FMO DATABASE

FMODB ID: 19N5Z

Calculation Name: 1X6C-A-Other547

Preferred Name: Protein-tyrosine phosphatase 1C

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X6C

Chain ID: A

ChEMBL ID: CHEMBL3166

UniProt ID: P29350

Base Structure: SolutionNMR

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-884466.26814
FMO2-HF: Nuclear repulsion	840263.775063
FMO2-HF: Total energy	-44202.493077
FMO2-MP2: Total energy	-44331.667757

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.
-42.474	-40.325	0.522	-1.278	-1.392	-0.011

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 : 0.859 / q_NPA : 0.919

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	0.060	0.034	3.799	4.879	5.715	0.002	-0.348	-0.489	-0.001
4	A	4	GLY	0	0.018	0.005	2.731	-18.521	-17.256	0.521	-0.930	-0.857	-0.010
5	A	5	SER	0	-0.028	-0.036	5.190	2.769	2.817	-0.001	0.000	-0.046	0.000
6	A	6	SER	0	-0.006	-0.002	7.970	0.217	0.217	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.014	0.019	10.801	0.538	0.538	0.000	0.000	0.000	0.000
8	A	8	TRP	0	0.047	0.014	11.593	0.606	0.606	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.067	-0.048	15.331	0.985	0.985	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.007	-0.011	16.379	-0.228	-0.228	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.028	0.028	18.802	0.554	0.554	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.007	0.009	20.966	0.331	0.331	0.000	0.000	0.000	0.000
13	A	13	MET	0	0.041	0.027	20.396	0.434	0.434	0.000	0.000	0.000	0.000
14	A	14	SER	0	0.061	0.021	24.660	0.348	0.348	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.007	-0.008	27.322	-0.261	-0.261	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.051	0.017	28.890	-0.133	-0.133	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.028	0.012	25.198	0.335	0.335	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.015	0.006	24.477	-0.266	-0.266	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.838	-0.924	25.181	-10.473	-10.473	0.000	0.000	0.000	0.000
20	A	20	THR	0	0.001	0.004	27.086	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.008	-0.007	21.171	-0.102	-0.102	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.015	0.006	21.254	-0.602	-0.602	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.070	-0.042	23.530	0.024	0.024	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.037	-0.012	24.117	0.092	0.092	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.861	0.945	16.308	17.671	17.671	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.012	0.009	22.199	-0.142	-0.142	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.895	-0.961	17.650	-17.823	-17.823	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.013	0.037	21.856	-0.045	-0.045	0.000	0.000	0.000	0.000
29	A	29	TRP	0	-0.016	-0.004	22.292	-0.719	-0.719	0.000	0.000	0.000	0.000
30	A	30	THR	0	-0.007	-0.016	18.138	-1.000	-1.000	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.007	0.006	15.992	0.685	0.685	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.022	-0.013	18.548	-1.141	-1.141	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.007	0.003	19.238	0.809	0.809	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.878	0.951	20.447	11.250	11.250	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.790	-0.885	23.198	-12.664	-12.664	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.077	-0.037	25.893	0.115	0.115	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.006	-0.004	27.378	0.307	0.307	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.036	-0.016	30.957	0.334	0.334	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.069	-0.022	32.675	0.341	0.341	0.000	0.000	0.000	0.000
40	A	40	PRO	0	0.035	0.023	31.338	-0.328	-0.328	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.065	0.027	29.689	0.262	0.262	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.821	-0.903	29.166	-9.977	-9.977	0.000	0.000	0.000	0.000
43	A	43	PHE	0	-0.017	-0.017	23.802	-0.362	-0.362	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.074	-0.044	25.828	0.508	0.508	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.008	0.006	21.597	-0.670	-0.670	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.033	-0.022	23.873	0.458	0.458	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.025	-0.008	23.045	-0.830	-0.830	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.017	0.012	23.822	0.653	0.653	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.037	0.005	25.224	-0.340	-0.340	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.884	-0.961	27.584	-10.964	-10.964	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.020	0.011	28.788	0.463	0.463	0.000	0.000	0.000	0.000
52	A	52	PRO	0	-0.025	-0.001	32.294	-0.046	-0.046	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.891	0.943	33.463	9.649	9.649	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.016	-0.013	36.230	0.255	0.255	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.029	0.021	36.285	0.193	0.193	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.027	0.016	33.694	-0.284	-0.284	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.019	0.005	33.073	0.242	0.242	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.054	-0.018	34.180	0.110	0.110	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.041	0.014	30.573	-0.195	-0.195	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.002	0.003	26.611	0.370	0.370	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.964	0.967	30.051	8.828	8.828	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.004	0.010	27.018	-0.392	-0.392	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.024	-0.010	28.336	0.316	0.316	0.000	0.000	0.000	0.000
64	A	64	HIS	0	-0.066	-0.036	27.891	-0.751	-0.751	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.037	0.020	26.470	0.397	0.397	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.887	0.929	27.806	8.913	8.913	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.029	-0.015	25.076	0.011	0.011	0.000	0.000	0.000	0.000
68	A	68	MET	0	0.007	0.008	28.484	0.141	0.141	0.000	0.000	0.000	0.000
69	A	69	CYS	0	-0.057	-0.033	29.102	-0.099	-0.099	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.922	-0.951	30.582	-8.846	-8.846	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.052	0.014	32.120	-0.205	-0.205	0.000	0.000	0.000	0.000
72	A	72	GLY	0	-0.057	-0.023	30.601	-0.046	-0.046	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.883	0.951	27.948	9.898	9.898	0.000	0.000	0.000	0.000
74	A	74	TYR	0	-0.003	-0.002	24.374	0.133	0.133	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.057	0.005	27.792	-0.134	-0.134	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.011	-0.007	27.150	-0.053	-0.053	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.014	0.010	29.954	0.203	0.203	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.021	0.005	32.059	0.264	0.264	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.014	-0.006	33.233	-0.029	-0.029	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.881	-0.915	29.004	-10.860	-10.860	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.011	-0.011	29.088	-0.028	-0.028	0.000	0.000	0.000	0.000
82	A	82	PHE	0	-0.011	-0.009	23.846	-0.227	-0.227	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.795	-0.895	24.078	-11.487	-11.487	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.025	-0.021	20.011	-0.486	-0.486	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.048	0.015	20.031	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.002	-0.007	15.037	-0.353	-0.353	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.908	-0.946	17.765	-14.244	-14.244	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.010	0.014	20.288	0.254	0.254	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.005	-0.008	17.004	0.227	0.227	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.857	-0.930	13.982	-20.685	-20.685	0.000	0.000	0.000	0.000
91	A	91	HIS	1	0.773	0.898	18.294	12.250	12.250	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.017	-0.017	22.081	0.248	0.248	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.796	0.892	13.920	20.501	20.501	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.880	0.961	20.225	13.747	13.747	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.051	-0.031	22.219	0.238	0.238	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.005	0.023	24.464	0.420	0.420	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.032	-0.029	25.087	0.047	0.047	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.911	-0.941	28.393	-8.925	-8.925	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.851	-0.906	31.725	-9.728	-9.728	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.008	-0.005	33.660	0.228	0.228	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.078	-0.059	35.586	0.239	0.239	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.010	0.013	37.245	0.170	0.170	0.000	0.000	0.000	0.000
103	A	103	ALA	0	-0.027	0.001	33.369	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.015	-0.002	29.818	-0.073	-0.073	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.015	-0.013	25.949	-0.150	-0.150	0.000	0.000	0.000	0.000
106	A	106	TYR	0	0.007	0.004	23.595	-0.143	-0.143	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.009	-0.012	19.970	-0.114	-0.114	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.937	0.971	18.806	14.444	14.444	0.000	0.000	0.000	0.000
109	A	109	GLN	0	-0.024	-0.006	15.148	-1.879	-1.879	0.000	0.000	0.000	0.000
110	A	110	PRO	0	-0.009	0.000	12.794	1.022	1.022	0.000	0.000	0.000	0.000
111	A	111	TYR	0	-0.003	-0.022	15.003	-0.983	-0.983	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.015	-0.001	8.472	-1.654	-1.654	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.050	-0.015	13.948	0.408	0.408	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.014	-0.001	15.251	-1.325	-1.325	0.000	0.000	0.000	0.000
115	A	115	PRO	0	-0.028	0.000	16.069	0.664	0.664	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.004	-0.003	18.966	0.591	0.591	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.043	-0.031	21.214	-0.483	-0.483	0.000	0.000	0.000	0.000
118	A	118	GLY	-1	-0.940	-0.951	23.748	-11.453	-11.453	0.000	0.000	0.000	0.000

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