FMO DATABASE

FMODB ID: 19KYZ

Calculation Name: 4J2C-C-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4J2C

Chain ID: C

ChEMBL ID:

UniProt ID: O43752

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-812739.035198
FMO2-HF: Nuclear repulsion	768483.295739
FMO2-HF: Total energy	-44255.73946
FMO2-MP2: Total energy	-44384.715387

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.
-78.12	-77.397	0.003	-0.322	-0.405	-0.001

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 : 0.850 / q_NPA : 0.910

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	MET	0	-0.021	-0.010	3.822	-4.089	-3.366	0.003	-0.322	-0.405	-0.001
4	A	4	GLU	-1	-0.879	-0.931	6.223	-26.968	-26.968	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.787	-0.880	9.683	-21.355	-21.355	0.000	0.000	0.000	0.000
6	A	6	PRO	0	0.018	0.005	11.899	1.312	1.312	0.000	0.000	0.000	0.000
7	A	7	PHE	0	0.030	0.019	14.574	1.598	1.598	0.000	0.000	0.000	0.000
8	A	8	PHE	0	-0.019	-0.030	15.439	1.367	1.367	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.035	0.001	15.855	0.802	0.802	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.110	0.056	17.861	0.858	0.858	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.889	0.951	20.501	13.958	13.958	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.026	-0.018	22.158	0.784	0.784	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.926	-0.967	20.085	-14.759	-14.759	0.000	0.000	0.000	0.000
14	A	14	VAL	0	0.073	0.037	24.427	0.725	0.725	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.001	0.004	26.498	0.549	0.549	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.951	0.990	27.268	11.308	11.308	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.048	0.040	28.620	0.459	0.459	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.012	0.002	30.402	0.435	0.435	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.042	-0.031	31.801	0.570	0.570	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.076	-0.043	32.264	0.336	0.336	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.016	0.000	34.437	0.305	0.305	0.000	0.000	0.000	0.000
22	A	22	GLN	0	0.033	0.005	36.039	0.165	0.165	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.007	0.005	37.931	0.257	0.257	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.051	-0.032	37.746	0.250	0.250	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.037	0.012	40.342	0.188	0.188	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.020	0.028	42.209	0.136	0.136	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.805	0.876	43.712	7.063	7.063	0.000	0.000	0.000	0.000
28	A	28	TRP	0	-0.029	-0.024	44.064	0.105	0.105	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.020	-0.001	45.934	0.153	0.153	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.904	-0.948	48.250	-6.568	-6.568	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.080	-0.044	47.247	0.153	0.153	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.016	0.015	49.442	0.111	0.111	0.000	0.000	0.000	0.000
33	A	33	GLN	0	-0.091	-0.034	52.130	0.053	0.053	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.836	-0.903	54.478	-5.747	-5.747	0.000	0.000	0.000	0.000
35	A	35	PRO	0	-0.059	-0.045	56.470	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.049	-0.024	54.278	0.044	0.044	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.049	-0.030	53.849	-0.078	-0.078	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.002	0.012	52.561	0.117	0.117	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.017	-0.032	52.733	0.046	0.046	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.853	0.893	48.046	6.434	6.434	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.828	-0.891	48.816	-6.410	-6.410	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.783	-0.865	47.358	-6.787	-6.787	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.082	0.063	46.349	-0.230	-0.230	0.000	0.000	0.000	0.000
44	A	44	ASP	0	-0.026	-0.011	45.286	-0.141	-0.141	0.000	0.000	0.000	0.000
45	A	45	TRP	0	0.034	0.032	39.015	-0.115	-0.115	0.000	0.000	0.000	0.000
46	A	46	THR	0	0.015	-0.008	41.845	-0.247	-0.247	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.011	-0.027	41.353	-0.176	-0.176	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.081	-0.056	40.159	-0.232	-0.232	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.817	-0.889	34.710	-9.524	-9.524	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.002	0.021	36.377	-0.317	-0.317	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.939	0.952	36.653	7.727	7.727	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.066	-0.031	32.609	-0.345	-0.345	0.000	0.000	0.000	0.000
53	A	53	ASN	0	-0.007	-0.011	32.042	-0.530	-0.530	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.010	0.005	31.742	-0.304	-0.304	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.886	0.949	31.557	9.260	9.260	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.042	-0.014	27.563	-0.262	-0.262	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.016	-0.001	27.505	-0.295	-0.295	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-1.002	-1.002	28.420	-10.456	-10.456	0.000	0.000	0.000	0.000
59	A	59	TRP	0	0.045	0.033	23.325	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.868	-0.937	23.661	-13.749	-13.749	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.087	-0.064	23.809	-0.452	-0.452	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.955	-0.955	25.999	-11.293	-11.293	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.846	-0.920	20.482	-15.146	-15.146	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.033	-0.028	19.974	-0.695	-0.695	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.798	-0.879	21.953	-12.233	-12.233	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.913	-0.940	21.402	-14.173	-14.173	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.107	-0.072	17.398	-0.706	-0.706	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.009	-0.009	19.231	-0.483	-0.483	0.000	0.000	0.000	0.000
69	A	69	SER	0	0.005	-0.002	21.806	0.185	0.185	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.039	-0.025	16.374	-0.142	-0.142	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.038	-0.021	16.935	-0.620	-0.620	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.874	-0.932	18.875	-12.602	-12.602	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.011	0.009	20.649	0.402	0.402	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.085	-0.047	15.802	-0.220	-0.220	0.000	0.000	0.000	0.000
75	A	75	PRO	0	0.085	0.044	17.103	-1.246	-1.246	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.923	0.953	15.745	16.122	16.122	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.901	0.970	10.178	26.963	26.963	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.015	-0.006	12.036	-2.580	-2.580	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.079	-0.027	14.098	0.402	0.402	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.043	0.034	16.020	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.802	-0.892	18.100	-12.780	-12.780	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.012	-0.003	21.340	0.045	0.045	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.021	-0.010	24.432	0.530	0.530	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.858	-0.906	19.066	-16.792	-16.792	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.002	-0.002	21.106	0.126	0.126	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.053	-0.041	23.224	0.425	0.425	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.011	-0.007	25.708	0.355	0.355	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.738	0.853	16.813	18.020	18.020	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.913	0.936	24.769	12.393	12.393	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.009	0.012	27.562	0.369	0.369	0.000	0.000	0.000	0.000
91	A	91	PHE	0	0.021	0.016	26.137	0.346	0.346	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.049	0.038	24.329	0.333	0.333	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.043	-0.027	28.576	0.403	0.403	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.040	-0.038	32.024	0.418	0.418	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.029	-0.022	29.697	0.301	0.301	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.816	0.876	28.287	11.350	11.350	0.000	0.000	0.000	0.000
97	A	97	GLN	0	-0.100	-0.047	33.475	0.129	0.129	0.000	0.000	0.000	0.000
98	A	98	VAL	0	0.039	0.016	34.977	0.211	0.211	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.012	0.000	33.095	0.195	0.195	0.000	0.000	0.000	0.000
100	A	100	ARG	1	0.892	0.947	36.296	8.409	8.409	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.804	-0.889	39.140	-7.861	-7.861	0.000	0.000	0.000	0.000
102	A	102	MET	0	-0.016	-0.006	36.278	0.180	0.180	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.948	0.973	37.022	8.777	8.777	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.913	-0.940	41.682	-7.418	-7.418	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.017	-0.009	44.572	0.064	0.064	0.000	0.000	0.000	0.000
106	A	106	MET	0	-0.060	-0.028	42.087	0.038	0.038	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.088	-0.041	44.907	0.048	0.048	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.110	-0.070	47.358	0.137	0.137	0.000	0.000	0.000	0.000
109	A	109	SER	-1	-0.949	-0.955	49.207	-6.263	-6.263	0.000	0.000	0.000	0.000

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