FMODB ID: KKY13

Calculation Name: 2B87-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2B87

Chain ID: A

ChEMBL ID:

UniProt ID: Q70AB8

Base Structure: SolutionNMR

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

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 method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	58
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

FMO2-HF: Electronic energy	-304500.066143
FMO2-HF: Nuclear repulsion	282250.859536
FMO2-HF: Total energy	-22249.206607
FMO2-MP2: Total energy	-22316.054303

Snapshot

Snapshot

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	ASN	0	-0.036	-0.025	2.842	7.093	9.700	0.726	-1.063	-2.270	-0.008
4	A	4	LYS	1	0.748	0.864	2.524	44.448	46.100	1.334	-0.754	-2.233	-0.011
5	A	5	PHE	0	0.122	0.053	3.524	5.797	6.070	0.030	0.018	-0.322	0.000
7	A	7	LYS	1	0.938	0.961	4.425	37.007	37.165	-0.001	-0.010	-0.147	0.000
6	A	6	ASN	0	0.036	0.029	5.753	5.587	5.587	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.796	-0.884	6.716	-35.546	-35.546	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.030	0.033	8.996	2.524	2.524	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.015	0.014	10.056	2.118	2.118	0.000	0.000	0.000	0.000
11	A	11	TRP	0	-0.047	-0.024	10.514	1.463	1.463	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.052	0.032	12.350	1.428	1.428	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.016	-0.028	14.229	1.729	1.729	0.000	0.000	0.000	0.000
14	A	14	TRP	0	-0.011	-0.001	15.222	1.140	1.140	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.824	-0.940	14.309	-18.734	-18.734	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.038	-0.017	17.893	0.946	0.946	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.040	-0.028	19.719	0.831	0.831	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.070	-0.034	20.098	0.678	0.678	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.062	-0.008	21.860	0.243	0.243	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.035	-0.024	24.160	0.305	0.305	0.000	0.000	0.000	0.000
21	A	21	ASN	0	-0.013	-0.012	27.758	0.686	0.686	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.016	0.021	24.094	0.187	0.187	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.036	0.017	28.313	-0.075	-0.075	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.050	0.013	27.784	-0.322	-0.322	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.025	-0.013	27.342	-0.292	-0.292	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.032	0.010	26.774	-0.374	-0.374	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.030	0.024	22.480	-0.467	-0.467	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.852	0.913	22.610	11.004	11.004	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.043	0.026	23.283	-0.385	-0.385	0.000	0.000	0.000	0.000
30	A	30	PHE	0	0.047	0.022	20.530	-0.322	-0.322	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.017	0.006	18.773	-0.796	-0.796	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.900	-0.958	19.178	-12.843	-12.843	0.000	0.000	0.000	0.000
33	A	33	SER	0	0.001	-0.016	20.556	-0.152	-0.152	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.052	-0.004	14.440	-0.767	-0.767	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.855	0.924	15.430	14.541	14.541	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.967	-0.957	17.268	-14.347	-14.347	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.773	-0.898	15.642	-19.513	-19.513	0.000	0.000	0.000	0.000
38	A	38	PRO	0	-0.016	-0.017	11.460	-0.734	-0.734	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.051	-0.020	11.893	-2.533	-2.533	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.051	-0.009	12.900	-0.274	-0.274	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.019	-0.005	11.592	0.689	0.689	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.021	0.000	12.802	1.074	1.074	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.008	-0.008	14.771	1.667	1.667	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.011	0.015	17.155	1.036	1.036	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.011	-0.006	15.126	0.823	0.823	0.000	0.000	0.000	0.000
46	A	46	ALA	0	-0.014	-0.004	18.504	0.652	0.652	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.874	-0.928	20.572	-11.866	-11.866	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.024	0.023	21.130	0.612	0.612	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.878	0.922	17.535	17.440	17.440	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.854	0.926	23.488	12.712	12.712	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.009	-0.002	26.204	0.495	0.495	0.000	0.000	0.000	0.000
52	A	52	ASN	0	0.029	0.011	25.799	0.466	0.466	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.869	-0.951	27.559	-10.176	-10.176	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.012	0.002	29.337	0.385	0.385	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.054	-0.030	30.101	0.091	0.091	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.008	0.020	30.458	0.170	0.170	0.000	0.000	0.000	0.000
57	A	57	PRO	0	-0.068	-0.040	32.585	0.171	0.171	0.000	0.000	0.000	0.000
58	A	58	LYS	0	-0.122	-0.049	31.766	1.033	1.033	0.000	0.000	0.000	0.000