FMO DATABASE

FMODB ID: QLNZY

Calculation Name: 2COD-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2COD

Chain ID: A

ChEMBL ID:

UniProt ID: Q8WZ64

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

Total energy (hartree)

FMO2-HF: Electronic energy	-881313.74315
FMO2-HF: Nuclear repulsion	836572.24367
FMO2-HF: Total energy	-44741.49948
FMO2-MP2: Total energy	-44873.031018

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.
54.17	55.825	0.001	-0.707	-0.949	-0.003

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 : 0.884 / q_NPA : 0.925

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	0.029	0.028	3.485	0.574	2.089	0.003	-0.694	-0.825	-0.003
4	A	4	GLY	0	0.001	-0.008	5.395	3.706	3.805	-0.001	-0.005	-0.092	0.000
112	A	112	PRO	0	-0.085	-0.040	4.265	-3.285	-3.244	-0.001	-0.008	-0.032	0.000
5	A	5	SER	0	0.007	0.022	9.085	0.035	0.035	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.027	0.004	12.137	0.726	0.726	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.027	0.020	15.598	-0.235	-0.235	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.924	0.951	12.583	22.232	22.232	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.006	0.016	16.785	0.332	0.332	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.836	0.913	20.483	13.709	13.709	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.005	-0.020	23.005	0.148	0.148	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.032	0.029	26.747	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.000	-0.003	29.523	0.016	0.016	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.007	0.019	26.435	-0.104	-0.104	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.862	-0.923	31.014	-8.680	-8.680	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.863	0.941	31.189	9.302	9.302	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.011	0.000	33.022	0.325	0.325	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.014	0.005	35.018	-0.088	-0.088	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.008	0.005	37.804	0.053	0.053	0.000	0.000	0.000	0.000
20	A	20	GLN	0	0.037	0.002	37.814	-0.312	-0.312	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.037	0.004	39.420	0.111	0.111	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.890	0.941	35.722	8.569	8.569	0.000	0.000	0.000	0.000
23	A	23	ARG	1	1.001	1.019	39.323	6.748	6.748	0.000	0.000	0.000	0.000
24	A	24	MET	0	0.033	0.020	41.052	0.136	0.136	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.015	-0.020	33.084	-0.183	-0.183	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.022	0.011	36.912	0.177	0.177	0.000	0.000	0.000	0.000
27	A	27	LYS	1	1.016	1.032	35.270	8.411	8.411	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.932	0.963	33.723	8.820	8.820	0.000	0.000	0.000	0.000
29	A	29	TRP	0	0.051	0.047	30.661	-0.206	-0.206	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.017	-0.019	26.673	0.028	0.028	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.991	0.986	26.121	11.397	11.397	0.000	0.000	0.000	0.000
32	A	32	PHE	0	-0.028	-0.004	17.981	0.181	0.181	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.842	-0.935	22.885	-13.286	-13.286	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.029	0.017	18.709	-0.438	-0.438	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.004	0.007	18.805	-0.670	-0.670	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.056	-0.056	21.508	0.438	0.438	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.006	0.010	22.752	-0.063	-0.063	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.009	0.003	25.408	0.505	0.505	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.063	-0.047	28.869	-0.019	-0.019	0.000	0.000	0.000	0.000
40	A	40	TYR	0	0.029	0.017	31.304	0.105	0.105	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.001	-0.010	35.019	-0.215	-0.215	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.062	-0.044	37.967	0.037	0.037	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.899	-0.931	38.991	-6.893	-6.893	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.926	0.958	41.368	7.156	7.156	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.819	-0.887	41.311	-7.468	-7.468	0.000	0.000	0.000	0.000
46	A	46	MET	0	-0.051	-0.048	42.532	-0.040	-0.040	0.000	0.000	0.000	0.000
47	A	47	TYR	0	0.000	-0.001	42.630	0.058	0.058	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.006	0.004	39.684	-0.104	-0.104	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.940	0.949	33.970	8.841	8.841	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.036	0.021	33.566	0.070	0.070	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.049	-0.021	28.074	-0.146	-0.146	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.023	-0.006	25.143	0.221	0.221	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.018	0.018	25.006	-0.382	-0.382	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.038	0.007	17.094	0.078	0.078	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.003	-0.010	20.652	-0.166	-0.166	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.043	-0.003	21.881	0.158	0.158	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.038	-0.011	20.042	0.399	0.399	0.000	0.000	0.000	0.000
58	A	58	SER	0	0.008	0.018	20.334	-0.731	-0.731	0.000	0.000	0.000	0.000
59	A	59	THR	0	0.011	-0.007	19.097	-0.806	-0.806	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.007	-0.004	18.547	0.748	0.748	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.904	0.966	19.274	11.396	11.396	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.053	0.021	21.095	0.412	0.412	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.002	-0.011	23.521	0.110	0.110	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.003	-0.004	27.335	0.138	0.138	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.847	-0.917	28.124	-10.562	-10.562	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.014	-0.020	27.345	-0.129	-0.129	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.910	0.966	27.852	9.541	9.541	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.014	0.006	23.249	-0.459	-0.459	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.903	-0.947	24.714	-10.513	-10.513	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.023	0.002	22.702	-0.631	-0.631	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.021	0.011	23.634	0.594	0.594	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.020	-0.033	23.936	-0.385	-0.385	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.001	-0.016	25.318	0.307	0.307	0.000	0.000	0.000	0.000
74	A	74	GLN	0	-0.054	-0.010	27.759	0.624	0.624	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.981	0.974	30.206	9.206	9.206	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.005	0.032	27.622	-0.298	-0.298	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.025	-0.016	28.052	0.494	0.494	0.000	0.000	0.000	0.000
78	A	78	VAL	0	0.020	0.016	27.726	-0.338	-0.338	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.000	-0.008	26.661	0.397	0.397	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.855	0.924	28.112	9.308	9.308	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.025	0.014	25.383	0.115	0.115	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.972	-0.992	28.809	-9.110	-9.110	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.908	0.943	27.244	11.468	11.468	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.892	-0.953	25.381	-12.007	-12.007	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.852	-0.918	22.546	-12.829	-12.829	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.829	-0.936	21.673	-12.502	-12.502	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.859	0.943	22.281	12.366	12.366	0.000	0.000	0.000	0.000
88	A	88	ASN	0	0.002	-0.006	18.644	-0.230	-0.230	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.786	-0.870	17.873	-16.631	-16.631	0.000	0.000	0.000	0.000
90	A	90	TRP	0	-0.054	-0.041	17.855	-0.885	-0.885	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.005	0.000	16.703	-0.345	-0.345	0.000	0.000	0.000	0.000
92	A	92	SER	0	0.001	0.011	13.576	-1.288	-1.288	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.020	-0.014	13.707	-1.317	-1.317	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.007	-0.002	15.294	-0.469	-0.469	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.026	0.003	12.382	-0.371	-0.371	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.049	-0.034	9.776	-3.353	-3.353	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.012	0.014	11.805	-0.792	-0.792	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.015	-0.017	14.303	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.934	0.970	6.457	35.205	35.205	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.051	-0.014	10.999	-1.104	-1.104	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.006	0.012	12.431	1.101	1.101	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.025	-0.006	13.744	0.725	0.725	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.065	0.026	10.142	-1.482	-1.482	0.000	0.000	0.000	0.000
104	A	104	THR	0	-0.035	-0.025	9.527	0.609	0.609	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.005	0.024	10.716	1.707	1.707	0.000	0.000	0.000	0.000
106	A	106	GLN	0	-0.004	-0.013	11.073	-1.472	-1.472	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.032	-0.011	8.707	-1.728	-1.728	0.000	0.000	0.000	0.000
108	A	108	GLN	0	-0.029	-0.006	10.557	0.882	0.882	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.058	0.016	10.515	0.791	0.791	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.055	-0.029	5.466	-3.809	-3.809	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.040	0.023	7.334	1.995	1.995	0.000	0.000	0.000	0.000
113	A	113	SER	0	0.042	0.017	5.672	3.419	3.419	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.099	-0.062	8.376	-2.870	-2.870	0.000	0.000	0.000	0.000
115	A	115	GLY	-1	-0.882	-0.912	10.118	-20.848	-20.848	0.000	0.000	0.000	0.000

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