FMO DATABASE

FMODB ID: 7NY1K

Calculation Name: 3UJ3-X-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3UJ3

Chain ID: X

ChEMBL ID:

UniProt ID: P03015

Base Structure: X-ray

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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1042939.677612
FMO2-HF: Nuclear repulsion	993125.562854
FMO2-HF: Total energy	-49814.114758
FMO2-MP2: Total energy	-49957.314003

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:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-104.853	-102.859	33.275	-16.38	-18.891	-0.196

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.785 / q_NPA : 0.891

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	4	GLY	0	0.022	0.012	3.887	-1.808	-0.543	-0.013	-0.627	-0.625	0.001
26	A	27	CYS	0	-0.144	-0.092	3.026	-9.225	-8.116	0.070	-0.438	-0.741	-0.003
27	A	28	GLU	-1	-0.897	-0.938	2.719	-36.746	-35.185	0.137	-0.495	-1.203	-0.002
28	A	29	GLN	0	-0.038	-0.032	4.594	6.879	7.024	-0.001	-0.013	-0.132	0.000
51	A	52	LEU	0	0.036	0.036	4.078	-3.513	-3.430	-0.001	-0.017	-0.065	0.000
55	A	56	ASP	-1	-0.752	-0.854	1.794	-124.489	-123.661	15.246	-7.916	-8.158	-0.119
56	A	57	THR	0	-0.065	-0.066	2.070	-7.570	-7.204	7.495	-3.280	-4.581	-0.029
57	A	58	LEU	0	-0.017	-0.010	1.986	-24.282	-28.162	10.322	-3.483	-2.959	-0.043
58	A	59	VAL	0	0.033	0.024	3.030	2.279	2.803	0.021	-0.110	-0.435	-0.001
59	A	60	VAL	0	0.003	0.000	5.384	3.498	3.491	-0.001	-0.001	0.008	0.000
4	A	5	TYR	0	-0.117	-0.091	6.352	3.642	3.642	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.024	0.019	9.777	0.365	0.365	0.000	0.000	0.000	0.000
6	A	7	ARG	1	0.853	0.940	13.274	17.869	17.869	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.011	0.008	16.654	0.525	0.525	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.015	0.004	20.103	0.231	0.231	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.007	-0.023	23.793	0.015	0.015	0.000	0.000	0.000	0.000
10	A	11	ASN	0	0.006	0.006	25.101	-0.147	-0.147	0.000	0.000	0.000	0.000
11	A	12	ASP	-1	-0.831	-0.921	21.482	-13.646	-13.646	0.000	0.000	0.000	0.000
12	A	13	GLN	0	0.083	0.044	20.970	-0.468	-0.468	0.000	0.000	0.000	0.000
13	A	14	ASN	0	-0.015	-0.010	21.224	-0.318	-0.318	0.000	0.000	0.000	0.000
14	A	15	THR	0	-0.036	-0.004	16.189	-1.056	-1.056	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.847	-0.921	16.150	-16.677	-16.677	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.010	-0.013	16.580	-0.775	-0.775	0.000	0.000	0.000	0.000
17	A	18	GLN	0	-0.039	-0.014	14.159	-1.354	-1.354	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.975	0.981	11.968	19.468	19.468	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.009	0.011	11.624	-2.118	-2.118	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.034	0.023	12.706	-0.549	-0.549	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.030	-0.029	8.196	-1.384	-1.384	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.005	0.011	7.522	-3.483	-3.483	0.000	0.000	0.000	0.000
23	A	24	CYS	0	-0.060	-0.030	8.799	-0.544	-0.544	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.049	-0.018	8.066	0.712	0.712	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.001	0.018	5.779	-2.134	-2.134	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.013	-0.002	7.230	-2.936	-2.936	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.001	-0.014	8.904	1.733	1.733	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.861	-0.951	11.989	-20.185	-20.185	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.762	-0.852	14.904	-18.339	-18.339	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.870	0.934	17.671	13.029	13.029	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.028	-0.016	20.802	-0.373	-0.373	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.025	-0.013	22.864	0.352	0.352	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.036	0.015	26.354	0.085	0.085	0.000	0.000	0.000	0.000
37	A	38	THR	0	0.004	0.010	24.486	0.216	0.216	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.910	0.943	21.207	12.939	12.939	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.010	-0.008	20.206	-0.688	-0.688	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.872	-0.919	21.202	-14.223	-14.223	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.919	0.960	16.070	17.632	17.632	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.039	0.024	18.019	0.064	0.064	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.051	0.021	16.624	-0.235	-0.235	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.017	-0.012	11.460	-1.202	-1.202	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.920	0.954	13.061	14.239	14.239	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.895	0.923	13.375	19.177	19.177	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.023	0.019	8.823	-1.025	-1.025	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.031	-0.014	8.929	-2.434	-2.434	0.000	0.000	0.000	0.000
49	A	50	LYS	0	0.001	0.033	11.399	0.261	0.261	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.865	0.935	8.796	25.570	25.570	0.000	0.000	0.000	0.000
52	A	53	GLN	0	0.027	0.012	5.782	0.149	0.149	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.965	0.972	6.915	17.818	17.818	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.025	-0.009	6.741	0.634	0.634	0.000	0.000	0.000	0.000
60	A	61	TRP	0	0.069	0.036	9.235	0.112	0.112	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.945	0.967	12.319	17.422	17.422	0.000	0.000	0.000	0.000
62	A	63	LEU	0	0.020	-0.006	13.813	-0.347	-0.347	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.795	-0.897	15.034	-15.705	-15.705	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.790	0.903	15.527	16.465	16.465	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.024	0.020	11.987	-1.081	-1.081	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.047	0.002	15.185	0.267	0.267	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.812	0.902	18.144	15.503	15.503	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.043	0.046	20.053	0.439	0.439	0.000	0.000	0.000	0.000
69	A	70	MET	0	0.045	0.031	20.168	-0.951	-0.951	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.981	0.991	20.673	12.091	12.091	0.000	0.000	0.000	0.000
71	A	72	HIS	0	-0.091	-0.044	17.697	-0.289	-0.289	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.014	0.005	15.643	-0.633	-0.633	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.030	0.007	16.143	-1.203	-1.203	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.069	-0.029	17.726	-0.132	-0.132	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.006	0.009	12.817	0.149	0.149	0.000	0.000	0.000	0.000
76	A	77	VAL	0	0.012	-0.010	10.819	-0.972	-0.972	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.017	-0.003	13.266	-0.724	-0.724	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.804	-0.886	14.725	-20.366	-20.366	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.023	-0.014	8.901	-0.377	-0.377	0.000	0.000	0.000	0.000
80	A	81	ARG	1	0.961	0.980	11.952	17.441	17.441	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.981	-0.978	13.412	-16.180	-16.180	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.842	0.919	11.458	23.911	23.911	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.004	0.001	11.720	-0.356	-0.356	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.055	-0.021	5.398	-1.910	-1.910	0.000	0.000	0.000	0.000
85	A	86	ASN	0	0.014	0.013	7.145	4.842	4.842	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.015	-0.011	6.234	-5.878	-5.878	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.948	0.979	6.286	31.564	31.564	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.009	0.009	7.525	-1.527	-1.527	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.010	-0.009	7.845	0.565	0.565	0.000	0.000	0.000	0.000
90	A	91	THR	0	-0.011	-0.003	11.462	1.572	1.572	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.792	-0.906	14.328	-18.776	-18.776	0.000	0.000	0.000	0.000
92	A	93	SER	0	-0.070	-0.023	13.959	0.657	0.657	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.002	0.014	13.186	0.415	0.415	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.838	-0.907	10.380	-25.771	-25.771	0.000	0.000	0.000	0.000
95	A	96	THR	0	-0.006	-0.022	9.930	1.758	1.758	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.013	0.004	8.814	0.294	0.294	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.016	-0.011	11.405	1.864	1.864	0.000	0.000	0.000	0.000
98	A	99	PRO	0	-0.039	-0.041	14.840	-0.043	-0.043	0.000	0.000	0.000	0.000
99	A	100	MET	0	0.039	0.023	17.274	0.614	0.614	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.049	0.032	15.151	0.424	0.424	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.893	0.926	13.800	20.538	20.538	0.000	0.000	0.000	0.000
102	A	103	PHE	0	0.005	0.015	16.606	0.259	0.259	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.074	0.029	17.107	0.424	0.424	0.000	0.000	0.000	0.000
104	A	105	PHE	0	0.002	0.014	14.361	0.050	0.050	0.000	0.000	0.000	0.000
105	A	106	HIS	0	0.010	-0.004	16.445	-0.045	-0.045	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.021	0.004	19.234	0.636	0.636	0.000	0.000	0.000	0.000
107	A	108	MET	0	0.045	0.020	17.943	0.687	0.687	0.000	0.000	0.000	0.000
108	A	109	GLY	0	-0.041	-0.019	18.871	0.081	0.081	0.000	0.000	0.000	0.000
109	A	110	ALA	0	-0.004	-0.015	19.392	0.396	0.396	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.005	0.016	22.330	0.452	0.452	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.040	0.012	20.128	0.375	0.375	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.895	-0.964	22.154	-12.373	-12.373	0.000	0.000	0.000	0.000
113	A	114	VAL	0	0.049	0.018	24.279	0.404	0.404	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.939	-0.957	23.421	-12.656	-12.656	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.838	0.897	25.010	11.991	11.991	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.902	-0.961	26.867	-10.781	-10.781	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.037	0.030	29.877	0.284	0.284	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.029	-0.013	27.608	0.284	0.284	0.000	0.000	0.000	0.000
119	A	120	ILE	0	-0.055	-0.021	29.774	0.210	0.210	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.883	-0.941	32.176	-8.582	-8.582	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.914	0.957	33.805	9.244	9.244	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.098	-0.059	34.383	0.060	0.060	0.000	0.000	0.000	0.000
123	A	124	MET	0	-0.124	-0.051	35.583	0.161	0.161	0.000	0.000	0.000	0.000
124	A	125	ALA	-1	-0.920	-0.943	39.772	-7.555	-7.555	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)