FMO DATABASE

FMODB ID: 6N9GZ

Calculation Name: 1OZ7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OZ7

Chain ID: A

ChEMBL ID:

UniProt ID: Q7T248

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1165304.014806
FMO2-HF: Nuclear repulsion	1109660.343066
FMO2-HF: Total energy	-55643.67174
FMO2-MP2: Total energy	-55799.56489

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:1:MET)

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

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.
-6.161	-1.537	1.298	-2.197	-3.728	-0.006

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : 0.005

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

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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	3	PRO	0	0.034	0.018	2.749	-5.054	-1.748	1.094	-1.760	-2.641	-0.007
4	A	4	PRO	0	0.021	-0.006	3.986	-0.152	-0.021	-0.001	-0.008	-0.123	0.000
5	A	5	GLY	0	0.018	0.015	6.259	0.264	0.264	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.011	-0.010	6.874	0.225	0.225	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.034	0.027	7.065	-0.226	-0.226	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.048	-0.054	4.144	-0.392	-0.291	-0.001	-0.036	-0.065	0.000
9	A	9	ASN	0	-0.023	-0.022	6.049	0.472	0.472	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.009	0.008	8.029	-0.126	-0.126	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.035	-0.018	4.531	-0.055	0.019	-0.001	-0.003	-0.070	0.000
12	A	12	TYR	0	0.050	0.027	6.100	-0.350	-0.350	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.058	-0.063	6.833	0.343	0.343	0.000	0.000	0.000	0.000
14	A	15	MET	0	0.022	0.014	10.087	-0.116	-0.116	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.004	0.012	12.658	0.069	0.069	0.000	0.000	0.000	0.000
16	A	17	PHE	0	0.067	0.023	13.466	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.858	0.935	18.585	0.207	0.207	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.870	-0.942	19.975	-0.215	-0.215	0.000	0.000	0.000	0.000
19	A	20	PRO	0	-0.063	-0.041	23.223	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.842	0.927	22.037	0.190	0.190	0.000	0.000	0.000	0.000
21	A	22	THR	0	0.018	-0.002	26.794	0.003	0.003	0.000	0.000	0.000	0.000
22	A	23	TRP	0	-0.017	-0.003	24.037	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.815	-0.927	24.715	-0.114	-0.114	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.901	-0.937	25.279	-0.131	-0.131	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.009	0.003	21.876	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.730	-0.843	20.256	-0.208	-0.208	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.841	0.908	20.513	0.100	0.100	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.000	-0.005	16.438	0.014	0.014	0.000	0.000	0.000	0.000
29	A	30	CYS	0	-0.027	0.020	14.092	0.026	0.026	0.000	0.000	0.000	0.000
30	A	31	ASN	0	-0.050	-0.010	16.147	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.886	0.943	17.257	0.168	0.168	0.000	0.000	0.000	0.000
32	A	33	GLN	0	-0.047	-0.012	12.376	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.043	0.024	11.546	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.865	0.940	12.622	0.056	0.056	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.847	-0.926	12.994	-0.151	-0.151	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.000	0.010	13.421	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	38	HIS	1	0.751	0.830	14.143	0.242	0.242	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.044	0.012	15.846	-0.052	-0.052	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.070	-0.027	15.747	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.012	-0.018	16.589	0.023	0.023	0.000	0.000	0.000	0.000
41	A	42	ILE	0	-0.016	-0.010	16.486	-0.030	-0.030	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.758	-0.849	15.515	-0.154	-0.154	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.025	-0.021	16.429	0.030	0.030	0.000	0.000	0.000	0.000
44	A	45	LYS	1	1.005	1.006	18.712	0.014	0.014	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.926	0.962	14.580	-0.054	-0.054	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.759	-0.836	13.385	-0.254	-0.254	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.797	-0.899	15.612	-0.146	-0.146	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.020	-0.011	18.081	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.061	-0.017	10.771	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.048	0.014	14.751	-0.047	-0.047	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.752	-0.856	16.215	-0.138	-0.138	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.003	0.020	15.857	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.042	0.028	12.574	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.020	0.003	15.982	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.078	-0.056	18.947	0.011	0.011	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.934	-0.948	15.517	-0.326	-0.326	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.069	-0.048	15.411	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.017	0.006	18.483	0.003	0.003	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.018	0.004	21.652	0.023	0.023	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.858	0.925	24.002	0.174	0.174	0.000	0.000	0.000	0.000
61	A	62	MET	0	0.017	0.007	26.500	0.005	0.005	0.000	0.000	0.000	0.000
62	A	63	TYR	0	0.037	0.023	27.494	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.886	0.954	27.335	0.097	0.097	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.002	0.006	20.724	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	66	TRP	0	-0.031	-0.016	22.765	0.007	0.007	0.000	0.000	0.000	0.000
66	A	67	THR	0	-0.002	-0.010	20.745	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.042	0.015	20.469	0.009	0.009	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.086	-0.027	21.652	0.011	0.011	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.002	-0.012	24.679	0.002	0.002	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.848	-0.926	27.389	-0.049	-0.049	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.878	0.924	27.191	0.051	0.051	0.000	0.000	0.000	0.000
72	A	73	SER	0	0.037	0.036	31.846	0.001	0.001	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.874	0.932	33.643	0.036	0.036	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.756	-0.870	36.908	-0.040	-0.040	0.000	0.000	0.000	0.000
75	A	76	GLN	0	-0.037	-0.024	38.789	0.002	0.002	0.000	0.000	0.000	0.000
76	A	77	HIS	0	-0.085	-0.049	38.419	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	CYS	0	-0.069	-0.033	36.820	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	SER	0	0.006	0.007	39.421	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.022	0.021	41.034	0.001	0.001	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.835	0.897	43.065	0.015	0.015	0.000	0.000	0.000	0.000
81	A	82	TRP	0	0.048	0.040	45.810	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.038	-0.023	48.032	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.817	-0.905	49.743	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	85	GLY	0	-0.013	-0.003	50.662	0.000	0.000	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.040	-0.026	48.084	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	PHE	0	-0.015	0.004	44.139	0.001	0.001	0.000	0.000	0.000	0.000
87	A	88	PHE	0	0.004	-0.003	46.888	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.930	0.970	49.282	0.022	0.022	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.008	-0.026	46.482	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.084	-0.067	49.109	0.001	0.001	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.808	-0.860	43.953	-0.035	-0.035	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.010	-0.005	46.700	0.000	0.000	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.004	0.006	42.972	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	95	ILE	0	-0.067	-0.040	40.829	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.858	0.926	36.582	0.072	0.072	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.007	0.026	37.546	0.001	0.001	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.029	-0.045	34.191	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.846	-0.924	32.561	-0.065	-0.065	0.000	0.000	0.000	0.000
99	A	100	CYS	0	0.022	0.028	27.939	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	101	PHE	0	0.043	0.010	26.593	0.007	0.007	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.042	-0.006	25.107	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.036	0.027	20.014	0.010	0.010	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.817	-0.913	24.748	-0.086	-0.086	0.000	0.000	0.000	0.000
104	A	105	LYN	0	-0.007	-0.012	26.948	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	GLN	0	-0.021	-0.008	28.029	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.016	-0.007	28.778	0.004	0.004	0.000	0.000	0.000	0.000
107	A	108	VAL	0	-0.022	-0.018	24.343	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.031	-0.033	22.373	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.818	0.888	21.959	0.089	0.089	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.053	-0.026	24.163	0.010	0.010	0.000	0.000	0.000	0.000
111	A	112	TRP	0	-0.035	-0.045	22.331	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.029	-0.012	27.123	0.009	0.009	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.042	0.023	29.529	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.032	-0.030	29.403	0.002	0.002	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.011	0.014	32.024	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.777	-0.897	30.238	-0.086	-0.086	0.000	0.000	0.000	0.000
117	A	119	ASN	0	-0.092	-0.028	31.682	0.003	0.003	0.000	0.000	0.000	0.000
118	A	120	THR	0	0.024	0.008	29.389	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.013	0.001	26.423	0.003	0.003	0.000	0.000	0.000	0.000
120	A	122	PRO	0	-0.031	-0.012	22.922	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.031	0.011	18.592	0.012	0.012	0.000	0.000	0.000	0.000
122	A	124	MET	0	0.001	0.017	12.462	-0.036	-0.036	0.000	0.000	0.000	0.000
123	A	126	LYS	1	0.818	0.879	11.482	0.174	0.174	0.000	0.000	0.000	0.000
124	A	127	TYR	0	0.040	0.021	6.562	0.004	0.004	0.000	0.000	0.000	0.000
125	A	128	PRO	0	0.009	0.029	7.911	-0.264	-0.264	0.000	0.000	0.000	0.000
126	A	129	VAL	0	0.066	0.020	2.576	-0.583	0.429	0.207	-0.390	-0.829	0.001
127	A	130	PRO	0	-0.053	-0.026	5.871	0.395	0.395	0.000	0.000	0.000	0.000
128	A	131	ARG	1	0.932	0.980	8.636	0.158	0.158	0.000	0.000	0.000	0.000

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