FMO DATABASE

FMODB ID: ZZ74N

Calculation Name: 2GN5-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2GN5

Chain ID: A

ChEMBL ID:

UniProt ID: P69542

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	87
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-547566.786932
FMO2-HF: Nuclear repulsion	513687.378409
FMO2-HF: Total energy	-33879.408523
FMO2-MP2: Total energy	-33978.285877

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:MET)

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

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.
-81.663	-76.426	1.083	-2.608	-3.711	-0.029

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.817 / q_NPA : 0.904

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	3	LYS	0	0.052	0.043	3.219	-0.879	1.174	0.051	-0.656	-1.447	-0.002
60	A	60	LEU	0	-0.018	-0.011	4.761	-0.068	-0.008	-0.001	0.000	-0.058	0.000
86	A	86	ALA	0	-0.023	-0.010	3.589	-1.365	-1.227	0.005	-0.026	-0.118	0.000
87	A	87	LYS	-1	-0.954	-0.974	2.522	-54.371	-51.385	1.028	-1.926	-2.088	-0.027
4	A	4	VAL	0	0.022	-0.012	5.832	0.799	0.799	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.879	-0.930	6.224	-28.573	-28.573	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.068	0.040	7.673	1.548	1.548	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.840	0.902	6.432	29.720	29.720	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.020	-0.007	8.449	0.108	0.108	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.093	0.072	11.687	0.473	0.473	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.040	-0.019	14.389	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.016	0.003	16.258	0.420	0.420	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.016	-0.007	19.491	0.404	0.404	0.000	0.000	0.000	0.000
13	A	13	PHE	0	-0.102	-0.033	15.924	0.612	0.612	0.000	0.000	0.000	0.000
14	A	14	THR	0	0.014	-0.002	18.711	-0.494	-0.494	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.043	-0.022	20.708	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	ARG	1	1.016	1.025	23.559	9.654	9.654	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.063	-0.053	25.424	0.273	0.273	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.011	0.013	28.361	0.134	0.134	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.045	0.026	29.991	0.161	0.161	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.012	-0.009	32.573	0.259	0.259	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.890	0.948	35.544	7.180	7.180	0.000	0.000	0.000	0.000
22	A	22	GLN	0	0.047	0.039	36.572	0.025	0.025	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.019	-0.004	38.818	0.110	0.110	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.906	0.930	40.247	6.783	6.783	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.004	0.001	41.221	-0.106	-0.106	0.000	0.000	0.000	0.000
26	A	26	TYR	0	0.058	0.047	39.430	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.059	-0.030	37.363	0.139	0.139	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.035	0.007	33.346	-0.127	-0.127	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.036	-0.001	31.054	0.317	0.317	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.828	-0.917	27.650	-10.430	-10.430	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.068	-0.046	24.073	0.558	0.558	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.009	0.005	24.380	-0.365	-0.365	0.000	0.000	0.000	0.000
33	A	33	CYS	0	-0.003	-0.014	18.767	0.181	0.181	0.000	0.000	0.000	0.000
34	A	34	TYR	0	0.014	0.007	20.083	-0.038	-0.038	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.003	0.002	14.266	-0.318	-0.318	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.818	-0.909	14.471	-15.725	-15.725	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.022	-0.012	11.745	-0.972	-0.972	0.000	0.000	0.000	0.000
38	A	38	GLY	0	-0.046	-0.015	10.193	0.801	0.801	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.006	-0.007	11.260	0.903	0.903	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.909	-0.946	13.384	-19.618	-19.618	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.034	-0.025	15.685	0.429	0.429	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.042	-0.018	12.338	-0.195	-0.195	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.002	-0.018	14.104	1.106	1.106	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.004	-0.005	16.823	-0.397	-0.397	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.019	0.007	17.193	0.312	0.312	0.000	0.000	0.000	0.000
46	A	46	LYS	0	-0.022	-0.021	19.720	0.162	0.162	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.004	0.009	15.439	-0.179	-0.179	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.048	-0.027	20.078	0.312	0.312	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.013	-0.015	19.582	-0.260	-0.260	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.785	-0.894	21.503	-12.833	-12.833	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.865	-0.961	24.367	-10.634	-10.634	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.075	-0.025	27.500	0.281	0.281	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.069	-0.023	22.675	0.015	0.015	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.008	-0.006	22.648	-0.040	-0.040	0.000	0.000	0.000	0.000
55	A	55	ALA	0	0.026	0.017	21.005	-0.387	-0.387	0.000	0.000	0.000	0.000
56	A	56	TYR	0	0.015	0.010	15.473	-0.164	-0.164	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.019	0.003	16.039	0.547	0.547	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.021	-0.035	14.651	-0.830	-0.830	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.009	0.012	11.520	0.071	0.071	0.000	0.000	0.000	0.000
61	A	61	TYR	0	0.024	0.022	8.182	-0.207	-0.207	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.056	-0.044	6.091	-0.890	-0.890	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.046	0.037	8.641	1.920	1.920	0.000	0.000	0.000	0.000
64	A	64	HIS	0	0.022	0.001	10.956	-1.023	-1.023	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.020	0.010	14.192	0.549	0.549	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.025	0.012	16.731	0.729	0.729	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.006	0.002	15.459	-1.018	-1.018	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.008	-0.009	13.149	0.374	0.374	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.829	0.905	19.050	11.952	11.952	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.007	-0.001	22.695	-0.213	-0.213	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.012	0.020	25.785	0.156	0.156	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.033	-0.034	28.752	0.398	0.398	0.000	0.000	0.000	0.000
73	A	73	PHE	0	0.034	0.007	28.551	-0.357	-0.357	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.006	-0.006	25.586	-0.136	-0.136	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.012	0.014	19.447	0.126	0.126	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.004	-0.013	22.206	0.210	0.210	0.000	0.000	0.000	0.000
77	A	77	MET	0	0.031	0.015	15.596	-0.119	-0.119	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.045	-0.008	20.432	0.277	0.277	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.851	-0.914	22.891	-11.819	-11.819	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.904	0.956	19.997	12.494	12.494	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.000	0.001	14.380	-0.553	-0.553	0.000	0.000	0.000	0.000
82	A	82	ARG	0	-0.064	-0.030	16.307	1.038	1.038	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.012	0.007	12.114	-1.240	-1.240	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.011	0.010	9.947	1.285	1.285	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.016	-0.001	8.993	-0.981	-0.981	0.000	0.000	0.000	0.000

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