FMO DATABASE

FMODB ID: 7ZJKK

Calculation Name: 2PWW-A-Xray549

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol

Ligand 3-letter code: EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2PWW

Chain ID: A

ChEMBL ID:

UniProt ID: Q5WFD8

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-939834.211021
FMO2-HF: Nuclear repulsion	894162.284199
FMO2-HF: Total energy	-45671.926823
FMO2-MP2: Total energy	-45806.720192

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:0:SER)

Summations of interaction energy for fragment #1(A:0: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.
-151.795	-157.874	42.058	-21.744	-14.236	-0.211

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.676 / q_NPA : 0.804

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	2	LYS	1	0.926	0.960	3.547	42.196	43.747	0.001	-0.743	-0.809	-0.001
53	A	52	TYR	0	-0.046	-0.017	4.498	0.343	0.506	-0.001	-0.015	-0.147	0.000
78	A	77	ILE	0	-0.042	-0.027	2.023	-8.031	-9.181	4.116	-1.378	-1.587	-0.012
79	A	78	LEU	0	0.007	0.019	3.809	5.084	5.917	0.001	-0.408	-0.427	-0.001
80	A	79	GLY	0	0.009	0.008	1.753	-49.220	-50.593	12.031	-6.733	-3.926	-0.084
81	A	80	LYS	1	0.941	0.995	3.593	38.790	39.024	0.009	-0.113	-0.131	-0.001
93	A	92	GLU	-1	-0.800	-0.886	1.572	-108.507	-115.595	25.215	-11.793	-6.334	-0.107
95	A	94	PHE	0	-0.025	-0.012	2.292	0.062	0.813	0.686	-0.561	-0.875	-0.005
4	A	3	PHE	0	0.014	-0.006	5.587	2.872	2.872	0.000	0.000	0.000	0.000
5	A	4	PRO	0	0.028	0.004	8.888	0.467	0.467	0.000	0.000	0.000	0.000
6	A	5	ASP	-1	-0.899	-0.933	11.337	-20.231	-20.231	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.070	-0.041	11.885	1.129	1.129	0.000	0.000	0.000	0.000
8	A	7	GLY	0	0.043	0.014	14.934	1.040	1.040	0.000	0.000	0.000	0.000
9	A	8	LEU	0	-0.069	-0.038	13.119	0.870	0.870	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.801	-0.896	12.421	-22.388	-22.388	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.927	-0.940	16.329	-14.647	-14.647	0.000	0.000	0.000	0.000
12	A	11	LYS	1	0.874	0.929	19.849	13.630	13.630	0.000	0.000	0.000	0.000
13	A	12	GLU	-1	-0.804	-0.892	20.697	-13.030	-13.030	0.000	0.000	0.000	0.000
14	A	13	VAL	0	-0.024	-0.018	20.412	0.553	0.553	0.000	0.000	0.000	0.000
15	A	14	ALA	0	0.028	0.018	23.110	-0.096	-0.096	0.000	0.000	0.000	0.000
16	A	15	PHE	0	0.053	0.013	19.883	-0.356	-0.356	0.000	0.000	0.000	0.000
17	A	16	SER	0	-0.054	-0.042	22.252	-0.416	-0.416	0.000	0.000	0.000	0.000
18	A	17	ILE	0	0.013	0.018	23.113	-0.082	-0.082	0.000	0.000	0.000	0.000
19	A	18	VAL	0	0.029	0.019	17.307	-0.285	-0.285	0.000	0.000	0.000	0.000
20	A	19	ASN	0	0.013	0.000	19.467	-1.060	-1.060	0.000	0.000	0.000	0.000
21	A	20	HIS	0	0.006	0.010	20.940	-0.258	-0.258	0.000	0.000	0.000	0.000
22	A	21	ALA	0	0.042	0.024	20.402	-0.031	-0.031	0.000	0.000	0.000	0.000
23	A	22	ALA	0	0.021	0.017	16.994	-0.280	-0.280	0.000	0.000	0.000	0.000
24	A	23	LYS	1	0.878	0.937	18.539	15.813	15.813	0.000	0.000	0.000	0.000
25	A	24	SER	0	-0.040	-0.019	21.068	0.206	0.206	0.000	0.000	0.000	0.000
26	A	25	LEU	0	-0.014	0.005	18.364	0.061	0.061	0.000	0.000	0.000	0.000
27	A	26	GLY	0	-0.011	-0.002	18.161	-0.848	-0.848	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.037	-0.019	11.878	-0.619	-0.619	0.000	0.000	0.000	0.000
29	A	28	ILE	0	-0.023	-0.018	14.389	1.379	1.379	0.000	0.000	0.000	0.000
30	A	29	HIS	0	-0.047	-0.025	15.305	-1.403	-1.403	0.000	0.000	0.000	0.000
31	A	30	VAL	0	0.001	0.000	11.390	0.436	0.436	0.000	0.000	0.000	0.000
32	A	31	ASP	-1	-0.883	-0.924	14.773	-14.757	-14.757	0.000	0.000	0.000	0.000
33	A	32	GLN	0	-0.021	-0.019	15.199	-0.865	-0.865	0.000	0.000	0.000	0.000
34	A	33	TRP	0	-0.055	-0.031	17.225	-0.233	-0.233	0.000	0.000	0.000	0.000
35	A	34	ASP	-1	-0.823	-0.926	17.510	-16.629	-16.629	0.000	0.000	0.000	0.000
36	A	35	TYR	0	0.015	0.017	20.261	0.211	0.211	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.917	-0.955	19.815	-13.878	-13.878	0.000	0.000	0.000	0.000
38	A	37	ARG	1	0.842	0.918	12.560	20.722	20.722	0.000	0.000	0.000	0.000
39	A	38	VAL	0	-0.004	0.016	16.077	0.700	0.700	0.000	0.000	0.000	0.000
40	A	39	MET	0	-0.015	-0.013	11.311	-2.630	-2.630	0.000	0.000	0.000	0.000
41	A	40	PHE	0	0.009	0.017	12.815	1.254	1.254	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.718	-0.832	10.042	-33.408	-33.408	0.000	0.000	0.000	0.000
43	A	42	TYR	0	-0.006	-0.007	11.018	2.746	2.746	0.000	0.000	0.000	0.000
44	A	43	LYS	1	0.977	0.988	10.864	16.776	16.776	0.000	0.000	0.000	0.000
45	A	44	ILE	0	-0.013	-0.009	10.167	1.893	1.893	0.000	0.000	0.000	0.000
46	A	45	VAL	0	-0.014	-0.013	12.468	-1.158	-1.158	0.000	0.000	0.000	0.000
47	A	46	HIS	0	0.005	0.006	13.235	0.221	0.221	0.000	0.000	0.000	0.000
48	A	47	HIS	0	0.029	0.017	15.288	0.105	0.105	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.863	-0.943	12.437	-21.846	-21.846	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.012	0.006	12.051	-1.488	-1.488	0.000	0.000	0.000	0.000
51	A	50	THR	0	-0.071	-0.039	12.032	1.083	1.083	0.000	0.000	0.000	0.000
52	A	51	PHE	0	0.041	0.004	6.867	-1.770	-1.770	0.000	0.000	0.000	0.000
54	A	53	LEU	0	0.020	0.006	6.015	-6.925	-6.925	0.000	0.000	0.000	0.000
55	A	54	ARG	1	0.831	0.875	6.528	40.277	40.277	0.000	0.000	0.000	0.000
56	A	55	VAL	0	0.039	0.008	7.782	-2.609	-2.609	0.000	0.000	0.000	0.000
57	A	56	PRO	0	-0.040	-0.010	8.520	1.913	1.913	0.000	0.000	0.000	0.000
58	A	57	ALA	0	0.009	-0.003	11.390	0.391	0.391	0.000	0.000	0.000	0.000
59	A	58	TYR	0	0.026	0.007	11.127	-0.195	-0.195	0.000	0.000	0.000	0.000
60	A	59	ALA	0	0.006	0.003	17.279	0.470	0.470	0.000	0.000	0.000	0.000
61	A	60	VAL	0	-0.038	-0.005	21.089	-0.100	-0.100	0.000	0.000	0.000	0.000
62	A	61	LYS	1	0.846	0.922	23.298	12.378	12.378	0.000	0.000	0.000	0.000
63	A	62	GLY	0	0.004	0.015	26.829	0.108	0.108	0.000	0.000	0.000	0.000
64	A	63	GLU	-1	-0.828	-0.920	24.982	-11.341	-11.341	0.000	0.000	0.000	0.000
65	A	64	ILE	0	-0.039	0.012	18.978	0.224	0.224	0.000	0.000	0.000	0.000
66	A	65	PRO	0	0.012	-0.007	22.820	0.173	0.173	0.000	0.000	0.000	0.000
67	A	66	ARG	1	0.966	0.985	24.069	10.439	10.439	0.000	0.000	0.000	0.000
68	A	67	PRO	0	0.029	-0.004	26.387	-0.237	-0.237	0.000	0.000	0.000	0.000
69	A	68	SER	0	-0.020	-0.017	26.960	-0.171	-0.171	0.000	0.000	0.000	0.000
70	A	69	THR	0	-0.045	-0.022	23.705	0.407	0.407	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.035	-0.004	24.182	-0.334	-0.334	0.000	0.000	0.000	0.000
72	A	71	VAL	0	0.008	-0.011	19.276	-0.116	-0.116	0.000	0.000	0.000	0.000
73	A	72	GLN	0	-0.011	-0.009	16.364	1.069	1.069	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.019	-0.014	13.361	-0.772	-0.772	0.000	0.000	0.000	0.000
75	A	74	MET	0	0.009	0.002	10.953	0.811	0.811	0.000	0.000	0.000	0.000
76	A	75	THR	0	-0.031	-0.035	8.064	-0.940	-0.940	0.000	0.000	0.000	0.000
77	A	76	PRO	0	-0.044	-0.012	7.613	-3.940	-3.940	0.000	0.000	0.000	0.000
82	A	81	TYR	0	-0.025	-0.023	6.295	-2.146	-2.146	0.000	0.000	0.000	0.000
83	A	82	TYR	0	0.040	0.022	5.058	4.832	4.832	0.000	0.000	0.000	0.000
84	A	83	TYR	0	-0.016	0.009	10.586	1.252	1.252	0.000	0.000	0.000	0.000
85	A	84	PRO	0	-0.029	-0.025	13.974	0.247	0.247	0.000	0.000	0.000	0.000
86	A	85	HIS	0	0.004	-0.021	14.737	-0.547	-0.547	0.000	0.000	0.000	0.000
87	A	86	GLY	0	0.024	0.020	10.554	0.093	0.093	0.000	0.000	0.000	0.000
88	A	87	VAL	0	-0.054	-0.024	10.186	-1.537	-1.537	0.000	0.000	0.000	0.000
89	A	88	GLU	-1	-0.911	-0.958	5.813	-38.719	-38.719	0.000	0.000	0.000	0.000
90	A	89	TYR	0	-0.027	-0.023	10.146	0.999	0.999	0.000	0.000	0.000	0.000
91	A	90	GLU	-1	-0.955	-0.974	10.957	-20.890	-20.890	0.000	0.000	0.000	0.000
92	A	91	GLY	0	-0.003	0.016	8.192	-0.299	-0.299	0.000	0.000	0.000	0.000
94	A	93	THR	0	-0.006	-0.019	6.290	2.186	2.186	0.000	0.000	0.000	0.000
96	A	95	PRO	0	0.042	0.032	8.058	1.869	1.869	0.000	0.000	0.000	0.000
97	A	96	GLN	0	0.016	0.009	11.797	-1.536	-1.536	0.000	0.000	0.000	0.000
98	A	97	ALA	0	0.031	0.010	13.905	-0.215	-0.215	0.000	0.000	0.000	0.000
99	A	98	VAL	0	-0.021	-0.009	9.406	0.587	0.587	0.000	0.000	0.000	0.000
100	A	99	ILE	0	0.044	0.028	9.304	-1.234	-1.234	0.000	0.000	0.000	0.000
101	A	100	ASP	-1	-0.823	-0.914	11.273	-19.465	-19.465	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.887	0.957	13.224	19.106	19.106	0.000	0.000	0.000	0.000
103	A	102	CYS	0	-0.038	-0.021	9.338	-0.333	-0.333	0.000	0.000	0.000	0.000
104	A	103	ASN	0	0.040	0.016	11.625	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	104	ASN	0	-0.031	-0.023	13.927	1.542	1.542	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.816	0.922	13.500	19.393	19.393	0.000	0.000	0.000	0.000
107	A	106	LEU	0	0.023	0.008	9.874	0.824	0.824	0.000	0.000	0.000	0.000
108	A	107	ALA	0	0.013	0.020	14.516	1.034	1.034	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.037	0.018	17.741	0.912	0.912	0.000	0.000	0.000	0.000
110	A	109	LEU	0	0.020	0.015	14.729	0.811	0.811	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.019	-0.003	17.182	0.735	0.735	0.000	0.000	0.000	0.000
112	A	111	LYS	1	0.795	0.892	18.951	16.087	16.087	0.000	0.000	0.000	0.000
113	A	112	THR	0	-0.040	-0.025	21.439	0.678	0.678	0.000	0.000	0.000	0.000
114	A	113	ILE	0	-0.042	-0.024	18.297	0.387	0.387	0.000	0.000	0.000	0.000
115	A	114	LYS	0	0.002	0.026	22.450	0.399	0.399	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)