FMO DATABASE

FMODB ID: LZKZ9

Calculation Name: 2FK9-A-Xray372

Preferred Name: Protein kinase C eta

Target Type: SINGLE PROTEIN

Ligand Name:
Warning: Undefined variable $Ligand in /home/FMODBwui_src/fmodbwui/detail.php on line 448

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 448

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 448

ligand 3-letter code:
Warning: Undefined variable $Ligand in /home/FMODBwui_src/fmodbwui/detail.php on line 449

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 449

Warning: Trying to access array offset on value of type null in /home/FMODBwui_src/fmodbwui/detail.php on line 449

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	OptH
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	-1215091.168545
FMO2-HF: Nuclear repulsion	1160366.777161
FMO2-HF: Total energy	-54724.391385
FMO2-MP2: Total energy	-54885.928933

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.
-2.85	-0.916	-0.007	-0.898	-1.029	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 : 0.008 / q_NPA : -0.009

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	0.022	0.008	3.654	-2.866	-0.932	-0.007	-0.898	-1.029	0.003
4	A	-6	GLY	0	-0.004	-0.008	6.161	0.257	0.257	0.000	0.000	0.000	0.000
5	A	-5	LEU	0	-0.055	-0.026	5.340	0.121	0.121	0.000	0.000	0.000	0.000
6	A	-4	VAL	0	0.021	0.016	8.573	0.088	0.088	0.000	0.000	0.000	0.000
7	A	-3	PRO	0	-0.010	0.003	12.257	-0.065	-0.065	0.000	0.000	0.000	0.000
8	A	5	THR	0	-0.006	-0.025	15.644	0.023	0.023	0.000	0.000	0.000	0.000
9	A	6	MET	0	-0.046	-0.023	16.105	-0.039	-0.039	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.953	1.002	18.637	0.110	0.110	0.000	0.000	0.000	0.000
11	A	8	PHE	0	0.022	0.018	21.632	-0.032	-0.032	0.000	0.000	0.000	0.000
12	A	9	ASN	0	0.002	0.007	21.226	0.009	0.009	0.000	0.000	0.000	0.000
13	A	10	GLY	0	0.025	0.016	24.734	-0.015	-0.015	0.000	0.000	0.000	0.000
14	A	11	TYR	0	-0.043	-0.015	27.892	0.012	0.012	0.000	0.000	0.000	0.000
15	A	12	LEU	0	0.054	0.035	31.641	0.003	0.003	0.000	0.000	0.000	0.000
16	A	13	ARG	1	0.933	0.963	33.702	0.105	0.105	0.000	0.000	0.000	0.000
17	A	14	VAL	0	0.033	0.014	37.096	0.002	0.002	0.000	0.000	0.000	0.000
18	A	15	ARG	1	0.877	0.933	38.956	0.081	0.081	0.000	0.000	0.000	0.000
19	A	16	ILE	0	0.018	0.021	41.813	0.003	0.003	0.000	0.000	0.000	0.000
20	A	17	GLY	0	0.055	0.024	44.858	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.952	-0.984	47.698	-0.025	-0.025	0.000	0.000	0.000	0.000
22	A	19	ALA	0	0.021	0.014	48.027	0.000	0.000	0.000	0.000	0.000	0.000
23	A	20	VAL	0	-0.054	-0.039	49.240	0.001	0.001	0.000	0.000	0.000	0.000
24	A	21	GLY	0	0.001	-0.002	49.786	0.001	0.001	0.000	0.000	0.000	0.000
25	A	22	LEU	0	0.022	0.024	48.515	0.002	0.002	0.000	0.000	0.000	0.000
26	A	23	GLN	0	-0.017	-0.025	50.767	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	24	PRO	0	-0.018	-0.003	51.507	0.000	0.000	0.000	0.000	0.000	0.000
28	A	25	THR	0	0.121	0.070	49.336	0.003	0.003	0.000	0.000	0.000	0.000
29	A	26	ARG	1	1.019	0.985	52.389	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	27	TRP	0	0.030	0.010	52.399	0.001	0.001	0.000	0.000	0.000	0.000
31	A	28	SER	0	0.071	0.017	53.735	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	29	LEU	0	0.008	0.017	55.540	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	30	ARG	1	0.887	0.946	57.847	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	31	HIS	1	0.814	0.908	56.721	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	32	SER	0	0.059	0.046	57.515	0.000	0.000	0.000	0.000	0.000	0.000
36	A	33	LEU	0	0.006	0.001	57.071	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	34	PHE	0	-0.004	0.008	60.563	0.002	0.002	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.907	0.938	63.084	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.908	0.960	62.985	0.002	0.002	0.000	0.000	0.000	0.000
40	A	37	GLY	0	0.010	0.017	66.253	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	38	HIS	0	0.013	0.022	61.406	0.000	0.000	0.000	0.000	0.000	0.000
42	A	39	GLN	0	-0.023	-0.025	59.287	0.001	0.001	0.000	0.000	0.000	0.000
43	A	40	LEU	0	-0.032	-0.005	58.479	0.001	0.001	0.000	0.000	0.000	0.000
44	A	41	LEU	0	-0.006	-0.019	52.246	0.000	0.000	0.000	0.000	0.000	0.000
45	A	42	ASP	-1	-0.811	-0.893	55.468	-0.016	-0.016	0.000	0.000	0.000	0.000
46	A	43	PRO	0	-0.024	0.004	50.928	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	44	TYR	0	-0.046	-0.037	46.786	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	45	LEU	0	0.024	0.008	42.550	0.003	0.003	0.000	0.000	0.000	0.000
49	A	46	THR	0	-0.029	-0.018	41.878	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	47	VAL	0	0.051	0.027	37.831	0.003	0.003	0.000	0.000	0.000	0.000
51	A	48	SER	0	-0.018	-0.016	36.276	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	49	VAL	0	0.027	0.015	30.374	0.002	0.002	0.000	0.000	0.000	0.000
53	A	50	ASP	-1	-0.752	-0.855	28.197	-0.081	-0.081	0.000	0.000	0.000	0.000
54	A	51	GLN	0	-0.026	-0.033	30.121	0.005	0.005	0.000	0.000	0.000	0.000
55	A	52	VAL	0	0.013	0.026	32.440	0.002	0.002	0.000	0.000	0.000	0.000
56	A	53	ARG	1	0.916	0.958	35.103	0.042	0.042	0.000	0.000	0.000	0.000
57	A	54	VAL	0	-0.007	-0.018	35.062	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	55	GLY	0	-0.018	-0.009	38.387	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	56	GLN	0	-0.055	-0.024	41.849	0.002	0.002	0.000	0.000	0.000	0.000
60	A	57	THR	0	-0.018	0.004	45.124	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	58	SER	0	-0.078	-0.074	47.765	0.003	0.003	0.000	0.000	0.000	0.000
62	A	59	THR	0	0.008	-0.015	51.183	0.000	0.000	0.000	0.000	0.000	0.000
63	A	60	LYS	1	0.853	0.946	53.275	0.033	0.033	0.000	0.000	0.000	0.000
64	A	61	GLN	0	0.018	0.001	55.652	0.003	0.003	0.000	0.000	0.000	0.000
65	A	62	LYS	1	0.847	0.908	58.843	0.014	0.014	0.000	0.000	0.000	0.000
66	A	63	THR	0	0.020	0.004	55.392	0.001	0.001	0.000	0.000	0.000	0.000
67	A	64	ASN	0	0.036	0.017	54.497	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	65	LYS	1	0.914	0.953	53.207	0.016	0.016	0.000	0.000	0.000	0.000
69	A	66	PRO	0	0.003	0.022	50.980	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	67	THR	0	0.057	0.018	51.895	0.001	0.001	0.000	0.000	0.000	0.000
71	A	68	TYR	0	-0.102	-0.086	48.624	0.001	0.001	0.000	0.000	0.000	0.000
72	A	69	ASN	0	-0.032	-0.016	48.634	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	70	GLU	-1	-0.785	-0.847	47.351	-0.045	-0.045	0.000	0.000	0.000	0.000
74	A	71	GLU	-1	-0.943	-0.983	43.502	-0.071	-0.071	0.000	0.000	0.000	0.000
75	A	72	PHE	0	-0.005	0.000	40.425	0.000	0.000	0.000	0.000	0.000	0.000
76	A	73	CYS	0	-0.073	-0.037	37.615	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	74	ALA	0	0.046	0.020	34.227	0.003	0.003	0.000	0.000	0.000	0.000
78	A	75	ASN	0	0.009	0.002	30.740	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	76	VAL	0	-0.029	-0.002	27.196	0.010	0.010	0.000	0.000	0.000	0.000
80	A	77	THR	0	-0.001	-0.019	24.875	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	78	ASP	-1	-0.927	-0.976	21.057	-0.250	-0.250	0.000	0.000	0.000	0.000
82	A	79	GLY	0	0.012	0.013	23.439	0.026	0.026	0.000	0.000	0.000	0.000
83	A	80	GLY	0	-0.116	-0.079	25.090	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	81	HIS	0	-0.051	-0.040	26.310	0.001	0.001	0.000	0.000	0.000	0.000
85	A	82	LEU	0	0.013	0.025	29.894	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	83	GLU	-1	-0.892	-0.957	33.509	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	84	LEU	0	-0.031	-0.015	36.222	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	85	ALA	0	0.032	0.007	39.847	0.007	0.007	0.000	0.000	0.000	0.000
89	A	86	VAL	0	0.000	0.003	42.270	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	87	PHE	0	-0.006	-0.010	43.282	0.005	0.005	0.000	0.000	0.000	0.000
91	A	88	HIS	0	0.000	-0.019	48.412	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	89	GLU	-1	-0.839	-0.909	52.200	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	90	THR	0	-0.099	-0.048	53.878	0.001	0.001	0.000	0.000	0.000	0.000
94	A	91	PRO	0	-0.043	-0.031	56.252	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	92	LEU	0	0.015	0.003	57.901	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	93	GLY	0	-0.018	-0.002	54.902	0.002	0.002	0.000	0.000	0.000	0.000
97	A	94	TYR	0	-0.010	-0.007	48.515	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	95	ASP	-1	-0.731	-0.826	49.558	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	96	HIS	0	-0.081	-0.041	50.074	0.004	0.004	0.000	0.000	0.000	0.000
100	A	97	PHE	0	0.035	0.029	42.341	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	98	VAL	0	-0.084	-0.044	46.851	0.002	0.002	0.000	0.000	0.000	0.000
102	A	99	ALA	0	0.019	0.004	44.622	0.004	0.004	0.000	0.000	0.000	0.000
103	A	100	ASN	0	-0.055	-0.024	38.293	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	101	CYS	0	0.041	0.040	38.379	0.002	0.002	0.000	0.000	0.000	0.000
105	A	102	THR	0	-0.015	0.002	32.091	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	103	LEU	0	0.027	0.012	33.250	0.005	0.005	0.000	0.000	0.000	0.000
107	A	104	GLN	0	0.003	-0.006	27.447	-0.015	-0.015	0.000	0.000	0.000	0.000
108	A	105	PHE	0	0.053	0.019	26.824	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	106	GLN	0	0.000	-0.013	22.707	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	107	GLU	-1	-0.894	-0.945	25.956	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	108	LEU	0	0.026	0.017	29.040	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	109	LEU	0	0.021	0.008	24.992	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	110	ARG	1	0.886	0.933	22.348	0.036	0.036	0.000	0.000	0.000	0.000
114	A	111	THR	0	-0.053	-0.017	28.068	0.007	0.007	0.000	0.000	0.000	0.000
115	A	112	THR	0	-0.034	-0.014	31.406	0.004	0.004	0.000	0.000	0.000	0.000
116	A	113	GLY	0	0.007	0.015	29.387	0.000	0.000	0.000	0.000	0.000	0.000
117	A	114	ALA	0	-0.046	-0.031	29.970	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	115	SER	0	-0.032	0.002	31.663	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	116	ASP	-1	-0.805	-0.900	31.255	-0.153	-0.153	0.000	0.000	0.000	0.000
120	A	117	THR	0	-0.103	-0.061	33.206	0.001	0.001	0.000	0.000	0.000	0.000
121	A	118	PHE	0	0.030	0.019	35.016	0.003	0.003	0.000	0.000	0.000	0.000
122	A	119	GLU	-1	-0.946	-0.983	36.832	-0.059	-0.059	0.000	0.000	0.000	0.000
123	A	120	GLY	0	0.008	0.004	40.560	0.003	0.003	0.000	0.000	0.000	0.000
124	A	121	TRP	0	-0.075	-0.037	41.959	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	122	VAL	0	0.008	0.005	38.273	0.001	0.001	0.000	0.000	0.000	0.000
126	A	123	ASP	-1	-0.877	-0.942	40.574	0.002	0.002	0.000	0.000	0.000	0.000
127	A	124	LEU	0	-0.099	-0.061	40.787	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	125	GLU	-1	-0.881	-0.918	39.504	0.025	0.025	0.000	0.000	0.000	0.000
129	A	126	PRO	0	-0.092	-0.066	42.683	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	127	GLU	-1	-0.851	-0.926	44.959	0.014	0.014	0.000	0.000	0.000	0.000
131	A	128	GLY	0	0.002	0.007	47.027	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	129	LYS	1	0.923	0.984	44.928	0.012	0.012	0.000	0.000	0.000	0.000
133	A	130	VAL	0	-0.004	-0.017	42.826	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	131	PHE	0	0.016	0.016	43.614	0.000	0.000	0.000	0.000	0.000	0.000
135	A	132	VAL	0	-0.016	-0.007	39.251	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	133	VAL	0	0.045	0.019	40.417	0.000	0.000	0.000	0.000	0.000	0.000
137	A	134	ILE	0	-0.037	-0.024	34.592	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	135	THR	0	-0.033	-0.008	34.795	0.003	0.003	0.000	0.000	0.000	0.000
139	A	136	LEU	0	-0.021	0.001	29.197	0.000	0.000	0.000	0.000	0.000	0.000
140	A	137	THR	0	0.032	0.020	28.069	-0.001	-0.001	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:-9:HIS)