FMO DATABASE

FMODB ID: XMMJZ

Calculation Name: 3KHF-A-Xray13

Preferred Name: Microtubule-associated serine/threonine-protein kinase 3

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3KHF

Chain ID: A

ChEMBL ID: CHEMBL2417352

UniProt ID: O60307

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	98
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-648127.202401
FMO2-HF: Nuclear repulsion	611258.863553
FMO2-HF: Total energy	-36868.338847
FMO2-MP2: Total energy	-36976.722973

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:947:ACE)

Summations of interaction energy for fragment #1(A:947:ACE)

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.
-0.185	0.591	-0.01	-0.324	-0.442	0

Interaction energy analysis for fragmet #1(A:947:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : -0.007

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].
3	A	949	PRO	0	-0.025	0.006	3.853	0.970	1.746	-0.010	-0.324	-0.442
4	A	950	PRO	0	-0.017	-0.014	6.828	-0.065	-0.065	0.000	0.000	0.000
5	A	951	ILE	0	0.039	0.028	9.714	-0.001	-0.001	0.000	0.000	0.000
6	A	952	VAL	0	-0.047	-0.027	12.707	0.077	0.077	0.000	0.000	0.000
7	A	953	ILE	0	0.009	0.015	15.606	0.001	0.001	0.000	0.000	0.000
8	A	954	HIS	0	-0.013	-0.015	18.952	0.020	0.020	0.000	0.000	0.000
9	A	955	SER	0	0.066	0.022	22.331	0.000	0.000	0.000	0.000	0.000
10	A	956	SER	0	0.028	-0.003	25.247	0.005	0.005	0.000	0.000	0.000
11	A	957	GLY	0	-0.017	-0.013	28.495	0.005	0.005	0.000	0.000	0.000
12	A	958	LYS	1	0.902	0.979	27.937	0.104	0.104	0.000	0.000	0.000
13	A	959	LYS	1	0.995	0.992	27.341	0.085	0.085	0.000	0.000	0.000
14	A	960	TYR	0	0.023	-0.025	21.923	-0.007	-0.007	0.000	0.000	0.000
15	A	961	GLY	0	-0.011	-0.007	23.715	-0.009	-0.009	0.000	0.000	0.000
16	A	962	PHE	0	0.027	0.024	19.525	-0.011	-0.011	0.000	0.000	0.000
17	A	963	SER	0	-0.012	0.014	23.282	0.011	0.011	0.000	0.000	0.000
18	A	964	LEU	0	0.039	0.007	19.851	-0.015	-0.015	0.000	0.000	0.000
19	A	965	ARG	1	0.908	0.972	21.889	0.082	0.082	0.000	0.000	0.000
20	A	966	ALA	0	0.047	0.030	21.511	-0.006	-0.006	0.000	0.000	0.000
21	A	967	ILE	0	-0.041	-0.030	21.129	0.003	0.003	0.000	0.000	0.000
22	A	968	ARG	1	0.948	0.978	22.176	0.018	0.018	0.000	0.000	0.000
23	A	969	VAL	0	0.011	0.011	19.713	-0.004	-0.004	0.000	0.000	0.000
24	A	970	TYR	0	0.048	0.016	22.923	0.007	0.007	0.000	0.000	0.000
25	A	971	MET	0	-0.032	-0.021	21.090	-0.001	-0.001	0.000	0.000	0.000
26	A	972	GLY	0	-0.009	-0.009	25.268	0.003	0.003	0.000	0.000	0.000
27	A	973	ASP	-1	-0.891	-0.935	29.055	0.009	0.009	0.000	0.000	0.000
28	A	974	SER	0	-0.075	-0.032	31.195	0.000	0.000	0.000	0.000	0.000
29	A	975	ASP	-1	-0.895	-0.945	30.678	0.008	0.008	0.000	0.000	0.000
30	A	976	VAL	0	-0.042	-0.029	26.481	0.002	0.002	0.000	0.000	0.000
31	A	977	TYR	0	-0.009	-0.018	24.769	-0.003	-0.003	0.000	0.000	0.000
32	A	978	THR	0	-0.010	0.006	18.629	0.010	0.010	0.000	0.000	0.000
33	A	979	VAL	0	-0.021	-0.002	21.357	-0.009	-0.009	0.000	0.000	0.000
34	A	980	HIS	0	-0.010	-0.008	15.920	0.014	0.014	0.000	0.000	0.000
35	A	981	HIS	0	0.011	0.017	17.293	-0.017	-0.017	0.000	0.000	0.000
36	A	982	VAL	0	0.017	0.007	16.641	-0.018	-0.018	0.000	0.000	0.000
37	A	983	VAL	0	0.016	0.006	16.788	0.020	0.020	0.000	0.000	0.000
38	A	984	TRP	0	0.012	-0.016	19.168	-0.004	-0.004	0.000	0.000	0.000
39	A	985	SER	0	-0.030	-0.010	22.369	0.004	0.004	0.000	0.000	0.000
40	A	986	VAL	0	-0.006	-0.018	19.718	-0.001	-0.001	0.000	0.000	0.000
41	A	987	GLU	-1	-0.940	-0.968	23.105	-0.098	-0.098	0.000	0.000	0.000
42	A	988	ASP	-1	-0.836	-0.901	25.484	-0.138	-0.138	0.000	0.000	0.000
43	A	989	GLY	0	-0.047	-0.025	26.521	0.009	0.009	0.000	0.000	0.000
44	A	990	SER	0	-0.115	-0.057	24.251	0.002	0.002	0.000	0.000	0.000
45	A	991	PRO	0	0.008	-0.022	23.229	-0.008	-0.008	0.000	0.000	0.000
46	A	992	ALA	0	0.006	0.004	19.855	-0.018	-0.018	0.000	0.000	0.000
47	A	993	GLN	0	0.075	0.026	19.309	-0.019	-0.019	0.000	0.000	0.000
48	A	994	GLU	-1	-1.032	-1.004	20.210	-0.176	-0.176	0.000	0.000	0.000
49	A	995	ALA	0	-0.043	-0.019	16.960	-0.016	-0.016	0.000	0.000	0.000
50	A	996	GLY	0	0.000	0.004	15.723	-0.056	-0.056	0.000	0.000	0.000
51	A	997	LEU	0	-0.088	-0.027	14.756	-0.046	-0.046	0.000	0.000	0.000
52	A	998	ARG	1	0.922	0.974	14.802	0.336	0.336	0.000	0.000	0.000
53	A	999	ALA	0	0.009	0.000	17.031	0.003	0.003	0.000	0.000	0.000
54	A	1000	GLY	0	0.024	0.001	17.721	-0.015	-0.015	0.000	0.000	0.000
55	A	1001	ASP	-1	-0.887	-0.940	13.557	-0.438	-0.438	0.000	0.000	0.000
56	A	1002	LEU	0	-0.021	-0.011	11.866	0.050	0.050	0.000	0.000	0.000
57	A	1003	ILE	0	0.000	-0.015	11.997	-0.061	-0.061	0.000	0.000	0.000
58	A	1004	THR	0	-0.032	-0.048	9.553	0.012	0.012	0.000	0.000	0.000
59	A	1005	HIS	0	-0.006	0.011	9.236	0.004	0.004	0.000	0.000	0.000
60	A	1006	ILE	0	0.066	0.036	12.679	-0.064	-0.064	0.000	0.000	0.000
61	A	1007	ASN	0	0.009	-0.010	15.343	0.008	0.008	0.000	0.000	0.000
62	A	1008	GLY	0	-0.028	-0.012	12.650	0.019	0.019	0.000	0.000	0.000
63	A	1009	GLU	-1	-0.931	-0.947	13.712	0.080	0.080	0.000	0.000	0.000
64	A	1010	SER	0	-0.033	-0.031	13.659	-0.016	-0.016	0.000	0.000	0.000
65	A	1011	VAL	0	0.048	0.010	14.579	-0.006	-0.006	0.000	0.000	0.000
66	A	1012	LEU	0	-0.041	-0.020	13.795	-0.012	-0.012	0.000	0.000	0.000
67	A	1013	GLY	0	-0.027	-0.015	16.328	0.016	0.016	0.000	0.000	0.000
68	A	1014	LEU	0	-0.003	0.028	19.678	-0.001	-0.001	0.000	0.000	0.000
69	A	1015	VAL	0	0.045	0.007	21.725	-0.010	-0.010	0.000	0.000	0.000
70	A	1016	HIS	0	0.032	-0.004	23.875	-0.002	-0.002	0.000	0.000	0.000
71	A	1017	MET	0	-0.024	-0.027	24.663	-0.007	-0.007	0.000	0.000	0.000
72	A	1018	ASP	-1	-0.826	-0.896	24.107	0.003	0.003	0.000	0.000	0.000
73	A	1019	VAL	0	0.002	0.004	19.726	-0.003	-0.003	0.000	0.000	0.000
74	A	1020	VAL	0	-0.030	-0.025	22.232	-0.009	-0.009	0.000	0.000	0.000
75	A	1021	GLU	-1	-0.850	-0.909	24.857	-0.013	-0.013	0.000	0.000	0.000
76	A	1022	LEU	0	0.004	0.000	19.698	-0.004	-0.004	0.000	0.000	0.000
77	A	1023	LEU	0	-0.054	-0.027	19.330	-0.009	-0.009	0.000	0.000	0.000
78	A	1024	LEU	0	-0.048	-0.031	22.865	-0.004	-0.004	0.000	0.000	0.000
79	A	1025	LYS	1	0.854	0.926	25.793	0.011	0.011	0.000	0.000	0.000
80	A	1026	SER	0	-0.037	-0.004	21.704	0.003	0.003	0.000	0.000	0.000
81	A	1027	GLY	0	0.032	0.022	23.619	0.001	0.001	0.000	0.000	0.000
82	A	1028	ASN	0	-0.050	-0.028	24.225	-0.002	-0.002	0.000	0.000	0.000
83	A	1029	LYS	1	0.941	0.987	20.123	0.095	0.095	0.000	0.000	0.000
84	A	1030	ILE	0	0.026	0.033	17.500	0.015	0.015	0.000	0.000	0.000
85	A	1031	SER	0	-0.009	-0.004	13.063	-0.047	-0.047	0.000	0.000	0.000
86	A	1032	LEU	0	0.051	0.026	13.159	0.048	0.048	0.000	0.000	0.000
87	A	1033	ARG	1	0.907	0.968	5.050	-0.333	-0.333	0.000	0.000	0.000
88	A	1034	THR	0	0.032	0.008	8.808	0.050	0.050	0.000	0.000	0.000
89	A	1035	THR	0	-0.057	-0.034	7.856	-0.317	-0.317	0.000	0.000	0.000
90	A	1036	ALA	0	0.041	0.023	9.349	0.108	0.108	0.000	0.000	0.000
91	A	1037	LEU	0	0.007	0.019	11.360	-0.048	-0.048	0.000	0.000	0.000
92	A	1038	GLU	-1	-0.882	-0.942	13.866	-0.202	-0.202	0.000	0.000	0.000
93	A	1039	ASN	0	-0.086	-0.057	16.310	0.016	0.016	0.000	0.000	0.000
94	A	1040	THR	0	-0.036	-0.025	17.619	0.009	0.009	0.000	0.000	0.000
95	A	1041	GLU	-1	-0.880	-0.928	21.133	-0.128	-0.128	0.000	0.000	0.000
96	A	1042	THR	0	-0.031	-0.024	23.431	0.000	0.000	0.000	0.000	0.000
97	A	1043	SER	0	-0.061	-0.029	26.300	0.006	0.006	0.000	0.000	0.000
98	A	1044	VAL	-1	-0.941	-0.960	29.640	-0.050	-0.050	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:947:ACE)