FMO DATABASE

FMODB ID: Z6NNN

Calculation Name: 3MOP-A-Xray372

Preferred Name: Interleukin-1 receptor-associated kinase-like 2

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3MOP

Chain ID: A

ChEMBL ID: CHEMBL4105759

UniProt ID: O43187

Base Structure: X-ray

Registration Date: 2023-06-22

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	105
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-809305.254637
FMO2-HF: Nuclear repulsion	767526.925504
FMO2-HF: Total energy	-41778.329133
FMO2-MP2: Total energy	-41899.697459

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:19:MET)

Summations of interaction energy for fragment #1(A:19:MET)

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.
-15.819	-18.641	17.97	-6.752	-8.394	0.025

Interaction energy analysis for fragmet #1(A:19:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.001

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	21	PRO	0	0.073	0.026	3.888	1.313	2.817	-0.015	-0.814	-0.674	0.002
4	A	22	LEU	0	0.042	-0.002	6.971	-0.152	-0.152	0.000	0.000	0.000	0.000
5	A	23	ALA	0	-0.004	0.014	8.525	-0.101	-0.101	0.000	0.000	0.000	0.000
6	A	24	ALA	0	-0.019	0.002	6.836	-0.033	-0.033	0.000	0.000	0.000	0.000
7	A	25	LEU	0	-0.059	-0.016	6.600	-0.014	-0.014	0.000	0.000	0.000	0.000
8	A	26	ASN	0	-0.002	-0.030	9.826	0.062	0.062	0.000	0.000	0.000	0.000
9	A	27	MET	0	0.013	-0.012	13.347	0.017	0.017	0.000	0.000	0.000	0.000
10	A	28	ARG	1	0.889	0.945	14.209	0.025	0.025	0.000	0.000	0.000	0.000
11	A	29	VAL	0	0.057	0.024	9.727	0.022	0.022	0.000	0.000	0.000	0.000
12	A	30	ARG	1	0.792	0.893	12.967	-0.067	-0.067	0.000	0.000	0.000	0.000
13	A	31	ARG	1	0.966	0.996	14.125	-0.025	-0.025	0.000	0.000	0.000	0.000
14	A	32	ARG	1	0.761	0.829	15.299	-0.039	-0.039	0.000	0.000	0.000	0.000
15	A	33	LEU	0	0.078	0.034	10.408	0.008	0.008	0.000	0.000	0.000	0.000
16	A	34	SER	0	-0.004	-0.033	14.696	0.017	0.017	0.000	0.000	0.000	0.000
17	A	35	LEU	0	-0.126	-0.057	17.986	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	36	PHE	0	0.003	0.024	16.911	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	37	LEU	0	0.024	0.019	13.286	0.002	0.002	0.000	0.000	0.000	0.000
20	A	38	ASN	0	0.012	0.014	17.999	0.011	0.011	0.000	0.000	0.000	0.000
21	A	39	VAL	0	-0.027	0.005	21.148	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	40	ARG	1	0.797	0.869	23.146	-0.102	-0.102	0.000	0.000	0.000	0.000
23	A	41	THR	0	-0.016	-0.023	23.542	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	42	GLN	0	-0.003	0.008	25.236	0.006	0.006	0.000	0.000	0.000	0.000
25	A	43	VAL	0	-0.036	-0.021	26.826	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	44	ALA	0	-0.003	0.005	22.725	0.001	0.001	0.000	0.000	0.000	0.000
27	A	45	ALA	0	0.071	0.050	18.079	0.000	0.000	0.000	0.000	0.000	0.000
28	A	46	ASP	-1	-0.733	-0.825	19.530	0.126	0.126	0.000	0.000	0.000	0.000
29	A	47	TRP	0	0.044	-0.009	17.457	0.018	0.018	0.000	0.000	0.000	0.000
30	A	48	THR	0	-0.053	-0.036	18.373	0.017	0.017	0.000	0.000	0.000	0.000
31	A	49	ALA	0	0.038	0.019	19.425	0.008	0.008	0.000	0.000	0.000	0.000
32	A	50	LEU	0	-0.014	-0.010	12.007	0.014	0.014	0.000	0.000	0.000	0.000
33	A	51	ALA	0	0.036	-0.003	15.432	0.045	0.045	0.000	0.000	0.000	0.000
34	A	52	GLU	-1	-0.970	-0.984	17.185	0.166	0.166	0.000	0.000	0.000	0.000
35	A	53	GLU	-1	-0.812	-0.886	14.391	0.307	0.307	0.000	0.000	0.000	0.000
36	A	54	MET	0	-0.071	-0.020	11.930	0.052	0.052	0.000	0.000	0.000	0.000
37	A	55	ASP	-1	-0.832	-0.884	12.494	0.421	0.421	0.000	0.000	0.000	0.000
38	A	56	PHE	0	-0.034	-0.015	14.849	-0.035	-0.035	0.000	0.000	0.000	0.000
39	A	57	GLU	-1	-0.881	-0.934	18.693	0.073	0.073	0.000	0.000	0.000	0.000
40	A	58	TYR	0	0.051	0.010	22.337	0.001	0.001	0.000	0.000	0.000	0.000
41	A	59	LEU	0	-0.007	-0.025	25.382	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	60	GLU	-1	-0.803	-0.873	19.484	0.155	0.155	0.000	0.000	0.000	0.000
43	A	61	ILE	0	0.025	0.010	20.976	0.001	0.001	0.000	0.000	0.000	0.000
44	A	62	ARG	1	0.859	0.913	23.412	-0.079	-0.079	0.000	0.000	0.000	0.000
45	A	63	GLN	0	-0.027	-0.012	24.346	0.000	0.000	0.000	0.000	0.000	0.000
46	A	64	LEU	0	0.015	0.007	19.816	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	65	GLU	-1	-0.895	-0.925	24.021	0.087	0.087	0.000	0.000	0.000	0.000
48	A	66	THR	0	-0.075	-0.023	25.893	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	67	GLN	0	-0.042	-0.018	24.797	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	68	ALA	0	0.049	0.010	24.389	0.008	0.008	0.000	0.000	0.000	0.000
51	A	69	ASP	-1	-0.779	-0.876	19.657	0.090	0.090	0.000	0.000	0.000	0.000
52	A	70	PRO	0	0.042	0.044	20.739	0.006	0.006	0.000	0.000	0.000	0.000
53	A	71	THR	0	0.013	-0.015	15.065	0.019	0.019	0.000	0.000	0.000	0.000
54	A	72	GLY	0	-0.003	-0.003	16.205	0.030	0.030	0.000	0.000	0.000	0.000
55	A	73	ARG	1	0.750	0.874	17.154	-0.074	-0.074	0.000	0.000	0.000	0.000
56	A	74	LEU	0	0.011	0.013	15.396	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	75	LEU	0	0.014	-0.002	11.101	0.042	0.042	0.000	0.000	0.000	0.000
58	A	76	ASP	-1	-0.817	-0.895	13.715	0.131	0.131	0.000	0.000	0.000	0.000
59	A	77	ALA	0	-0.029	-0.017	16.104	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	78	TRP	0	0.022	-0.005	8.318	0.103	0.103	0.000	0.000	0.000	0.000
61	A	79	GLN	0	-0.043	-0.027	11.038	0.043	0.043	0.000	0.000	0.000	0.000
62	A	80	GLY	0	-0.008	0.006	10.931	-0.030	-0.030	0.000	0.000	0.000	0.000
63	A	81	ARG	1	0.811	0.893	10.987	-0.272	-0.272	0.000	0.000	0.000	0.000
64	A	82	PRO	0	-0.016	-0.024	9.835	0.078	0.078	0.000	0.000	0.000	0.000
65	A	83	GLY	0	0.024	0.022	7.254	-0.188	-0.188	0.000	0.000	0.000	0.000
66	A	84	ALA	0	-0.038	0.010	6.651	0.590	0.590	0.000	0.000	0.000	0.000
67	A	85	SER	0	-0.014	-0.036	1.867	-8.419	-15.396	15.150	-5.243	-2.929	0.023
68	A	86	VAL	0	0.024	-0.003	2.969	-1.742	-0.655	0.111	-0.237	-0.961	0.000
69	A	87	GLY	0	-0.024	-0.003	2.271	-5.795	-3.536	2.533	-2.174	-2.618	0.001
70	A	88	ARG	1	0.831	0.907	2.977	-1.074	-2.407	0.172	1.801	-0.640	-0.001
71	A	89	LEU	0	0.004	-0.010	6.097	-0.741	-0.741	0.000	0.000	0.000	0.000
72	A	90	LEU	0	0.000	0.008	4.224	-0.452	-0.266	-0.001	-0.012	-0.173	0.000
73	A	91	GLU	-1	-0.879	-0.938	6.171	0.783	0.783	0.000	0.000	0.000	0.000
74	A	92	LEU	0	-0.023	-0.003	8.060	-0.145	-0.145	0.000	0.000	0.000	0.000
75	A	93	LEU	0	-0.022	-0.018	9.264	-0.104	-0.104	0.000	0.000	0.000	0.000
76	A	94	THR	0	-0.028	-0.030	8.989	-0.052	-0.052	0.000	0.000	0.000	0.000
77	A	95	LYS	1	0.794	0.879	11.602	-0.329	-0.329	0.000	0.000	0.000	0.000
78	A	96	LEU	0	-0.050	-0.027	13.900	-0.042	-0.042	0.000	0.000	0.000	0.000
79	A	97	GLY	0	0.016	0.030	15.206	-0.027	-0.027	0.000	0.000	0.000	0.000
80	A	98	ARG	1	0.748	0.847	14.366	-0.172	-0.172	0.000	0.000	0.000	0.000
81	A	99	ASP	-1	-0.856	-0.946	13.856	0.217	0.217	0.000	0.000	0.000	0.000
82	A	100	ASP	-1	-0.879	-0.936	14.799	0.109	0.109	0.000	0.000	0.000	0.000
83	A	101	VAL	0	0.028	0.012	12.564	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	102	LEU	0	-0.007	0.005	9.362	-0.037	-0.037	0.000	0.000	0.000	0.000
85	A	103	LEU	0	-0.049	-0.029	11.247	-0.024	-0.024	0.000	0.000	0.000	0.000
86	A	104	GLU	-1	-0.797	-0.856	13.215	0.044	0.044	0.000	0.000	0.000	0.000
87	A	105	LEU	0	-0.044	-0.031	10.544	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	106	GLY	0	0.057	0.045	7.942	-0.065	-0.065	0.000	0.000	0.000	0.000
89	A	107	PRO	0	0.056	0.027	8.061	-0.086	-0.086	0.000	0.000	0.000	0.000
90	A	108	SER	0	-0.095	-0.055	10.220	0.018	0.018	0.000	0.000	0.000	0.000
91	A	109	ILE	0	0.018	0.016	4.292	-0.081	-0.006	-0.001	-0.004	-0.069	0.000
92	A	110	GLU	-1	-0.908	-0.958	5.114	-0.093	-0.093	0.000	0.000	0.000	0.000
93	A	111	GLU	-1	-0.847	-0.901	6.066	0.069	0.069	0.000	0.000	0.000	0.000
94	A	112	ASP	-1	-0.759	-0.862	8.402	-0.119	-0.119	0.000	0.000	0.000	0.000
95	A	113	CYS	0	-0.051	-0.023	4.180	-0.215	0.162	0.021	-0.069	-0.330	0.000
96	A	114	GLN	0	-0.020	-0.006	6.151	0.035	0.035	0.000	0.000	0.000	0.000
97	A	115	LYS	1	0.766	0.857	9.354	0.100	0.100	0.000	0.000	0.000	0.000
98	A	116	TYR	0	-0.003	0.001	8.173	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	117	ILE	0	-0.002	-0.012	5.136	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	118	ALA	0	-0.058	-0.035	9.576	0.008	0.008	0.000	0.000	0.000	0.000
101	A	119	ALA	0	-0.005	0.011	12.777	0.027	0.027	0.000	0.000	0.000	0.000
102	A	120	ALA	0	-0.014	-0.002	11.306	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	121	LEU	0	-0.051	-0.030	12.175	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	122	GLU	-1	-0.871	-0.911	15.266	-0.151	-0.151	0.000	0.000	0.000	0.000
105	A	123	HIS	0	-0.117	-0.064	17.692	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:19:MET)