FMO DATABASE

FMODB ID: MN9YZ

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:

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	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1100719.439099
FMO2-HF: Nuclear repulsion	1049208.784905
FMO2-HF: Total energy	-51510.654193
FMO2-MP2: Total energy	-51659.132364

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.
-23.671	-12.418	5.843	-5.633	-11.466	0.022

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 : 0.038 / 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

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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	0.010	0.011	3.666	-0.290	1.948	-0.003	-1.011	-1.225	0.004
4	A	1	MET	0	0.030	0.021	2.445	0.256	1.240	1.772	-0.898	-1.857	-0.003
5	A	2	ASP	-1	-0.908	-0.945	3.878	-9.689	-9.135	0.005	-0.225	-0.335	-0.001
6	A	3	ALA	0	0.017	-0.001	5.868	1.285	1.285	0.000	0.000	0.000	0.000
7	A	4	ALA	0	-0.005	0.003	6.978	0.600	0.600	0.000	0.000	0.000	0.000
8	A	5	LYS	1	0.820	0.887	7.903	2.626	2.626	0.000	0.000	0.000	0.000
9	A	6	ASP	-1	-0.865	-0.930	9.783	-2.014	-2.014	0.000	0.000	0.000	0.000
10	A	7	ASP	-1	-0.799	-0.889	11.644	-0.922	-0.922	0.000	0.000	0.000	0.000
11	A	8	LEU	0	-0.074	-0.038	12.565	0.220	0.220	0.000	0.000	0.000	0.000
12	A	9	GLU	-1	-0.917	-0.957	13.977	-0.796	-0.796	0.000	0.000	0.000	0.000
13	A	10	HIS	0	-0.002	0.000	15.825	0.101	0.101	0.000	0.000	0.000	0.000
14	A	11	ALA	0	0.004	-0.009	17.167	0.111	0.111	0.000	0.000	0.000	0.000
15	A	12	LYS	1	0.839	0.910	15.889	0.826	0.826	0.000	0.000	0.000	0.000
16	A	13	HIS	0	0.017	0.020	20.066	0.080	0.080	0.000	0.000	0.000	0.000
17	A	14	ASP	-1	-0.838	-0.942	21.782	-0.470	-0.470	0.000	0.000	0.000	0.000
18	A	15	LEU	0	-0.057	-0.036	22.924	0.059	0.059	0.000	0.000	0.000	0.000
19	A	16	GLU	-1	-0.959	-0.965	24.417	-0.428	-0.428	0.000	0.000	0.000	0.000
20	A	17	HIS	1	0.790	0.884	25.379	0.488	0.488	0.000	0.000	0.000	0.000
21	A	18	GLY	0	-0.019	0.002	28.080	0.022	0.022	0.000	0.000	0.000	0.000
22	A	19	PHE	0	-0.052	-0.015	26.026	0.031	0.031	0.000	0.000	0.000	0.000
23	A	20	TYR	0	0.019	-0.009	25.677	-0.020	-0.020	0.000	0.000	0.000	0.000
24	A	21	ASN	0	0.005	0.002	25.302	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	22	TRP	0	0.040	0.015	23.082	0.007	0.007	0.000	0.000	0.000	0.000
26	A	23	ALA	0	0.056	0.040	21.319	-0.035	-0.035	0.000	0.000	0.000	0.000
27	A	24	CYS	0	-0.042	0.004	20.331	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	25	PHE	0	0.021	0.005	19.952	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	26	SER	0	0.026	0.007	17.220	-0.011	-0.011	0.000	0.000	0.000	0.000
30	A	27	SER	0	0.003	-0.016	15.657	-0.091	-0.091	0.000	0.000	0.000	0.000
31	A	28	GLN	0	-0.060	-0.039	15.463	-0.029	-0.029	0.000	0.000	0.000	0.000
32	A	29	GLN	0	-0.045	-0.011	14.244	-0.086	-0.086	0.000	0.000	0.000	0.000
33	A	30	ALA	0	0.026	0.016	11.361	-0.078	-0.078	0.000	0.000	0.000	0.000
34	A	31	ALA	0	-0.005	-0.013	10.440	-0.068	-0.068	0.000	0.000	0.000	0.000
35	A	32	GLU	-1	-0.862	-0.936	11.212	-0.200	-0.200	0.000	0.000	0.000	0.000
36	A	33	LYS	1	0.760	0.878	7.866	1.247	1.247	0.000	0.000	0.000	0.000
37	A	34	ALA	0	0.019	0.008	6.547	-0.166	-0.166	0.000	0.000	0.000	0.000
38	A	35	VAL	0	0.034	0.003	6.758	0.513	0.513	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.899	0.958	7.723	-0.137	-0.137	0.000	0.000	0.000	0.000
40	A	37	ALA	0	-0.004	-0.012	2.762	-0.269	0.368	0.190	-0.203	-0.624	0.000
41	A	38	VAL	0	0.006	0.006	3.102	0.548	2.109	0.087	-0.789	-0.859	-0.008
42	A	39	PHE	0	0.020	0.006	5.391	0.956	0.988	-0.001	-0.002	-0.029	0.000
43	A	40	GLN	0	-0.057	-0.027	3.544	-1.420	-0.703	0.018	-0.248	-0.488	-0.001
44	A	41	ARG	1	0.860	0.928	2.770	-12.814	-10.088	1.414	-1.265	-2.875	0.018
45	A	42	MET	0	-0.041	-0.023	4.647	-1.178	-1.107	0.000	-0.034	-0.037	0.000
46	A	43	GLY	0	-0.036	-0.001	7.623	-0.693	-0.693	0.000	0.000	0.000	0.000
47	A	44	ALA	0	-0.042	-0.014	9.386	-0.526	-0.526	0.000	0.000	0.000	0.000
48	A	45	GLN	0	-0.050	-0.031	10.473	0.067	0.067	0.000	0.000	0.000	0.000
49	A	46	ALA	0	-0.024	-0.008	10.852	0.029	0.029	0.000	0.000	0.000	0.000
50	A	47	TRP	0	-0.072	-0.048	12.950	-0.180	-0.180	0.000	0.000	0.000	0.000
51	A	48	GLY	0	0.030	0.020	16.582	0.014	0.014	0.000	0.000	0.000	0.000
52	A	49	TYR	0	-0.089	-0.048	16.746	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	50	SER	0	0.029	0.025	16.659	-0.043	-0.043	0.000	0.000	0.000	0.000
54	A	51	VAL	0	0.017	-0.006	14.196	0.055	0.055	0.000	0.000	0.000	0.000
55	A	52	PRO	0	0.006	-0.010	16.052	0.094	0.094	0.000	0.000	0.000	0.000
56	A	53	ASP	-1	-0.807	-0.880	17.408	0.254	0.254	0.000	0.000	0.000	0.000
57	A	54	PHE	0	0.011	0.006	12.328	0.099	0.099	0.000	0.000	0.000	0.000
58	A	55	LEU	0	0.002	-0.016	12.881	0.177	0.177	0.000	0.000	0.000	0.000
59	A	56	GLY	0	0.027	0.028	15.094	0.070	0.070	0.000	0.000	0.000	0.000
60	A	57	GLU	-1	-0.842	-0.923	14.890	0.769	0.769	0.000	0.000	0.000	0.000
61	A	58	LEU	0	-0.032	-0.011	10.169	0.134	0.134	0.000	0.000	0.000	0.000
62	A	59	SER	0	0.009	-0.008	13.865	0.092	0.092	0.000	0.000	0.000	0.000
63	A	60	SER	0	-0.101	-0.031	16.652	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	61	ARG	1	0.843	0.921	13.127	-1.520	-1.520	0.000	0.000	0.000	0.000
65	A	62	PHE	0	-0.045	-0.042	10.531	0.146	0.146	0.000	0.000	0.000	0.000
66	A	63	GLU	-1	-0.861	-0.922	15.109	0.516	0.516	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.042	-0.025	13.814	0.088	0.088	0.000	0.000	0.000	0.000
68	A	65	PRO	0	0.010	0.006	16.779	-0.071	-0.071	0.000	0.000	0.000	0.000
69	A	66	GLU	-1	-0.871	-0.940	19.667	0.219	0.219	0.000	0.000	0.000	0.000
70	A	67	GLU	-1	-0.851	-0.920	20.763	0.142	0.142	0.000	0.000	0.000	0.000
71	A	68	LEU	0	-0.027	-0.020	15.205	-0.053	-0.053	0.000	0.000	0.000	0.000
72	A	69	MET	0	0.024	0.024	18.523	-0.045	-0.045	0.000	0.000	0.000	0.000
73	A	70	ASP	-1	-0.873	-0.940	20.047	0.103	0.103	0.000	0.000	0.000	0.000
74	A	71	HIS	0	-0.083	-0.047	19.358	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	72	ALA	0	0.034	0.015	17.588	-0.053	-0.053	0.000	0.000	0.000	0.000
76	A	73	LEU	0	0.021	0.007	19.218	-0.036	-0.036	0.000	0.000	0.000	0.000
77	A	74	GLU	-1	-0.848	-0.894	22.681	-0.052	-0.052	0.000	0.000	0.000	0.000
78	A	75	LEU	0	-0.051	-0.033	16.839	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	76	ASP	-1	-0.887	-0.937	20.733	-0.021	-0.021	0.000	0.000	0.000	0.000
80	A	77	LYS	1	0.824	0.921	21.655	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	78	ALA	0	-0.019	-0.002	24.233	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	80	ILE	0	-0.009	-0.027	25.427	0.007	0.007	0.000	0.000	0.000	0.000
83	A	81	PRO	0	-0.016	0.000	26.494	0.006	0.006	0.000	0.000	0.000	0.000
84	A	82	THR	0	-0.005	-0.009	29.695	0.010	0.010	0.000	0.000	0.000	0.000
85	A	83	ARG	1	0.865	0.916	27.942	0.160	0.160	0.000	0.000	0.000	0.000
86	A	84	TYR	0	-0.061	-0.037	31.442	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	85	PRO	0	0.014	0.025	32.959	0.010	0.010	0.000	0.000	0.000	0.000
88	A	86	ASP	-1	-0.883	-0.946	35.721	-0.074	-0.074	0.000	0.000	0.000	0.000
89	A	87	ALA	0	0.023	0.013	38.859	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	88	LEU	0	-0.038	-0.002	36.927	0.003	0.003	0.000	0.000	0.000	0.000
91	A	89	PRO	0	0.023	0.002	40.912	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	90	SER	0	0.033	-0.004	40.468	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	91	GLY	0	0.029	0.034	40.119	0.005	0.005	0.000	0.000	0.000	0.000
94	A	92	SER	0	0.012	-0.012	38.914	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	93	PRO	0	0.014	0.008	38.134	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	94	ARG	1	0.959	0.989	35.954	0.107	0.107	0.000	0.000	0.000	0.000
97	A	95	ASN	0	0.028	0.004	34.421	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	96	ARG	1	0.943	0.977	33.287	0.105	0.105	0.000	0.000	0.000	0.000
99	A	97	TYR	0	-0.033	-0.019	31.097	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	98	SER	0	-0.002	-0.022	30.630	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	99	ARG	1	0.833	0.920	27.351	0.272	0.272	0.000	0.000	0.000	0.000
102	A	100	ILE	0	0.008	0.002	27.934	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	101	GLU	-1	-0.800	-0.865	26.989	-0.132	-0.132	0.000	0.000	0.000	0.000
104	A	102	ALA	0	0.019	0.005	24.574	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	103	GLU	-1	-0.827	-0.904	23.135	-0.270	-0.270	0.000	0.000	0.000	0.000
106	A	104	ARG	1	0.794	0.882	22.722	0.063	0.063	0.000	0.000	0.000	0.000
107	A	105	LEU	0	0.033	0.013	21.101	0.006	0.006	0.000	0.000	0.000	0.000
108	A	106	VAL	0	0.075	0.040	18.374	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	107	ASN	0	-0.044	-0.033	17.725	-0.062	-0.062	0.000	0.000	0.000	0.000
110	A	108	TYR	0	-0.020	-0.003	18.064	0.024	0.024	0.000	0.000	0.000	0.000
111	A	109	ALA	0	0.053	0.033	14.561	0.053	0.053	0.000	0.000	0.000	0.000
112	A	110	GLU	-1	-0.818	-0.880	13.478	-0.666	-0.666	0.000	0.000	0.000	0.000
113	A	111	LYS	1	0.799	0.883	13.719	-0.052	-0.052	0.000	0.000	0.000	0.000
114	A	112	ILE	0	0.033	0.020	11.656	0.106	0.106	0.000	0.000	0.000	0.000
115	A	113	ILE	0	0.012	0.002	8.835	0.192	0.192	0.000	0.000	0.000	0.000
116	A	114	ARG	1	0.888	0.936	9.400	0.581	0.581	0.000	0.000	0.000	0.000
117	A	115	PHE	0	0.034	0.027	11.701	0.206	0.206	0.000	0.000	0.000	0.000
118	A	116	CYS	0	-0.041	-0.028	7.167	0.350	0.350	0.000	0.000	0.000	0.000
119	A	117	GLU	-1	-0.828	-0.905	6.517	-0.414	-0.414	0.000	0.000	0.000	0.000
120	A	118	ASP	-1	-0.850	-0.910	8.029	1.043	1.043	0.000	0.000	0.000	0.000
121	A	119	LEU	0	-0.059	-0.013	8.708	0.146	0.146	0.000	0.000	0.000	0.000
122	A	120	LEU	0	-0.024	-0.019	2.697	-2.051	-0.318	2.361	-0.958	-3.137	0.013
123	A	121	SER	0	-0.075	-0.042	5.233	0.218	0.218	0.000	0.000	0.000	0.000
124	A	122	ARG	1	0.840	0.897	7.252	-1.764	-1.764	0.000	0.000	0.000	0.000
125	A	123	ILE	0	-0.059	0.014	5.928	-0.145	-0.145	0.000	0.000	0.000	0.000

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