FMO DATABASE

FMODB ID: LZL19

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

Total energy (hartree)

FMO2-HF: Electronic energy	-647998.846534
FMO2-HF: Nuclear repulsion	612165.97464
FMO2-HF: Total energy	-35832.871894
FMO2-MP2: Total energy	-35939.204311

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.
-5.824	-2.328	7.09	-3.766	-6.82	-0.018

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 : 0.032 / q_NPA : 0.011

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	0.909	0.952	3.812	1.110	2.674	-0.010	-0.707	-0.848	0.004
4	A	4	PRO	0	0.012	0.034	5.259	-0.414	-0.414	0.000	0.000	0.000	0.000
5	A	5	LYS	1	0.954	0.963	6.425	0.886	0.886	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.006	0.002	8.762	0.136	0.136	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.001	0.005	10.120	-0.121	-0.121	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.001	0.005	12.796	0.093	0.093	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.008	-0.013	15.217	-0.039	-0.039	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.021	-0.013	16.438	0.031	0.031	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.966	0.989	19.661	0.187	0.187	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.761	-0.845	21.183	-0.352	-0.352	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.009	-0.010	23.290	0.022	0.022	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.026	-0.004	19.780	-0.028	-0.028	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.022	0.012	17.359	-0.038	-0.038	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.001	-0.027	16.628	-0.064	-0.064	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.022	-0.012	17.323	-0.032	-0.032	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.042	-0.017	12.728	-0.021	-0.021	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.035	-0.014	12.441	-0.079	-0.079	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.823	-0.876	13.463	-0.503	-0.503	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.008	0.001	13.126	0.020	0.020	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.919	0.964	13.974	0.352	0.352	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.797	0.907	15.998	0.340	0.340	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.102	0.041	12.851	-0.055	-0.055	0.000	0.000	0.000	0.000
25	A	25	TRP	0	0.016	0.017	13.358	0.018	0.018	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.788	-0.885	15.054	-0.236	-0.236	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.014	0.002	16.693	0.036	0.036	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.820	0.891	17.905	0.187	0.187	0.000	0.000	0.000	0.000
29	A	29	ARG	1	1.001	0.996	20.690	0.051	0.051	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.935	0.979	21.145	-0.048	-0.048	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.887	0.948	18.139	-0.217	-0.217	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.022	-0.028	13.647	0.011	0.011	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.896	0.919	13.831	-0.402	-0.402	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.012	0.007	6.704	0.322	0.322	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.855	0.919	7.235	-0.737	-0.737	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.054	0.040	3.632	0.724	1.013	0.008	-0.091	-0.205	0.000
37	A	37	PRO	0	0.018	0.025	2.204	-0.823	-1.192	4.685	-1.268	-3.048	-0.001
38	A	38	LEU	0	-0.064	-0.025	4.951	0.358	0.462	-0.001	-0.017	-0.085	0.000
39	A	39	GLY	0	-0.003	-0.005	8.612	-0.127	-0.127	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.003	0.003	11.010	0.147	0.147	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.015	-0.021	14.152	0.002	0.002	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.042	0.024	17.308	0.056	0.056	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.005	-0.001	20.719	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.016	-0.011	22.237	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.942	0.976	20.302	0.282	0.282	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.044	-0.014	12.578	0.006	0.006	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.023	-0.008	15.317	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.085	0.048	12.461	0.008	0.008	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.060	-0.007	5.206	0.434	0.434	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.070	0.032	7.397	0.018	0.018	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.803	-0.884	2.625	-9.608	-8.112	2.386	-1.587	-2.295	-0.021
52	A	52	LEU	0	-0.048	-0.022	5.276	0.259	0.305	-0.001	-0.001	-0.044	0.000
53	A	53	VAL	0	0.048	0.022	5.096	0.416	0.416	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.008	0.005	7.573	0.292	0.292	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.056	-0.019	11.343	-0.097	-0.097	0.000	0.000	0.000	0.000
56	A	86	PRO	0	0.039	0.000	27.841	0.000	0.000	0.000	0.000	0.000	0.000
57	A	87	LEU	0	-0.095	-0.042	23.638	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	88	TYR	0	0.028	0.006	19.382	0.020	0.020	0.000	0.000	0.000	0.000
59	A	89	ALA	0	0.032	0.012	17.744	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	90	TRP	0	-0.051	-0.029	13.272	0.023	0.023	0.000	0.000	0.000	0.000
61	A	91	VAL	0	0.035	0.016	10.928	-0.051	-0.051	0.000	0.000	0.000	0.000
62	A	92	LEU	0	-0.054	-0.037	8.950	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	93	GLU	-1	-0.872	-0.938	6.262	-0.827	-0.827	0.000	0.000	0.000	0.000
64	A	94	ASN	0	-0.036	-0.034	3.299	0.362	0.728	0.023	-0.095	-0.295	0.000
65	A	95	ALA	0	-0.030	-0.008	6.601	-0.152	-0.152	0.000	0.000	0.000	0.000
66	A	96	PHE	0	0.011	0.008	6.150	0.205	0.205	0.000	0.000	0.000	0.000
67	A	97	ARG	1	0.824	0.877	10.793	0.426	0.426	0.000	0.000	0.000	0.000
68	A	98	TYR	0	-0.123	-0.097	9.153	0.078	0.078	0.000	0.000	0.000	0.000
69	A	99	GLU	-1	-0.850	-0.932	14.449	-0.380	-0.380	0.000	0.000	0.000	0.000
70	A	100	LYS	1	0.925	0.968	17.554	0.401	0.401	0.000	0.000	0.000	0.000
71	A	101	PRO	0	-0.029	-0.007	17.805	-0.051	-0.051	0.000	0.000	0.000	0.000
72	A	102	LEU	0	0.037	0.020	14.381	0.039	0.039	0.000	0.000	0.000	0.000
73	A	103	HIS	0	0.036	0.017	18.362	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	104	VAL	0	0.000	0.015	17.664	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	105	PRO	0	0.008	-0.004	20.178	0.022	0.022	0.000	0.000	0.000	0.000
76	A	106	ARG	1	0.909	0.939	17.004	0.397	0.397	0.000	0.000	0.000	0.000
77	A	107	ARG	1	1.021	0.991	18.489	0.114	0.114	0.000	0.000	0.000	0.000
78	A	108	PRO	0	0.049	0.032	16.880	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	109	GLY	0	0.000	0.027	13.649	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	110	ARG	1	0.830	0.898	10.783	0.577	0.577	0.000	0.000	0.000	0.000
81	A	111	VAL	0	-0.009	0.000	14.985	0.009	0.009	0.000	0.000	0.000	0.000
82	A	112	MET	0	-0.005	-0.001	16.653	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	113	PHE	0	0.029	0.001	14.799	0.013	0.013	0.000	0.000	0.000	0.000
84	A	114	VAL	0	0.018	0.014	18.129	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	115	ASP	-1	-0.778	-0.823	15.668	0.237	0.237	0.000	0.000	0.000	0.000
86	A	116	LEU	0	0.037	0.005	16.974	-0.012	-0.012	0.000	0.000	0.000	0.000
87	A	117	SER	0	-0.028	-0.030	14.548	0.021	0.021	0.000	0.000	0.000	0.000
88	A	118	GLU	-1	-0.845	-0.910	16.598	0.272	0.272	0.000	0.000	0.000	0.000
89	A	119	VAL	0	-0.045	-0.010	19.779	-0.031	-0.031	0.000	0.000	0.000	0.000
90	A	120	ARG	1	0.977	0.999	22.042	-0.126	-0.126	0.000	0.000	0.000	0.000

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