FMO DATABASE

FMODB ID: 4QZGN

Calculation Name: 1UIX-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1UIX

Chain ID: A

ChEMBL ID:

UniProt ID: Q28021

Base Structure: X-ray

Registration Date: 2025-10-03

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	69
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-288544.884979
FMO2-HF: Nuclear repulsion	261449.368047
FMO2-HF: Total energy	-27095.516933
FMO2-MP2: Total energy	-27175.037597

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:-2:GLY)

Summations of interaction energy for fragment #1(A:-2: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.
-116	-108.826	11.342	-10.018	-8.499	-0.134

Interaction energy analysis for fragmet #1(A:-2:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.792 / 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	979	THR	0	0.042	0.016	3.848	3.370	4.138	-0.002	-0.254	-0.512	0.000
4	A	980	SER	0	0.034	0.010	2.163	-5.662	-3.461	2.100	-2.141	-2.160	-0.029
5	A	981	ASP	-1	-0.841	-0.911	2.055	-129.040	-125.017	9.245	-7.574	-5.694	-0.105
6	A	982	VAL	0	0.016	0.002	4.576	9.337	9.519	-0.001	-0.049	-0.133	0.000
7	A	983	ALA	0	0.006	0.008	7.325	4.627	4.627	0.000	0.000	0.000	0.000
8	A	984	ASN	0	0.005	0.004	6.321	6.618	6.618	0.000	0.000	0.000	0.000
9	A	985	LEU	0	0.048	0.018	8.052	3.395	3.395	0.000	0.000	0.000	0.000
10	A	986	ALA	0	-0.064	-0.026	10.584	2.822	2.822	0.000	0.000	0.000	0.000
11	A	987	ASN	0	0.011	0.003	12.392	3.114	3.114	0.000	0.000	0.000	0.000
12	A	988	GLU	-1	-0.921	-0.958	11.490	-23.888	-23.888	0.000	0.000	0.000	0.000
13	A	989	LYS	1	0.909	0.945	14.312	21.752	21.752	0.000	0.000	0.000	0.000
14	A	990	GLU	-1	-0.952	-0.961	16.556	-15.582	-15.582	0.000	0.000	0.000	0.000
15	A	991	GLU	-1	-0.890	-0.952	17.927	-14.078	-14.078	0.000	0.000	0.000	0.000
16	A	992	LEU	0	-0.032	-0.024	17.161	1.048	1.048	0.000	0.000	0.000	0.000
17	A	993	ASN	0	-0.036	-0.012	20.395	1.055	1.055	0.000	0.000	0.000	0.000
18	A	994	ASN	0	-0.009	-0.006	22.250	1.114	1.114	0.000	0.000	0.000	0.000
19	A	995	LYS	1	0.992	0.994	22.682	14.239	14.239	0.000	0.000	0.000	0.000
20	A	996	LEU	0	-0.030	0.001	24.482	0.542	0.542	0.000	0.000	0.000	0.000
21	A	997	LYS	1	0.919	0.959	26.201	11.365	11.365	0.000	0.000	0.000	0.000
22	A	998	GLU	-1	-0.921	-0.952	28.079	-10.725	-10.725	0.000	0.000	0.000	0.000
23	A	999	ALA	0	0.033	0.012	29.181	0.474	0.474	0.000	0.000	0.000	0.000
24	A	1000	GLN	0	-0.054	-0.032	29.340	0.279	0.279	0.000	0.000	0.000	0.000
25	A	1001	GLU	-1	-0.899	-0.957	32.189	-9.699	-9.699	0.000	0.000	0.000	0.000
26	A	1002	GLN	0	-0.040	-0.023	33.047	0.163	0.163	0.000	0.000	0.000	0.000
27	A	1003	LEU	0	0.003	-0.003	32.957	0.317	0.317	0.000	0.000	0.000	0.000
28	A	1004	SER	0	-0.016	-0.004	36.267	0.370	0.370	0.000	0.000	0.000	0.000
29	A	1005	ARG	1	0.889	0.929	38.180	8.087	8.087	0.000	0.000	0.000	0.000
30	A	1006	LEU	0	0.000	-0.008	39.264	0.232	0.232	0.000	0.000	0.000	0.000
31	A	1007	LYS	1	0.847	0.934	39.544	8.152	8.152	0.000	0.000	0.000	0.000
32	A	1008	ASP	-1	-0.875	-0.945	42.291	-7.434	-7.434	0.000	0.000	0.000	0.000
33	A	1009	GLU	-1	-0.884	-0.930	44.089	-7.214	-7.214	0.000	0.000	0.000	0.000
34	A	1010	GLU	-1	-0.938	-0.963	44.993	-7.056	-7.056	0.000	0.000	0.000	0.000
35	A	1011	ILE	0	0.000	0.001	46.791	0.202	0.202	0.000	0.000	0.000	0.000
36	A	1012	SER	0	0.007	0.003	48.631	0.205	0.205	0.000	0.000	0.000	0.000
37	A	1013	ALA	0	-0.017	-0.008	49.528	0.174	0.174	0.000	0.000	0.000	0.000
38	A	1014	ALA	0	-0.008	0.001	51.080	0.156	0.156	0.000	0.000	0.000	0.000
39	A	1015	ALA	0	-0.001	-0.001	52.981	0.158	0.158	0.000	0.000	0.000	0.000
40	A	1016	ILE	0	-0.008	-0.008	52.494	0.152	0.152	0.000	0.000	0.000	0.000
41	A	1017	LYS	1	0.951	0.981	55.191	5.918	5.918	0.000	0.000	0.000	0.000
42	A	1018	ALA	0	0.026	0.013	56.895	0.122	0.122	0.000	0.000	0.000	0.000
43	A	1019	GLN	0	0.013	0.012	59.067	0.220	0.220	0.000	0.000	0.000	0.000
44	A	1020	PHE	0	0.030	0.006	56.938	0.115	0.115	0.000	0.000	0.000	0.000
45	A	1021	GLU	-1	-0.953	-0.968	60.359	-5.301	-5.301	0.000	0.000	0.000	0.000
46	A	1022	LYS	1	0.936	0.968	62.696	5.137	5.137	0.000	0.000	0.000	0.000
47	A	1023	GLN	0	-0.011	-0.007	63.281	0.058	0.058	0.000	0.000	0.000	0.000
48	A	1024	LEU	0	0.008	0.017	64.690	0.097	0.097	0.000	0.000	0.000	0.000
49	A	1025	LEU	0	0.021	0.005	66.626	0.087	0.087	0.000	0.000	0.000	0.000
50	A	1026	THR	0	-0.024	-0.010	68.872	0.107	0.107	0.000	0.000	0.000	0.000
51	A	1027	GLU	-1	-0.875	-0.947	68.888	-4.548	-4.548	0.000	0.000	0.000	0.000
52	A	1028	ARG	1	0.884	0.921	69.543	4.594	4.594	0.000	0.000	0.000	0.000
53	A	1029	THR	0	-0.041	-0.011	72.347	0.090	0.090	0.000	0.000	0.000	0.000
54	A	1030	LEU	0	0.006	0.003	73.338	0.083	0.083	0.000	0.000	0.000	0.000
55	A	1031	LYS	0	0.046	0.048	73.029	0.065	0.065	0.000	0.000	0.000	0.000
56	A	1032	THR	0	-0.036	-0.034	75.855	0.062	0.062	0.000	0.000	0.000	0.000
57	A	1033	GLN	0	-0.027	-0.016	78.283	0.062	0.062	0.000	0.000	0.000	0.000
58	A	1034	ALA	0	0.004	0.008	79.466	0.067	0.067	0.000	0.000	0.000	0.000
59	A	1035	VAL	0	0.000	-0.002	78.836	0.056	0.056	0.000	0.000	0.000	0.000
60	A	1036	ASN	0	0.012	0.001	81.643	0.053	0.053	0.000	0.000	0.000	0.000
61	A	1037	LYS	1	0.820	0.899	84.029	3.766	3.766	0.000	0.000	0.000	0.000
62	A	1038	LEU	0	0.014	0.006	83.705	0.053	0.053	0.000	0.000	0.000	0.000
63	A	1039	ALA	0	0.013	-0.002	85.648	0.048	0.048	0.000	0.000	0.000	0.000
64	A	1040	GLU	-1	-0.860	-0.911	87.464	-3.606	-3.606	0.000	0.000	0.000	0.000
65	A	1041	ILE	0	-0.041	-0.029	89.754	0.053	0.053	0.000	0.000	0.000	0.000
66	A	1042	MET	0	-0.053	-0.028	88.185	0.026	0.026	0.000	0.000	0.000	0.000
67	A	1043	ASN	0	-0.031	-0.010	89.666	0.039	0.039	0.000	0.000	0.000	0.000
68	A	1044	ARG	1	0.896	0.968	93.232	3.386	3.386	0.000	0.000	0.000	0.000
69	A	1045	LYS	0	0.047	0.029	95.870	-0.050	-0.050	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:-2:GLY)