FMO DATABASE

FMODB ID: 9L3Z2

Calculation Name: 2A0S-A-Xray547

Preferred Name:

Target Type:

Ligand Name: biopterin

Ligand 3-letter code: BIO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A0S

Chain ID: A

ChEMBL ID:

UniProt ID: A5K2B2

Base Structure: X-ray

Registration Date: 2025-10-03

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	163
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1656369.735117
FMO2-HF: Nuclear repulsion	1590042.936204
FMO2-HF: Total energy	-66326.798913
FMO2-MP2: Total energy	-66519.924824

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:18:ASP)

Summations of interaction energy for fragment #1(A:18: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.
-14.46	-18.391	21.47	-7.244	-10.294	0.062

Interaction energy analysis for fragmet #1(A:18:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.038 / q_NPA : -0.033

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	20	ILE	0	0.045	0.030	3.095	10.798	14.072	1.090	-1.240	-3.124	0.005
4	A	21	ALA	0	0.000	-0.002	4.217	-5.893	-5.826	0.003	-0.040	-0.029	0.000
44	A	61	ASN	0	-0.067	-0.035	1.764	-16.326	-24.735	20.343	-5.678	-6.256	0.053
45	A	62	ILE	0	-0.023	-0.008	3.539	-10.372	-9.637	0.030	-0.240	-0.525	0.004
46	A	63	GLN	0	0.036	0.039	3.987	5.933	6.335	0.004	-0.046	-0.360	0.000
5	A	22	GLU	-1	-0.835	-0.911	7.519	3.670	3.670	0.000	0.000	0.000	0.000
6	A	23	LEU	0	-0.034	-0.009	10.385	-0.390	-0.390	0.000	0.000	0.000	0.000
7	A	24	LEU	0	0.010	0.002	13.218	-0.183	-0.183	0.000	0.000	0.000	0.000
8	A	25	VAL	0	-0.046	-0.023	16.990	-0.094	-0.094	0.000	0.000	0.000	0.000
9	A	26	GLU	-1	-0.874	-0.957	19.899	1.460	1.460	0.000	0.000	0.000	0.000
10	A	27	SER	0	0.004	-0.014	23.489	-0.061	-0.061	0.000	0.000	0.000	0.000
11	A	28	PRO	0	0.063	0.045	26.975	0.013	0.013	0.000	0.000	0.000	0.000
12	A	29	LEU	0	-0.057	-0.010	28.239	-0.040	-0.040	0.000	0.000	0.000	0.000
13	A	30	PHE	0	-0.079	-0.022	23.644	0.026	0.026	0.000	0.000	0.000	0.000
14	A	31	SER	0	0.053	0.003	28.485	0.008	0.008	0.000	0.000	0.000	0.000
15	A	32	PHE	0	-0.034	-0.027	30.291	0.006	0.006	0.000	0.000	0.000	0.000
16	A	33	ASN	0	-0.016	-0.003	34.310	0.013	0.013	0.000	0.000	0.000	0.000
17	A	34	CYS	0	-0.027	-0.002	37.479	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	35	ALA	0	0.014	0.005	39.376	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	36	HIS	1	0.815	0.885	39.187	-0.600	-0.600	0.000	0.000	0.000	0.000
20	A	37	PHE	0	0.003	0.002	42.268	-0.019	-0.019	0.000	0.000	0.000	0.000
21	A	38	ILE	0	-0.027	-0.011	38.820	0.017	0.017	0.000	0.000	0.000	0.000
22	A	39	ALA	0	0.032	0.003	42.845	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	40	PHE	0	-0.044	-0.034	42.457	0.029	0.029	0.000	0.000	0.000	0.000
24	A	41	LYS	1	0.968	0.988	44.848	-0.379	-0.379	0.000	0.000	0.000	0.000
25	A	42	GLY	0	-0.011	0.004	47.688	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	43	PHE	0	-0.048	-0.018	44.422	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	44	ARG	1	0.862	0.902	47.192	-0.350	-0.350	0.000	0.000	0.000	0.000
28	A	45	GLU	-1	-0.817	-0.852	42.962	0.494	0.494	0.000	0.000	0.000	0.000
29	A	46	THR	0	0.004	-0.015	47.637	0.002	0.002	0.000	0.000	0.000	0.000
30	A	47	LEU	0	-0.020	-0.005	45.797	0.019	0.019	0.000	0.000	0.000	0.000
31	A	48	HIS	1	0.841	0.912	41.292	-0.540	-0.540	0.000	0.000	0.000	0.000
32	A	49	GLY	0	0.021	0.001	41.951	0.012	0.012	0.000	0.000	0.000	0.000
33	A	50	HIS	0	-0.039	-0.021	37.222	-0.040	-0.040	0.000	0.000	0.000	0.000
34	A	51	ASN	0	0.003	0.005	36.216	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	52	TYR	0	-0.011	0.007	32.499	0.003	0.003	0.000	0.000	0.000	0.000
36	A	53	ASN	0	-0.037	-0.025	27.804	-0.042	-0.042	0.000	0.000	0.000	0.000
37	A	54	VAL	0	-0.008	-0.005	24.315	0.003	0.003	0.000	0.000	0.000	0.000
38	A	55	SER	0	-0.029	-0.018	22.286	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	56	LEU	0	0.014	0.008	17.951	-0.057	-0.057	0.000	0.000	0.000	0.000
40	A	57	ARG	1	0.902	0.943	15.628	-2.024	-2.024	0.000	0.000	0.000	0.000
41	A	58	LEU	0	0.002	0.000	12.563	-0.147	-0.147	0.000	0.000	0.000	0.000
42	A	59	ARG	1	0.815	0.902	9.030	-3.497	-3.497	0.000	0.000	0.000	0.000
43	A	60	GLY	0	0.101	0.046	6.829	-1.684	-1.684	0.000	0.000	0.000	0.000
47	A	64	GLY	0	-0.003	-0.015	6.162	-1.660	-1.660	0.000	0.000	0.000	0.000
48	A	65	ASP	-1	-0.813	-0.875	8.342	4.579	4.579	0.000	0.000	0.000	0.000
49	A	66	GLY	0	-0.016	0.001	9.005	-0.816	-0.816	0.000	0.000	0.000	0.000
50	A	67	TYR	0	-0.041	-0.022	9.826	-0.046	-0.046	0.000	0.000	0.000	0.000
51	A	68	VAL	0	0.019	0.037	6.808	0.915	0.915	0.000	0.000	0.000	0.000
52	A	69	ILE	0	0.023	0.001	8.787	-0.533	-0.533	0.000	0.000	0.000	0.000
53	A	70	ASP	-1	-0.786	-0.858	12.378	2.607	2.607	0.000	0.000	0.000	0.000
54	A	71	PHE	0	0.040	-0.001	15.282	-0.154	-0.154	0.000	0.000	0.000	0.000
55	A	72	SER	0	-0.090	-0.062	17.853	-0.268	-0.268	0.000	0.000	0.000	0.000
56	A	73	ILE	0	0.069	0.031	17.012	-0.186	-0.186	0.000	0.000	0.000	0.000
57	A	74	LEU	0	0.019	0.013	15.388	-0.209	-0.209	0.000	0.000	0.000	0.000
58	A	75	LYS	1	0.921	0.956	19.915	-1.953	-1.953	0.000	0.000	0.000	0.000
59	A	76	GLU	-1	-0.948	-0.975	23.139	1.440	1.440	0.000	0.000	0.000	0.000
60	A	77	LYS	1	0.889	0.941	21.771	-1.908	-1.908	0.000	0.000	0.000	0.000
61	A	78	VAL	0	0.041	0.020	21.959	-0.115	-0.115	0.000	0.000	0.000	0.000
62	A	79	ARG	1	0.939	0.975	24.698	-1.318	-1.318	0.000	0.000	0.000	0.000
63	A	80	LYS	1	0.878	0.960	27.351	-1.292	-1.292	0.000	0.000	0.000	0.000
64	A	81	VAL	0	0.039	0.019	26.129	-0.085	-0.085	0.000	0.000	0.000	0.000
65	A	82	CYS	0	-0.038	-0.011	27.783	-0.075	-0.075	0.000	0.000	0.000	0.000
66	A	83	LYS	1	0.860	0.908	30.538	-0.884	-0.884	0.000	0.000	0.000	0.000
67	A	84	GLN	0	-0.037	-0.013	30.217	-0.054	-0.054	0.000	0.000	0.000	0.000
68	A	85	LEU	0	0.007	0.013	31.638	-0.052	-0.052	0.000	0.000	0.000	0.000
69	A	86	ASP	-1	-0.769	-0.893	34.837	0.720	0.720	0.000	0.000	0.000	0.000
70	A	87	HIS	0	-0.115	-0.048	36.576	-0.050	-0.050	0.000	0.000	0.000	0.000
71	A	88	HIS	1	0.855	0.938	38.736	-0.699	-0.699	0.000	0.000	0.000	0.000
72	A	89	PHE	0	0.040	0.016	40.899	0.009	0.009	0.000	0.000	0.000	0.000
73	A	90	ILE	0	-0.004	-0.012	36.053	0.009	0.009	0.000	0.000	0.000	0.000
74	A	91	LEU	0	0.006	0.005	39.993	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	92	PRO	0	-0.032	-0.022	39.240	0.021	0.021	0.000	0.000	0.000	0.000
76	A	93	MET	0	-0.002	0.009	39.081	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	94	TYR	0	-0.001	0.007	36.301	-0.014	-0.014	0.000	0.000	0.000	0.000
78	A	95	SER	0	0.032	0.017	41.055	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	96	ASP	-1	-0.931	-0.979	43.013	0.449	0.449	0.000	0.000	0.000	0.000
80	A	97	VAL	0	-0.006	0.010	45.229	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	98	LEU	0	-0.048	-0.020	44.562	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	99	ASN	0	-0.007	0.006	47.833	0.016	0.016	0.000	0.000	0.000	0.000
83	A	100	ILE	0	0.017	0.006	44.864	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	101	GLN	0	0.029	0.011	49.280	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	102	GLU	-1	-0.871	-0.930	48.595	0.445	0.445	0.000	0.000	0.000	0.000
86	A	103	VAL	0	-0.029	-0.022	52.146	-0.018	-0.018	0.000	0.000	0.000	0.000
87	A	104	ASN	0	0.004	0.004	54.879	0.002	0.002	0.000	0.000	0.000	0.000
88	A	105	ASP	-1	-0.876	-0.933	52.174	0.398	0.398	0.000	0.000	0.000	0.000
89	A	106	ASN	0	-0.032	-0.026	51.029	0.023	0.023	0.000	0.000	0.000	0.000
90	A	107	PHE	0	-0.001	-0.005	45.087	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	108	LYS	1	0.854	0.923	49.928	-0.319	-0.319	0.000	0.000	0.000	0.000
92	A	109	ILE	0	-0.011	-0.010	46.690	0.008	0.008	0.000	0.000	0.000	0.000
93	A	110	THR	0	-0.001	-0.003	50.700	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	111	CYS	0	-0.040	-0.012	50.543	0.018	0.018	0.000	0.000	0.000	0.000
95	A	112	GLU	-1	-0.785	-0.903	50.247	0.339	0.339	0.000	0.000	0.000	0.000
96	A	113	ASP	-1	-0.804	-0.859	52.935	0.326	0.326	0.000	0.000	0.000	0.000
97	A	114	ASN	0	-0.050	-0.030	55.238	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	115	SER	0	-0.060	-0.040	53.089	0.002	0.002	0.000	0.000	0.000	0.000
99	A	116	GLU	-1	-0.842	-0.918	53.737	0.316	0.316	0.000	0.000	0.000	0.000
100	A	117	TYR	0	-0.008	-0.007	50.634	0.001	0.001	0.000	0.000	0.000	0.000
101	A	118	SER	0	-0.006	-0.010	52.231	0.003	0.003	0.000	0.000	0.000	0.000
102	A	119	PHE	0	0.011	0.010	47.394	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	120	PRO	0	0.048	0.032	49.009	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	121	LYS	1	0.827	0.896	46.993	-0.402	-0.402	0.000	0.000	0.000	0.000
105	A	122	ARG	1	0.913	0.958	44.811	-0.468	-0.468	0.000	0.000	0.000	0.000
106	A	123	ASP	-1	-0.838	-0.918	43.989	0.512	0.512	0.000	0.000	0.000	0.000
107	A	124	CYS	0	-0.077	-0.021	43.402	0.013	0.013	0.000	0.000	0.000	0.000
108	A	125	VAL	0	-0.003	0.004	36.781	0.011	0.011	0.000	0.000	0.000	0.000
109	A	126	GLN	0	-0.015	-0.008	39.859	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	127	ILE	0	0.046	0.021	34.091	0.036	0.036	0.000	0.000	0.000	0.000
111	A	128	PRO	0	0.014	0.017	33.499	-0.040	-0.040	0.000	0.000	0.000	0.000
112	A	129	ILE	0	-0.053	-0.024	33.418	0.028	0.028	0.000	0.000	0.000	0.000
113	A	130	LYS	1	0.840	0.907	36.202	-0.567	-0.567	0.000	0.000	0.000	0.000
114	A	131	HIS	1	0.838	0.887	37.619	-0.604	-0.604	0.000	0.000	0.000	0.000
115	A	132	SER	0	0.054	0.048	36.914	0.037	0.037	0.000	0.000	0.000	0.000
116	A	133	SER	0	0.030	0.011	34.898	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	134	THR	0	0.034	0.002	30.573	0.026	0.026	0.000	0.000	0.000	0.000
118	A	135	GLU	-1	-0.878	-0.944	29.915	0.836	0.836	0.000	0.000	0.000	0.000
119	A	136	GLU	-1	-0.786	-0.872	29.895	0.740	0.740	0.000	0.000	0.000	0.000
120	A	137	ILE	0	0.016	0.005	31.314	0.041	0.041	0.000	0.000	0.000	0.000
121	A	138	GLY	0	0.021	0.013	27.895	0.062	0.062	0.000	0.000	0.000	0.000
122	A	139	LEU	0	-0.003	-0.014	26.066	0.110	0.110	0.000	0.000	0.000	0.000
123	A	140	TYR	0	-0.013	-0.003	27.064	0.060	0.060	0.000	0.000	0.000	0.000
124	A	141	ILE	0	0.016	-0.001	25.370	0.060	0.060	0.000	0.000	0.000	0.000
125	A	142	LEU	0	-0.021	-0.005	20.271	0.102	0.102	0.000	0.000	0.000	0.000
126	A	143	ASN	0	-0.011	-0.005	22.948	0.212	0.212	0.000	0.000	0.000	0.000
127	A	144	GLN	0	0.056	0.029	24.715	0.018	0.018	0.000	0.000	0.000	0.000
128	A	145	LEU	0	-0.002	-0.006	21.712	0.053	0.053	0.000	0.000	0.000	0.000
129	A	146	ILE	0	-0.052	-0.023	18.970	0.159	0.159	0.000	0.000	0.000	0.000
130	A	147	GLU	-1	-0.956	-0.964	21.045	1.389	1.389	0.000	0.000	0.000	0.000
131	A	148	GLU	-1	-0.904	-0.964	23.860	1.382	1.382	0.000	0.000	0.000	0.000
132	A	149	ILE	0	-0.069	-0.050	17.791	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	150	ASP	-1	-0.769	-0.886	19.827	2.245	2.245	0.000	0.000	0.000	0.000
134	A	151	LEU	0	0.014	0.020	17.017	0.296	0.296	0.000	0.000	0.000	0.000
135	A	152	PRO	0	-0.012	-0.023	16.687	0.353	0.353	0.000	0.000	0.000	0.000
136	A	153	PHE	0	-0.002	0.015	15.821	0.467	0.467	0.000	0.000	0.000	0.000
137	A	154	LEU	0	0.036	0.010	14.133	0.586	0.586	0.000	0.000	0.000	0.000
138	A	155	LYS	1	0.885	0.949	12.165	-2.031	-2.031	0.000	0.000	0.000	0.000
139	A	156	THR	0	-0.097	-0.057	11.220	0.612	0.612	0.000	0.000	0.000	0.000
140	A	157	ARG	1	0.686	0.795	9.762	-5.820	-5.820	0.000	0.000	0.000	0.000
141	A	158	SER	0	0.003	0.002	5.941	1.621	1.621	0.000	0.000	0.000	0.000
142	A	159	VAL	0	-0.033	-0.009	7.783	1.134	1.134	0.000	0.000	0.000	0.000
143	A	160	ASN	0	0.018	0.000	9.175	-0.238	-0.238	0.000	0.000	0.000	0.000
144	A	161	TYR	0	-0.105	-0.070	11.047	-0.954	-0.954	0.000	0.000	0.000	0.000
145	A	162	MET	0	0.015	0.016	13.270	0.541	0.541	0.000	0.000	0.000	0.000
146	A	163	GLU	-1	-0.790	-0.880	16.194	1.913	1.913	0.000	0.000	0.000	0.000
147	A	164	VAL	0	-0.007	0.002	18.679	0.100	0.100	0.000	0.000	0.000	0.000
148	A	165	THR	0	-0.011	-0.012	21.952	-0.080	-0.080	0.000	0.000	0.000	0.000
149	A	166	VAL	0	0.005	0.000	24.270	0.021	0.021	0.000	0.000	0.000	0.000
150	A	167	SER	0	-0.016	-0.020	27.831	-0.037	-0.037	0.000	0.000	0.000	0.000
151	A	168	GLU	-1	-0.794	-0.892	30.726	0.656	0.656	0.000	0.000	0.000	0.000
152	A	169	SER	0	0.002	0.003	33.930	-0.035	-0.035	0.000	0.000	0.000	0.000
153	A	170	PRO	0	0.029	0.003	32.966	0.040	0.040	0.000	0.000	0.000	0.000
154	A	171	SER	0	-0.020	-0.011	32.725	0.035	0.035	0.000	0.000	0.000	0.000
155	A	172	GLN	0	-0.016	0.005	33.219	-0.010	-0.010	0.000	0.000	0.000	0.000
156	A	173	LYS	1	0.941	0.955	27.677	-0.892	-0.892	0.000	0.000	0.000	0.000
157	A	174	ALA	0	0.022	0.034	28.548	-0.045	-0.045	0.000	0.000	0.000	0.000
158	A	175	THR	0	-0.013	-0.006	21.964	0.077	0.077	0.000	0.000	0.000	0.000
159	A	176	VAL	0	-0.018	0.005	23.462	-0.084	-0.084	0.000	0.000	0.000	0.000
160	A	177	HIS	0	0.012	0.003	18.167	0.240	0.240	0.000	0.000	0.000	0.000
161	A	178	ARG	1	0.921	0.957	18.541	-2.006	-2.006	0.000	0.000	0.000	0.000
162	A	179	ASN	0	-0.005	-0.002	15.199	0.510	0.510	0.000	0.000	0.000	0.000
163	A	180	ILE	-1	-0.878	-0.934	13.341	3.029	3.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:ASP)