FMO DATABASE

FMODB ID: 1957Z

Calculation Name: 2EH0-A-Other547

Preferred Name: Kinesin-like protein KIF1B

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EH0

Chain ID: A

ChEMBL ID: CHEMBL5889

UniProt ID: O60333

Base Structure: SolutionNMR

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1070982.328546
FMO2-HF: Nuclear repulsion	1019684.191103
FMO2-HF: Total energy	-51298.137443
FMO2-MP2: Total energy	-51445.786123

3D Structure Molmil

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:1:GLY)

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

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.
-4.241	-3.281	-0.012	-0.384	-0.564	-0.002

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.922

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	3	SER	0	0.056	0.043	3.836	5.147	6.107	-0.012	-0.384	-0.564	-0.002
4	A	4	GLY	0	0.037	-0.002	6.580	4.138	4.138	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.044	-0.010	9.617	-0.879	-0.879	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.011	0.014	11.267	0.786	0.786	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.048	0.011	12.600	-1.593	-1.593	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.058	0.021	13.785	-0.469	-0.469	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.014	0.009	15.847	-0.855	-0.855	0.000	0.000	0.000	0.000
10	A	10	HIS	0	0.023	0.019	11.586	-1.290	-1.290	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.004	0.003	15.864	0.190	0.190	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.007	-0.012	11.216	-0.872	-0.872	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.048	0.020	13.481	1.994	1.994	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.068	-0.034	13.884	-1.315	-1.315	0.000	0.000	0.000	0.000
15	A	15	ASN	0	0.053	0.033	16.306	0.887	0.887	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.967	-0.986	18.210	-13.517	-13.517	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.903	-0.938	19.648	-13.795	-13.795	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.021	-0.030	15.720	-0.764	-0.764	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.030	-0.024	15.551	-0.887	-0.887	0.000	0.000	0.000	0.000
20	A	20	MET	0	-0.077	-0.015	13.995	0.673	0.673	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.003	-0.025	15.816	-1.009	-1.009	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.909	-0.920	15.980	-16.635	-16.635	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.036	-0.021	13.088	-1.121	-1.121	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.031	0.014	9.238	0.301	0.301	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.050	-0.025	8.928	0.219	0.219	0.000	0.000	0.000	0.000
26	A	26	TYR	0	0.056	0.028	12.760	-0.149	-0.149	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.035	-0.035	10.955	-0.390	-0.390	0.000	0.000	0.000	0.000
28	A	28	ILE	0	-0.028	-0.005	15.819	0.749	0.749	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.849	0.934	19.505	13.042	13.042	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.897	-0.960	21.358	-12.073	-12.073	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.076	0.044	24.541	0.206	0.206	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.055	-0.047	26.825	-0.251	-0.251	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.040	-0.031	22.349	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.879	0.939	25.730	9.783	9.783	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.007	-0.009	24.086	-0.466	-0.466	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.011	-0.003	26.377	0.466	0.466	0.000	0.000	0.000	0.000
37	A	37	GLN	0	0.014	-0.005	27.034	-0.397	-0.397	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.000	-0.012	26.880	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.909	-0.947	28.532	-9.802	-9.802	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.068	-0.021	31.371	0.348	0.348	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.924	-0.959	33.032	-8.398	-8.398	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.850	0.925	31.848	9.570	9.570	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.999	0.995	25.526	11.573	11.573	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.003	-0.014	26.875	-0.114	-0.114	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.908	-0.932	21.969	-14.750	-14.750	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.006	0.001	19.527	-0.722	-0.722	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.002	0.002	22.223	0.710	0.710	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.015	0.003	22.318	-0.621	-0.621	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.047	0.029	23.462	0.416	0.416	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.014	0.003	25.522	0.026	0.026	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.040	0.011	28.834	0.028	0.028	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.074	-0.029	30.285	0.324	0.324	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.008	-0.002	27.102	-0.075	-0.075	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.893	0.949	30.642	9.295	9.295	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.804	-0.909	30.977	-9.654	-9.654	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.865	-0.927	31.415	-9.412	-9.412	0.000	0.000	0.000	0.000
57	A	57	HIS	0	-0.044	-0.011	28.735	0.283	0.283	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.028	0.000	26.677	0.093	0.093	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.019	0.020	27.901	-0.192	-0.192	0.000	0.000	0.000	0.000
60	A	60	PHE	0	0.022	0.012	22.833	-0.044	-0.044	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.956	0.979	26.020	10.282	10.282	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.004	-0.007	22.260	0.041	0.041	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.872	-0.938	25.355	-10.697	-10.697	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.905	0.964	24.678	12.127	12.127	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.003	0.013	28.521	0.563	0.563	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.020	-0.005	31.175	-0.150	-0.150	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.051	-0.010	31.464	0.181	0.181	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.020	0.012	30.321	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.936	-0.970	26.793	-11.379	-11.379	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.039	0.011	22.251	0.358	0.358	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.027	-0.002	24.583	-0.353	-0.353	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.020	0.011	22.109	-0.083	-0.083	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.053	-0.026	25.429	0.321	0.321	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.001	-0.001	25.654	-0.238	-0.238	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.899	-0.976	28.231	-9.674	-9.674	0.000	0.000	0.000	0.000
76	A	76	PRO	0	-0.032	-0.004	30.755	-0.120	-0.120	0.000	0.000	0.000	0.000
77	A	77	CYS	0	0.029	0.027	31.985	0.409	0.409	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.824	-0.902	35.043	-7.651	-7.651	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.795	0.873	37.520	7.652	7.652	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.004	-0.015	32.173	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.833	-0.902	31.881	-9.172	-9.172	0.000	0.000	0.000	0.000
82	A	82	THR	0	0.035	0.021	28.060	-0.521	-0.521	0.000	0.000	0.000	0.000
83	A	83	TYR	0	-0.030	-0.016	28.215	0.418	0.418	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.042	0.024	26.110	-0.523	-0.523	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.055	-0.034	25.756	0.082	0.082	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.004	0.012	26.997	0.245	0.245	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.976	0.999	28.588	9.783	9.783	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.902	0.945	30.688	8.808	8.808	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.060	-0.032	29.195	0.076	0.076	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.012	-0.013	32.542	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	GLN	0	0.002	0.004	34.265	0.154	0.154	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.040	0.022	32.597	-0.294	-0.294	0.000	0.000	0.000	0.000
93	A	93	VAL	0	-0.006	0.003	29.763	0.171	0.171	0.000	0.000	0.000	0.000
94	A	94	GLN	0	0.015	0.001	28.379	-0.258	-0.258	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.025	0.010	23.428	0.031	0.031	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.921	0.948	23.973	12.075	12.075	0.000	0.000	0.000	0.000
97	A	97	SER	0	0.048	0.026	18.460	-0.611	-0.611	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.013	-0.004	18.335	0.364	0.364	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.043	-0.030	19.317	0.668	0.668	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.967	0.981	20.775	12.577	12.577	0.000	0.000	0.000	0.000
101	A	101	ILE	0	-0.010	-0.009	21.787	0.729	0.729	0.000	0.000	0.000	0.000
102	A	102	ILE	0	-0.020	-0.007	22.675	-0.538	-0.538	0.000	0.000	0.000	0.000
103	A	103	MET	0	0.019	0.010	23.004	0.341	0.341	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.012	0.003	26.524	-0.204	-0.204	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.909	0.954	28.060	10.643	10.643	0.000	0.000	0.000	0.000
106	A	106	ASN	0	0.005	-0.011	23.899	0.452	0.452	0.000	0.000	0.000	0.000
107	A	107	HIS	0	-0.006	0.017	21.966	-1.083	-1.083	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.000	-0.018	20.117	0.572	0.572	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.039	0.004	17.140	-0.840	-0.840	0.000	0.000	0.000	0.000
110	A	110	ARG	1	0.887	0.940	13.757	21.346	21.346	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.003	0.000	16.239	-1.042	-1.042	0.000	0.000	0.000	0.000
112	A	112	ASN	0	-0.005	0.001	11.659	1.509	1.509	0.000	0.000	0.000	0.000
113	A	113	HIS	0	0.003	-0.014	15.850	-0.648	-0.648	0.000	0.000	0.000	0.000
114	A	114	PRO	0	0.007	0.008	13.395	0.552	0.552	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.939	-0.976	16.025	-15.351	-15.351	0.000	0.000	0.000	0.000
116	A	116	GLN	0	0.048	0.014	18.586	0.338	0.338	0.000	0.000	0.000	0.000
117	A	117	ALA	0	0.001	-0.007	17.820	0.418	0.418	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.906	0.964	17.899	16.328	16.328	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.039	0.023	19.390	0.348	0.348	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.990	-0.994	21.114	-14.518	-14.518	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.898	0.940	22.362	13.440	13.440	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.917	-0.951	23.762	-12.843	-12.843	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.922	0.972	26.902	11.118	11.118	0.000	0.000	0.000	0.000
124	A	124	THR	0	-0.008	-0.022	29.026	-0.068	-0.068	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.025	0.013	29.700	-0.198	-0.198	0.000	0.000	0.000	0.000
126	A	126	GLY	0	-0.036	0.002	31.886	0.075	0.075	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.019	-0.005	35.160	0.161	0.161	0.000	0.000	0.000	0.000
128	A	128	SER	0	0.026	0.013	34.444	-0.245	-0.245	0.000	0.000	0.000	0.000
129	A	129	SER	0	-0.083	-0.066	32.745	0.108	0.108	0.000	0.000	0.000	0.000
130	A	130	GLY	-1	-0.917	-0.933	33.029	-9.499	-9.499	0.000	0.000	0.000	0.000

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