FMO DATABASE

FMODB ID: VV7M1

Calculation Name: 2DM0-A-Other547

Preferred Name: Tyrosine-protein kinase TXK

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DM0

Chain ID: A

ChEMBL ID: CHEMBL4367

UniProt ID: P42681

Base Structure: SolutionNMR

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	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1043598.128737
FMO2-HF: Nuclear repulsion	994033.310546
FMO2-HF: Total energy	-49564.818191
FMO2-MP2: Total energy	-49710.231581

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.
65.503	66.71	-0.015	-0.538	-0.654	-0.002

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 : 0.877 / q_NPA : 0.925

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	0.058	0.030	3.843	2.962	4.169	-0.015	-0.538	-0.654	-0.002
4	A	4	GLY	0	0.000	0.016	6.717	0.911	0.911	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.004	-0.007	10.364	-0.926	-0.926	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.013	0.005	13.051	0.881	0.881	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.041	0.027	16.607	0.323	0.323	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.030	-0.017	17.784	-0.652	-0.652	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.909	0.956	15.318	18.281	18.281	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.079	0.035	18.119	0.584	0.584	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.018	-0.007	17.690	0.710	0.710	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.031	0.019	19.574	-1.131	-1.131	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.008	-0.008	18.918	0.356	0.356	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.895	-0.943	21.694	-14.049	-14.049	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.017	0.021	24.042	0.323	0.323	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.020	-0.001	25.109	0.540	0.540	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.903	-0.939	27.252	-10.149	-10.149	0.000	0.000	0.000	0.000
18	A	18	TRP	0	0.061	0.024	23.363	-0.432	-0.432	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.082	-0.073	17.482	-0.501	-0.501	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.008	0.005	23.417	-0.301	-0.301	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.865	0.917	19.212	13.658	13.658	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.039	-0.030	18.540	0.338	0.338	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.048	0.050	19.626	0.395	0.395	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.016	-0.020	18.906	-1.217	-1.217	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.986	0.987	20.292	14.558	14.558	0.000	0.000	0.000	0.000
26	A	26	ASN	0	0.041	0.016	21.921	0.392	0.392	0.000	0.000	0.000	0.000
27	A	27	GLN	0	0.043	0.019	23.922	0.412	0.412	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.014	0.001	22.772	0.306	0.306	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.849	-0.940	24.926	-11.685	-11.685	0.000	0.000	0.000	0.000
30	A	30	HIS	0	-0.004	0.002	27.636	0.303	0.303	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.028	0.009	26.506	0.327	0.327	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.037	-0.013	27.481	0.350	0.350	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.873	0.926	31.288	10.008	10.008	0.000	0.000	0.000	0.000
34	A	34	GLN	0	0.011	0.010	32.882	0.053	0.053	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.852	-0.914	34.278	-8.512	-8.512	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.042	-0.021	35.573	0.262	0.262	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.868	0.945	36.352	8.630	8.630	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.825	-0.902	35.820	-8.765	-8.765	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.017	0.002	33.567	0.149	0.149	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.003	0.021	33.008	-0.141	-0.141	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.027	-0.013	27.178	-0.311	-0.311	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.023	0.047	24.797	0.048	0.048	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.011	-0.015	20.525	-0.353	-0.353	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.908	0.965	16.867	17.065	17.065	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.757	-0.887	14.395	-18.942	-18.942	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.043	-0.017	12.614	0.981	0.981	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.890	0.935	11.865	18.765	18.765	0.000	0.000	0.000	0.000
48	A	48	HIS	0	0.027	0.026	9.072	-0.818	-0.818	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.031	0.009	5.665	-4.787	-4.787	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.012	0.024	8.065	3.332	3.332	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.037	-0.024	10.033	0.678	0.678	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.010	0.007	12.884	0.145	0.145	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.061	-0.041	16.625	-0.301	-0.301	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.028	0.026	19.163	0.227	0.227	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.041	-0.026	22.962	0.067	0.067	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.042	0.006	25.117	0.240	0.240	0.000	0.000	0.000	0.000
57	A	57	PHE	0	0.037	0.025	28.825	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.079	-0.047	31.495	0.225	0.225	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.038	0.017	34.169	0.267	0.267	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.019	-0.004	36.600	-0.063	-0.063	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.962	0.964	38.728	8.097	8.097	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.960	0.974	41.595	6.795	6.795	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.003	0.007	41.642	0.100	0.100	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.001	0.007	42.535	0.051	0.051	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.895	-0.942	37.916	-8.178	-8.178	0.000	0.000	0.000	0.000
66	A	66	ALA	0	-0.014	-0.011	34.190	-0.032	-0.032	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.020	-0.003	32.877	-0.128	-0.128	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.013	0.017	27.187	0.104	0.104	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.901	0.964	27.160	10.164	10.164	0.000	0.000	0.000	0.000
70	A	70	HIS	0	-0.010	-0.001	21.774	-0.377	-0.377	0.000	0.000	0.000	0.000
71	A	71	TYR	0	0.030	0.007	22.441	-0.160	-0.160	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.022	-0.014	14.612	-0.998	-0.998	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.024	-0.009	17.499	0.429	0.429	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.876	0.954	14.939	15.890	15.890	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.943	0.970	11.931	24.869	24.869	0.000	0.000	0.000	0.000
76	A	76	ASN	0	-0.005	-0.007	14.604	-1.148	-1.148	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.826	-0.908	15.334	-17.549	-17.549	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.040	-0.022	16.396	-0.323	-0.323	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.063	-0.030	15.502	0.282	0.282	0.000	0.000	0.000	0.000
80	A	80	GLN	0	0.033	0.020	16.556	0.208	0.208	0.000	0.000	0.000	0.000
81	A	81	TRP	0	-0.017	-0.014	12.980	-1.054	-1.054	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.035	-0.043	17.685	0.794	0.794	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.017	0.000	19.708	-0.677	-0.677	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.015	-0.001	22.194	-0.153	-0.153	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.815	-0.899	20.211	-15.115	-15.115	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.897	0.961	23.369	11.466	11.466	0.000	0.000	0.000	0.000
87	A	87	HIS	0	0.034	0.025	26.323	-0.129	-0.129	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.015	-0.016	21.629	-0.484	-0.484	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.021	0.016	22.183	0.527	0.527	0.000	0.000	0.000	0.000
90	A	90	GLN	0	0.043	0.023	21.294	-0.929	-0.929	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.013	-0.023	20.472	-1.060	-1.060	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.034	-0.018	17.478	0.452	0.452	0.000	0.000	0.000	0.000
93	A	93	PRO	0	0.011	-0.012	21.259	0.362	0.362	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.828	-0.903	24.516	-12.117	-12.117	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.040	0.000	21.715	0.384	0.384	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.011	-0.021	24.256	0.451	0.451	0.000	0.000	0.000	0.000
97	A	97	TRP	0	-0.008	0.012	27.186	0.426	0.426	0.000	0.000	0.000	0.000
98	A	98	TYR	0	0.062	0.026	29.408	0.340	0.340	0.000	0.000	0.000	0.000
99	A	99	HIS	0	-0.067	-0.034	26.333	0.200	0.200	0.000	0.000	0.000	0.000
100	A	100	GLN	0	0.018	-0.001	30.526	0.276	0.276	0.000	0.000	0.000	0.000
101	A	101	HIS	0	0.030	0.034	33.058	0.418	0.418	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.064	-0.054	33.007	0.509	0.509	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.027	0.025	31.168	-0.241	-0.241	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.017	-0.005	30.189	-0.285	-0.285	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.028	-0.008	28.667	-0.225	-0.225	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.046	-0.019	28.853	-0.220	-0.220	0.000	0.000	0.000	0.000
107	A	107	MET	0	-0.025	0.002	26.193	-0.125	-0.125	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.028	-0.034	31.190	0.216	0.216	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.884	0.940	32.585	8.111	8.111	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.032	-0.013	28.641	0.144	0.144	0.000	0.000	0.000	0.000
111	A	111	ARG	1	0.883	0.942	33.153	8.514	8.514	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.026	0.005	34.592	0.246	0.246	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.025	0.005	31.165	-0.294	-0.294	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.015	0.008	29.960	0.188	0.188	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.088	0.032	29.338	-0.459	-0.459	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.060	-0.041	25.461	0.038	0.038	0.000	0.000	0.000	0.000
117	A	117	MET	0	-0.042	-0.006	29.183	0.145	0.145	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.016	0.009	32.310	0.142	0.142	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.031	-0.006	33.604	0.221	0.221	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.037	-0.001	37.358	0.133	0.133	0.000	0.000	0.000	0.000
121	A	121	GLY	0	-0.018	-0.012	37.148	-0.160	-0.160	0.000	0.000	0.000	0.000
122	A	122	PRO	0	-0.022	0.009	38.154	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.003	-0.002	36.811	-0.237	-0.237	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.071	-0.049	35.867	0.201	0.201	0.000	0.000	0.000	0.000
125	A	125	GLY	-1	-0.906	-0.936	37.862	-7.513	-7.513	0.000	0.000	0.000	0.000

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