FMO DATABASE

FMODB ID: RL218

Calculation Name: 4GL9-E-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-tert-butyl-9-fluoro-3,6-dihydro-7h-benz[h]-imidaz[4,5-f]isoquinoline-7-one | o-phosphotyrosine | phosphate ion

Ligand 3-letter code: IZA | PTR | PO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4GL9

Chain ID: E

ChEMBL ID:

UniProt ID: Q00560

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1182662.317635
FMO2-HF: Nuclear repulsion	1130328.488787
FMO2-HF: Total energy	-52333.828849
FMO2-MP2: Total energy	-52487.60911

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:22:LEU)

Summations of interaction energy for fragment #1(A:22: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.
-7.146	-4.525	10.802	-5.417	-8.006	-0.051

Interaction energy analysis for fragmet #1(A:22:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.920

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	24	THR	0	0.012	0.009	3.042	-1.798	0.477	0.145	-1.102	-1.318	-0.006
4	A	25	PHE	0	0.007	-0.010	5.160	1.652	1.709	-0.001	-0.003	-0.053	0.000
55	A	76	GLN	0	0.043	0.003	1.982	-30.997	-30.838	10.662	-4.445	-6.376	-0.044
56	A	77	ARG	1	0.915	0.957	3.399	22.115	22.245	-0.004	0.133	-0.259	-0.001
5	A	26	SER	0	-0.028	-0.037	8.519	0.147	0.147	0.000	0.000	0.000	0.000
6	A	27	SER	0	0.022	0.009	11.385	1.782	1.782	0.000	0.000	0.000	0.000
7	A	28	LYS	1	0.978	0.991	13.222	15.611	15.611	0.000	0.000	0.000	0.000
8	A	29	SER	0	0.038	0.009	15.353	0.130	0.130	0.000	0.000	0.000	0.000
9	A	30	GLU	-1	-0.790	-0.881	10.825	-24.485	-24.485	0.000	0.000	0.000	0.000
10	A	31	TYR	0	-0.007	-0.001	10.725	0.296	0.296	0.000	0.000	0.000	0.000
11	A	32	GLN	0	0.011	-0.005	12.763	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	33	LEU	0	-0.003	0.016	14.822	0.596	0.596	0.000	0.000	0.000	0.000
13	A	34	VAL	0	0.016	0.008	9.801	0.573	0.573	0.000	0.000	0.000	0.000
14	A	35	VAL	0	-0.022	0.003	13.177	0.444	0.444	0.000	0.000	0.000	0.000
15	A	36	ASN	0	0.011	-0.010	15.158	0.758	0.758	0.000	0.000	0.000	0.000
16	A	37	ALA	0	-0.011	0.001	14.617	0.628	0.628	0.000	0.000	0.000	0.000
17	A	38	VAL	0	0.032	0.013	13.166	0.481	0.481	0.000	0.000	0.000	0.000
18	A	39	ARG	1	0.923	0.982	15.295	13.827	13.827	0.000	0.000	0.000	0.000
19	A	40	LYS	1	0.850	0.884	18.768	12.223	12.223	0.000	0.000	0.000	0.000
20	A	41	LEU	0	-0.011	0.006	14.990	0.460	0.460	0.000	0.000	0.000	0.000
21	A	42	GLN	0	0.000	0.007	16.102	0.720	0.720	0.000	0.000	0.000	0.000
22	A	43	GLU	-1	-0.840	-0.904	19.886	-11.256	-11.256	0.000	0.000	0.000	0.000
23	A	44	SER	0	-0.095	-0.055	21.093	0.428	0.428	0.000	0.000	0.000	0.000
24	A	45	GLY	0	0.045	0.029	22.881	0.341	0.341	0.000	0.000	0.000	0.000
25	A	46	PHE	0	-0.001	-0.002	21.178	0.006	0.006	0.000	0.000	0.000	0.000
26	A	47	TYR	0	-0.102	-0.093	12.130	-0.193	-0.193	0.000	0.000	0.000	0.000
27	A	48	TRP	0	0.032	0.003	16.891	-0.131	-0.131	0.000	0.000	0.000	0.000
28	A	49	SER	0	-0.040	-0.037	11.970	-0.798	-0.798	0.000	0.000	0.000	0.000
29	A	50	ALA	0	-0.031	-0.045	10.287	0.535	0.535	0.000	0.000	0.000	0.000
30	A	51	VAL	0	-0.015	0.023	11.317	-0.141	-0.141	0.000	0.000	0.000	0.000
31	A	52	THR	0	-0.007	-0.031	11.973	-0.995	-0.995	0.000	0.000	0.000	0.000
32	A	53	GLY	0	-0.005	-0.023	13.549	0.751	0.751	0.000	0.000	0.000	0.000
33	A	54	GLY	0	0.010	0.013	15.796	0.850	0.850	0.000	0.000	0.000	0.000
34	A	55	GLU	-1	-0.759	-0.872	16.381	-15.401	-15.401	0.000	0.000	0.000	0.000
35	A	56	ALA	0	-0.012	0.007	17.442	0.641	0.641	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.061	-0.060	19.383	0.995	0.995	0.000	0.000	0.000	0.000
37	A	58	LEU	0	0.029	0.030	21.839	0.524	0.524	0.000	0.000	0.000	0.000
38	A	59	LEU	0	0.019	0.024	20.647	0.532	0.532	0.000	0.000	0.000	0.000
39	A	60	LEU	0	-0.012	0.002	21.873	0.412	0.412	0.000	0.000	0.000	0.000
40	A	61	SER	0	-0.068	-0.045	25.267	0.445	0.445	0.000	0.000	0.000	0.000
41	A	62	ALA	0	0.000	-0.010	27.801	0.301	0.301	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.837	-0.904	27.125	-9.590	-9.590	0.000	0.000	0.000	0.000
43	A	64	PRO	0	-0.015	-0.002	29.861	0.013	0.013	0.000	0.000	0.000	0.000
44	A	65	ALA	0	-0.019	-0.022	29.905	-0.338	-0.338	0.000	0.000	0.000	0.000
45	A	66	GLY	0	0.027	0.003	28.780	0.269	0.269	0.000	0.000	0.000	0.000
46	A	67	THR	0	-0.038	-0.007	26.328	0.047	0.047	0.000	0.000	0.000	0.000
47	A	68	PHE	0	-0.014	-0.016	22.538	-0.349	-0.349	0.000	0.000	0.000	0.000
48	A	69	LEU	0	0.041	0.034	17.892	0.218	0.218	0.000	0.000	0.000	0.000
49	A	70	ILE	0	-0.026	-0.013	15.424	-0.445	-0.445	0.000	0.000	0.000	0.000
50	A	71	ARG	1	0.901	0.971	11.972	19.300	19.300	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.707	-0.819	8.715	-21.696	-21.696	0.000	0.000	0.000	0.000
52	A	73	SER	0	-0.078	-0.034	7.513	1.647	1.647	0.000	0.000	0.000	0.000
53	A	74	SER	0	0.021	-0.003	7.181	-0.428	-0.428	0.000	0.000	0.000	0.000
54	A	75	ASP	-1	-0.864	-0.914	6.372	-36.929	-36.929	0.000	0.000	0.000	0.000
57	A	78	HIS	0	-0.066	-0.019	6.444	2.456	2.456	0.000	0.000	0.000	0.000
58	A	79	PHE	0	0.039	0.025	6.382	-1.869	-1.869	0.000	0.000	0.000	0.000
59	A	80	PHE	0	0.040	0.025	8.097	0.274	0.274	0.000	0.000	0.000	0.000
60	A	81	THR	0	-0.075	-0.055	11.371	-0.796	-0.796	0.000	0.000	0.000	0.000
61	A	82	LEU	0	0.027	0.039	13.931	0.382	0.382	0.000	0.000	0.000	0.000
62	A	83	SER	0	-0.014	-0.020	17.460	-0.490	-0.490	0.000	0.000	0.000	0.000
63	A	84	VAL	0	0.042	0.010	19.330	0.355	0.355	0.000	0.000	0.000	0.000
64	A	85	LYS	1	0.863	0.954	23.141	9.979	9.979	0.000	0.000	0.000	0.000
65	A	86	THR	0	-0.059	-0.043	25.840	0.263	0.263	0.000	0.000	0.000	0.000
66	A	87	GLN	0	0.062	0.009	28.426	0.036	0.036	0.000	0.000	0.000	0.000
67	A	88	SER	0	-0.039	-0.051	28.150	0.041	0.041	0.000	0.000	0.000	0.000
68	A	89	GLY	0	0.024	0.022	27.567	-0.196	-0.196	0.000	0.000	0.000	0.000
69	A	90	THR	0	-0.036	-0.014	21.802	0.131	0.131	0.000	0.000	0.000	0.000
70	A	91	LYS	1	0.832	0.931	21.692	11.532	11.532	0.000	0.000	0.000	0.000
71	A	92	ASN	0	0.025	0.009	16.361	-0.569	-0.569	0.000	0.000	0.000	0.000
72	A	93	LEU	0	0.009	0.013	17.593	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	94	ARG	1	0.839	0.897	9.902	24.648	24.648	0.000	0.000	0.000	0.000
74	A	95	ILE	0	0.019	0.008	13.198	0.900	0.900	0.000	0.000	0.000	0.000
75	A	96	GLN	0	0.025	0.022	12.000	-2.829	-2.829	0.000	0.000	0.000	0.000
76	A	97	CYS	0	-0.027	-0.017	10.954	1.661	1.661	0.000	0.000	0.000	0.000
77	A	98	GLU	-1	-0.877	-0.934	11.644	-22.201	-22.201	0.000	0.000	0.000	0.000
78	A	99	GLY	0	0.040	0.024	14.275	1.187	1.187	0.000	0.000	0.000	0.000
79	A	100	GLY	0	-0.006	0.003	15.458	0.897	0.897	0.000	0.000	0.000	0.000
80	A	101	SER	0	-0.024	-0.019	16.698	1.207	1.207	0.000	0.000	0.000	0.000
81	A	102	PHE	0	0.005	0.002	12.819	-0.885	-0.885	0.000	0.000	0.000	0.000
82	A	103	SER	0	0.028	0.008	16.296	0.944	0.944	0.000	0.000	0.000	0.000
83	A	104	LEU	0	0.019	0.012	16.497	-1.017	-1.017	0.000	0.000	0.000	0.000
84	A	105	GLN	0	0.017	0.000	13.963	-1.174	-1.174	0.000	0.000	0.000	0.000
85	A	106	SER	0	0.010	0.009	17.438	0.739	0.739	0.000	0.000	0.000	0.000
86	A	107	ASP	-1	-0.789	-0.873	20.385	-12.746	-12.746	0.000	0.000	0.000	0.000
87	A	108	PRO	0	0.014	-0.006	22.391	0.191	0.191	0.000	0.000	0.000	0.000
88	A	109	ARG	1	0.845	0.903	24.689	11.620	11.620	0.000	0.000	0.000	0.000
89	A	110	SER	0	-0.073	-0.037	25.596	0.473	0.473	0.000	0.000	0.000	0.000
90	A	111	THR	0	0.016	0.003	27.541	-0.115	-0.115	0.000	0.000	0.000	0.000
91	A	112	GLN	0	-0.016	0.009	29.243	0.173	0.173	0.000	0.000	0.000	0.000
92	A	113	PRO	0	0.034	0.026	26.010	-0.415	-0.415	0.000	0.000	0.000	0.000
93	A	114	VAL	0	0.003	-0.003	20.543	0.197	0.197	0.000	0.000	0.000	0.000
94	A	115	PRO	0	-0.014	-0.003	23.441	-0.218	-0.218	0.000	0.000	0.000	0.000
95	A	116	ARG	1	0.830	0.896	16.262	16.124	16.124	0.000	0.000	0.000	0.000
96	A	117	PHE	0	-0.003	0.002	20.362	0.627	0.627	0.000	0.000	0.000	0.000
97	A	118	ASP	-1	-0.783	-0.872	19.709	-12.901	-12.901	0.000	0.000	0.000	0.000
98	A	119	CYS	0	-0.006	-0.010	19.385	-0.525	-0.525	0.000	0.000	0.000	0.000
99	A	120	VAL	0	0.030	0.018	15.812	0.419	0.419	0.000	0.000	0.000	0.000
100	A	121	LEU	0	0.041	0.008	18.542	0.210	0.210	0.000	0.000	0.000	0.000
101	A	122	LYS	1	0.825	0.888	21.827	11.919	11.919	0.000	0.000	0.000	0.000
102	A	123	LEU	0	-0.038	0.009	17.960	0.284	0.284	0.000	0.000	0.000	0.000
103	A	124	VAL	0	-0.020	-0.014	20.757	0.219	0.219	0.000	0.000	0.000	0.000
104	A	125	HIS	0	0.008	-0.006	23.068	0.282	0.282	0.000	0.000	0.000	0.000
105	A	126	HIS	0	0.001	0.017	25.278	0.378	0.378	0.000	0.000	0.000	0.000
106	A	127	TYR	0	0.019	-0.001	21.926	0.066	0.066	0.000	0.000	0.000	0.000
107	A	128	MET	0	-0.020	0.005	27.421	0.227	0.227	0.000	0.000	0.000	0.000
108	A	129	GLY	0	0.039	0.031	28.796	0.268	0.268	0.000	0.000	0.000	0.000
109	A	130	SER	0	-0.023	0.001	30.221	0.348	0.348	0.000	0.000	0.000	0.000
110	A	131	GLY	0	0.036	0.001	31.673	0.134	0.134	0.000	0.000	0.000	0.000
111	A	132	SER	0	-0.031	-0.015	33.063	0.244	0.244	0.000	0.000	0.000	0.000
112	A	133	GLY	0	0.059	0.041	35.018	0.165	0.165	0.000	0.000	0.000	0.000
113	A	134	SER	0	0.040	0.018	34.761	-0.280	-0.280	0.000	0.000	0.000	0.000
114	A	135	GLY	0	0.040	0.022	33.193	-0.041	-0.041	0.000	0.000	0.000	0.000
115	A	136	SER	0	-0.014	-0.005	30.719	-0.286	-0.286	0.000	0.000	0.000	0.000
116	A	137	ARG	1	0.838	0.891	31.236	8.259	8.259	0.000	0.000	0.000	0.000
117	A	141	ALA	0	-0.016	0.000	32.680	0.106	0.106	0.000	0.000	0.000	0.000
118	A	142	TYR	0	0.002	0.007	27.292	-0.260	-0.260	0.000	0.000	0.000	0.000
119	A	143	TYR	0	0.037	0.008	28.021	0.304	0.304	0.000	0.000	0.000	0.000
120	A	144	ILE	0	-0.032	-0.005	24.890	-0.542	-0.542	0.000	0.000	0.000	0.000
121	A	145	TYR	0	0.023	0.002	18.287	0.284	0.284	0.000	0.000	0.000	0.000
122	A	146	SER	0	0.005	0.000	21.926	0.200	0.200	0.000	0.000	0.000	0.000
123	A	147	GLY	0	0.026	0.020	24.089	-0.068	-0.068	0.000	0.000	0.000	0.000
124	A	148	GLY	0	0.017	0.020	27.703	-0.028	-0.028	0.000	0.000	0.000	0.000
125	A	149	GLU	-1	-0.814	-0.887	30.350	-9.716	-9.716	0.000	0.000	0.000	0.000
126	A	150	LYS	1	0.810	0.939	29.583	9.717	9.717	0.000	0.000	0.000	0.000
127	A	151	ILE	0	0.061	0.026	29.253	0.165	0.165	0.000	0.000	0.000	0.000
128	A	152	PRO	0	0.020	-0.003	29.765	-0.352	-0.352	0.000	0.000	0.000	0.000
129	A	153	LEU	0	-0.040	-0.015	24.001	-0.152	-0.152	0.000	0.000	0.000	0.000
130	A	154	VAL	0	0.001	-0.001	27.885	0.220	0.220	0.000	0.000	0.000	0.000
131	A	155	LEU	0	-0.033	-0.019	24.090	-0.352	-0.352	0.000	0.000	0.000	0.000
132	A	156	SER	0	-0.061	-0.040	28.078	0.383	0.383	0.000	0.000	0.000	0.000
133	A	157	ARG	1	0.960	0.979	29.081	9.255	9.255	0.000	0.000	0.000	0.000
134	A	158	PRO	0	0.026	0.023	25.281	-0.248	-0.248	0.000	0.000	0.000	0.000
135	A	159	LEU	0	0.003	-0.001	22.976	0.309	0.309	0.000	0.000	0.000	0.000
136	A	160	SER	0	-0.043	-0.034	23.456	-0.519	-0.519	0.000	0.000	0.000	0.000
137	A	161	SER	-1	-0.916	-0.940	21.457	-11.472	-11.472	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:LEU)