FMO DATABASE

FMODB ID: 9GKK2

Calculation Name: 1WTY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WTY

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SM95

Base Structure: X-ray

Registration Date: 2023-06-19

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1021076.939563
FMO2-HF: Nuclear repulsion	974311.464994
FMO2-HF: Total energy	-46765.474569
FMO2-MP2: Total energy	-46905.612287

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.
-2.047	0.734	1.502	-1.758	-2.524	0.002

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 : 0.039 / q_NPA : 0.023

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	LEU	0	0.088	0.034	3.800	-0.887	1.526	-0.019	-1.242	-1.151	0.006
4	A	5	ALA	0	0.084	0.044	6.021	0.604	0.604	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.860	0.920	5.629	0.451	0.451	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.052	-0.031	5.023	0.334	0.334	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.097	0.034	6.893	0.176	0.176	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.858	-0.905	9.963	-0.138	-0.138	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.908	0.952	6.571	-0.246	-0.246	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.030	0.027	11.164	0.057	0.057	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.856	0.908	13.017	0.225	0.225	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.026	-0.019	14.638	0.029	0.029	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.069	-0.039	15.696	0.022	0.022	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.020	0.006	16.925	0.010	0.010	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.840	-0.891	19.281	-0.149	-0.149	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.881	0.955	19.513	0.026	0.026	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.014	0.000	22.707	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.870	0.923	24.537	0.030	0.030	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.834	-0.912	24.791	0.030	0.030	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.888	-0.954	24.458	0.043	0.043	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.037	0.024	22.386	0.006	0.006	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.076	-0.035	20.395	0.007	0.007	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.698	0.800	19.685	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.733	-0.850	19.709	0.036	0.036	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.103	-0.048	16.068	0.012	0.012	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.001	-0.003	14.906	0.000	0.000	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.039	0.017	15.254	-0.025	-0.025	0.000	0.000	0.000	0.000
28	A	29	GLN	0	0.008	0.003	11.174	0.006	0.006	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.859	0.901	10.876	-0.017	-0.017	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.006	0.020	10.655	-0.072	-0.072	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.808	-0.872	12.081	0.052	0.052	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.067	-0.025	6.513	0.013	0.013	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.003	-0.014	7.163	-0.142	-0.142	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.059	0.031	8.465	-0.201	-0.201	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.853	-0.903	7.949	-0.090	-0.090	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.015	-0.016	2.377	-0.529	-0.161	1.521	-0.516	-1.373	-0.004
37	A	38	ALA	0	0.042	0.033	5.843	-0.406	-0.406	0.000	0.000	0.000	0.000
38	A	39	TRP	0	0.009	-0.011	8.857	-0.041	-0.041	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.825	0.919	6.176	0.099	0.099	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.012	-0.018	6.498	-0.323	-0.323	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.000	0.010	8.411	0.108	0.108	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.750	0.860	11.135	0.315	0.315	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.019	-0.015	8.333	0.072	0.072	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.055	0.030	10.789	0.074	0.074	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.010	-0.005	12.969	0.090	0.090	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.809	-0.887	13.366	-0.227	-0.227	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.066	-0.013	13.622	0.043	0.043	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.074	-0.044	15.897	0.066	0.066	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.018	0.011	18.590	0.036	0.036	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.057	-0.022	19.134	0.033	0.033	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.783	-0.861	18.350	-0.127	-0.127	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.014	-0.007	15.980	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.790	0.856	16.202	0.079	0.079	0.000	0.000	0.000	0.000
54	A	55	SER	0	0.016	0.002	16.601	0.024	0.024	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.083	0.046	13.963	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.820	0.896	15.528	0.090	0.090	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.016	-0.006	18.805	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.024	0.001	14.252	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.014	0.008	15.850	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.955	0.975	17.688	0.142	0.142	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.045	0.032	19.631	0.010	0.010	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.018	-0.006	16.592	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.033	-0.009	18.620	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.031	-0.009	21.984	0.006	0.006	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.039	-0.030	18.675	0.009	0.009	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.021	0.027	22.041	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.066	-0.027	14.169	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.005	-0.019	15.837	-0.047	-0.047	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.045	-0.003	19.618	0.027	0.027	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.885	-0.950	22.353	-0.196	-0.196	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.760	-0.861	21.661	-0.212	-0.212	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.007	-0.008	22.605	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.039	0.022	20.227	0.006	0.006	0.000	0.000	0.000	0.000
74	A	75	TRP	0	0.057	0.008	13.134	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.085	-0.049	18.921	0.005	0.005	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.843	-0.923	21.243	-0.111	-0.111	0.000	0.000	0.000	0.000
77	A	78	MET	0	-0.040	0.002	15.662	0.016	0.016	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.017	-0.012	16.249	0.009	0.009	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.849	-0.912	18.068	-0.069	-0.069	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.005	-0.006	19.236	0.021	0.021	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.801	0.895	11.934	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	83	ASN	0	-0.043	-0.032	17.037	0.034	0.034	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.010	-0.001	19.427	0.018	0.018	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.016	-0.012	16.726	0.004	0.004	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.064	-0.025	19.554	0.023	0.023	0.000	0.000	0.000	0.000
86	A	87	HIS	0	0.009	0.004	20.586	0.015	0.015	0.000	0.000	0.000	0.000
87	A	88	THR	0	0.005	-0.008	20.896	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.042	-0.007	23.772	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.877	-0.936	26.377	0.009	0.009	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.776	-0.903	26.914	0.024	0.024	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.017	0.005	27.657	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.030	-0.016	24.532	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.025	0.010	23.320	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.807	-0.892	23.628	-0.019	-0.019	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.902	0.961	25.743	0.042	0.042	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.020	-0.015	19.598	-0.013	-0.013	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.054	0.018	20.707	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.029	-0.014	22.014	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.827	-0.901	22.087	-0.118	-0.118	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.040	-0.016	16.975	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.004	0.006	18.562	-0.030	-0.030	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.899	0.946	20.100	0.115	0.115	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.009	-0.006	16.448	-0.027	-0.027	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.046	-0.028	14.804	-0.054	-0.054	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.858	-0.924	16.178	-0.253	-0.253	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.774	0.864	16.994	0.195	0.195	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.034	-0.019	12.076	-0.057	-0.057	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.001	-0.018	13.685	-0.072	-0.072	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.761	-0.854	15.475	-0.398	-0.398	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.038	-0.018	11.331	-0.021	-0.021	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.045	-0.039	9.650	-0.090	-0.090	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.841	0.911	13.377	0.371	0.371	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.825	0.916	16.544	0.374	0.374	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.074	-0.046	10.196	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-1.034	-0.991	13.733	-0.810	-0.810	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.892	-0.935	15.330	-0.315	-0.315	0.000	0.000	0.000	0.000

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