FMO DATABASE

FMODB ID: 98QN2

Calculation Name: 3OR5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3OR5

Chain ID: A

ChEMBL ID:

UniProt ID: Q8KAD0

Base Structure: X-ray

Registration Date: 2023-09-23

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1278231.738688
FMO2-HF: Nuclear repulsion	1223249.158613
FMO2-HF: Total energy	-54982.580075
FMO2-MP2: Total energy	-55141.138929

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:28:ALA)

Summations of interaction energy for fragment #1(A:28:ALA)

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.
1.644	3.97	-0.022	-1.278	-1.026	0.005

Interaction energy analysis for fragmet #1(A:28:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / 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	30	ALA	0	-0.012	-0.010	3.828	-0.519	1.807	-0.022	-1.278	-1.026	0.005
4	A	31	ARG	1	0.881	0.946	5.767	1.799	1.799	0.000	0.000	0.000	0.000
5	A	32	PRO	0	0.047	0.036	9.475	0.155	0.155	0.000	0.000	0.000	0.000
6	A	33	THR	0	0.001	0.008	12.706	0.051	0.051	0.000	0.000	0.000	0.000
7	A	34	PRO	0	0.005	0.015	15.583	0.039	0.039	0.000	0.000	0.000	0.000
8	A	35	ALA	0	0.011	0.002	18.744	0.032	0.032	0.000	0.000	0.000	0.000
9	A	36	PRO	0	-0.012	0.014	21.819	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	37	SER	0	-0.044	-0.023	24.744	0.003	0.003	0.000	0.000	0.000	0.000
11	A	38	PHE	0	0.003	-0.021	27.443	0.012	0.012	0.000	0.000	0.000	0.000
12	A	39	SER	0	-0.028	-0.014	30.992	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	40	GLY	0	0.048	0.015	34.532	0.003	0.003	0.000	0.000	0.000	0.000
14	A	41	VAL	0	-0.007	0.005	37.931	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	42	THR	0	-0.037	-0.039	38.573	0.001	0.001	0.000	0.000	0.000	0.000
16	A	43	VAL	0	0.001	-0.005	40.908	0.003	0.003	0.000	0.000	0.000	0.000
17	A	44	ASP	-1	-0.954	-0.983	43.034	-0.061	-0.061	0.000	0.000	0.000	0.000
18	A	45	GLY	0	-0.004	0.009	44.598	0.001	0.001	0.000	0.000	0.000	0.000
19	A	46	LYS	1	0.935	0.974	42.062	0.066	0.066	0.000	0.000	0.000	0.000
20	A	47	PRO	0	0.022	0.016	40.376	0.000	0.000	0.000	0.000	0.000	0.000
21	A	48	PHE	0	0.012	0.000	31.373	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	49	SER	0	0.068	0.021	33.892	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	50	SER	0	0.078	0.041	28.518	0.002	0.002	0.000	0.000	0.000	0.000
24	A	51	ALA	0	0.018	0.019	29.526	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	52	SER	0	-0.085	-0.039	31.072	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	53	LEU	0	-0.033	-0.032	28.093	0.004	0.004	0.000	0.000	0.000	0.000
27	A	54	LYS	1	0.968	0.986	26.270	0.222	0.222	0.000	0.000	0.000	0.000
28	A	55	GLY	0	-0.004	0.000	24.940	0.010	0.010	0.000	0.000	0.000	0.000
29	A	56	LYS	1	0.896	0.963	25.962	0.146	0.146	0.000	0.000	0.000	0.000
30	A	57	ALA	0	0.061	0.047	24.041	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	58	TYR	0	-0.021	-0.035	24.763	0.021	0.021	0.000	0.000	0.000	0.000
32	A	59	ILE	0	-0.020	0.001	25.085	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	60	VAL	0	-0.021	0.005	26.538	0.008	0.008	0.000	0.000	0.000	0.000
34	A	61	ASN	0	0.012	-0.004	27.936	0.004	0.004	0.000	0.000	0.000	0.000
35	A	62	PHE	0	0.031	0.018	28.159	0.003	0.003	0.000	0.000	0.000	0.000
36	A	63	PHE	0	0.014	-0.016	32.088	0.006	0.006	0.000	0.000	0.000	0.000
37	A	64	ALA	0	0.036	0.012	35.196	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	65	THR	0	-0.073	-0.066	38.826	0.002	0.002	0.000	0.000	0.000	0.000
39	A	66	TRP	0	0.028	0.010	39.554	0.002	0.002	0.000	0.000	0.000	0.000
40	A	67	CYS	0	-0.037	0.009	36.670	0.004	0.004	0.000	0.000	0.000	0.000
41	A	68	PRO	0	0.025	-0.001	39.769	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	69	PRO	0	0.071	0.028	35.161	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	70	CYS	0	0.022	0.029	36.100	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	71	ARG	1	0.878	0.938	37.093	0.027	0.027	0.000	0.000	0.000	0.000
45	A	72	SER	0	-0.031	-0.005	37.653	0.001	0.001	0.000	0.000	0.000	0.000
46	A	73	GLU	-1	-0.891	-0.959	32.319	-0.053	-0.053	0.000	0.000	0.000	0.000
47	A	74	ILE	0	0.000	-0.005	35.884	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	75	PRO	0	0.020	0.006	37.335	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	76	ASP	-1	-0.902	-0.949	35.218	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	77	MET	0	-0.025	-0.001	31.929	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	78	VAL	0	-0.026	-0.003	34.747	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	79	GLN	0	-0.031	-0.030	37.521	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	80	VAL	0	0.047	0.018	31.060	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	81	GLN	0	0.015	-0.002	33.969	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	82	LYS	1	0.905	0.951	35.159	0.052	0.052	0.000	0.000	0.000	0.000
56	A	83	THR	0	-0.035	0.003	33.937	0.000	0.000	0.000	0.000	0.000	0.000
57	A	84	TRP	0	-0.050	-0.045	29.744	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	85	ALA	0	0.002	0.017	32.991	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	86	SER	0	-0.026	-0.002	35.033	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	87	ARG	1	0.868	0.923	31.579	0.104	0.104	0.000	0.000	0.000	0.000
61	A	88	GLY	0	0.015	0.012	29.376	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	89	PHE	0	0.057	0.035	27.152	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	90	THR	0	-0.077	-0.046	29.380	0.013	0.013	0.000	0.000	0.000	0.000
64	A	91	PHE	0	0.054	0.028	29.740	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	92	VAL	0	0.002	0.003	30.742	0.000	0.000	0.000	0.000	0.000	0.000
66	A	93	GLY	0	-0.014	-0.006	31.746	0.000	0.000	0.000	0.000	0.000	0.000
67	A	94	ILE	0	-0.017	-0.010	30.922	0.000	0.000	0.000	0.000	0.000	0.000
68	A	95	ALA	0	0.005	0.006	34.666	0.003	0.003	0.000	0.000	0.000	0.000
69	A	96	VAL	0	0.037	0.003	34.002	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	97	ASN	0	-0.021	-0.019	37.389	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	98	GLU	-1	-0.685	-0.816	40.340	-0.035	-0.035	0.000	0.000	0.000	0.000
72	A	99	GLN	0	-0.014	-0.014	42.552	0.000	0.000	0.000	0.000	0.000	0.000
73	A	100	LEU	0	0.049	0.023	45.157	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	101	PRO	0	0.013	-0.001	46.320	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	102	ASN	0	-0.039	-0.010	45.227	0.001	0.001	0.000	0.000	0.000	0.000
76	A	103	VAL	0	0.050	0.018	41.212	0.000	0.000	0.000	0.000	0.000	0.000
77	A	104	LYS	1	0.998	0.997	44.213	0.047	0.047	0.000	0.000	0.000	0.000
78	A	105	ASN	0	-0.011	-0.019	46.352	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	106	TYR	0	0.036	0.020	40.472	0.002	0.002	0.000	0.000	0.000	0.000
80	A	107	MET	0	0.028	0.013	41.314	0.000	0.000	0.000	0.000	0.000	0.000
81	A	108	LYS	1	0.910	0.971	44.181	0.036	0.036	0.000	0.000	0.000	0.000
82	A	109	THR	0	-0.108	-0.057	46.988	0.001	0.001	0.000	0.000	0.000	0.000
83	A	110	GLN	0	0.012	-0.002	42.876	0.001	0.001	0.000	0.000	0.000	0.000
84	A	111	GLY	0	-0.008	0.011	43.513	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	112	ILE	0	-0.034	-0.015	38.804	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	113	ILE	0	-0.059	-0.023	38.703	0.000	0.000	0.000	0.000	0.000	0.000
87	A	114	TYR	0	0.001	0.007	35.190	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	115	PRO	0	-0.008	-0.007	34.880	0.005	0.005	0.000	0.000	0.000	0.000
89	A	116	VAL	0	0.046	0.025	35.900	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	117	MET	0	0.004	0.014	33.751	0.002	0.002	0.000	0.000	0.000	0.000
91	A	118	MET	0	0.005	0.011	37.838	0.002	0.002	0.000	0.000	0.000	0.000
92	A	119	ALA	0	0.008	0.007	35.696	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	120	THR	0	0.051	0.019	35.792	0.003	0.003	0.000	0.000	0.000	0.000
94	A	121	PRO	0	0.031	-0.004	34.981	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	122	GLU	-1	-0.964	-0.982	32.680	-0.099	-0.099	0.000	0.000	0.000	0.000
96	A	123	LEU	0	0.005	0.012	31.325	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	124	ILE	0	0.000	-0.006	30.233	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	125	ARG	1	0.941	0.961	29.015	0.073	0.073	0.000	0.000	0.000	0.000
99	A	126	ALA	0	-0.011	0.000	27.238	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	127	PHE	0	0.030	0.001	24.399	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	128	ASN	0	0.029	0.015	24.418	0.003	0.003	0.000	0.000	0.000	0.000
102	A	129	GLY	0	-0.004	-0.006	22.758	0.010	0.010	0.000	0.000	0.000	0.000
103	A	130	TYR	0	-0.042	-0.007	18.754	0.005	0.005	0.000	0.000	0.000	0.000
104	A	131	ILE	0	-0.028	-0.013	20.002	0.001	0.001	0.000	0.000	0.000	0.000
105	A	132	ASP	-1	-0.898	-0.937	21.142	0.006	0.006	0.000	0.000	0.000	0.000
106	A	133	GLY	0	0.012	0.009	22.756	0.004	0.004	0.000	0.000	0.000	0.000
107	A	134	GLY	0	-0.067	-0.029	25.258	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	135	ILE	0	-0.047	-0.039	26.875	0.004	0.004	0.000	0.000	0.000	0.000
109	A	136	THR	0	-0.004	0.002	28.801	0.002	0.002	0.000	0.000	0.000	0.000
110	A	137	GLY	0	0.011	0.015	30.588	0.007	0.007	0.000	0.000	0.000	0.000
111	A	138	ILE	0	-0.067	0.010	31.318	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	139	PRO	0	0.025	-0.032	31.574	0.006	0.006	0.000	0.000	0.000	0.000
113	A	140	THR	0	-0.027	-0.018	26.291	0.006	0.006	0.000	0.000	0.000	0.000
114	A	141	SER	0	-0.036	-0.022	26.815	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	142	PHE	0	0.018	0.026	22.222	0.002	0.002	0.000	0.000	0.000	0.000
116	A	143	VAL	0	0.016	-0.007	20.915	0.004	0.004	0.000	0.000	0.000	0.000
117	A	144	ILE	0	-0.010	0.004	20.509	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	145	ASP	-1	-0.797	-0.908	17.183	-0.351	-0.351	0.000	0.000	0.000	0.000
119	A	146	ALA	0	0.020	-0.001	20.712	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	147	SER	0	-0.065	-0.031	17.578	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	148	GLY	0	-0.075	-0.020	19.476	-0.022	-0.022	0.000	0.000	0.000	0.000
122	A	149	ASN	0	0.014	-0.007	15.011	0.010	0.010	0.000	0.000	0.000	0.000
123	A	150	VAL	0	-0.023	-0.023	17.879	0.035	0.035	0.000	0.000	0.000	0.000
124	A	151	SER	0	-0.014	0.009	15.752	-0.033	-0.033	0.000	0.000	0.000	0.000
125	A	152	GLY	0	-0.007	-0.018	16.189	0.015	0.015	0.000	0.000	0.000	0.000
126	A	153	VAL	0	-0.004	0.009	18.677	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	154	ILE	0	-0.067	-0.028	21.684	0.013	0.013	0.000	0.000	0.000	0.000
128	A	155	VAL	0	0.072	0.027	24.654	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	156	GLY	0	-0.005	-0.004	26.827	0.010	0.010	0.000	0.000	0.000	0.000
130	A	157	PRO	0	0.006	0.018	28.510	-0.008	-0.008	0.000	0.000	0.000	0.000
131	A	158	ARG	1	0.920	0.953	23.723	0.048	0.048	0.000	0.000	0.000	0.000
132	A	159	SER	0	0.043	0.033	30.175	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	160	LYS	1	1.020	1.004	31.453	0.039	0.039	0.000	0.000	0.000	0.000
134	A	161	ALA	0	0.021	0.018	31.996	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	162	ASP	-1	-0.858	-0.941	27.558	-0.045	-0.045	0.000	0.000	0.000	0.000
136	A	163	PHE	0	-0.002	-0.021	27.301	-0.011	-0.011	0.000	0.000	0.000	0.000
137	A	164	ASP	-1	-0.888	-0.940	28.191	-0.092	-0.092	0.000	0.000	0.000	0.000
138	A	165	ARG	1	0.941	0.967	23.397	0.056	0.056	0.000	0.000	0.000	0.000
139	A	166	ILE	0	0.000	0.008	22.954	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	167	VAL	0	0.015	0.018	23.701	-0.019	-0.019	0.000	0.000	0.000	0.000
141	A	168	LYS	1	0.944	0.970	25.162	0.106	0.106	0.000	0.000	0.000	0.000
142	A	169	MET	0	-0.057	-0.037	20.278	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	170	ALA	0	0.016	0.011	20.486	-0.025	-0.025	0.000	0.000	0.000	0.000
144	A	171	LEU	0	-0.033	-0.015	21.556	-0.021	-0.021	0.000	0.000	0.000	0.000
145	A	172	GLY	0	-0.050	-0.005	20.236	-0.010	-0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:ALA)