FMO DATABASE

FMODB ID: ZV94N

Calculation Name: 5J45-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5J45

Chain ID: A

ChEMBL ID:

UniProt ID: Q8T0Q4

Base Structure: X-ray

Registration Date: 2023-09-23

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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-689606.738335
FMO2-HF: Nuclear repulsion	643916.668627
FMO2-HF: Total energy	-45690.069708
FMO2-MP2: Total energy	-45820.303513

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:18:THR)

Summations of interaction energy for fragment #1(A:18:THR)

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.
-42.829	-42.585	23.732	-13.71	-10.266	-0.06

Interaction energy analysis for fragmet #1(A:18:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / 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	20	GLU	-1	-0.872	-0.910	1.625	-43.689	-44.391	23.718	-13.409	-9.607	-0.061
4	A	21	ALA	0	-0.007	-0.003	3.270	-0.646	0.163	0.015	-0.288	-0.535	0.001
5	A	22	ILE	0	0.020	0.011	4.789	0.405	0.542	-0.001	-0.013	-0.124	0.000
6	A	23	GLN	0	0.019	0.007	7.395	0.252	0.252	0.000	0.000	0.000	0.000
7	A	24	LYS	1	0.927	0.977	7.460	1.053	1.053	0.000	0.000	0.000	0.000
8	A	25	LEU	0	0.000	0.033	8.294	0.125	0.125	0.000	0.000	0.000	0.000
9	A	26	ARG	1	0.969	0.970	10.869	0.219	0.219	0.000	0.000	0.000	0.000
10	A	27	GLU	-1	-0.912	-0.951	11.960	-0.882	-0.882	0.000	0.000	0.000	0.000
11	A	28	THR	0	-0.061	-0.050	12.218	0.084	0.084	0.000	0.000	0.000	0.000
12	A	29	GLU	-1	-0.835	-0.919	14.769	-0.157	-0.157	0.000	0.000	0.000	0.000
13	A	30	ASN	0	0.010	0.004	16.753	0.057	0.057	0.000	0.000	0.000	0.000
14	A	31	MET	0	-0.036	-0.014	18.053	0.047	0.047	0.000	0.000	0.000	0.000
15	A	32	LEU	0	-0.001	-0.008	19.082	0.026	0.026	0.000	0.000	0.000	0.000
16	A	33	ILE	0	0.088	0.044	20.577	0.021	0.021	0.000	0.000	0.000	0.000
17	A	34	LYS	1	0.800	0.893	22.661	0.156	0.156	0.000	0.000	0.000	0.000
18	A	35	LYS	1	0.872	0.932	22.910	0.200	0.200	0.000	0.000	0.000	0.000
19	A	36	GLN	0	0.011	-0.004	25.096	0.005	0.005	0.000	0.000	0.000	0.000
20	A	37	GLU	-1	-0.747	-0.858	26.904	-0.111	-0.111	0.000	0.000	0.000	0.000
21	A	38	PHE	0	-0.072	-0.027	28.456	0.009	0.009	0.000	0.000	0.000	0.000
22	A	39	LEU	0	-0.028	-0.018	28.646	0.008	0.008	0.000	0.000	0.000	0.000
23	A	40	GLU	-1	-0.902	-0.953	30.568	-0.070	-0.070	0.000	0.000	0.000	0.000
24	A	41	ALA	0	0.005	0.007	32.973	0.007	0.007	0.000	0.000	0.000	0.000
25	A	42	LYS	1	0.862	0.909	34.310	0.085	0.085	0.000	0.000	0.000	0.000
26	A	43	ILE	0	-0.021	-0.007	33.811	0.006	0.006	0.000	0.000	0.000	0.000
27	A	44	GLU	-1	-0.701	-0.835	37.332	-0.040	-0.040	0.000	0.000	0.000	0.000
28	A	45	ASP	-1	-0.841	-0.883	38.100	-0.065	-0.065	0.000	0.000	0.000	0.000
29	A	46	GLU	-1	-0.801	-0.903	39.525	-0.054	-0.054	0.000	0.000	0.000	0.000
30	A	47	LEU	0	-0.015	-0.001	41.541	0.004	0.004	0.000	0.000	0.000	0.000
31	A	48	ASN	0	-0.016	-0.011	42.521	0.006	0.006	0.000	0.000	0.000	0.000
32	A	49	ILE	0	-0.034	-0.012	43.092	0.003	0.003	0.000	0.000	0.000	0.000
33	A	50	ALA	0	-0.011	-0.008	45.838	0.002	0.002	0.000	0.000	0.000	0.000
34	A	51	ARG	1	0.813	0.859	43.722	0.043	0.043	0.000	0.000	0.000	0.000
35	A	52	LYS	1	0.955	0.991	47.020	0.045	0.045	0.000	0.000	0.000	0.000
36	A	53	ASN	0	-0.071	-0.053	49.740	0.002	0.002	0.000	0.000	0.000	0.000
37	A	54	ALA	0	0.019	0.028	51.362	0.001	0.001	0.000	0.000	0.000	0.000
38	A	55	SER	0	0.020	0.018	52.981	0.001	0.001	0.000	0.000	0.000	0.000
39	A	56	LYS	1	0.985	0.988	53.715	0.035	0.035	0.000	0.000	0.000	0.000
40	A	57	ASN	0	-0.012	-0.016	53.808	0.000	0.000	0.000	0.000	0.000	0.000
41	A	58	LYS	1	0.984	0.979	53.089	0.025	0.025	0.000	0.000	0.000	0.000
42	A	59	ARG	1	0.966	0.987	50.139	0.037	0.037	0.000	0.000	0.000	0.000
43	A	60	VAL	0	-0.007	-0.005	48.789	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	61	ALA	0	0.036	0.018	48.171	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	62	LEU	0	0.013	0.003	47.451	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	63	GLN	0	-0.035	-0.012	45.759	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	64	ALA	0	-0.003	0.010	43.698	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	65	LEU	0	0.052	0.014	42.539	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	66	LYS	1	0.922	0.973	42.356	0.038	0.038	0.000	0.000	0.000	0.000
50	A	67	LYS	1	0.794	0.883	39.489	0.055	0.055	0.000	0.000	0.000	0.000
51	A	68	LYS	1	0.838	0.911	38.123	0.043	0.043	0.000	0.000	0.000	0.000
52	A	69	LYS	1	1.018	1.012	37.443	0.036	0.036	0.000	0.000	0.000	0.000
53	A	70	ARG	1	0.890	0.945	36.117	0.060	0.060	0.000	0.000	0.000	0.000
54	A	71	LEU	0	0.041	0.027	33.535	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	72	GLU	-1	-0.747	-0.867	32.607	-0.052	-0.052	0.000	0.000	0.000	0.000
56	A	73	LYS	1	0.855	0.945	30.814	0.063	0.063	0.000	0.000	0.000	0.000
57	A	74	GLN	0	-0.029	-0.032	29.591	0.001	0.001	0.000	0.000	0.000	0.000
58	A	75	LEU	0	0.022	0.021	28.234	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	76	GLN	0	0.053	0.027	27.804	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	77	GLN	0	-0.008	0.000	26.315	0.008	0.008	0.000	0.000	0.000	0.000
61	A	78	ILE	0	-0.011	0.012	23.741	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	79	ASP	-1	-0.783	-0.892	23.127	-0.095	-0.095	0.000	0.000	0.000	0.000
63	A	80	GLY	0	-0.006	0.011	23.529	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	81	THR	0	-0.051	-0.034	19.043	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	82	LEU	0	-0.019	-0.014	18.791	-0.024	-0.024	0.000	0.000	0.000	0.000
66	A	83	SER	0	0.044	0.016	18.705	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	84	THR	0	-0.057	-0.034	16.903	0.011	0.011	0.000	0.000	0.000	0.000
68	A	85	ILE	0	-0.051	-0.033	13.615	-0.017	-0.017	0.000	0.000	0.000	0.000
69	A	86	GLU	-1	-0.886	-0.949	14.322	-0.129	-0.129	0.000	0.000	0.000	0.000
70	A	87	MET	0	0.031	0.017	15.586	0.011	0.011	0.000	0.000	0.000	0.000
71	A	88	GLN	0	-0.036	-0.018	12.160	0.014	0.014	0.000	0.000	0.000	0.000
72	A	89	ARG	1	0.695	0.813	11.129	0.048	0.048	0.000	0.000	0.000	0.000
73	A	90	GLU	-1	-0.789	-0.888	11.992	0.007	0.007	0.000	0.000	0.000	0.000
74	A	91	ALA	0	-0.016	0.011	13.020	0.065	0.065	0.000	0.000	0.000	0.000
75	A	92	LEU	0	-0.003	-0.014	6.334	0.044	0.044	0.000	0.000	0.000	0.000
76	A	93	GLU	-1	-0.817	-0.891	9.461	0.228	0.228	0.000	0.000	0.000	0.000
77	A	94	SER	0	-0.012	-0.010	11.517	0.108	0.108	0.000	0.000	0.000	0.000
78	A	95	ALA	0	-0.002	0.008	9.340	0.055	0.055	0.000	0.000	0.000	0.000
79	A	96	ASN	0	-0.051	-0.017	6.238	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	97	THR	0	0.021	0.000	9.061	0.068	0.068	0.000	0.000	0.000	0.000
81	A	98	ASN	0	-0.025	-0.031	12.430	-0.019	-0.019	0.000	0.000	0.000	0.000
82	A	99	THR	0	-0.022	-0.007	8.006	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	100	ALA	0	0.019	0.026	11.100	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	101	VAL	0	0.012	0.024	12.585	-0.064	-0.064	0.000	0.000	0.000	0.000
85	A	102	LEU	0	0.021	0.005	14.436	-0.037	-0.037	0.000	0.000	0.000	0.000
86	A	103	THR	0	-0.046	-0.035	12.107	-0.041	-0.041	0.000	0.000	0.000	0.000
87	A	104	THR	0	-0.026	-0.030	15.250	-0.056	-0.056	0.000	0.000	0.000	0.000
88	A	105	MET	0	0.016	0.015	17.714	-0.040	-0.040	0.000	0.000	0.000	0.000
89	A	106	LYS	1	0.944	0.978	18.098	-0.308	-0.308	0.000	0.000	0.000	0.000
90	A	107	ASN	0	-0.042	-0.017	18.890	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	108	ALA	0	0.045	0.023	20.735	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	109	ALA	0	0.011	0.007	23.238	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	110	ASP	-1	-0.871	-0.946	22.037	0.203	0.203	0.000	0.000	0.000	0.000
94	A	111	ALA	0	-0.016	-0.004	24.884	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	112	LEU	0	-0.005	0.003	26.738	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	113	LYS	1	0.881	0.930	25.466	-0.181	-0.181	0.000	0.000	0.000	0.000
97	A	114	ARG	1	0.951	0.970	28.790	-0.131	-0.131	0.000	0.000	0.000	0.000
98	A	115	ALA	0	-0.005	0.009	30.648	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	116	HIS	0	-0.014	-0.034	32.616	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	117	GLN	0	0.019	-0.001	30.973	0.001	0.001	0.000	0.000	0.000	0.000
101	A	118	ASN	0	-0.035	-0.014	34.469	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	119	MET	0	0.035	0.037	36.628	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	120	ASP	-1	-0.891	-0.935	37.806	0.080	0.080	0.000	0.000	0.000	0.000
104	A	121	VAL	0	-0.042	-0.026	37.742	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	122	ASP	-1	-0.916	-0.958	40.419	0.070	0.070	0.000	0.000	0.000	0.000
106	A	123	LYS	1	0.731	0.851	42.668	-0.063	-0.063	0.000	0.000	0.000	0.000
107	A	124	VAL	0	0.017	-0.010	42.619	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	125	HIS	0	-0.016	-0.001	44.463	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	126	ASP	-1	-0.790	-0.893	46.156	0.052	0.052	0.000	0.000	0.000	0.000
110	A	127	MET	0	-0.098	-0.043	47.945	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	128	MET	0	-0.053	-0.008	47.596	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	129	ASP	-1	-1.049	-1.011	51.119	0.039	0.039	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:THR)