FMO DATABASE

FMODB ID: 98M92

Calculation Name: 1O3U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O3U

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZ82

Base Structure: X-ray

Registration Date: 2023-09-22

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	125
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1099897.632396
FMO2-HF: Nuclear repulsion	1048387.598229
FMO2-HF: Total energy	-51510.034167
FMO2-MP2: Total energy	-51658.492541

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:HIS)

Summations of interaction energy for fragment #1(A:-2:HIS)

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.
-20.56	-10.365	4.769	-4.983	-9.98	0.024

Interaction energy analysis for fragmet #1(A:-2:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.043 / q_NPA : 0.019

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

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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	0	HIS	0	0.015	0.008	3.683	-0.637	1.568	-0.003	-1.008	-1.194	0.004
4	A	1	MET	0	0.024	0.017	2.335	0.252	1.135	2.243	-1.071	-2.054	-0.003
5	A	2	ASP	-1	-0.914	-0.946	3.918	-8.098	-7.688	0.003	-0.117	-0.296	0.000
6	A	3	ALA	0	0.019	-0.002	5.739	1.269	1.269	0.000	0.000	0.000	0.000
7	A	4	ALA	0	-0.006	0.002	7.079	0.584	0.584	0.000	0.000	0.000	0.000
8	A	5	LYS	1	0.840	0.912	7.946	2.517	2.517	0.000	0.000	0.000	0.000
9	A	6	ASP	-1	-0.862	-0.932	9.671	-2.070	-2.070	0.000	0.000	0.000	0.000
10	A	7	ASP	-1	-0.832	-0.910	11.731	-0.912	-0.912	0.000	0.000	0.000	0.000
11	A	8	LEU	0	-0.072	-0.035	12.613	0.207	0.207	0.000	0.000	0.000	0.000
12	A	9	GLU	-1	-0.930	-0.964	13.863	-0.821	-0.821	0.000	0.000	0.000	0.000
13	A	10	HIS	0	0.005	0.000	15.702	0.132	0.132	0.000	0.000	0.000	0.000
14	A	11	ALA	0	0.012	-0.007	17.207	0.107	0.107	0.000	0.000	0.000	0.000
15	A	12	LYS	1	0.855	0.927	16.491	0.777	0.777	0.000	0.000	0.000	0.000
16	A	13	HIS	0	0.043	0.034	19.950	0.077	0.077	0.000	0.000	0.000	0.000
17	A	14	ASP	-1	-0.873	-0.952	21.689	-0.453	-0.453	0.000	0.000	0.000	0.000
18	A	15	LEU	0	-0.058	-0.041	22.885	0.058	0.058	0.000	0.000	0.000	0.000
19	A	16	GLU	-1	-1.015	-0.996	24.303	-0.427	-0.427	0.000	0.000	0.000	0.000
20	A	17	HIS	1	0.840	0.913	25.447	0.464	0.464	0.000	0.000	0.000	0.000
21	A	18	GLY	0	-0.013	0.007	27.997	0.021	0.021	0.000	0.000	0.000	0.000
22	A	19	PHE	0	-0.040	-0.013	26.162	0.031	0.031	0.000	0.000	0.000	0.000
23	A	20	TYR	0	0.011	-0.014	25.773	-0.019	-0.019	0.000	0.000	0.000	0.000
24	A	21	ASN	0	0.012	0.010	25.390	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	22	TRP	0	0.038	0.013	22.897	0.007	0.007	0.000	0.000	0.000	0.000
26	A	23	ALA	0	0.054	0.035	21.414	-0.034	-0.034	0.000	0.000	0.000	0.000
27	A	24	CYS	0	-0.042	0.002	20.419	-0.022	-0.022	0.000	0.000	0.000	0.000
28	A	25	PHE	0	0.022	0.002	19.839	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	26	SER	0	0.022	0.007	17.260	-0.016	-0.016	0.000	0.000	0.000	0.000
30	A	27	SER	0	-0.002	-0.011	15.747	-0.089	-0.089	0.000	0.000	0.000	0.000
31	A	28	GLN	0	-0.066	-0.043	15.538	-0.038	-0.038	0.000	0.000	0.000	0.000
32	A	29	GLN	0	0.002	0.008	14.307	-0.043	-0.043	0.000	0.000	0.000	0.000
33	A	30	ALA	0	0.025	0.012	11.446	-0.073	-0.073	0.000	0.000	0.000	0.000
34	A	31	ALA	0	-0.010	-0.011	10.513	-0.067	-0.067	0.000	0.000	0.000	0.000
35	A	32	GLU	-1	-0.923	-0.963	11.261	-0.121	-0.121	0.000	0.000	0.000	0.000
36	A	33	LYS	1	0.806	0.901	7.954	1.292	1.292	0.000	0.000	0.000	0.000
37	A	34	ALA	0	0.026	0.010	6.599	-0.139	-0.139	0.000	0.000	0.000	0.000
38	A	35	VAL	0	0.043	0.007	6.853	0.500	0.500	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.901	0.970	7.911	-0.094	-0.094	0.000	0.000	0.000	0.000
40	A	37	ALA	0	-0.011	-0.019	2.769	-0.229	0.345	0.147	-0.177	-0.543	-0.001
41	A	38	VAL	0	0.004	0.009	3.424	1.002	2.047	0.022	-0.496	-0.571	-0.004
42	A	39	PHE	0	0.012	0.003	5.655	0.814	0.814	0.000	0.000	0.000	0.000
43	A	40	GLN	0	-0.058	-0.027	3.993	-0.962	-0.627	0.001	-0.085	-0.251	0.000
44	A	41	ARG	1	0.891	0.956	2.818	-12.501	-9.870	0.780	-1.108	-2.303	0.016
45	A	42	MET	0	-0.045	-0.020	4.751	-0.764	-0.742	-0.001	-0.014	-0.007	0.000
46	A	43	GLY	0	-0.036	-0.001	7.800	-0.589	-0.589	0.000	0.000	0.000	0.000
47	A	44	ALA	0	-0.037	-0.014	9.620	-0.463	-0.463	0.000	0.000	0.000	0.000
48	A	45	GLN	0	-0.052	-0.027	10.763	0.066	0.066	0.000	0.000	0.000	0.000
49	A	46	ALA	0	-0.020	-0.009	11.227	0.027	0.027	0.000	0.000	0.000	0.000
50	A	47	TRP	0	-0.090	-0.054	13.288	-0.161	-0.161	0.000	0.000	0.000	0.000
51	A	48	GLY	0	0.050	0.032	16.926	0.011	0.011	0.000	0.000	0.000	0.000
52	A	49	TYR	0	-0.110	-0.057	17.036	-0.017	-0.017	0.000	0.000	0.000	0.000
53	A	50	SER	0	0.068	0.065	16.708	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	51	VAL	0	0.024	0.000	14.433	0.051	0.051	0.000	0.000	0.000	0.000
55	A	52	PRO	0	-0.010	-0.020	16.281	0.088	0.088	0.000	0.000	0.000	0.000
56	A	53	ASP	-1	-0.821	-0.906	17.870	0.245	0.245	0.000	0.000	0.000	0.000
57	A	54	PHE	0	0.002	0.000	12.660	0.105	0.105	0.000	0.000	0.000	0.000
58	A	55	LEU	0	-0.003	-0.019	13.209	0.165	0.165	0.000	0.000	0.000	0.000
59	A	56	GLY	0	0.025	0.022	15.378	0.066	0.066	0.000	0.000	0.000	0.000
60	A	57	GLU	-1	-0.843	-0.933	15.316	0.696	0.696	0.000	0.000	0.000	0.000
61	A	58	LEU	0	-0.032	-0.022	10.277	0.130	0.130	0.000	0.000	0.000	0.000
62	A	59	SER	0	0.015	0.004	14.125	0.089	0.089	0.000	0.000	0.000	0.000
63	A	60	SER	0	-0.102	-0.023	16.903	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	61	ARG	1	0.850	0.932	13.230	-1.415	-1.415	0.000	0.000	0.000	0.000
65	A	62	PHE	0	-0.045	-0.051	10.496	0.142	0.142	0.000	0.000	0.000	0.000
66	A	63	GLU	-1	-0.870	-0.926	15.257	0.486	0.486	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.044	-0.026	13.877	0.084	0.084	0.000	0.000	0.000	0.000
68	A	65	PRO	0	0.002	0.001	16.947	-0.065	-0.065	0.000	0.000	0.000	0.000
69	A	66	GLU	-1	-0.869	-0.942	19.846	0.192	0.192	0.000	0.000	0.000	0.000
70	A	67	GLU	-1	-0.846	-0.919	21.142	0.121	0.121	0.000	0.000	0.000	0.000
71	A	68	LEU	0	-0.032	-0.021	15.144	-0.049	-0.049	0.000	0.000	0.000	0.000
72	A	69	MET	0	0.016	0.021	18.560	-0.039	-0.039	0.000	0.000	0.000	0.000
73	A	70	ASP	-1	-0.873	-0.937	20.279	0.103	0.103	0.000	0.000	0.000	0.000
74	A	71	HIS	0	-0.061	-0.043	19.218	-0.042	-0.042	0.000	0.000	0.000	0.000
75	A	72	ALA	0	0.037	0.016	17.808	-0.051	-0.051	0.000	0.000	0.000	0.000
76	A	73	LEU	0	0.016	0.006	19.252	-0.035	-0.035	0.000	0.000	0.000	0.000
77	A	74	GLU	-1	-0.950	-0.985	22.716	-0.051	-0.051	0.000	0.000	0.000	0.000
78	A	75	LEU	0	-0.048	-0.031	16.850	-0.030	-0.030	0.000	0.000	0.000	0.000
79	A	76	ASP	-1	-0.868	-0.924	20.790	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	77	LYS	1	0.873	0.966	21.709	0.006	0.006	0.000	0.000	0.000	0.000
81	A	78	ALA	0	-0.015	-0.001	24.301	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	80	ILE	0	-0.016	-0.033	25.528	0.009	0.009	0.000	0.000	0.000	0.000
83	A	81	PRO	0	-0.019	0.000	26.705	0.006	0.006	0.000	0.000	0.000	0.000
84	A	82	THR	0	0.000	-0.008	29.916	0.009	0.009	0.000	0.000	0.000	0.000
85	A	83	ARG	1	0.860	0.913	28.016	0.162	0.162	0.000	0.000	0.000	0.000
86	A	84	TYR	0	-0.053	-0.026	31.577	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	85	PRO	0	0.007	0.019	33.033	0.010	0.010	0.000	0.000	0.000	0.000
88	A	86	ASP	-1	-0.907	-0.967	35.759	-0.075	-0.075	0.000	0.000	0.000	0.000
89	A	87	ALA	0	0.033	0.025	38.935	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	88	LEU	0	-0.043	-0.007	37.064	0.003	0.003	0.000	0.000	0.000	0.000
91	A	89	PRO	0	0.024	0.005	40.990	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	90	SER	0	0.049	-0.001	40.555	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	91	GLY	0	0.014	0.029	40.199	0.005	0.005	0.000	0.000	0.000	0.000
94	A	92	SER	0	0.031	-0.005	39.012	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	93	PRO	0	-0.018	-0.007	38.212	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	94	ARG	1	0.983	1.003	35.988	0.110	0.110	0.000	0.000	0.000	0.000
97	A	95	ASN	0	0.029	0.002	34.506	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	96	ARG	1	0.946	0.977	33.367	0.107	0.107	0.000	0.000	0.000	0.000
99	A	97	TYR	0	0.015	0.023	31.495	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	98	SER	0	-0.016	-0.025	30.707	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	99	ARG	1	0.864	0.941	27.401	0.267	0.267	0.000	0.000	0.000	0.000
102	A	100	ILE	0	0.009	0.006	28.008	-0.012	-0.012	0.000	0.000	0.000	0.000
103	A	101	GLU	-1	-0.851	-0.908	26.909	-0.141	-0.141	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.036	0.010	24.650	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	103	GLU	-1	-0.859	-0.929	23.209	-0.261	-0.261	0.000	0.000	0.000	0.000
106	A	104	ARG	1	0.842	0.942	22.786	0.075	0.075	0.000	0.000	0.000	0.000
107	A	105	LEU	0	0.025	0.004	21.161	0.006	0.006	0.000	0.000	0.000	0.000
108	A	106	VAL	0	0.070	0.039	18.440	-0.018	-0.018	0.000	0.000	0.000	0.000
109	A	107	ASN	0	-0.030	-0.026	17.789	-0.068	-0.068	0.000	0.000	0.000	0.000
110	A	108	TYR	0	-0.021	-0.011	18.110	0.023	0.023	0.000	0.000	0.000	0.000
111	A	109	ALA	0	0.051	0.032	14.569	0.051	0.051	0.000	0.000	0.000	0.000
112	A	110	GLU	-1	-0.895	-0.944	13.530	-0.602	-0.602	0.000	0.000	0.000	0.000
113	A	111	LYS	1	0.793	0.886	13.756	-0.027	-0.027	0.000	0.000	0.000	0.000
114	A	112	ILE	0	0.037	0.020	11.665	0.099	0.099	0.000	0.000	0.000	0.000
115	A	113	ILE	0	0.013	-0.003	8.588	0.176	0.176	0.000	0.000	0.000	0.000
116	A	114	ARG	1	0.943	0.979	9.416	0.572	0.572	0.000	0.000	0.000	0.000
117	A	115	PHE	0	0.037	0.035	11.690	0.196	0.196	0.000	0.000	0.000	0.000
118	A	116	CYS	0	-0.038	-0.025	7.259	0.336	0.336	0.000	0.000	0.000	0.000
119	A	117	GLU	-1	-0.859	-0.925	6.725	-0.243	-0.243	0.000	0.000	0.000	0.000
120	A	118	ASP	-1	-0.860	-0.927	7.881	1.022	1.022	0.000	0.000	0.000	0.000
121	A	119	LEU	0	-0.043	-0.008	8.584	0.146	0.146	0.000	0.000	0.000	0.000
122	A	120	LEU	0	-0.018	-0.020	2.712	-2.125	-0.159	1.578	-0.905	-2.640	0.012
123	A	121	SER	0	-0.075	-0.032	5.191	0.284	0.408	-0.001	-0.002	-0.121	0.000
124	A	122	ARG	1	0.831	0.895	7.061	-1.706	-1.706	0.000	0.000	0.000	0.000
125	A	123	ILE	0	-0.071	-0.010	6.007	-0.143	-0.143	0.000	0.000	0.000	0.000

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