FMO DATABASE

FMODB ID: QLY5Y

Calculation Name: 1UJD-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1UJD

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y6V0

Base Structure: SolutionNMR

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	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-834616.686542
FMO2-HF: Nuclear repulsion	791192.535118
FMO2-HF: Total energy	-43424.151424
FMO2-MP2: Total energy	-43549.451922

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:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-42.554	-40.699	-0.019	-0.852	-0.984	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.913

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	SER	0	0.046	0.029	3.849	8.057	9.744	-0.018	-0.840	-0.829	-0.004
4	A	4	GLY	0	0.019	-0.001	4.641	-6.963	-6.795	-0.001	-0.012	-0.155	0.000
5	A	5	SER	0	-0.025	-0.005	7.400	1.829	1.829	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.017	0.013	11.012	1.242	1.242	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.014	-0.006	9.949	-2.255	-2.255	0.000	0.000	0.000	0.000
8	A	8	HIS	0	-0.021	0.010	10.797	-0.339	-0.339	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.015	-0.026	11.839	-0.717	-0.717	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.017	-0.016	15.966	0.751	0.751	0.000	0.000	0.000	0.000
11	A	11	PHE	0	0.004	0.011	16.345	1.039	1.039	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.008	0.008	19.582	-0.692	-0.692	0.000	0.000	0.000	0.000
13	A	13	HIS	0	-0.012	-0.018	14.875	-0.791	-0.791	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.000	0.002	19.038	0.346	0.346	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.871	0.922	10.076	24.681	24.681	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.031	-0.016	16.070	0.572	0.572	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.962	0.986	15.321	17.140	17.140	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.010	0.002	16.958	1.025	1.025	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.037	0.002	19.171	-0.702	-0.702	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.955	0.976	20.897	14.224	14.224	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.812	-0.884	22.646	-11.763	-11.763	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.054	-0.037	26.248	-0.246	-0.246	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.903	0.939	27.925	9.682	9.682	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.851	-0.917	30.858	-9.984	-9.984	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.004	0.005	32.701	0.520	0.520	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.043	-0.033	29.584	-0.023	-0.023	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.023	-0.017	33.045	0.013	0.013	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.019	0.003	30.542	0.084	0.084	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.021	0.018	27.107	-0.183	-0.183	0.000	0.000	0.000	0.000
30	A	30	ASN	0	0.011	-0.008	25.099	-0.038	-0.038	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.018	0.025	21.115	-0.189	-0.189	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.007	-0.005	18.854	-0.207	-0.207	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.015	0.000	22.817	0.322	0.322	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.009	-0.007	20.020	0.255	0.255	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.946	0.975	23.030	12.109	12.109	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.006	0.007	18.476	0.262	0.262	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.032	-0.004	22.056	-0.018	-0.018	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.050	0.009	20.447	-0.250	-0.250	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.011	0.007	21.024	0.626	0.626	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.891	0.955	22.915	11.766	11.766	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.893	-0.951	23.834	-11.537	-11.537	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.038	-0.016	20.640	0.159	0.159	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.004	-0.002	25.255	0.218	0.218	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.008	-0.003	27.633	-0.158	-0.158	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.015	-0.007	20.622	0.348	0.348	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.025	-0.018	25.580	0.515	0.515	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.008	0.016	26.491	-0.131	-0.131	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.858	-0.904	20.862	-15.345	-15.345	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.008	-0.005	20.853	0.310	0.310	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.032	0.001	19.178	-0.972	-0.972	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.018	0.000	18.328	0.538	0.538	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.005	0.000	20.274	0.027	0.027	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.028	0.015	21.495	-0.116	-0.116	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.041	-0.018	23.814	0.521	0.521	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.852	0.901	26.597	11.045	11.045	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.013	0.013	25.459	-0.646	-0.646	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.037	-0.014	27.453	0.329	0.329	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.027	0.021	29.944	-0.140	-0.140	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.009	-0.003	31.820	0.101	0.101	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.007	0.002	28.201	-0.079	-0.079	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.022	-0.041	23.992	-0.067	-0.067	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.019	-0.004	22.950	-0.388	-0.388	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.813	-0.892	24.285	-10.391	-10.391	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.019	-0.005	26.464	0.272	0.272	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.077	-0.048	22.061	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.012	0.002	25.314	0.034	0.034	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.902	0.948	21.893	13.717	13.717	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.060	-0.026	20.235	-0.248	-0.248	0.000	0.000	0.000	0.000
69	A	69	MET	0	0.065	0.027	24.185	0.415	0.415	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.873	-0.949	25.765	-11.055	-11.055	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.049	-0.024	27.125	0.225	0.225	0.000	0.000	0.000	0.000
72	A	72	MET	0	0.037	0.031	22.857	-0.058	-0.058	0.000	0.000	0.000	0.000
73	A	73	GLN	0	0.029	0.009	19.579	0.334	0.334	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.043	-0.038	16.091	-0.262	-0.262	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.047	-0.004	15.063	0.337	0.337	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.812	-0.922	10.093	-25.252	-25.252	0.000	0.000	0.000	0.000
77	A	77	TRP	0	0.033	0.016	11.746	1.950	1.950	0.000	0.000	0.000	0.000
78	A	78	ASN	0	0.031	0.009	9.768	-1.074	-1.074	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.012	-0.002	6.830	-4.005	-4.005	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.021	-0.007	7.319	-2.899	-2.899	0.000	0.000	0.000	0.000
81	A	81	PRO	0	-0.002	-0.001	8.466	2.755	2.755	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.015	-0.020	11.358	0.710	0.710	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.017	-0.021	14.882	1.731	1.731	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.033	-0.032	15.647	-1.300	-1.300	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.828	0.940	13.344	21.241	21.241	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.016	-0.028	18.197	1.054	1.054	0.000	0.000	0.000	0.000
87	A	87	TYR	0	0.011	-0.001	19.999	-0.634	-0.634	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.902	-0.960	21.305	-13.267	-13.267	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.818	-0.879	16.540	-18.517	-18.517	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.013	0.007	16.466	-0.943	-0.943	0.000	0.000	0.000	0.000
91	A	91	GLN	0	0.014	0.012	17.199	-0.611	-0.611	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.004	0.001	17.649	-0.292	-0.292	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.020	-0.010	12.075	-0.774	-0.774	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.032	-0.016	14.119	-0.824	-0.824	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.072	-0.049	16.678	0.085	0.085	0.000	0.000	0.000	0.000
96	A	96	GLN	0	-0.059	-0.035	14.811	0.890	0.890	0.000	0.000	0.000	0.000
97	A	97	GLN	0	-0.003	0.003	12.670	-2.049	-2.049	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.047	-0.026	16.326	1.460	1.460	0.000	0.000	0.000	0.000
99	A	99	GLY	0	-0.024	-0.022	17.870	0.346	0.346	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.934	-0.961	15.723	-18.284	-18.284	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.014	0.023	14.538	-1.120	-1.120	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.878	-0.929	11.163	-24.849	-24.849	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.016	0.002	13.106	-1.177	-1.177	0.000	0.000	0.000	0.000
104	A	104	CYS	0	-0.029	-0.008	11.267	0.420	0.420	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.059	0.034	14.780	0.097	0.097	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.890	0.940	18.470	13.290	13.290	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.046	-0.027	20.517	0.380	0.380	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.914	-0.946	23.383	-10.927	-10.927	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.003	-0.018	23.643	-0.186	-0.186	0.000	0.000	0.000	0.000
110	A	110	ASN	0	0.014	0.022	26.219	-0.151	-0.151	0.000	0.000	0.000	0.000
111	A	111	MET	0	-0.037	-0.019	23.293	0.217	0.217	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.028	-0.009	28.547	0.322	0.322	0.000	0.000	0.000	0.000
113	A	113	GLY	0	-0.001	0.006	30.280	0.210	0.210	0.000	0.000	0.000	0.000
114	A	114	PRO	0	-0.015	-0.012	31.489	0.054	0.054	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.043	-0.019	30.774	0.046	0.046	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.012	-0.007	33.505	0.075	0.075	0.000	0.000	0.000	0.000
117	A	117	GLY	-1	-0.853	-0.886	32.752	-9.785	-9.785	0.000	0.000	0.000	0.000

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