FMO DATABASE

FMODB ID: 4G97N

Calculation Name: 7TN2-D-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7TN2

Chain ID: D

ChEMBL ID:

UniProt ID:

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	96
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-593359.19825
FMO2-HF: Nuclear repulsion	555617.555691
FMO2-HF: Total energy	-37741.642559
FMO2-MP2: Total energy	-37851.624566

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:26:ARG)

Summations of interaction energy for fragment #1(A:26:ARG)

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.
136.294	138.878	0.059	-1.415	-1.228	-0.011

Interaction energy analysis for fragmet #1(A:26:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.853 / q_NPA : 1.908

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	28	LYS	1	1.001	1.009	3.038	39.220	41.721	0.060	-1.413	-1.149	-0.011
4	A	29	THR	0	0.033	0.008	5.152	2.258	2.341	-0.001	-0.002	-0.079	0.000
5	A	30	ARG	1	0.959	0.981	7.715	41.202	41.202	0.000	0.000	0.000	0.000
6	A	31	LYS	1	0.981	0.985	11.272	34.143	34.143	0.000	0.000	0.000	0.000
7	A	32	GLU	-1	-0.906	-0.938	14.054	-30.535	-30.535	0.000	0.000	0.000	0.000
8	A	33	SER	0	-0.045	-0.034	17.704	0.322	0.322	0.000	0.000	0.000	0.000
9	A	34	TYR	0	0.082	0.032	20.765	0.154	0.154	0.000	0.000	0.000	0.000
10	A	35	ALA	0	0.036	0.010	22.294	0.927	0.927	0.000	0.000	0.000	0.000
11	A	36	ILE	0	0.001	-0.010	22.150	0.880	0.880	0.000	0.000	0.000	0.000
12	A	37	TYR	0	-0.032	-0.017	23.669	0.486	0.486	0.000	0.000	0.000	0.000
13	A	38	VAL	0	0.056	0.018	27.572	0.754	0.754	0.000	0.000	0.000	0.000
14	A	39	TYR	0	0.021	0.007	27.480	0.756	0.756	0.000	0.000	0.000	0.000
15	A	40	LYS	1	0.929	0.970	27.266	21.811	21.811	0.000	0.000	0.000	0.000
16	A	41	VAL	0	0.035	0.021	31.535	0.510	0.510	0.000	0.000	0.000	0.000
17	A	42	LEU	0	-0.012	-0.010	31.578	0.469	0.469	0.000	0.000	0.000	0.000
18	A	43	LYS	1	0.811	0.890	32.378	18.221	18.221	0.000	0.000	0.000	0.000
19	A	44	GLN	0	-0.033	-0.009	35.149	0.334	0.334	0.000	0.000	0.000	0.000
20	A	45	VAL	0	-0.037	-0.005	37.433	0.419	0.419	0.000	0.000	0.000	0.000
21	A	46	HIS	0	0.007	0.000	37.772	0.422	0.422	0.000	0.000	0.000	0.000
22	A	47	PRO	0	0.034	0.023	37.190	-0.486	-0.486	0.000	0.000	0.000	0.000
23	A	48	ASP	-1	-0.851	-0.920	36.648	-15.707	-15.707	0.000	0.000	0.000	0.000
24	A	49	THR	0	-0.044	-0.007	35.268	-0.163	-0.163	0.000	0.000	0.000	0.000
25	A	50	GLY	0	-0.012	0.000	32.303	-0.427	-0.427	0.000	0.000	0.000	0.000
26	A	51	ILE	0	-0.010	-0.020	28.196	0.294	0.294	0.000	0.000	0.000	0.000
27	A	52	SER	0	0.017	0.010	27.832	-0.518	-0.518	0.000	0.000	0.000	0.000
28	A	53	CYS	-1	-0.840	-0.911	22.412	-26.115	-26.115	0.000	0.000	0.000	0.000
29	A	54	LYS	1	1.002	0.980	24.533	23.695	23.695	0.000	0.000	0.000	0.000
30	A	55	ALA	0	0.024	0.016	26.043	0.134	0.134	0.000	0.000	0.000	0.000
31	A	56	MET	0	0.014	0.030	24.295	0.262	0.262	0.000	0.000	0.000	0.000
32	A	57	SER	0	-0.046	-0.022	22.261	-0.102	-0.102	0.000	0.000	0.000	0.000
33	A	58	ILE	0	0.024	0.021	24.340	-0.165	-0.165	0.000	0.000	0.000	0.000
34	A	59	MET	0	0.027	0.013	27.800	0.274	0.274	0.000	0.000	0.000	0.000
35	A	60	ASN	0	-0.001	-0.009	21.829	0.079	0.079	0.000	0.000	0.000	0.000
36	A	61	SER	0	-0.020	-0.018	25.288	-0.544	-0.544	0.000	0.000	0.000	0.000
37	A	62	PHE	0	0.008	0.005	26.439	0.211	0.211	0.000	0.000	0.000	0.000
38	A	63	VAL	0	-0.002	-0.002	27.629	0.365	0.365	0.000	0.000	0.000	0.000
39	A	64	ASN	0	-0.050	-0.024	23.495	-0.074	-0.074	0.000	0.000	0.000	0.000
40	A	65	ASP	-1	-0.748	-0.836	27.390	-18.411	-18.411	0.000	0.000	0.000	0.000
41	A	66	VAL	0	-0.018	-0.011	30.307	0.547	0.547	0.000	0.000	0.000	0.000
42	A	67	PHE	0	-0.015	-0.005	27.341	0.477	0.477	0.000	0.000	0.000	0.000
43	A	68	GLU	-1	-0.917	-0.968	26.584	-22.106	-22.106	0.000	0.000	0.000	0.000
44	A	69	ARG	1	0.797	0.872	30.680	18.069	18.069	0.000	0.000	0.000	0.000
45	A	70	ILE	0	0.000	-0.001	34.287	0.468	0.468	0.000	0.000	0.000	0.000
46	A	71	ALA	0	0.012	0.005	31.454	0.412	0.412	0.000	0.000	0.000	0.000
47	A	72	GLY	0	0.007	0.003	33.442	0.196	0.196	0.000	0.000	0.000	0.000
48	A	73	GLU	-1	-0.843	-0.905	34.589	-15.040	-15.040	0.000	0.000	0.000	0.000
49	A	74	ALA	0	0.002	-0.002	36.210	0.375	0.375	0.000	0.000	0.000	0.000
50	A	75	SER	0	0.013	0.000	34.270	0.405	0.405	0.000	0.000	0.000	0.000
51	A	76	ARG	1	0.846	0.909	36.548	16.497	16.497	0.000	0.000	0.000	0.000
52	A	77	LEU	0	-0.010	0.001	39.592	0.404	0.404	0.000	0.000	0.000	0.000
53	A	78	ALA	0	0.029	0.021	38.713	0.395	0.395	0.000	0.000	0.000	0.000
54	A	79	HIS	0	0.021	0.011	35.975	0.639	0.639	0.000	0.000	0.000	0.000
55	A	80	TYR	0	-0.015	-0.010	41.211	0.261	0.261	0.000	0.000	0.000	0.000
56	A	81	ASN	0	-0.080	-0.041	44.235	0.624	0.624	0.000	0.000	0.000	0.000
57	A	82	LYS	1	0.927	0.960	43.629	13.126	13.126	0.000	0.000	0.000	0.000
58	A	83	ARG	1	0.905	0.961	41.653	13.554	13.554	0.000	0.000	0.000	0.000
59	A	84	SER	0	0.017	0.011	38.276	-0.263	-0.263	0.000	0.000	0.000	0.000
60	A	85	THR	0	-0.027	-0.029	37.014	-0.248	-0.248	0.000	0.000	0.000	0.000
61	A	86	ILE	0	0.005	0.024	34.014	0.302	0.302	0.000	0.000	0.000	0.000
62	A	87	THR	0	-0.019	-0.041	37.048	-0.093	-0.093	0.000	0.000	0.000	0.000
63	A	88	SER	0	0.049	0.007	39.384	-0.094	-0.094	0.000	0.000	0.000	0.000
64	A	89	ARG	1	0.971	0.989	40.459	13.425	13.425	0.000	0.000	0.000	0.000
65	A	90	GLU	-1	-0.785	-0.851	39.621	-14.634	-14.634	0.000	0.000	0.000	0.000
66	A	91	ILE	0	0.036	0.017	35.316	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	92	GLN	0	0.003	0.003	39.234	0.291	0.291	0.000	0.000	0.000	0.000
68	A	93	THR	0	-0.052	-0.040	42.537	0.350	0.350	0.000	0.000	0.000	0.000
69	A	94	ALA	0	0.036	0.014	38.841	0.129	0.129	0.000	0.000	0.000	0.000
70	A	95	VAL	0	-0.015	-0.014	39.250	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	96	ARG	1	0.886	0.926	41.353	13.247	13.247	0.000	0.000	0.000	0.000
72	A	97	LEU	0	-0.019	0.006	42.859	0.244	0.244	0.000	0.000	0.000	0.000
73	A	98	LEU	0	-0.030	0.001	37.713	-0.042	-0.042	0.000	0.000	0.000	0.000
74	A	99	LEU	0	-0.036	-0.008	38.877	-0.138	-0.138	0.000	0.000	0.000	0.000
75	A	100	PRO	0	0.032	0.020	42.708	0.320	0.320	0.000	0.000	0.000	0.000
76	A	101	GLY	0	0.039	0.006	45.893	0.002	0.002	0.000	0.000	0.000	0.000
77	A	102	GLU	-1	-0.824	-0.939	48.090	-12.334	-12.334	0.000	0.000	0.000	0.000
78	A	103	LEU	0	0.010	0.020	41.657	-0.131	-0.131	0.000	0.000	0.000	0.000
79	A	104	ALA	0	0.031	0.023	43.676	-0.242	-0.242	0.000	0.000	0.000	0.000
80	A	105	LYS	1	0.878	0.949	45.106	12.061	12.061	0.000	0.000	0.000	0.000
81	A	106	HIS	0	0.022	0.007	44.585	0.054	0.054	0.000	0.000	0.000	0.000
82	A	107	ALA	0	0.046	0.040	40.801	-0.118	-0.118	0.000	0.000	0.000	0.000
83	A	108	VAL	0	-0.036	-0.022	42.078	-0.182	-0.182	0.000	0.000	0.000	0.000
84	A	109	SER	0	-0.058	-0.009	44.268	0.071	0.071	0.000	0.000	0.000	0.000
85	A	110	GLU	-1	-0.822	-0.900	40.641	-14.484	-14.484	0.000	0.000	0.000	0.000
86	A	111	GLY	0	0.010	0.001	39.980	-0.182	-0.182	0.000	0.000	0.000	0.000
87	A	112	THR	0	-0.025	-0.037	40.916	-0.083	-0.083	0.000	0.000	0.000	0.000
88	A	113	LYS	1	0.864	0.929	42.866	14.338	14.338	0.000	0.000	0.000	0.000
89	A	114	ALA	0	-0.030	-0.012	38.581	0.004	0.004	0.000	0.000	0.000	0.000
90	A	115	VAL	0	0.002	-0.009	39.346	-0.104	-0.104	0.000	0.000	0.000	0.000
91	A	116	THR	0	-0.022	-0.013	41.131	0.131	0.131	0.000	0.000	0.000	0.000
92	A	117	LYS	1	0.957	0.974	41.358	14.736	14.736	0.000	0.000	0.000	0.000
93	A	118	TYR	0	-0.063	-0.025	35.256	-0.227	-0.227	0.000	0.000	0.000	0.000
94	A	119	THR	0	-0.025	-0.028	40.134	-0.131	-0.131	0.000	0.000	0.000	0.000
95	A	120	SER	0	-0.088	-0.037	42.747	0.227	0.227	0.000	0.000	0.000	0.000
96	A	121	ALA	-1	-0.931	-0.945	40.657	-14.539	-14.539	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:26:ARG)