FMO DATABASE

FMODB ID: ZV52N

Calculation Name: 1WMH-A-Xray372

Preferred Name: Protein kinase C iota

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1WMH

Chain ID: A

ChEMBL ID: CHEMBL2598

UniProt ID: P41743

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	83
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-600820.709458
FMO2-HF: Nuclear repulsion	565428.998035
FMO2-HF: Total energy	-35391.711423
FMO2-MP2: Total energy	-35491.45608

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:16:GLN)

Summations of interaction energy for fragment #1(A:16:GLN)

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.
-40.528	-33.586	15.317	-9.973	-12.286	-0.074

Interaction energy analysis for fragmet #1(A:16:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.062 / q_NPA : -0.042

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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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	18	ARG	1	0.831	0.919	3.786	-1.033	1.254	-0.015	-1.062	-1.210	0.005
4	A	19	VAL	0	0.024	0.011	5.558	-0.771	-0.771	0.000	0.000	0.000	0.000
5	A	20	LYS	1	0.817	0.902	8.377	-0.146	-0.146	0.000	0.000	0.000	0.000
6	A	21	ALA	0	0.046	0.012	11.815	-0.205	-0.205	0.000	0.000	0.000	0.000
7	A	22	TYR	0	-0.006	-0.002	14.075	0.073	0.073	0.000	0.000	0.000	0.000
8	A	23	TYR	0	0.075	0.015	17.767	-0.094	-0.094	0.000	0.000	0.000	0.000
9	A	24	ARG	1	0.903	0.948	20.158	-0.102	-0.102	0.000	0.000	0.000	0.000
10	A	25	GLY	0	-0.013	-0.004	22.687	0.003	0.003	0.000	0.000	0.000	0.000
11	A	26	ASP	-1	-0.909	-0.932	19.904	0.393	0.393	0.000	0.000	0.000	0.000
12	A	27	ILE	0	-0.063	-0.045	15.300	-0.029	-0.029	0.000	0.000	0.000	0.000
13	A	28	MET	0	-0.021	-0.004	14.145	0.087	0.087	0.000	0.000	0.000	0.000
14	A	29	ILE	0	-0.059	-0.035	8.790	-0.131	-0.131	0.000	0.000	0.000	0.000
15	A	30	THR	0	0.006	0.001	7.648	0.507	0.507	0.000	0.000	0.000	0.000
16	A	31	HIS	0	-0.030	-0.016	2.598	-2.916	-1.126	0.821	-0.870	-1.742	0.009
17	A	32	PHE	0	0.054	0.032	3.327	-1.344	-0.406	0.030	-0.227	-0.741	-0.001
18	A	33	GLU	-1	-0.825	-0.909	1.784	-33.250	-32.200	12.901	-6.714	-7.237	-0.085
19	A	34	PRO	0	0.033	0.008	2.129	0.932	1.652	1.583	-1.049	-1.254	-0.002
20	A	35	SER	0	-0.047	-0.017	5.130	0.442	0.476	-0.001	-0.004	-0.029	0.000
21	A	36	ILE	0	-0.064	-0.016	7.331	0.396	0.396	0.000	0.000	0.000	0.000
22	A	37	SER	0	0.034	0.014	9.135	0.172	0.172	0.000	0.000	0.000	0.000
23	A	38	PHE	0	0.072	0.013	12.484	0.028	0.028	0.000	0.000	0.000	0.000
24	A	39	GLU	-1	-0.962	-0.975	14.536	-0.413	-0.413	0.000	0.000	0.000	0.000
25	A	40	GLY	0	0.008	0.001	12.016	0.084	0.084	0.000	0.000	0.000	0.000
26	A	41	LEU	0	0.017	0.009	9.288	0.122	0.122	0.000	0.000	0.000	0.000
27	A	42	CYS	0	-0.054	-0.029	11.976	0.201	0.201	0.000	0.000	0.000	0.000
28	A	43	ASN	0	-0.011	-0.020	14.508	0.148	0.148	0.000	0.000	0.000	0.000
29	A	44	GLU	-1	-0.821	-0.888	9.742	0.893	0.893	0.000	0.000	0.000	0.000
30	A	45	VAL	0	-0.004	-0.015	12.707	0.156	0.156	0.000	0.000	0.000	0.000
31	A	46	ARG	1	0.839	0.921	14.665	0.201	0.201	0.000	0.000	0.000	0.000
32	A	47	ASP	-1	-0.902	-0.934	14.300	0.375	0.375	0.000	0.000	0.000	0.000
33	A	48	MET	0	-0.029	-0.012	11.683	0.044	0.044	0.000	0.000	0.000	0.000
34	A	49	CYS	0	-0.114	-0.056	15.759	0.029	0.029	0.000	0.000	0.000	0.000
35	A	50	SER	0	-0.066	-0.025	18.869	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	51	PHE	0	-0.093	-0.044	19.949	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	52	ASP	-1	-0.850	-0.922	21.409	0.045	0.045	0.000	0.000	0.000	0.000
38	A	53	ASN	0	-0.012	-0.030	21.258	-0.022	-0.022	0.000	0.000	0.000	0.000
39	A	54	GLU	-1	-0.936	-0.969	22.629	-0.093	-0.093	0.000	0.000	0.000	0.000
40	A	55	GLN	0	-0.084	-0.021	23.133	0.000	0.000	0.000	0.000	0.000	0.000
41	A	56	LEU	0	0.006	0.002	23.207	-0.023	-0.023	0.000	0.000	0.000	0.000
42	A	57	PHE	0	-0.028	-0.028	17.526	0.034	0.034	0.000	0.000	0.000	0.000
43	A	58	THR	0	-0.023	-0.008	21.790	-0.037	-0.037	0.000	0.000	0.000	0.000
44	A	59	MET	0	0.015	0.026	15.592	0.059	0.059	0.000	0.000	0.000	0.000
45	A	60	LYS	1	0.928	0.963	18.522	0.079	0.079	0.000	0.000	0.000	0.000
46	A	61	TRP	0	0.044	0.024	14.567	0.041	0.041	0.000	0.000	0.000	0.000
47	A	62	ILE	0	-0.054	-0.017	16.397	0.013	0.013	0.000	0.000	0.000	0.000
48	A	63	ASP	-1	-0.787	-0.884	16.628	-0.325	-0.325	0.000	0.000	0.000	0.000
49	A	64	GLU	-1	-0.894	-0.956	17.450	-0.359	-0.359	0.000	0.000	0.000	0.000
50	A	65	GLU	-1	-1.008	-0.996	18.949	-0.190	-0.190	0.000	0.000	0.000	0.000
51	A	66	GLY	0	-0.087	-0.040	21.142	0.034	0.034	0.000	0.000	0.000	0.000
52	A	67	ASP	-1	-0.889	-0.947	22.213	-0.119	-0.119	0.000	0.000	0.000	0.000
53	A	68	PRO	0	-0.133	-0.060	20.720	-0.024	-0.024	0.000	0.000	0.000	0.000
54	A	69	CYS	0	0.022	0.004	18.742	0.001	0.001	0.000	0.000	0.000	0.000
55	A	70	THR	0	-0.078	-0.061	18.994	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	71	VAL	0	-0.006	0.018	14.810	-0.030	-0.030	0.000	0.000	0.000	0.000
57	A	72	SER	0	-0.045	-0.041	18.233	0.046	0.046	0.000	0.000	0.000	0.000
58	A	73	SER	0	-0.045	-0.058	18.419	0.000	0.000	0.000	0.000	0.000	0.000
59	A	74	GLN	0	0.017	-0.018	12.891	0.018	0.018	0.000	0.000	0.000	0.000
60	A	75	LEU	0	0.001	0.006	15.302	-0.073	-0.073	0.000	0.000	0.000	0.000
61	A	76	GLU	-1	-0.806	-0.875	16.455	-0.454	-0.454	0.000	0.000	0.000	0.000
62	A	77	LEU	0	-0.004	0.005	10.542	0.010	0.010	0.000	0.000	0.000	0.000
63	A	78	GLU	-1	-0.869	-0.922	11.624	-1.119	-1.119	0.000	0.000	0.000	0.000
64	A	79	GLU	-1	-0.779	-0.849	12.094	-0.841	-0.841	0.000	0.000	0.000	0.000
65	A	80	ALA	0	-0.017	0.002	12.057	-0.024	-0.024	0.000	0.000	0.000	0.000
66	A	81	PHE	0	0.020	-0.013	7.784	-0.181	-0.181	0.000	0.000	0.000	0.000
67	A	82	ARG	1	0.779	0.857	8.976	0.550	0.550	0.000	0.000	0.000	0.000
68	A	83	LEU	0	-0.005	-0.015	11.246	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	84	TYR	0	0.042	0.052	4.489	0.874	0.989	-0.001	-0.031	-0.082	0.000
70	A	85	GLU	-1	-0.912	-0.962	4.442	-4.959	-4.951	-0.001	-0.016	0.009	0.000
71	A	86	LEU	0	-0.085	-0.034	8.371	0.272	0.272	0.000	0.000	0.000	0.000
72	A	87	ASN	0	-0.036	-0.031	12.029	0.133	0.133	0.000	0.000	0.000	0.000
73	A	88	LYS	1	0.740	0.873	9.499	0.834	0.834	0.000	0.000	0.000	0.000
74	A	89	ASP	-1	-0.840	-0.908	10.182	-0.451	-0.451	0.000	0.000	0.000	0.000
75	A	90	SER	0	-0.075	-0.047	8.566	-0.157	-0.157	0.000	0.000	0.000	0.000
76	A	91	GLU	-1	-0.834	-0.914	8.475	1.033	1.033	0.000	0.000	0.000	0.000
77	A	92	LEU	0	0.054	0.047	9.044	-0.095	-0.095	0.000	0.000	0.000	0.000
78	A	93	LEU	0	-0.036	-0.015	10.714	0.218	0.218	0.000	0.000	0.000	0.000
79	A	94	ILE	0	0.028	0.005	11.249	-0.098	-0.098	0.000	0.000	0.000	0.000
80	A	95	HIS	0	-0.004	0.008	14.932	0.119	0.119	0.000	0.000	0.000	0.000
81	A	96	VAL	0	0.014	-0.002	16.595	-0.062	-0.062	0.000	0.000	0.000	0.000
82	A	97	PHE	0	-0.046	-0.036	19.273	0.035	0.035	0.000	0.000	0.000	0.000
83	A	98	PRO	0	0.014	0.013	22.983	-0.028	-0.028	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:GLN)