FMO DATABASE

FMODB ID: 94Y32

Calculation Name: 1WK2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WK2

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SM30

Base Structure: X-ray

Registration Date: 2023-06-21

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	90
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-648923.260867
FMO2-HF: Nuclear repulsion	613090.103878
FMO2-HF: Total energy	-35833.156989
FMO2-MP2: Total energy	-35939.487933

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-5.812	-2.047	6.67	-3.638	-6.797	-0.022

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : 0.014

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	3	ARG	1	0.892	0.948	3.734	1.201	2.599	-0.006	-0.577	-0.815	0.003
4	A	4	PRO	0	-0.002	0.029	5.408	-0.151	-0.151	0.000	0.000	0.000	0.000
5	A	5	LYS	1	0.957	0.967	6.427	0.953	0.953	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.005	0.001	8.519	0.147	0.147	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.015	-0.010	10.090	-0.163	-0.163	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.008	0.011	12.598	0.093	0.093	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.012	0.010	15.353	-0.039	-0.039	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.016	0.020	16.824	0.029	0.029	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.902	0.948	20.119	0.235	0.235	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.703	-0.797	21.534	-0.360	-0.360	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.034	0.008	23.491	0.020	0.020	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.024	-0.008	20.375	-0.030	-0.030	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.007	-0.005	17.680	-0.038	-0.038	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.006	-0.026	16.827	-0.062	-0.062	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.023	-0.008	17.437	-0.034	-0.034	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.021	-0.005	12.700	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.031	-0.011	12.678	-0.074	-0.074	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.830	-0.888	13.570	-0.488	-0.488	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.032	0.013	13.171	0.025	0.025	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.896	0.955	14.088	0.355	0.355	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.806	0.898	15.895	0.384	0.384	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.100	0.052	12.940	-0.040	-0.040	0.000	0.000	0.000	0.000
25	A	25	TRP	0	0.016	0.020	13.474	0.016	0.016	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.766	-0.869	15.154	-0.269	-0.269	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.024	0.002	16.803	0.033	0.033	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.804	0.880	18.316	0.228	0.228	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.947	0.964	21.056	0.072	0.072	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.932	0.972	21.043	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.898	0.945	18.372	-0.162	-0.162	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.008	-0.029	13.558	0.011	0.011	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.886	0.937	13.783	-0.327	-0.327	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.015	0.012	6.555	0.294	0.294	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.828	0.900	7.513	-0.499	-0.499	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.057	0.049	3.778	0.612	0.880	0.006	-0.084	-0.189	0.000
37	A	37	PRO	0	0.015	0.016	2.186	-0.971	-0.687	3.782	-1.150	-2.916	-0.001
38	A	38	LEU	0	-0.053	-0.015	5.106	0.461	0.550	-0.001	-0.009	-0.079	0.000
39	A	39	GLY	0	0.014	-0.001	8.645	-0.153	-0.153	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.017	-0.007	11.034	0.152	0.152	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.021	-0.019	14.315	0.004	0.004	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.031	-0.054	17.387	0.051	0.051	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.028	0.009	20.900	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.006	0.003	22.511	0.009	0.009	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.921	0.957	19.954	0.275	0.275	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.026	0.004	12.186	0.011	0.011	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.001	-0.012	15.672	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.077	0.035	12.774	0.020	0.020	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.047	-0.003	5.421	0.424	0.424	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.059	0.025	7.389	0.066	0.066	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.789	-0.884	2.655	-10.426	-9.040	2.878	-1.750	-2.514	-0.024
52	A	52	LEU	0	-0.051	-0.029	5.262	0.329	0.372	-0.001	-0.001	-0.041	0.000
53	A	53	VAL	0	0.036	0.023	5.439	0.332	0.332	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.003	-0.002	7.672	0.291	0.291	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.064	-0.012	11.458	-0.062	-0.062	0.000	0.000	0.000	0.000
56	A	86	PRO	0	0.052	0.005	28.012	0.000	0.000	0.000	0.000	0.000	0.000
57	A	87	LEU	0	-0.056	-0.025	23.785	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	88	TYR	0	0.023	0.012	19.596	0.020	0.020	0.000	0.000	0.000	0.000
59	A	89	ALA	0	0.040	0.015	17.839	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	90	TRP	0	-0.054	-0.040	13.485	0.026	0.026	0.000	0.000	0.000	0.000
61	A	91	VAL	0	0.026	0.008	11.197	-0.046	-0.046	0.000	0.000	0.000	0.000
62	A	92	LEU	0	-0.058	-0.040	9.232	-0.036	-0.036	0.000	0.000	0.000	0.000
63	A	93	GLU	-1	-0.843	-0.933	6.733	-0.916	-0.916	0.000	0.000	0.000	0.000
64	A	94	ASN	0	-0.053	-0.046	3.361	0.570	0.867	0.012	-0.067	-0.243	0.000
65	A	95	ALA	0	-0.029	-0.009	6.807	-0.077	-0.077	0.000	0.000	0.000	0.000
66	A	96	PHE	0	0.015	0.010	6.455	0.191	0.191	0.000	0.000	0.000	0.000
67	A	97	ARG	1	0.823	0.888	10.997	0.409	0.409	0.000	0.000	0.000	0.000
68	A	98	TYR	0	-0.090	-0.078	9.259	0.043	0.043	0.000	0.000	0.000	0.000
69	A	99	GLU	-1	-0.809	-0.895	14.792	-0.350	-0.350	0.000	0.000	0.000	0.000
70	A	100	LYS	1	0.881	0.929	17.755	0.405	0.405	0.000	0.000	0.000	0.000
71	A	101	PRO	0	-0.019	-0.001	17.868	-0.052	-0.052	0.000	0.000	0.000	0.000
72	A	102	LEU	0	0.030	0.017	14.521	0.043	0.043	0.000	0.000	0.000	0.000
73	A	103	HIS	0	0.049	0.020	18.469	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	104	VAL	0	0.000	0.030	17.613	-0.030	-0.030	0.000	0.000	0.000	0.000
75	A	105	PRO	0	-0.006	-0.022	19.647	0.024	0.024	0.000	0.000	0.000	0.000
76	A	106	ARG	1	0.906	0.936	16.678	0.388	0.388	0.000	0.000	0.000	0.000
77	A	107	ARG	1	1.017	0.998	17.764	0.107	0.107	0.000	0.000	0.000	0.000
78	A	108	PRO	0	0.057	0.036	16.081	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	109	GLY	0	-0.004	0.016	13.316	-0.050	-0.050	0.000	0.000	0.000	0.000
80	A	110	ARG	1	0.838	0.907	10.580	0.574	0.574	0.000	0.000	0.000	0.000
81	A	111	VAL	0	-0.003	0.002	14.675	0.014	0.014	0.000	0.000	0.000	0.000
82	A	112	MET	0	-0.004	-0.002	16.304	-0.027	-0.027	0.000	0.000	0.000	0.000
83	A	113	PHE	0	0.032	0.007	14.593	0.017	0.017	0.000	0.000	0.000	0.000
84	A	114	VAL	0	0.014	0.011	18.022	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	115	ASP	-1	-0.785	-0.839	15.736	0.180	0.180	0.000	0.000	0.000	0.000
86	A	116	LEU	0	0.027	0.004	17.047	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	117	SER	0	-0.021	-0.032	14.380	0.023	0.023	0.000	0.000	0.000	0.000
88	A	118	GLU	-1	-0.818	-0.899	16.417	0.209	0.209	0.000	0.000	0.000	0.000
89	A	119	VAL	0	-0.022	0.003	19.558	-0.031	-0.031	0.000	0.000	0.000	0.000
90	A	120	ARG	1	0.983	0.994	21.938	-0.104	-0.104	0.000	0.000	0.000	0.000

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