FMO DATABASE

FMODB ID: 24RQR

Calculation Name: 2BWL-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion

Ligand 3-letter code: PO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BWL

Chain ID: A

ChEMBL ID:

UniProt ID: P21570

Base Structure: X-ray

Registration Date: 2025-09-02

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-998482.365494
FMO2-HF: Nuclear repulsion	949755.84024
FMO2-HF: Total energy	-48726.525254
FMO2-MP2: Total energy	-48863.307873

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:2:ASP)

Summations of interaction energy for fragment #1(A:2:ASP)

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.
-94.486	-95.609	29.201	-15.757	-12.319	0.164

Interaction energy analysis for fragmet #1(A:2:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.040 / q_NPA : 0.034

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	4	SER	0	0.022	0.008	1.831	-34.348	-32.079	14.372	-8.969	-7.671	0.099
4	A	5	ARG	1	0.900	0.929	3.707	-8.148	-7.955	0.016	-0.013	-0.195	0.002
6	A	7	THR	0	0.013	-0.009	1.695	-25.402	-29.107	14.814	-6.750	-4.358	0.063
7	A	8	LYS	1	0.860	0.924	4.829	-0.202	-0.082	-0.001	-0.025	-0.095	0.000
5	A	6	TYR	0	0.086	0.046	6.191	-2.907	-2.907	0.000	0.000	0.000	0.000
8	A	9	PHE	0	-0.006	0.016	7.680	-2.199	-2.199	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.014	-0.020	7.149	-1.864	-1.864	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.028	-0.026	7.454	-1.948	-1.948	0.000	0.000	0.000	0.000
11	A	12	GLN	0	0.028	0.022	10.125	-0.980	-0.980	0.000	0.000	0.000	0.000
12	A	13	HIS	1	0.869	0.952	12.798	-3.153	-3.153	0.000	0.000	0.000	0.000
13	A	14	HIS	0	-0.030	-0.005	12.904	0.210	0.210	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.758	-0.870	14.560	1.289	1.289	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.016	0.030	16.896	-0.181	-0.181	0.000	0.000	0.000	0.000
16	A	17	LYS	1	1.019	1.010	18.537	-1.072	-1.072	0.000	0.000	0.000	0.000
17	A	18	PRO	0	-0.020	0.026	21.896	-0.076	-0.076	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.797	0.866	19.717	-1.153	-1.153	0.000	0.000	0.000	0.000
19	A	20	GLY	0	0.065	0.045	25.237	-0.099	-0.099	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.763	0.852	25.816	-0.917	-0.917	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.766	-0.883	27.691	0.434	0.434	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.753	-0.882	27.533	0.371	0.371	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.830	0.904	27.809	-0.116	-0.116	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.063	-0.074	20.412	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	26	CYS	0	-0.022	-0.012	22.848	-0.048	-0.048	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.726	-0.820	23.008	0.035	0.035	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.848	0.915	20.905	-0.504	-0.504	0.000	0.000	0.000	0.000
28	A	29	MET	0	-0.037	0.013	17.339	-0.154	-0.154	0.000	0.000	0.000	0.000
29	A	30	MET	0	0.014	0.022	18.455	0.074	0.074	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.980	0.998	18.579	0.370	0.370	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.918	0.962	16.191	-0.423	-0.423	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.775	0.860	13.196	-2.054	-2.054	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.007	0.008	13.187	-0.154	-0.154	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.058	-0.026	14.623	-0.090	-0.090	0.000	0.000	0.000	0.000
35	A	36	THR	0	0.021	-0.013	17.383	0.079	0.079	0.000	0.000	0.000	0.000
36	A	37	SER	0	0.013	0.017	17.292	0.046	0.046	0.000	0.000	0.000	0.000
37	A	38	PRO	0	0.016	0.001	18.364	-0.226	-0.226	0.000	0.000	0.000	0.000
38	A	39	CYS	0	-0.107	-0.004	20.057	0.003	0.003	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.843	0.930	16.092	-1.204	-1.204	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.863	-0.924	21.327	0.429	0.429	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.049	0.020	22.414	0.018	0.018	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.052	-0.032	16.980	0.166	0.166	0.000	0.000	0.000	0.000
43	A	44	THR	0	0.001	-0.002	19.917	-0.166	-0.166	0.000	0.000	0.000	0.000
44	A	45	PHE	0	-0.043	-0.010	16.224	0.284	0.284	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.036	0.017	16.606	-0.162	-0.162	0.000	0.000	0.000	0.000
46	A	47	HIS	0	-0.046	-0.008	18.235	0.010	0.010	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.055	0.026	20.540	0.019	0.019	0.000	0.000	0.000	0.000
48	A	49	ASN	0	-0.003	-0.006	18.295	0.447	0.447	0.000	0.000	0.000	0.000
49	A	50	LYS	1	1.025	0.998	9.608	-6.903	-6.903	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.005	0.007	15.053	0.503	0.503	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.057	0.012	17.017	0.115	0.115	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.030	0.016	15.205	-0.023	-0.023	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.948	0.975	11.557	-6.274	-6.274	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.013	0.012	15.731	-0.066	-0.066	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.017	0.006	18.700	-0.228	-0.228	0.000	0.000	0.000	0.000
56	A	57	CYS	0	-0.075	-0.044	14.337	0.399	0.399	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.020	0.030	18.481	-0.110	-0.110	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.052	0.019	20.859	-0.136	-0.136	0.000	0.000	0.000	0.000
59	A	60	ASN	0	0.019	0.010	22.612	-0.232	-0.232	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.019	0.013	22.903	-0.036	-0.036	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.083	-0.030	23.851	-0.116	-0.116	0.000	0.000	0.000	0.000
62	A	63	PRO	0	0.024	0.001	24.483	0.096	0.096	0.000	0.000	0.000	0.000
63	A	64	TYR	0	0.016	0.005	24.688	-0.145	-0.145	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.949	0.971	25.154	-0.897	-0.897	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.857	-0.922	25.453	1.113	1.113	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.027	-0.018	20.149	0.002	0.002	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.012	0.010	20.151	0.304	0.304	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.855	0.908	19.620	-2.410	-2.410	0.000	0.000	0.000	0.000
69	A	70	MET	0	0.034	0.028	21.981	0.069	0.069	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.035	-0.030	22.652	0.028	0.028	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.895	0.942	24.292	-1.715	-1.715	0.000	0.000	0.000	0.000
72	A	73	SER	0	0.017	0.023	25.426	-0.083	-0.083	0.000	0.000	0.000	0.000
73	A	74	PRO	0	0.023	0.021	25.972	0.114	0.114	0.000	0.000	0.000	0.000
74	A	75	PHE	0	-0.013	-0.014	20.147	0.135	0.135	0.000	0.000	0.000	0.000
75	A	76	GLN	0	0.026	0.024	24.077	-0.149	-0.149	0.000	0.000	0.000	0.000
76	A	77	VAL	0	0.011	-0.001	21.738	0.180	0.180	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.010	-0.024	22.568	-0.203	-0.203	0.000	0.000	0.000	0.000
78	A	79	THR	0	-0.016	-0.014	22.537	0.076	0.076	0.000	0.000	0.000	0.000
79	A	81	LYS	1	1.005	0.990	24.205	-0.688	-0.688	0.000	0.000	0.000	0.000
80	A	82	HIS	0	0.022	0.002	25.914	0.001	0.001	0.000	0.000	0.000	0.000
81	A	83	THR	0	-0.015	-0.010	27.722	0.020	0.020	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.033	0.016	30.549	-0.042	-0.042	0.000	0.000	0.000	0.000
83	A	85	GLY	0	0.014	0.012	30.525	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	86	SER	0	0.041	0.028	28.716	-0.043	-0.043	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.045	0.016	25.418	0.006	0.006	0.000	0.000	0.000	0.000
86	A	88	ARG	1	0.875	0.932	21.899	0.764	0.764	0.000	0.000	0.000	0.000
87	A	89	PRO	0	0.063	0.028	22.724	0.082	0.082	0.000	0.000	0.000	0.000
88	A	90	PRO	0	0.000	-0.009	25.502	-0.043	-0.043	0.000	0.000	0.000	0.000
89	A	92	GLN	0	-0.011	-0.008	26.119	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	93	TYR	0	-0.060	-0.068	22.947	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.913	0.968	28.007	-0.320	-0.320	0.000	0.000	0.000	0.000
92	A	95	ALA	0	-0.004	-0.020	27.516	0.063	0.063	0.000	0.000	0.000	0.000
93	A	96	SER	0	0.024	0.022	27.537	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	97	ALA	0	-0.021	-0.005	27.124	0.100	0.100	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.019	0.005	27.433	-0.068	-0.068	0.000	0.000	0.000	0.000
96	A	99	PHE	0	-0.024	-0.016	27.091	0.102	0.102	0.000	0.000	0.000	0.000
97	A	100	ARG	1	0.919	0.962	26.298	-1.042	-1.042	0.000	0.000	0.000	0.000
98	A	101	HIS	0	-0.018	-0.004	25.796	0.048	0.048	0.000	0.000	0.000	0.000
99	A	102	VAL	0	-0.018	-0.012	20.647	-0.038	-0.038	0.000	0.000	0.000	0.000
100	A	103	VAL	0	0.056	0.037	22.186	0.055	0.055	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.023	-0.014	16.607	0.132	0.132	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.064	0.037	16.074	-0.235	-0.235	0.000	0.000	0.000	0.000
103	A	107	GLU	-1	-0.792	-0.882	11.949	3.397	3.397	0.000	0.000	0.000	0.000
104	A	108	ASN	0	-0.020	-0.019	10.537	0.293	0.293	0.000	0.000	0.000	0.000
105	A	109	GLY	0	0.016	0.018	13.054	0.355	0.355	0.000	0.000	0.000	0.000
106	A	110	LEU	0	-0.090	-0.045	8.276	0.340	0.340	0.000	0.000	0.000	0.000
107	A	111	PRO	0	0.014	0.006	11.623	-0.326	-0.326	0.000	0.000	0.000	0.000
108	A	112	VAL	0	0.007	-0.013	9.549	1.418	1.418	0.000	0.000	0.000	0.000
109	A	113	HIS	0	0.002	-0.006	11.680	0.014	0.014	0.000	0.000	0.000	0.000
110	A	114	PHE	0	0.011	-0.011	14.804	0.206	0.206	0.000	0.000	0.000	0.000
111	A	115	ASP	-1	-0.814	-0.881	17.762	1.178	1.178	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.804	-0.904	19.535	1.466	1.466	0.000	0.000	0.000	0.000
113	A	117	SER	0	-0.110	-0.065	22.761	-0.146	-0.146	0.000	0.000	0.000	0.000
114	A	118	PHE	0	-0.014	-0.007	25.072	-0.048	-0.048	0.000	0.000	0.000	0.000
115	A	119	PHE	-1	-0.940	-0.967	23.947	0.837	0.837	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASP)