FMO DATABASE

FMODB ID: Q5YYY

Calculation Name: 7C7X-B-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7C7X

Chain ID: B

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

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	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-496872.647566
FMO2-HF: Nuclear repulsion	461656.224037
FMO2-HF: Total energy	-35216.423529
FMO2-MP2: Total energy	-35320.113767

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:57:ASN)

Summations of interaction energy for fragment #1(A:57:ASN)

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.
-1.8	3.602	1.164	-2.923	-3.642	-0.032

Interaction energy analysis for fragmet #1(A:57:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.846 / q_NPA : 0.914

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	59	GLU	-1	-0.828	-0.893	2.488	-70.820	-65.554	1.167	-2.918	-3.515	-0.032
4	A	60	THR	0	-0.039	-0.016	5.323	4.140	4.136	-0.001	0.000	0.005	0.000
35	A	91	ASN	0	-0.032	-0.025	4.984	-7.275	-7.262	-0.001	-0.002	-0.010	0.000
39	A	95	GLU	-1	-0.894	-0.955	4.952	-51.408	-51.281	-0.001	-0.003	-0.122	0.000
5	A	61	TYR	0	0.086	0.023	6.927	1.333	1.333	0.000	0.000	0.000	0.000
6	A	62	LYS	1	0.945	0.959	11.384	26.613	26.613	0.000	0.000	0.000	0.000
7	A	63	ILE	0	0.017	0.020	14.054	1.257	1.257	0.000	0.000	0.000	0.000
8	A	64	TYR	0	0.043	0.010	12.981	0.845	0.845	0.000	0.000	0.000	0.000
9	A	65	ILE	0	0.009	0.009	13.171	0.781	0.781	0.000	0.000	0.000	0.000
10	A	66	PHE	0	-0.001	-0.004	17.173	0.887	0.887	0.000	0.000	0.000	0.000
11	A	67	LYS	1	0.944	0.967	19.627	14.305	14.305	0.000	0.000	0.000	0.000
12	A	68	VAL	0	0.076	0.043	19.643	0.611	0.611	0.000	0.000	0.000	0.000
13	A	69	LEU	0	-0.023	-0.005	21.376	0.526	0.526	0.000	0.000	0.000	0.000
14	A	70	LYS	1	0.756	0.860	23.209	12.455	12.455	0.000	0.000	0.000	0.000
15	A	71	GLN	0	-0.017	-0.002	24.236	0.014	0.014	0.000	0.000	0.000	0.000
16	A	72	VAL	0	-0.032	-0.016	24.666	0.370	0.370	0.000	0.000	0.000	0.000
17	A	73	HIS	0	0.024	0.006	26.775	0.502	0.502	0.000	0.000	0.000	0.000
18	A	74	PRO	0	0.024	0.020	27.950	-0.295	-0.295	0.000	0.000	0.000	0.000
19	A	75	ASP	-1	-0.867	-0.923	29.132	-9.783	-9.783	0.000	0.000	0.000	0.000
20	A	76	ILE	0	-0.017	0.013	26.945	0.017	0.017	0.000	0.000	0.000	0.000
21	A	77	GLY	0	0.000	0.006	25.802	-0.392	-0.392	0.000	0.000	0.000	0.000
22	A	78	ILE	0	0.004	-0.014	19.193	-0.197	-0.197	0.000	0.000	0.000	0.000
23	A	79	SER	0	0.047	0.028	22.089	-0.260	-0.260	0.000	0.000	0.000	0.000
24	A	80	SER	0	0.062	0.012	18.067	-0.523	-0.523	0.000	0.000	0.000	0.000
25	A	81	LYS	1	0.968	0.987	16.129	17.487	17.487	0.000	0.000	0.000	0.000
26	A	82	ALA	0	0.036	0.032	17.145	-0.855	-0.855	0.000	0.000	0.000	0.000
27	A	83	MET	0	0.047	0.029	15.290	-1.082	-1.082	0.000	0.000	0.000	0.000
28	A	84	GLY	0	-0.036	-0.022	13.288	-1.542	-1.542	0.000	0.000	0.000	0.000
29	A	85	ILE	0	-0.009	0.017	12.811	-2.037	-2.037	0.000	0.000	0.000	0.000
30	A	86	MET	0	0.054	0.023	14.079	-0.920	-0.920	0.000	0.000	0.000	0.000
31	A	87	ASN	0	-0.023	-0.028	8.283	1.135	1.135	0.000	0.000	0.000	0.000
32	A	88	SER	0	-0.023	-0.016	9.625	-3.527	-3.527	0.000	0.000	0.000	0.000
33	A	89	PHE	0	0.016	0.005	10.366	-1.271	-1.271	0.000	0.000	0.000	0.000
34	A	90	ILE	0	0.007	0.006	10.302	-0.170	-0.170	0.000	0.000	0.000	0.000
36	A	92	ASP	-1	-0.819	-0.908	7.687	-28.181	-28.181	0.000	0.000	0.000	0.000
37	A	93	ILE	0	-0.038	-0.016	9.764	1.646	1.646	0.000	0.000	0.000	0.000
38	A	94	PHE	0	0.005	0.003	5.590	2.078	2.078	0.000	0.000	0.000	0.000
40	A	96	LYS	1	0.833	0.920	8.170	26.311	26.311	0.000	0.000	0.000	0.000
41	A	97	LEU	0	0.020	0.013	11.827	1.529	1.529	0.000	0.000	0.000	0.000
42	A	98	ALA	0	0.016	0.025	8.304	1.729	1.729	0.000	0.000	0.000	0.000
43	A	99	GLN	0	-0.001	-0.012	7.825	3.225	3.225	0.000	0.000	0.000	0.000
44	A	100	GLU	-1	-0.838	-0.905	11.038	-16.330	-16.330	0.000	0.000	0.000	0.000
45	A	101	SER	0	-0.002	-0.015	13.182	1.634	1.634	0.000	0.000	0.000	0.000
46	A	102	SER	0	-0.026	-0.011	11.489	1.127	1.127	0.000	0.000	0.000	0.000
47	A	103	LYS	1	0.823	0.901	13.636	19.167	19.167	0.000	0.000	0.000	0.000
48	A	104	LEU	0	0.027	0.007	16.478	0.997	0.997	0.000	0.000	0.000	0.000
49	A	105	ALA	0	-0.020	-0.018	16.193	0.850	0.850	0.000	0.000	0.000	0.000
50	A	106	ARG	1	0.921	0.973	12.106	20.440	20.440	0.000	0.000	0.000	0.000
51	A	107	TYR	0	-0.021	0.004	18.996	0.626	0.626	0.000	0.000	0.000	0.000
52	A	108	ASN	0	0.020	0.005	21.778	0.998	0.998	0.000	0.000	0.000	0.000
53	A	109	LYS	1	0.923	0.956	22.134	12.583	12.583	0.000	0.000	0.000	0.000
54	A	110	LYS	1	0.922	0.968	25.374	10.395	10.395	0.000	0.000	0.000	0.000
55	A	111	PRO	0	0.018	0.018	25.330	-0.404	-0.404	0.000	0.000	0.000	0.000
56	A	112	THR	0	-0.003	-0.009	22.436	0.100	0.100	0.000	0.000	0.000	0.000
57	A	113	ILE	0	-0.002	0.007	24.958	-0.141	-0.141	0.000	0.000	0.000	0.000
58	A	114	THR	0	-0.024	-0.041	21.192	-0.217	-0.217	0.000	0.000	0.000	0.000
59	A	115	SER	0	0.062	0.011	22.936	0.338	0.338	0.000	0.000	0.000	0.000
60	A	116	ARG	1	0.958	0.988	18.384	13.997	13.997	0.000	0.000	0.000	0.000
61	A	117	GLU	-1	-0.790	-0.860	23.964	-11.743	-11.743	0.000	0.000	0.000	0.000
62	A	118	ILE	0	0.024	0.015	27.183	0.407	0.407	0.000	0.000	0.000	0.000
63	A	119	GLN	0	0.018	0.019	25.623	0.339	0.339	0.000	0.000	0.000	0.000
64	A	120	THR	0	-0.039	-0.030	27.070	0.214	0.214	0.000	0.000	0.000	0.000
65	A	121	ALA	0	0.020	0.002	29.670	0.296	0.296	0.000	0.000	0.000	0.000
66	A	122	VAL	0	0.000	-0.005	32.193	0.301	0.301	0.000	0.000	0.000	0.000
67	A	123	ARG	1	0.874	0.917	27.874	10.154	10.154	0.000	0.000	0.000	0.000
68	A	124	LEU	0	-0.027	0.001	32.748	0.150	0.150	0.000	0.000	0.000	0.000
69	A	125	VAL	0	-0.019	0.007	35.896	0.216	0.216	0.000	0.000	0.000	0.000
70	A	126	LEU	0	-0.019	-0.003	37.037	0.227	0.227	0.000	0.000	0.000	0.000
71	A	127	PRO	0	0.035	0.019	38.595	-0.109	-0.109	0.000	0.000	0.000	0.000
72	A	128	GLY	0	0.033	0.002	38.660	0.054	0.054	0.000	0.000	0.000	0.000
73	A	129	GLU	-1	-0.829	-0.912	37.736	-8.060	-8.060	0.000	0.000	0.000	0.000
74	A	130	LEU	0	0.015	0.006	38.490	-0.129	-0.129	0.000	0.000	0.000	0.000
75	A	131	ALA	0	0.016	0.018	35.114	-0.163	-0.163	0.000	0.000	0.000	0.000
76	A	132	LYS	1	0.860	0.917	33.855	7.839	7.839	0.000	0.000	0.000	0.000
77	A	133	HIS	0	0.028	0.013	33.757	-0.393	-0.393	0.000	0.000	0.000	0.000
78	A	134	ALA	0	0.031	0.019	34.682	-0.183	-0.183	0.000	0.000	0.000	0.000
79	A	135	VAL	0	-0.017	-0.011	28.939	-0.280	-0.280	0.000	0.000	0.000	0.000
80	A	136	SER	0	-0.031	0.008	29.895	-0.475	-0.475	0.000	0.000	0.000	0.000
81	A	137	GLU	-1	-0.896	-0.949	30.539	-8.978	-8.978	0.000	0.000	0.000	0.000
82	A	138	GLY	0	0.007	0.003	30.412	-0.196	-0.196	0.000	0.000	0.000	0.000
83	A	139	THR	0	-0.040	-0.050	24.867	-0.444	-0.444	0.000	0.000	0.000	0.000
84	A	140	LYS	1	0.954	0.996	26.225	8.820	8.820	0.000	0.000	0.000	0.000
85	A	141	ALA	0	-0.009	0.007	27.915	-0.220	-0.220	0.000	0.000	0.000	0.000
86	A	142	VAL	0	-0.002	-0.009	22.804	-0.208	-0.208	0.000	0.000	0.000	0.000
87	A	143	THR	0	-0.031	-0.036	22.549	-0.565	-0.565	0.000	0.000	0.000	0.000
88	A	144	LYS	1	0.944	0.969	23.637	9.832	9.832	0.000	0.000	0.000	0.000
89	A	145	PHE	0	-0.061	-0.022	22.605	0.126	0.126	0.000	0.000	0.000	0.000
90	A	146	THR	0	-0.072	-0.038	18.845	-0.434	-0.434	0.000	0.000	0.000	0.000
91	A	147	SER	-1	-0.965	-0.962	20.392	-13.613	-13.613	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:57:ASN)