FMO DATABASE

FMODB ID: 53V1Z

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1367238.320698
FMO2-HF: Nuclear repulsion	1311109.703931
FMO2-HF: Total energy	-56128.616767
FMO2-MP2: Total energy	-56296.555037

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.
-63.513	-62.596	12.046	-7.046	-5.915	-0.064

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 : 0.923 / q_NPA : 0.958

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	0.893	0.944	3.687	20.116	22.705	-0.022	-1.483	-1.083	0.005
4	A	11	VAL	0	0.028	0.016	6.103	1.794	1.794	0.000	0.000	0.000	0.000
5	A	12	LEU	0	-0.050	-0.017	8.690	0.987	0.987	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.011	0.011	11.797	0.844	0.844	0.000	0.000	0.000	0.000
7	A	14	LYS	1	0.934	0.964	14.535	14.493	14.493	0.000	0.000	0.000	0.000
8	A	15	LEU	0	-0.005	-0.003	18.059	0.139	0.139	0.000	0.000	0.000	0.000
9	A	16	LYS	1	0.818	0.897	20.995	10.184	10.184	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.796	0.895	24.225	9.937	9.937	0.000	0.000	0.000	0.000
11	A	18	ARG	1	0.931	0.944	22.610	10.739	10.739	0.000	0.000	0.000	0.000
12	A	19	LYS	1	0.868	0.939	24.318	9.515	9.515	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.016	0.015	19.433	0.053	0.053	0.000	0.000	0.000	0.000
14	A	21	ARG	1	0.843	0.879	17.475	13.829	13.829	0.000	0.000	0.000	0.000
15	A	22	LYS	1	0.894	0.930	12.442	17.363	17.363	0.000	0.000	0.000	0.000
16	A	23	ASP	-1	-0.739	-0.845	13.685	-16.148	-16.148	0.000	0.000	0.000	0.000
17	A	24	LYS	1	0.781	0.878	13.207	12.355	12.355	0.000	0.000	0.000	0.000
18	A	25	ILE	0	0.024	0.015	14.207	-0.719	-0.719	0.000	0.000	0.000	0.000
19	A	26	GLU	-1	-0.785	-0.889	9.511	-20.171	-20.171	0.000	0.000	0.000	0.000
20	A	27	LYS	1	1.019	1.019	9.570	18.963	18.963	0.000	0.000	0.000	0.000
21	A	28	TRP	0	-0.018	-0.023	10.054	-1.222	-1.222	0.000	0.000	0.000	0.000
22	A	29	ALA	0	0.051	0.030	10.609	-0.732	-0.732	0.000	0.000	0.000	0.000
23	A	30	GLU	-1	-0.919	-0.961	5.524	-32.481	-32.481	0.000	0.000	0.000	0.000
24	A	31	LEU	0	-0.070	-0.045	6.429	-3.107	-3.107	0.000	0.000	0.000	0.000
25	A	32	ALA	0	0.018	0.007	8.833	-0.808	-0.808	0.000	0.000	0.000	0.000
26	A	33	LEU	0	0.018	0.008	6.200	-0.396	-0.396	0.000	0.000	0.000	0.000
27	A	34	SER	0	0.001	-0.003	5.338	-4.658	-4.658	0.000	0.000	0.000	0.000
28	A	35	ALA	0	-0.100	-0.042	6.469	-0.576	-0.576	0.000	0.000	0.000	0.000
29	A	36	LEU	0	-0.016	-0.023	9.546	1.460	1.460	0.000	0.000	0.000	0.000
30	A	37	GLY	0	-0.018	0.010	6.717	1.033	1.033	0.000	0.000	0.000	0.000
31	A	38	LEU	0	-0.018	0.002	6.528	-2.524	-2.524	0.000	0.000	0.000	0.000
32	A	39	ASN	0	-0.020	-0.015	1.735	-50.939	-53.369	12.068	-5.296	-4.342	-0.070
33	A	40	ASN	0	-0.008	0.002	3.705	4.806	5.430	0.001	-0.261	-0.364	0.001
34	A	41	VAL	0	0.033	0.024	5.386	4.644	4.778	-0.001	-0.006	-0.126	0.000
35	A	42	GLU	-1	-0.813	-0.855	6.985	-23.289	-23.289	0.000	0.000	0.000	0.000
36	A	43	LEU	0	-0.005	-0.002	9.632	1.073	1.073	0.000	0.000	0.000	0.000
37	A	44	SER	0	0.009	-0.006	11.404	-0.664	-0.664	0.000	0.000	0.000	0.000
38	A	45	VAL	0	-0.023	-0.008	13.290	0.389	0.389	0.000	0.000	0.000	0.000
39	A	46	TYR	0	-0.097	-0.075	16.013	0.136	0.136	0.000	0.000	0.000	0.000
40	A	47	ILE	0	0.022	0.016	19.019	0.192	0.192	0.000	0.000	0.000	0.000
41	A	48	THR	0	0.025	-0.018	21.864	0.407	0.407	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.824	-0.903	25.305	-9.566	-9.566	0.000	0.000	0.000	0.000
43	A	50	ASP	-1	-0.715	-0.824	29.000	-9.468	-9.468	0.000	0.000	0.000	0.000
44	A	51	GLN	0	-0.034	-0.015	31.375	0.084	0.084	0.000	0.000	0.000	0.000
45	A	52	GLU	-1	-0.700	-0.816	26.481	-10.631	-10.631	0.000	0.000	0.000	0.000
46	A	53	ILE	0	-0.023	-0.007	25.301	-0.036	-0.036	0.000	0.000	0.000	0.000
47	A	54	ARG	1	0.866	0.931	28.649	8.050	8.050	0.000	0.000	0.000	0.000
48	A	55	GLU	-1	-0.934	-0.955	31.329	-8.832	-8.832	0.000	0.000	0.000	0.000
49	A	56	LEU	0	0.004	0.011	25.221	0.027	0.027	0.000	0.000	0.000	0.000
50	A	57	ASN	0	0.008	-0.016	29.212	-0.220	-0.220	0.000	0.000	0.000	0.000
51	A	58	LYS	1	0.856	0.921	30.537	7.991	7.991	0.000	0.000	0.000	0.000
52	A	59	THR	0	-0.044	-0.038	30.748	0.221	0.221	0.000	0.000	0.000	0.000
53	A	60	TYR	0	-0.015	-0.018	27.387	0.062	0.062	0.000	0.000	0.000	0.000
54	A	61	ARG	1	0.931	0.976	24.931	11.256	11.256	0.000	0.000	0.000	0.000
55	A	62	LYS	1	0.931	0.982	31.330	8.688	8.688	0.000	0.000	0.000	0.000
56	A	63	LYS	1	0.940	0.971	31.417	9.753	9.753	0.000	0.000	0.000	0.000
57	A	64	ASP	-1	-0.808	-0.877	34.045	-8.123	-8.123	0.000	0.000	0.000	0.000
58	A	65	LYS	1	0.960	0.969	34.202	8.687	8.687	0.000	0.000	0.000	0.000
59	A	66	PRO	0	0.020	0.019	31.817	-0.214	-0.214	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.002	-0.002	27.309	0.252	0.252	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.757	-0.883	25.948	-11.154	-11.154	0.000	0.000	0.000	0.000
62	A	69	VAL	0	-0.029	-0.027	20.578	-0.378	-0.378	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.064	-0.016	22.873	0.364	0.364	0.000	0.000	0.000	0.000
64	A	71	SER	0	0.018	0.008	19.344	-0.393	-0.393	0.000	0.000	0.000	0.000
65	A	72	PHE	0	-0.054	-0.042	19.686	0.682	0.682	0.000	0.000	0.000	0.000
66	A	73	PRO	0	0.053	0.027	18.365	-0.592	-0.592	0.000	0.000	0.000	0.000
67	A	74	MET	0	-0.019	-0.001	17.210	0.774	0.774	0.000	0.000	0.000	0.000
68	A	75	GLY	0	0.001	-0.011	16.588	0.536	0.536	0.000	0.000	0.000	0.000
69	A	76	GLU	-1	-0.936	-0.953	17.112	-15.053	-15.053	0.000	0.000	0.000	0.000
70	A	77	GLU	-1	-0.869	-0.925	14.299	-20.646	-20.646	0.000	0.000	0.000	0.000
71	A	78	PHE	0	-0.013	-0.008	13.370	1.049	1.049	0.000	0.000	0.000	0.000
72	A	79	GLY	0	0.004	0.000	12.899	-1.193	-1.193	0.000	0.000	0.000	0.000
73	A	80	GLY	0	0.010	-0.001	11.612	-1.047	-1.047	0.000	0.000	0.000	0.000
74	A	81	TYR	0	-0.102	-0.063	6.405	-3.319	-3.319	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.832	0.889	9.885	21.551	21.551	0.000	0.000	0.000	0.000
76	A	83	ILE	0	0.026	0.014	10.897	-1.854	-1.854	0.000	0.000	0.000	0.000
77	A	84	LEU	0	-0.008	0.002	10.290	1.091	1.091	0.000	0.000	0.000	0.000
78	A	85	GLY	0	0.028	0.010	13.724	1.287	1.287	0.000	0.000	0.000	0.000
79	A	86	ASP	-1	-0.878	-0.932	14.912	-16.337	-16.337	0.000	0.000	0.000	0.000
80	A	87	VAL	0	0.013	0.010	15.818	0.466	0.466	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.026	-0.011	18.081	-0.072	-0.072	0.000	0.000	0.000	0.000
82	A	89	ILE	0	0.019	0.010	18.953	0.250	0.250	0.000	0.000	0.000	0.000
83	A	90	SER	0	-0.034	-0.016	22.717	0.109	0.109	0.000	0.000	0.000	0.000
84	A	91	GLN	0	0.018	-0.034	25.453	-0.276	-0.276	0.000	0.000	0.000	0.000
85	A	92	ASP	-1	-0.798	-0.893	26.560	-9.233	-9.233	0.000	0.000	0.000	0.000
86	A	93	THR	0	-0.042	-0.044	28.867	0.314	0.314	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.049	0.029	25.371	0.085	0.085	0.000	0.000	0.000	0.000
88	A	95	GLU	-1	-0.868	-0.924	27.316	-9.600	-9.600	0.000	0.000	0.000	0.000
89	A	96	ARG	1	0.791	0.893	29.832	9.021	9.021	0.000	0.000	0.000	0.000
90	A	97	GLN	0	0.023	0.004	27.546	0.392	0.392	0.000	0.000	0.000	0.000
91	A	98	ALA	0	-0.020	-0.003	27.914	0.054	0.054	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.788	0.873	29.651	8.447	8.447	0.000	0.000	0.000	0.000
93	A	100	GLU	-1	-0.849	-0.922	33.365	-8.376	-8.376	0.000	0.000	0.000	0.000
94	A	101	LEU	0	-0.043	-0.022	28.764	0.110	0.110	0.000	0.000	0.000	0.000
95	A	102	GLY	0	-0.002	0.030	32.129	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	103	HIS	0	-0.083	-0.059	26.767	-0.084	-0.084	0.000	0.000	0.000	0.000
97	A	104	SER	0	0.013	0.001	25.168	0.037	0.037	0.000	0.000	0.000	0.000
98	A	105	LEU	0	0.083	0.031	24.744	-0.192	-0.192	0.000	0.000	0.000	0.000
99	A	106	GLU	-1	-0.833	-0.899	21.472	-13.268	-13.268	0.000	0.000	0.000	0.000
100	A	107	GLU	-1	-0.781	-0.861	21.346	-13.917	-13.917	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.780	-0.880	22.173	-11.712	-11.712	0.000	0.000	0.000	0.000
102	A	109	VAL	0	-0.023	-0.027	19.160	-0.305	-0.305	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.859	0.929	16.707	14.001	14.001	0.000	0.000	0.000	0.000
104	A	111	ARG	1	0.856	0.910	17.783	11.394	11.394	0.000	0.000	0.000	0.000
105	A	112	LEU	0	0.021	0.023	19.986	-0.310	-0.310	0.000	0.000	0.000	0.000
106	A	113	ILE	0	-0.021	-0.008	14.066	-0.298	-0.298	0.000	0.000	0.000	0.000
107	A	114	VAL	0	-0.029	-0.009	14.833	-0.719	-0.719	0.000	0.000	0.000	0.000
108	A	115	HIS	0	0.004	-0.008	16.423	-0.037	-0.037	0.000	0.000	0.000	0.000
109	A	116	GLY	0	0.019	-0.005	18.345	0.107	0.107	0.000	0.000	0.000	0.000
110	A	117	ILE	0	-0.011	-0.015	11.478	-0.237	-0.237	0.000	0.000	0.000	0.000
111	A	118	VAL	0	0.000	-0.004	15.185	-0.551	-0.551	0.000	0.000	0.000	0.000
112	A	119	HIS	0	-0.017	-0.009	17.187	0.027	0.027	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.077	-0.025	14.831	0.234	0.234	0.000	0.000	0.000	0.000
114	A	121	LEU	0	-0.104	-0.037	12.504	-0.479	-0.479	0.000	0.000	0.000	0.000
115	A	122	GLY	0	-0.025	-0.006	16.581	0.064	0.064	0.000	0.000	0.000	0.000
116	A	123	TYR	0	-0.054	-0.013	17.512	0.723	0.723	0.000	0.000	0.000	0.000
117	A	124	ASP	-1	-0.800	-0.927	21.943	-11.512	-11.512	0.000	0.000	0.000	0.000
118	A	125	HIS	0	-0.038	-0.024	24.677	0.347	0.347	0.000	0.000	0.000	0.000
119	A	126	GLU	-1	-0.961	-0.985	27.013	-9.742	-9.742	0.000	0.000	0.000	0.000
120	A	127	LYS	1	0.757	0.879	29.509	10.737	10.737	0.000	0.000	0.000	0.000
121	A	128	GLY	0	0.052	0.036	30.427	0.388	0.388	0.000	0.000	0.000	0.000
122	A	129	GLY	0	-0.017	-0.029	30.836	-0.239	-0.239	0.000	0.000	0.000	0.000
123	A	130	GLU	-1	-0.789	-0.900	27.582	-11.569	-11.569	0.000	0.000	0.000	0.000
124	A	131	GLU	-1	-0.791	-0.871	26.656	-11.275	-11.275	0.000	0.000	0.000	0.000
125	A	132	GLU	-1	-0.836	-0.893	25.843	-11.086	-11.086	0.000	0.000	0.000	0.000
126	A	133	LYS	1	0.801	0.903	26.233	11.007	11.007	0.000	0.000	0.000	0.000
127	A	134	LYS	1	0.848	0.904	22.136	13.371	13.371	0.000	0.000	0.000	0.000
128	A	135	PHE	0	-0.007	0.009	21.477	-0.767	-0.767	0.000	0.000	0.000	0.000
129	A	136	ARG	1	0.798	0.877	21.526	11.130	11.130	0.000	0.000	0.000	0.000
130	A	137	GLU	-1	-0.866	-0.919	22.233	-13.420	-13.420	0.000	0.000	0.000	0.000
131	A	138	LEU	0	-0.006	0.008	15.488	-0.711	-0.711	0.000	0.000	0.000	0.000
132	A	139	GLU	-1	-0.745	-0.869	17.698	-14.362	-14.362	0.000	0.000	0.000	0.000
133	A	140	ASN	0	0.001	-0.012	18.823	-0.331	-0.331	0.000	0.000	0.000	0.000
134	A	141	TYR	0	-0.042	-0.011	12.635	0.122	0.122	0.000	0.000	0.000	0.000
135	A	142	VAL	0	0.049	0.020	13.193	-0.749	-0.749	0.000	0.000	0.000	0.000
136	A	143	LEU	0	0.027	0.009	15.452	-0.474	-0.474	0.000	0.000	0.000	0.000
137	A	144	SER	0	-0.064	-0.036	17.815	0.062	0.062	0.000	0.000	0.000	0.000
138	A	145	LYS	1	0.887	0.937	12.444	22.642	22.642	0.000	0.000	0.000	0.000
139	A	146	LEU	0	-0.035	-0.004	12.158	-0.658	-0.658	0.000	0.000	0.000	0.000
140	A	147	SER	0	-0.081	-0.023	15.382	0.671	0.671	0.000	0.000	0.000	0.000
141	A	148	LYS	1	0.911	0.969	15.570	16.385	16.385	0.000	0.000	0.000	0.000

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