FMO DATABASE

FMODB ID: 4GZ8N

Calculation Name: 1K8H-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1K8H

Chain ID: A

ChEMBL ID:

UniProt ID: O66640

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1167857.258273
FMO2-HF: Nuclear repulsion	1115084.908369
FMO2-HF: Total energy	-52772.349904
FMO2-MP2: Total energy	-52930.650519

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.
132.853	134.395	-0.016	-0.678	-0.849	-0.003

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 : 0.861 / q_NPA : 0.918

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	0.061	0.032	3.843	7.249	8.638	-0.015	-0.636	-0.738	-0.003
4	A	4	ASP	-1	-0.837	-0.926	4.341	-40.963	-40.810	-0.001	-0.042	-0.111	0.000
5	A	5	LYS	1	0.897	0.937	6.801	23.872	23.872	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.036	-0.002	6.377	3.608	3.608	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.033	-0.015	6.405	-4.388	-4.388	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.023	-0.013	6.689	3.158	3.158	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.034	-0.001	9.684	0.223	0.223	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.022	0.028	13.231	0.592	0.592	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.890	-0.957	14.679	-22.484	-22.484	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.011	-0.001	16.564	1.623	1.623	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.942	0.953	17.946	15.240	15.240	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.881	-0.942	20.668	-12.147	-12.147	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.000	0.012	23.994	0.503	0.503	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.964	0.977	22.026	13.425	13.425	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.003	0.018	25.093	0.187	0.187	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.967	0.979	26.754	10.757	10.757	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.041	-0.023	28.736	0.376	0.376	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.907	-0.933	28.572	-10.669	-10.669	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.048	-0.046	24.439	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.027	0.005	28.456	0.048	0.048	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.887	-0.951	28.874	-9.678	-9.678	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.069	-0.045	23.515	-0.129	-0.129	0.000	0.000	0.000	0.000
25	A	25	TYR	0	0.017	0.004	25.175	0.275	0.275	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.971	-0.975	22.184	-13.473	-13.473	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.080	0.031	22.145	0.601	0.601	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.014	0.007	21.448	-0.878	-0.878	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.012	-0.001	19.430	0.606	0.606	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.014	0.004	20.929	-0.621	-0.621	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.014	-0.017	20.325	0.610	0.610	0.000	0.000	0.000	0.000
32	A	32	LYS	1	1.023	1.010	22.978	10.845	10.845	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.077	0.030	20.556	-0.450	-0.450	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.032	0.018	20.156	-0.716	-0.716	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.853	-0.902	21.204	-13.171	-13.171	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.002	-0.005	16.270	-0.489	-0.489	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.924	0.942	16.129	16.807	16.807	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.015	0.011	16.909	-0.892	-0.892	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.046	0.017	16.877	-0.198	-0.198	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.888	0.966	10.749	25.542	25.542	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.906	-0.957	12.320	-19.271	-19.271	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.886	0.958	13.851	15.230	15.230	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.001	0.016	12.686	-0.909	-0.909	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.028	0.001	13.643	0.275	0.275	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.037	-0.040	16.659	0.462	0.462	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.027	-0.023	19.362	0.275	0.275	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.003	0.007	17.193	-0.405	-0.405	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.914	0.942	21.779	11.906	11.906	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.820	-0.893	25.154	-10.628	-10.628	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.063	-0.016	23.507	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	PHE	0	0.016	-0.008	25.784	-0.179	-0.179	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.028	-0.024	24.993	-0.195	-0.195	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.880	0.944	28.132	9.280	9.280	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.006	-0.009	30.250	-0.308	-0.308	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.775	-0.895	32.709	-8.434	-8.434	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.067	-0.030	34.642	-0.027	-0.027	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.073	0.043	35.255	0.121	0.121	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.962	-0.987	29.973	-9.698	-9.698	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.023	0.015	27.253	0.146	0.146	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.002	-0.016	28.460	-0.145	-0.145	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.005	0.001	21.943	-0.085	-0.085	0.000	0.000	0.000	0.000
62	A	62	TYR	0	0.010	-0.015	26.552	0.347	0.347	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.012	-0.013	23.041	-0.184	-0.184	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.038	0.027	26.576	0.079	0.079	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.045	0.031	23.359	-0.104	-0.104	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.047	-0.013	22.605	-0.715	-0.715	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.067	0.040	20.623	0.262	0.262	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.059	-0.033	19.298	0.159	0.159	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.074	0.038	21.776	0.467	0.467	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.776	0.846	22.841	12.478	12.478	0.000	0.000	0.000	0.000
71	A	71	HIS	0	-0.043	-0.016	25.965	0.395	0.395	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.028	0.019	29.737	-0.179	-0.179	0.000	0.000	0.000	0.000
73	A	73	THR	0	0.056	0.027	32.009	0.117	0.117	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.007	-0.004	34.869	-0.215	-0.215	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.911	-0.947	36.396	-7.814	-7.814	0.000	0.000	0.000	0.000
76	A	76	ASN	0	-0.127	-0.068	33.005	-0.324	-0.324	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.040	0.022	34.072	0.087	0.087	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.851	-0.919	33.190	-9.087	-9.087	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.017	-0.006	29.190	-0.287	-0.287	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.009	-0.004	29.812	-0.203	-0.203	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.931	0.943	25.223	11.018	11.018	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.942	1.006	26.636	9.174	9.174	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.859	0.928	23.864	11.958	11.958	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.988	1.004	27.047	10.240	10.240	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.024	-0.036	23.654	-0.476	-0.476	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.025	0.010	25.785	0.342	0.342	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.010	0.000	26.390	-0.374	-0.374	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.074	0.043	28.685	0.302	0.302	0.000	0.000	0.000	0.000
89	A	89	LYS	1	1.007	0.988	31.315	8.394	8.394	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.952	0.988	35.166	8.563	8.563	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.878	-0.953	31.619	-9.285	-9.285	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.002	0.012	31.511	-0.029	-0.029	0.000	0.000	0.000	0.000
93	A	93	MET	0	0.048	0.032	33.891	0.099	0.099	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.958	0.971	36.346	8.630	8.630	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.023	-0.005	31.015	0.099	0.099	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.035	-0.010	35.208	0.103	0.103	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.053	0.026	36.839	0.098	0.098	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.927	0.961	37.903	7.748	7.748	0.000	0.000	0.000	0.000
99	A	99	VAL	0	-0.024	-0.025	33.220	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	100	GLN	0	-0.011	-0.004	36.325	0.165	0.165	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.933	-0.955	38.277	-7.169	-7.169	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.894	0.947	39.507	7.729	7.729	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.030	0.037	39.311	0.077	0.077	0.000	0.000	0.000	0.000
104	A	104	TYR	0	-0.066	-0.039	32.137	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.033	-0.022	31.979	0.106	0.106	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.011	-0.004	27.888	-0.207	-0.207	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.021	-0.004	24.561	0.036	0.036	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.005	0.011	21.626	-0.213	-0.213	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.038	-0.020	18.800	-0.150	-0.150	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.929	0.964	12.217	21.569	21.569	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.022	-0.015	15.575	0.860	0.860	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.057	0.033	10.565	-0.948	-0.948	0.000	0.000	0.000	0.000
113	A	113	TRP	0	0.026	0.016	11.653	2.222	2.222	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.963	0.986	11.263	19.112	19.112	0.000	0.000	0.000	0.000
115	A	115	ASN	0	-0.004	-0.016	12.399	1.653	1.653	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.006	-0.002	14.367	-0.321	-0.321	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.875	0.928	16.152	16.258	16.258	0.000	0.000	0.000	0.000
118	A	118	VAL	0	0.061	0.024	15.741	-0.891	-0.891	0.000	0.000	0.000	0.000
119	A	119	LYS	0	-0.028	0.014	14.990	1.386	1.386	0.000	0.000	0.000	0.000
120	A	120	VAL	0	0.007	-0.008	17.031	-1.091	-1.091	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.002	0.019	18.426	0.436	0.436	0.000	0.000	0.000	0.000
122	A	122	ILE	0	-0.016	-0.015	20.263	-0.198	-0.198	0.000	0.000	0.000	0.000
123	A	123	ALA	0	0.017	0.002	23.605	0.031	0.031	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.002	0.011	25.641	0.190	0.190	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.021	0.003	28.106	-0.069	-0.069	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.951	1.000	30.225	8.675	8.675	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.003	-0.010	33.004	-0.179	-0.179	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.953	0.980	33.429	9.233	9.233	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.942	0.960	34.853	8.485	8.485	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.008	0.001	34.373	-0.138	-0.138	0.000	0.000	0.000	0.000
131	A	131	TYR	0	0.014	0.001	36.066	0.236	0.236	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.966	-0.975	37.085	-8.088	-8.088	0.000	0.000	0.000	0.000
133	A	133	ARG	0	0.064	0.048	36.603	-0.013	-0.013	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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