FMO DATABASE

FMODB ID: 3ZG1L

Calculation Name: 4PCW-A-Xray547

Preferred Name:

Target Type:

Ligand Name: nonaethylene glycol | calcium ion

Ligand 3-letter code: 2PE | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4PCW

Chain ID: A

ChEMBL ID:

UniProt ID: P20930

Base Structure: X-ray

Registration Date: 2025-10-04

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	-643407.925283
FMO2-HF: Nuclear repulsion	607032.680988
FMO2-HF: Total energy	-36375.244295
FMO2-MP2: Total energy	-36481.519138

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.
-169.608	-161.601	12.912	-10.801	-10.118	-0.136

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 : 0.767 / q_NPA : 0.880

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	LEU	0	0.071	0.023	2.923	-12.617	-10.752	0.166	-1.108	-0.924	-0.007
4	A	4	LEU	0	0.030	0.014	5.392	2.564	2.658	-0.001	-0.003	-0.090	0.000
5	A	5	GLU	-1	-0.749	-0.848	2.027	-130.428	-126.761	12.508	-8.267	-7.908	-0.111
6	A	6	ASN	0	-0.002	-0.002	2.650	-10.702	-8.373	0.240	-1.421	-1.148	-0.018
7	A	7	ILE	0	0.050	0.030	4.993	6.123	6.175	-0.001	-0.002	-0.048	0.000
8	A	8	PHE	0	0.003	-0.012	7.600	3.823	3.823	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.016	0.002	6.915	3.365	3.365	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.025	0.013	8.712	3.338	3.338	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.022	-0.010	10.988	2.503	2.503	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.041	-0.039	10.896	3.423	3.423	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.025	0.030	12.259	1.597	1.597	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.021	0.008	14.176	1.384	1.384	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.950	0.972	16.583	18.247	18.247	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.033	0.006	16.048	0.166	0.166	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.117	-0.098	17.019	1.452	1.452	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.005	-0.019	20.795	0.371	0.371	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.902	0.964	20.763	15.149	15.149	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.836	0.935	21.967	14.172	14.172	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.814	-0.887	26.178	-10.601	-10.601	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.891	0.943	28.788	9.225	9.225	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.113	-0.069	28.669	0.308	0.308	0.000	0.000	0.000	0.000
24	A	24	THR	0	0.013	-0.016	24.413	-0.176	-0.176	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.882	-0.915	22.844	-14.050	-14.050	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.070	-0.046	23.312	-0.083	-0.083	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.023	0.007	20.393	0.173	0.173	0.000	0.000	0.000	0.000
28	A	28	SER	0	0.012	-0.024	24.620	0.509	0.509	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.885	0.916	26.892	9.445	9.445	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.933	0.969	28.367	10.461	10.461	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.747	-0.851	23.970	-12.441	-12.441	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.027	0.017	22.542	-0.600	-0.600	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.764	0.884	23.661	10.510	10.510	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.882	-0.969	23.254	-13.531	-13.531	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.001	0.014	17.615	-0.448	-0.448	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.025	-0.018	19.943	-0.528	-0.528	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.893	-0.938	22.077	-11.650	-11.650	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.821	0.917	18.898	13.978	13.978	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.829	-0.886	14.259	-20.991	-20.991	0.000	0.000	0.000	0.000
40	A	40	PHE	0	-0.007	-0.019	15.482	-0.934	-0.934	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.910	0.971	17.946	13.052	13.052	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.036	-0.051	21.391	0.309	0.309	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.021	0.005	17.192	0.354	0.354	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.026	0.023	19.574	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.846	0.915	21.842	12.123	12.123	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.009	0.001	25.042	0.318	0.318	0.000	0.000	0.000	0.000
47	A	47	PRO	0	-0.023	0.000	24.548	0.387	0.387	0.000	0.000	0.000	0.000
48	A	48	ASP	-1	-0.774	-0.880	27.674	-10.053	-10.053	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.855	-0.940	27.735	-10.722	-10.722	0.000	0.000	0.000	0.000
50	A	50	PRO	0	-0.083	-0.063	29.650	-0.121	-0.121	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.894	-0.926	32.817	-8.799	-8.799	0.000	0.000	0.000	0.000
52	A	52	MET	0	0.042	0.034	30.137	-0.145	-0.145	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.076	-0.048	28.428	-0.574	-0.574	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.846	-0.924	29.557	-9.661	-9.661	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.076	0.037	30.113	-0.137	-0.137	0.000	0.000	0.000	0.000
56	A	56	PHE	0	0.019	0.000	22.508	-0.225	-0.225	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.050	-0.007	26.754	-0.472	-0.472	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.904	-0.958	28.658	-9.770	-9.770	0.000	0.000	0.000	0.000
59	A	59	HIS	0	-0.062	-0.025	27.050	0.119	0.119	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.069	-0.035	22.228	-0.393	-0.393	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.791	-0.892	26.116	-10.451	-10.451	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.048	-0.028	26.319	0.459	0.459	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.868	-0.919	29.705	-10.169	-10.169	0.000	0.000	0.000	0.000
64	A	64	HIS	1	0.835	0.927	31.436	10.073	10.073	0.000	0.000	0.000	0.000
65	A	65	ASN	0	0.000	0.005	29.149	0.365	0.365	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.893	0.927	32.038	9.347	9.347	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.796	0.879	27.812	10.369	10.369	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.030	0.039	22.869	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.778	-0.893	23.573	-13.638	-13.638	0.000	0.000	0.000	0.000
70	A	70	PHE	0	0.005	-0.019	14.139	-0.651	-0.651	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.005	-0.005	18.921	-1.015	-1.015	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.798	-0.904	20.713	-12.357	-12.357	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.007	-0.008	14.869	-0.225	-0.225	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.018	-0.006	14.128	-0.761	-0.761	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.019	-0.003	17.344	-0.407	-0.407	0.000	0.000	0.000	0.000
76	A	76	MET	0	-0.036	0.002	18.745	-0.085	-0.085	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.029	0.003	12.897	-0.327	-0.327	0.000	0.000	0.000	0.000
78	A	78	PHE	0	-0.021	-0.024	12.345	-1.015	-1.015	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.974	0.991	16.272	13.015	13.015	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.011	0.001	16.056	0.282	0.282	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.019	-0.010	13.170	-0.161	-0.161	0.000	0.000	0.000	0.000
82	A	82	GLN	0	-0.049	-0.029	14.725	0.013	0.013	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.046	-0.022	17.948	0.575	0.575	0.000	0.000	0.000	0.000
84	A	84	TYR	0	0.012	-0.016	15.392	0.377	0.377	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.067	-0.015	15.287	-0.170	-0.170	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-1.034	-1.000	17.111	-14.047	-14.047	0.000	0.000	0.000	0.000
87	A	87	SER	-1	-0.962	-0.973	17.032	-17.088	-17.088	0.000	0.000	0.000	0.000

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