FMO DATABASE

FMODB ID: M3JJZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1024176.112565
FMO2-HF: Nuclear repulsion	977410.444956
FMO2-HF: Total energy	-46765.667609
FMO2-MP2: Total energy	-46905.786987

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.
-1.36	1.149	1.777	-1.681	-2.604	0.001

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 : 0.060 / q_NPA : 0.032

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	0.086	0.034	3.878	-0.502	1.511	-0.010	-1.023	-0.979	0.005
4	A	5	ALA	0	0.063	0.037	5.910	0.641	0.641	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.862	0.914	5.601	0.492	0.492	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.049	-0.024	5.158	0.341	0.341	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.102	0.039	6.975	0.203	0.203	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.858	-0.903	10.100	-0.172	-0.172	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.907	0.954	6.517	-0.067	-0.067	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.023	0.026	11.190	0.068	0.068	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.868	0.915	13.111	0.276	0.276	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.013	-0.011	14.581	0.035	0.035	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.068	-0.036	16.168	0.035	0.035	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.036	0.007	17.164	0.012	0.012	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.858	-0.902	19.019	-0.182	-0.182	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.870	0.945	19.237	0.066	0.066	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.004	-0.010	23.073	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.859	0.927	24.892	0.054	0.054	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.811	-0.900	24.626	0.003	0.003	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.876	-0.947	24.603	0.013	0.013	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.034	0.019	22.102	0.003	0.003	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.073	-0.028	20.294	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.693	0.800	19.796	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.751	-0.857	19.838	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.098	-0.062	16.207	0.003	0.003	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.007	-0.002	15.175	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.036	0.019	15.438	-0.033	-0.033	0.000	0.000	0.000	0.000
28	A	29	GLN	0	0.011	0.001	11.290	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.873	0.907	11.028	0.038	0.038	0.000	0.000	0.000	0.000
30	A	31	PHE	0	0.001	0.022	10.747	-0.090	-0.090	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.798	-0.858	11.866	-0.024	-0.024	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.071	-0.022	6.914	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.019	-0.022	6.831	-0.206	-0.206	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.069	0.027	8.416	-0.218	-0.218	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.830	-0.888	7.903	-0.143	-0.143	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.018	-0.006	2.483	-0.562	-0.066	1.787	-0.658	-1.625	-0.004
37	A	38	ALA	0	0.042	0.035	5.643	-0.361	-0.361	0.000	0.000	0.000	0.000
38	A	39	TRP	0	-0.014	-0.021	8.625	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.838	0.914	6.610	0.209	0.209	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.014	-0.001	6.329	-0.297	-0.297	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.002	0.005	7.877	0.162	0.162	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.782	0.873	10.873	0.269	0.269	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.031	-0.028	7.915	0.112	0.112	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.044	0.020	10.411	0.075	0.075	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.002	0.001	12.496	0.094	0.094	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.823	-0.889	13.225	-0.166	-0.166	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.053	-0.015	12.925	0.045	0.045	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.069	-0.037	15.368	0.059	0.059	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.020	0.003	18.172	0.032	0.032	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.049	-0.017	18.762	0.029	0.029	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.787	-0.869	17.804	-0.100	-0.100	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.003	-0.004	15.167	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.794	0.853	15.424	0.064	0.064	0.000	0.000	0.000	0.000
54	A	55	SER	0	0.002	0.003	16.432	0.024	0.024	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.086	0.034	13.975	-0.032	-0.032	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.816	0.893	15.530	0.110	0.110	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.021	-0.004	18.554	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.028	0.007	14.001	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.008	0.010	15.937	-0.031	-0.031	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.951	0.977	17.681	0.155	0.155	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.053	0.028	18.982	0.010	0.010	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.015	-0.008	16.097	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.021	-0.004	17.993	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.047	-0.015	21.587	0.008	0.008	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.030	-0.018	18.163	0.015	0.015	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.011	0.019	21.140	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.030	-0.003	13.507	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.025	-0.021	15.579	-0.046	-0.046	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.027	-0.010	19.146	0.030	0.030	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.897	-0.959	22.051	-0.211	-0.211	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.742	-0.853	21.269	-0.241	-0.241	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.014	0.003	22.445	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	74	PHE	0	0.044	0.018	19.674	0.001	0.001	0.000	0.000	0.000	0.000
74	A	75	TRP	0	0.059	0.008	12.644	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.089	-0.046	18.550	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.872	-0.945	21.031	-0.137	-0.137	0.000	0.000	0.000	0.000
77	A	78	MET	0	-0.043	-0.002	15.232	0.017	0.017	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.004	0.004	16.112	0.005	0.005	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.837	-0.897	17.827	-0.085	-0.085	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.001	-0.002	19.098	0.021	0.021	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.774	0.871	12.182	0.047	0.047	0.000	0.000	0.000	0.000
82	A	83	ASN	0	-0.049	-0.029	16.777	0.030	0.030	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.018	-0.007	19.170	0.021	0.021	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.006	-0.021	16.682	0.004	0.004	0.000	0.000	0.000	0.000
85	A	86	ASN	0	-0.065	-0.028	19.449	0.021	0.021	0.000	0.000	0.000	0.000
86	A	87	HIS	0	0.028	0.021	20.492	0.016	0.016	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.020	-0.016	20.796	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.028	-0.013	23.865	0.001	0.001	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.849	-0.912	26.592	-0.012	-0.012	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.783	-0.895	27.041	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.037	-0.010	27.862	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.038	-0.024	24.592	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.025	0.012	23.510	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.787	-0.880	23.711	-0.049	-0.049	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.897	0.963	25.341	0.068	0.068	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.015	-0.018	19.716	-0.014	-0.014	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.026	0.001	21.030	-0.018	-0.018	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.028	-0.018	22.213	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.821	-0.897	21.874	-0.150	-0.150	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.045	-0.005	17.154	-0.027	-0.027	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.009	-0.013	18.419	-0.034	-0.034	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.897	0.950	20.108	0.141	0.141	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.001	-0.010	16.029	-0.027	-0.027	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.045	-0.018	15.245	-0.062	-0.062	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.846	-0.922	16.335	-0.281	-0.281	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.774	0.855	16.869	0.219	0.219	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.013	-0.018	12.040	-0.062	-0.062	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.022	-0.015	13.389	-0.082	-0.082	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.768	-0.862	15.677	-0.422	-0.422	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.036	-0.014	10.970	-0.028	-0.028	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.050	-0.035	9.600	-0.104	-0.104	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.850	0.907	13.063	0.380	0.380	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.827	0.907	15.805	0.384	0.384	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.079	-0.039	9.449	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.972	-0.966	13.101	-0.756	-0.756	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.958	-0.960	14.716	-0.286	-0.286	0.000	0.000	0.000	0.000

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