FMO DATABASE

FMODB ID: QYVJY

Calculation Name: 1U78-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U78

Chain ID: A

ChEMBL ID:

UniProt ID: P34257

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	OptH
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	103
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-636591.273484
FMO2-HF: Nuclear repulsion	595381.147811
FMO2-HF: Total energy	-41210.125673
FMO2-MP2: Total energy	-41329.514793

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:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-11.367	-5.812	1.613	-3.035	-4.134	-0.016

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.020

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	GLY	0	0.047	0.034	2.535	-0.881	1.722	0.179	-1.238	-1.545	0.003
4	A	5	SER	0	0.029	0.017	2.580	-5.526	-3.398	0.854	-1.481	-1.501	-0.019
5	A	6	ALA	0	-0.012	-0.002	4.871	0.120	0.120	0.000	0.000	0.000	0.000
6	A	7	LEU	0	0.017	-0.007	5.575	0.197	0.197	0.000	0.000	0.000	0.000
7	A	8	SER	0	0.038	0.034	8.777	0.159	0.159	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.791	-0.909	11.597	-0.354	-0.354	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.036	0.026	14.793	0.028	0.028	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.751	-0.845	10.580	-1.095	-1.095	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.775	0.875	10.381	0.539	0.539	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.095	0.050	14.454	0.050	0.050	0.000	0.000	0.000	0.000
13	A	14	GLN	0	-0.038	-0.024	17.212	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.003	-0.012	12.731	0.033	0.033	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.833	-0.867	17.105	-0.155	-0.155	0.000	0.000	0.000	0.000
16	A	17	VAL	0	0.023	0.008	19.370	0.025	0.025	0.000	0.000	0.000	0.000
17	A	18	MET	0	-0.016	-0.015	18.049	0.018	0.018	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.970	0.980	19.903	0.073	0.073	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.009	-0.001	21.731	0.016	0.016	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.035	0.000	24.563	0.009	0.009	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.051	-0.025	24.798	0.003	0.003	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.004	0.019	21.444	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.024	0.003	22.159	0.002	0.002	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.065	0.002	15.749	-0.015	-0.015	0.000	0.000	0.000	0.000
25	A	26	HIS	0	-0.016	-0.019	17.490	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.881	-0.943	18.683	-0.224	-0.224	0.000	0.000	0.000	0.000
27	A	28	MET	0	0.022	0.030	16.832	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.076	-0.040	13.941	-0.048	-0.048	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.944	0.956	15.395	0.155	0.155	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.917	0.964	18.031	0.205	0.205	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.032	0.020	12.815	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	SER	0	-0.024	0.008	13.692	-0.081	-0.081	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.760	0.860	6.508	1.578	1.578	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.029	0.004	7.746	0.149	0.149	0.000	0.000	0.000	0.000
35	A	36	ARG	1	1.032	0.996	10.720	0.150	0.150	0.000	0.000	0.000	0.000
36	A	37	HIS	0	-0.075	-0.036	6.771	-0.146	-0.146	0.000	0.000	0.000	0.000
37	A	38	CYS	0	0.012	0.016	6.933	0.126	0.126	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.082	0.051	8.565	0.075	0.075	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.891	0.948	12.155	0.023	0.023	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.017	-0.006	9.247	0.039	0.039	0.000	0.000	0.000	0.000
41	A	42	TYR	0	-0.048	-0.070	10.542	0.012	0.012	0.000	0.000	0.000	0.000
42	A	43	LEU	0	0.014	-0.014	11.892	0.025	0.025	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.819	0.908	14.927	-0.073	-0.073	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.868	-0.932	14.424	0.165	0.165	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.050	0.048	13.921	0.014	0.014	0.000	0.000	0.000	0.000
46	A	47	VAL	0	0.002	-0.001	14.000	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	48	SER	0	0.012	0.010	13.633	0.004	0.004	0.000	0.000	0.000	0.000
48	A	49	TYR	0	0.009	-0.006	5.892	-0.058	-0.058	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.067	-0.033	7.564	-0.065	-0.065	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.033	0.016	8.575	0.034	0.034	0.000	0.000	0.000	0.000
51	A	52	SER	0	-0.030	-0.002	9.161	0.032	0.032	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.935	0.967	9.069	-0.311	-0.311	0.000	0.000	0.000	0.000
53	A	54	ARG	1	1.015	1.013	2.728	-4.895	-4.071	0.580	-0.316	-1.088	0.000
54	A	55	ALA	0	-0.029	-0.020	9.472	-0.162	-0.162	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.011	0.016	11.568	0.120	0.120	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.974	0.988	12.899	-0.308	-0.308	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.995	0.990	14.757	-0.565	-0.565	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.848	0.905	18.548	-0.183	-0.183	0.000	0.000	0.000	0.000
59	A	60	ALA	0	-0.003	-0.010	21.006	0.012	0.012	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.028	0.020	23.474	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.012	0.013	25.570	0.011	0.011	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.094	0.027	27.046	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.932	0.975	29.120	-0.146	-0.146	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.796	-0.903	29.817	0.129	0.129	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.829	-0.915	26.266	0.136	0.136	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.972	0.986	30.688	-0.119	-0.119	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.028	-0.020	33.891	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	69	VAL	0	0.002	0.000	31.871	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	70	ILE	0	-0.008	-0.008	31.555	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.967	0.995	35.606	-0.081	-0.081	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.036	0.009	38.205	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	ALA	0	-0.030	-0.026	37.040	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.038	-0.023	39.038	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.076	-0.013	40.607	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.040	0.025	42.938	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	77	CYS	0	0.001	-0.006	42.265	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.982	1.010	41.005	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	79	THR	0	0.005	0.003	39.020	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.026	-0.001	33.684	0.003	0.003	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.909	0.944	35.378	-0.036	-0.036	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.806	-0.894	36.520	0.038	0.038	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.068	0.034	35.193	0.005	0.005	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.812	0.906	30.379	-0.074	-0.074	0.000	0.000	0.000	0.000
84	A	85	ASN	0	-0.008	-0.017	34.997	0.008	0.008	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.924	-0.949	37.937	0.056	0.056	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.053	-0.024	35.107	0.003	0.003	0.000	0.000	0.000	0.000
87	A	88	GLN	0	-0.007	-0.008	35.720	0.009	0.009	0.000	0.000	0.000	0.000
88	A	89	LEU	0	0.021	-0.003	31.123	0.006	0.006	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.061	-0.023	28.935	0.010	0.010	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.055	0.044	26.964	0.012	0.012	0.000	0.000	0.000	0.000
91	A	92	SER	0	0.013	-0.001	25.972	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	93	LYS	1	1.066	1.018	28.356	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.954	0.977	26.649	-0.014	-0.014	0.000	0.000	0.000	0.000
94	A	95	THR	0	0.006	0.001	24.987	0.002	0.002	0.000	0.000	0.000	0.000
95	A	96	ILE	0	0.062	0.043	26.885	0.002	0.002	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.021	0.001	30.263	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.057	-0.029	24.178	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	99	VAL	0	-0.051	-0.016	27.347	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.050	0.014	28.914	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.960	0.986	28.625	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.897	0.937	23.059	-0.101	-0.101	0.000	0.000	0.000	0.000
102	A	103	SER	0	-0.025	0.001	29.090	0.006	0.006	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.013	0.030	32.149	-0.003	-0.003	0.000	0.000	0.000	0.000

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