FMO DATABASE

FMODB ID: YZ9L2

Calculation Name: 1O22-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O22

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZX8

Base Structure: X-ray

Registration Date: 2023-06-22

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1348159.664499
FMO2-HF: Nuclear repulsion	1287832.564818
FMO2-HF: Total energy	-60327.099682
FMO2-MP2: Total energy	-60505.447228

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:6:ILE)

Summations of interaction energy for fragment #1(A:6:ILE)

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.
-12.718	-3.079	10.951	-6.571	-14.018	-0.04

Interaction energy analysis for fragmet #1(A:6:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.036 / q_NPA : -0.011

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	8	GLU	-1	-0.802	-0.892	3.358	-3.315	0.039	0.085	-1.640	-1.799	0.002
4	A	9	ILE	0	-0.016	-0.025	5.165	0.105	0.150	-0.001	-0.004	-0.039	0.000
5	A	10	LEU	0	0.007	0.022	8.333	0.133	0.133	0.000	0.000	0.000	0.000
6	A	11	TYR	0	-0.028	-0.030	11.463	0.016	0.016	0.000	0.000	0.000	0.000
7	A	12	TYR	0	0.012	-0.008	14.427	0.038	0.038	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.859	0.943	18.069	0.144	0.144	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.845	0.900	21.363	0.202	0.202	0.000	0.000	0.000	0.000
10	A	15	GLY	0	-0.023	-0.006	23.630	0.016	0.016	0.000	0.000	0.000	0.000
11	A	16	LYS	1	0.852	0.953	23.208	0.194	0.194	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.878	-0.934	23.906	-0.229	-0.229	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.002	-0.025	20.842	0.016	0.016	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.111	0.070	23.365	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	20	ILE	0	-0.037	-0.034	25.339	0.005	0.005	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.024	-0.011	20.888	0.011	0.011	0.000	0.000	0.000	0.000
17	A	22	GLU	-1	-0.838	-0.934	20.305	-0.296	-0.296	0.000	0.000	0.000	0.000
18	A	23	LYS	1	0.875	0.953	22.891	0.146	0.146	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.978	0.982	26.391	0.128	0.128	0.000	0.000	0.000	0.000
20	A	25	MET	0	0.004	0.020	18.297	0.013	0.013	0.000	0.000	0.000	0.000
21	A	26	LYS	1	0.837	0.943	22.666	0.207	0.207	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.895	-0.980	24.735	-0.126	-0.126	0.000	0.000	0.000	0.000
23	A	28	ILE	0	0.059	0.028	25.699	0.008	0.008	0.000	0.000	0.000	0.000
24	A	29	PHE	0	-0.010	0.014	21.452	0.006	0.006	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.048	-0.042	25.163	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	31	GLU	-1	-0.965	-0.958	27.992	-0.086	-0.086	0.000	0.000	0.000	0.000
27	A	32	THR	0	-0.035	-0.047	27.223	0.007	0.007	0.000	0.000	0.000	0.000
28	A	33	GLY	0	0.005	0.016	25.804	0.008	0.008	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.054	-0.024	22.901	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	35	SER	0	-0.018	-0.013	18.498	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	36	LEU	0	-0.034	-0.015	19.855	0.008	0.008	0.000	0.000	0.000	0.000
32	A	37	GLU	-1	-0.841	-0.921	13.545	-0.442	-0.442	0.000	0.000	0.000	0.000
33	A	38	PRO	0	-0.039	-0.021	15.928	0.036	0.036	0.000	0.000	0.000	0.000
34	A	39	VAL	0	0.012	0.017	15.742	-0.016	-0.016	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.030	-0.019	10.883	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	41	SER	0	0.011	0.005	15.398	0.037	0.037	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.812	-0.895	17.765	-0.140	-0.140	0.000	0.000	0.000	0.000
38	A	43	LEU	0	-0.016	-0.004	20.253	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	44	ILE	0	0.015	0.007	16.184	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	45	GLY	0	0.009	0.007	13.957	0.047	0.047	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.843	0.916	7.865	0.677	0.677	0.000	0.000	0.000	0.000
42	A	47	ILE	0	-0.032	-0.005	7.438	0.143	0.143	0.000	0.000	0.000	0.000
43	A	48	PHE	0	0.000	0.005	2.220	-1.114	-0.640	1.577	-0.496	-1.555	-0.001
44	A	49	LEU	0	0.019	0.021	2.924	-0.579	0.488	0.151	-0.295	-0.923	-0.001
45	A	50	LYS	1	0.926	0.955	2.399	-7.021	-4.107	3.093	-2.451	-3.556	-0.031
46	A	51	ILE	0	0.001	-0.008	3.859	-0.805	-0.620	0.008	-0.036	-0.157	0.000
47	A	52	SER	0	-0.022	-0.002	6.591	0.554	0.554	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.024	-0.019	9.270	-0.185	-0.185	0.000	0.000	0.000	0.000
49	A	54	LEU	0	-0.029	0.011	12.531	0.067	0.067	0.000	0.000	0.000	0.000
50	A	55	GLU	-1	-0.896	-0.961	15.649	0.310	0.310	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.955	-1.005	18.223	0.136	0.136	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.040	-0.019	21.576	0.003	0.003	0.000	0.000	0.000	0.000
53	A	58	GLU	-1	-0.818	-0.877	17.812	0.463	0.463	0.000	0.000	0.000	0.000
54	A	59	GLU	-1	-0.985	-0.992	20.621	0.208	0.208	0.000	0.000	0.000	0.000
55	A	60	VAL	0	-0.016	-0.021	17.218	0.042	0.042	0.000	0.000	0.000	0.000
56	A	61	PRO	0	0.048	0.038	14.186	-0.032	-0.032	0.000	0.000	0.000	0.000
57	A	62	SER	0	0.007	-0.015	17.371	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	63	PHE	0	-0.003	-0.002	17.674	-0.023	-0.023	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.005	0.012	13.373	0.040	0.040	0.000	0.000	0.000	0.000
60	A	65	ILE	0	0.013	-0.002	15.335	-0.045	-0.045	0.000	0.000	0.000	0.000
61	A	66	LYS	1	0.757	0.873	13.484	-0.332	-0.332	0.000	0.000	0.000	0.000
62	A	67	ALA	0	0.030	0.001	16.812	-0.046	-0.046	0.000	0.000	0.000	0.000
63	A	68	LEU	0	-0.006	0.011	18.863	0.026	0.026	0.000	0.000	0.000	0.000
64	A	69	THR	0	0.014	-0.016	21.233	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	70	PRO	0	0.004	0.003	23.653	0.004	0.004	0.000	0.000	0.000	0.000
66	A	71	LYS	1	0.813	0.897	25.264	-0.259	-0.259	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.913	-0.957	25.015	0.173	0.173	0.000	0.000	0.000	0.000
68	A	73	ASN	0	-0.074	-0.038	24.299	0.012	0.012	0.000	0.000	0.000	0.000
69	A	74	ALA	0	0.078	0.022	20.073	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	75	VAL	0	-0.041	-0.015	21.613	0.023	0.023	0.000	0.000	0.000	0.000
71	A	76	ASP	-1	-0.851	-0.907	23.733	0.265	0.265	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.036	-0.010	19.534	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	78	PRO	0	-0.003	0.023	18.768	0.016	0.016	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.009	-0.017	11.468	0.045	0.045	0.000	0.000	0.000	0.000
75	A	80	GLY	0	-0.063	-0.043	13.981	0.013	0.013	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.839	-0.907	14.504	0.373	0.373	0.000	0.000	0.000	0.000
77	A	82	TRP	0	-0.103	-0.063	18.223	0.009	0.009	0.000	0.000	0.000	0.000
78	A	83	THR	0	-0.015	-0.022	20.604	-0.027	-0.027	0.000	0.000	0.000	0.000
79	A	84	ASP	-1	-0.853	-0.898	23.018	0.219	0.219	0.000	0.000	0.000	0.000
80	A	85	LEU	0	-0.017	-0.017	19.773	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	86	LYS	1	0.827	0.895	24.512	-0.218	-0.218	0.000	0.000	0.000	0.000
82	A	87	ASN	0	-0.053	-0.026	27.198	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	88	VAL	0	0.020	0.017	22.794	0.003	0.003	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.004	0.000	23.091	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	90	VAL	0	-0.017	-0.010	21.368	0.024	0.024	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.932	-0.967	18.921	0.251	0.251	0.000	0.000	0.000	0.000
87	A	92	GLU	-1	-0.855	-0.918	16.405	0.292	0.292	0.000	0.000	0.000	0.000
88	A	93	ILE	0	-0.041	-0.022	18.513	0.025	0.025	0.000	0.000	0.000	0.000
89	A	94	ASP	-1	-0.847	-0.901	14.865	0.316	0.316	0.000	0.000	0.000	0.000
90	A	95	TYR	0	-0.019	-0.019	16.940	0.028	0.028	0.000	0.000	0.000	0.000
91	A	96	LEU	0	-0.047	-0.020	12.991	0.012	0.012	0.000	0.000	0.000	0.000
92	A	97	ASP	-1	-0.814	-0.873	15.433	0.097	0.097	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.040	-0.046	16.462	0.037	0.037	0.000	0.000	0.000	0.000
94	A	99	TYR	0	-0.066	-0.051	16.449	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	100	GLY	0	0.010	0.003	17.839	0.001	0.001	0.000	0.000	0.000	0.000
96	A	101	ASP	-1	-0.843	-0.902	18.617	0.112	0.112	0.000	0.000	0.000	0.000
97	A	102	MET	0	-0.086	-0.027	12.966	0.042	0.042	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.856	0.930	14.898	-0.280	-0.280	0.000	0.000	0.000	0.000
99	A	104	ILE	0	0.012	-0.005	10.641	0.079	0.079	0.000	0.000	0.000	0.000
100	A	105	LEU	0	0.014	0.020	9.709	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	106	SER	0	0.011	0.002	9.140	0.032	0.032	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.783	-0.884	7.520	0.801	0.801	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.875	0.934	7.649	-0.330	-0.330	0.000	0.000	0.000	0.000
104	A	109	ASN	0	-0.012	-0.008	8.414	0.079	0.079	0.000	0.000	0.000	0.000
105	A	110	TRP	0	-0.010	0.001	2.192	-0.854	-0.644	2.289	-0.533	-1.966	-0.003
106	A	111	TYR	0	0.065	0.025	4.697	0.040	0.093	-0.001	-0.002	-0.050	0.000
107	A	112	LYS	1	0.812	0.895	5.017	-1.018	-0.882	-0.001	-0.007	-0.128	0.000
108	A	113	ILE	0	0.026	0.008	6.941	-0.184	-0.184	0.000	0.000	0.000	0.000
109	A	114	TYR	0	0.004	-0.004	9.354	0.317	0.317	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.027	0.012	11.881	-0.111	-0.111	0.000	0.000	0.000	0.000
111	A	116	PRO	0	0.094	0.051	14.433	0.055	0.055	0.000	0.000	0.000	0.000
112	A	117	TYR	0	0.108	0.040	16.917	-0.053	-0.053	0.000	0.000	0.000	0.000
113	A	118	SER	0	-0.029	-0.033	17.837	-0.030	-0.030	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.068	-0.053	18.415	-0.020	-0.020	0.000	0.000	0.000	0.000
115	A	120	VAL	0	-0.056	-0.032	14.027	-0.039	-0.039	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.923	0.990	16.363	-0.111	-0.111	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.883	0.937	18.426	-0.009	-0.009	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.960	1.010	15.793	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	124	ASN	0	-0.026	-0.023	13.740	-0.055	-0.055	0.000	0.000	0.000	0.000
120	A	125	ARG	1	0.884	0.903	6.990	1.500	1.500	0.000	0.000	0.000	0.000
121	A	126	ASN	0	0.000	-0.005	11.060	-0.097	-0.097	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.820	-0.898	13.569	-0.124	-0.124	0.000	0.000	0.000	0.000
123	A	128	LEU	0	0.008	0.004	10.693	0.025	0.025	0.000	0.000	0.000	0.000
124	A	129	VAL	0	0.012	0.004	8.548	0.015	0.015	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.854	-0.930	11.226	-0.225	-0.225	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.916	-0.957	14.850	-0.046	-0.046	0.000	0.000	0.000	0.000
127	A	132	PHE	0	0.010	-0.002	8.911	0.028	0.028	0.000	0.000	0.000	0.000
128	A	133	MET	0	-0.010	0.003	11.488	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	134	LYS	1	0.780	0.900	13.676	0.163	0.163	0.000	0.000	0.000	0.000
130	A	135	TYR	0	0.002	-0.015	12.482	0.015	0.015	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.011	-0.007	11.564	0.007	0.007	0.000	0.000	0.000	0.000
132	A	137	PHE	0	0.000	-0.006	14.508	0.007	0.007	0.000	0.000	0.000	0.000
133	A	138	GLU	-1	-0.834	-0.894	17.550	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	139	SER	0	-0.089	-0.055	15.802	0.016	0.016	0.000	0.000	0.000	0.000
135	A	140	LYS	1	0.850	0.931	13.196	0.074	0.074	0.000	0.000	0.000	0.000
136	A	141	GLY	0	-0.029	0.007	18.851	0.002	0.002	0.000	0.000	0.000	0.000
137	A	142	TRP	0	-0.040	-0.024	16.402	-0.012	-0.012	0.000	0.000	0.000	0.000
138	A	143	ASN	0	0.038	0.004	21.706	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	144	PRO	0	0.085	0.028	19.152	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	145	GLY	0	-0.003	0.011	20.588	-0.022	-0.022	0.000	0.000	0.000	0.000
141	A	146	GLU	-1	-0.905	-0.951	22.855	-0.126	-0.126	0.000	0.000	0.000	0.000
142	A	147	TYR	0	-0.035	-0.027	18.012	0.000	0.000	0.000	0.000	0.000	0.000
143	A	148	THR	0	-0.026	-0.010	18.495	0.008	0.008	0.000	0.000	0.000	0.000
144	A	149	PHE	0	0.012	-0.008	12.475	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.029	-0.011	12.281	0.073	0.073	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.011	-0.011	7.918	-0.047	-0.047	0.000	0.000	0.000	0.000
147	A	152	GLN	0	0.017	0.011	7.972	0.321	0.321	0.000	0.000	0.000	0.000
148	A	153	GLU	-1	-0.792	-0.870	5.032	-2.515	-2.515	0.000	0.000	0.000	0.000
149	A	154	ILE	0	-0.045	-0.014	2.119	-1.044	0.157	3.751	-1.107	-3.845	-0.006

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ILE)