FMO DATABASE

FMODB ID: 1V4VZ

Calculation Name: 6TBM-P-Other547

Preferred Name:

Target Type:

Ligand Name: amino-acetaldehyde

Ligand 3-letter code: GLZ

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6TBM

Chain ID: P

ChEMBL ID:

UniProt ID: C4R2D9

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-584823.221184
FMO2-HF: Nuclear repulsion	548840.006402
FMO2-HF: Total energy	-35983.214782
FMO2-MP2: Total energy	-36090.155345

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:6:VAL)

Summations of interaction energy for fragment #1(A:6:VAL)

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.
-57.937	-53.652	2.008	-2.337	-3.955	-0.015

Interaction energy analysis for fragmet #1(A:6:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.869 / q_NPA : 0.919

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	8	HIS	0	0.050	0.032	2.087	3.478	7.328	2.006	-2.281	-3.574	-0.015
4	A	9	LEU	0	0.035	0.039	3.715	5.089	5.524	0.002	-0.056	-0.381	0.000
5	A	10	LYS	1	0.963	0.985	5.676	30.488	30.488	0.000	0.000	0.000	0.000
6	A	11	GLN	0	-0.049	-0.028	7.264	2.591	2.591	0.000	0.000	0.000	0.000
7	A	12	GLN	0	0.029	0.004	5.804	-2.861	-2.861	0.000	0.000	0.000	0.000
8	A	13	ILE	0	0.024	0.021	9.031	2.405	2.405	0.000	0.000	0.000	0.000
9	A	14	GLN	0	-0.027	-0.024	11.371	0.981	0.981	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.817	-0.901	10.727	-22.759	-22.759	0.000	0.000	0.000	0.000
11	A	16	VAL	0	0.046	0.027	13.032	1.573	1.573	0.000	0.000	0.000	0.000
12	A	17	LEU	0	-0.007	0.014	15.160	1.527	1.527	0.000	0.000	0.000	0.000
13	A	18	VAL	0	-0.031	-0.014	16.765	1.207	1.207	0.000	0.000	0.000	0.000
14	A	19	GLU	-1	-0.957	-0.975	16.829	-16.413	-16.413	0.000	0.000	0.000	0.000
15	A	20	SER	0	-0.071	-0.051	18.939	0.883	0.883	0.000	0.000	0.000	0.000
16	A	21	GLY	0	0.017	0.008	21.158	0.614	0.614	0.000	0.000	0.000	0.000
17	A	22	LYS	1	0.845	0.915	20.484	13.165	13.165	0.000	0.000	0.000	0.000
18	A	23	TYR	0	0.012	0.000	17.346	-0.128	-0.128	0.000	0.000	0.000	0.000
19	A	24	ASP	-1	-0.871	-0.933	20.885	-12.506	-12.506	0.000	0.000	0.000	0.000
20	A	25	GLU	-1	-0.877	-0.941	24.517	-11.632	-11.632	0.000	0.000	0.000	0.000
21	A	26	LEU	0	-0.026	0.002	20.220	0.451	0.451	0.000	0.000	0.000	0.000
22	A	27	SER	0	0.009	0.007	23.160	0.540	0.540	0.000	0.000	0.000	0.000
23	A	28	ASN	0	0.019	-0.008	24.771	0.625	0.625	0.000	0.000	0.000	0.000
24	A	29	PHE	0	-0.021	0.017	27.469	0.513	0.513	0.000	0.000	0.000	0.000
25	A	30	LEU	0	0.063	0.026	24.218	0.378	0.378	0.000	0.000	0.000	0.000
26	A	31	ARG	1	0.933	0.971	27.836	10.480	10.480	0.000	0.000	0.000	0.000
27	A	32	SER	0	-0.032	-0.039	29.716	0.456	0.456	0.000	0.000	0.000	0.000
28	A	33	LYS	1	0.805	0.908	30.660	10.218	10.218	0.000	0.000	0.000	0.000
29	A	34	LEU	0	0.027	0.003	27.846	0.272	0.272	0.000	0.000	0.000	0.000
30	A	35	TYR	0	-0.027	-0.010	32.370	0.254	0.254	0.000	0.000	0.000	0.000
31	A	36	GLN	0	-0.052	-0.042	35.163	0.427	0.427	0.000	0.000	0.000	0.000
32	A	37	VAL	0	-0.049	-0.009	34.169	0.198	0.198	0.000	0.000	0.000	0.000
33	A	38	GLY	0	0.029	0.021	37.260	0.078	0.078	0.000	0.000	0.000	0.000
34	A	39	TRP	0	-0.009	-0.006	28.333	0.079	0.079	0.000	0.000	0.000	0.000
35	A	40	THR	0	-0.004	-0.017	33.391	-0.131	-0.131	0.000	0.000	0.000	0.000
36	A	41	ASP	-1	-0.865	-0.935	34.429	-8.289	-8.289	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.801	-0.850	36.363	-8.149	-8.149	0.000	0.000	0.000	0.000
38	A	43	ILE	0	0.009	-0.002	30.849	0.051	0.051	0.000	0.000	0.000	0.000
39	A	44	ASN	0	-0.043	0.002	34.704	-0.134	-0.134	0.000	0.000	0.000	0.000
40	A	45	ARG	1	0.826	0.876	37.087	8.020	8.020	0.000	0.000	0.000	0.000
41	A	46	LEU	0	-0.013	-0.007	34.078	0.146	0.146	0.000	0.000	0.000	0.000
42	A	47	THR	0	0.017	-0.021	34.537	-0.066	-0.066	0.000	0.000	0.000	0.000
43	A	48	GLN	0	-0.015	-0.009	36.540	0.144	0.144	0.000	0.000	0.000	0.000
44	A	49	SER	0	-0.036	0.003	39.829	0.132	0.132	0.000	0.000	0.000	0.000
45	A	50	ILE	0	0.001	-0.004	34.829	0.129	0.129	0.000	0.000	0.000	0.000
46	A	51	VAL	0	0.008	0.004	37.434	0.069	0.069	0.000	0.000	0.000	0.000
47	A	52	THR	0	-0.041	-0.024	39.400	0.193	0.193	0.000	0.000	0.000	0.000
48	A	53	ASN	0	-0.056	-0.036	40.229	0.269	0.269	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.845	-0.914	36.632	-8.440	-8.440	0.000	0.000	0.000	0.000
50	A	55	ALA	0	0.010	0.018	40.037	0.001	0.001	0.000	0.000	0.000	0.000
51	A	56	LYS	1	0.795	0.884	36.512	8.315	8.315	0.000	0.000	0.000	0.000
52	A	57	PRO	0	0.042	0.019	37.939	-0.127	-0.127	0.000	0.000	0.000	0.000
53	A	58	THR	0	-0.032	-0.021	33.176	-0.114	-0.114	0.000	0.000	0.000	0.000
54	A	59	PHE	0	0.072	0.034	26.939	-0.080	-0.080	0.000	0.000	0.000	0.000
55	A	60	SER	0	0.037	0.013	28.415	-0.094	-0.094	0.000	0.000	0.000	0.000
56	A	61	ASN	0	0.016	0.002	29.542	0.105	0.105	0.000	0.000	0.000	0.000
57	A	62	VAL	0	-0.015	0.004	32.152	0.107	0.107	0.000	0.000	0.000	0.000
58	A	63	ILE	0	0.018	0.004	26.723	0.048	0.048	0.000	0.000	0.000	0.000
59	A	64	GLU	-1	-0.899	-0.950	27.014	-11.023	-11.023	0.000	0.000	0.000	0.000
60	A	65	ARG	1	0.827	0.917	28.606	8.993	8.993	0.000	0.000	0.000	0.000
61	A	66	ILE	0	-0.064	-0.013	30.437	0.224	0.224	0.000	0.000	0.000	0.000
62	A	67	GLU	-1	-0.921	-0.962	23.738	-13.133	-13.133	0.000	0.000	0.000	0.000
63	A	68	PRO	0	0.020	0.001	26.317	-0.127	-0.127	0.000	0.000	0.000	0.000
64	A	69	LYS	1	0.984	0.992	27.436	9.177	9.177	0.000	0.000	0.000	0.000
65	A	70	ALA	0	0.017	0.010	28.871	0.141	0.141	0.000	0.000	0.000	0.000
66	A	71	MET	0	-0.039	-0.025	21.698	-0.110	-0.110	0.000	0.000	0.000	0.000
67	A	72	ASP	-1	-0.936	-0.963	27.061	-11.409	-11.409	0.000	0.000	0.000	0.000
68	A	73	ILE	0	-0.060	-0.029	29.331	0.267	0.267	0.000	0.000	0.000	0.000
69	A	74	VAL	0	-0.048	-0.010	27.079	0.227	0.227	0.000	0.000	0.000	0.000
70	A	75	PRO	0	0.010	0.001	29.905	-0.098	-0.098	0.000	0.000	0.000	0.000
71	A	76	GLU	-1	-0.898	-0.952	29.405	-10.484	-10.484	0.000	0.000	0.000	0.000
72	A	77	HIS	0	-0.018	-0.001	29.271	-0.218	-0.218	0.000	0.000	0.000	0.000
73	A	78	ILE	0	0.016	0.007	28.125	-0.204	-0.204	0.000	0.000	0.000	0.000
74	A	79	LYS	1	0.961	0.979	23.985	12.342	12.342	0.000	0.000	0.000	0.000
75	A	80	THR	0	-0.008	-0.025	24.749	-0.520	-0.520	0.000	0.000	0.000	0.000
76	A	81	GLU	-1	-0.760	-0.857	25.709	-10.415	-10.415	0.000	0.000	0.000	0.000
77	A	82	ILE	0	-0.052	-0.034	23.140	-0.167	-0.167	0.000	0.000	0.000	0.000
78	A	83	LEU	0	-0.002	0.002	19.607	-0.580	-0.580	0.000	0.000	0.000	0.000
79	A	84	ALA	0	0.041	0.031	21.193	-0.625	-0.625	0.000	0.000	0.000	0.000
80	A	85	LYS	1	0.923	0.960	22.636	11.707	11.707	0.000	0.000	0.000	0.000
81	A	86	ILE	0	-0.045	-0.031	17.401	-0.369	-0.369	0.000	0.000	0.000	0.000
82	A	87	GLU	-1	-0.894	-0.963	17.893	-15.848	-15.848	0.000	0.000	0.000	0.000
83	A	88	GLU	-1	-1.004	-0.992	18.724	-13.096	-13.096	0.000	0.000	0.000	0.000
84	A	89	PHE	0	0.031	0.004	19.316	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	90	LEU	0	-0.041	-0.015	13.422	-1.052	-1.052	0.000	0.000	0.000	0.000
86	A	91	LYS	1	0.863	0.930	15.780	13.989	13.989	0.000	0.000	0.000	0.000
87	A	92	ASP	-1	-0.909	-0.941	18.179	-14.634	-14.634	0.000	0.000	0.000	0.000
88	A	93	VAL	0	-0.097	-0.056	13.957	0.028	0.028	0.000	0.000	0.000	0.000
89	A	94	VAL	0	-0.088	-0.041	11.387	-1.798	-1.798	0.000	0.000	0.000	0.000
90	A	95	PRO	-1	-0.962	-0.964	10.704	-23.890	-23.890	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:VAL)