FMO DATABASE

FMODB ID: 59K9Z

Calculation Name: 1F3U-A-Xray308

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1F3U

Chain ID: A

ChEMBL ID:

UniProt ID: P35269

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	118
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-778429.187023
FMO2-HF: Nuclear repulsion	734509.274121
FMO2-HF: Total energy	-43919.912902
FMO2-MP2: Total energy	-44050.177578

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:ALA )

Summations of interaction energy for fragment #1(A:2: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.
-50.099	-43.343	1.616	-4.606	-3.766	-0.044

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.812 / q_NPA : 0.896

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	4	ARG	1	1.004	0.979	3.800	30.477	31.753	-0.017	-0.570	-0.689	0.000
4	A	5	GLY	0	0.010	0.006	6.811	1.475	1.475	0.000	0.000	0.000	0.000
5	A	6	GLU	-1	-0.899	-0.937	2.509	-89.222	-83.959	1.632	-4.005	-2.890	-0.044
6	A	7	LEU	0	-0.039	-0.007	5.466	0.105	0.105	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.883	-0.950	4.943	-43.768	-43.676	0.000	-0.009	-0.083	0.000
8	A	9	LEU	0	0.035	-0.003	6.332	5.599	5.599	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.044	-0.017	7.918	4.278	4.278	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.092	0.048	10.531	2.280	2.280	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.000	-0.008	13.081	1.766	1.766	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.946	0.963	12.789	23.511	23.511	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.048	-0.006	13.734	0.307	0.307	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.058	-0.022	16.210	1.024	1.024	0.000	0.000	0.000	0.000
15	A	16	THR	0	0.007	0.019	16.044	0.946	0.946	0.000	0.000	0.000	0.000
16	A	17	GLY	0	-0.004	0.006	18.528	-0.114	-0.114	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.001	0.000	19.403	0.180	0.180	0.000	0.000	0.000	0.000
18	A	19	TRP	0	0.004	-0.010	22.457	0.593	0.593	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.001	0.005	24.433	-0.245	-0.245	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.003	-0.019	26.309	0.408	0.408	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.931	0.982	29.080	8.635	8.635	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.022	0.003	30.185	0.281	0.281	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.008	0.015	32.772	-0.038	-0.038	0.000	0.000	0.000	0.000
24	A	25	LYS	1	1.020	0.992	30.920	9.501	9.501	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.081	0.034	35.262	-0.136	-0.136	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.024	0.026	34.484	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.002	-0.002	30.858	-0.139	-0.139	0.000	0.000	0.000	0.000
28	A	29	GLN	0	-0.033	-0.027	32.139	-0.232	-0.232	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.037	-0.024	34.434	-0.070	-0.070	0.000	0.000	0.000	0.000
30	A	31	TRP	0	-0.013	-0.021	29.140	-0.152	-0.152	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.019	-0.002	30.674	-0.188	-0.188	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.876	0.953	31.718	8.082	8.082	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.005	0.019	30.940	0.189	0.189	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.034	0.016	32.107	-0.072	-0.072	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.023	0.005	32.113	-0.054	-0.054	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.929	0.951	28.922	9.332	9.332	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.029	0.032	27.880	-0.384	-0.384	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.981	-0.983	29.203	-9.547	-9.547	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.037	0.007	30.690	0.256	0.256	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.013	-0.007	33.022	0.319	0.319	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.889	0.950	33.363	8.479	8.479	0.000	0.000	0.000	0.000
42	A	43	LEU	0	0.025	0.027	30.342	0.156	0.156	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.946	0.969	33.807	7.497	7.497	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.022	0.007	31.919	0.033	0.033	0.000	0.000	0.000	0.000
45	A	46	ALA	0	-0.022	-0.009	36.512	0.045	0.045	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.948	0.973	34.717	8.763	8.763	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.064	0.026	40.922	0.083	0.083	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.008	-0.002	43.526	-0.079	-0.079	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.013	0.004	43.149	0.062	0.062	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.883	0.938	42.932	7.121	7.121	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.028	-0.016	36.792	-0.110	-0.110	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.862	-0.919	40.242	-7.111	-7.111	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.008	-0.011	34.004	-0.116	-0.116	0.000	0.000	0.000	0.000
54	A	55	SER	0	0.019	0.023	37.044	0.052	0.052	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.028	0.013	32.981	-0.226	-0.226	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.011	0.004	36.410	0.287	0.287	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.004	-0.001	36.000	-0.208	-0.208	0.000	0.000	0.000	0.000
58	A	59	ASN	0	0.029	0.012	35.184	0.336	0.336	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.895	-0.962	38.338	-6.966	-6.966	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.861	-0.920	37.966	-7.752	-7.752	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.035	-0.025	34.181	0.076	0.076	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.075	-0.026	38.843	0.098	0.098	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.046	-0.032	41.913	0.320	0.320	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.007	0.022	38.602	0.090	0.090	0.000	0.000	0.000	0.000
65	A	66	HIS	0	-0.014	-0.020	42.274	-0.098	-0.098	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.903	-0.938	42.055	-7.369	-7.369	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.021	-0.043	44.826	0.130	0.130	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.019	0.008	48.241	0.034	0.034	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.022	-0.002	48.828	0.114	0.114	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.886	0.964	46.185	6.648	6.648	0.000	0.000	0.000	0.000
71	A	72	PRO	0	0.044	0.019	50.324	0.090	0.090	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.041	0.013	53.662	0.025	0.025	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.014	0.020	53.324	-0.132	-0.132	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.004	-0.028	49.437	-0.032	-0.032	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.063	-0.046	49.135	-0.098	-0.098	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.045	0.050	46.850	-0.024	-0.024	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.004	-0.015	41.980	0.013	0.013	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.962	0.986	43.543	6.526	6.526	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.932	-0.962	41.222	-7.501	-7.501	0.000	0.000	0.000	0.000
80	A	81	HIS	0	-0.006	0.002	38.043	0.118	0.118	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.051	0.025	38.555	-0.258	-0.258	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.014	-0.023	31.829	-0.181	-0.181	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.018	0.003	37.075	0.173	0.173	0.000	0.000	0.000	0.000
84	A	85	LEU	0	0.000	-0.015	34.057	-0.253	-0.253	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.027	-0.018	33.443	-0.023	-0.023	0.000	0.000	0.000	0.000
86	A	87	SER	0	0.013	-0.003	33.266	-0.299	-0.299	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.021	-0.003	26.809	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.007	0.013	28.881	-0.249	-0.249	0.000	0.000	0.000	0.000
89	A	90	GLY	0	-0.014	0.007	30.174	-0.107	-0.107	0.000	0.000	0.000	0.000
90	A	91	GLN	0	-0.003	-0.031	26.537	0.208	0.208	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.004	0.023	21.306	-0.066	-0.066	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.023	-0.010	22.324	-0.197	-0.197	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.014	0.004	17.098	0.148	0.148	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.008	0.006	16.296	0.437	0.437	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.013	-0.006	12.745	-0.832	-0.832	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.069	-0.029	11.600	0.762	0.762	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.866	-0.941	10.906	-22.634	-22.634	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.077	-0.033	8.964	1.070	1.070	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.049	-0.006	11.388	-0.097	-0.097	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.092	-0.034	8.608	-0.291	-0.291	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.853	-0.930	8.890	-24.926	-24.926	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.870	0.957	3.850	40.809	40.934	0.001	-0.022	-0.104	0.000
103	A	104	LEU	0	0.060	0.030	6.474	3.459	3.459	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.055	-0.038	6.907	-5.551	-5.551	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.003	-0.009	8.920	3.196	3.196	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.813	-0.901	11.477	-24.070	-24.070	0.000	0.000	0.000	0.000
107	A	108	GLY	0	-0.025	-0.020	13.738	0.604	0.604	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.047	-0.017	16.827	-0.038	-0.038	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.027	-0.019	20.039	0.456	0.456	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.009	-0.004	23.322	0.312	0.312	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.049	-0.019	25.899	0.524	0.524	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.957	0.994	27.824	10.155	10.155	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.022	0.009	30.112	0.351	0.351	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.905	-0.947	32.105	-8.542	-8.542	0.000	0.000	0.000	0.000
115	A	116	CYS	0	-0.052	-0.007	34.086	0.283	0.283	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.892	0.925	35.810	7.893	7.893	0.000	0.000	0.000	0.000
117	A	118	PRO	0	-0.021	-0.026	39.424	-0.043	-0.043	0.000	0.000	0.000	0.000
118	A	119	ALA	-1	-0.919	-0.942	41.228	-6.825	-6.825	0.000	0.000	0.000	0.000

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