FMO DATABASE

FMODB ID: LJ999

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1020606.81079
FMO2-HF: Nuclear repulsion	973842.180746
FMO2-HF: Total energy	-46764.630044
FMO2-MP2: Total energy	-46904.79586

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.
0.602	0.925	3.667	-1.495	-2.495	-0.005

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 : 0.019 / q_NPA : -0.004

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	0.093	0.041	3.800	-0.392	1.122	-0.013	-0.682	-0.819	0.001
4	A	5	ALA	0	0.088	0.044	5.671	0.538	0.538	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.873	0.930	5.538	0.276	0.276	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.037	-0.026	4.897	0.284	0.284	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.094	0.035	6.750	0.189	0.189	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.880	-0.922	9.812	0.017	0.017	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.890	0.945	7.139	0.092	0.092	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.028	0.032	11.053	0.056	0.056	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.976	0.985	12.903	0.211	0.211	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.019	-0.017	14.566	0.031	0.031	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.058	-0.031	15.651	0.023	0.023	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.012	0.001	17.099	0.010	0.010	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.961	-0.966	19.166	-0.100	-0.100	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.880	0.951	19.726	0.043	0.043	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.007	-0.002	22.676	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.874	0.908	24.513	0.083	0.083	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.857	-0.907	24.746	-0.030	-0.030	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.863	-0.947	24.467	-0.037	-0.037	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.028	0.021	22.464	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.063	-0.036	20.357	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.764	0.858	19.678	0.055	0.055	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.760	-0.868	19.673	-0.095	-0.095	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.087	-0.042	16.062	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.001	-0.004	14.908	-0.023	-0.023	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.024	0.013	15.165	-0.043	-0.043	0.000	0.000	0.000	0.000
28	A	29	GLN	0	0.009	0.007	11.487	-0.018	-0.018	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.850	0.885	10.842	0.062	0.062	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.006	0.013	10.528	-0.104	-0.104	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.890	-0.948	11.890	-0.282	-0.282	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.058	-0.023	6.382	-0.037	-0.037	0.000	0.000	0.000	0.000
33	A	34	THR	0	0.013	0.005	6.977	-0.258	-0.258	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.037	0.023	8.231	-0.182	-0.182	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.916	-0.959	7.627	-0.721	-0.721	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.025	-0.026	2.046	0.360	-0.831	3.680	-0.813	-1.676	-0.006
37	A	38	ALA	0	0.032	0.031	6.019	-0.303	-0.303	0.000	0.000	0.000	0.000
38	A	39	TRP	0	0.006	0.007	9.072	0.029	0.029	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.879	0.949	5.979	1.019	1.019	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.008	-0.023	6.636	-0.248	-0.248	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.004	0.006	8.505	0.186	0.186	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.781	0.880	11.214	0.619	0.619	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.007	-0.002	8.458	0.082	0.082	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.042	0.021	10.850	0.113	0.113	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.001	-0.015	12.916	0.097	0.097	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.842	-0.905	13.393	-0.416	-0.416	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.069	-0.015	13.218	0.057	0.057	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.073	-0.038	15.817	0.075	0.075	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.018	0.012	18.568	0.033	0.033	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.057	-0.022	19.160	0.022	0.022	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.865	-0.936	18.513	-0.226	-0.226	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.014	-0.009	16.111	0.002	0.002	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.875	0.937	16.201	0.175	0.175	0.000	0.000	0.000	0.000
54	A	55	SER	0	0.022	0.005	16.614	0.007	0.007	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.097	0.050	13.870	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.958	0.977	15.602	0.234	0.234	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.022	-0.013	18.797	0.010	0.010	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.032	0.006	14.364	0.008	0.008	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.012	0.011	16.273	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.939	0.970	17.831	0.240	0.240	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.054	0.040	19.744	0.021	0.021	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.023	-0.002	16.730	0.011	0.011	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.033	-0.009	18.726	0.010	0.010	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.012	-0.001	22.150	0.004	0.004	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.052	-0.034	18.647	0.016	0.016	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.032	0.030	22.000	0.009	0.009	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.048	-0.014	14.354	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.018	-0.032	15.990	-0.044	-0.044	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.027	0.001	19.831	0.027	0.027	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.885	-0.948	22.577	-0.231	-0.231	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.805	-0.881	22.119	-0.235	-0.235	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.011	-0.011	22.830	-0.021	-0.021	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.050	0.021	19.667	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	75	TRP	0	0.058	0.010	13.500	-0.032	-0.032	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.086	-0.050	19.123	-0.016	-0.016	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.841	-0.913	21.420	-0.185	-0.185	0.000	0.000	0.000	0.000
77	A	78	MET	0	-0.042	-0.002	15.506	0.007	0.007	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.035	-0.020	16.717	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.983	-0.998	18.232	-0.180	-0.180	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.011	-0.002	19.123	0.014	0.014	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.915	0.968	11.702	0.355	0.355	0.000	0.000	0.000	0.000
82	A	83	ASN	0	-0.038	-0.028	17.083	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.014	0.003	19.536	0.020	0.020	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.016	0.005	16.590	0.020	0.020	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.045	-0.027	19.465	0.003	0.003	0.000	0.000	0.000	0.000
86	A	87	HIS	0	-0.005	-0.006	20.544	0.022	0.022	0.000	0.000	0.000	0.000
87	A	88	THR	0	0.006	-0.007	20.888	0.009	0.009	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.042	0.003	23.738	0.007	0.007	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.882	-0.934	26.387	-0.072	-0.072	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.821	-0.948	26.880	-0.061	-0.061	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.021	0.007	27.592	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.042	-0.021	24.300	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.026	0.009	23.234	-0.014	-0.014	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.812	-0.885	23.530	-0.090	-0.090	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.923	0.969	25.682	0.134	0.134	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.017	-0.010	19.398	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.032	0.008	20.719	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.023	-0.011	21.878	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.901	-0.948	21.619	-0.167	-0.167	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.038	-0.021	16.685	-0.027	-0.027	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.000	0.008	18.325	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.982	1.003	19.835	0.173	0.173	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.016	-0.006	16.144	-0.022	-0.022	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.040	-0.032	14.199	-0.053	-0.053	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.914	-0.946	15.873	-0.248	-0.248	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.825	0.902	16.825	0.245	0.245	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.031	-0.015	11.800	-0.056	-0.056	0.000	0.000	0.000	0.000
108	A	109	GLN	0	0.008	-0.017	13.395	-0.051	-0.051	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.804	-0.880	15.142	-0.304	-0.304	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.037	-0.018	11.465	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.053	-0.043	9.411	-0.059	-0.059	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.913	0.953	13.212	0.299	0.299	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.865	0.938	16.407	0.334	0.334	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.063	-0.040	9.990	-0.019	-0.019	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-1.037	-0.991	13.549	-0.423	-0.423	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.997	-0.989	14.961	-0.202	-0.202	0.000	0.000	0.000	0.000

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