FMO DATABASE

FMODB ID: P4NZN

Calculation Name: 1O8X-A-Xray13

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O8X

Chain ID: A

ChEMBL ID:

UniProt ID: O96438

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1381973.986702
FMO2-HF: Nuclear repulsion	1325809.92954
FMO2-HF: Total energy	-56164.057162
FMO2-MP2: Total energy	-56330.233628

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:2:ACE)

Summations of interaction energy for fragment #1(A:2:ACE)

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.
-3.554	-2.385	0.001	-0.626	-0.544	-0.002

Interaction energy analysis for fragmet #1(A:2:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.052 / q_NPA : -0.038

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	4	LEU	0	-0.001	-0.019	3.842	1.123	1.957	-0.010	-0.380	-0.444	-0.001
4	A	5	ASP	-1	-0.882	-0.937	4.358	0.436	0.604	-0.001	-0.012	-0.155	0.000
5	A	6	LYS	1	0.922	0.970	6.056	0.937	0.937	0.000	0.000	0.000	0.000
6	A	7	TYR	0	-0.103	-0.084	8.213	0.215	0.215	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.041	-0.024	9.209	0.091	0.091	0.000	0.000	0.000	0.000
8	A	9	PRO	0	0.014	0.023	9.269	0.089	0.089	0.000	0.000	0.000	0.000
9	A	10	GLY	0	-0.002	-0.001	9.313	0.002	0.002	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.046	-0.012	10.571	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.916	-0.964	10.420	0.552	0.552	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.896	0.954	11.765	-0.209	-0.209	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.011	0.013	12.312	-0.033	-0.033	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.925	0.971	15.835	-0.045	-0.045	0.000	0.000	0.000	0.000
15	A	16	ARG	1	1.011	0.989	18.826	-0.081	-0.081	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.015	0.024	20.687	0.009	0.009	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.890	-0.953	24.469	0.025	0.025	0.000	0.000	0.000	0.000
18	A	19	GLY	0	-0.070	-0.029	23.018	0.006	0.006	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.936	-0.982	17.957	0.114	0.114	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.040	-0.019	14.304	0.005	0.005	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.902	-0.956	11.693	0.401	0.401	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.031	0.016	7.361	-0.026	-0.026	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.976	0.974	6.902	-1.438	-1.438	0.000	0.000	0.000	0.000
24	A	25	SER	0	-0.086	-0.041	8.282	-0.040	-0.040	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.022	-0.022	8.491	-0.063	-0.063	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.006	0.003	6.664	-0.127	-0.127	0.000	0.000	0.000	0.000
27	A	28	GLY	0	0.004	0.002	7.275	0.036	0.036	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.847	0.947	9.327	0.022	0.022	0.000	0.000	0.000	0.000
29	A	30	LEU	0	0.003	0.013	10.089	-0.123	-0.123	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.002	-0.016	9.806	0.088	0.088	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.002	-0.004	12.673	-0.049	-0.049	0.000	0.000	0.000	0.000
32	A	33	PHE	0	0.020	0.005	11.047	0.041	0.041	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.001	-0.032	16.662	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.029	0.022	17.507	0.015	0.015	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.030	-0.006	22.367	0.006	0.006	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.049	0.020	25.690	0.001	0.001	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.055	-0.067	28.337	0.000	0.000	0.000	0.000	0.000	0.000
38	A	39	TRP	0	-0.016	-0.012	29.536	0.000	0.000	0.000	0.000	0.000	0.000
39	A	40	CYS	0	-0.018	0.016	29.562	0.000	0.000	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.018	-0.018	32.466	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	PRO	0	0.008	-0.006	32.051	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.059	0.019	29.087	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.933	0.981	30.717	0.034	0.034	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.033	0.020	33.347	0.002	0.002	0.000	0.000	0.000	0.000
45	A	46	PHE	0	-0.022	-0.001	25.011	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.060	0.024	26.823	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	48	PRO	0	0.017	0.005	28.182	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.002	-0.003	29.885	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.026	0.004	22.139	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.016	-0.004	25.230	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.908	-0.940	26.792	-0.046	-0.046	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.028	-0.022	22.121	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.080	-0.076	18.929	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.909	-0.963	23.426	-0.030	-0.030	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.798	0.919	25.932	0.058	0.058	0.000	0.000	0.000	0.000
56	A	57	PHE	0	-0.030	-0.023	22.941	0.001	0.001	0.000	0.000	0.000	0.000
57	A	58	HIS	1	0.882	0.956	18.900	0.032	0.032	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.926	-0.965	18.703	-0.022	-0.022	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.014	-0.011	19.674	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.883	0.943	19.969	0.096	0.096	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.006	0.009	13.256	0.007	0.007	0.000	0.000	0.000	0.000
62	A	63	PHE	0	-0.020	-0.008	14.731	-0.041	-0.041	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.836	-0.894	13.725	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.018	-0.011	15.637	-0.042	-0.042	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.030	0.008	13.246	0.029	0.029	0.000	0.000	0.000	0.000
66	A	67	PHE	0	-0.032	-0.025	16.652	-0.022	-0.022	0.000	0.000	0.000	0.000
67	A	68	CYS	0	-0.058	-0.024	17.370	0.005	0.005	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.035	0.009	19.896	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	70	TRP	0	0.008	-0.015	22.751	0.000	0.000	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.829	-0.873	25.922	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.907	-0.963	27.088	-0.037	-0.037	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.960	-0.967	29.376	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.934	-0.970	27.205	0.016	0.016	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.875	-0.942	29.469	0.004	0.004	0.000	0.000	0.000	0.000
75	A	76	GLY	0	-0.024	-0.006	31.759	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.008	-0.019	22.505	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.023	0.006	27.430	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.011	0.007	28.477	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	TYR	0	-0.107	-0.069	27.017	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.035	-0.003	21.390	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.020	0.022	26.109	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.835	0.923	28.399	0.019	0.019	0.000	0.000	0.000	0.000
83	A	84	MET	0	-0.046	0.003	24.096	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.012	0.016	23.728	0.007	0.007	0.000	0.000	0.000	0.000
85	A	86	TRP	0	-0.041	-0.014	19.167	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.015	-0.018	14.459	0.017	0.017	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.003	0.007	18.386	-0.021	-0.021	0.000	0.000	0.000	0.000
88	A	89	VAL	0	-0.004	0.004	15.260	0.022	0.022	0.000	0.000	0.000	0.000
89	A	90	PRO	0	-0.006	-0.004	16.972	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	91	PHE	0	0.042	0.036	20.041	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	92	ALA	0	0.042	0.026	21.559	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	GLN	0	-0.012	-0.010	16.324	0.002	0.002	0.000	0.000	0.000	0.000
93	A	94	SER	0	0.053	0.002	18.569	-0.021	-0.021	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.934	-0.959	20.295	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.044	-0.023	14.992	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.042	0.025	16.752	-0.035	-0.035	0.000	0.000	0.000	0.000
97	A	98	GLN	0	0.023	0.015	18.635	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.933	0.958	17.330	0.051	0.051	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.010	0.024	13.657	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.006	-0.009	16.791	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.958	0.988	20.290	0.117	0.117	0.000	0.000	0.000	0.000
102	A	103	HIS	0	-0.079	-0.032	14.051	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	104	PHE	0	-0.026	-0.026	13.773	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	105	ASN	0	-0.025	-0.006	19.071	0.016	0.016	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.003	0.004	20.805	0.007	0.007	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.938	-0.966	23.578	-0.096	-0.096	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.066	-0.027	27.060	0.012	0.012	0.000	0.000	0.000	0.000
108	A	109	ILE	0	0.003	0.041	25.179	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	110	PRO	0	-0.061	-0.057	26.413	0.008	0.008	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.018	-0.024	21.734	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.047	-0.019	19.826	0.005	0.005	0.000	0.000	0.000	0.000
112	A	113	ILE	0	0.000	0.008	15.861	0.002	0.002	0.000	0.000	0.000	0.000
113	A	114	GLY	0	-0.012	0.008	15.258	0.002	0.002	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.007	-0.008	9.922	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.795	-0.881	8.577	-0.923	-0.923	0.000	0.000	0.000	0.000
116	A	117	ALA	0	-0.031	-0.017	6.561	-0.341	-0.341	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.859	-0.929	3.972	-1.381	-1.263	0.000	-0.028	-0.091	0.000
118	A	119	SER	0	-0.037	-0.032	3.951	-2.183	-2.134	0.012	-0.206	0.146	-0.001
119	A	120	GLY	0	0.013	0.003	6.365	-0.253	-0.253	0.000	0.000	0.000	0.000
120	A	121	ASP	-1	-0.952	-0.948	7.428	-0.624	-0.624	0.000	0.000	0.000	0.000
121	A	122	VAL	0	-0.023	-0.025	10.776	0.067	0.067	0.000	0.000	0.000	0.000
122	A	123	VAL	0	-0.018	0.004	13.286	0.037	0.037	0.000	0.000	0.000	0.000
123	A	124	THR	0	-0.041	-0.042	15.891	0.057	0.057	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.011	-0.030	18.237	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.863	0.922	20.487	0.206	0.206	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.079	0.045	21.115	0.018	0.018	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.929	0.979	23.075	0.108	0.108	0.000	0.000	0.000	0.000
128	A	129	ALA	0	-0.049	-0.030	25.557	0.013	0.013	0.000	0.000	0.000	0.000
129	A	130	THR	0	-0.027	-0.024	24.738	0.006	0.006	0.000	0.000	0.000	0.000
130	A	131	LEU	0	0.029	0.028	23.889	0.007	0.007	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.034	-0.022	26.900	0.007	0.007	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.879	0.938	30.115	0.084	0.084	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.756	-0.851	27.415	-0.101	-0.101	0.000	0.000	0.000	0.000
134	A	135	PRO	0	0.031	0.025	28.282	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	136	GLU	-1	-0.798	-0.913	28.987	-0.057	-0.057	0.000	0.000	0.000	0.000
136	A	137	GLY	0	-0.067	-0.027	25.710	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.972	-0.992	25.749	-0.080	-0.080	0.000	0.000	0.000	0.000
138	A	139	GLN	0	-0.061	-0.043	26.236	-0.013	-0.013	0.000	0.000	0.000	0.000
139	A	140	PHE	0	-0.001	0.036	17.978	-0.018	-0.018	0.000	0.000	0.000	0.000
140	A	141	PRO	0	-0.063	-0.039	17.872	0.004	0.004	0.000	0.000	0.000	0.000
141	A	142	TRP	0	-0.036	-0.065	20.226	-0.023	-0.023	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.961	0.990	18.852	0.221	0.221	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.750	-0.846	19.991	-0.223	-0.223	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.054	-0.026	21.686	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	146	NME	0	0.017	0.018	21.353	-0.013	-0.013	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE)