FMO DATABASE

FMODB ID: N662Q

Calculation Name: 6OGF-x-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6OGF

Chain ID: x

ChEMBL ID:

UniProt ID: P0ADY7

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	77
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-455721.909678
FMO2-HF: Nuclear repulsion	424896.320468
FMO2-HF: Total energy	-30825.589211
FMO2-MP2: Total energy	-30916.262096

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.
181.405	183.093	0.159	-0.623	-1.225	-0.002

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 : 0.929 / q_NPA : 0.948

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	VAL	0	-0.005	-0.008	2.791	5.318	6.996	0.160	-0.619	-1.220	-0.002
4	A	4	CYS	-1	-0.868	-0.690	5.264	-28.048	-28.038	-0.001	-0.004	-0.005	0.000
5	A	5	GLN	0	0.063	0.023	6.977	0.170	0.170	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.048	0.032	8.798	1.993	1.993	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.029	-0.132	11.623	1.077	1.077	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.083	0.050	8.663	1.150	1.150	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.897	0.947	8.740	19.229	19.229	0.000	0.000	0.000	0.000
10	A	10	ARG	1	1.015	1.003	4.951	32.177	32.177	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.066	-0.042	6.007	2.975	2.975	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.047	0.050	9.109	-0.181	-0.181	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.031	0.004	12.282	0.375	0.375	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.008	-0.001	14.722	0.543	0.543	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.018	-0.025	18.284	-0.230	-0.230	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.008	0.020	19.754	-0.213	-0.213	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.919	0.955	22.819	11.303	11.303	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.024	0.005	26.532	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	HIS	0	0.069	0.025	29.214	-0.195	-0.195	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.026	0.024	32.503	0.238	0.238	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.015	-0.003	30.431	-0.086	-0.086	0.000	0.000	0.000	0.000
22	A	22	ASN	0	0.066	0.038	29.265	-0.154	-0.154	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.027	-0.006	24.772	-0.326	-0.326	0.000	0.000	0.000	0.000
24	A	24	THR	0	0.060	0.039	22.185	-0.176	-0.176	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.948	0.977	17.380	15.943	15.943	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.901	0.950	16.356	16.726	16.726	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.960	0.972	6.958	29.694	29.694	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.024	0.008	13.518	0.074	0.074	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.017	-0.016	8.091	-2.381	-2.381	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.000	0.013	8.501	2.206	2.206	0.000	0.000	0.000	0.000
31	A	31	ASN	0	0.021	0.000	10.760	-1.239	-1.239	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.059	-0.038	6.888	-0.695	-0.695	0.000	0.000	0.000	0.000
33	A	33	HIS	0	0.052	0.030	11.433	-0.806	-0.806	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.035	-0.016	9.777	-2.084	-2.084	0.000	0.000	0.000	0.000
35	A	35	HIS	0	0.014	0.019	11.261	1.832	1.832	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.969	0.989	14.302	14.521	14.521	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.003	-0.007	15.089	0.664	0.664	0.000	0.000	0.000	0.000
38	A	38	TRP	0	0.017	0.004	19.329	-0.625	-0.625	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.010	-0.005	20.836	-0.072	-0.072	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.787	-0.897	23.528	-10.809	-10.809	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.065	-0.044	23.858	0.358	0.358	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.855	-0.925	22.181	-13.845	-13.845	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.842	0.944	24.964	10.705	10.705	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.893	0.930	19.799	15.013	15.013	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.016	-0.023	19.100	-0.190	-0.190	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.044	0.033	16.051	-0.314	-0.314	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.037	-0.027	12.476	0.529	0.529	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.041	0.027	11.130	-1.534	-1.534	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.904	0.947	5.274	44.392	44.392	0.000	0.000	0.000	0.000
50	A	50	VAL	0	0.050	0.034	9.004	-0.326	-0.326	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.005	-0.127	11.766	0.409	0.409	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.043	0.017	12.874	1.165	1.165	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.874	0.935	15.710	16.448	16.448	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.054	0.011	14.465	0.883	0.883	0.000	0.000	0.000	0.000
55	A	55	MET	0	0.027	0.011	15.511	0.302	0.302	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.992	0.994	17.840	14.483	14.483	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.085	-0.040	17.675	0.690	0.690	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.012	-0.002	16.214	0.351	0.351	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.862	-0.913	20.371	-13.360	-13.360	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.827	0.924	22.904	12.159	12.159	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.837	0.906	19.737	15.443	15.443	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.084	0.053	23.159	-0.141	-0.141	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.071	0.048	19.950	-0.564	-0.564	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.801	-0.896	20.257	-13.997	-13.997	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.075	-0.054	21.575	-0.163	-0.163	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.014	0.008	15.926	-0.489	-0.489	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.042	0.016	16.924	-1.007	-1.007	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.011	0.004	17.903	-0.379	-0.379	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.835	-0.914	17.106	-15.841	-15.841	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.053	-0.024	11.748	-0.910	-0.910	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.949	0.976	14.559	13.732	13.732	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.013	0.002	17.175	-0.078	-0.078	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.844	0.916	11.822	22.075	22.075	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.028	0.032	13.015	-1.190	-1.190	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.923	-0.971	8.082	-35.378	-35.378	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.799	0.895	10.055	25.809	25.809	0.000	0.000	0.000	0.000
77	A	77	TYR	-1	-0.867	-0.930	10.812	-23.724	-23.724	0.000	0.000	0.000	0.000

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