FMO DATABASE

FMODB ID: 762MK

Calculation Name: 2OX7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OX7

Chain ID: A

ChEMBL ID:

UniProt ID: Q835D7

Base Structure: X-ray

Registration Date: 2023-09-21

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1292222.168446
FMO2-HF: Nuclear repulsion	1233391.494484
FMO2-HF: Total energy	-58830.673963
FMO2-MP2: Total energy	-59002.224123

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-3.327	-0.913	-0.022	-1.198	-1.195	0.002

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.017

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	4	ILE	0	-0.031	-0.010	3.806	-0.815	1.599	-0.022	-1.198	-1.195	0.002
4	A	5	PRO	0	0.000	0.018	5.764	-0.127	-0.127	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.925	0.958	8.775	0.487	0.487	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.015	-0.006	11.792	-0.138	-0.138	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.826	0.896	15.139	0.440	0.440	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.002	-0.017	18.666	-0.031	-0.031	0.000	0.000	0.000	0.000
9	A	10	TRP	0	0.043	0.029	21.845	0.019	0.019	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.743	-0.860	25.139	-0.133	-0.133	0.000	0.000	0.000	0.000
11	A	12	THR	0	0.008	-0.019	28.004	0.003	0.003	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.071	-0.024	30.444	0.008	0.008	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.886	-0.976	31.406	-0.083	-0.083	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.658	0.840	31.121	0.124	0.124	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.879	-0.929	28.829	-0.110	-0.110	0.000	0.000	0.000	0.000
16	A	17	MET	0	-0.049	-0.012	22.919	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.016	-0.008	23.244	0.015	0.015	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.874	-0.972	18.634	-0.305	-0.305	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.097	-0.038	15.491	0.009	0.009	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.058	0.042	17.648	0.038	0.038	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.057	-0.040	15.889	-0.032	-0.032	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.002	0.014	15.878	0.031	0.031	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.018	-0.016	17.990	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.004	-0.011	17.241	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.824	-0.914	21.139	-0.121	-0.121	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.906	-0.961	21.629	-0.112	-0.112	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.116	-0.057	22.684	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.098	-0.049	19.130	-0.027	-0.027	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.029	0.028	21.504	-0.019	-0.019	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.058	-0.014	21.497	0.001	0.001	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.009	-0.009	23.016	0.012	0.012	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.007	-0.011	24.023	0.018	0.018	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.004	0.012	21.340	-0.024	-0.024	0.000	0.000	0.000	0.000
34	A	35	ILE	0	0.012	0.009	20.748	0.021	0.021	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.001	-0.018	20.905	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.860	-0.898	22.167	-0.054	-0.054	0.000	0.000	0.000	0.000
37	A	38	PHE	0	-0.024	-0.016	16.908	0.007	0.007	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.033	-0.010	22.148	0.019	0.019	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.001	0.004	19.894	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.831	0.940	23.362	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.061	0.026	26.924	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.014	-0.013	28.167	0.008	0.008	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.059	0.033	26.161	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	GLY	0	-0.040	-0.014	25.859	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.101	-0.061	27.353	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.027	-0.005	24.086	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.938	-0.977	25.594	0.032	0.032	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.001	-0.003	20.436	0.008	0.008	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.858	-0.935	23.994	0.010	0.010	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.003	-0.017	23.975	0.001	0.001	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.013	0.002	25.471	0.003	0.003	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.012	-0.030	26.108	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.046	-0.028	25.466	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.700	-0.798	26.523	-0.092	-0.092	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.072	-0.051	26.922	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.072	0.011	28.553	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.074	-0.026	30.293	0.004	0.004	0.000	0.000	0.000	0.000
58	A	59	ASN	0	-0.112	-0.060	32.280	0.009	0.009	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.028	-0.028	31.468	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.955	-0.957	34.127	-0.083	-0.083	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.988	-1.007	31.255	-0.126	-0.126	0.000	0.000	0.000	0.000
62	A	63	PHE	0	-0.019	-0.008	24.819	0.001	0.001	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.019	0.037	28.433	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	65	TYR	0	-0.034	-0.038	24.405	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.036	-0.011	22.321	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.000	-0.011	16.954	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.045	0.009	17.266	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.037	-0.032	9.816	-0.062	-0.062	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.051	-0.047	10.988	-0.087	-0.087	0.000	0.000	0.000	0.000
70	A	71	THR	0	-0.027	-0.055	10.135	-0.262	-0.262	0.000	0.000	0.000	0.000
71	A	72	GLY	0	-0.014	-0.005	7.574	-0.545	-0.545	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.088	-0.034	8.412	0.155	0.155	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.876	0.929	10.764	0.534	0.534	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.735	-0.873	13.919	-0.311	-0.311	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.782	0.862	17.422	0.203	0.203	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.055	-0.027	19.955	0.040	0.040	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.056	-0.027	16.675	0.031	0.031	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.003	0.007	16.713	0.015	0.015	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.883	-0.912	11.767	-0.557	-0.557	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.022	0.021	13.899	0.056	0.056	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.033	0.013	13.788	-0.184	-0.184	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.838	-0.919	14.575	-0.656	-0.656	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.052	0.024	16.945	0.047	0.047	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.783	-0.862	18.606	-0.369	-0.369	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.005	0.002	20.752	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.021	-0.010	17.914	0.013	0.013	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.021	-0.018	22.497	0.019	0.019	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.023	-0.039	23.790	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.801	-0.877	25.168	-0.145	-0.145	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.005	0.005	26.902	0.014	0.014	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.011	-0.014	29.918	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.913	0.952	33.112	0.117	0.117	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.947	0.973	34.735	0.105	0.105	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.035	-0.005	38.132	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.015	-0.006	40.629	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	HIS	0	0.035	0.036	36.883	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.814	0.892	33.830	0.130	0.130	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.802	0.892	28.345	0.170	0.170	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.005	0.013	28.117	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.040	0.012	26.333	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	102	HIS	1	0.783	0.895	22.473	0.288	0.288	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.795	-0.892	21.688	-0.334	-0.334	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.062	-0.022	15.567	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	105	ALA	0	0.092	0.049	17.735	0.025	0.025	0.000	0.000	0.000	0.000
105	A	106	TYR	0	0.034	0.003	10.963	-0.035	-0.035	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.026	-0.017	15.448	0.087	0.087	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.975	-0.989	15.875	-0.438	-0.438	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.024	0.019	12.311	0.022	0.022	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.850	0.945	10.829	0.373	0.373	0.000	0.000	0.000	0.000
110	A	111	PHE	0	0.079	0.036	8.742	0.102	0.102	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.096	-0.060	13.035	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	113	TRP	0	-0.011	-0.005	15.973	0.000	0.000	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.872	-0.946	19.061	-0.326	-0.326	0.000	0.000	0.000	0.000
114	A	115	PHE	0	0.014	-0.003	22.195	0.020	0.020	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.035	-0.024	21.323	0.028	0.028	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.902	-0.928	21.528	-0.289	-0.289	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.071	-0.043	19.688	0.021	0.021	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.001	0.007	14.056	-0.027	-0.027	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.067	0.049	12.172	0.031	0.031	0.000	0.000	0.000	0.000
120	A	121	CYS	0	0.004	-0.001	11.572	-0.113	-0.113	0.000	0.000	0.000	0.000
121	A	122	GLN	0	0.074	0.033	10.436	0.045	0.045	0.000	0.000	0.000	0.000
122	A	123	SER	0	0.016	-0.003	12.429	0.085	0.085	0.000	0.000	0.000	0.000
123	A	124	ASN	0	-0.034	-0.047	15.147	0.111	0.111	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.026	0.007	13.605	0.065	0.065	0.000	0.000	0.000	0.000
125	A	126	LEU	0	0.005	0.002	15.268	0.055	0.055	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.004	0.022	18.595	0.060	0.060	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.875	0.923	20.827	0.165	0.165	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.860	-0.897	24.316	-0.151	-0.151	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.039	0.041	21.292	0.006	0.006	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.000	-0.016	19.721	0.022	0.022	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.051	-0.022	20.585	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	133	VAL	0	0.032	0.011	18.946	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.101	-0.062	21.951	0.029	0.029	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.058	0.032	24.277	0.024	0.024	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.059	-0.041	22.861	-0.029	-0.029	0.000	0.000	0.000	0.000
136	A	137	ILE	0	0.024	-0.001	23.406	0.025	0.025	0.000	0.000	0.000	0.000
137	A	138	HIS	0	0.003	0.006	22.937	0.034	0.034	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.831	-0.902	25.546	-0.182	-0.182	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.095	-0.046	27.807	0.004	0.004	0.000	0.000	0.000	0.000
140	A	141	PRO	0	0.061	0.043	29.882	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.950	-0.975	31.008	-0.126	-0.126	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.077	-0.034	27.810	0.005	0.005	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.005	-0.018	26.220	0.002	0.002	0.000	0.000	0.000	0.000
144	A	145	GLU	-1	-0.901	-0.904	30.351	-0.128	-0.128	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)