FMO DATABASE

FMODB ID: ZY74N

Calculation Name: 1F3U-A-Xray372

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: 2023-03-13

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-778701.277681
FMO2-HF: Nuclear repulsion	734780.807969
FMO2-HF: Total energy	-43920.469712
FMO2-MP2: Total energy	-44050.702746

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.
-11.377	-7.386	3.578	-3.999	-3.57	-0.031

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 : 0 / q_Mulliken : -0.050 / q_NPA : -0.033

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	4	ARG	1	0.970	0.962	3.800	0.328	1.616	-0.020	-0.631	-0.637	0.002
4	A	5	GLY	0	-0.004	-0.005	6.800	0.063	0.063	0.000	0.000	0.000	0.000
5	A	6	GLU	-1	-0.904	-0.931	2.369	-11.085	-8.754	3.593	-3.271	-2.653	-0.034
6	A	7	LEU	0	-0.037	-0.011	5.467	0.286	0.286	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.791	-0.888	4.877	0.010	0.107	-0.001	-0.007	-0.089	0.000
8	A	9	LEU	0	0.035	0.001	6.342	0.235	0.235	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.039	-0.019	7.948	0.095	0.095	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.065	0.037	10.412	0.030	0.030	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.001	-0.006	12.987	0.021	0.021	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.958	0.969	12.723	0.329	0.329	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.042	-0.001	13.049	0.050	0.050	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.069	-0.031	16.093	0.009	0.009	0.000	0.000	0.000	0.000
15	A	16	THR	0	0.023	0.020	15.419	0.020	0.020	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.004	0.013	18.442	-0.020	-0.020	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.000	-0.003	19.458	0.015	0.015	0.000	0.000	0.000	0.000
18	A	19	TRP	0	-0.001	-0.010	22.402	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.011	0.013	24.289	0.001	0.001	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.010	-0.027	26.234	0.001	0.001	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.861	0.933	29.020	0.043	0.043	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.022	0.003	30.308	0.004	0.004	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.010	0.007	32.721	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	25	LYS	1	1.022	0.997	30.762	0.042	0.042	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.071	0.019	35.233	0.001	0.001	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.007	0.015	34.597	0.003	0.003	0.000	0.000	0.000	0.000
27	A	28	SER	0	-0.004	-0.002	30.770	0.001	0.001	0.000	0.000	0.000	0.000
28	A	29	GLN	0	-0.029	-0.026	32.110	0.000	0.000	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.010	-0.007	34.410	0.001	0.001	0.000	0.000	0.000	0.000
30	A	31	TRP	0	-0.020	-0.030	29.250	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.008	0.005	30.658	0.004	0.004	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.799	0.904	31.696	0.001	0.001	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.010	0.013	30.931	0.002	0.002	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.022	0.011	32.059	0.002	0.002	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.027	0.009	32.087	0.001	0.001	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.932	0.959	28.889	-0.064	-0.064	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.025	0.029	27.839	0.003	0.003	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.968	-0.981	29.159	0.044	0.044	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.042	0.011	30.494	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.006	-0.008	32.964	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.895	0.954	33.300	-0.023	-0.023	0.000	0.000	0.000	0.000
42	A	43	LEU	0	0.019	0.023	30.204	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.938	0.970	33.789	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.018	-0.001	31.880	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	46	ALA	0	-0.011	-0.001	36.466	0.003	0.003	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.952	0.974	34.562	0.006	0.006	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.056	0.020	40.858	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.011	-0.001	43.451	0.000	0.000	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.003	0.010	43.064	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.836	0.887	42.836	0.008	0.008	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.024	-0.018	36.732	0.003	0.003	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.832	-0.871	40.178	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.006	-0.011	33.903	0.002	0.002	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.063	-0.060	37.005	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.043	0.021	32.843	0.002	0.002	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.018	-0.001	36.337	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.005	0.002	35.833	0.002	0.002	0.000	0.000	0.000	0.000
58	A	59	ASN	0	0.029	0.008	34.999	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.898	-0.963	38.282	0.018	0.018	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.878	-0.928	37.848	0.026	0.026	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.013	-0.008	34.310	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.080	-0.022	38.803	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.041	-0.036	41.867	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.027	0.043	38.759	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	HIS	0	-0.006	-0.016	42.242	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.856	-0.914	41.808	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.001	-0.028	44.806	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.022	0.008	48.225	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.029	-0.004	48.801	0.000	0.000	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.822	0.927	45.521	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	72	PRO	0	0.050	0.018	50.287	0.000	0.000	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.041	0.021	53.620	0.001	0.001	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.002	0.019	53.272	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.002	-0.017	49.305	0.001	0.001	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.056	-0.041	49.731	0.000	0.000	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.074	0.066	46.880	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	PRO	0	0.007	-0.006	41.932	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.911	0.953	43.598	0.000	0.000	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.828	-0.872	41.081	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	81	HIS	0	-0.019	-0.005	38.007	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	PRO	0	0.050	0.025	38.483	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.018	-0.016	31.666	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.033	-0.005	36.999	0.000	0.000	0.000	0.000	0.000	0.000
84	A	85	LEU	0	0.006	-0.009	33.905	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	86	GLN	0	0.018	0.006	33.205	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	87	SER	0	0.019	-0.004	33.197	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.023	-0.005	26.913	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.010	0.018	28.889	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	GLY	0	-0.015	0.006	30.181	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.000	-0.021	26.044	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.002	0.015	21.495	0.005	0.005	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.019	-0.005	22.316	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.010	0.001	17.067	0.015	0.015	0.000	0.000	0.000	0.000
94	A	95	VAL	0	0.004	0.001	16.336	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.013	-0.004	12.662	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.070	-0.051	11.565	0.005	0.005	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.871	-0.942	10.904	-0.388	-0.388	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.072	-0.022	9.017	0.088	0.088	0.000	0.000	0.000	0.000
99	A	100	SER	0	0.040	-0.009	11.399	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.089	-0.038	8.557	0.028	0.028	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.869	-0.933	8.969	-0.339	-0.339	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.797	0.906	3.345	-1.385	-1.110	0.006	-0.090	-0.191	0.001
103	A	104	LEU	0	0.043	0.020	6.473	0.162	0.162	0.000	0.000	0.000	0.000
104	A	105	SER	0	-0.043	-0.042	6.856	-0.136	-0.136	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.015	-0.016	8.848	0.050	0.050	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.805	-0.869	11.301	0.025	0.025	0.000	0.000	0.000	0.000
107	A	108	GLY	0	-0.023	-0.020	13.685	0.035	0.035	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.046	-0.017	16.753	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.026	-0.019	19.956	0.022	0.022	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.006	-0.001	23.251	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.063	-0.029	25.819	0.005	0.005	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.935	0.983	27.767	0.073	0.073	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.013	0.009	30.029	0.004	0.004	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.829	-0.892	32.034	-0.042	-0.042	0.000	0.000	0.000	0.000
115	A	116	CYS	0	-0.015	0.004	33.992	0.004	0.004	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.875	0.924	35.744	0.029	0.029	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.011	-0.004	39.362	0.002	0.002	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.001	0.018	41.173	0.000	0.000	0.000	0.000	0.000	0.000

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