FMO DATABASE

FMODB ID: 5R4LZ

Calculation Name: 1Q1U-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1Q1U

Chain ID: A

ChEMBL ID:

UniProt ID: P61328

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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1307150.61583
FMO2-HF: Nuclear repulsion	1252493.554421
FMO2-HF: Total energy	-54657.061408
FMO2-MP2: Total energy	-54817.393784

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:PRO)

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

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.
42.601	44.128	-0.014	-0.527	-0.987	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / q_NPA : 0.900

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	LEU	0	0.007	0.021	3.819	1.662	3.189	-0.014	-0.527	-0.987	-0.001
4	A	9	LYS	1	0.921	0.939	5.450	21.732	21.732	0.000	0.000	0.000	0.000
5	A	10	GLY	0	0.008	0.006	9.210	0.646	0.646	0.000	0.000	0.000	0.000
6	A	11	ILE	0	-0.037	-0.004	11.151	0.973	0.973	0.000	0.000	0.000	0.000
7	A	12	VAL	0	0.060	0.035	14.699	-0.109	-0.109	0.000	0.000	0.000	0.000
8	A	13	THR	0	-0.027	-0.025	17.470	0.972	0.972	0.000	0.000	0.000	0.000
9	A	14	ARG	1	0.904	0.971	19.904	11.643	11.643	0.000	0.000	0.000	0.000
10	A	15	LEU	0	-0.009	-0.004	18.739	-0.198	-0.198	0.000	0.000	0.000	0.000
11	A	16	PHE	0	0.015	0.014	23.047	0.363	0.363	0.000	0.000	0.000	0.000
12	A	17	SER	0	0.023	0.018	26.783	0.090	0.090	0.000	0.000	0.000	0.000
13	A	18	GLN	0	0.056	0.019	28.270	0.120	0.120	0.000	0.000	0.000	0.000
14	A	19	GLN	0	-0.098	-0.061	31.066	0.630	0.630	0.000	0.000	0.000	0.000
15	A	20	GLY	0	-0.020	0.002	32.247	0.280	0.280	0.000	0.000	0.000	0.000
16	A	21	TYR	0	-0.061	-0.035	30.410	0.209	0.209	0.000	0.000	0.000	0.000
17	A	22	PHE	0	0.004	0.004	26.884	-0.361	-0.361	0.000	0.000	0.000	0.000
18	A	23	LEU	0	-0.035	-0.009	21.379	0.248	0.248	0.000	0.000	0.000	0.000
19	A	24	GLN	0	-0.024	-0.043	24.418	-0.242	-0.242	0.000	0.000	0.000	0.000
20	A	25	MET	0	-0.043	-0.014	18.557	-0.216	-0.216	0.000	0.000	0.000	0.000
21	A	26	HIS	0	-0.008	0.008	23.746	-0.299	-0.299	0.000	0.000	0.000	0.000
22	A	27	PRO	0	0.001	-0.025	23.403	-0.493	-0.493	0.000	0.000	0.000	0.000
23	A	28	ASP	-1	-0.834	-0.887	23.794	-11.982	-11.982	0.000	0.000	0.000	0.000
24	A	29	GLY	0	0.006	0.000	22.502	-0.160	-0.160	0.000	0.000	0.000	0.000
25	A	30	THR	0	-0.051	-0.016	23.293	-0.166	-0.166	0.000	0.000	0.000	0.000
26	A	31	ILE	0	-0.043	-0.025	21.234	-0.366	-0.366	0.000	0.000	0.000	0.000
27	A	32	ASP	-1	-0.853	-0.914	25.453	-10.425	-10.425	0.000	0.000	0.000	0.000
28	A	33	GLY	0	-0.008	-0.008	26.966	-0.476	-0.476	0.000	0.000	0.000	0.000
29	A	34	THR	0	0.023	0.013	29.023	0.555	0.555	0.000	0.000	0.000	0.000
30	A	35	LYS	1	0.941	0.952	31.247	8.375	8.375	0.000	0.000	0.000	0.000
31	A	36	ASP	-1	-0.858	-0.917	32.752	-9.680	-9.680	0.000	0.000	0.000	0.000
32	A	37	GLU	-1	-0.872	-0.941	28.538	-11.188	-11.188	0.000	0.000	0.000	0.000
33	A	38	ASN	0	-0.065	-0.052	28.861	-0.449	-0.449	0.000	0.000	0.000	0.000
34	A	39	SER	0	0.027	0.029	28.974	-0.310	-0.310	0.000	0.000	0.000	0.000
35	A	40	ASP	-1	-0.854	-0.925	24.856	-12.474	-12.474	0.000	0.000	0.000	0.000
36	A	41	TYR	0	-0.013	-0.015	23.988	-0.727	-0.727	0.000	0.000	0.000	0.000
37	A	42	THR	0	-0.050	-0.031	23.954	-0.464	-0.464	0.000	0.000	0.000	0.000
38	A	43	LEU	0	-0.039	-0.001	20.923	-0.338	-0.338	0.000	0.000	0.000	0.000
39	A	44	PHE	0	-0.002	-0.012	17.194	-0.371	-0.371	0.000	0.000	0.000	0.000
40	A	45	ASN	0	-0.002	0.003	12.801	0.880	0.880	0.000	0.000	0.000	0.000
41	A	46	LEU	0	-0.018	-0.010	13.716	-0.815	-0.815	0.000	0.000	0.000	0.000
42	A	47	ILE	0	0.038	0.011	7.270	-0.494	-0.494	0.000	0.000	0.000	0.000
43	A	48	PRO	0	-0.013	0.008	8.005	-0.159	-0.159	0.000	0.000	0.000	0.000
44	A	49	VAL	0	-0.021	-0.023	4.824	-5.441	-5.441	0.000	0.000	0.000	0.000
45	A	50	GLY	0	-0.010	-0.013	5.817	-0.803	-0.803	0.000	0.000	0.000	0.000
46	A	51	LEU	0	0.019	0.016	7.886	1.117	1.117	0.000	0.000	0.000	0.000
47	A	52	ARG	1	0.937	0.969	11.304	19.387	19.387	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.035	-0.021	9.803	1.603	1.603	0.000	0.000	0.000	0.000
49	A	54	VAL	0	0.017	0.014	9.398	-2.588	-2.588	0.000	0.000	0.000	0.000
50	A	55	ALA	0	0.011	0.016	9.075	0.937	0.937	0.000	0.000	0.000	0.000
51	A	56	ILE	0	-0.004	-0.004	10.911	-0.040	-0.040	0.000	0.000	0.000	0.000
52	A	57	GLN	0	0.023	0.016	12.527	0.083	0.083	0.000	0.000	0.000	0.000
53	A	58	GLY	0	0.056	0.031	15.093	0.365	0.365	0.000	0.000	0.000	0.000
54	A	59	VAL	0	-0.049	-0.036	17.313	-0.211	-0.211	0.000	0.000	0.000	0.000
55	A	60	LYS	1	0.905	0.956	18.656	13.789	13.789	0.000	0.000	0.000	0.000
56	A	61	ALA	0	0.030	0.021	20.041	0.182	0.182	0.000	0.000	0.000	0.000
57	A	62	SER	0	-0.010	0.007	15.591	-0.326	-0.326	0.000	0.000	0.000	0.000
58	A	63	LEU	0	0.029	0.035	15.181	-1.340	-1.340	0.000	0.000	0.000	0.000
59	A	64	TYR	0	-0.018	-0.030	9.007	-0.491	-0.491	0.000	0.000	0.000	0.000
60	A	65	VAL	0	0.013	0.012	15.077	1.065	1.065	0.000	0.000	0.000	0.000
61	A	66	ALA	0	0.004	-0.007	15.610	-1.376	-1.376	0.000	0.000	0.000	0.000
62	A	67	MET	0	-0.069	-0.033	17.394	1.234	1.234	0.000	0.000	0.000	0.000
63	A	68	ASN	0	0.019	0.010	19.170	-0.371	-0.371	0.000	0.000	0.000	0.000
64	A	69	GLY	0	0.074	0.033	21.546	0.252	0.252	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.837	-0.920	23.381	-11.707	-11.707	0.000	0.000	0.000	0.000
66	A	71	GLY	0	-0.042	-0.036	24.450	0.531	0.531	0.000	0.000	0.000	0.000
67	A	72	TYR	0	-0.038	-0.038	25.164	0.459	0.459	0.000	0.000	0.000	0.000
68	A	73	LEU	0	-0.030	-0.009	20.434	-0.521	-0.521	0.000	0.000	0.000	0.000
69	A	74	TYR	0	-0.049	-0.058	17.841	0.391	0.391	0.000	0.000	0.000	0.000
70	A	75	SER	0	0.039	0.001	19.014	-0.772	-0.772	0.000	0.000	0.000	0.000
71	A	76	SER	0	-0.054	-0.042	14.660	1.022	1.022	0.000	0.000	0.000	0.000
72	A	77	ASP	-1	-0.872	-0.933	15.578	-20.271	-20.271	0.000	0.000	0.000	0.000
73	A	78	VAL	0	0.022	0.010	11.504	-1.895	-1.895	0.000	0.000	0.000	0.000
74	A	79	PHE	0	0.009	0.011	6.318	-0.377	-0.377	0.000	0.000	0.000	0.000
75	A	80	THR	0	0.048	0.003	10.024	-0.708	-0.708	0.000	0.000	0.000	0.000
76	A	81	PRO	0	0.006	-0.022	11.169	-0.732	-0.732	0.000	0.000	0.000	0.000
77	A	82	GLU	-1	-0.767	-0.838	12.247	-15.832	-15.832	0.000	0.000	0.000	0.000
78	A	83	CYS	0	-0.030	0.021	11.649	0.924	0.924	0.000	0.000	0.000	0.000
79	A	84	LYS	1	0.916	0.980	7.182	32.035	32.035	0.000	0.000	0.000	0.000
80	A	85	PHE	0	0.031	0.016	11.980	1.920	1.920	0.000	0.000	0.000	0.000
81	A	86	LYS	1	0.889	0.954	13.362	14.325	14.325	0.000	0.000	0.000	0.000
82	A	87	GLU	-1	-0.801	-0.901	14.519	-17.750	-17.750	0.000	0.000	0.000	0.000
83	A	88	SER	0	-0.102	-0.077	16.994	0.255	0.255	0.000	0.000	0.000	0.000
84	A	89	VAL	0	0.051	0.041	20.381	0.055	0.055	0.000	0.000	0.000	0.000
85	A	90	PHE	0	-0.052	-0.038	23.550	0.275	0.275	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.865	-0.957	27.197	-9.588	-9.588	0.000	0.000	0.000	0.000
87	A	92	ASN	0	-0.050	-0.016	26.897	-0.054	-0.054	0.000	0.000	0.000	0.000
88	A	93	TYR	0	0.004	0.008	27.404	-0.048	-0.048	0.000	0.000	0.000	0.000
89	A	94	TYR	0	0.024	0.015	26.065	-0.319	-0.319	0.000	0.000	0.000	0.000
90	A	95	VAL	0	0.006	0.004	19.156	-0.086	-0.086	0.000	0.000	0.000	0.000
91	A	96	ILE	0	-0.064	-0.033	21.913	0.385	0.385	0.000	0.000	0.000	0.000
92	A	97	TYR	0	0.047	0.018	16.317	-0.104	-0.104	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.060	-0.041	18.302	0.668	0.668	0.000	0.000	0.000	0.000
94	A	99	SER	0	0.054	0.035	17.216	-1.126	-1.126	0.000	0.000	0.000	0.000
95	A	100	THR	0	-0.046	-0.043	12.582	0.468	0.468	0.000	0.000	0.000	0.000
96	A	101	LEU	0	-0.033	0.000	14.549	0.272	0.272	0.000	0.000	0.000	0.000
97	A	102	TYR	0	-0.060	-0.047	17.796	0.821	0.821	0.000	0.000	0.000	0.000
98	A	103	ARG	1	0.882	0.932	19.224	14.068	14.068	0.000	0.000	0.000	0.000
99	A	104	GLN	0	-0.048	-0.011	24.312	0.002	0.002	0.000	0.000	0.000	0.000
100	A	105	GLN	0	0.074	0.030	27.790	-0.031	-0.031	0.000	0.000	0.000	0.000
101	A	106	GLU	-1	-0.874	-0.930	29.585	-9.270	-9.270	0.000	0.000	0.000	0.000
102	A	107	SER	0	-0.047	-0.026	30.811	-0.127	-0.127	0.000	0.000	0.000	0.000
103	A	108	GLY	0	0.043	0.028	26.634	-0.093	-0.093	0.000	0.000	0.000	0.000
104	A	109	ARG	1	0.823	0.903	25.490	9.907	9.907	0.000	0.000	0.000	0.000
105	A	110	ALA	0	-0.002	-0.002	22.061	-0.071	-0.071	0.000	0.000	0.000	0.000
106	A	111	TRP	0	-0.036	-0.009	22.686	0.449	0.449	0.000	0.000	0.000	0.000
107	A	112	PHE	0	-0.028	-0.038	21.850	-0.592	-0.592	0.000	0.000	0.000	0.000
108	A	113	LEU	0	0.083	0.049	19.948	0.417	0.417	0.000	0.000	0.000	0.000
109	A	114	GLY	0	0.006	-0.025	22.810	0.218	0.218	0.000	0.000	0.000	0.000
110	A	115	LEU	0	0.013	0.036	26.247	0.003	0.003	0.000	0.000	0.000	0.000
111	A	116	ASN	0	0.035	0.007	29.192	0.057	0.057	0.000	0.000	0.000	0.000
112	A	117	LYS	1	0.903	0.948	32.937	8.455	8.455	0.000	0.000	0.000	0.000
113	A	118	GLU	-1	-0.844	-0.929	35.694	-8.476	-8.476	0.000	0.000	0.000	0.000
114	A	119	GLY	0	0.036	0.030	32.012	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	120	GLN	0	0.012	0.003	30.838	-0.461	-0.461	0.000	0.000	0.000	0.000
116	A	121	ILE	0	0.033	0.016	24.651	0.031	0.031	0.000	0.000	0.000	0.000
117	A	122	MET	0	-0.081	-0.034	28.122	0.384	0.384	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.880	0.963	27.103	10.122	10.122	0.000	0.000	0.000	0.000
119	A	124	GLY	0	0.129	0.057	24.653	0.265	0.265	0.000	0.000	0.000	0.000
120	A	125	ASN	0	0.021	0.005	25.672	-0.029	-0.029	0.000	0.000	0.000	0.000
121	A	126	ARG	1	0.908	0.955	27.870	9.736	9.736	0.000	0.000	0.000	0.000
122	A	127	VAL	0	-0.006	0.022	26.293	0.441	0.441	0.000	0.000	0.000	0.000
123	A	128	LYS	1	0.893	0.934	28.095	9.405	9.405	0.000	0.000	0.000	0.000
124	A	129	LYS	1	1.033	1.031	25.065	11.707	11.707	0.000	0.000	0.000	0.000
125	A	130	THR	0	0.003	0.008	27.864	-0.029	-0.029	0.000	0.000	0.000	0.000
126	A	131	LYS	1	0.928	0.965	30.646	8.945	8.945	0.000	0.000	0.000	0.000
127	A	132	PRO	0	0.069	0.028	30.150	-0.334	-0.334	0.000	0.000	0.000	0.000
128	A	133	SER	0	0.025	0.023	29.802	-0.207	-0.207	0.000	0.000	0.000	0.000
129	A	134	SER	0	-0.052	-0.025	25.702	-0.361	-0.361	0.000	0.000	0.000	0.000
130	A	135	HIS	1	0.760	0.889	25.102	9.950	9.950	0.000	0.000	0.000	0.000
131	A	136	PHE	0	0.071	0.027	23.130	0.299	0.299	0.000	0.000	0.000	0.000
132	A	137	VAL	0	0.022	0.013	24.964	-0.031	-0.031	0.000	0.000	0.000	0.000
133	A	138	PRO	0	-0.019	-0.011	20.134	0.097	0.097	0.000	0.000	0.000	0.000
134	A	139	LYS	1	0.925	0.966	22.301	11.637	11.637	0.000	0.000	0.000	0.000
135	A	140	PRO	0	0.044	0.016	19.772	-0.101	-0.101	0.000	0.000	0.000	0.000
136	A	141	ILE	0	-0.030	-0.020	20.652	0.619	0.619	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.956	-0.966	20.588	-13.883	-13.883	0.000	0.000	0.000	0.000
138	A	143	VAL	-1	-0.894	-0.923	16.220	-16.859	-16.859	0.000	0.000	0.000	0.000

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