FMO DATABASE

FMODB ID: YZN32

Calculation Name: 4O1I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4O1I

Chain ID: A

ChEMBL ID:

UniProt ID: O53830

Base Structure: X-ray

Registration Date: 2023-06-22

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	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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-815802.6868
FMO2-HF: Nuclear repulsion	775193.858601
FMO2-HF: Total energy	-40608.828198
FMO2-MP2: Total energy	-40728.599428

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:1:MET)

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

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.
-20.229	-14.789	8.552	-5.679	-8.313	-0.029

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.053 / q_NPA : -0.028

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	3	GLU	-1	-0.857	-0.906	3.862	-3.082	-0.975	-0.014	-1.089	-1.005	0.002
4	A	4	LEU	0	-0.017	-0.004	6.588	0.384	0.384	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.002	0.013	9.099	0.210	0.210	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.031	-0.009	12.797	0.020	0.020	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.012	-0.004	14.945	0.073	0.073	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.015	-0.053	18.133	0.036	0.036	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.000	-0.004	20.496	0.007	0.007	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.873	-0.914	19.832	-0.234	-0.234	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.044	-0.029	20.577	-0.027	-0.027	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.023	-0.012	17.093	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.086	0.026	12.638	0.016	0.016	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.850	-0.899	14.721	-0.305	-0.305	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.031	-0.022	16.237	0.030	0.030	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.030	-0.013	16.265	0.024	0.024	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.027	-0.001	12.725	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	PRO	0	0.006	0.018	13.757	-0.025	-0.025	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.009	-0.006	13.489	0.053	0.053	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.001	-0.005	7.568	0.085	0.085	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.010	-0.036	8.531	-0.082	-0.082	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.073	-0.024	10.279	0.141	0.141	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.054	-0.014	5.416	0.335	0.335	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.040	-0.023	2.598	-2.033	-0.676	0.940	-0.901	-1.395	0.008
25	A	25	HIS	0	-0.019	-0.009	2.226	-12.946	-10.912	7.578	-4.050	-5.562	-0.039
26	A	26	THR	0	-0.004	-0.001	3.187	2.564	2.506	0.048	0.361	-0.351	0.000
27	A	27	VAL	0	0.006	-0.010	5.801	-0.152	-0.152	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.763	0.874	9.356	1.402	1.402	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.011	-0.009	12.455	-0.034	-0.034	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.011	0.006	15.878	0.029	0.029	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.068	0.037	19.095	0.000	0.000	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.009	0.035	21.884	-0.040	-0.040	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.900	-0.943	23.289	-0.292	-0.292	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.010	-0.019	23.937	-0.033	-0.033	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.045	-0.038	25.461	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.027	-0.015	20.271	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.022	-0.004	20.286	-0.062	-0.062	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.051	-0.024	20.559	-0.039	-0.039	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.847	-0.914	17.753	-0.700	-0.700	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.029	-0.010	16.052	-0.088	-0.088	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.000	0.001	14.356	-0.148	-0.148	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.064	-0.047	11.117	0.117	0.117	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.022	0.036	9.598	-0.272	-0.272	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.841	-0.926	5.588	-4.678	-4.678	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.010	-0.023	8.388	0.324	0.324	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.037	-0.024	11.207	-0.061	-0.061	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.009	0.007	11.002	0.128	0.128	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.006	-0.008	14.875	0.040	0.040	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.758	-0.844	18.595	-0.352	-0.352	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.046	-0.015	20.302	0.040	0.040	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.711	0.843	19.700	0.346	0.346	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.009	-0.004	23.630	0.042	0.042	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.804	-0.873	26.232	-0.232	-0.232	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.054	0.020	26.104	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.046	-0.013	27.826	-0.012	-0.012	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.045	-0.050	27.288	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.056	0.032	23.980	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.920	0.948	24.113	0.226	0.226	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.031	-0.018	26.257	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.003	-0.005	22.407	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	61	CYS	0	-0.025	0.002	21.555	-0.045	-0.045	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.847	0.912	22.534	0.270	0.270	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.040	-0.014	24.687	0.002	0.002	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.007	0.005	18.599	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.046	0.027	20.036	-0.030	-0.030	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.075	-0.040	21.598	0.034	0.034	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.015	-0.047	23.285	-0.027	-0.027	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.022	0.008	23.587	0.018	0.018	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.807	0.918	18.179	0.646	0.646	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.005	-0.013	16.388	0.050	0.050	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.022	0.023	12.083	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.000	0.013	11.642	0.100	0.100	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.015	-0.006	14.334	-0.081	-0.081	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.002	0.001	12.693	0.053	0.053	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.005	0.001	16.197	0.002	0.002	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.026	-0.009	15.735	0.010	0.010	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.004	-0.007	18.560	0.027	0.027	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.023	-0.002	21.848	0.013	0.013	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.915	-0.972	24.440	-0.127	-0.127	0.000	0.000	0.000	0.000
80	A	80	GLY	0	-0.024	-0.014	26.171	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.006	-0.001	27.274	0.006	0.006	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.022	-0.002	23.189	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.043	-0.015	26.815	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.021	-0.004	29.139	0.006	0.006	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.004	0.015	23.501	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.005	-0.030	26.724	0.017	0.017	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.035	0.003	25.921	-0.020	-0.020	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.795	-0.853	26.347	-0.281	-0.281	0.000	0.000	0.000	0.000
89	A	89	TRP	0	-0.042	-0.026	23.488	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	90	GLY	0	-0.022	0.002	23.782	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.031	-0.027	19.301	-0.033	-0.033	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.829	-0.902	16.193	-0.668	-0.668	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.815	-0.892	14.657	-0.427	-0.427	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.053	-0.026	17.077	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.003	0.002	12.706	0.000	0.000	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.041	0.037	17.315	0.012	0.012	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.036	0.019	17.806	-0.019	-0.019	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.032	-0.017	18.547	0.001	0.001	0.000	0.000	0.000	0.000
99	A	99	THR	0	-0.046	-0.028	15.111	0.041	0.041	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.056	0.027	15.569	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.039	0.006	11.015	-0.049	-0.049	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.003	-0.006	10.746	-0.041	-0.041	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.880	-0.919	11.871	-0.217	-0.217	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.034	0.013	9.180	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.765	-0.859	5.677	0.058	0.058	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.056	-0.022	8.062	-0.147	-0.147	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.785	0.848	10.703	0.277	0.277	0.000	0.000	0.000	0.000
108	A	108	LEU	0	0.016	0.014	7.008	-0.069	-0.069	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.847	0.892	5.493	-0.224	-0.224	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.059	-0.021	7.846	-0.017	-0.017	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.013	0.003	10.858	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.010	0.010	6.475	0.001	0.001	0.000	0.000	0.000	0.000
113	A	113	GLY	0	-0.114	-0.058	9.702	0.177	0.177	0.000	0.000	0.000	0.000

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