FMO DATABASE

FMODB ID: 2NJLR

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1291037.891632
FMO2-HF: Nuclear repulsion	1232206.832264
FMO2-HF: Total energy	-58831.059367
FMO2-MP2: Total energy	-59002.494435

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.
-2.98	-0.793	-0.013	-1.114	-1.061	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 : -0.022 / q_NPA : -0.014

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	-0.015	-0.003	3.876	-0.612	1.575	-0.013	-1.114	-1.061	0.002
4	A	5	PRO	0	-0.007	0.007	6.000	-0.183	-0.183	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.908	0.954	8.768	0.546	0.546	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.018	-0.004	11.810	-0.140	-0.140	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.805	0.874	15.165	0.455	0.455	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.003	-0.017	18.774	-0.028	-0.028	0.000	0.000	0.000	0.000
9	A	10	TRP	0	0.053	0.027	22.006	0.016	0.016	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.786	-0.885	25.173	-0.133	-0.133	0.000	0.000	0.000	0.000
11	A	12	THR	0	0.001	-0.015	28.083	0.004	0.004	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.030	0.005	30.432	0.009	0.009	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.908	-0.977	31.780	-0.086	-0.086	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.668	0.834	31.341	0.125	0.125	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.850	-0.929	29.106	-0.126	-0.126	0.000	0.000	0.000	0.000
16	A	17	MET	0	-0.067	-0.010	23.306	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.014	0.005	23.558	0.013	0.013	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.833	-0.951	18.302	-0.346	-0.346	0.000	0.000	0.000	0.000
19	A	20	ASN	0	-0.090	-0.049	15.593	0.009	0.009	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.031	0.045	17.535	0.036	0.036	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.057	-0.039	16.359	-0.028	-0.028	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.010	0.016	16.189	0.032	0.032	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.021	-0.017	18.156	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.001	-0.010	17.424	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.783	-0.877	21.578	-0.104	-0.104	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.909	-0.958	21.908	-0.094	-0.094	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.112	-0.054	22.517	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.100	-0.056	19.006	-0.031	-0.031	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.001	-0.003	21.510	-0.022	-0.022	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.071	-0.018	21.808	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	32	ILE	0	-0.013	-0.014	23.232	0.011	0.011	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.007	-0.008	24.134	0.017	0.017	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.004	0.013	21.433	-0.024	-0.024	0.000	0.000	0.000	0.000
34	A	35	ILE	0	0.002	0.000	21.060	0.022	0.022	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.007	-0.027	21.065	-0.022	-0.022	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.844	-0.884	22.125	-0.069	-0.069	0.000	0.000	0.000	0.000
37	A	38	PHE	0	-0.027	-0.018	17.308	0.009	0.009	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.040	-0.023	22.595	0.016	0.016	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.010	-0.002	20.299	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.835	0.943	23.977	-0.031	-0.031	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.063	0.031	27.332	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.009	-0.007	28.866	0.004	0.004	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.025	-0.004	26.392	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.001	0.013	26.144	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.108	-0.066	27.546	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.024	0.001	24.736	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.930	-0.966	25.912	0.032	0.032	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.006	-0.007	20.520	0.008	0.008	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.857	-0.927	24.353	0.004	0.004	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.015	-0.006	23.897	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.027	-0.006	25.852	0.004	0.004	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.044	-0.028	26.030	0.003	0.003	0.000	0.000	0.000	0.000
53	A	54	TYR	0	-0.031	-0.029	25.457	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.700	-0.798	26.644	-0.091	-0.091	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.054	-0.052	27.037	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	57	THR	0	0.049	0.008	28.762	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	58	PHE	0	-0.085	-0.034	30.445	0.005	0.005	0.000	0.000	0.000	0.000
58	A	59	ASN	0	-0.094	-0.056	32.380	0.010	0.010	0.000	0.000	0.000	0.000
59	A	60	TRP	0	-0.042	-0.033	31.628	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.962	-0.967	34.263	-0.081	-0.081	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.982	-0.996	30.992	-0.125	-0.125	0.000	0.000	0.000	0.000
62	A	63	PHE	0	-0.009	-0.002	24.866	0.002	0.002	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.018	0.038	28.105	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	65	TYR	0	-0.037	-0.048	24.389	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.024	-0.012	22.482	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.015	-0.017	17.200	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.044	0.029	17.392	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.025	-0.023	10.208	-0.026	-0.026	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.045	-0.043	11.010	-0.082	-0.082	0.000	0.000	0.000	0.000
70	A	71	THR	0	-0.024	-0.048	9.961	-0.240	-0.240	0.000	0.000	0.000	0.000
71	A	72	GLY	0	-0.009	0.000	7.752	-0.556	-0.556	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.066	-0.038	7.968	0.293	0.293	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.835	0.908	10.313	0.774	0.774	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.728	-0.860	13.741	-0.337	-0.337	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.768	0.855	17.281	0.219	0.219	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.055	-0.027	20.000	0.042	0.042	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.035	-0.011	16.631	0.033	0.033	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.017	-0.007	16.361	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.854	-0.900	11.684	-0.689	-0.689	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.001	0.009	13.774	0.064	0.064	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.030	0.018	13.513	-0.198	-0.198	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.845	-0.928	14.565	-0.655	-0.655	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.056	0.021	16.977	0.047	0.047	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.783	-0.860	18.387	-0.398	-0.398	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.015	-0.010	20.618	-0.012	-0.012	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.000	-0.003	17.821	0.014	0.014	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.029	-0.017	22.052	0.025	0.025	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.022	-0.041	23.248	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.799	-0.892	24.681	-0.168	-0.168	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.008	0.018	26.346	0.016	0.016	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.001	-0.005	29.342	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.929	0.968	32.578	0.128	0.128	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.869	0.922	34.436	0.118	0.118	0.000	0.000	0.000	0.000
94	A	95	TYR	0	0.060	0.020	37.954	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.008	0.012	40.363	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	97	HIS	0	-0.009	0.001	36.158	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.817	0.870	33.103	0.135	0.135	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.781	0.885	27.720	0.191	0.191	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.005	0.005	27.532	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	101	MET	0	0.016	0.018	26.110	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	102	HIS	1	0.782	0.880	22.035	0.299	0.299	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.802	-0.894	21.289	-0.347	-0.347	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.064	-0.013	15.349	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	105	ALA	0	0.078	0.042	17.184	0.020	0.020	0.000	0.000	0.000	0.000
105	A	106	TYR	0	0.024	0.003	10.617	-0.032	-0.032	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.027	-0.017	15.235	0.090	0.090	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.957	-0.976	15.707	-0.397	-0.397	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.022	0.022	12.509	0.009	0.009	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.828	0.930	10.671	0.342	0.342	0.000	0.000	0.000	0.000
110	A	111	PHE	0	0.073	0.032	8.493	0.081	0.081	0.000	0.000	0.000	0.000
111	A	112	PHE	0	-0.075	-0.058	12.435	0.004	0.004	0.000	0.000	0.000	0.000
112	A	113	TRP	0	0.004	-0.007	15.386	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.836	-0.924	18.549	-0.315	-0.315	0.000	0.000	0.000	0.000
114	A	115	PHE	0	-0.021	-0.012	21.882	0.014	0.014	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.018	-0.018	20.805	0.027	0.027	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.900	-0.925	20.927	-0.289	-0.289	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.075	-0.047	19.007	0.019	0.019	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.003	0.000	13.270	-0.028	-0.028	0.000	0.000	0.000	0.000
119	A	120	PHE	0	0.069	0.049	11.591	0.021	0.021	0.000	0.000	0.000	0.000
120	A	121	CYS	0	-0.007	-0.005	10.961	-0.129	-0.129	0.000	0.000	0.000	0.000
121	A	122	GLN	0	0.059	0.015	10.104	0.031	0.031	0.000	0.000	0.000	0.000
122	A	123	SER	0	0.009	0.006	12.130	0.086	0.086	0.000	0.000	0.000	0.000
123	A	124	ASN	0	-0.028	-0.035	14.966	0.109	0.109	0.000	0.000	0.000	0.000
124	A	125	ILE	0	0.007	0.016	13.097	0.066	0.066	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.007	-0.003	15.255	0.051	0.051	0.000	0.000	0.000	0.000
126	A	127	TYR	0	0.002	0.018	18.427	0.061	0.061	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.881	0.927	20.637	0.174	0.174	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.829	-0.879	24.286	-0.163	-0.163	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.023	0.026	21.032	0.004	0.004	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.007	-0.005	19.362	0.022	0.022	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.044	-0.013	20.497	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	133	VAL	0	0.030	0.008	18.958	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.098	-0.059	21.814	0.031	0.031	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.045	0.024	24.222	0.025	0.025	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.042	-0.035	22.855	-0.027	-0.027	0.000	0.000	0.000	0.000
136	A	137	ILE	0	0.000	-0.011	23.428	0.025	0.025	0.000	0.000	0.000	0.000
137	A	138	HIS	0	-0.003	0.003	22.514	0.034	0.034	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.795	-0.884	25.637	-0.193	-0.193	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.095	-0.046	27.769	0.003	0.003	0.000	0.000	0.000	0.000
140	A	141	PRO	0	0.053	0.041	29.603	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.950	-0.982	30.610	-0.132	-0.132	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.057	-0.019	27.544	0.005	0.005	0.000	0.000	0.000	0.000
143	A	144	LEU	0	0.016	-0.001	25.894	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	145	GLU	-1	-0.901	-0.895	30.027	-0.130	-0.130	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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