FMO DATABASE

FMODB ID: YYG82

Calculation Name: 1OZ9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OZ9

Chain ID: A

ChEMBL ID:

UniProt ID: O67367

Base Structure: X-ray

Registration Date: 2023-06-20

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	OptAll
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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1370702.686989
FMO2-HF: Nuclear repulsion	1314573.73222
FMO2-HF: Total energy	-56128.954769
FMO2-MP2: Total energy	-56296.850901

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:8:LYS)

Summations of interaction energy for fragment #1(A:8:LYS)

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.
-62.582	-61.662	12.68	-7.356	-6.244	-0.073

Interaction energy analysis for fragmet #1(A:8:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.929 / q_NPA : 0.961

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	10	ARG	1	0.887	0.939	3.856	20.188	22.477	-0.017	-1.350	-0.922	0.004
4	A	11	VAL	0	0.032	0.019	6.667	2.095	2.095	0.000	0.000	0.000	0.000
5	A	12	LEU	0	-0.048	-0.020	8.932	0.740	0.740	0.000	0.000	0.000	0.000
6	A	13	VAL	0	-0.016	-0.001	12.041	1.127	1.127	0.000	0.000	0.000	0.000
7	A	14	LYS	1	0.943	0.971	14.509	14.836	14.836	0.000	0.000	0.000	0.000
8	A	15	LEU	0	0.006	-0.003	18.030	0.104	0.104	0.000	0.000	0.000	0.000
9	A	16	LYS	1	0.802	0.889	21.058	10.248	10.248	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.791	0.889	24.735	9.947	9.947	0.000	0.000	0.000	0.000
11	A	18	ARG	1	0.913	0.935	22.814	10.706	10.706	0.000	0.000	0.000	0.000
12	A	19	LYS	1	0.817	0.908	23.962	9.423	9.423	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.032	0.015	19.300	0.064	0.064	0.000	0.000	0.000	0.000
14	A	21	ARG	1	0.841	0.883	17.141	14.147	14.147	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.835	0.903	12.749	17.219	17.219	0.000	0.000	0.000	0.000
16	A	23	ASP	-1	-0.716	-0.835	13.378	-16.331	-16.331	0.000	0.000	0.000	0.000
17	A	24	LYS	1	0.784	0.883	12.810	12.327	12.327	0.000	0.000	0.000	0.000
18	A	25	ILE	0	0.035	0.016	13.822	-0.790	-0.790	0.000	0.000	0.000	0.000
19	A	26	GLU	-1	-0.751	-0.861	9.431	-20.158	-20.158	0.000	0.000	0.000	0.000
20	A	27	LYS	1	0.999	1.003	9.212	20.043	20.043	0.000	0.000	0.000	0.000
21	A	28	TRP	0	-0.001	-0.015	9.772	-1.223	-1.223	0.000	0.000	0.000	0.000
22	A	29	ALA	0	0.051	0.030	10.421	-0.634	-0.634	0.000	0.000	0.000	0.000
23	A	30	GLU	-1	-0.923	-0.962	4.320	-36.329	-36.179	-0.001	-0.029	-0.121	0.000
24	A	31	LEU	0	-0.061	-0.034	6.405	-3.098	-3.098	0.000	0.000	0.000	0.000
25	A	32	ALA	0	0.017	0.008	8.893	-0.679	-0.679	0.000	0.000	0.000	0.000
26	A	33	LEU	0	0.011	0.005	5.889	-0.211	-0.211	0.000	0.000	0.000	0.000
27	A	34	SER	0	0.011	0.000	4.926	-4.848	-4.726	-0.001	-0.003	-0.117	0.000
28	A	35	ALA	0	-0.080	-0.035	6.387	-0.318	-0.318	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.020	-0.009	9.729	1.540	1.540	0.000	0.000	0.000	0.000
30	A	37	GLY	0	0.001	0.018	6.685	1.061	1.061	0.000	0.000	0.000	0.000
31	A	38	LEU	0	-0.018	0.001	6.312	-3.405	-3.405	0.000	0.000	0.000	0.000
32	A	39	ASN	0	-0.019	-0.015	1.736	-50.983	-53.197	12.699	-5.727	-4.758	-0.078
33	A	40	ASN	0	0.003	0.004	3.918	4.736	5.309	0.000	-0.247	-0.326	0.001
34	A	41	VAL	0	0.025	0.018	5.627	4.882	4.882	0.000	0.000	0.000	0.000
35	A	42	GLU	-1	-0.813	-0.866	7.134	-23.268	-23.268	0.000	0.000	0.000	0.000
36	A	43	LEU	0	-0.003	-0.002	9.862	0.988	0.988	0.000	0.000	0.000	0.000
37	A	44	SER	0	-0.021	-0.021	11.602	-0.538	-0.538	0.000	0.000	0.000	0.000
38	A	45	VAL	0	-0.014	-0.008	13.178	0.120	0.120	0.000	0.000	0.000	0.000
39	A	46	TYR	0	-0.094	-0.067	15.911	0.088	0.088	0.000	0.000	0.000	0.000
40	A	47	ILE	0	0.024	0.022	18.757	0.353	0.353	0.000	0.000	0.000	0.000
41	A	48	THR	0	0.040	-0.013	21.750	0.409	0.409	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.788	-0.889	25.349	-9.565	-9.565	0.000	0.000	0.000	0.000
43	A	50	ASP	-1	-0.728	-0.823	28.986	-9.525	-9.525	0.000	0.000	0.000	0.000
44	A	51	GLN	0	-0.042	-0.013	31.295	0.183	0.183	0.000	0.000	0.000	0.000
45	A	52	GLU	-1	-0.682	-0.794	26.447	-10.704	-10.704	0.000	0.000	0.000	0.000
46	A	53	ILE	0	-0.023	-0.006	25.072	-0.067	-0.067	0.000	0.000	0.000	0.000
47	A	54	ARG	1	0.864	0.934	28.531	8.051	8.051	0.000	0.000	0.000	0.000
48	A	55	GLU	-1	-0.929	-0.961	31.495	-8.793	-8.793	0.000	0.000	0.000	0.000
49	A	56	LEU	0	-0.007	0.012	25.106	0.028	0.028	0.000	0.000	0.000	0.000
50	A	57	ASN	0	0.012	-0.014	29.072	-0.230	-0.230	0.000	0.000	0.000	0.000
51	A	58	LYS	1	0.841	0.910	30.298	8.046	8.046	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.051	-0.038	30.620	0.221	0.221	0.000	0.000	0.000	0.000
53	A	60	TYR	0	-0.018	-0.018	27.570	0.071	0.071	0.000	0.000	0.000	0.000
54	A	61	ARG	1	0.936	0.974	24.403	11.377	11.377	0.000	0.000	0.000	0.000
55	A	62	LYS	1	0.931	0.982	30.937	8.727	8.727	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.852	0.939	30.704	9.975	9.975	0.000	0.000	0.000	0.000
57	A	64	ASP	-1	-0.793	-0.870	33.844	-8.148	-8.148	0.000	0.000	0.000	0.000
58	A	65	LYS	1	0.942	0.957	34.151	8.763	8.763	0.000	0.000	0.000	0.000
59	A	66	PRO	0	0.009	0.009	31.732	-0.211	-0.211	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.004	-0.004	27.074	0.253	0.253	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.763	-0.871	25.853	-11.226	-11.226	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.039	-0.032	20.594	-0.354	-0.354	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.060	-0.019	22.747	0.384	0.384	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.018	-0.003	19.563	-0.497	-0.497	0.000	0.000	0.000	0.000
65	A	72	PHE	0	-0.037	-0.019	19.636	0.650	0.650	0.000	0.000	0.000	0.000
66	A	73	PRO	0	0.044	0.020	18.120	-0.585	-0.585	0.000	0.000	0.000	0.000
67	A	74	MET	0	-0.030	-0.016	17.529	0.847	0.847	0.000	0.000	0.000	0.000
68	A	75	GLY	0	0.002	0.002	16.680	0.517	0.517	0.000	0.000	0.000	0.000
69	A	76	GLU	-1	-0.914	-0.949	17.403	-15.046	-15.046	0.000	0.000	0.000	0.000
70	A	77	GLU	-1	-0.875	-0.932	14.483	-20.817	-20.817	0.000	0.000	0.000	0.000
71	A	78	PHE	0	-0.023	-0.010	13.703	1.015	1.015	0.000	0.000	0.000	0.000
72	A	79	GLY	0	-0.003	-0.002	13.486	-1.004	-1.004	0.000	0.000	0.000	0.000
73	A	80	GLY	0	0.029	0.013	12.431	-0.858	-0.858	0.000	0.000	0.000	0.000
74	A	81	TYR	0	-0.085	-0.050	6.710	-3.333	-3.333	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.824	0.885	10.183	21.448	21.448	0.000	0.000	0.000	0.000
76	A	83	ILE	0	0.021	0.015	11.107	-1.838	-1.838	0.000	0.000	0.000	0.000
77	A	84	LEU	0	-0.007	-0.002	10.077	0.894	0.894	0.000	0.000	0.000	0.000
78	A	85	GLY	0	0.054	0.017	13.695	1.363	1.363	0.000	0.000	0.000	0.000
79	A	86	ASP	-1	-0.886	-0.920	14.927	-16.239	-16.239	0.000	0.000	0.000	0.000
80	A	87	VAL	0	0.009	0.003	15.596	0.469	0.469	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.038	-0.019	17.999	-0.028	-0.028	0.000	0.000	0.000	0.000
82	A	89	ILE	0	0.017	0.005	18.839	0.167	0.167	0.000	0.000	0.000	0.000
83	A	90	SER	0	-0.016	-0.016	22.732	0.128	0.128	0.000	0.000	0.000	0.000
84	A	91	GLN	0	0.018	-0.026	25.363	-0.285	-0.285	0.000	0.000	0.000	0.000
85	A	92	ASP	-1	-0.804	-0.895	26.397	-9.326	-9.326	0.000	0.000	0.000	0.000
86	A	93	THR	0	-0.034	-0.046	29.046	0.344	0.344	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.029	0.023	25.365	0.060	0.060	0.000	0.000	0.000	0.000
88	A	95	GLU	-1	-0.830	-0.909	27.321	-9.610	-9.610	0.000	0.000	0.000	0.000
89	A	96	ARG	1	0.791	0.902	29.656	9.088	9.088	0.000	0.000	0.000	0.000
90	A	97	GLN	0	0.000	-0.018	27.276	0.389	0.389	0.000	0.000	0.000	0.000
91	A	98	ALA	0	-0.018	-0.012	27.557	0.017	0.017	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.789	0.856	29.293	8.496	8.496	0.000	0.000	0.000	0.000
93	A	100	GLU	-1	-0.820	-0.891	33.029	-8.368	-8.368	0.000	0.000	0.000	0.000
94	A	101	LEU	0	-0.047	-0.012	28.793	0.104	0.104	0.000	0.000	0.000	0.000
95	A	102	GLY	0	0.004	0.029	31.853	-0.035	-0.035	0.000	0.000	0.000	0.000
96	A	103	HIS	0	-0.073	-0.053	26.502	-0.053	-0.053	0.000	0.000	0.000	0.000
97	A	104	SER	0	0.020	0.004	24.785	0.077	0.077	0.000	0.000	0.000	0.000
98	A	105	LEU	0	0.053	0.013	24.406	-0.243	-0.243	0.000	0.000	0.000	0.000
99	A	106	GLU	-1	-0.815	-0.897	21.154	-13.356	-13.356	0.000	0.000	0.000	0.000
100	A	107	GLU	-1	-0.775	-0.865	20.796	-14.271	-14.271	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.796	-0.881	22.023	-11.814	-11.814	0.000	0.000	0.000	0.000
102	A	109	VAL	0	-0.017	-0.019	18.841	-0.362	-0.362	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.833	0.921	16.571	14.284	14.284	0.000	0.000	0.000	0.000
104	A	111	ARG	1	0.848	0.917	17.513	11.564	11.564	0.000	0.000	0.000	0.000
105	A	112	LEU	0	0.012	0.011	19.487	-0.400	-0.400	0.000	0.000	0.000	0.000
106	A	113	ILE	0	-0.015	-0.007	13.882	-0.261	-0.261	0.000	0.000	0.000	0.000
107	A	114	VAL	0	-0.023	-0.006	14.600	-0.700	-0.700	0.000	0.000	0.000	0.000
108	A	115	HIS	0	0.028	-0.001	16.173	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.021	0.004	18.102	0.143	0.143	0.000	0.000	0.000	0.000
110	A	117	ILE	0	-0.006	-0.016	11.290	-0.209	-0.209	0.000	0.000	0.000	0.000
111	A	118	VAL	0	-0.023	-0.009	14.972	-0.547	-0.547	0.000	0.000	0.000	0.000
112	A	119	HIS	0	-0.017	-0.009	17.286	0.143	0.143	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.084	-0.031	14.750	0.170	0.170	0.000	0.000	0.000	0.000
114	A	121	LEU	0	-0.072	-0.028	12.582	-0.547	-0.547	0.000	0.000	0.000	0.000
115	A	122	GLY	0	-0.015	0.002	16.558	0.144	0.144	0.000	0.000	0.000	0.000
116	A	123	TYR	0	-0.043	-0.012	17.633	0.847	0.847	0.000	0.000	0.000	0.000
117	A	124	ASP	-1	-0.771	-0.907	21.880	-11.319	-11.319	0.000	0.000	0.000	0.000
118	A	125	HIS	0	-0.065	-0.036	24.664	0.217	0.217	0.000	0.000	0.000	0.000
119	A	126	GLU	-1	-0.866	-0.935	27.144	-9.634	-9.634	0.000	0.000	0.000	0.000
120	A	127	LYS	1	0.759	0.871	29.471	10.674	10.674	0.000	0.000	0.000	0.000
121	A	128	GLY	0	0.045	0.032	30.483	0.327	0.327	0.000	0.000	0.000	0.000
122	A	129	GLY	0	-0.007	-0.015	30.545	-0.222	-0.222	0.000	0.000	0.000	0.000
123	A	130	GLU	-1	-0.814	-0.909	27.291	-11.767	-11.767	0.000	0.000	0.000	0.000
124	A	131	GLU	-1	-0.810	-0.882	26.522	-11.243	-11.243	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.792	-0.873	25.575	-11.112	-11.112	0.000	0.000	0.000	0.000
126	A	133	LYS	1	0.786	0.889	25.902	11.297	11.297	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.837	0.898	21.789	13.565	13.565	0.000	0.000	0.000	0.000
128	A	135	PHE	0	0.002	0.020	21.381	-0.818	-0.818	0.000	0.000	0.000	0.000
129	A	136	ARG	1	0.781	0.851	21.457	11.168	11.168	0.000	0.000	0.000	0.000
130	A	137	GLU	-1	-0.818	-0.883	22.001	-13.510	-13.510	0.000	0.000	0.000	0.000
131	A	138	LEU	0	0.000	0.005	15.576	-0.717	-0.717	0.000	0.000	0.000	0.000
132	A	139	GLU	-1	-0.779	-0.878	17.595	-14.334	-14.334	0.000	0.000	0.000	0.000
133	A	140	ASN	0	-0.024	-0.032	18.850	-0.294	-0.294	0.000	0.000	0.000	0.000
134	A	141	TYR	0	-0.015	0.000	12.024	0.014	0.014	0.000	0.000	0.000	0.000
135	A	142	VAL	0	0.034	0.017	13.063	-0.718	-0.718	0.000	0.000	0.000	0.000
136	A	143	LEU	0	0.007	0.001	15.422	-0.476	-0.476	0.000	0.000	0.000	0.000
137	A	144	SER	0	-0.040	-0.017	17.643	0.110	0.110	0.000	0.000	0.000	0.000
138	A	145	LYS	1	0.881	0.940	11.607	24.216	24.216	0.000	0.000	0.000	0.000
139	A	146	LEU	0	-0.030	-0.009	12.183	-0.374	-0.374	0.000	0.000	0.000	0.000
140	A	147	SER	0	-0.095	-0.048	15.267	1.076	1.076	0.000	0.000	0.000	0.000
141	A	148	LYS	1	0.900	0.961	14.900	16.744	16.744	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:LYS)