FMO DATABASE

FMODB ID: 52NMZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-812722.55791
FMO2-HF: Nuclear repulsion	772113.972864
FMO2-HF: Total energy	-40608.585046
FMO2-MP2: Total energy	-40728.350932

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.
-13.747	-7.042	1.134	-3.239	-4.6	-0.01

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 : -0.046 / 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

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	-0.877	-0.925	3.851	-3.131	-0.890	-0.012	-1.149	-1.079	0.003
4	A	4	LEU	0	-0.022	-0.014	6.403	0.517	0.517	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.010	0.019	9.011	0.245	0.245	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.029	-0.004	12.677	0.034	0.034	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.021	-0.018	14.692	0.082	0.082	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.004	-0.051	18.049	0.032	0.032	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.007	0.001	20.351	0.006	0.006	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.901	-0.934	20.201	-0.225	-0.225	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.023	-0.018	20.805	-0.020	-0.020	0.000	0.000	0.000	0.000
12	A	12	TYR	0	-0.029	-0.020	17.541	0.003	0.003	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.082	0.022	13.068	0.009	0.009	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.866	-0.921	15.161	-0.297	-0.297	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.021	-0.015	16.632	0.014	0.014	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.042	-0.011	16.793	0.016	0.016	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.020	-0.004	13.265	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	PRO	0	0.010	0.019	14.292	-0.031	-0.031	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.010	-0.011	13.965	0.042	0.042	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.010	-0.009	8.076	0.043	0.043	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.010	-0.009	8.985	-0.106	-0.106	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.089	-0.036	9.864	0.142	0.142	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.071	-0.021	6.350	0.251	0.251	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.019	-0.015	3.231	-0.819	-0.136	0.042	-0.256	-0.469	0.001
25	A	25	HIS	0	-0.021	-0.002	2.526	-6.976	-3.430	1.097	-1.881	-2.763	-0.014
26	A	26	THR	0	0.012	0.016	3.447	1.898	2.133	0.007	0.047	-0.289	0.000
27	A	27	VAL	0	0.011	-0.004	5.877	-0.301	-0.301	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.778	0.878	9.363	1.265	1.265	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.015	0.002	12.255	-0.051	-0.051	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.005	0.003	15.714	0.036	0.036	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.076	0.047	18.784	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.001	0.040	21.864	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.923	-0.979	23.093	-0.254	-0.254	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.016	-0.012	23.842	-0.031	-0.031	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.004	-0.002	24.834	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.053	-0.008	20.006	0.000	0.000	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.014	0.005	19.850	-0.055	-0.055	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.101	-0.055	20.486	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.878	-0.943	17.234	-0.548	-0.548	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.054	0.005	15.823	-0.071	-0.071	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.004	-0.008	14.410	-0.113	-0.113	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.067	-0.056	11.377	0.041	0.041	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.044	0.055	9.991	-0.188	-0.188	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.848	-0.924	5.748	-4.162	-4.162	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.020	-0.028	8.576	0.253	0.253	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.019	-0.009	11.032	-0.029	-0.029	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.016	-0.010	11.215	0.084	0.084	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.012	-0.003	15.136	0.049	0.049	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.798	-0.871	18.783	-0.369	-0.369	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.032	-0.019	20.222	0.037	0.037	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.752	0.867	20.477	0.352	0.352	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.026	-0.017	24.307	0.035	0.035	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.827	-0.880	26.722	-0.229	-0.229	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.062	0.029	26.504	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.021	-0.006	27.987	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.045	-0.048	27.907	-0.015	-0.015	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.084	0.049	24.437	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.912	0.936	24.455	0.237	0.237	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.051	-0.031	26.384	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.006	-0.007	22.608	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	61	CYS	0	-0.021	-0.007	21.803	-0.038	-0.038	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.860	0.933	22.664	0.281	0.281	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.032	-0.006	24.779	0.004	0.004	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.012	0.009	18.491	0.002	0.002	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.063	0.028	20.203	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.092	-0.046	21.585	0.040	0.040	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.033	-0.057	23.309	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.002	0.015	23.055	0.014	0.014	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.840	0.941	18.306	0.588	0.588	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.021	0.001	15.996	0.030	0.030	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.042	-0.001	12.152	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.025	0.030	11.521	0.097	0.097	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.010	-0.016	14.018	-0.087	-0.087	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.005	0.002	12.860	0.044	0.044	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.010	0.004	16.433	0.014	0.014	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.025	-0.007	16.232	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.010	0.004	19.047	0.036	0.036	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.027	0.005	22.312	0.005	0.005	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.879	-0.970	24.837	-0.184	-0.184	0.000	0.000	0.000	0.000
80	A	80	GLY	0	-0.034	-0.015	26.709	0.005	0.005	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.002	-0.002	27.771	0.009	0.009	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.019	0.001	23.464	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.045	-0.014	26.949	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.028	-0.008	29.211	0.006	0.006	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.003	0.017	23.841	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.012	-0.032	27.083	0.018	0.018	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.039	0.002	26.350	-0.021	-0.021	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.880	-0.889	26.632	-0.292	-0.292	0.000	0.000	0.000	0.000
89	A	89	TRP	0	-0.001	-0.018	23.900	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	90	GLY	0	-0.017	0.000	23.594	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.053	-0.024	19.822	-0.029	-0.029	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.824	-0.901	16.005	-0.699	-0.699	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.814	-0.906	15.081	-0.564	-0.564	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.040	-0.008	17.551	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.004	0.000	13.078	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.040	0.036	17.750	0.024	0.024	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.037	0.023	18.512	-0.024	-0.024	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.032	-0.016	18.799	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	99	THR	0	-0.045	-0.032	15.648	0.038	0.038	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.043	0.020	16.368	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.059	0.010	11.840	-0.066	-0.066	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.019	-0.014	11.363	-0.079	-0.079	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.868	-0.922	12.414	-0.390	-0.390	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.047	0.022	9.652	-0.085	-0.085	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.785	-0.880	6.127	-0.928	-0.928	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.047	-0.025	8.609	-0.193	-0.193	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.792	0.860	11.203	0.435	0.435	0.000	0.000	0.000	0.000
108	A	108	LEU	0	0.008	0.006	7.292	-0.046	-0.046	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.837	0.894	5.938	0.486	0.486	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.081	-0.043	8.152	0.015	0.015	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.021	0.002	10.761	0.052	0.052	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.010	0.009	6.734	0.041	0.041	0.000	0.000	0.000	0.000
113	A	113	GLY	0	-0.064	-0.015	8.798	0.283	0.283	0.000	0.000	0.000	0.000

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