FMO DATABASE

FMODB ID: G6171

Calculation Name: 5A15-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5A15

Chain ID: A

ChEMBL ID:

UniProt ID: Q68DU8

Base Structure: X-ray

Registration Date: 2023-09-20

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	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-749121.724805
FMO2-HF: Nuclear repulsion	710594.623575
FMO2-HF: Total energy	-38527.10123
FMO2-MP2: Total energy	-38642.692409

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:23:PHE)

Summations of interaction energy for fragment #1(A:23:PHE)

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.
-20.16	-8.43	10.51	-5.621	-16.62	-0.009

Interaction energy analysis for fragmet #1(A:23:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / q_NPA : -0.024

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	25	GLU	-1	-0.874	-0.940	3.288	-3.493	-1.310	0.040	-1.069	-1.154	0.000
4	A	26	VAL	0	-0.047	-0.031	6.030	0.325	0.325	0.000	0.000	0.000	0.000
5	A	27	VAL	0	-0.017	-0.009	3.525	-0.228	0.162	0.009	-0.065	-0.335	0.000
6	A	28	GLU	-1	-0.893	-0.949	6.232	0.436	0.436	0.000	0.000	0.000	0.000
7	A	29	LEU	0	-0.030	-0.025	6.215	0.177	0.177	0.000	0.000	0.000	0.000
8	A	30	ASN	0	-0.033	-0.018	9.319	-0.132	-0.132	0.000	0.000	0.000	0.000
9	A	31	VAL	0	0.028	0.004	11.736	0.011	0.011	0.000	0.000	0.000	0.000
10	A	32	GLY	0	0.039	0.035	13.754	-0.028	-0.028	0.000	0.000	0.000	0.000
11	A	33	GLY	0	-0.021	-0.010	15.620	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	34	GLN	0	-0.041	-0.016	16.586	0.001	0.001	0.000	0.000	0.000	0.000
13	A	35	VAL	0	-0.027	-0.011	12.929	0.026	0.026	0.000	0.000	0.000	0.000
14	A	36	TYR	0	-0.059	-0.044	12.549	-0.061	-0.061	0.000	0.000	0.000	0.000
15	A	37	PHE	0	0.028	0.023	10.840	0.077	0.077	0.000	0.000	0.000	0.000
16	A	38	THR	0	-0.019	-0.022	8.529	-0.093	-0.093	0.000	0.000	0.000	0.000
17	A	39	ARG	1	0.978	1.004	7.995	0.312	0.312	0.000	0.000	0.000	0.000
18	A	40	HIS	0	0.038	0.003	2.688	-2.353	-0.381	0.789	-0.791	-1.970	0.001
19	A	41	SER	0	0.012	-0.007	5.629	0.147	0.147	0.000	0.000	0.000	0.000
20	A	42	THR	0	-0.020	-0.014	8.819	0.049	0.049	0.000	0.000	0.000	0.000
21	A	43	LEU	0	-0.008	0.002	5.404	0.013	0.013	0.000	0.000	0.000	0.000
22	A	44	ILE	0	-0.014	-0.001	6.015	0.019	0.019	0.000	0.000	0.000	0.000
23	A	45	SER	0	-0.020	0.004	9.186	-0.090	-0.090	0.000	0.000	0.000	0.000
24	A	46	ILE	0	-0.008	-0.002	12.795	0.005	0.005	0.000	0.000	0.000	0.000
25	A	47	PRO	0	0.043	0.031	12.065	0.004	0.004	0.000	0.000	0.000	0.000
26	A	48	HIS	0	0.015	0.006	12.184	0.055	0.055	0.000	0.000	0.000	0.000
27	A	49	SER	0	0.003	-0.007	12.452	0.070	0.070	0.000	0.000	0.000	0.000
28	A	50	LEU	0	-0.021	-0.005	10.735	-0.083	-0.083	0.000	0.000	0.000	0.000
29	A	51	LEU	0	0.048	0.004	8.570	-0.051	-0.051	0.000	0.000	0.000	0.000
30	A	52	TRP	0	0.026	0.033	7.402	0.117	0.117	0.000	0.000	0.000	0.000
31	A	53	LYS	1	0.811	0.895	6.762	0.099	0.099	0.000	0.000	0.000	0.000
32	A	54	MET	0	-0.066	-0.011	5.075	-0.294	-0.294	0.000	0.000	0.000	0.000
33	A	55	PHE	0	0.015	0.001	2.703	-6.302	-2.982	4.482	-2.305	-5.497	0.012
34	A	56	SER	0	-0.012	0.007	3.009	-1.856	-1.381	1.324	0.358	-2.158	-0.007
35	A	57	PRO	0	-0.020	-0.003	3.058	-2.853	-1.036	0.143	-0.575	-1.385	-0.006
36	A	65	LEU	0	-0.004	-0.014	2.098	-0.213	-0.457	2.453	-0.550	-1.659	-0.002
37	A	66	ALA	0	0.020	0.024	6.510	0.187	0.187	0.000	0.000	0.000	0.000
38	A	67	LYS	1	0.948	0.975	6.141	-1.538	-1.538	0.000	0.000	0.000	0.000
39	A	68	ASP	-1	-0.725	-0.844	9.239	0.475	0.475	0.000	0.000	0.000	0.000
40	A	69	SER	0	-0.007	-0.009	12.499	0.068	0.068	0.000	0.000	0.000	0.000
41	A	70	LYS	1	0.922	0.958	13.917	-0.345	-0.345	0.000	0.000	0.000	0.000
42	A	71	GLY	0	-0.002	0.010	10.502	0.048	0.048	0.000	0.000	0.000	0.000
43	A	72	ARG	1	0.840	0.913	8.263	-0.235	-0.235	0.000	0.000	0.000	0.000
44	A	73	PHE	0	0.018	0.005	2.883	-2.519	-0.702	1.270	-0.624	-2.462	-0.007
45	A	74	PHE	0	-0.007	-0.016	6.560	-0.050	-0.050	0.000	0.000	0.000	0.000
46	A	75	ILE	0	-0.052	-0.027	7.994	-0.048	-0.048	0.000	0.000	0.000	0.000
47	A	76	ASP	-1	-0.921	-0.957	11.156	0.125	0.125	0.000	0.000	0.000	0.000
48	A	77	ARG	1	0.815	0.886	14.635	-0.071	-0.071	0.000	0.000	0.000	0.000
49	A	78	ASP	-1	-0.815	-0.920	16.665	0.087	0.087	0.000	0.000	0.000	0.000
50	A	79	GLY	0	0.048	0.019	16.909	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	80	PHE	0	0.010	0.013	17.948	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	81	LEU	0	-0.005	-0.012	20.424	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	82	PHE	0	0.006	0.007	11.308	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	83	ARG	1	0.975	1.005	16.828	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	84	TYR	0	0.042	0.012	18.729	-0.017	-0.017	0.000	0.000	0.000	0.000
56	A	85	ILE	0	-0.032	-0.003	15.482	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	86	LEU	0	-0.052	-0.031	11.928	-0.027	-0.027	0.000	0.000	0.000	0.000
58	A	87	ASP	-1	-0.875	-0.960	15.640	-0.073	-0.073	0.000	0.000	0.000	0.000
59	A	88	TYR	0	-0.007	0.003	18.244	-0.025	-0.025	0.000	0.000	0.000	0.000
60	A	89	LEU	0	-0.046	-0.012	12.644	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	90	ARG	1	0.857	0.934	13.689	0.045	0.045	0.000	0.000	0.000	0.000
62	A	91	ASP	-1	-0.871	-0.926	15.857	-0.172	-0.172	0.000	0.000	0.000	0.000
63	A	92	ARG	1	0.846	0.921	17.488	0.277	0.277	0.000	0.000	0.000	0.000
64	A	93	GLN	0	-0.033	-0.018	20.545	0.017	0.017	0.000	0.000	0.000	0.000
65	A	94	VAL	0	-0.011	-0.009	21.829	0.003	0.003	0.000	0.000	0.000	0.000
66	A	95	VAL	0	0.034	0.025	24.283	0.002	0.002	0.000	0.000	0.000	0.000
67	A	96	LEU	0	-0.057	-0.032	26.041	0.006	0.006	0.000	0.000	0.000	0.000
68	A	97	PRO	0	0.012	0.001	27.696	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	98	ASP	-1	-0.882	-0.937	30.903	-0.028	-0.028	0.000	0.000	0.000	0.000
70	A	99	HIS	0	-0.036	-0.020	34.611	0.004	0.004	0.000	0.000	0.000	0.000
71	A	100	PHE	0	-0.009	-0.003	25.748	0.003	0.003	0.000	0.000	0.000	0.000
72	A	101	PRO	0	0.027	0.015	30.589	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	102	GLU	-1	-0.903	-0.956	26.474	0.023	0.023	0.000	0.000	0.000	0.000
74	A	103	LYS	1	1.014	0.997	27.169	0.038	0.038	0.000	0.000	0.000	0.000
75	A	104	GLY	0	-0.022	-0.004	27.498	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	105	ARG	1	0.962	0.979	24.250	-0.031	-0.031	0.000	0.000	0.000	0.000
77	A	106	LEU	0	0.055	0.033	21.667	0.001	0.001	0.000	0.000	0.000	0.000
78	A	107	LYS	1	0.941	0.966	22.680	0.046	0.046	0.000	0.000	0.000	0.000
79	A	108	ARG	1	0.955	0.983	21.041	0.030	0.030	0.000	0.000	0.000	0.000
80	A	109	GLU	-1	-0.815	-0.914	18.733	0.023	0.023	0.000	0.000	0.000	0.000
81	A	110	ALA	0	0.004	0.001	18.465	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	111	GLU	-1	-0.924	-0.966	19.066	-0.080	-0.080	0.000	0.000	0.000	0.000
83	A	112	TYR	0	-0.065	-0.015	13.209	-0.025	-0.025	0.000	0.000	0.000	0.000
84	A	113	PHE	0	0.032	-0.013	12.147	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	114	GLN	0	0.011	0.018	14.813	-0.079	-0.079	0.000	0.000	0.000	0.000
86	A	115	LEU	0	0.004	0.002	15.442	-0.032	-0.032	0.000	0.000	0.000	0.000
87	A	116	PRO	0	0.062	0.017	18.941	0.019	0.019	0.000	0.000	0.000	0.000
88	A	117	ASP	-1	-0.852	-0.924	21.857	-0.168	-0.168	0.000	0.000	0.000	0.000
89	A	118	LEU	0	0.001	0.013	20.152	0.011	0.011	0.000	0.000	0.000	0.000
90	A	119	VAL	0	0.027	0.000	22.418	0.014	0.014	0.000	0.000	0.000	0.000
91	A	120	LYS	1	0.873	0.938	24.883	0.150	0.150	0.000	0.000	0.000	0.000
92	A	121	LEU	0	-0.010	-0.006	24.900	0.007	0.007	0.000	0.000	0.000	0.000
93	A	122	LEU	0	-0.032	0.003	24.438	0.009	0.009	0.000	0.000	0.000	0.000
94	A	123	THR	0	-0.090	-0.049	28.526	0.008	0.008	0.000	0.000	0.000	0.000
95	A	124	PRO	0	-0.010	0.009	31.051	-0.001	-0.001	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:23:PHE)