FMO DATABASE

FMODB ID: 49VNN

Calculation Name: 1E5P-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1E5P

Chain ID: A

ChEMBL ID:

UniProt ID: P09465

Base Structure: X-ray

Registration Date: 2023-09-19

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	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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1485860.102689
FMO2-HF: Nuclear repulsion	1425591.512522
FMO2-HF: Total energy	-60268.590167
FMO2-MP2: Total energy	-60442.320682

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:3:PHE)

Summations of interaction energy for fragment #1(A:3:PHE)

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.
-19.76	-7.664	14.927	-7.1	-19.919	-0.004

Interaction energy analysis for fragmet #1(A:3:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.046 / q_NPA : 0.004

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	5	GLU	-1	-0.978	-0.987	3.300	-0.213	2.074	0.013	-0.818	-1.481	0.002
4	A	6	LEU	0	0.025	0.001	2.403	-1.995	-0.413	1.449	-0.710	-2.321	-0.001
5	A	7	GLN	0	-0.017	0.009	5.157	0.088	0.161	-0.001	-0.003	-0.069	0.000
6	A	8	GLY	0	-0.036	-0.021	8.236	0.207	0.207	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.967	0.989	11.604	-0.052	-0.052	0.000	0.000	0.000	0.000
8	A	10	TRP	0	-0.074	-0.022	8.489	0.089	0.089	0.000	0.000	0.000	0.000
9	A	11	TYR	0	0.034	0.019	13.968	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	12	THR	0	0.021	0.000	15.592	0.007	0.007	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.054	-0.007	16.405	0.002	0.002	0.000	0.000	0.000	0.000
12	A	14	VAL	0	0.035	0.003	17.008	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	15	ILE	0	-0.016	-0.002	17.086	0.001	0.001	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.023	0.026	17.584	0.003	0.003	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.000	-0.008	17.874	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.757	-0.871	19.884	-0.090	-0.090	0.000	0.000	0.000	0.000
17	A	19	ASN	0	-0.031	0.000	21.817	0.011	0.011	0.000	0.000	0.000	0.000
18	A	20	LEU	0	0.033	0.007	23.684	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.840	-0.928	25.270	-0.068	-0.068	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.827	0.895	22.249	0.106	0.106	0.000	0.000	0.000	0.000
21	A	23	ILE	0	-0.045	-0.025	20.129	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.884	-0.925	23.334	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.986	-0.999	26.800	-0.042	-0.042	0.000	0.000	0.000	0.000
24	A	26	GLY	0	-0.026	-0.017	28.182	0.001	0.001	0.000	0.000	0.000	0.000
25	A	27	GLY	0	-0.008	0.011	25.920	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.025	-0.015	23.140	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.025	-0.026	18.532	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	30	ARG	1	0.851	0.918	19.877	0.046	0.046	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.036	-0.015	13.923	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	32	TYR	0	0.037	0.037	18.636	0.012	0.012	0.000	0.000	0.000	0.000
31	A	33	PHE	0	-0.011	-0.015	10.903	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	34	ARG	1	0.701	0.826	15.362	0.075	0.075	0.000	0.000	0.000	0.000
33	A	35	HIS	0	-0.070	-0.050	13.063	0.078	0.078	0.000	0.000	0.000	0.000
34	A	36	ILE	0	0.000	0.018	6.666	-0.026	-0.026	0.000	0.000	0.000	0.000
35	A	37	ASP	-1	-0.828	-0.899	9.842	-0.192	-0.192	0.000	0.000	0.000	0.000
36	A	38	CYS	0	0.008	0.018	2.636	-1.822	-0.792	0.386	-0.331	-1.084	-0.001
37	A	39	TYR	0	0.037	0.017	7.497	0.303	0.303	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.915	0.952	7.913	0.219	0.219	0.000	0.000	0.000	0.000
39	A	41	ASN	0	-0.002	-0.013	4.950	0.208	0.248	-0.001	-0.007	-0.031	0.000
40	A	43	SER	0	-0.010	0.011	4.238	-1.377	-0.969	0.001	-0.076	-0.332	0.000
41	A	44	GLU	-1	-0.922	-0.959	5.985	-0.436	-0.436	0.000	0.000	0.000	0.000
42	A	45	MET	0	-0.027	-0.010	3.907	-0.150	0.047	0.000	-0.018	-0.179	0.000
43	A	46	GLU	-1	-0.883	-0.952	7.340	-0.177	-0.177	0.000	0.000	0.000	0.000
44	A	47	ILE	0	-0.032	-0.006	8.982	0.013	0.013	0.000	0.000	0.000	0.000
45	A	48	THR	0	0.002	-0.009	11.831	0.037	0.037	0.000	0.000	0.000	0.000
46	A	49	PHE	0	-0.013	-0.018	15.184	0.017	0.017	0.000	0.000	0.000	0.000
47	A	50	TYR	0	0.024	0.000	17.349	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	51	VAL	0	0.070	0.034	20.409	0.001	0.001	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.006	0.006	22.793	0.003	0.003	0.000	0.000	0.000	0.000
50	A	53	THR	0	0.041	0.012	26.186	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	54	ASN	0	-0.033	-0.023	28.317	0.004	0.004	0.000	0.000	0.000	0.000
52	A	55	ASN	0	-0.022	-0.016	31.538	0.004	0.004	0.000	0.000	0.000	0.000
53	A	56	GLN	0	0.018	0.017	30.496	0.006	0.006	0.000	0.000	0.000	0.000
54	A	57	CYS	0	-0.041	0.000	24.167	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	58	SER	0	0.012	0.009	24.151	0.003	0.003	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.921	0.966	20.104	0.090	0.090	0.000	0.000	0.000	0.000
57	A	60	THR	0	-0.038	-0.012	18.533	0.002	0.002	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.009	0.008	16.005	0.005	0.005	0.000	0.000	0.000	0.000
59	A	62	VAL	0	-0.005	0.009	13.030	0.014	0.014	0.000	0.000	0.000	0.000
60	A	63	ILE	0	0.016	0.012	11.165	-0.027	-0.027	0.000	0.000	0.000	0.000
61	A	64	GLY	0	-0.007	0.013	8.812	0.073	0.073	0.000	0.000	0.000	0.000
62	A	65	TYR	0	-0.035	-0.024	8.349	-0.170	-0.170	0.000	0.000	0.000	0.000
63	A	66	LEU	0	0.000	0.009	2.668	-0.920	0.081	0.407	-0.238	-1.169	0.000
64	A	67	LYS	1	0.884	0.958	5.996	1.102	1.102	0.000	0.000	0.000	0.000
65	A	68	GLY	0	-0.001	-0.009	6.339	-0.211	-0.211	0.000	0.000	0.000	0.000
66	A	69	ASN	0	0.007	0.011	7.509	-0.143	-0.143	0.000	0.000	0.000	0.000
67	A	70	GLY	0	0.016	0.012	3.717	0.051	0.236	0.002	-0.031	-0.156	0.000
68	A	71	THR	0	-0.080	-0.037	2.744	-3.635	-1.645	0.445	-1.079	-1.356	-0.014
69	A	72	TYR	0	-0.019	-0.036	2.319	-4.492	-4.581	7.841	-1.952	-5.800	-0.009
70	A	73	GLU	-1	-0.905	-0.953	6.343	-0.314	-0.314	0.000	0.000	0.000	0.000
71	A	74	THR	0	-0.021	-0.035	10.132	-0.032	-0.032	0.000	0.000	0.000	0.000
72	A	75	GLN	0	-0.048	-0.013	12.888	0.056	0.056	0.000	0.000	0.000	0.000
73	A	76	PHE	0	0.030	-0.002	16.634	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.904	-0.936	18.320	-0.124	-0.124	0.000	0.000	0.000	0.000
75	A	78	GLY	0	0.009	0.014	19.957	0.009	0.009	0.000	0.000	0.000	0.000
76	A	79	ASN	0	-0.101	-0.054	16.019	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	80	ASN	0	0.019	0.020	12.803	0.044	0.044	0.000	0.000	0.000	0.000
78	A	81	ILE	0	0.026	0.013	9.245	-0.065	-0.065	0.000	0.000	0.000	0.000
79	A	82	PHE	0	0.001	-0.015	7.050	0.032	0.032	0.000	0.000	0.000	0.000
80	A	83	GLN	0	-0.002	-0.013	3.151	-0.606	0.089	0.030	-0.181	-0.545	0.001
81	A	84	PRO	0	0.001	0.010	2.672	-3.635	-2.040	4.189	-1.370	-4.413	0.018
82	A	85	LEU	0	-0.071	-0.035	4.342	-0.785	-0.545	-0.001	-0.027	-0.212	0.000
83	A	86	TYR	0	0.004	-0.009	6.592	-0.097	-0.097	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.006	0.007	2.892	-0.946	-0.084	0.167	-0.259	-0.771	0.000
85	A	88	THR	0	0.021	0.012	7.341	0.066	0.066	0.000	0.000	0.000	0.000
86	A	89	SER	0	0.020	-0.011	9.390	0.045	0.045	0.000	0.000	0.000	0.000
87	A	90	ASP	-1	-0.911	-0.949	11.306	0.144	0.144	0.000	0.000	0.000	0.000
88	A	91	LYS	1	0.845	0.913	11.552	-0.170	-0.170	0.000	0.000	0.000	0.000
89	A	92	ILE	0	0.009	0.031	6.823	0.045	0.045	0.000	0.000	0.000	0.000
90	A	93	PHE	0	0.029	0.025	8.737	-0.042	-0.042	0.000	0.000	0.000	0.000
91	A	94	PHE	0	0.022	0.002	6.342	0.095	0.095	0.000	0.000	0.000	0.000
92	A	95	THR	0	-0.022	-0.004	7.687	-0.109	-0.109	0.000	0.000	0.000	0.000
93	A	96	ASN	0	0.018	-0.042	9.228	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	97	LYS	1	0.905	0.979	11.760	0.255	0.255	0.000	0.000	0.000	0.000
95	A	98	ASN	0	-0.019	-0.019	14.144	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	99	MET	0	0.064	0.048	16.702	0.016	0.016	0.000	0.000	0.000	0.000
97	A	100	ASP	-1	-0.741	-0.862	19.187	-0.126	-0.126	0.000	0.000	0.000	0.000
98	A	101	ARG	1	0.949	0.954	22.063	0.139	0.139	0.000	0.000	0.000	0.000
99	A	102	ALA	0	-0.059	-0.025	24.679	0.004	0.004	0.000	0.000	0.000	0.000
100	A	103	GLY	0	-0.017	-0.003	23.582	0.005	0.005	0.000	0.000	0.000	0.000
101	A	104	GLN	0	-0.077	-0.032	23.712	0.004	0.004	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.863	-0.945	16.991	-0.200	-0.200	0.000	0.000	0.000	0.000
103	A	106	THR	0	-0.025	-0.012	19.027	0.018	0.018	0.000	0.000	0.000	0.000
104	A	107	ASN	0	-0.077	-0.041	15.904	-0.034	-0.034	0.000	0.000	0.000	0.000
105	A	108	MET	0	0.011	0.007	14.672	0.007	0.007	0.000	0.000	0.000	0.000
106	A	109	ILE	0	-0.012	-0.004	12.735	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.021	0.003	12.686	-0.010	-0.010	0.000	0.000	0.000	0.000
108	A	111	VAL	0	0.009	0.010	12.164	0.032	0.032	0.000	0.000	0.000	0.000
109	A	112	ALA	0	0.013	0.013	11.103	-0.022	-0.022	0.000	0.000	0.000	0.000
110	A	113	GLY	0	0.064	0.002	12.842	0.030	0.030	0.000	0.000	0.000	0.000
111	A	114	LYS	1	0.836	0.909	11.821	-0.117	-0.117	0.000	0.000	0.000	0.000
112	A	115	GLY	0	0.007	0.001	16.216	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	116	ASN	0	-0.055	-0.013	19.558	-0.015	-0.015	0.000	0.000	0.000	0.000
114	A	117	ALA	0	0.042	0.022	19.814	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	118	LEU	0	-0.021	-0.008	17.186	0.010	0.010	0.000	0.000	0.000	0.000
116	A	119	THR	0	-0.002	0.001	19.671	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	120	PRO	0	0.008	-0.016	21.153	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	121	GLU	-1	-0.899	-0.946	19.242	0.107	0.107	0.000	0.000	0.000	0.000
119	A	122	GLU	-1	-0.816	-0.913	15.992	0.114	0.114	0.000	0.000	0.000	0.000
120	A	123	ASN	0	-0.004	-0.016	17.239	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.923	-0.950	19.534	0.024	0.024	0.000	0.000	0.000	0.000
122	A	125	ILE	0	-0.004	-0.005	13.031	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.020	-0.009	15.410	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	127	VAL	0	0.021	0.011	16.406	-0.014	-0.014	0.000	0.000	0.000	0.000
125	A	128	GLN	0	-0.029	-0.013	16.588	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	129	PHE	0	0.027	0.008	10.182	-0.009	-0.009	0.000	0.000	0.000	0.000
127	A	130	ALA	0	-0.011	-0.005	15.064	-0.016	-0.016	0.000	0.000	0.000	0.000
128	A	131	HIS	0	0.003	-0.003	17.958	-0.013	-0.013	0.000	0.000	0.000	0.000
129	A	132	GLU	-1	-0.968	-0.978	12.596	-0.106	-0.106	0.000	0.000	0.000	0.000
130	A	133	LYS	1	0.856	0.932	10.659	0.137	0.137	0.000	0.000	0.000	0.000
131	A	134	LYS	1	0.883	0.941	16.268	0.052	0.052	0.000	0.000	0.000	0.000
132	A	135	ILE	0	-0.011	0.006	16.497	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	136	PRO	0	0.018	0.009	20.440	0.007	0.007	0.000	0.000	0.000	0.000
134	A	137	VAL	0	0.053	0.008	22.007	0.000	0.000	0.000	0.000	0.000	0.000
135	A	138	GLU	-1	-1.001	-0.985	23.753	-0.023	-0.023	0.000	0.000	0.000	0.000
136	A	139	ASN	0	-0.027	-0.027	23.049	0.004	0.004	0.000	0.000	0.000	0.000
137	A	140	ILE	0	-0.020	-0.017	19.988	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	141	LEU	0	-0.004	0.005	21.837	0.004	0.004	0.000	0.000	0.000	0.000
139	A	142	ASN	0	-0.006	-0.019	21.850	0.002	0.002	0.000	0.000	0.000	0.000
140	A	143	ILE	0	-0.015	-0.010	20.467	-0.003	-0.003	0.000	0.000	0.000	0.000
141	A	144	LEU	0	0.038	0.023	20.846	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	145	ALA	0	-0.049	-0.022	22.829	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	146	THR	0	0.014	0.009	25.626	0.000	0.000	0.000	0.000	0.000	0.000
144	A	147	ASP	-1	-0.840	-0.898	21.511	-0.045	-0.045	0.000	0.000	0.000	0.000
145	A	148	THR	0	-0.019	-0.010	24.641	0.003	0.003	0.000	0.000	0.000	0.000
146	A	150	PRO	0	0.031	0.014	25.461	0.004	0.004	0.000	0.000	0.000	0.000
147	A	151	GLU	-1	-0.956	-0.971	21.693	-0.019	-0.019	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:PHE)