FMO DATABASE

FMODB ID: MNZ6Z

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:

Apendix: None

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1278118.787479
FMO2-HF: Nuclear repulsion	1223135.503392
FMO2-HF: Total energy	-54983.284087
FMO2-MP2: Total energy	-55141.72489

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.
1.594	3.924	-0.022	-1.281	-1.027	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 : 0.032 / q_NPA : 0.016

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	-0.018	-0.015	3.828	-0.616	1.714	-0.022	-1.281	-1.027	0.005
4	A	31	ARG	1	0.856	0.917	5.561	1.857	1.857	0.000	0.000	0.000	0.000
5	A	32	PRO	0	0.040	0.033	9.494	0.160	0.160	0.000	0.000	0.000	0.000
6	A	33	THR	0	0.009	0.012	12.706	0.053	0.053	0.000	0.000	0.000	0.000
7	A	34	PRO	0	0.004	0.011	15.584	0.042	0.042	0.000	0.000	0.000	0.000
8	A	35	ALA	0	0.013	0.009	18.744	0.031	0.031	0.000	0.000	0.000	0.000
9	A	36	PRO	0	-0.011	0.017	21.821	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	37	SER	0	-0.045	-0.029	24.745	0.002	0.002	0.000	0.000	0.000	0.000
11	A	38	PHE	0	0.014	-0.015	27.513	0.012	0.012	0.000	0.000	0.000	0.000
12	A	39	SER	0	-0.004	-0.007	30.993	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	40	GLY	0	0.027	0.009	34.534	0.004	0.004	0.000	0.000	0.000	0.000
14	A	41	VAL	0	-0.009	0.001	37.933	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	42	THR	0	-0.026	-0.037	38.645	0.001	0.001	0.000	0.000	0.000	0.000
16	A	43	VAL	0	0.009	-0.004	40.912	0.003	0.003	0.000	0.000	0.000	0.000
17	A	44	ASP	-1	-0.924	-0.957	42.958	-0.062	-0.062	0.000	0.000	0.000	0.000
18	A	45	GLY	0	0.009	0.019	44.589	0.001	0.001	0.000	0.000	0.000	0.000
19	A	46	LYS	1	0.897	0.938	42.062	0.066	0.066	0.000	0.000	0.000	0.000
20	A	47	PRO	0	0.013	0.014	40.374	0.000	0.000	0.000	0.000	0.000	0.000
21	A	48	PHE	0	0.010	0.000	31.365	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	49	SER	0	0.071	0.019	33.973	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	50	SER	0	0.080	0.061	28.565	0.002	0.002	0.000	0.000	0.000	0.000
24	A	51	ALA	0	0.029	0.027	29.528	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	52	SER	0	-0.081	-0.051	31.073	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	53	LEU	0	-0.027	-0.025	28.251	0.004	0.004	0.000	0.000	0.000	0.000
27	A	54	LYS	1	0.980	0.996	26.464	0.214	0.214	0.000	0.000	0.000	0.000
28	A	55	GLY	0	0.000	0.001	24.941	0.010	0.010	0.000	0.000	0.000	0.000
29	A	56	LYS	1	0.847	0.932	25.964	0.150	0.150	0.000	0.000	0.000	0.000
30	A	57	ALA	0	0.050	0.045	24.062	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	58	TYR	0	-0.015	-0.035	24.769	0.022	0.022	0.000	0.000	0.000	0.000
32	A	59	ILE	0	-0.016	0.001	25.093	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	60	VAL	0	-0.022	0.006	26.544	0.008	0.008	0.000	0.000	0.000	0.000
34	A	61	ASN	0	-0.022	-0.028	27.943	0.004	0.004	0.000	0.000	0.000	0.000
35	A	62	PHE	0	0.038	0.020	28.110	0.004	0.004	0.000	0.000	0.000	0.000
36	A	63	PHE	0	0.012	-0.017	32.096	0.006	0.006	0.000	0.000	0.000	0.000
37	A	64	ALA	0	0.039	0.017	35.204	0.000	0.000	0.000	0.000	0.000	0.000
38	A	65	THR	0	-0.075	-0.066	38.834	0.002	0.002	0.000	0.000	0.000	0.000
39	A	66	TRP	0	0.021	0.006	39.472	0.002	0.002	0.000	0.000	0.000	0.000
40	A	67	CYS	0	-0.019	0.011	36.674	0.004	0.004	0.000	0.000	0.000	0.000
41	A	68	PRO	0	0.036	-0.001	39.780	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	69	PRO	0	0.053	0.021	35.155	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	70	CYS	0	0.023	0.032	35.000	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	71	ARG	1	0.894	0.939	37.104	0.028	0.028	0.000	0.000	0.000	0.000
45	A	72	SER	0	-0.029	-0.002	37.695	0.001	0.001	0.000	0.000	0.000	0.000
46	A	73	GLU	-1	-0.880	-0.950	32.300	-0.056	-0.056	0.000	0.000	0.000	0.000
47	A	74	ILE	0	0.009	-0.003	35.895	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	75	PRO	0	0.018	0.006	37.346	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	76	ASP	-1	-0.817	-0.901	35.064	-0.046	-0.046	0.000	0.000	0.000	0.000
50	A	77	MET	0	-0.021	0.010	32.011	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	78	VAL	0	-0.030	-0.006	34.764	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	79	GLN	0	-0.034	-0.030	37.626	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	80	VAL	0	0.036	0.016	31.072	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	81	GLN	0	0.016	-0.006	33.875	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	82	LYS	1	0.914	0.958	35.168	0.053	0.053	0.000	0.000	0.000	0.000
56	A	83	THR	0	-0.028	0.001	34.183	0.000	0.000	0.000	0.000	0.000	0.000
57	A	84	TRP	0	-0.038	-0.055	29.377	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	85	ALA	0	0.006	0.028	32.998	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	86	SER	0	-0.018	-0.003	35.039	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	87	ARG	1	0.843	0.918	31.709	0.103	0.103	0.000	0.000	0.000	0.000
61	A	88	GLY	0	0.017	0.016	29.382	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	89	PHE	0	0.051	0.025	27.167	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	90	THR	0	-0.064	-0.027	29.389	0.013	0.013	0.000	0.000	0.000	0.000
64	A	91	PHE	0	0.051	0.026	29.747	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	92	VAL	0	-0.002	-0.003	30.840	0.000	0.000	0.000	0.000	0.000	0.000
66	A	93	GLY	0	-0.017	-0.006	31.753	0.000	0.000	0.000	0.000	0.000	0.000
67	A	94	ILE	0	-0.020	-0.013	30.997	0.000	0.000	0.000	0.000	0.000	0.000
68	A	95	ALA	0	0.006	0.006	34.672	0.003	0.003	0.000	0.000	0.000	0.000
69	A	96	VAL	0	0.040	0.004	34.072	0.000	0.000	0.000	0.000	0.000	0.000
70	A	97	ASN	0	-0.022	-0.017	37.395	0.000	0.000	0.000	0.000	0.000	0.000
71	A	98	GLU	-1	-0.677	-0.799	40.347	-0.036	-0.036	0.000	0.000	0.000	0.000
72	A	99	GLN	0	-0.013	-0.010	42.559	0.000	0.000	0.000	0.000	0.000	0.000
73	A	100	LEU	0	0.051	0.022	44.769	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	101	PRO	0	0.012	-0.002	46.326	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	102	ASN	0	-0.052	-0.027	45.059	0.001	0.001	0.000	0.000	0.000	0.000
76	A	103	VAL	0	0.047	0.018	41.181	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	104	LYS	1	0.981	0.995	44.221	0.048	0.048	0.000	0.000	0.000	0.000
78	A	105	ASN	0	-0.005	-0.011	46.359	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	106	TYR	0	0.059	0.031	40.644	0.002	0.002	0.000	0.000	0.000	0.000
80	A	107	MET	0	0.018	0.009	41.126	0.000	0.000	0.000	0.000	0.000	0.000
81	A	108	LYS	1	0.897	0.961	44.188	0.036	0.036	0.000	0.000	0.000	0.000
82	A	109	THR	0	-0.100	-0.055	47.347	0.000	0.000	0.000	0.000	0.000	0.000
83	A	110	GLN	0	0.000	-0.003	42.853	0.001	0.001	0.000	0.000	0.000	0.000
84	A	111	GLY	0	-0.003	0.013	43.522	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	112	ILE	0	-0.039	-0.020	38.780	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	113	ILE	0	-0.051	-0.022	38.982	0.000	0.000	0.000	0.000	0.000	0.000
87	A	114	TYR	0	0.007	0.012	35.170	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	115	PRO	0	-0.004	-0.006	34.925	0.005	0.005	0.000	0.000	0.000	0.000
89	A	116	VAL	0	0.052	0.028	35.906	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	117	MET	0	-0.001	0.013	33.838	0.002	0.002	0.000	0.000	0.000	0.000
91	A	118	MET	0	0.005	0.013	37.832	0.002	0.002	0.000	0.000	0.000	0.000
92	A	119	ALA	0	0.005	0.004	35.595	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	120	THR	0	0.045	0.017	35.800	0.003	0.003	0.000	0.000	0.000	0.000
94	A	121	PRO	0	0.047	0.002	34.984	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	122	GLU	-1	-0.973	-0.987	32.747	-0.096	-0.096	0.000	0.000	0.000	0.000
96	A	123	LEU	0	0.009	0.019	31.327	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	124	ILE	0	-0.010	-0.013	30.236	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	125	ARG	1	0.952	0.968	29.019	0.072	0.072	0.000	0.000	0.000	0.000
99	A	126	ALA	0	-0.021	-0.004	27.248	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	127	PHE	0	0.035	0.001	24.295	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	128	ASN	0	0.029	0.016	24.422	0.001	0.001	0.000	0.000	0.000	0.000
102	A	129	GLY	0	0.006	0.006	22.761	0.010	0.010	0.000	0.000	0.000	0.000
103	A	130	TYR	0	-0.049	-0.017	18.799	0.006	0.006	0.000	0.000	0.000	0.000
104	A	131	ILE	0	-0.032	-0.015	20.009	0.001	0.001	0.000	0.000	0.000	0.000
105	A	132	ASP	-1	-0.874	-0.929	21.093	0.003	0.003	0.000	0.000	0.000	0.000
106	A	133	GLY	0	-0.002	0.008	22.763	0.003	0.003	0.000	0.000	0.000	0.000
107	A	134	GLY	0	-0.075	-0.032	25.261	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	135	ILE	0	-0.047	-0.044	26.880	0.004	0.004	0.000	0.000	0.000	0.000
109	A	136	THR	0	-0.002	0.000	28.808	0.003	0.003	0.000	0.000	0.000	0.000
110	A	137	GLY	0	0.003	0.015	30.582	0.007	0.007	0.000	0.000	0.000	0.000
111	A	138	ILE	0	-0.076	0.006	31.327	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	139	PRO	0	0.032	-0.026	31.588	0.007	0.007	0.000	0.000	0.000	0.000
113	A	140	THR	0	-0.026	-0.011	26.266	0.005	0.005	0.000	0.000	0.000	0.000
114	A	141	SER	0	-0.037	-0.020	26.804	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	142	PHE	0	0.015	0.020	22.159	0.001	0.001	0.000	0.000	0.000	0.000
116	A	143	VAL	0	0.012	-0.007	20.890	0.005	0.005	0.000	0.000	0.000	0.000
117	A	144	ILE	0	-0.010	0.002	20.517	-0.018	-0.018	0.000	0.000	0.000	0.000
118	A	145	ASP	-1	-0.749	-0.839	17.194	-0.354	-0.354	0.000	0.000	0.000	0.000
119	A	146	ALA	0	0.032	0.007	20.718	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	147	SER	0	-0.093	-0.076	17.488	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	148	GLY	0	-0.062	-0.014	19.477	-0.022	-0.022	0.000	0.000	0.000	0.000
122	A	149	ASN	0	-0.005	-0.016	15.614	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	150	VAL	0	-0.022	-0.020	17.882	0.035	0.035	0.000	0.000	0.000	0.000
124	A	151	SER	0	-0.020	-0.029	15.769	-0.030	-0.030	0.000	0.000	0.000	0.000
125	A	152	GLY	0	-0.017	-0.007	16.198	0.015	0.015	0.000	0.000	0.000	0.000
126	A	153	VAL	0	-0.007	0.003	18.686	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	154	ILE	0	-0.070	-0.028	21.694	0.013	0.013	0.000	0.000	0.000	0.000
128	A	155	VAL	0	0.076	0.029	24.381	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	156	GLY	0	0.002	0.002	26.838	0.010	0.010	0.000	0.000	0.000	0.000
130	A	157	PRO	0	0.006	0.010	28.523	-0.008	-0.008	0.000	0.000	0.000	0.000
131	A	158	ARG	1	0.906	0.950	23.755	0.049	0.049	0.000	0.000	0.000	0.000
132	A	159	SER	0	0.009	-0.017	30.188	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	160	LYS	1	0.918	0.940	31.465	0.040	0.040	0.000	0.000	0.000	0.000
134	A	161	ALA	0	0.012	0.012	32.066	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	162	ASP	-1	-0.846	-0.899	27.567	-0.050	-0.050	0.000	0.000	0.000	0.000
136	A	163	PHE	0	0.011	-0.013	27.314	-0.011	-0.011	0.000	0.000	0.000	0.000
137	A	164	ASP	-1	-0.880	-0.928	28.202	-0.096	-0.096	0.000	0.000	0.000	0.000
138	A	165	ARG	1	0.951	0.971	23.822	0.058	0.058	0.000	0.000	0.000	0.000
139	A	166	ILE	0	0.000	0.007	22.989	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	167	VAL	0	0.014	0.017	23.711	-0.019	-0.019	0.000	0.000	0.000	0.000
141	A	168	LYS	1	0.959	0.979	25.171	0.109	0.109	0.000	0.000	0.000	0.000
142	A	169	MET	0	-0.049	-0.030	20.274	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	170	ALA	0	0.014	0.006	20.606	-0.025	-0.025	0.000	0.000	0.000	0.000
144	A	171	LEU	0	-0.029	-0.011	21.563	-0.021	-0.021	0.000	0.000	0.000	0.000
145	A	172	GLY	0	-0.080	-0.021	20.242	-0.007	-0.007	0.000	0.000	0.000	0.000

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