FMO DATABASE

FMODB ID: 7Y88K

Calculation Name: 2LBB-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2LBB

Chain ID: A

ChEMBL ID:

UniProt ID: A7AV23

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	88
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-607871.829847
FMO2-HF: Nuclear repulsion	571282.325129
FMO2-HF: Total energy	-36589.504718
FMO2-MP2: Total energy	-36691.808359

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.
-59.206	-53.252	1.587	-2.653	-4.888	-0.009

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 : 0.875 / q_NPA : 0.926

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].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	ALA	0	0.035	0.014	2.654	6.287	10.236	1.146	-1.999	-3.096	-0.004
4	A	4	ASP	-1	-0.893	-0.948	2.565	-37.096	-35.293	0.440	-0.596	-1.647	-0.005
5	A	5	ASP	-1	-0.875	-0.935	4.106	-50.466	-50.264	0.001	-0.058	-0.145	0.000
6	A	6	PHE	0	0.004	-0.022	6.430	5.660	5.660	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.872	-0.926	8.420	-21.131	-21.131	0.000	0.000	0.000	0.000
8	A	8	ALA	0	-0.007	-0.006	10.112	2.434	2.434	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.019	0.009	10.543	2.007	2.007	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.028	-0.025	12.363	2.095	2.095	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.930	0.962	14.231	18.251	18.251	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.039	0.021	15.355	1.447	1.447	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.016	-0.016	16.293	1.017	1.017	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.075	-0.031	18.254	1.158	1.158	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.040	-0.017	19.914	0.925	0.925	0.000	0.000	0.000	0.000
16	A	16	THR	0	-0.021	-0.002	20.856	0.990	0.990	0.000	0.000	0.000	0.000
17	A	17	THR	0	0.004	-0.010	21.715	-0.241	-0.241	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.045	-0.026	24.198	0.312	0.312	0.000	0.000	0.000	0.000
19	A	19	MET	0	-0.030	0.018	19.894	0.063	0.063	0.000	0.000	0.000	0.000
20	A	20	MET	0	0.003	-0.006	24.351	0.368	0.368	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.034	0.021	23.638	-0.589	-0.589	0.000	0.000	0.000	0.000
22	A	22	SER	0	0.024	0.022	24.358	0.786	0.786	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.045	-0.044	25.615	-0.222	-0.222	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.891	-0.947	24.604	-11.659	-11.659	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.781	-0.891	20.973	-14.356	-14.356	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.925	0.949	20.854	11.919	11.919	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.071	-0.020	22.723	0.078	0.078	0.000	0.000	0.000	0.000
28	A	28	CYS	0	-0.051	-0.045	18.036	-0.238	-0.238	0.000	0.000	0.000	0.000
29	A	29	PHE	0	0.063	0.034	16.569	-0.458	-0.458	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.063	-0.032	17.176	-0.292	-0.292	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.928	0.981	17.872	15.310	15.310	0.000	0.000	0.000	0.000
32	A	32	TYR	0	0.052	0.021	13.607	0.063	0.063	0.000	0.000	0.000	0.000
33	A	33	TYR	0	0.049	0.030	14.496	-0.383	-0.383	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.882	0.966	15.934	13.557	13.557	0.000	0.000	0.000	0.000
35	A	35	GLN	0	0.022	-0.011	14.830	0.102	0.102	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.033	-0.010	11.578	-0.466	-0.466	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.069	-0.045	12.772	-0.924	-0.924	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.067	-0.029	15.572	0.576	0.576	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.075	0.061	16.230	0.160	0.160	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.892	-0.943	17.117	-12.470	-12.470	0.000	0.000	0.000	0.000
41	A	41	CYS	0	-0.069	0.001	20.764	0.100	0.100	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.009	-0.024	24.040	0.166	0.166	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.910	0.952	26.751	10.813	10.813	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.050	0.029	29.172	-0.040	-0.040	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.894	0.956	31.926	8.661	8.661	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.039	-0.006	31.346	0.196	0.196	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.046	0.027	34.046	0.191	0.191	0.000	0.000	0.000	0.000
48	A	48	MET	0	-0.007	-0.026	36.783	-0.203	-0.203	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.004	0.010	38.702	0.135	0.135	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.039	-0.013	33.867	-0.065	-0.065	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.024	0.001	34.765	-0.051	-0.051	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.082	0.015	30.199	-0.056	-0.056	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.808	-0.901	29.760	-9.149	-9.149	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.934	0.979	30.330	8.603	8.603	0.000	0.000	0.000	0.000
55	A	55	TYR	0	0.096	0.040	27.675	-0.172	-0.172	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.967	0.986	25.669	10.725	10.725	0.000	0.000	0.000	0.000
57	A	57	TRP	0	-0.005	-0.005	25.361	-0.430	-0.430	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.897	-0.954	26.286	-10.449	-10.449	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.015	-0.008	22.379	-0.331	-0.331	0.000	0.000	0.000	0.000
60	A	60	TRP	0	-0.017	-0.018	20.715	-0.198	-0.198	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.020	-0.003	21.786	-0.455	-0.455	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.006	-0.010	22.632	-0.075	-0.075	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.043	-0.013	16.593	-0.385	-0.385	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.912	0.954	18.390	10.772	10.772	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.038	0.007	18.953	0.224	0.224	0.000	0.000	0.000	0.000
66	A	66	MET	0	-0.047	-0.001	13.228	-0.615	-0.615	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.032	0.009	11.249	0.274	0.274	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.029	-0.003	9.731	-0.386	-0.386	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.893	-0.948	5.259	-32.007	-32.007	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.023	0.008	7.317	-1.406	-1.406	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.011	0.005	9.264	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.850	0.951	6.979	25.937	25.937	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.923	-0.970	4.810	-39.445	-39.445	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.044	-0.015	7.269	0.640	0.640	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.017	-0.021	10.626	1.595	1.595	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.003	0.006	6.746	1.199	1.199	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.928	0.959	7.037	34.384	34.384	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.031	-0.004	11.051	1.510	1.510	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.007	0.006	13.289	1.399	1.399	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.833	-0.924	13.404	-20.971	-20.971	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.010	-0.009	15.312	0.952	0.952	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.119	-0.039	17.855	0.935	0.935	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.044	-0.006	17.965	0.952	0.952	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.049	0.039	15.484	-0.986	-0.986	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.028	-0.017	15.126	-0.899	-0.899	0.000	0.000	0.000	0.000
86	A	86	TRP	0	-0.066	-0.028	9.149	-0.593	-0.593	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.788	0.902	10.349	24.329	24.329	0.000	0.000	0.000	0.000
88	A	88	ASN	-1	-0.943	-0.954	11.772	-19.105	-19.105	0.000	0.000	0.000	0.000

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