FMO DATABASE

FMODB ID: QLN3Y

Calculation Name: 2D89-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2D89

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NDI1

Base Structure: SolutionNMR

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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-976125.173124
FMO2-HF: Nuclear repulsion	929879.433036
FMO2-HF: Total energy	-46245.740088
FMO2-MP2: Total energy	-46380.509527

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:GLY)

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

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.
59.5	60.36	-0.01	-0.31	-0.541	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.919

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	SER	0	0.043	0.019	3.837	3.544	4.404	-0.010	-0.310	-0.541	-0.001
4	A	4	GLY	0	0.039	0.033	7.000	1.167	1.167	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.009	-0.006	10.525	2.208	2.208	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.024	-0.003	10.089	2.125	2.125	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.042	0.027	10.553	-1.862	-1.862	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.037	-0.006	10.176	-1.706	-1.706	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.014	-0.009	10.105	2.270	2.270	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.065	0.014	8.449	-3.341	-3.341	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.005	0.026	10.468	1.536	1.536	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.047	0.017	10.165	0.619	0.619	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.083	0.043	10.270	1.748	1.748	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.030	0.025	12.181	1.202	1.202	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.011	-0.005	15.322	1.146	1.146	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.003	-0.015	13.630	1.025	1.025	0.000	0.000	0.000	0.000
17	A	17	TRP	0	0.077	0.046	15.876	1.106	1.106	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.033	-0.013	17.578	1.059	1.059	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.937	0.977	18.862	16.725	16.725	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.944	-0.953	17.512	-17.110	-17.110	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.014	-0.016	20.726	0.747	0.747	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.043	-0.047	23.459	0.606	0.606	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.844	0.937	23.104	13.623	13.623	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.000	-0.007	25.073	0.083	0.083	0.000	0.000	0.000	0.000
25	A	25	TYR	0	-0.018	0.014	28.620	0.486	0.486	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.960	0.973	30.396	9.020	9.020	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.036	0.007	32.277	0.022	0.022	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.010	0.013	25.975	-0.051	-0.051	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.958	0.973	25.757	11.387	11.387	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.044	0.022	21.395	0.067	0.067	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.034	-0.018	21.862	-0.716	-0.716	0.000	0.000	0.000	0.000
32	A	32	ASN	0	0.036	0.026	22.064	-0.334	-0.334	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.031	-0.004	17.203	0.142	0.142	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.048	0.028	22.701	0.110	0.110	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.003	-0.024	26.346	0.363	0.363	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.047	-0.031	25.437	0.203	0.203	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.000	-0.004	22.121	-0.063	-0.063	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.955	0.959	27.911	9.744	9.744	0.000	0.000	0.000	0.000
39	A	39	ASN	0	0.011	0.009	31.002	-0.035	-0.035	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.102	0.051	30.499	0.213	0.213	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.016	-0.006	30.679	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.010	-0.009	25.455	0.098	0.098	0.000	0.000	0.000	0.000
43	A	43	PHE	0	0.038	0.010	25.675	-0.358	-0.358	0.000	0.000	0.000	0.000
44	A	44	CYS	0	0.021	0.017	28.356	0.022	0.022	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.042	-0.008	28.087	0.038	0.038	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.024	0.002	23.304	-0.094	-0.094	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.005	0.015	26.663	-0.057	-0.057	0.000	0.000	0.000	0.000
48	A	48	HIS	0	0.018	0.012	29.427	0.441	0.441	0.000	0.000	0.000	0.000
49	A	49	HIS	0	-0.029	-0.008	25.294	-0.219	-0.219	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.005	0.000	23.186	0.008	0.008	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.953	0.970	29.307	10.741	10.741	0.000	0.000	0.000	0.000
52	A	52	PRO	0	-0.020	0.000	32.775	0.100	0.100	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.862	-0.945	34.559	-8.190	-8.190	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.040	-0.018	33.233	0.139	0.139	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.018	-0.019	32.918	0.008	0.008	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.817	-0.905	36.936	-7.940	-7.940	0.000	0.000	0.000	0.000
57	A	57	TYR	0	-0.028	-0.030	31.963	-0.031	-0.031	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.860	0.924	36.098	8.592	8.592	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.028	-0.011	38.261	0.168	0.168	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.017	0.027	35.571	0.119	0.119	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.022	-0.008	37.341	-0.097	-0.097	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.050	-0.029	34.708	-0.042	-0.042	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.043	-0.035	36.271	0.013	0.013	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.825	-0.869	38.464	-7.787	-7.787	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.053	-0.030	35.147	-0.301	-0.301	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.986	0.989	35.867	7.427	7.427	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.797	-0.894	37.525	-8.062	-8.062	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.012	-0.030	34.232	-0.065	-0.065	0.000	0.000	0.000	0.000
69	A	69	ASN	0	-0.043	-0.003	32.090	-0.523	-0.523	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.836	0.914	33.713	8.124	8.124	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.891	0.940	35.867	7.967	7.967	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.015	0.013	30.581	-0.067	-0.067	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.001	-0.018	29.533	-0.250	-0.250	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.840	-0.900	32.969	-8.437	-8.437	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.024	0.002	33.929	0.019	0.019	0.000	0.000	0.000	0.000
76	A	76	PHE	0	-0.024	-0.038	27.240	-0.208	-0.208	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.008	0.001	30.787	-0.139	-0.139	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.052	-0.009	32.836	0.092	0.092	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.039	-0.018	28.433	0.100	0.100	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.027	0.025	31.341	-0.148	-0.148	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.067	-0.032	26.079	-0.329	-0.329	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.002	-0.009	28.696	0.311	0.311	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.921	0.967	28.550	8.677	8.677	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.002	-0.010	25.477	0.023	0.023	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.016	-0.002	27.787	-0.074	-0.074	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.845	-0.917	30.627	-9.029	-9.029	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.050	-0.030	34.194	-0.055	-0.055	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.008	-0.018	35.815	0.111	0.111	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.812	-0.906	34.224	-8.914	-8.914	0.000	0.000	0.000	0.000
90	A	90	MET	0	-0.085	-0.028	29.337	-0.072	-0.072	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.051	-0.034	34.661	0.031	0.031	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.040	-0.004	38.124	0.198	0.198	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.009	0.016	33.214	0.063	0.063	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.029	0.021	35.529	-0.035	-0.035	0.000	0.000	0.000	0.000
95	A	95	ILE	0	-0.049	-0.041	29.240	-0.190	-0.190	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.055	0.040	28.253	0.051	0.051	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.836	-0.921	26.691	-11.273	-11.273	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.937	0.956	17.981	16.106	16.106	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.010	0.004	20.837	-0.567	-0.567	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.080	0.058	22.506	-0.599	-0.599	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.001	0.009	23.427	-0.137	-0.137	0.000	0.000	0.000	0.000
102	A	102	MET	0	-0.073	-0.041	16.162	-0.226	-0.226	0.000	0.000	0.000	0.000
103	A	103	THR	0	0.000	-0.008	20.156	-0.663	-0.663	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.025	0.015	21.560	-0.072	-0.072	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.019	-0.015	20.766	-0.112	-0.112	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.043	-0.053	13.974	-0.392	-0.392	0.000	0.000	0.000	0.000
107	A	107	GLN	0	0.033	0.030	19.191	-0.794	-0.794	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.003	0.007	22.261	0.057	0.057	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.878	0.928	12.808	21.597	21.597	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.006	-0.006	18.763	-0.327	-0.327	0.000	0.000	0.000	0.000
111	A	111	HIS	0	-0.007	0.007	19.642	0.413	0.413	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.066	-0.035	22.089	0.378	0.378	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.054	-0.022	16.680	-0.297	-0.297	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.017	0.014	17.815	-0.951	-0.951	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.026	-0.012	15.539	-1.145	-1.145	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.076	-0.023	15.642	-0.324	-0.324	0.000	0.000	0.000	0.000
117	A	117	SER	0	0.032	0.011	17.140	0.872	0.872	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.078	-0.040	20.081	-0.642	-0.642	0.000	0.000	0.000	0.000
119	A	119	GLY	-1	-0.900	-0.933	22.160	-12.443	-12.443	0.000	0.000	0.000	0.000

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