FMO DATABASE

FMODB ID: 4Q57N

Calculation Name: 1PPA-A-Xray547

Preferred Name:

Target Type:

Ligand Name: aniline

Ligand 3-letter code: ANL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1PPA

Chain ID: A

ChEMBL ID:

UniProt ID: P04361

Base Structure: X-ray

Registration Date: 2025-10-03

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1064874.553918
FMO2-HF: Nuclear repulsion	1012487.0807
FMO2-HF: Total energy	-52387.473218
FMO2-MP2: Total energy	-52527.98673

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:SER)

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

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.
-89.624	-84.235	54.004	-29.891	-29.502	-0.235

Interaction energy analysis for fragmet #1(A:1:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.746 / q_NPA : 0.858

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	LEU	0	-0.031	-0.002	2.134	2.163	4.533	4.181	-2.841	-3.710	0.027
4	A	4	GLU	-1	-0.759	-0.856	1.772	-132.193	-136.689	27.325	-13.077	-9.752	-0.131
5	A	5	LEU	0	0.028	0.034	4.000	10.823	11.185	-0.001	-0.106	-0.255	0.000
50	A	52	TYR	0	-0.005	-0.060	4.799	-0.119	-0.087	-0.001	-0.004	-0.026	0.000
58	A	68	HIS	0	0.063	0.007	3.990	-10.977	-10.424	0.001	-0.132	-0.422	0.000
59	A	69	LYS	1	0.860	0.933	2.415	15.191	17.203	2.109	-2.246	-1.875	-0.024
60	A	70	THR	0	0.020	-0.005	2.609	-11.157	-8.829	1.741	-1.990	-2.079	-0.024
61	A	71	ASP	-1	-0.805	-0.884	3.129	-45.395	-43.778	0.370	-0.974	-1.014	-0.008
62	A	72	ARG	1	0.893	0.938	1.846	0.582	0.834	12.725	-6.244	-6.733	-0.055
63	A	73	TYR	0	-0.017	-0.045	2.442	11.145	12.184	1.217	-0.580	-1.676	-0.012
80	A	92	LEU	0	0.012	-0.005	4.619	-3.611	-3.555	-0.001	-0.005	-0.050	0.000
83	A	95	MET	0	-0.067	0.002	2.846	-14.248	-15.475	4.334	-1.391	-1.716	-0.006
85	A	99	ASP	-1	-0.751	-0.831	3.450	-65.118	-64.627	0.004	-0.301	-0.194	-0.002
6	A	6	GLY	0	-0.011	-0.016	5.849	6.998	6.998	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.910	0.964	7.198	30.368	30.368	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.054	0.030	6.339	4.041	4.041	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.025	0.011	9.896	3.186	3.186	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.053	0.007	11.800	2.305	2.305	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.024	-0.008	11.461	-0.139	-0.139	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.773	-0.866	13.854	-17.932	-17.932	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.035	-0.053	14.996	1.397	1.397	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.012	0.017	16.980	1.045	1.045	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.892	0.949	16.380	15.828	15.828	0.000	0.000	0.000	0.000
16	A	17	ASN	0	0.024	0.019	14.166	-2.124	-2.124	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.090	0.030	10.846	0.835	0.835	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.033	0.014	10.391	0.532	0.532	0.000	0.000	0.000	0.000
19	A	20	THR	0	-0.009	-0.013	13.567	0.732	0.732	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.063	-0.022	16.504	1.438	1.438	0.000	0.000	0.000	0.000
21	A	22	TYR	0	0.110	0.039	14.195	0.720	0.720	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.029	0.024	13.863	-0.057	-0.057	0.000	0.000	0.000	0.000
23	A	24	SER	0	-0.037	-0.020	14.669	0.222	0.222	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.041	-0.040	17.434	1.003	1.003	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.007	0.003	18.695	-0.521	-0.521	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.025	-0.002	20.998	0.200	0.200	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.054	-0.053	16.930	-0.562	-0.562	0.000	0.000	0.000	0.000
28	A	29	CYS	0	0.004	0.029	13.537	-2.555	-2.555	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.013	0.031	13.881	-1.348	-1.348	0.000	0.000	0.000	0.000
30	A	31	TRP	0	0.055	0.008	7.939	-0.746	-0.746	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.020	-0.008	13.482	1.201	1.201	0.000	0.000	0.000	0.000
32	A	33	HIS	0	-0.088	-0.033	15.537	0.768	0.768	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.904	0.960	16.765	15.905	15.905	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.038	0.010	19.293	0.722	0.722	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.058	-0.027	21.897	-0.141	-0.141	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.017	-0.014	20.970	0.094	0.094	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.821	0.926	22.923	12.398	12.398	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.774	-0.858	22.216	-13.483	-13.483	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.054	0.026	22.492	-0.422	-0.422	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.075	0.036	18.144	-0.979	-0.979	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.718	-0.890	17.748	-16.800	-16.800	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.958	0.977	18.143	13.810	13.810	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.032	0.013	15.098	1.428	1.428	0.000	0.000	0.000	0.000
44	A	46	PHE	0	-0.045	-0.012	14.062	-1.160	-1.160	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.015	0.001	14.874	-0.393	-0.393	0.000	0.000	0.000	0.000
46	A	48	HIS	0	-0.050	-0.020	6.891	2.866	2.866	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.798	0.875	11.046	20.049	20.049	0.000	0.000	0.000	0.000
48	A	133	CYS	-1	-0.946	-0.954	12.644	-14.918	-14.918	0.000	0.000	0.000	0.000
49	A	51	CYS	0	-0.057	-0.005	7.499	3.323	3.323	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.916	0.958	10.031	17.753	17.753	0.000	0.000	0.000	0.000
52	A	54	LYS	1	0.850	0.936	11.784	25.910	25.910	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.064	-0.029	6.942	0.003	0.003	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.012	-0.027	11.162	-0.336	-0.336	0.000	0.000	0.000	0.000
55	A	59	ASP	-1	-0.878	-0.913	12.023	-21.497	-21.497	0.000	0.000	0.000	0.000
56	A	61	CYS	0	-0.035	-0.003	6.844	-2.673	-2.673	0.000	0.000	0.000	0.000
57	A	67	ASN	0	0.026	0.010	6.157	-2.164	-2.164	0.000	0.000	0.000	0.000
64	A	74	SER	0	-0.008	-0.008	5.427	-0.097	-0.097	0.000	0.000	0.000	0.000
65	A	75	TYR	0	-0.050	-0.067	6.450	-0.767	-0.767	0.000	0.000	0.000	0.000
66	A	76	SER	0	-0.007	-0.022	9.281	1.237	1.237	0.000	0.000	0.000	0.000
67	A	77	TRP	0	-0.032	-0.011	12.410	-0.495	-0.495	0.000	0.000	0.000	0.000
68	A	78	LYS	1	0.903	0.943	14.208	20.034	20.034	0.000	0.000	0.000	0.000
69	A	79	ASN	0	-0.021	-0.021	17.668	-0.159	-0.159	0.000	0.000	0.000	0.000
70	A	80	LYS	1	0.936	0.974	18.301	14.052	14.052	0.000	0.000	0.000	0.000
71	A	81	ALA	0	0.071	0.046	16.804	0.107	0.107	0.000	0.000	0.000	0.000
72	A	82	ILE	0	-0.002	-0.001	10.255	-0.401	-0.401	0.000	0.000	0.000	0.000
73	A	83	ILE	0	0.000	-0.004	12.971	0.613	0.613	0.000	0.000	0.000	0.000
74	A	84	CYS	0	-0.027	0.002	5.761	-1.812	-1.812	0.000	0.000	0.000	0.000
75	A	86	GLU	-1	-0.788	-0.874	10.846	-20.353	-20.353	0.000	0.000	0.000	0.000
76	A	87	GLU	-1	-0.804	-0.875	7.627	-33.048	-33.048	0.000	0.000	0.000	0.000
77	A	88	LYS	1	0.942	0.951	10.532	22.165	22.165	0.000	0.000	0.000	0.000
78	A	89	ASN	0	0.000	0.009	9.640	1.442	1.442	0.000	0.000	0.000	0.000
79	A	90	PRO	0	0.078	0.029	10.344	-2.408	-2.408	0.000	0.000	0.000	0.000
81	A	93	LYS	1	0.820	0.902	6.527	20.134	20.134	0.000	0.000	0.000	0.000
82	A	94	GLU	-1	-0.847	-0.925	9.170	-24.647	-24.647	0.000	0.000	0.000	0.000
84	A	97	GLU	-1	-0.773	-0.889	6.515	-22.130	-22.130	0.000	0.000	0.000	0.000
86	A	100	LYS	1	0.933	0.958	7.163	25.702	25.702	0.000	0.000	0.000	0.000
87	A	101	ALA	0	-0.028	-0.001	10.162	2.405	2.405	0.000	0.000	0.000	0.000
88	A	102	VAL	0	-0.022	-0.014	9.336	2.190	2.190	0.000	0.000	0.000	0.000
89	A	103	ALA	0	-0.009	-0.001	10.532	1.785	1.785	0.000	0.000	0.000	0.000
90	A	104	ILE	0	0.025	0.012	12.386	1.670	1.670	0.000	0.000	0.000	0.000
91	A	106	LEU	0	-0.014	-0.022	13.163	1.244	1.244	0.000	0.000	0.000	0.000
92	A	107	ARG	1	0.775	0.858	16.748	17.457	17.457	0.000	0.000	0.000	0.000
93	A	108	GLU	-1	-0.857	-0.920	18.511	-13.564	-13.564	0.000	0.000	0.000	0.000
94	A	109	ASN	0	-0.064	-0.039	19.862	1.253	1.253	0.000	0.000	0.000	0.000
95	A	110	LEU	0	-0.049	-0.031	19.727	0.059	0.059	0.000	0.000	0.000	0.000
96	A	111	ASP	-1	-0.883	-0.937	22.365	-11.969	-11.969	0.000	0.000	0.000	0.000
97	A	112	THR	0	-0.033	-0.011	24.843	0.313	0.313	0.000	0.000	0.000	0.000
98	A	113	TYR	0	-0.104	-0.045	19.444	0.243	0.243	0.000	0.000	0.000	0.000
99	A	114	ASN	0	0.062	0.017	23.521	0.623	0.623	0.000	0.000	0.000	0.000
100	A	115	LYS	1	1.002	0.992	24.649	10.233	10.233	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.874	0.932	25.720	10.915	10.915	0.000	0.000	0.000	0.000
102	A	117	TYR	0	-0.026	-0.013	23.379	0.434	0.434	0.000	0.000	0.000	0.000
103	A	118	LYS	1	0.976	1.000	20.792	13.629	13.629	0.000	0.000	0.000	0.000
104	A	119	ALA	0	0.003	0.004	21.054	-0.612	-0.612	0.000	0.000	0.000	0.000
105	A	120	TYR	0	-0.030	-0.050	22.013	0.928	0.928	0.000	0.000	0.000	0.000
106	A	121	PHE	0	0.029	0.024	19.621	0.412	0.412	0.000	0.000	0.000	0.000
107	A	122	LYS	1	0.960	0.985	22.370	11.072	11.072	0.000	0.000	0.000	0.000
108	A	124	LEU	0	-0.042	-0.006	25.512	0.569	0.569	0.000	0.000	0.000	0.000
109	A	125	LYS	1	1.005	0.999	26.302	9.147	9.147	0.000	0.000	0.000	0.000
110	A	128	LYS	1	0.970	0.998	26.227	10.515	10.515	0.000	0.000	0.000	0.000
111	A	129	LYS	1	1.026	1.002	25.850	9.703	9.703	0.000	0.000	0.000	0.000
112	A	130	PRO	0	-0.030	-0.015	22.055	0.144	0.144	0.000	0.000	0.000	0.000
113	A	131	ASP	-1	-0.830	-0.897	22.996	-12.216	-12.216	0.000	0.000	0.000	0.000
114	A	132	THR	0	-0.026	-0.032	22.365	-0.591	-0.591	0.000	0.000	0.000	0.000

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