FMO DATABASE

FMODB ID: 975M2

Calculation Name: 1BUN-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BUN

Chain ID: A

ChEMBL ID:

UniProt ID: P00617

Base Structure: X-ray

Registration Date: 2025-10-05

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-989376.144601
FMO2-HF: Nuclear repulsion	938607.00023
FMO2-HF: Total energy	-50769.14437
FMO2-MP2: Total energy	-50905.339674

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:ASN)

Summations of interaction energy for fragment #1(A:1: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.
-82.561	-67.809	34.135	-21.994	-26.89	-0.193

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.750 / q_NPA : 0.869

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	ILE	0	0.054	0.026	2.283	-4.255	-0.361	2.640	-2.290	-4.244	0.020
4	A	4	ASN	0	0.005	0.002	1.863	-19.901	-21.333	12.049	-4.673	-5.943	-0.049
5	A	5	PHE	0	0.029	0.025	3.881	7.859	8.350	0.000	-0.173	-0.318	0.000
6	A	6	MET	0	0.002	0.002	5.363	6.563	6.740	-0.001	-0.009	-0.167	0.000
51	A	52	TYR	0	-0.031	-0.067	3.169	-6.666	-5.667	0.023	-0.504	-0.517	-0.005
62	A	63	PRO	0	0.017	0.008	4.187	-8.579	-8.235	-0.001	-0.097	-0.245	0.000
63	A	64	LYS	1	1.034	1.010	2.024	-6.936	-5.485	4.580	-3.037	-2.995	-0.040
64	A	65	THR	0	0.001	0.001	2.209	-5.126	-3.452	5.546	-3.787	-3.433	-0.027
65	A	66	GLN	0	-0.062	-0.018	2.701	-1.768	0.507	0.844	-1.157	-1.961	-0.016
66	A	67	SER	0	0.046	0.022	2.040	-34.737	-32.954	6.356	-3.973	-4.166	-0.054
67	A	68	TYR	0	-0.006	-0.049	2.238	11.931	12.900	1.593	-1.048	-1.514	-0.008
88	A	90	VAL	0	0.030	0.011	2.889	-0.865	-0.446	0.180	-0.179	-0.420	-0.001
90	A	94	ASP	-1	-0.742	-0.822	2.672	-85.437	-83.729	0.326	-1.067	-0.967	-0.013
7	A	7	GLU	-1	-0.930	-0.964	7.343	-24.548	-24.548	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.085	-0.039	6.577	3.521	3.521	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.026	0.026	9.377	3.020	3.020	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.953	0.984	11.527	21.119	21.119	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.060	-0.031	12.833	2.160	2.160	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.074	-0.057	13.481	0.922	0.922	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.004	0.030	15.048	0.910	0.910	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.016	0.009	17.466	0.294	0.294	0.000	0.000	0.000	0.000
15	A	15	CYS	0	-0.048	-0.057	20.996	-0.232	-0.232	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.906	-0.929	22.083	-11.778	-11.778	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.757	0.882	19.584	13.776	13.776	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.032	-0.020	18.440	-0.690	-0.690	0.000	0.000	0.000	0.000
19	A	19	TRP	0	0.038	-0.004	10.160	-0.656	-0.656	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.021	0.006	15.368	-0.448	-0.448	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.762	-0.863	16.995	-14.021	-14.021	0.000	0.000	0.000	0.000
22	A	22	TYR	0	0.013	0.002	14.593	0.633	0.633	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.084	-0.030	14.125	-1.077	-1.077	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.848	-0.926	15.117	-15.272	-15.272	0.000	0.000	0.000	0.000
25	A	25	TYR	0	-0.073	-0.053	18.011	0.967	0.967	0.000	0.000	0.000	0.000
26	A	26	GLY	0	-0.020	-0.017	18.724	-0.627	-0.627	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.098	-0.031	20.499	0.179	0.179	0.000	0.000	0.000	0.000
28	A	28	TYR	0	-0.030	-0.041	15.496	-0.221	-0.221	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.109	-0.001	12.917	-3.683	-3.683	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.115	0.049	13.682	0.909	0.909	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.108	-0.048	12.550	-1.856	-1.856	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.015	-0.002	13.067	1.222	1.222	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.072	0.019	14.799	-0.231	-0.231	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.080	-0.048	17.842	0.109	0.109	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.068	0.051	21.316	0.026	0.026	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.746	0.830	22.608	11.182	11.182	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.015	-0.001	19.584	0.113	0.113	0.000	0.000	0.000	0.000
38	A	38	ILE	0	0.004	-0.001	21.597	0.561	0.561	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.774	-0.858	22.056	-13.473	-13.473	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.017	-0.003	21.821	-0.554	-0.554	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.035	0.027	16.604	-0.875	-0.875	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.670	-0.843	17.296	-17.123	-17.123	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.900	0.957	17.457	14.598	14.598	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.061	-0.007	14.175	1.276	1.276	0.000	0.000	0.000	0.000
45	A	46	TYR	0	0.070	0.038	13.006	-1.321	-1.321	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.034	-0.019	13.634	-0.158	-0.158	0.000	0.000	0.000	0.000
47	A	48	HIS	1	0.823	0.916	5.864	38.836	38.836	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.858	-0.933	9.556	-28.660	-28.660	0.000	0.000	0.000	0.000
49	A	50	ASN	0	-0.043	-0.018	11.283	0.180	0.180	0.000	0.000	0.000	0.000
50	A	51	CYS	0	-0.059	0.003	6.573	2.218	2.218	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.035	0.021	8.496	-0.173	-0.173	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.907	-0.958	11.910	-18.917	-18.917	0.000	0.000	0.000	0.000
54	A	55	ALA	0	-0.043	-0.040	8.310	0.456	0.456	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.996	-0.994	9.753	-24.578	-24.578	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.930	0.970	10.829	20.426	20.426	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.952	0.982	14.592	18.870	18.870	0.000	0.000	0.000	0.000
58	A	59	HIS	0	-0.037	-0.039	12.094	1.025	1.025	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.960	0.999	12.849	17.756	17.756	0.000	0.000	0.000	0.000
60	A	61	CYS	0	0.030	0.024	7.688	-0.893	-0.893	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.067	0.024	6.854	-0.458	-0.458	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.001	0.012	6.333	0.126	0.126	0.000	0.000	0.000	0.000
69	A	70	TYR	0	0.020	0.002	5.426	-0.706	-0.706	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.923	0.967	9.587	19.514	19.514	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.050	0.041	10.495	0.026	0.026	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.036	-0.031	13.969	1.645	1.645	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.976	0.989	17.787	14.537	14.537	0.000	0.000	0.000	0.000
74	A	75	ARG	1	1.015	1.008	18.237	14.465	14.465	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.027	0.002	16.656	-0.328	-0.328	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.076	0.024	10.029	-0.506	-0.506	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.050	-0.008	13.009	0.852	0.852	0.000	0.000	0.000	0.000
78	A	79	CYS	0	-0.009	0.022	5.356	-3.963	-3.963	0.000	0.000	0.000	0.000
79	A	80	TYR	0	0.006	-0.012	11.458	2.213	2.213	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.024	0.030	10.719	0.892	0.892	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.055	0.024	11.705	1.091	1.091	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.030	0.007	13.508	-1.391	-1.391	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.060	0.038	13.742	1.389	1.389	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.045	-0.032	11.304	-0.953	-0.953	0.000	0.000	0.000	0.000
85	A	87	ALA	0	0.011	0.004	6.086	-4.224	-4.224	0.000	0.000	0.000	0.000
86	A	88	ARG	1	0.757	0.871	6.556	20.502	20.502	0.000	0.000	0.000	0.000
87	A	89	ILE	0	0.037	0.017	8.921	-0.866	-0.866	0.000	0.000	0.000	0.000
89	A	92	ASP	-1	-0.791	-0.898	6.278	-24.698	-24.698	0.000	0.000	0.000	0.000
91	A	95	ARG	1	0.926	0.929	6.384	27.942	27.942	0.000	0.000	0.000	0.000
92	A	96	THR	0	-0.070	-0.054	9.340	2.858	2.858	0.000	0.000	0.000	0.000
93	A	97	ALA	0	0.034	0.029	9.430	2.028	2.028	0.000	0.000	0.000	0.000
94	A	98	ALA	0	0.039	0.012	9.512	1.956	1.956	0.000	0.000	0.000	0.000
95	A	99	LEU	0	-0.038	-0.018	11.439	2.007	2.007	0.000	0.000	0.000	0.000
96	A	101	PHE	0	0.035	-0.003	12.314	0.865	0.865	0.000	0.000	0.000	0.000
97	A	102	GLY	0	-0.001	0.006	15.673	0.919	0.919	0.000	0.000	0.000	0.000
98	A	103	ASN	0	-0.108	-0.053	17.545	1.462	1.462	0.000	0.000	0.000	0.000
99	A	104	SER	0	-0.028	-0.020	18.709	0.755	0.755	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.953	-0.972	20.940	-11.452	-11.452	0.000	0.000	0.000	0.000
101	A	106	TYR	0	-0.040	-0.043	19.571	-0.050	-0.050	0.000	0.000	0.000	0.000
102	A	107	ILE	0	0.011	0.007	23.246	0.596	0.596	0.000	0.000	0.000	0.000
103	A	108	GLU	-1	-0.736	-0.868	25.277	-12.720	-12.720	0.000	0.000	0.000	0.000
104	A	109	GLY	0	-0.017	-0.006	26.364	-0.130	-0.130	0.000	0.000	0.000	0.000
105	A	110	HIS	1	0.815	0.882	23.724	12.442	12.442	0.000	0.000	0.000	0.000
106	A	111	LYS	1	0.835	0.910	22.155	12.599	12.599	0.000	0.000	0.000	0.000
107	A	112	ASN	0	-0.042	-0.016	22.037	0.655	0.655	0.000	0.000	0.000	0.000
108	A	113	ILE	0	-0.037	0.008	23.282	0.673	0.673	0.000	0.000	0.000	0.000
109	A	114	ASP	-1	-0.853	-0.947	24.779	-10.818	-10.818	0.000	0.000	0.000	0.000
110	A	115	THR	0	0.059	0.002	22.617	0.193	0.193	0.000	0.000	0.000	0.000
111	A	116	ALA	0	0.008	0.014	25.202	0.059	0.059	0.000	0.000	0.000	0.000
112	A	117	ARG	1	0.879	0.956	28.405	9.628	9.628	0.000	0.000	0.000	0.000
113	A	118	PHE	0	-0.047	-0.043	26.792	0.350	0.350	0.000	0.000	0.000	0.000
114	A	120	GLN	-1	-0.762	-0.827	24.980	-11.819	-11.819	0.000	0.000	0.000	0.000

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