FMO DATABASE

FMODB ID: MVQVZ

Calculation Name: 2FK9-A-Xray372

Preferred Name: Protein kinase C eta

Target Type: SINGLE PROTEIN

Ligand Name:
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ligand 3-letter code:
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PDB ID: 2FK9

Chain ID: A

ChEMBL ID: CHEMBL3616

UniProt ID: P24723

Base Structure: X-ray

Registration Date: 2023-09-20

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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1216152.702174
FMO2-HF: Nuclear repulsion	1161427.190763
FMO2-HF: Total energy	-54725.511411
FMO2-MP2: Total energy	-54886.835526

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:-9:HIS)

Summations of interaction energy for fragment #1(A:-9:HIS)

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.
-2.387	-0.84	-0.013	-0.693	-0.841	0.003

Interaction energy analysis for fragmet #1(A:-9:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.012

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	-7	SER	0	0.053	0.018	3.863	-2.350	-0.803	-0.013	-0.693	-0.841	0.003
4	A	-6	GLY	0	-0.025	0.002	6.172	0.076	0.076	0.000	0.000	0.000	0.000
5	A	-5	LEU	0	-0.038	-0.023	5.358	0.175	0.175	0.000	0.000	0.000	0.000
6	A	-4	VAL	0	0.009	0.005	8.901	0.058	0.058	0.000	0.000	0.000	0.000
7	A	-3	PRO	0	-0.015	0.004	12.588	-0.073	-0.073	0.000	0.000	0.000	0.000
8	A	5	THR	0	-0.021	-0.032	15.465	0.006	0.006	0.000	0.000	0.000	0.000
9	A	6	MET	0	0.005	0.010	15.741	-0.019	-0.019	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.799	0.912	18.353	0.024	0.024	0.000	0.000	0.000	0.000
11	A	8	PHE	0	0.010	0.009	21.617	-0.036	-0.036	0.000	0.000	0.000	0.000
12	A	9	ASN	0	-0.041	-0.036	21.583	0.002	0.002	0.000	0.000	0.000	0.000
13	A	10	GLY	0	0.010	0.014	24.795	-0.016	-0.016	0.000	0.000	0.000	0.000
14	A	11	TYR	0	-0.021	-0.009	27.883	0.012	0.012	0.000	0.000	0.000	0.000
15	A	12	LEU	0	0.029	0.022	31.702	0.002	0.002	0.000	0.000	0.000	0.000
16	A	13	ARG	1	0.834	0.889	33.895	0.067	0.067	0.000	0.000	0.000	0.000
17	A	14	VAL	0	0.000	0.004	36.901	0.002	0.002	0.000	0.000	0.000	0.000
18	A	15	ARG	1	0.876	0.934	38.775	0.052	0.052	0.000	0.000	0.000	0.000
19	A	16	ILE	0	0.017	0.015	41.809	0.003	0.003	0.000	0.000	0.000	0.000
20	A	17	GLY	0	0.056	0.027	44.989	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.791	-0.870	47.975	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	19	ALA	0	0.015	0.018	47.882	0.000	0.000	0.000	0.000	0.000	0.000
23	A	20	VAL	0	-0.045	-0.030	49.146	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	21	GLY	0	0.016	0.006	49.630	0.002	0.002	0.000	0.000	0.000	0.000
25	A	22	LEU	0	0.023	0.028	48.079	0.002	0.002	0.000	0.000	0.000	0.000
26	A	23	GLN	0	-0.022	-0.028	50.506	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	24	PRO	0	-0.039	-0.022	51.573	0.001	0.001	0.000	0.000	0.000	0.000
28	A	25	THR	0	0.104	0.070	49.437	0.003	0.003	0.000	0.000	0.000	0.000
29	A	26	ARG	1	0.992	0.974	52.465	-0.043	-0.043	0.000	0.000	0.000	0.000
30	A	27	TRP	0	0.048	0.021	52.404	0.000	0.000	0.000	0.000	0.000	0.000
31	A	28	SER	0	0.068	0.027	53.557	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	29	LEU	0	0.017	0.013	55.571	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	30	ARG	1	0.875	0.941	57.763	-0.028	-0.028	0.000	0.000	0.000	0.000
34	A	31	HIS	1	0.809	0.904	56.494	-0.027	-0.027	0.000	0.000	0.000	0.000
35	A	32	SER	0	0.052	0.033	57.095	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	33	LEU	0	0.051	0.023	57.012	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	34	PHE	0	-0.038	-0.007	60.527	0.000	0.000	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.946	0.959	62.768	-0.020	-0.020	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.849	0.934	62.501	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	37	GLY	0	0.013	0.015	65.925	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	38	HIS	0	0.006	0.017	61.192	0.000	0.000	0.000	0.000	0.000	0.000
42	A	39	GLN	0	-0.020	-0.024	59.438	0.000	0.000	0.000	0.000	0.000	0.000
43	A	40	LEU	0	-0.015	-0.002	58.425	0.001	0.001	0.000	0.000	0.000	0.000
44	A	41	LEU	0	0.024	-0.003	52.217	0.000	0.000	0.000	0.000	0.000	0.000
45	A	42	ASP	-1	-0.783	-0.866	55.466	0.002	0.002	0.000	0.000	0.000	0.000
46	A	43	PRO	0	0.018	0.026	50.708	0.000	0.000	0.000	0.000	0.000	0.000
47	A	44	TYR	0	-0.045	-0.045	46.773	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	45	LEU	0	0.041	0.013	42.147	0.004	0.004	0.000	0.000	0.000	0.000
49	A	46	THR	0	-0.046	-0.024	41.901	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	47	VAL	0	0.018	0.008	37.913	0.004	0.004	0.000	0.000	0.000	0.000
51	A	48	SER	0	0.011	-0.008	35.935	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	49	VAL	0	0.030	0.013	30.478	0.000	0.000	0.000	0.000	0.000	0.000
53	A	50	ASP	-1	-0.747	-0.848	26.918	0.004	0.004	0.000	0.000	0.000	0.000
54	A	51	GLN	0	0.003	0.000	29.696	0.006	0.006	0.000	0.000	0.000	0.000
55	A	52	VAL	0	-0.008	0.016	32.273	0.000	0.000	0.000	0.000	0.000	0.000
56	A	53	ARG	1	0.941	0.970	34.851	0.004	0.004	0.000	0.000	0.000	0.000
57	A	54	VAL	0	-0.024	-0.021	35.092	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	55	GLY	0	-0.002	0.000	38.384	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	56	GLN	0	-0.041	-0.027	41.829	0.005	0.005	0.000	0.000	0.000	0.000
60	A	57	THR	0	-0.031	0.009	44.985	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	58	SER	0	-0.057	-0.052	47.797	0.002	0.002	0.000	0.000	0.000	0.000
62	A	59	THR	0	-0.013	-0.042	51.282	0.001	0.001	0.000	0.000	0.000	0.000
63	A	60	LYS	1	0.780	0.923	52.145	0.014	0.014	0.000	0.000	0.000	0.000
64	A	61	GLN	0	0.004	-0.016	55.240	0.003	0.003	0.000	0.000	0.000	0.000
65	A	62	LYS	1	0.794	0.866	58.340	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	63	THR	0	0.009	0.005	55.286	0.001	0.001	0.000	0.000	0.000	0.000
67	A	64	ASN	0	0.042	0.019	54.406	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	65	LYS	1	0.781	0.874	53.082	0.004	0.004	0.000	0.000	0.000	0.000
69	A	66	PRO	0	0.012	0.021	50.670	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	67	THR	0	-0.002	-0.030	51.921	0.001	0.001	0.000	0.000	0.000	0.000
71	A	68	TYR	0	-0.110	-0.075	48.436	0.000	0.000	0.000	0.000	0.000	0.000
72	A	69	ASN	0	-0.012	-0.015	49.076	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	70	GLU	-1	-0.745	-0.836	47.442	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	71	GLU	-1	-0.815	-0.902	43.661	-0.052	-0.052	0.000	0.000	0.000	0.000
75	A	72	PHE	0	0.021	0.007	40.749	0.000	0.000	0.000	0.000	0.000	0.000
76	A	73	CYS	0	-0.064	-0.036	37.713	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	74	ALA	0	0.042	0.028	34.492	0.003	0.003	0.000	0.000	0.000	0.000
78	A	75	ASN	0	0.001	0.002	31.013	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	76	VAL	0	-0.031	-0.010	27.775	0.012	0.012	0.000	0.000	0.000	0.000
80	A	77	THR	0	0.012	0.002	25.296	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	78	ASP	-1	-0.836	-0.920	21.058	-0.134	-0.134	0.000	0.000	0.000	0.000
82	A	79	GLY	0	0.013	0.029	23.645	0.031	0.031	0.000	0.000	0.000	0.000
83	A	80	GLY	0	-0.074	-0.065	25.099	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	81	HIS	0	-0.062	-0.050	25.970	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	82	LEU	0	0.029	0.028	29.666	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	83	GLU	-1	-0.883	-0.948	33.221	0.037	0.037	0.000	0.000	0.000	0.000
87	A	84	LEU	0	-0.034	-0.017	36.024	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	85	ALA	0	0.042	0.011	39.728	0.006	0.006	0.000	0.000	0.000	0.000
89	A	86	VAL	0	-0.019	-0.005	41.978	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	87	PHE	0	0.008	-0.004	43.161	0.005	0.005	0.000	0.000	0.000	0.000
91	A	88	HIS	0	-0.021	0.001	48.427	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	89	GLU	-1	-0.821	-0.895	52.271	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	90	THR	0	-0.112	-0.074	53.929	0.001	0.001	0.000	0.000	0.000	0.000
94	A	91	PRO	0	-0.027	-0.022	56.108	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	92	LEU	0	0.011	0.000	57.856	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	93	GLY	0	-0.031	-0.005	55.152	0.002	0.002	0.000	0.000	0.000	0.000
97	A	94	TYR	0	0.000	0.005	48.734	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	95	ASP	-1	-0.729	-0.827	49.566	0.007	0.007	0.000	0.000	0.000	0.000
99	A	96	HIS	0	-0.097	-0.049	49.573	0.004	0.004	0.000	0.000	0.000	0.000
100	A	97	PHE	0	0.046	0.036	42.112	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	98	VAL	0	-0.082	-0.041	46.962	0.001	0.001	0.000	0.000	0.000	0.000
102	A	99	ALA	0	0.033	0.008	44.686	0.003	0.003	0.000	0.000	0.000	0.000
103	A	100	ASN	0	-0.070	-0.037	38.125	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	101	CYS	0	0.008	0.017	38.238	0.003	0.003	0.000	0.000	0.000	0.000
105	A	102	THR	0	-0.003	-0.005	32.070	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	103	LEU	0	0.030	0.019	32.735	0.004	0.004	0.000	0.000	0.000	0.000
107	A	104	GLN	0	0.037	0.008	26.963	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	105	PHE	0	0.022	0.011	26.708	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	106	GLN	0	0.023	-0.010	22.099	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	107	GLU	-1	-0.905	-0.940	25.748	0.056	0.056	0.000	0.000	0.000	0.000
111	A	108	LEU	0	0.021	0.017	28.887	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	109	LEU	0	0.045	0.016	25.713	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	110	ARG	1	0.851	0.921	22.084	-0.042	-0.042	0.000	0.000	0.000	0.000
114	A	111	THR	0	-0.056	-0.028	28.372	0.005	0.005	0.000	0.000	0.000	0.000
115	A	112	THR	0	-0.036	-0.023	31.732	0.002	0.002	0.000	0.000	0.000	0.000
116	A	113	GLY	0	-0.010	-0.001	29.237	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	114	ALA	0	-0.044	-0.017	29.661	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	115	SER	0	-0.012	0.002	31.904	-0.007	-0.007	0.000	0.000	0.000	0.000
119	A	116	ASP	-1	-0.832	-0.910	31.946	-0.115	-0.115	0.000	0.000	0.000	0.000
120	A	117	THR	0	-0.070	-0.030	33.323	0.003	0.003	0.000	0.000	0.000	0.000
121	A	118	PHE	0	0.028	0.020	35.352	0.002	0.002	0.000	0.000	0.000	0.000
122	A	119	GLU	-1	-0.929	-0.972	37.219	-0.040	-0.040	0.000	0.000	0.000	0.000
123	A	120	GLY	0	0.013	0.002	40.933	0.003	0.003	0.000	0.000	0.000	0.000
124	A	121	TRP	0	-0.041	-0.033	42.241	0.000	0.000	0.000	0.000	0.000	0.000
125	A	122	VAL	0	0.020	0.016	38.104	0.001	0.001	0.000	0.000	0.000	0.000
126	A	123	ASP	-1	-0.879	-0.951	40.855	0.024	0.024	0.000	0.000	0.000	0.000
127	A	124	LEU	0	-0.075	-0.038	40.905	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	125	GLU	-1	-0.857	-0.902	39.329	0.058	0.058	0.000	0.000	0.000	0.000
129	A	126	PRO	0	-0.092	-0.061	42.565	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	127	GLU	-1	-0.844	-0.930	44.947	0.035	0.035	0.000	0.000	0.000	0.000
131	A	128	GLY	0	0.015	0.017	47.367	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	129	LYS	1	0.882	0.964	44.800	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	130	VAL	0	0.012	-0.016	42.733	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	131	PHE	0	-0.016	0.004	43.686	0.001	0.001	0.000	0.000	0.000	0.000
135	A	132	VAL	0	-0.005	-0.014	39.597	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	133	VAL	0	0.018	0.009	40.516	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	134	ILE	0	-0.037	-0.016	34.689	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	135	THR	0	-0.024	-0.018	35.306	0.002	0.002	0.000	0.000	0.000	0.000
139	A	136	LEU	0	-0.033	-0.009	29.716	0.002	0.002	0.000	0.000	0.000	0.000
140	A	137	THR	0	0.029	0.019	28.496	-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:-9:HIS)