FMO DATABASE

FMODB ID: 7643K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1280347.184894
FMO2-HF: Nuclear repulsion	1225363.405935
FMO2-HF: Total energy	-54983.778959
FMO2-MP2: Total energy	-55142.104841

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.
2.714	4.572	-0.014	-0.967	-0.877	0.003

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 : 0.028 / q_NPA : 0.013

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	-0.013	0.003	3.857	0.133	1.991	-0.014	-0.967	-0.877	0.003
4	A	31	ARG	1	0.809	0.877	6.239	2.240	2.240	0.000	0.000	0.000	0.000
5	A	32	PRO	0	0.024	0.023	9.162	0.184	0.184	0.000	0.000	0.000	0.000
6	A	33	THR	0	-0.015	-0.009	12.603	0.049	0.049	0.000	0.000	0.000	0.000
7	A	34	PRO	0	0.005	0.011	15.437	0.049	0.049	0.000	0.000	0.000	0.000
8	A	35	ALA	0	0.032	0.031	18.746	0.029	0.029	0.000	0.000	0.000	0.000
9	A	36	PRO	0	-0.001	0.020	21.877	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	37	SER	0	-0.012	-0.013	24.942	0.004	0.004	0.000	0.000	0.000	0.000
11	A	38	PHE	0	-0.003	-0.014	27.349	0.011	0.011	0.000	0.000	0.000	0.000
12	A	39	SER	0	-0.003	-0.010	30.951	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	40	GLY	0	-0.001	0.000	34.520	0.003	0.003	0.000	0.000	0.000	0.000
14	A	41	VAL	0	-0.001	0.000	37.955	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	42	THR	0	-0.041	-0.041	38.707	0.001	0.001	0.000	0.000	0.000	0.000
16	A	43	VAL	0	0.004	-0.010	40.886	0.003	0.003	0.000	0.000	0.000	0.000
17	A	44	ASP	-1	-0.883	-0.938	42.978	-0.054	-0.054	0.000	0.000	0.000	0.000
18	A	45	GLY	0	0.005	0.020	44.538	0.001	0.001	0.000	0.000	0.000	0.000
19	A	46	LYS	1	0.873	0.929	41.761	0.058	0.058	0.000	0.000	0.000	0.000
20	A	47	PRO	0	0.031	0.021	40.120	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	48	PHE	0	0.017	0.000	31.190	0.000	0.000	0.000	0.000	0.000	0.000
22	A	49	SER	0	0.057	0.004	33.507	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	50	SER	0	0.012	0.036	27.968	0.002	0.002	0.000	0.000	0.000	0.000
24	A	51	ALA	0	0.058	0.036	29.029	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	52	SER	0	-0.084	-0.052	30.578	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	53	LEU	0	-0.028	-0.022	28.054	0.007	0.007	0.000	0.000	0.000	0.000
27	A	54	LYS	1	0.986	0.996	26.225	0.201	0.201	0.000	0.000	0.000	0.000
28	A	55	GLY	0	-0.002	0.005	24.676	0.010	0.010	0.000	0.000	0.000	0.000
29	A	56	LYS	1	0.864	0.937	25.695	0.141	0.141	0.000	0.000	0.000	0.000
30	A	57	ALA	0	0.042	0.041	23.955	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	58	TYR	0	-0.020	-0.040	24.577	0.018	0.018	0.000	0.000	0.000	0.000
32	A	59	ILE	0	-0.015	0.004	24.943	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	60	VAL	0	-0.007	0.015	26.454	0.008	0.008	0.000	0.000	0.000	0.000
34	A	61	ASN	0	-0.032	-0.035	27.766	0.004	0.004	0.000	0.000	0.000	0.000
35	A	62	PHE	0	0.047	0.021	28.219	0.002	0.002	0.000	0.000	0.000	0.000
36	A	63	PHE	0	-0.015	-0.024	32.130	0.006	0.006	0.000	0.000	0.000	0.000
37	A	64	ALA	0	0.059	0.022	35.223	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	65	THR	0	-0.086	-0.071	38.965	0.002	0.002	0.000	0.000	0.000	0.000
39	A	66	TRP	0	0.023	0.004	39.768	0.003	0.003	0.000	0.000	0.000	0.000
40	A	67	CYS	0	-0.020	0.013	36.693	0.004	0.004	0.000	0.000	0.000	0.000
41	A	68	PRO	0	0.041	0.007	39.586	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	69	PRO	0	0.043	0.016	34.906	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	70	CYS	0	-0.006	0.024	34.829	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	71	ARG	1	0.888	0.930	36.853	0.019	0.019	0.000	0.000	0.000	0.000
45	A	72	SER	0	-0.021	0.003	37.340	0.001	0.001	0.000	0.000	0.000	0.000
46	A	73	GLU	-1	-0.873	-0.944	31.943	-0.039	-0.039	0.000	0.000	0.000	0.000
47	A	74	ILE	0	0.033	0.011	35.478	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	75	PRO	0	0.004	0.000	36.994	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	76	ASP	-1	-0.768	-0.879	34.851	-0.028	-0.028	0.000	0.000	0.000	0.000
50	A	77	MET	0	-0.042	0.003	31.879	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	78	VAL	0	-0.020	-0.010	34.384	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	79	GLN	0	0.012	0.007	37.292	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	80	VAL	0	0.013	-0.002	30.708	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	81	GLN	0	0.029	0.004	33.649	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	82	LYS	1	0.857	0.929	34.783	0.040	0.040	0.000	0.000	0.000	0.000
56	A	83	THR	0	-0.018	0.008	33.587	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	84	TRP	0	-0.010	-0.034	28.429	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	85	ALA	0	0.030	0.039	32.385	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	86	SER	0	-0.047	-0.031	34.114	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	87	ARG	1	0.801	0.900	31.163	0.081	0.081	0.000	0.000	0.000	0.000
61	A	88	GLY	0	0.047	0.033	28.957	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	89	PHE	0	0.020	0.005	27.123	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	90	THR	0	-0.042	-0.026	29.338	0.010	0.010	0.000	0.000	0.000	0.000
64	A	91	PHE	0	0.032	0.022	29.635	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	92	VAL	0	0.001	-0.003	30.533	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	93	GLY	0	-0.011	0.007	31.623	0.000	0.000	0.000	0.000	0.000	0.000
67	A	94	ILE	0	-0.017	-0.015	30.939	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	95	ALA	0	0.022	0.012	34.756	0.003	0.003	0.000	0.000	0.000	0.000
69	A	96	VAL	0	0.042	0.009	34.372	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	97	ASN	0	-0.014	-0.014	37.589	0.000	0.000	0.000	0.000	0.000	0.000
71	A	98	GLU	-1	-0.697	-0.803	40.617	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	99	GLN	0	0.002	-0.002	42.755	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	100	LEU	0	0.057	0.025	44.651	0.000	0.000	0.000	0.000	0.000	0.000
74	A	101	PRO	0	0.020	0.002	46.160	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	102	ASN	0	-0.044	-0.031	45.212	0.001	0.001	0.000	0.000	0.000	0.000
76	A	103	VAL	0	0.040	0.016	41.153	0.000	0.000	0.000	0.000	0.000	0.000
77	A	104	LYS	1	0.949	0.988	44.281	0.042	0.042	0.000	0.000	0.000	0.000
78	A	105	ASN	0	0.020	0.003	46.451	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	106	TYR	0	0.054	0.027	40.304	0.002	0.002	0.000	0.000	0.000	0.000
80	A	107	MET	0	0.032	0.011	40.942	0.000	0.000	0.000	0.000	0.000	0.000
81	A	108	LYS	1	0.815	0.906	44.121	0.030	0.030	0.000	0.000	0.000	0.000
82	A	109	THR	0	-0.058	-0.027	46.424	0.002	0.002	0.000	0.000	0.000	0.000
83	A	110	GLN	0	0.004	0.005	42.375	0.002	0.002	0.000	0.000	0.000	0.000
84	A	111	GLY	0	-0.002	0.014	42.927	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	112	ILE	0	-0.030	-0.018	38.648	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	113	ILE	0	-0.041	-0.008	38.889	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	114	TYR	0	0.012	-0.007	35.087	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	115	PRO	0	0.008	0.006	34.843	0.004	0.004	0.000	0.000	0.000	0.000
89	A	116	VAL	0	0.039	0.026	35.663	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	117	MET	0	-0.002	0.011	33.821	0.001	0.001	0.000	0.000	0.000	0.000
91	A	118	MET	0	-0.008	0.007	37.928	0.002	0.002	0.000	0.000	0.000	0.000
92	A	119	ALA	0	0.011	0.008	35.996	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	120	THR	0	0.023	0.005	35.863	0.002	0.002	0.000	0.000	0.000	0.000
94	A	121	PRO	0	0.047	0.004	34.987	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	122	GLU	-1	-0.866	-0.906	32.649	-0.095	-0.095	0.000	0.000	0.000	0.000
96	A	123	LEU	0	-0.011	-0.009	31.359	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	124	ILE	0	0.016	0.008	30.312	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	125	ARG	1	0.880	0.918	29.039	0.078	0.078	0.000	0.000	0.000	0.000
99	A	126	ALA	0	-0.024	-0.003	27.133	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	127	PHE	0	0.025	-0.004	24.174	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	128	ASN	0	0.031	0.005	24.616	0.004	0.004	0.000	0.000	0.000	0.000
102	A	129	GLY	0	-0.010	0.009	22.557	0.008	0.008	0.000	0.000	0.000	0.000
103	A	130	TYR	0	-0.066	-0.040	18.829	0.005	0.005	0.000	0.000	0.000	0.000
104	A	131	ILE	0	-0.036	-0.024	20.379	0.006	0.006	0.000	0.000	0.000	0.000
105	A	132	ASP	-1	-0.839	-0.911	21.140	0.006	0.006	0.000	0.000	0.000	0.000
106	A	133	GLY	0	-0.032	-0.008	22.962	0.004	0.004	0.000	0.000	0.000	0.000
107	A	134	GLY	0	-0.029	-0.006	25.680	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	135	ILE	0	-0.045	-0.045	27.244	0.006	0.006	0.000	0.000	0.000	0.000
109	A	136	THR	0	-0.011	-0.005	28.808	0.003	0.003	0.000	0.000	0.000	0.000
110	A	137	GLY	0	0.006	0.009	31.067	0.006	0.006	0.000	0.000	0.000	0.000
111	A	138	ILE	0	-0.077	-0.007	31.685	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	139	PRO	0	0.022	-0.017	31.355	0.005	0.005	0.000	0.000	0.000	0.000
113	A	140	THR	0	-0.015	-0.011	26.686	0.006	0.006	0.000	0.000	0.000	0.000
114	A	141	SER	0	-0.042	-0.022	26.840	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	142	PHE	0	0.019	0.011	22.281	0.003	0.003	0.000	0.000	0.000	0.000
116	A	143	VAL	0	-0.021	-0.018	20.829	0.002	0.002	0.000	0.000	0.000	0.000
117	A	144	ILE	0	-0.005	-0.003	20.461	-0.015	-0.015	0.000	0.000	0.000	0.000
118	A	145	ASP	-1	-0.726	-0.819	17.078	-0.315	-0.315	0.000	0.000	0.000	0.000
119	A	146	ALA	0	0.006	-0.007	20.325	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	147	SER	0	-0.092	-0.069	17.404	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	148	GLY	0	-0.032	-0.006	19.178	-0.029	-0.029	0.000	0.000	0.000	0.000
122	A	149	ASN	0	-0.022	-0.019	15.608	-0.037	-0.037	0.000	0.000	0.000	0.000
123	A	150	VAL	0	0.000	-0.005	17.914	0.036	0.036	0.000	0.000	0.000	0.000
124	A	151	SER	0	-0.005	-0.030	15.580	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	152	GLY	0	-0.035	-0.008	16.133	0.022	0.022	0.000	0.000	0.000	0.000
126	A	153	VAL	0	-0.013	0.002	18.527	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	154	ILE	0	-0.053	-0.022	21.603	0.014	0.014	0.000	0.000	0.000	0.000
128	A	155	VAL	0	0.055	0.023	24.521	-0.005	-0.005	0.000	0.000	0.000	0.000
129	A	156	GLY	0	0.031	0.015	27.027	0.009	0.009	0.000	0.000	0.000	0.000
130	A	157	PRO	0	-0.006	0.004	28.491	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	158	ARG	1	0.906	0.951	23.569	0.020	0.020	0.000	0.000	0.000	0.000
132	A	159	SER	0	0.011	-0.011	30.126	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	160	LYS	1	0.879	0.909	31.108	0.023	0.023	0.000	0.000	0.000	0.000
134	A	161	ALA	0	0.008	0.010	31.495	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	162	ASP	-1	-0.849	-0.895	27.131	-0.018	-0.018	0.000	0.000	0.000	0.000
136	A	163	PHE	0	0.025	-0.006	26.851	-0.008	-0.008	0.000	0.000	0.000	0.000
137	A	164	ASP	-1	-0.869	-0.915	27.736	-0.070	-0.070	0.000	0.000	0.000	0.000
138	A	165	ARG	1	0.968	0.982	23.872	0.015	0.015	0.000	0.000	0.000	0.000
139	A	166	ILE	0	0.000	0.001	22.747	-0.009	-0.009	0.000	0.000	0.000	0.000
140	A	167	VAL	0	0.016	0.016	23.201	-0.017	-0.017	0.000	0.000	0.000	0.000
141	A	168	LYS	1	0.965	0.982	24.659	0.076	0.076	0.000	0.000	0.000	0.000
142	A	169	MET	0	-0.059	-0.031	19.753	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	170	ALA	0	0.017	0.019	20.102	-0.024	-0.024	0.000	0.000	0.000	0.000
144	A	171	LEU	0	-0.041	-0.026	21.325	-0.022	-0.022	0.000	0.000	0.000	0.000
145	A	172	GLY	0	-0.083	-0.029	19.798	0.000	0.000	0.000	0.000	0.000	0.000

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