FMO DATABASE

FMODB ID: 43V1N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1365704.013939
FMO2-HF: Nuclear repulsion	1309576.52693
FMO2-HF: Total energy	-56127.487008
FMO2-MP2: Total energy	-56295.392477

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.
-63.059	-62.908	10.632	-5.023	-5.76	-0.051

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 : 0.913 / q_NPA : 0.943

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	0.929	0.982	3.546	20.544	22.365	-0.016	-0.960	-0.845	-0.001
4	A	11	VAL	0	0.046	0.022	5.892	1.626	1.626	0.000	0.000	0.000	0.000
5	A	12	LEU	0	-0.050	-0.013	8.588	1.049	1.049	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.031	0.015	11.665	0.794	0.794	0.000	0.000	0.000	0.000
7	A	14	LYS	1	0.925	0.954	14.464	14.250	14.250	0.000	0.000	0.000	0.000
8	A	15	LEU	0	-0.002	-0.003	17.968	0.130	0.130	0.000	0.000	0.000	0.000
9	A	16	LYS	1	0.959	0.993	20.944	10.044	10.044	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.874	0.944	24.175	9.998	9.998	0.000	0.000	0.000	0.000
11	A	18	ARG	1	0.958	0.958	22.361	10.835	10.835	0.000	0.000	0.000	0.000
12	A	19	LYS	1	0.939	0.994	24.281	9.519	9.519	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.030	0.023	19.308	0.071	0.071	0.000	0.000	0.000	0.000
14	A	21	ARG	1	0.840	0.897	17.635	13.910	13.910	0.000	0.000	0.000	0.000
15	A	22	LYS	1	1.000	0.997	13.615	15.894	15.894	0.000	0.000	0.000	0.000
16	A	23	ASP	-1	-0.730	-0.850	13.611	-16.009	-16.009	0.000	0.000	0.000	0.000
17	A	24	LYS	1	0.827	0.916	13.149	12.503	12.503	0.000	0.000	0.000	0.000
18	A	25	ILE	0	0.020	0.014	14.163	-0.713	-0.713	0.000	0.000	0.000	0.000
19	A	26	GLU	-1	-0.918	-0.964	8.995	-22.153	-22.153	0.000	0.000	0.000	0.000
20	A	27	LYS	1	1.027	1.019	9.507	18.323	18.323	0.000	0.000	0.000	0.000
21	A	28	TRP	0	-0.034	-0.026	10.033	-1.276	-1.276	0.000	0.000	0.000	0.000
22	A	29	ALA	0	0.042	0.024	10.312	-0.729	-0.729	0.000	0.000	0.000	0.000
23	A	30	GLU	-1	-0.914	-0.960	5.630	-32.093	-32.093	0.000	0.000	0.000	0.000
24	A	31	LEU	0	-0.070	-0.047	6.328	-3.209	-3.209	0.000	0.000	0.000	0.000
25	A	32	ALA	0	0.013	0.009	8.756	-0.771	-0.771	0.000	0.000	0.000	0.000
26	A	33	LEU	0	0.014	0.004	6.051	-0.445	-0.445	0.000	0.000	0.000	0.000
27	A	34	SER	0	-0.032	-0.013	4.996	-3.866	-3.866	0.000	0.000	0.000	0.000
28	A	35	ALA	0	-0.049	-0.024	6.244	-0.302	-0.302	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.028	-0.028	9.280	1.494	1.494	0.000	0.000	0.000	0.000
30	A	37	GLY	0	-0.021	0.010	6.418	1.113	1.113	0.000	0.000	0.000	0.000
31	A	38	LEU	0	-0.016	0.002	6.361	-2.720	-2.720	0.000	0.000	0.000	0.000
32	A	39	ASN	0	-0.039	-0.037	1.912	-48.496	-50.698	10.647	-3.899	-4.545	-0.050
33	A	40	ASN	0	0.002	0.007	3.721	4.987	5.519	0.001	-0.164	-0.370	0.000
34	A	41	VAL	0	0.014	0.017	5.402	5.012	5.012	0.000	0.000	0.000	0.000
35	A	42	GLU	-1	-0.848	-0.903	6.985	-22.127	-22.127	0.000	0.000	0.000	0.000
36	A	43	LEU	0	-0.004	0.003	9.507	0.945	0.945	0.000	0.000	0.000	0.000
37	A	44	SER	0	0.009	0.008	11.198	-0.485	-0.485	0.000	0.000	0.000	0.000
38	A	45	VAL	0	-0.001	-0.002	13.074	0.350	0.350	0.000	0.000	0.000	0.000
39	A	46	TYR	0	-0.113	-0.077	15.788	0.162	0.162	0.000	0.000	0.000	0.000
40	A	47	ILE	0	0.019	0.017	18.944	0.166	0.166	0.000	0.000	0.000	0.000
41	A	48	THR	0	-0.004	-0.042	21.725	0.400	0.400	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.903	-0.962	25.236	-9.567	-9.567	0.000	0.000	0.000	0.000
43	A	50	ASP	-1	-0.704	-0.837	28.818	-9.488	-9.488	0.000	0.000	0.000	0.000
44	A	51	GLN	0	-0.049	-0.027	31.160	0.086	0.086	0.000	0.000	0.000	0.000
45	A	52	GLU	-1	-0.737	-0.828	26.414	-10.730	-10.730	0.000	0.000	0.000	0.000
46	A	53	ILE	0	-0.029	-0.012	25.086	-0.040	-0.040	0.000	0.000	0.000	0.000
47	A	54	ARG	1	0.861	0.931	28.436	8.069	8.069	0.000	0.000	0.000	0.000
48	A	55	GLU	-1	-0.955	-0.966	31.109	-8.960	-8.960	0.000	0.000	0.000	0.000
49	A	56	LEU	0	0.009	0.003	24.972	0.027	0.027	0.000	0.000	0.000	0.000
50	A	57	ASN	0	0.007	-0.015	29.005	-0.232	-0.232	0.000	0.000	0.000	0.000
51	A	58	LYS	1	0.921	0.968	30.343	8.020	8.020	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.044	-0.029	30.441	0.228	0.228	0.000	0.000	0.000	0.000
53	A	60	TYR	0	-0.008	-0.011	26.996	0.063	0.063	0.000	0.000	0.000	0.000
54	A	61	ARG	1	0.935	0.981	24.383	11.303	11.303	0.000	0.000	0.000	0.000
55	A	62	LYS	1	0.925	0.978	31.158	8.647	8.647	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.941	0.968	31.947	9.637	9.637	0.000	0.000	0.000	0.000
57	A	64	ASP	-1	-0.867	-0.919	33.855	-8.167	-8.167	0.000	0.000	0.000	0.000
58	A	65	LYS	1	0.944	0.964	33.769	8.716	8.716	0.000	0.000	0.000	0.000
59	A	66	PRO	0	0.041	0.027	31.616	-0.220	-0.220	0.000	0.000	0.000	0.000
60	A	67	THR	0	0.001	-0.005	27.098	0.249	0.249	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.746	-0.876	25.693	-11.211	-11.211	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.047	-0.032	20.405	-0.393	-0.393	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.052	-0.020	22.676	0.340	0.340	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.012	-0.005	18.937	-0.421	-0.421	0.000	0.000	0.000	0.000
65	A	72	PHE	0	-0.053	-0.031	19.508	0.684	0.684	0.000	0.000	0.000	0.000
66	A	73	PRO	0	0.061	0.032	18.213	-0.609	-0.609	0.000	0.000	0.000	0.000
67	A	74	MET	0	-0.022	-0.002	17.091	0.775	0.775	0.000	0.000	0.000	0.000
68	A	75	GLY	0	-0.002	-0.014	16.551	0.524	0.524	0.000	0.000	0.000	0.000
69	A	76	GLU	-1	-0.931	-0.944	17.128	-14.898	-14.898	0.000	0.000	0.000	0.000
70	A	77	GLU	-1	-0.882	-0.950	14.608	-20.231	-20.231	0.000	0.000	0.000	0.000
71	A	78	PHE	0	0.000	-0.003	13.873	1.051	1.051	0.000	0.000	0.000	0.000
72	A	79	GLY	0	0.006	-0.002	13.222	-1.124	-1.124	0.000	0.000	0.000	0.000
73	A	80	GLY	0	0.002	-0.004	11.627	-0.998	-0.998	0.000	0.000	0.000	0.000
74	A	81	TYR	0	-0.099	-0.056	7.246	-3.288	-3.288	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.839	0.900	9.900	21.416	21.416	0.000	0.000	0.000	0.000
76	A	83	ILE	0	0.013	0.010	10.897	-1.831	-1.831	0.000	0.000	0.000	0.000
77	A	84	LEU	0	-0.012	-0.004	10.227	1.077	1.077	0.000	0.000	0.000	0.000
78	A	85	GLY	0	0.029	0.014	13.582	1.281	1.281	0.000	0.000	0.000	0.000
79	A	86	ASP	-1	-0.874	-0.940	14.716	-16.276	-16.276	0.000	0.000	0.000	0.000
80	A	87	VAL	0	0.002	0.001	15.668	0.433	0.433	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.033	-0.013	17.881	-0.084	-0.084	0.000	0.000	0.000	0.000
82	A	89	ILE	0	0.023	0.011	18.838	0.239	0.239	0.000	0.000	0.000	0.000
83	A	90	SER	0	-0.027	-0.014	22.511	0.097	0.097	0.000	0.000	0.000	0.000
84	A	91	GLN	0	0.055	-0.007	25.345	-0.397	-0.397	0.000	0.000	0.000	0.000
85	A	92	ASP	-1	-0.832	-0.911	26.361	-9.253	-9.253	0.000	0.000	0.000	0.000
86	A	93	THR	0	-0.068	-0.045	28.482	0.301	0.301	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.042	0.025	25.169	0.080	0.080	0.000	0.000	0.000	0.000
88	A	95	GLU	-1	-0.970	-1.004	27.131	-9.540	-9.540	0.000	0.000	0.000	0.000
89	A	96	ARG	1	0.784	0.884	29.648	9.094	9.094	0.000	0.000	0.000	0.000
90	A	97	GLN	0	0.034	0.012	27.272	0.444	0.444	0.000	0.000	0.000	0.000
91	A	98	ALA	0	-0.022	0.000	27.783	0.054	0.054	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.905	0.945	29.495	8.509	8.509	0.000	0.000	0.000	0.000
93	A	100	GLU	-1	-0.993	-1.004	33.188	-8.566	-8.566	0.000	0.000	0.000	0.000
94	A	101	LEU	0	-0.028	-0.018	28.637	0.104	0.104	0.000	0.000	0.000	0.000
95	A	102	GLY	0	-0.013	0.025	32.009	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	103	HIS	0	-0.087	-0.064	26.413	-0.067	-0.067	0.000	0.000	0.000	0.000
97	A	104	SER	0	0.007	-0.002	25.087	0.051	0.051	0.000	0.000	0.000	0.000
98	A	105	LEU	0	0.082	0.030	24.688	-0.195	-0.195	0.000	0.000	0.000	0.000
99	A	106	GLU	-1	-0.888	-0.947	21.389	-13.237	-13.237	0.000	0.000	0.000	0.000
100	A	107	GLU	-1	-0.826	-0.886	21.193	-14.027	-14.027	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.780	-0.875	22.035	-11.866	-11.866	0.000	0.000	0.000	0.000
102	A	109	VAL	0	-0.021	-0.025	18.954	-0.311	-0.311	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.889	0.957	16.558	14.289	14.289	0.000	0.000	0.000	0.000
104	A	111	ARG	1	0.880	0.903	17.640	11.432	11.432	0.000	0.000	0.000	0.000
105	A	112	LEU	0	0.024	0.027	19.851	-0.320	-0.320	0.000	0.000	0.000	0.000
106	A	113	ILE	0	-0.031	-0.011	13.845	-0.294	-0.294	0.000	0.000	0.000	0.000
107	A	114	VAL	0	-0.034	-0.013	14.785	-0.732	-0.732	0.000	0.000	0.000	0.000
108	A	115	HIS	0	0.004	-0.007	16.295	-0.077	-0.077	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.014	-0.007	18.180	0.109	0.109	0.000	0.000	0.000	0.000
110	A	117	ILE	0	-0.014	-0.015	11.290	-0.240	-0.240	0.000	0.000	0.000	0.000
111	A	118	VAL	0	-0.004	-0.004	15.046	-0.559	-0.559	0.000	0.000	0.000	0.000
112	A	119	HIS	0	-0.012	-0.004	17.089	-0.023	-0.023	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.069	-0.023	14.355	0.208	0.208	0.000	0.000	0.000	0.000
114	A	121	LEU	0	-0.107	-0.038	12.512	-0.517	-0.517	0.000	0.000	0.000	0.000
115	A	122	GLY	0	-0.027	-0.008	16.499	0.050	0.050	0.000	0.000	0.000	0.000
116	A	123	TYR	0	-0.061	-0.015	17.312	0.698	0.698	0.000	0.000	0.000	0.000
117	A	124	ASP	-1	-0.800	-0.927	21.871	-11.611	-11.611	0.000	0.000	0.000	0.000
118	A	125	HIS	0	-0.064	-0.039	24.612	0.370	0.370	0.000	0.000	0.000	0.000
119	A	126	GLU	-1	-0.958	-0.980	26.927	-9.973	-9.973	0.000	0.000	0.000	0.000
120	A	127	LYS	1	0.801	0.920	29.420	10.693	10.693	0.000	0.000	0.000	0.000
121	A	128	GLY	0	0.046	0.034	30.352	0.394	0.394	0.000	0.000	0.000	0.000
122	A	129	GLY	0	-0.013	-0.029	30.702	-0.240	-0.240	0.000	0.000	0.000	0.000
123	A	130	GLU	-1	-0.908	-0.969	27.485	-11.505	-11.505	0.000	0.000	0.000	0.000
124	A	131	GLU	-1	-0.840	-0.916	26.456	-11.533	-11.533	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.922	-0.943	25.652	-10.860	-10.860	0.000	0.000	0.000	0.000
126	A	133	LYS	1	0.934	0.981	26.095	10.866	10.866	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.932	0.954	21.864	13.489	13.489	0.000	0.000	0.000	0.000
128	A	135	PHE	0	0.011	0.015	21.377	-0.766	-0.766	0.000	0.000	0.000	0.000
129	A	136	ARG	1	0.890	0.925	21.474	11.395	11.395	0.000	0.000	0.000	0.000
130	A	137	GLU	-1	-0.951	-0.970	22.114	-13.371	-13.371	0.000	0.000	0.000	0.000
131	A	138	LEU	0	-0.006	0.008	15.461	-0.704	-0.704	0.000	0.000	0.000	0.000
132	A	139	GLU	-1	-0.741	-0.870	17.525	-14.597	-14.597	0.000	0.000	0.000	0.000
133	A	140	ASN	0	0.006	-0.008	18.769	-0.440	-0.440	0.000	0.000	0.000	0.000
134	A	141	TYR	0	-0.028	-0.004	12.607	0.217	0.217	0.000	0.000	0.000	0.000
135	A	142	VAL	0	0.050	0.037	13.223	-0.744	-0.744	0.000	0.000	0.000	0.000
136	A	143	LEU	0	0.023	0.008	15.414	-0.481	-0.481	0.000	0.000	0.000	0.000
137	A	144	SER	0	-0.092	-0.070	17.764	0.034	0.034	0.000	0.000	0.000	0.000
138	A	145	LYS	1	0.900	0.941	12.840	21.703	21.703	0.000	0.000	0.000	0.000
139	A	146	LEU	0	-0.038	-0.006	12.095	-0.631	-0.631	0.000	0.000	0.000	0.000
140	A	147	SER	0	-0.080	-0.062	15.189	0.731	0.731	0.000	0.000	0.000	0.000
141	A	148	LYS	1	0.922	1.016	15.308	16.398	16.398	0.000	0.000	0.000	0.000

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