FMO DATABASE

FMODB ID: MNV9Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1291726.949992
FMO2-HF: Nuclear repulsion	1232897.199271
FMO2-HF: Total energy	-58829.750721
FMO2-MP2: Total energy	-59001.336166

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.
-3.565	-1.17	-0.022	-1.186	-1.187	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 : -0.044 / q_NPA : -0.023

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	-0.035	-0.013	3.806	-0.832	1.563	-0.022	-1.186	-1.187	0.002
4	A	5	PRO	0	0.012	0.020	5.817	-0.179	-0.179	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.927	0.968	8.816	0.378	0.378	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.009	-0.006	11.842	-0.149	-0.149	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.845	0.913	15.185	0.417	0.417	0.000	0.000	0.000	0.000
8	A	9	ALA	0	-0.004	-0.019	18.715	-0.034	-0.034	0.000	0.000	0.000	0.000
9	A	10	TRP	0	0.046	0.028	21.890	0.017	0.017	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.738	-0.874	25.136	-0.124	-0.124	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.044	-0.046	28.084	0.003	0.003	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.121	-0.057	30.442	0.006	0.006	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.921	-0.982	31.473	-0.075	-0.075	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.779	0.922	31.154	0.125	0.125	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.879	-0.931	29.042	-0.094	-0.094	0.000	0.000	0.000	0.000
16	A	17	MET	0	-0.037	-0.008	22.949	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.016	-0.002	23.149	0.019	0.019	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.914	-0.986	19.710	-0.242	-0.242	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.076	-0.044	15.460	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.060	0.050	17.700	0.035	0.035	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.058	-0.042	15.982	-0.024	-0.024	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.004	0.013	15.890	0.027	0.027	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.026	-0.023	18.013	0.002	0.002	0.000	0.000	0.000	0.000
24	A	25	PHE	0	0.000	-0.008	17.629	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.809	-0.899	21.123	-0.120	-0.120	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.886	-0.955	21.616	-0.118	-0.118	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.159	-0.113	22.677	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.086	-0.019	19.327	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.031	0.030	21.500	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.056	-0.011	21.529	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.006	-0.007	23.024	0.012	0.012	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.006	-0.008	24.046	0.018	0.018	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.001	0.009	21.325	-0.023	-0.023	0.000	0.000	0.000	0.000
34	A	35	ILE	0	0.005	0.008	20.721	0.020	0.020	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.005	-0.015	20.945	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.869	-0.925	22.214	-0.024	-0.024	0.000	0.000	0.000	0.000
37	A	38	PHE	0	-0.019	-0.011	17.158	0.005	0.005	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.006	-0.008	22.189	0.021	0.021	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.022	0.003	20.081	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.869	0.951	23.391	-0.051	-0.051	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.059	0.028	26.945	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.004	-0.009	28.187	0.009	0.009	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.044	0.027	26.147	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	GLY	0	-0.033	-0.010	25.868	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.103	-0.062	27.356	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.054	-0.018	23.405	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.899	-0.956	25.612	0.046	0.046	0.000	0.000	0.000	0.000
48	A	49	ILE	0	-0.006	-0.007	20.592	0.011	0.011	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.918	-0.969	24.017	0.020	0.020	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.008	-0.014	23.991	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.002	0.008	25.505	0.001	0.001	0.000	0.000	0.000	0.000
52	A	53	SER	0	0.004	-0.010	26.708	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.046	-0.027	25.506	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.712	-0.821	26.560	-0.082	-0.082	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.079	-0.051	26.953	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.080	0.017	28.508	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.074	-0.030	30.311	0.003	0.003	0.000	0.000	0.000	0.000
58	A	59	ASN	0	-0.120	-0.056	32.053	0.009	0.009	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.006	-0.001	31.784	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.958	-0.960	34.117	-0.081	-0.081	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.995	-1.011	31.182	-0.124	-0.124	0.000	0.000	0.000	0.000
62	A	63	PHE	0	-0.008	-0.002	24.836	0.002	0.002	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.044	0.049	28.428	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	65	TYR	0	-0.043	-0.051	24.408	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.037	-0.011	22.313	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.010	-0.017	16.943	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.037	0.019	17.289	-0.018	-0.018	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.051	-0.042	9.318	-0.173	-0.173	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.068	-0.096	11.066	-0.076	-0.076	0.000	0.000	0.000	0.000
70	A	71	THR	0	-0.020	-0.037	10.135	-0.259	-0.259	0.000	0.000	0.000	0.000
71	A	72	GLY	0	-0.006	-0.002	7.430	-0.560	-0.560	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.096	-0.043	8.481	0.158	0.158	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.949	0.976	10.626	0.369	0.369	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.732	-0.861	13.811	-0.303	-0.303	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.779	0.860	17.304	0.197	0.197	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.056	-0.030	19.859	0.043	0.043	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.078	-0.038	16.610	0.033	0.033	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.007	0.008	16.477	0.025	0.025	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.906	-0.885	11.194	-0.494	-0.494	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.014	0.011	13.762	0.047	0.047	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.025	0.012	13.630	-0.171	-0.171	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.848	-0.923	14.674	-0.622	-0.622	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.060	0.026	17.002	0.050	0.050	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.787	-0.882	18.469	-0.346	-0.346	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.001	0.006	20.735	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.030	-0.014	17.751	0.014	0.014	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.024	-0.015	22.342	0.015	0.015	0.000	0.000	0.000	0.000
88	A	89	TYR	0	0.023	0.019	23.675	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.861	-0.919	25.029	-0.137	-0.137	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.006	0.011	26.770	0.014	0.014	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.015	-0.013	29.787	0.005	0.005	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.934	0.980	32.989	0.113	0.113	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.951	0.971	34.599	0.102	0.102	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.024	-0.012	37.991	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.028	-0.008	40.511	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	97	HIS	0	0.038	0.032	36.778	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.965	0.976	33.827	0.121	0.121	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.879	0.939	29.559	0.158	0.158	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.005	0.005	27.931	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.039	0.013	26.347	-0.011	-0.011	0.000	0.000	0.000	0.000
101	A	102	HIS	1	0.825	0.923	22.435	0.297	0.297	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.787	-0.883	21.830	-0.335	-0.335	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.069	-0.027	15.707	-0.027	-0.027	0.000	0.000	0.000	0.000
104	A	105	ALA	0	0.105	0.057	17.883	0.026	0.026	0.000	0.000	0.000	0.000
105	A	106	TYR	0	0.036	0.005	10.969	-0.035	-0.035	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.025	-0.018	15.514	0.090	0.090	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.985	-0.992	15.922	-0.492	-0.492	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.028	0.021	12.305	0.017	0.017	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.875	0.950	10.852	0.398	0.398	0.000	0.000	0.000	0.000
110	A	111	PHE	0	0.085	0.037	9.211	0.102	0.102	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.095	-0.064	13.157	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	113	TRP	0	-0.008	-0.002	16.108	0.006	0.006	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.908	-0.960	19.216	-0.337	-0.337	0.000	0.000	0.000	0.000
114	A	115	PHE	0	-0.003	-0.017	22.335	0.021	0.021	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.027	-0.023	21.228	0.030	0.030	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.910	-0.930	21.662	-0.304	-0.304	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.072	-0.048	19.729	0.020	0.020	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.003	0.007	14.282	-0.028	-0.028	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.056	0.045	12.745	0.031	0.031	0.000	0.000	0.000	0.000
120	A	121	CYS	0	0.012	0.005	11.586	-0.122	-0.122	0.000	0.000	0.000	0.000
121	A	122	GLN	0	0.063	0.016	10.343	0.057	0.057	0.000	0.000	0.000	0.000
122	A	123	SER	0	-0.002	-0.009	12.306	0.098	0.098	0.000	0.000	0.000	0.000
123	A	124	ASN	0	0.003	-0.031	15.048	0.116	0.116	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.041	0.003	13.409	0.067	0.067	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.003	-0.001	15.164	0.058	0.058	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.020	0.008	18.492	0.059	0.059	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.881	0.932	20.724	0.169	0.169	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.858	-0.933	24.220	-0.146	-0.146	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.018	0.025	21.171	0.006	0.006	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.000	-0.010	19.528	0.021	0.021	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.045	-0.031	20.455	-0.008	-0.008	0.000	0.000	0.000	0.000
132	A	133	VAL	0	0.040	0.019	18.905	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.105	-0.064	21.803	0.030	0.030	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.054	0.035	24.121	0.024	0.024	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.047	-0.025	22.872	-0.033	-0.033	0.000	0.000	0.000	0.000
136	A	137	ILE	0	0.019	-0.002	23.656	0.026	0.026	0.000	0.000	0.000	0.000
137	A	138	HIS	0	0.005	0.007	23.312	0.030	0.030	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.858	-0.921	25.908	-0.159	-0.159	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.101	-0.052	27.824	0.003	0.003	0.000	0.000	0.000	0.000
140	A	141	PRO	0	0.064	0.041	29.927	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.952	-0.979	31.058	-0.123	-0.123	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.091	-0.037	27.740	0.004	0.004	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.014	-0.024	26.388	0.001	0.001	0.000	0.000	0.000	0.000
144	A	145	GLU	-1	-1.046	-1.004	30.514	-0.134	-0.134	0.000	0.000	0.000	0.000

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