0.068	-0.068	0.000	0.000	0.000	0.000
42	A	45	LEU	0	0.045	0.024	37.768	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.790	0.874	31.432	-0.131	-0.131	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.879	-0.922	35.371	0.074	0.074	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.098	-0.045	37.018	0.000	0.000	0.000	0.000	0.000	0.000
46	A	49	CYS	0	-0.098	-0.044	27.375	0.017	0.017	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.962	0.977	31.631	-0.085	-0.085	0.000	0.000	0.000	0.000
48	A	51	GLU	-1	-0.757	-0.858	27.936	0.095	0.095	0.000	0.000	0.000	0.000
49	A	52	ARG	1	0.873	0.924	29.941	-0.106	-0.106	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.021	0.002	30.631	0.001	0.001	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.028	0.016	30.584	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	ALA	0	-0.067	-0.017	27.208	0.002	0.002	0.000	0.000	0.000	0.000
53	A	56	PHE	0	-0.015	-0.009	21.523	0.011	0.011	0.000	0.000	0.000	0.000
54	A	57	PRO	0	0.012	0.016	22.795	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	58	SER	0	0.086	0.056	25.536	0.005	0.005	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.750	-0.891	25.521	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.962	-0.972	26.746	-0.019	-0.019	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.028	0.004	26.471	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.042	-0.034	21.752	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	63	ARG	1	0.785	0.873	24.150	0.021	0.021	0.000	0.000	0.000	0.000
61	A	64	GLY	0	0.003	0.006	26.233	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.026	0.011	22.318	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	66	GLY	0	0.025	0.030	24.386	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	67	ARG	1	0.894	0.937	18.682	0.278	0.278	0.000	0.000	0.000	0.000
65	A	68	ARG	1	0.924	0.947	15.347	0.398	0.398	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.073	0.037	18.505	0.007	0.007	0.000	0.000	0.000	0.000
67	A	70	PHE	0	0.017	0.017	17.370	0.025	0.025	0.000	0.000	0.000	0.000
68	A	71	LEU	0	0.009	0.006	13.639	0.027	0.027	0.000	0.000	0.000	0.000
69	A	72	GLN	0	0.000	-0.013	15.381	0.007	0.007	0.000	0.000	0.000	0.000
70	A	73	THR	0	0.018	0.007	17.192	0.043	0.043	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.003	0.019	14.767	0.042	0.042	0.000	0.000	0.000	0.000
72	A	75	ASN	0	0.023	-0.006	11.811	0.143	0.143	0.000	0.000	0.000	0.000
73	A	76	ALA	0	0.010	0.012	14.414	0.072	0.072	0.000	0.000	0.000	0.000
74	A	77	THR	0	-0.026	-0.021	17.208	0.036	0.036	0.000	0.000	0.000	0.000
75	A	78	LEU	0	0.013	0.000	12.823	0.038	0.038	0.000	0.000	0.000	0.000
76	A	79	GLY	0	0.029	0.026	14.894	0.072	0.072	0.000	0.000	0.000	0.000
77	A	80	CYS	0	-0.016	-0.001	15.746	0.034	0.034	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.006	-0.003	17.332	0.006	0.006	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.015	-0.007	11.961	0.028	0.028	0.000	0.000	0.000	0.000
80	A	83	HIS	0	-0.036	-0.028	16.508	0.013	0.013	0.000	0.000	0.000	0.000
81	A	84	ARG	1	0.939	0.973	19.364	-0.195	-0.195	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.007	0.004	17.254	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	86	ALA	0	-0.006	0.008	18.563	0.002	0.002	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.815	-0.879	20.300	0.209	0.209	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.053	-0.043	23.569	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	89	GLU	-1	-0.892	-0.947	19.479	0.519	0.519	0.000	0.000	0.000	0.000
87	A	90	GLN	0	-0.052	-0.017	23.539	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	91	ARG	1	0.736	0.844	25.495	-0.230	-0.230	0.000	0.000	0.000	0.000
89	A	92	LEU	0	-0.025	0.005	24.610	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	93	PRO	0	0.003	0.004	28.130	0.002	0.002	0.000	0.000	0.000	0.000
91	A	94	LYS	1	0.929	0.959	28.275	-0.227	-0.227	0.000	0.000	0.000	0.000
92	A	95	ALA	0	0.065	0.020	26.471	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	96	GLN	0	-0.012	0.009	28.593	0.007	0.007	0.000	0.000	0.000	0.000
94	A	97	ASP	-1	-0.868	-0.951	31.723	0.178	0.178	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.043	-0.003	28.264	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.875	-0.928	32.951	0.145	0.145	0.000	0.000	0.000	0.000
97	A	100	ARG	1	0.948	0.977	35.594	-0.132	-0.132	0.000	0.000	0.000	0.000
98	A	101	SER	0	-0.075	-0.042	35.380	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	102	GLY	0	-0.015	-0.001	37.251	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	103	LEU	0	-0.097	-0.042	31.965	0.001	0.001	0.000	0.000	0.000	0.000
101	A	104	ASN	0	0.032	0.000	29.085	0.002	0.002	0.000	0.000	0.000	0.000
102	A	105	ILE	0	0.052	0.015	26.065	0.011	0.011	0.000	0.000	0.000	0.000
103	A	106	GLU	-1	-0.772	-0.871	24.996	0.260	0.260	0.000	0.000	0.000	0.000
104	A	107	ASP	-1	-0.798	-0.890	24.626	0.236	0.236	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.001	-0.010	23.901	0.018	0.018	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.888	-0.950	21.471	0.378	0.378	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.790	0.891	19.873	-0.192	-0.192	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.040	-0.021	19.392	0.048	0.048	0.000	0.000	0.000	0.000
109	A	112	GLN	0	-0.038	-0.011	18.430	0.027	0.027	0.000	0.000	0.000	0.000
110	A	113	MET	0	-0.015	-0.001	13.773	0.129	0.129	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.045	-0.012	14.278	0.111	0.111	0.000	0.000	0.000	0.000
112	A	115	ARG	1	1.023	0.997	12.697	-0.829	-0.829	0.000	0.000	0.000	0.000
113	A	116	PRO	0	0.040	0.013	10.447	0.159	0.159	0.000	0.000	0.000	0.000
114	A	117	ASN	0	0.011	0.009	9.334	0.404	0.404	0.000	0.000	0.000	0.000
115	A	118	ILE	0	0.003	0.003	10.020	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.033	-0.016	7.481	-0.172	-0.172	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.038	0.026	5.434	0.300	0.300	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.023	-0.009	6.016	-0.666	-0.666	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.899	0.932	8.122	-0.816	-0.816	0.000	0.000	0.000	0.000
120	A	123	ASN	0	0.015	0.014	2.533	-5.157	-3.502	1.330	-1.359	-1.626	-0.001
121	A	124	ASN	0	0.022	0.008	5.020	-1.662	-1.705	-0.001	-0.003	0.048	0.000
122	A	125	ILE	0	-0.011	-0.006	6.672	-0.079	-0.079	0.000	0.000	0.000	0.000
123	A	126	TYR	0	0.024	0.016	6.132	0.020	0.020	0.000	0.000	0.000	0.000
124	A	128	MET	0	0.044	0.015	8.383	0.184	0.184	0.000	0.000	0.000	0.000
125	A	129	ALA	0	-0.006	0.000	11.536	0.106	0.106	0.000	0.000	0.000	0.000
126	A	130	GLN	0	-0.048	-0.026	10.133	0.177	0.177	0.000	0.000	0.000	0.000
127	A	131	LEU	0	-0.093	-0.036	12.696	0.000	0.000	0.000	0.000	0.000	0.000
128	A	132	LEU	0	-0.055	-0.016	14.715	0.085	0.085	0.000	0.000	0.000	0.000
129	A	133	ASP	-1	-0.852	-0.911	17.517	-0.398	-0.398	0.000	0.000	0.000	0.000
130	A	134	ASN	0	0.004	0.010	19.592	0.004	0.004	0.000	0.000	0.000	0.000
131	A	156	ALA	0	0.012	-0.002	35.946	0.003	0.003	0.000	0.000	0.000	0.000
132	A	157	SER	0	0.004	0.009	35.564	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	158	ASP	-1	-0.769	-0.871	37.007	0.114	0.114	0.000	0.000	0.000	0.000
134	A	159	ALA	0	0.007	-0.030	35.417	0.005	0.005	0.000	0.000	0.000	0.000
135	A	160	PHE	0	0.027	0.023	35.264	0.008	0.008	0.000	0.000	0.000	0.000
136	A	161	GLN	0	0.045	0.007	36.183	0.007	0.007	0.000	0.000	0.000	0.000
137	A	162	ARG	1	0.890	0.928	31.993	-0.141	-0.141	0.000	0.000	0.000	0.000
138	A	163	LYS	1	0.888	0.969	31.444	-0.146	-0.146	0.000	0.000	0.000	0.000
139	A	164	LEU	0	0.067	0.029	31.501	0.007	0.007	0.000	0.000	0.000	0.000
140	A	165	GLU	-1	-0.796	-0.868	30.819	0.116	0.116	0.000	0.000	0.000	0.000
141	A	166	GLY	0	0.004	0.007	27.659	0.006	0.006	0.000	0.000	0.000	0.000
142	A	168	ARG	1	0.803	0.896	28.777	-0.110	-0.110	0.000	0.000	0.000	0.000
143	A	169	PHE	0	-0.025	-0.017	21.160	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	170	LEU	0	0.033	0.005	22.370	0.003	0.003	0.000	0.000	0.000	0.000
145	A	171	HIS	0	0.002	0.010	24.376	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	172	GLY	0	0.007	-0.013	26.249	-0.010	-0.010	0.000	0.000	0.000	0.000
147	A	173	TYR	0	-0.010	0.000	15.944	0.002	0.002	0.000	0.000	0.000	0.000
148	A	174	HIS	0	0.036	0.010	21.092	0.003	0.003	0.000	0.000	0.000	0.000
149	A	175	ARG	1	0.793	0.877	22.750	-0.087	-0.087	0.000	0.000	0.000	0.000
150	A	176	PHE	0	0.014	-0.008	18.247	-0.020	-0.020	0.000	0.000	0.000	0.000
151	A	177	MET	0	-0.026	-0.021	15.543	-0.015	-0.015	0.000	0.000	0.000	0.000
152	A	178	HIS	0	0.022	0.009	19.906	-0.033	-0.033	0.000	0.000	0.000	0.000
153	A	179	SER	0	-0.007	-0.008	22.605	-0.017	-0.017	0.000	0.000	0.000	0.000
154	A	180	VAL	0	-0.049	-0.020	16.859	-0.027	-0.027	0.000	0.000	0.000	0.000
155	A	181	GLY	0	0.045	0.032	18.676	-0.031	-0.031	0.000	0.000	0.000	0.000
156	A	182	ARG	1	0.862	0.917	19.649	-0.018	-0.018	0.000	0.000	0.000	0.000
157	A	183	VAL	0	-0.032	-0.001	20.784	-0.019	-0.019	0.000	0.000	0.000	0.000
158	A	184	PHE	0	0.029	0.005	14.227	-0.032	-0.032	0.000	0.000	0.000	0.000
159	A	185	SER	0	-0.073	-0.026	19.199	-0.029	-0.029	0.000	0.000	0.000	0.000
160	A	186	LYS	1	0.938	0.969	21.501	0.065	0.065	0.000	0.000	0.000	0.000
161	A	187	TRP	0	0.001	0.007	15.969	-0.028	-0.028	0.000	0.000	0.000	0.000

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