FMO DATABASE

FMODB ID: Z7M8N

Calculation Name: 2K8E-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2K8E

Chain ID: A

ChEMBL ID:

UniProt ID: P76402

Base Structure: SolutionNMR

Registration Date: 2025-10-04

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-880291.969958
FMO2-HF: Nuclear repulsion	836310.040698
FMO2-HF: Total energy	-43981.92926
FMO2-MP2: Total energy	-44110.970113

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:14:GLY)

Summations of interaction energy for fragment #1(A:14: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.
33.371	34.052	-0.003	-0.288	-0.39	-0.001

Interaction energy analysis for fragmet #1(A:14:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.864 / q_NPA : 0.920

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	16	ILE	0	0.039	0.020	3.836	-3.103	-2.422	-0.003	-0.288	-0.390	-0.001
4	A	17	MET	0	-0.011	-0.008	5.674	2.214	2.214	0.000	0.000	0.000	0.000
5	A	18	ALA	0	0.008	0.010	8.633	1.343	1.343	0.000	0.000	0.000	0.000
6	A	19	GLY	0	0.061	0.034	12.415	1.341	1.341	0.000	0.000	0.000	0.000
7	A	20	TRP	0	-0.120	-0.075	12.459	-2.287	-2.287	0.000	0.000	0.000	0.000
8	A	21	PHE	0	0.056	0.022	14.605	1.444	1.444	0.000	0.000	0.000	0.000
9	A	22	GLU	-1	-0.822	-0.891	16.961	-16.061	-16.061	0.000	0.000	0.000	0.000
10	A	23	LEU	0	-0.006	-0.002	19.675	0.737	0.737	0.000	0.000	0.000	0.000
11	A	24	SER	0	0.020	-0.014	22.173	0.041	0.041	0.000	0.000	0.000	0.000
12	A	25	LYS	1	0.840	0.925	25.273	9.939	9.939	0.000	0.000	0.000	0.000
13	A	26	SER	0	-0.006	-0.007	28.873	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	27	SER	0	0.015	-0.002	31.599	0.056	0.056	0.000	0.000	0.000	0.000
15	A	28	ASP	-1	-0.842	-0.906	34.917	-8.130	-8.130	0.000	0.000	0.000	0.000
16	A	29	ASN	0	0.003	-0.001	32.931	-0.195	-0.195	0.000	0.000	0.000	0.000
17	A	30	GLN	0	-0.005	0.003	32.098	-0.446	-0.446	0.000	0.000	0.000	0.000
18	A	31	PHE	0	0.026	-0.004	27.141	-0.287	-0.287	0.000	0.000	0.000	0.000
19	A	32	ARG	1	0.933	0.978	27.020	10.593	10.593	0.000	0.000	0.000	0.000
20	A	33	PHE	0	0.002	0.007	21.731	-0.313	-0.313	0.000	0.000	0.000	0.000
21	A	34	VAL	0	0.017	0.023	21.683	0.502	0.502	0.000	0.000	0.000	0.000
22	A	35	LEU	0	-0.021	-0.009	17.526	-0.638	-0.638	0.000	0.000	0.000	0.000
23	A	36	LYS	1	0.827	0.907	18.016	15.326	15.326	0.000	0.000	0.000	0.000
24	A	37	ALA	0	0.057	0.027	17.117	-1.059	-1.059	0.000	0.000	0.000	0.000
25	A	38	GLY	0	0.002	-0.013	14.648	-0.160	-0.160	0.000	0.000	0.000	0.000
26	A	39	ASN	0	-0.032	-0.021	15.466	-1.162	-1.162	0.000	0.000	0.000	0.000
27	A	40	GLY	0	-0.005	0.003	17.921	0.610	0.610	0.000	0.000	0.000	0.000
28	A	41	GLU	-1	-0.892	-0.942	19.429	-13.194	-13.194	0.000	0.000	0.000	0.000
29	A	42	THR	0	-0.014	-0.007	21.406	-0.461	-0.461	0.000	0.000	0.000	0.000
30	A	43	ILE	0	0.002	0.009	20.235	0.627	0.627	0.000	0.000	0.000	0.000
31	A	44	LEU	0	-0.064	-0.016	23.477	0.461	0.461	0.000	0.000	0.000	0.000
32	A	45	THR	0	0.002	-0.007	24.258	-0.587	-0.587	0.000	0.000	0.000	0.000
33	A	46	SER	0	-0.050	-0.016	25.783	0.374	0.374	0.000	0.000	0.000	0.000
34	A	47	GLU	-1	-0.834	-0.921	27.665	-9.507	-9.507	0.000	0.000	0.000	0.000
35	A	48	LEU	0	-0.046	-0.024	30.057	-0.284	-0.284	0.000	0.000	0.000	0.000
36	A	49	TYR	0	0.031	0.012	27.521	0.116	0.116	0.000	0.000	0.000	0.000
37	A	50	THR	0	0.035	0.015	31.814	-0.123	-0.123	0.000	0.000	0.000	0.000
38	A	51	SER	0	-0.039	-0.032	31.383	0.097	0.097	0.000	0.000	0.000	0.000
39	A	52	LYS	1	0.967	0.995	25.871	10.333	10.333	0.000	0.000	0.000	0.000
40	A	53	THR	0	0.048	0.030	26.401	-0.299	-0.299	0.000	0.000	0.000	0.000
41	A	54	SER	0	-0.038	-0.019	27.994	0.023	0.023	0.000	0.000	0.000	0.000
42	A	55	ALA	0	0.024	0.021	25.345	-0.114	-0.114	0.000	0.000	0.000	0.000
43	A	56	GLU	-1	-0.905	-0.958	22.811	-12.973	-12.973	0.000	0.000	0.000	0.000
44	A	57	LYS	1	0.935	0.965	23.592	11.296	11.296	0.000	0.000	0.000	0.000
45	A	58	GLY	0	0.059	0.045	26.155	0.029	0.029	0.000	0.000	0.000	0.000
46	A	59	ILE	0	0.007	0.004	17.914	-0.106	-0.106	0.000	0.000	0.000	0.000
47	A	60	ALA	0	0.002	-0.003	21.508	-0.407	-0.407	0.000	0.000	0.000	0.000
48	A	61	SER	0	-0.035	-0.025	22.513	0.048	0.048	0.000	0.000	0.000	0.000
49	A	62	VAL	0	-0.005	-0.005	21.320	0.105	0.105	0.000	0.000	0.000	0.000
50	A	63	ARG	1	0.839	0.918	13.479	19.816	19.816	0.000	0.000	0.000	0.000
51	A	64	SER	0	-0.049	-0.017	20.586	-0.234	-0.234	0.000	0.000	0.000	0.000
52	A	65	ASN	0	-0.034	-0.056	23.284	0.459	0.459	0.000	0.000	0.000	0.000
53	A	66	SER	0	-0.009	0.031	20.632	0.161	0.161	0.000	0.000	0.000	0.000
54	A	67	PRO	0	0.039	0.007	21.600	0.233	0.233	0.000	0.000	0.000	0.000
55	A	68	GLN	0	0.003	0.019	23.989	0.703	0.703	0.000	0.000	0.000	0.000
56	A	69	GLU	-1	-0.859	-0.943	27.551	-10.694	-10.694	0.000	0.000	0.000	0.000
57	A	70	GLU	-1	-0.858	-0.915	29.142	-8.894	-8.894	0.000	0.000	0.000	0.000
58	A	71	ARG	1	0.835	0.912	29.712	9.630	9.630	0.000	0.000	0.000	0.000
59	A	72	TYR	0	0.008	-0.007	24.377	0.079	0.079	0.000	0.000	0.000	0.000
60	A	73	GLU	-1	-0.819	-0.898	31.125	-8.568	-8.568	0.000	0.000	0.000	0.000
61	A	74	LYS	1	0.811	0.892	33.034	9.494	9.494	0.000	0.000	0.000	0.000
62	A	75	LYS	1	0.917	0.963	34.699	8.425	8.425	0.000	0.000	0.000	0.000
63	A	76	THR	0	0.034	0.003	36.898	-0.257	-0.257	0.000	0.000	0.000	0.000
64	A	77	ALA	0	-0.022	0.007	39.462	0.168	0.168	0.000	0.000	0.000	0.000
65	A	78	SER	0	0.055	0.001	41.146	-0.051	-0.051	0.000	0.000	0.000	0.000
66	A	79	ASN	0	-0.008	0.009	41.295	0.088	0.088	0.000	0.000	0.000	0.000
67	A	80	GLY	0	0.051	0.034	42.298	-0.056	-0.056	0.000	0.000	0.000	0.000
68	A	81	LYS	1	0.861	0.937	37.102	7.865	7.865	0.000	0.000	0.000	0.000
69	A	82	PHE	0	0.034	0.013	35.329	0.113	0.113	0.000	0.000	0.000	0.000
70	A	83	TYR	0	0.008	-0.001	32.857	-0.218	-0.218	0.000	0.000	0.000	0.000
71	A	84	PHE	0	0.029	0.003	26.503	0.212	0.212	0.000	0.000	0.000	0.000
72	A	85	ASN	0	0.024	0.012	31.025	-0.273	-0.273	0.000	0.000	0.000	0.000
73	A	86	LEU	0	0.006	0.019	25.702	0.201	0.201	0.000	0.000	0.000	0.000
74	A	87	LYS	1	0.858	0.931	29.804	8.724	8.724	0.000	0.000	0.000	0.000
75	A	88	ALA	0	0.038	0.018	30.493	-0.280	-0.280	0.000	0.000	0.000	0.000
76	A	89	ALA	0	0.034	0.006	31.614	0.278	0.278	0.000	0.000	0.000	0.000
77	A	90	ASN	0	-0.030	-0.018	33.148	0.055	0.055	0.000	0.000	0.000	0.000
78	A	91	HIS	0	0.030	0.012	35.695	0.102	0.102	0.000	0.000	0.000	0.000
79	A	92	GLN	0	-0.024	-0.007	33.007	-0.029	-0.029	0.000	0.000	0.000	0.000
80	A	93	ILE	0	-0.018	-0.002	30.967	-0.163	-0.163	0.000	0.000	0.000	0.000
81	A	94	ILE	0	-0.013	-0.017	26.817	-0.060	-0.060	0.000	0.000	0.000	0.000
82	A	95	GLY	0	0.021	-0.011	26.640	-0.521	-0.521	0.000	0.000	0.000	0.000
83	A	96	SER	0	-0.020	-0.002	27.883	0.106	0.106	0.000	0.000	0.000	0.000
84	A	97	SER	0	-0.024	-0.008	27.236	-0.358	-0.358	0.000	0.000	0.000	0.000
85	A	98	GLN	0	0.009	0.009	26.461	0.602	0.602	0.000	0.000	0.000	0.000
86	A	99	MET	0	-0.040	-0.020	30.648	0.059	0.059	0.000	0.000	0.000	0.000
87	A	100	TYR	0	0.050	0.023	27.555	0.037	0.037	0.000	0.000	0.000	0.000
88	A	101	ALA	0	0.006	-0.004	33.488	0.289	0.289	0.000	0.000	0.000	0.000
89	A	102	THR	0	0.028	0.007	34.659	0.147	0.147	0.000	0.000	0.000	0.000
90	A	103	ALA	0	0.046	0.024	34.300	-0.264	-0.264	0.000	0.000	0.000	0.000
91	A	104	GLN	0	0.059	0.026	32.756	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	105	SER	0	0.014	0.025	30.091	-0.419	-0.419	0.000	0.000	0.000	0.000
93	A	106	ARG	1	0.789	0.893	29.363	8.818	8.818	0.000	0.000	0.000	0.000
94	A	107	GLU	-1	-0.824	-0.907	29.470	-10.044	-10.044	0.000	0.000	0.000	0.000
95	A	108	THR	0	-0.004	-0.015	25.580	-0.454	-0.454	0.000	0.000	0.000	0.000
96	A	109	GLY	0	0.029	0.016	25.165	-0.619	-0.619	0.000	0.000	0.000	0.000
97	A	110	ILE	0	-0.030	-0.015	24.956	-0.491	-0.491	0.000	0.000	0.000	0.000
98	A	111	ALA	0	0.008	0.003	24.030	-0.471	-0.471	0.000	0.000	0.000	0.000
99	A	112	SER	0	0.035	0.015	20.995	-1.067	-1.067	0.000	0.000	0.000	0.000
100	A	113	VAL	0	-0.007	-0.005	20.115	-0.899	-0.899	0.000	0.000	0.000	0.000
101	A	114	LYS	1	0.870	0.943	20.894	11.914	11.914	0.000	0.000	0.000	0.000
102	A	115	ALA	0	0.006	0.014	17.569	-0.596	-0.596	0.000	0.000	0.000	0.000
103	A	116	ASN	0	-0.007	-0.033	15.674	-1.979	-1.979	0.000	0.000	0.000	0.000
104	A	117	GLY	0	0.001	0.009	16.182	-0.602	-0.602	0.000	0.000	0.000	0.000
105	A	118	THR	0	-0.005	-0.006	15.265	-0.331	-0.331	0.000	0.000	0.000	0.000
106	A	119	SER	0	0.007	0.012	12.210	-1.406	-1.406	0.000	0.000	0.000	0.000
107	A	120	GLN	0	0.020	-0.007	12.777	1.052	1.052	0.000	0.000	0.000	0.000
108	A	121	THR	0	-0.020	-0.006	9.609	0.392	0.392	0.000	0.000	0.000	0.000
109	A	122	VAL	0	-0.021	-0.010	12.558	0.683	0.683	0.000	0.000	0.000	0.000
110	A	123	LYS	1	0.928	0.977	13.172	20.055	20.055	0.000	0.000	0.000	0.000
111	A	124	ASP	-1	-0.913	-0.954	16.803	-15.103	-15.103	0.000	0.000	0.000	0.000
112	A	125	ASN	0	0.029	0.025	19.995	0.503	0.503	0.000	0.000	0.000	0.000
113	A	126	THR	0	-0.066	-0.036	22.752	0.538	0.538	0.000	0.000	0.000	0.000
114	A	127	GLY	0	0.029	0.009	24.683	-0.313	-0.313	0.000	0.000	0.000	0.000
115	A	128	SER	0	-0.033	0.000	27.340	0.296	0.296	0.000	0.000	0.000	0.000
116	A	129	ASN	-1	-0.921	-0.961	29.281	-8.954	-8.954	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:GLY)