FMO DATABASE

FMODB ID: 3M3ZL

Calculation Name: 1GXT-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-amino-2-hydroxymethyl-propane-1,3-diol | sulfate ion | chloride ion

Ligand 3-letter code: TRS | SO4 | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1GXT

Chain ID: A

ChEMBL ID:

UniProt ID: P30131

Base Structure: X-ray

Registration Date: 2025-10-05

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	-640408.028746
FMO2-HF: Nuclear repulsion	604952.144693
FMO2-HF: Total energy	-35455.884053
FMO2-MP2: Total energy	-35559.462917

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:4:ASN)

Summations of interaction energy for fragment #1(A:4:ASN)

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.
-35.006	-32.148	0.084	-1.244	-1.7	-0.007

Interaction energy analysis for fragmet #1(A:4:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.794 / q_NPA : 0.886

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	6	SER	0	-0.020	0.000	3.846	1.267	2.567	-0.011	-0.532	-0.758	-0.001
80	A	83	GLN	0	-0.032	-0.023	3.167	-15.917	-14.616	0.096	-0.682	-0.716	-0.006
81	A	84	LEU	0	0.008	0.008	3.801	7.764	8.021	-0.001	-0.030	-0.226	0.000
4	A	7	CYS	0	0.011	0.002	6.745	1.482	1.482	0.000	0.000	0.000	0.000
5	A	8	GLY	0	0.037	0.027	10.396	-1.248	-1.248	0.000	0.000	0.000	0.000
6	A	9	VAL	0	-0.028	-0.018	12.269	1.318	1.318	0.000	0.000	0.000	0.000
7	A	10	GLN	0	-0.025	-0.012	15.937	-1.286	-1.286	0.000	0.000	0.000	0.000
8	A	11	LEU	0	-0.012	-0.020	18.070	0.732	0.732	0.000	0.000	0.000	0.000
9	A	12	ARG	1	0.799	0.864	21.496	13.271	13.271	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.006	0.001	24.209	0.498	0.498	0.000	0.000	0.000	0.000
11	A	14	ARG	1	0.812	0.858	27.164	11.154	11.154	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.093	0.045	30.507	0.170	0.170	0.000	0.000	0.000	0.000
13	A	16	LYS	1	0.787	0.903	33.590	8.166	8.166	0.000	0.000	0.000	0.000
14	A	17	VAL	0	0.056	0.024	29.310	0.068	0.068	0.000	0.000	0.000	0.000
15	A	18	GLN	0	0.014	0.001	30.326	-0.611	-0.611	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.000	-0.007	32.458	0.280	0.280	0.000	0.000	0.000	0.000
17	A	20	VAL	0	-0.056	-0.026	32.984	0.232	0.232	0.000	0.000	0.000	0.000
18	A	21	GLY	0	0.018	0.010	31.791	-0.029	-0.029	0.000	0.000	0.000	0.000
19	A	22	PHE	0	0.056	0.019	26.989	-0.195	-0.195	0.000	0.000	0.000	0.000
20	A	23	ARG	1	0.971	1.000	24.825	11.696	11.696	0.000	0.000	0.000	0.000
21	A	24	PRO	0	0.029	0.002	25.126	-0.379	-0.379	0.000	0.000	0.000	0.000
22	A	25	PHE	0	-0.005	0.017	26.720	-0.220	-0.220	0.000	0.000	0.000	0.000
23	A	26	VAL	0	0.032	0.015	22.133	-0.159	-0.159	0.000	0.000	0.000	0.000
24	A	27	TRP	0	0.000	-0.007	20.403	-0.032	-0.032	0.000	0.000	0.000	0.000
25	A	28	GLN	0	-0.003	-0.013	22.713	-0.568	-0.568	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.050	-0.013	24.443	-0.026	-0.026	0.000	0.000	0.000	0.000
27	A	30	ALA	0	0.034	0.005	19.231	-0.130	-0.130	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.027	-0.011	19.847	-1.147	-1.147	0.000	0.000	0.000	0.000
29	A	32	GLN	0	-0.039	-0.016	21.808	0.215	0.215	0.000	0.000	0.000	0.000
30	A	33	LEU	0	-0.030	-0.005	21.839	0.210	0.210	0.000	0.000	0.000	0.000
31	A	34	ASN	0	-0.056	-0.025	17.819	-1.068	-1.068	0.000	0.000	0.000	0.000
32	A	35	LEU	0	-0.006	0.014	16.465	-0.858	-0.858	0.000	0.000	0.000	0.000
33	A	36	HIS	1	0.772	0.857	12.228	20.983	20.983	0.000	0.000	0.000	0.000
34	A	37	GLY	0	-0.004	-0.025	12.698	-0.862	-0.862	0.000	0.000	0.000	0.000
35	A	38	ASP	-1	-0.814	-0.860	13.642	-20.262	-20.262	0.000	0.000	0.000	0.000
36	A	39	VAL	0	0.020	0.014	16.600	0.377	0.377	0.000	0.000	0.000	0.000
37	A	40	CYS	0	-0.010	0.010	20.211	0.128	0.128	0.000	0.000	0.000	0.000
38	A	41	ASN	0	-0.041	-0.042	22.247	0.348	0.348	0.000	0.000	0.000	0.000
39	A	42	ASP	-1	-0.782	-0.856	23.312	-13.188	-13.188	0.000	0.000	0.000	0.000
40	A	43	GLY	0	-0.006	0.007	25.664	0.190	0.190	0.000	0.000	0.000	0.000
41	A	44	ASP	-1	-0.842	-0.888	26.973	-10.660	-10.660	0.000	0.000	0.000	0.000
42	A	45	GLY	0	-0.015	0.002	27.518	-0.228	-0.228	0.000	0.000	0.000	0.000
43	A	46	VAL	0	-0.060	-0.043	24.282	-0.127	-0.127	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.830	-0.907	18.860	-16.154	-16.154	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.037	-0.023	18.862	-0.136	-0.136	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.820	0.896	12.350	22.245	22.245	0.000	0.000	0.000	0.000
47	A	50	LEU	0	0.024	0.003	14.759	-0.297	-0.297	0.000	0.000	0.000	0.000
48	A	51	ARG	1	0.926	0.963	8.861	29.677	29.677	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.785	-0.875	12.049	-22.934	-22.934	0.000	0.000	0.000	0.000
50	A	53	ASP	-1	-0.899	-0.941	15.092	-17.385	-17.385	0.000	0.000	0.000	0.000
51	A	54	PRO	0	-0.011	-0.003	18.250	0.484	0.484	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.811	-0.900	20.611	-13.641	-13.641	0.000	0.000	0.000	0.000
53	A	56	VAL	0	0.013	-0.001	23.595	0.587	0.587	0.000	0.000	0.000	0.000
54	A	57	PHE	0	0.059	0.022	22.064	0.445	0.445	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.003	-0.004	23.441	0.501	0.501	0.000	0.000	0.000	0.000
56	A	59	VAL	0	-0.011	-0.003	25.980	0.514	0.514	0.000	0.000	0.000	0.000
57	A	60	GLN	0	-0.012	-0.021	27.317	0.176	0.176	0.000	0.000	0.000	0.000
58	A	61	LEU	0	-0.003	0.003	25.581	0.311	0.311	0.000	0.000	0.000	0.000
59	A	62	TYR	0	-0.007	-0.015	28.425	0.342	0.342	0.000	0.000	0.000	0.000
60	A	63	GLN	0	-0.047	-0.027	31.725	0.444	0.444	0.000	0.000	0.000	0.000
61	A	64	HIS	0	-0.017	0.002	31.218	0.346	0.346	0.000	0.000	0.000	0.000
62	A	65	CYS	0	-0.009	0.016	32.064	-0.169	-0.169	0.000	0.000	0.000	0.000
63	A	66	PRO	0	-0.010	-0.004	31.636	0.326	0.326	0.000	0.000	0.000	0.000
64	A	67	PRO	0	0.045	0.024	34.661	0.075	0.075	0.000	0.000	0.000	0.000
65	A	68	LEU	0	-0.013	-0.004	37.329	0.178	0.178	0.000	0.000	0.000	0.000
66	A	69	ALA	0	-0.017	-0.008	33.476	0.058	0.058	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.798	0.845	34.820	8.623	8.623	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.008	0.011	29.842	-0.141	-0.141	0.000	0.000	0.000	0.000
69	A	72	ASP	-1	-0.794	-0.860	33.172	-8.510	-8.510	0.000	0.000	0.000	0.000
70	A	73	SER	0	-0.012	-0.012	31.170	0.052	0.052	0.000	0.000	0.000	0.000
71	A	74	VAL	0	-0.022	-0.017	25.575	-0.171	-0.171	0.000	0.000	0.000	0.000
72	A	75	GLU	-1	-0.866	-0.895	25.634	-11.117	-11.117	0.000	0.000	0.000	0.000
73	A	76	ARG	1	0.857	0.895	19.768	14.211	14.211	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.873	-0.913	18.763	-14.795	-14.795	0.000	0.000	0.000	0.000
75	A	78	PRO	0	-0.024	-0.007	15.551	-0.683	-0.683	0.000	0.000	0.000	0.000
76	A	79	PHE	0	0.009	0.002	11.479	0.045	0.045	0.000	0.000	0.000	0.000
77	A	80	ILE	0	-0.020	-0.017	7.635	-1.461	-1.461	0.000	0.000	0.000	0.000
78	A	81	TRP	0	-0.012	0.009	6.903	-0.275	-0.275	0.000	0.000	0.000	0.000
79	A	82	SER	0	0.011	-0.024	5.172	-3.840	-3.840	0.000	0.000	0.000	0.000
82	A	85	PRO	0	0.000	0.033	5.787	0.282	0.282	0.000	0.000	0.000	0.000
83	A	86	THR	0	0.009	-0.013	9.043	-0.548	-0.548	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.945	-0.959	11.179	-17.824	-17.824	0.000	0.000	0.000	0.000
85	A	88	PHE	0	0.018	0.012	14.074	-0.897	-0.897	0.000	0.000	0.000	0.000
86	A	89	THR	0	-0.017	-0.001	15.810	0.892	0.892	0.000	0.000	0.000	0.000
87	A	90	ILE	0	-0.025	-0.030	18.241	0.232	0.232	0.000	0.000	0.000	0.000
88	A	91	ARG	0	0.019	-0.001	16.909	3.577	3.577	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)