FMO DATABASE

FMODB ID: 8GKNY

Calculation Name: 1E7N-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1E7N

Chain ID: A

ChEMBL ID:

UniProt ID: P62696

Base Structure: X-ray

Registration Date: 2025-09-02

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	89
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-633680.546042
FMO2-HF: Nuclear repulsion	598209.34791
FMO2-HF: Total energy	-35471.198131
FMO2-MP2: Total energy	-35574.386167

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:-2:LEU)

Summations of interaction energy for fragment #1(A:-2:LEU)

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.
-41.779	-39.794	-0.011	-0.802	-1.172	-0.001

Interaction energy analysis for fragmet #1(A:-2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.886 / q_NPA : 0.930

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

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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	1	PRO	0	0.009	0.019	3.484	3.386	5.371	-0.011	-0.802	-1.172	-0.001
4	A	2	LYS	1	0.827	0.921	5.782	26.105	26.105	0.000	0.000	0.000	0.000
5	A	3	ILE	0	0.002	0.016	9.415	0.444	0.444	0.000	0.000	0.000	0.000
6	A	4	ILE	0	0.004	-0.005	12.541	0.233	0.233	0.000	0.000	0.000	0.000
7	A	5	ILE	0	0.003	0.011	16.276	0.280	0.280	0.000	0.000	0.000	0.000
8	A	6	PHE	0	0.046	0.005	19.273	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	7	GLU	-1	-0.712	-0.840	22.823	-12.038	-12.038	0.000	0.000	0.000	0.000
10	A	8	GLN	0	-0.072	-0.049	26.214	0.498	0.498	0.000	0.000	0.000	0.000
11	A	9	GLU	-1	-0.852	-0.918	25.870	-10.868	-10.868	0.000	0.000	0.000	0.000
12	A	10	ASN	0	-0.078	-0.062	25.964	0.026	0.026	0.000	0.000	0.000	0.000
13	A	11	PHE	0	-0.017	-0.003	20.728	0.071	0.071	0.000	0.000	0.000	0.000
14	A	12	GLN	0	-0.038	-0.001	24.271	0.327	0.327	0.000	0.000	0.000	0.000
15	A	13	GLY	0	0.036	0.009	26.587	-0.163	-0.163	0.000	0.000	0.000	0.000
16	A	14	HIS	0	-0.019	-0.012	25.647	-0.487	-0.487	0.000	0.000	0.000	0.000
17	A	15	SER	0	0.015	0.009	20.310	-0.069	-0.069	0.000	0.000	0.000	0.000
18	A	16	HIS	1	0.761	0.869	19.852	13.983	13.983	0.000	0.000	0.000	0.000
19	A	17	GLU	-1	-0.858	-0.930	13.106	-22.452	-22.452	0.000	0.000	0.000	0.000
20	A	18	LEU	0	-0.011	-0.005	13.110	0.409	0.409	0.000	0.000	0.000	0.000
21	A	19	SER	0	0.031	0.001	8.833	-0.523	-0.523	0.000	0.000	0.000	0.000
22	A	20	GLY	0	0.011	0.002	7.973	-4.891	-4.891	0.000	0.000	0.000	0.000
23	A	21	PRO	0	-0.043	-0.037	9.708	1.596	1.596	0.000	0.000	0.000	0.000
24	A	22	CYS	0	0.002	0.033	12.690	0.970	0.970	0.000	0.000	0.000	0.000
25	A	23	PRO	0	0.022	0.008	16.197	0.371	0.371	0.000	0.000	0.000	0.000
26	A	24	ASN	0	0.048	-0.013	19.059	0.838	0.838	0.000	0.000	0.000	0.000
27	A	25	LEU	0	0.072	0.031	18.152	-0.180	-0.180	0.000	0.000	0.000	0.000
28	A	26	LYS	1	0.969	1.021	21.406	11.389	11.389	0.000	0.000	0.000	0.000
29	A	27	GLU	-1	-0.914	-0.960	21.923	-12.059	-12.059	0.000	0.000	0.000	0.000
30	A	28	THR	0	-0.111	-0.070	18.854	-0.248	-0.248	0.000	0.000	0.000	0.000
31	A	28	GLY	0	0.028	0.012	21.932	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	29	MET	0	-0.121	-0.032	22.739	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	30	GLU	-1	-0.915	-0.954	24.962	-10.215	-10.215	0.000	0.000	0.000	0.000
34	A	31	LYS	1	0.895	0.935	26.516	10.520	10.520	0.000	0.000	0.000	0.000
35	A	32	ALA	0	0.046	0.015	22.157	-0.296	-0.296	0.000	0.000	0.000	0.000
36	A	33	GLY	0	-0.018	0.001	23.884	0.288	0.288	0.000	0.000	0.000	0.000
37	A	34	SER	0	-0.066	-0.045	22.721	0.082	0.082	0.000	0.000	0.000	0.000
38	A	35	VAL	0	-0.024	-0.004	16.432	-0.395	-0.395	0.000	0.000	0.000	0.000
39	A	36	LEU	0	0.023	0.023	15.797	0.074	0.074	0.000	0.000	0.000	0.000
40	A	37	VAL	0	-0.014	-0.005	10.797	-1.275	-1.275	0.000	0.000	0.000	0.000
41	A	38	GLN	0	-0.012	-0.007	10.658	0.486	0.486	0.000	0.000	0.000	0.000
42	A	39	ALA	0	-0.014	-0.022	5.687	-0.833	-0.833	0.000	0.000	0.000	0.000
43	A	40	GLY	0	0.019	0.026	7.142	0.341	0.341	0.000	0.000	0.000	0.000
44	A	41	PRO	0	0.027	0.021	6.334	-4.261	-4.261	0.000	0.000	0.000	0.000
45	A	42	TRP	0	-0.005	-0.024	8.496	-2.809	-2.809	0.000	0.000	0.000	0.000
46	A	43	VAL	0	-0.020	-0.005	11.169	1.424	1.424	0.000	0.000	0.000	0.000
47	A	44	GLY	0	0.013	0.001	14.510	-0.645	-0.645	0.000	0.000	0.000	0.000
48	A	45	TYR	0	0.000	-0.005	16.030	-0.279	-0.279	0.000	0.000	0.000	0.000
49	A	46	GLU	-1	-0.805	-0.896	20.577	-11.258	-11.258	0.000	0.000	0.000	0.000
50	A	47	GLN	0	-0.001	0.002	23.893	0.273	0.273	0.000	0.000	0.000	0.000
51	A	48	ALA	0	0.043	0.019	22.464	-0.670	-0.670	0.000	0.000	0.000	0.000
52	A	49	ASN	0	-0.078	-0.064	20.449	-0.317	-0.317	0.000	0.000	0.000	0.000
53	A	50	CYS	0	-0.036	-0.007	16.992	-0.343	-0.343	0.000	0.000	0.000	0.000
54	A	51	LYS	1	0.897	0.966	19.607	13.689	13.689	0.000	0.000	0.000	0.000
55	A	52	GLY	0	0.091	0.043	23.153	-0.074	-0.074	0.000	0.000	0.000	0.000
56	A	53	GLU	-1	-0.865	-0.917	23.624	-12.118	-12.118	0.000	0.000	0.000	0.000
57	A	54	GLN	0	-0.042	-0.026	18.604	-1.158	-1.158	0.000	0.000	0.000	0.000
58	A	55	PHE	0	0.051	0.020	19.433	0.389	0.389	0.000	0.000	0.000	0.000
59	A	56	VAL	0	0.006	-0.002	14.368	-0.971	-0.971	0.000	0.000	0.000	0.000
60	A	57	PHE	0	0.001	0.004	14.048	0.679	0.679	0.000	0.000	0.000	0.000
61	A	58	GLU	-1	-0.897	-0.965	12.016	-22.870	-22.870	0.000	0.000	0.000	0.000
62	A	59	LYS	1	0.897	0.936	9.416	26.699	26.699	0.000	0.000	0.000	0.000
63	A	60	GLY	0	0.035	0.016	12.215	0.960	0.960	0.000	0.000	0.000	0.000
64	A	61	GLU	-1	-0.939	-0.967	15.811	-15.590	-15.590	0.000	0.000	0.000	0.000
65	A	62	TYR	0	0.016	0.010	15.821	0.117	0.117	0.000	0.000	0.000	0.000
66	A	63	PRO	0	0.052	0.027	20.658	0.031	0.031	0.000	0.000	0.000	0.000
67	A	64	ARG	1	0.854	0.889	23.892	10.913	10.913	0.000	0.000	0.000	0.000
68	A	65	TRP	0	0.100	0.035	24.620	-0.230	-0.230	0.000	0.000	0.000	0.000
69	A	66	ASP	-1	-0.836	-0.881	25.665	-11.193	-11.193	0.000	0.000	0.000	0.000
70	A	67	SER	0	-0.051	-0.023	22.568	-0.065	-0.065	0.000	0.000	0.000	0.000
71	A	68	TRP	0	0.002	0.006	20.220	-0.682	-0.682	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.010	0.015	21.826	-0.196	-0.196	0.000	0.000	0.000	0.000
73	A	70	SER	0	0.033	0.028	24.884	0.264	0.264	0.000	0.000	0.000	0.000
74	A	70	SER	0	-0.059	-0.060	27.261	0.513	0.513	0.000	0.000	0.000	0.000
75	A	71	ARG	1	0.935	0.989	29.196	8.711	8.711	0.000	0.000	0.000	0.000
76	A	71	ARG	1	0.843	0.902	27.903	11.225	11.225	0.000	0.000	0.000	0.000
77	A	72	THR	0	-0.022	-0.015	27.011	0.299	0.299	0.000	0.000	0.000	0.000
78	A	73	ASP	-1	-0.928	-0.961	27.375	-10.851	-10.851	0.000	0.000	0.000	0.000
79	A	74	SER	0	-0.046	-0.005	26.173	-0.387	-0.387	0.000	0.000	0.000	0.000
80	A	75	LEU	0	0.004	-0.005	19.043	-0.446	-0.446	0.000	0.000	0.000	0.000
81	A	76	SER	0	0.007	0.004	22.571	0.117	0.117	0.000	0.000	0.000	0.000
82	A	77	SER	0	-0.075	-0.040	18.498	-0.251	-0.251	0.000	0.000	0.000	0.000
83	A	78	LEU	0	0.038	0.030	14.475	-0.039	-0.039	0.000	0.000	0.000	0.000
84	A	79	ARG	1	0.853	0.925	11.555	22.632	22.632	0.000	0.000	0.000	0.000
85	A	80	PRO	0	0.045	0.036	6.823	0.771	0.771	0.000	0.000	0.000	0.000
86	A	81	ILE	0	-0.034	-0.016	8.867	2.668	2.668	0.000	0.000	0.000	0.000
87	A	82	LYS	1	0.884	0.939	7.584	21.126	21.126	0.000	0.000	0.000	0.000
88	A	83	VAL	0	-0.038	-0.023	5.594	2.064	2.064	0.000	0.000	0.000	0.000
89	A	84	ASP	-2	-1.841	-1.902	7.091	-65.312	-65.312	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:LEU)