FMO DATABASE

FMODB ID: 94142

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1216195.701129
FMO2-HF: Nuclear repulsion	1161470.543357
FMO2-HF: Total energy	-54725.157772
FMO2-MP2: Total energy	-54886.638413

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.
-2.969	-0.956	-0.005	-0.948	-1.059	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 : 0.005 / q_NPA : -0.008

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	0.047	0.018	3.616	-2.993	-0.980	-0.005	-0.948	-1.059	0.003
4	A	-6	GLY	0	-0.029	-0.017	6.106	0.218	0.218	0.000	0.000	0.000	0.000
5	A	-5	LEU	0	-0.055	-0.027	5.246	0.124	0.124	0.000	0.000	0.000	0.000
6	A	-4	VAL	0	0.028	0.017	8.566	0.076	0.076	0.000	0.000	0.000	0.000
7	A	-3	PRO	0	-0.011	0.006	12.258	-0.065	-0.065	0.000	0.000	0.000	0.000
8	A	5	THR	0	-0.015	-0.030	15.608	0.014	0.014	0.000	0.000	0.000	0.000
9	A	6	MET	0	-0.029	-0.012	16.129	-0.034	-0.034	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.876	0.951	18.663	0.096	0.096	0.000	0.000	0.000	0.000
11	A	8	PHE	0	0.003	0.008	21.693	-0.031	-0.031	0.000	0.000	0.000	0.000
12	A	9	ASN	0	-0.030	-0.021	21.511	0.006	0.006	0.000	0.000	0.000	0.000
13	A	10	GLY	0	0.031	0.021	24.775	-0.015	-0.015	0.000	0.000	0.000	0.000
14	A	11	TYR	0	-0.033	-0.009	27.919	0.013	0.013	0.000	0.000	0.000	0.000
15	A	12	LEU	0	0.045	0.028	31.670	0.003	0.003	0.000	0.000	0.000	0.000
16	A	13	ARG	1	0.891	0.937	33.746	0.087	0.087	0.000	0.000	0.000	0.000
17	A	14	VAL	0	0.015	0.005	37.026	0.002	0.002	0.000	0.000	0.000	0.000
18	A	15	ARG	1	0.861	0.928	38.698	0.070	0.070	0.000	0.000	0.000	0.000
19	A	16	ILE	0	0.018	0.015	41.834	0.003	0.003	0.000	0.000	0.000	0.000
20	A	17	GLY	0	0.052	0.026	44.881	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.797	-0.894	47.717	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	19	ALA	0	0.012	0.009	48.045	0.000	0.000	0.000	0.000	0.000	0.000
23	A	20	VAL	0	-0.048	-0.036	49.258	0.000	0.000	0.000	0.000	0.000	0.000
24	A	21	GLY	0	0.011	0.006	49.803	0.001	0.001	0.000	0.000	0.000	0.000
25	A	22	LEU	0	0.011	0.018	48.516	0.002	0.002	0.000	0.000	0.000	0.000
26	A	23	GLN	0	-0.031	-0.032	50.786	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	24	PRO	0	-0.023	-0.006	51.522	0.001	0.001	0.000	0.000	0.000	0.000
28	A	25	THR	0	0.110	0.066	49.331	0.003	0.003	0.000	0.000	0.000	0.000
29	A	26	ARG	1	1.020	0.983	52.403	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	27	TRP	0	0.035	0.013	52.410	0.001	0.001	0.000	0.000	0.000	0.000
31	A	28	SER	0	0.088	0.032	53.564	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	29	LEU	0	0.007	0.016	55.554	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	30	ARG	1	0.891	0.948	57.858	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	31	HIS	1	0.815	0.909	56.575	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	32	SER	0	0.104	0.045	57.764	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	33	LEU	0	-0.030	-0.004	57.025	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	34	PHE	0	-0.014	0.008	60.577	0.001	0.001	0.000	0.000	0.000	0.000
38	A	35	LYS	1	0.922	0.951	63.098	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	36	LYS	1	0.886	0.934	62.900	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	37	GLY	0	0.010	0.019	66.267	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	38	HIS	0	0.012	0.022	61.417	0.000	0.000	0.000	0.000	0.000	0.000
42	A	39	GLN	0	-0.027	-0.027	59.330	0.000	0.000	0.000	0.000	0.000	0.000
43	A	40	LEU	0	-0.027	-0.003	58.487	0.001	0.001	0.000	0.000	0.000	0.000
44	A	41	LEU	0	0.009	-0.016	52.251	0.000	0.000	0.000	0.000	0.000	0.000
45	A	42	ASP	-1	-0.771	-0.858	55.505	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	43	PRO	0	0.002	0.016	50.934	0.000	0.000	0.000	0.000	0.000	0.000
47	A	44	TYR	0	-0.043	-0.039	46.812	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	45	LEU	0	0.020	0.003	42.413	0.004	0.004	0.000	0.000	0.000	0.000
49	A	46	THR	0	-0.009	-0.003	41.603	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	47	VAL	0	0.018	0.007	37.881	0.004	0.004	0.000	0.000	0.000	0.000
51	A	48	SER	0	-0.002	-0.009	36.109	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	49	VAL	0	0.026	0.016	30.570	0.002	0.002	0.000	0.000	0.000	0.000
53	A	50	ASP	-1	-0.758	-0.869	27.574	-0.052	-0.052	0.000	0.000	0.000	0.000
54	A	51	GLN	0	-0.004	-0.012	29.944	0.004	0.004	0.000	0.000	0.000	0.000
55	A	52	VAL	0	0.012	0.028	32.566	0.001	0.001	0.000	0.000	0.000	0.000
56	A	53	ARG	1	0.920	0.960	35.205	0.029	0.029	0.000	0.000	0.000	0.000
57	A	54	VAL	0	-0.007	-0.016	35.138	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	55	GLY	0	-0.014	-0.006	38.465	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	56	GLN	0	-0.053	-0.025	41.926	0.003	0.003	0.000	0.000	0.000	0.000
60	A	57	THR	0	-0.016	0.009	45.208	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	58	SER	0	-0.047	-0.043	47.844	0.002	0.002	0.000	0.000	0.000	0.000
62	A	59	THR	0	0.002	-0.030	51.268	0.001	0.001	0.000	0.000	0.000	0.000
63	A	60	LYS	1	0.776	0.905	52.465	0.027	0.027	0.000	0.000	0.000	0.000
64	A	61	GLN	0	0.015	-0.007	55.668	0.003	0.003	0.000	0.000	0.000	0.000
65	A	62	LYS	1	0.774	0.857	58.866	0.008	0.008	0.000	0.000	0.000	0.000
66	A	63	THR	0	0.032	0.009	55.453	0.001	0.001	0.000	0.000	0.000	0.000
67	A	64	ASN	0	0.034	0.022	54.519	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	65	LYS	1	0.800	0.887	53.216	0.014	0.014	0.000	0.000	0.000	0.000
69	A	66	PRO	0	0.004	0.022	51.010	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	67	THR	0	0.007	-0.013	51.918	0.001	0.001	0.000	0.000	0.000	0.000
71	A	68	TYR	0	-0.096	-0.072	48.650	0.000	0.000	0.000	0.000	0.000	0.000
72	A	69	ASN	0	-0.030	-0.015	48.630	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	70	GLU	-1	-0.758	-0.845	47.366	-0.036	-0.036	0.000	0.000	0.000	0.000
74	A	71	GLU	-1	-0.853	-0.935	43.375	-0.065	-0.065	0.000	0.000	0.000	0.000
75	A	72	PHE	0	-0.009	-0.004	40.519	0.000	0.000	0.000	0.000	0.000	0.000
76	A	73	CYS	0	-0.055	-0.030	37.631	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	74	ALA	0	0.035	0.019	34.319	0.002	0.002	0.000	0.000	0.000	0.000
78	A	75	ASN	0	-0.003	-0.001	30.779	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	76	VAL	0	-0.028	-0.006	27.489	0.010	0.010	0.000	0.000	0.000	0.000
80	A	77	THR	0	0.020	-0.002	24.974	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	78	ASP	-1	-0.867	-0.938	21.038	-0.217	-0.217	0.000	0.000	0.000	0.000
82	A	79	GLY	0	0.003	0.016	23.519	0.028	0.028	0.000	0.000	0.000	0.000
83	A	80	GLY	0	-0.102	-0.072	25.161	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	81	HIS	0	-0.051	-0.042	26.325	0.003	0.003	0.000	0.000	0.000	0.000
85	A	82	LEU	0	0.014	0.023	29.910	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	83	GLU	-1	-0.888	-0.945	33.524	0.009	0.009	0.000	0.000	0.000	0.000
87	A	84	LEU	0	-0.028	-0.014	36.238	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	85	ALA	0	0.023	0.002	39.863	0.006	0.006	0.000	0.000	0.000	0.000
89	A	86	VAL	0	0.002	0.004	42.285	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	87	PHE	0	0.008	-0.005	43.224	0.005	0.005	0.000	0.000	0.000	0.000
91	A	88	HIS	0	-0.009	-0.002	48.426	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	89	GLU	-1	-0.834	-0.902	52.215	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	90	THR	0	-0.099	-0.048	53.892	0.002	0.002	0.000	0.000	0.000	0.000
94	A	91	PRO	0	-0.027	-0.022	56.265	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	92	LEU	0	0.005	-0.001	57.896	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	93	GLY	0	-0.015	0.004	54.914	0.002	0.002	0.000	0.000	0.000	0.000
97	A	94	TYR	0	-0.025	-0.015	48.559	0.000	0.000	0.000	0.000	0.000	0.000
98	A	95	ASP	-1	-0.735	-0.833	49.524	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	96	HIS	0	-0.101	-0.060	50.078	0.004	0.004	0.000	0.000	0.000	0.000
100	A	97	PHE	0	0.038	0.033	42.106	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	98	VAL	0	-0.083	-0.044	46.868	0.002	0.002	0.000	0.000	0.000	0.000
102	A	99	ALA	0	0.025	0.009	44.640	0.004	0.004	0.000	0.000	0.000	0.000
103	A	100	ASN	0	-0.074	-0.040	38.219	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	101	CYS	0	0.030	0.023	38.404	0.003	0.003	0.000	0.000	0.000	0.000
105	A	102	THR	0	-0.009	0.009	32.236	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	103	LEU	0	0.018	0.007	33.252	0.005	0.005	0.000	0.000	0.000	0.000
107	A	104	GLN	0	0.029	0.009	27.459	-0.012	-0.012	0.000	0.000	0.000	0.000
108	A	105	PHE	0	0.037	0.013	26.887	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	106	GLN	0	0.019	-0.007	22.171	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	107	GLU	-1	-0.897	-0.942	25.969	0.014	0.014	0.000	0.000	0.000	0.000
111	A	108	LEU	0	0.004	0.012	29.047	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	109	LEU	0	0.030	0.010	25.103	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	110	ARG	1	0.886	0.936	22.254	0.001	0.001	0.000	0.000	0.000	0.000
114	A	111	THR	0	-0.061	-0.032	28.064	0.006	0.006	0.000	0.000	0.000	0.000
115	A	112	THR	0	-0.034	-0.014	31.386	0.003	0.003	0.000	0.000	0.000	0.000
116	A	113	GLY	0	0.004	0.012	29.375	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	114	ALA	0	-0.047	-0.033	29.962	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	115	SER	0	-0.023	0.008	31.650	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	116	ASP	-1	-0.826	-0.912	31.473	-0.134	-0.134	0.000	0.000	0.000	0.000
120	A	117	THR	0	-0.075	-0.041	33.211	0.001	0.001	0.000	0.000	0.000	0.000
121	A	118	PHE	0	0.027	0.020	34.974	0.003	0.003	0.000	0.000	0.000	0.000
122	A	119	GLU	-1	-0.945	-0.978	36.837	-0.051	-0.051	0.000	0.000	0.000	0.000
123	A	120	GLY	0	0.015	-0.001	40.566	0.003	0.003	0.000	0.000	0.000	0.000
124	A	121	TRP	0	-0.065	-0.046	41.965	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	122	VAL	0	0.018	0.012	38.247	0.001	0.001	0.000	0.000	0.000	0.000
126	A	123	ASP	-1	-0.881	-0.946	40.592	0.012	0.012	0.000	0.000	0.000	0.000
127	A	124	LEU	0	-0.088	-0.050	40.804	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	125	GLU	-1	-0.879	-0.914	39.471	0.040	0.040	0.000	0.000	0.000	0.000
129	A	126	PRO	0	-0.075	-0.059	42.699	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	127	GLU	-1	-0.844	-0.926	44.975	0.023	0.023	0.000	0.000	0.000	0.000
131	A	128	GLY	0	0.006	0.013	47.043	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	129	LYS	1	0.909	0.980	44.957	0.003	0.003	0.000	0.000	0.000	0.000
133	A	130	VAL	0	0.010	-0.013	42.824	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	131	PHE	0	-0.003	0.015	43.629	0.000	0.000	0.000	0.000	0.000	0.000
135	A	132	VAL	0	-0.016	-0.012	39.333	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	133	VAL	0	0.049	0.023	40.387	0.000	0.000	0.000	0.000	0.000	0.000
137	A	134	ILE	0	-0.042	-0.023	34.626	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	135	THR	0	-0.035	-0.015	34.976	0.003	0.003	0.000	0.000	0.000	0.000
139	A	136	LEU	0	-0.019	0.002	29.385	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	137	THR	0	0.035	0.021	28.034	-0.005	-0.005	0.000	0.000	0.000	0.000

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