FMO DATABASE

FMODB ID: 9L5V2

Calculation Name: 2K1H-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2K1H

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-585850.26224
FMO2-HF: Nuclear repulsion	551200.881425
FMO2-HF: Total energy	-34649.380815
FMO2-MP2: Total energy	-34750.632399

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:MET)

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

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.
-215.397	-210.46	8.788	-6.444	-7.28	-0.059

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.800 / q_NPA : 0.900

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	ILE	0	-0.014	-0.008	3.478	-7.145	-5.162	-0.012	-1.021	-0.950	-0.002
4	A	4	ILE	0	-0.014	0.005	4.686	3.915	4.014	-0.001	-0.008	-0.089	0.000
19	A	19	LEU	0	-0.009	-0.013	2.436	-0.209	0.417	0.424	-0.358	-0.692	-0.004
20	A	20	SER	0	0.020	0.020	4.345	1.905	2.109	-0.001	-0.035	-0.167	0.000
21	A	21	GLU	-1	-0.910	-0.964	2.016	-108.774	-107.513	8.341	-4.952	-4.651	-0.051
22	A	22	PRO	0	0.021	0.017	3.124	10.969	11.458	0.039	-0.016	-0.512	-0.002
82	A	82	PHE	0	0.013	-0.006	4.685	-1.681	-1.506	-0.001	-0.044	-0.130	0.000
85	A	85	SER	0	-0.124	-0.072	4.105	-0.890	-0.790	-0.001	-0.010	-0.089	0.000
5	A	5	ALA	0	0.004	-0.005	7.593	4.178	4.178	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.018	0.009	9.936	-2.440	-2.440	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.047	-0.021	12.588	1.692	1.692	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.917	-0.960	15.184	-16.479	-16.479	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.051	-0.034	18.126	1.028	1.028	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.013	0.015	20.323	0.169	0.169	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.106	-0.059	21.279	-0.051	-0.051	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.029	0.023	23.432	-0.115	-0.115	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.036	0.006	20.830	-0.251	-0.251	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.010	0.017	17.861	-0.609	-0.609	0.000	0.000	0.000	0.000
15	A	15	MET	0	0.017	0.005	14.253	-0.083	-0.083	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.857	0.957	12.167	21.713	21.713	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.028	0.012	7.575	0.648	0.648	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.013	-0.012	8.519	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.991	0.980	5.736	27.145	27.145	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.100	-0.045	8.656	4.276	4.276	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.845	-0.918	8.849	-29.376	-29.376	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.019	0.008	10.058	-0.267	-0.267	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.038	-0.030	11.077	1.975	1.975	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.025	0.026	13.097	-1.070	-1.070	0.000	0.000	0.000	0.000
29	A	29	THR	0	-0.077	-0.057	14.252	1.230	1.230	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.008	0.027	14.428	-1.129	-1.129	0.000	0.000	0.000	0.000
31	A	31	TYR	0	0.002	-0.017	9.749	1.446	1.446	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.009	-0.012	15.467	-1.093	-1.093	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.025	0.012	16.306	1.119	1.119	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.002	0.027	16.242	-1.224	-1.224	0.000	0.000	0.000	0.000
35	A	35	GLN	0	-0.061	-0.040	16.229	1.119	1.119	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.898	-0.948	15.813	-16.550	-16.550	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.037	-0.015	14.797	0.373	0.373	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.027	-0.008	12.917	-1.099	-1.099	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.029	0.006	7.574	-0.119	-0.119	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.822	-0.915	9.585	-23.823	-23.823	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.008	-0.014	4.811	0.268	0.268	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.037	-0.004	8.436	0.424	0.424	0.000	0.000	0.000	0.000
43	A	43	ASN	0	0.042	0.009	11.032	2.163	2.163	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.861	0.920	12.604	23.382	23.382	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.017	-0.010	11.043	1.082	1.082	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.024	-0.009	14.675	1.166	1.166	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.962	-0.967	17.361	-14.765	-14.765	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.055	-0.028	18.014	0.597	0.597	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.923	-0.954	20.334	-12.190	-12.190	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.024	0.010	21.940	-0.292	-0.292	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.035	-0.016	16.175	-0.127	-0.127	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.841	0.912	19.413	13.154	13.154	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.029	-0.013	17.705	0.139	0.139	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.018	0.010	10.973	-0.409	-0.409	0.000	0.000	0.000	0.000
55	A	55	PHE	0	-0.019	-0.007	13.176	0.582	0.582	0.000	0.000	0.000	0.000
56	A	56	TYR	0	-0.022	-0.013	5.841	-2.565	-2.565	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.006	-0.021	9.893	2.801	2.801	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.035	-0.012	10.057	0.395	0.395	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.904	-0.941	6.625	-38.412	-38.412	0.000	0.000	0.000	0.000
60	A	60	PHE	0	-0.014	-0.037	7.630	1.138	1.138	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.046	0.041	6.573	1.443	1.443	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.006	-0.007	9.420	1.186	1.186	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.036	-0.025	10.445	-0.121	-0.121	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.901	-0.933	14.446	-15.934	-15.934	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.833	0.914	14.574	20.115	20.115	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.859	-0.922	20.151	-11.918	-11.918	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.894	-0.956	23.308	-12.464	-12.464	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.025	-0.013	25.648	0.309	0.309	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.008	0.011	20.434	-0.050	-0.050	0.000	0.000	0.000	0.000
70	A	70	ASN	0	0.018	-0.014	21.252	-0.049	-0.049	0.000	0.000	0.000	0.000
71	A	71	TRP	0	0.075	0.010	12.470	-0.949	-0.949	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.010	-0.009	17.447	-1.239	-1.239	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.872	-0.927	19.796	-14.122	-14.122	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.032	-0.019	14.913	-0.591	-0.591	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.017	-0.001	14.310	-1.460	-1.460	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.066	0.033	14.355	-1.456	-1.456	0.000	0.000	0.000	0.000
77	A	77	GLN	0	-0.032	-0.010	15.713	-0.905	-0.905	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.024	-0.024	9.981	-0.905	-0.905	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.942	-0.957	10.790	-23.934	-23.934	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.044	-0.021	11.376	-0.704	-0.704	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.011	-0.008	8.423	1.318	1.318	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.060	0.031	7.326	-0.842	-0.842	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.871	0.951	9.615	23.291	23.291	0.000	0.000	0.000	0.000
86	A	86	ASN	-1	-0.976	-0.985	5.335	-24.359	-24.359	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:MET)