FMO DATABASE

FMODB ID: 9RZZ2

Calculation Name: 3TEK-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3TEK

Chain ID: A

ChEMBL ID:

UniProt ID: H0USY6

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1317840.228371
FMO2-HF: Nuclear repulsion	1262060.830401
FMO2-HF: Total energy	-55779.39797
FMO2-MP2: Total energy	-55946.292828

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:10:ARG)

Summations of interaction energy for fragment #1(A:10:ARG)

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.
27.158	34.79	1.439	-3.237	-5.833	-0.031

Interaction energy analysis for fragmet #1(A:10:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.783 / q_NPA : 1.872

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	12	GLU	-1	-0.898	-0.920	2.605	-81.593	-78.986	0.248	-1.082	-1.773	-0.008
4	A	13	VAL	0	0.041	0.007	4.212	4.989	5.084	0.000	-0.024	-0.071	0.000
22	A	31	ASN	0	0.025	-0.010	3.072	-9.308	-7.837	0.167	-0.714	-0.924	-0.007
23	A	32	THR	0	0.019	0.005	5.173	-4.488	-4.459	-0.001	-0.006	-0.022	0.000
24	A	33	GLY	0	-0.007	-0.012	2.590	-3.015	-2.459	0.276	-0.259	-0.572	-0.003
25	A	34	LYS	1	0.869	0.953	2.757	77.845	79.427	0.093	-0.614	-1.060	-0.007
26	A	35	THR	0	0.020	0.003	4.180	5.404	5.467	-0.001	-0.022	-0.040	0.000
108	A	117	MET	0	-0.087	-0.027	3.289	-18.506	-17.277	0.657	-0.516	-1.371	-0.006
5	A	14	ARG	1	0.868	0.926	6.640	62.815	62.815	0.000	0.000	0.000	0.000
6	A	15	SER	0	0.010	0.008	10.478	1.864	1.864	0.000	0.000	0.000	0.000
7	A	16	GLU	-1	-0.794	-0.873	14.162	-33.916	-33.916	0.000	0.000	0.000	0.000
8	A	17	LEU	0	0.001	0.007	17.678	0.385	0.385	0.000	0.000	0.000	0.000
9	A	18	ILE	0	-0.004	0.005	20.621	0.333	0.333	0.000	0.000	0.000	0.000
10	A	19	THR	0	-0.014	-0.006	23.213	0.523	0.523	0.000	0.000	0.000	0.000
11	A	20	LYS	1	0.956	0.983	27.011	19.844	19.844	0.000	0.000	0.000	0.000
12	A	21	GLY	0	0.014	0.006	29.386	0.407	0.407	0.000	0.000	0.000	0.000
13	A	22	GLU	-1	-0.913	-0.969	31.642	-17.152	-17.152	0.000	0.000	0.000	0.000
14	A	23	LYS	1	0.908	0.974	28.675	18.133	18.133	0.000	0.000	0.000	0.000
15	A	24	LYS	1	0.937	0.956	25.151	21.186	21.186	0.000	0.000	0.000	0.000
16	A	25	LEU	0	0.020	0.011	22.641	-0.027	-0.027	0.000	0.000	0.000	0.000
17	A	26	VAL	0	0.012	0.003	17.032	-0.368	-0.368	0.000	0.000	0.000	0.000
18	A	27	LEU	0	-0.023	0.009	15.837	-0.086	-0.086	0.000	0.000	0.000	0.000
19	A	28	ILE	0	0.005	-0.010	11.853	-1.315	-1.315	0.000	0.000	0.000	0.000
20	A	29	ARG	1	0.792	0.880	10.062	39.248	39.248	0.000	0.000	0.000	0.000
21	A	30	TRP	0	0.010	0.003	7.404	-1.382	-1.382	0.000	0.000	0.000	0.000
27	A	36	SER	0	0.105	0.046	7.742	1.551	1.551	0.000	0.000	0.000	0.000
28	A	37	ALA	0	0.046	0.035	11.391	0.225	0.225	0.000	0.000	0.000	0.000
29	A	38	GLY	0	-0.006	-0.007	14.302	1.428	1.428	0.000	0.000	0.000	0.000
30	A	39	ARG	1	0.840	0.907	10.082	48.672	48.672	0.000	0.000	0.000	0.000
31	A	40	LEU	0	-0.003	0.013	10.060	0.899	0.899	0.000	0.000	0.000	0.000
32	A	41	PHE	0	0.086	0.016	12.829	1.190	1.190	0.000	0.000	0.000	0.000
33	A	42	GLY	0	-0.033	-0.004	16.384	2.186	2.186	0.000	0.000	0.000	0.000
34	A	43	ARG	1	0.936	0.958	18.332	25.152	25.152	0.000	0.000	0.000	0.000
35	A	44	TYR	0	0.005	-0.003	16.099	1.212	1.212	0.000	0.000	0.000	0.000
36	A	45	GLY	0	0.049	0.038	14.230	-1.793	-1.793	0.000	0.000	0.000	0.000
37	A	46	PRO	0	-0.033	-0.028	13.321	2.208	2.208	0.000	0.000	0.000	0.000
38	A	47	GLY	0	-0.017	0.005	16.195	0.730	0.730	0.000	0.000	0.000	0.000
39	A	48	GLY	0	0.060	0.025	19.943	0.051	0.051	0.000	0.000	0.000	0.000
40	A	49	ARG	1	0.884	0.938	18.763	27.854	27.854	0.000	0.000	0.000	0.000
41	A	50	PRO	0	0.021	0.025	16.354	-1.271	-1.271	0.000	0.000	0.000	0.000
42	A	51	GLU	-1	-0.865	-0.934	10.392	-49.867	-49.867	0.000	0.000	0.000	0.000
43	A	52	PHE	0	0.036	0.017	12.673	-1.781	-1.781	0.000	0.000	0.000	0.000
44	A	53	PHE	0	0.020	0.016	13.679	-1.111	-1.111	0.000	0.000	0.000	0.000
45	A	54	LYS	1	0.916	0.967	13.604	35.156	35.156	0.000	0.000	0.000	0.000
46	A	55	LEU	0	-0.021	-0.006	8.427	-0.209	-0.209	0.000	0.000	0.000	0.000
47	A	56	LEU	0	0.045	0.036	11.740	-0.757	-0.757	0.000	0.000	0.000	0.000
48	A	57	PHE	0	-0.006	-0.010	13.513	0.860	0.860	0.000	0.000	0.000	0.000
49	A	58	GLY	0	0.008	0.014	13.286	1.071	1.071	0.000	0.000	0.000	0.000
50	A	59	ALA	0	0.007	-0.001	10.413	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	60	VAL	0	-0.001	0.012	12.093	0.646	0.646	0.000	0.000	0.000	0.000
52	A	61	ALA	0	0.023	0.010	15.698	0.891	0.891	0.000	0.000	0.000	0.000
53	A	62	GLY	0	-0.015	-0.011	13.715	0.919	0.919	0.000	0.000	0.000	0.000
54	A	63	SER	0	0.010	-0.021	13.442	0.238	0.238	0.000	0.000	0.000	0.000
55	A	64	LEU	0	-0.019	-0.004	15.413	1.303	1.303	0.000	0.000	0.000	0.000
56	A	65	ARG	1	0.795	0.878	16.545	33.276	33.276	0.000	0.000	0.000	0.000
57	A	66	GLU	-1	-0.985	-0.986	14.298	-37.300	-37.300	0.000	0.000	0.000	0.000
58	A	67	GLN	0	-0.042	-0.019	16.714	2.418	2.418	0.000	0.000	0.000	0.000
59	A	68	PHE	0	0.003	-0.007	20.339	1.182	1.182	0.000	0.000	0.000	0.000
60	A	69	GLY	0	0.041	0.039	21.910	1.120	1.120	0.000	0.000	0.000	0.000
61	A	70	PRO	0	-0.026	-0.031	22.796	-0.588	-0.588	0.000	0.000	0.000	0.000
62	A	71	ASP	-1	-0.833	-0.905	24.870	-21.181	-21.181	0.000	0.000	0.000	0.000
63	A	72	GLY	0	0.030	0.023	22.069	0.163	0.163	0.000	0.000	0.000	0.000
64	A	73	GLU	-1	-0.817	-0.901	20.992	-29.199	-29.199	0.000	0.000	0.000	0.000
65	A	74	ASN	0	-0.056	-0.041	23.441	0.183	0.183	0.000	0.000	0.000	0.000
66	A	75	ILE	0	-0.015	-0.003	23.705	0.342	0.342	0.000	0.000	0.000	0.000
67	A	76	PHE	0	0.006	-0.005	19.391	-0.210	-0.210	0.000	0.000	0.000	0.000
68	A	77	ASN	0	-0.055	-0.047	22.822	-0.104	-0.104	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.850	0.925	25.504	21.300	21.300	0.000	0.000	0.000	0.000
70	A	79	ILE	0	0.039	0.027	21.306	0.365	0.365	0.000	0.000	0.000	0.000
71	A	80	ARG	1	0.927	0.991	21.809	24.589	24.589	0.000	0.000	0.000	0.000
72	A	81	ASP	-1	-0.956	-1.001	23.904	-21.677	-21.677	0.000	0.000	0.000	0.000
73	A	82	SER	0	-0.001	0.009	26.287	0.680	0.680	0.000	0.000	0.000	0.000
74	A	83	GLU	-1	-0.903	-0.973	27.053	-20.346	-20.346	0.000	0.000	0.000	0.000
75	A	84	LYS	1	0.972	0.999	27.009	20.083	20.083	0.000	0.000	0.000	0.000
76	A	85	PHE	0	0.033	0.045	18.928	-1.101	-1.101	0.000	0.000	0.000	0.000
77	A	86	ARG	1	0.796	0.893	22.847	22.386	22.386	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.868	-0.915	23.867	-22.577	-22.577	0.000	0.000	0.000	0.000
79	A	88	THR	0	0.018	-0.006	22.762	-1.008	-1.008	0.000	0.000	0.000	0.000
80	A	89	SER	0	-0.077	-0.054	19.353	-1.522	-1.522	0.000	0.000	0.000	0.000
81	A	90	ARG	1	0.892	0.938	19.684	23.852	23.852	0.000	0.000	0.000	0.000
82	A	91	GLU	-1	-0.845	-0.925	21.770	-23.431	-23.431	0.000	0.000	0.000	0.000
83	A	92	LEU	0	-0.021	0.000	15.307	-0.743	-0.743	0.000	0.000	0.000	0.000
84	A	93	PHE	0	-0.094	-0.045	16.740	-1.244	-1.244	0.000	0.000	0.000	0.000
85	A	94	ASP	-1	-0.899	-0.961	18.312	-26.037	-26.037	0.000	0.000	0.000	0.000
86	A	95	GLY	0	0.005	0.004	20.147	0.204	0.204	0.000	0.000	0.000	0.000
87	A	96	LEU	0	0.008	-0.011	13.211	-0.638	-0.638	0.000	0.000	0.000	0.000
88	A	97	LYS	1	0.916	0.972	16.406	26.578	26.578	0.000	0.000	0.000	0.000
89	A	98	LYS	1	0.854	0.911	18.012	23.075	23.075	0.000	0.000	0.000	0.000
90	A	99	TRP	0	0.033	0.023	12.970	-1.471	-1.471	0.000	0.000	0.000	0.000
91	A	100	PHE	0	-0.006	-0.017	13.485	-0.306	-0.306	0.000	0.000	0.000	0.000
92	A	101	PHE	0	-0.044	-0.045	16.864	-0.200	-0.200	0.000	0.000	0.000	0.000
93	A	102	GLU	-1	-0.842	-0.900	20.136	-22.386	-22.386	0.000	0.000	0.000	0.000
94	A	103	GLU	-1	-0.904	-0.949	19.688	-26.626	-26.626	0.000	0.000	0.000	0.000
95	A	104	ALA	0	-0.038	-0.022	15.576	-0.041	-0.041	0.000	0.000	0.000	0.000
96	A	105	VAL	0	-0.019	-0.012	17.656	-0.272	-0.272	0.000	0.000	0.000	0.000
97	A	106	PRO	0	0.022	0.006	19.144	0.118	0.118	0.000	0.000	0.000	0.000
98	A	107	ARG	1	0.899	0.962	19.107	29.283	29.283	0.000	0.000	0.000	0.000
99	A	108	TYR	0	-0.045	-0.038	15.697	-0.019	-0.019	0.000	0.000	0.000	0.000
100	A	109	ASN	0	-0.053	-0.012	18.829	0.738	0.738	0.000	0.000	0.000	0.000
101	A	110	LEU	0	-0.036	0.003	14.806	-0.765	-0.765	0.000	0.000	0.000	0.000
102	A	111	GLU	-1	-0.877	-0.939	18.144	-24.962	-24.962	0.000	0.000	0.000	0.000
103	A	112	ARG	1	0.896	0.929	17.847	23.732	23.732	0.000	0.000	0.000	0.000
104	A	113	GLY	0	-0.039	-0.026	16.188	0.558	0.558	0.000	0.000	0.000	0.000
105	A	114	ASP	-1	-0.811	-0.880	14.051	-36.894	-36.894	0.000	0.000	0.000	0.000
106	A	115	ILE	0	-0.098	-0.055	8.138	-2.206	-2.206	0.000	0.000	0.000	0.000
107	A	116	PHE	0	0.022	-0.002	8.653	0.698	0.698	0.000	0.000	0.000	0.000
109	A	118	ILE	0	0.041	0.030	6.276	3.559	3.559	0.000	0.000	0.000	0.000
110	A	119	SER	0	-0.050	-0.022	6.756	-7.204	-7.204	0.000	0.000	0.000	0.000
111	A	120	THR	0	0.030	0.000	8.203	4.236	4.236	0.000	0.000	0.000	0.000
112	A	121	GLU	-1	-0.831	-0.919	10.995	-39.666	-39.666	0.000	0.000	0.000	0.000
113	A	122	LEU	0	-0.016	-0.013	13.637	1.539	1.539	0.000	0.000	0.000	0.000
114	A	123	VAL	0	0.013	0.005	16.048	-0.515	-0.515	0.000	0.000	0.000	0.000
115	A	124	LEU	0	-0.009	0.007	18.854	0.550	0.550	0.000	0.000	0.000	0.000
116	A	125	ASP	-1	-0.797	-0.894	20.516	-21.541	-21.541	0.000	0.000	0.000	0.000
117	A	126	PRO	0	0.012	0.004	23.314	-0.099	-0.099	0.000	0.000	0.000	0.000
118	A	127	ASP	-1	-0.906	-0.935	24.699	-19.853	-19.853	0.000	0.000	0.000	0.000
119	A	128	THR	0	-0.047	-0.046	27.533	0.218	0.218	0.000	0.000	0.000	0.000
120	A	129	GLY	0	0.014	0.010	24.321	0.210	0.210	0.000	0.000	0.000	0.000
121	A	130	GLU	-1	-0.908	-0.951	23.954	-22.042	-22.042	0.000	0.000	0.000	0.000
122	A	131	LEU	0	-0.019	-0.015	17.121	-0.902	-0.902	0.000	0.000	0.000	0.000
123	A	132	LEU	0	0.038	0.021	21.053	0.106	0.106	0.000	0.000	0.000	0.000
124	A	133	TRP	0	-0.034	-0.025	15.370	-0.553	-0.553	0.000	0.000	0.000	0.000
125	A	134	ASN	0	-0.034	-0.020	16.839	2.377	2.377	0.000	0.000	0.000	0.000
126	A	135	ARG	1	0.983	0.985	17.081	24.440	24.440	0.000	0.000	0.000	0.000
127	A	136	ASP	-1	-0.837	-0.903	17.283	-28.454	-28.454	0.000	0.000	0.000	0.000
128	A	137	LYS	1	0.878	0.948	14.157	33.256	33.256	0.000	0.000	0.000	0.000
129	A	138	THR	0	-0.057	-0.028	12.917	-3.755	-3.755	0.000	0.000	0.000	0.000
130	A	139	GLN	0	-0.018	-0.002	10.944	2.912	2.912	0.000	0.000	0.000	0.000
131	A	140	LEU	0	-0.010	-0.006	9.944	-3.507	-3.507	0.000	0.000	0.000	0.000
132	A	141	ILE	0	-0.012	0.000	6.746	0.113	0.113	0.000	0.000	0.000	0.000
133	A	142	TYR	0	0.036	-0.003	8.566	-4.165	-4.165	0.000	0.000	0.000	0.000
134	A	143	TRP	0	-0.019	-0.025	5.428	-4.570	-4.570	0.000	0.000	0.000	0.000
135	A	144	ILE	0	0.043	0.026	12.080	1.636	1.636	0.000	0.000	0.000	0.000
136	A	145	ARG	1	0.809	0.869	15.878	25.807	25.807	0.000	0.000	0.000	0.000
137	A	146	SER	0	0.031	-0.001	18.511	0.378	0.378	0.000	0.000	0.000	0.000
138	A	147	ASP	-1	-0.849	-0.880	19.722	-26.173	-26.173	0.000	0.000	0.000	0.000
139	A	148	ARG	0	0.025	0.031	20.480	-2.501	-2.501	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:ARG)