FMO DATABASE

FMODB ID: J4JY9

Calculation Name: 2COF-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2COF

Chain ID: A

ChEMBL ID:

UniProt ID: Q8N4X5

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

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	107
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-783835.336308
FMO2-HF: Nuclear repulsion	742377.282244
FMO2-HF: Total energy	-41458.054065
FMO2-MP2: Total energy	-41578.791251

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.
-41.999	-42.075	5.882	-2.801	-3.006	-0.026

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 : 0.866 / q_NPA : 0.927

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	0.015	0.021	3.842	2.690	3.458	-0.007	-0.240	-0.522	0.000
84	A	84	LYS	1	0.899	0.938	4.695	41.494	41.502	-0.001	-0.006	0.000	0.000
85	A	85	SER	0	-0.092	-0.058	3.621	-9.396	-8.958	0.002	-0.197	-0.244	-0.001
87	A	87	GLU	-1	-0.884	-0.944	2.167	-64.598	-66.002	5.889	-2.337	-2.148	-0.025
88	A	88	GLU	-1	-0.889	-0.925	4.034	-35.260	-35.146	-0.001	-0.021	-0.092	0.000
4	A	4	GLY	0	0.017	-0.001	5.522	6.303	6.303	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.041	-0.010	7.885	3.296	3.296	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.010	-0.009	9.182	-1.003	-1.003	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.020	0.026	11.944	0.983	0.983	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.037	-0.026	8.131	-1.408	-1.408	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.830	-0.916	12.260	-19.950	-19.950	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.021	-0.004	13.200	1.249	1.249	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.079	-0.038	13.903	1.342	1.342	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.051	0.024	10.234	0.068	0.068	0.000	0.000	0.000	0.000
13	A	13	TYR	0	-0.038	-0.024	12.359	1.285	1.285	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.009	0.012	11.298	-1.976	-1.976	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.076	-0.030	13.862	1.857	1.857	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.012	-0.010	16.036	-0.263	-0.263	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.005	0.005	19.304	0.442	0.442	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.009	-0.019	21.588	0.478	0.478	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.016	-0.015	25.103	-0.131	-0.131	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.019	0.010	25.393	0.145	0.145	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.009	0.000	23.746	-0.273	-0.273	0.000	0.000	0.000	0.000
22	A	22	TRP	0	0.058	0.032	17.497	0.013	0.013	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.906	0.955	20.206	12.834	12.834	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.040	0.037	17.034	-0.299	-0.299	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.883	0.945	17.353	14.913	14.913	0.000	0.000	0.000	0.000
26	A	26	TRP	0	0.000	-0.007	16.862	-0.491	-0.491	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.009	0.013	16.126	1.350	1.350	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.017	-0.014	16.778	-0.558	-0.558	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.047	0.026	16.986	0.867	0.867	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.859	0.907	19.272	12.516	12.516	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.851	-0.916	22.181	-11.126	-11.126	0.000	0.000	0.000	0.000
32	A	32	ASN	0	0.035	0.039	23.195	0.296	0.296	0.000	0.000	0.000	0.000
33	A	33	HIS	0	-0.044	-0.025	23.626	0.565	0.565	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.000	0.008	18.566	-0.627	-0.627	0.000	0.000	0.000	0.000
35	A	35	HIS	0	-0.006	-0.006	21.801	0.777	0.777	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.053	0.023	20.846	-0.877	-0.877	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.011	0.001	21.694	0.840	0.840	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.025	0.006	21.818	-1.034	-1.034	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.872	-0.934	22.093	-12.029	-12.029	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.981	0.981	20.116	13.353	13.353	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.001	-0.011	21.734	0.092	0.092	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.960	0.994	21.826	13.904	13.904	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.031	0.012	24.158	0.499	0.499	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.896	0.927	26.728	11.194	11.194	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.011	0.010	26.281	-0.505	-0.505	0.000	0.000	0.000	0.000
46	A	46	ALA	0	-0.079	-0.052	24.724	0.310	0.310	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.009	-0.001	25.258	0.553	0.553	0.000	0.000	0.000	0.000
48	A	48	GLN	0	0.005	0.005	27.786	-0.173	-0.173	0.000	0.000	0.000	0.000
49	A	49	PRO	0	-0.026	-0.009	25.898	-0.278	-0.278	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.031	0.010	22.612	0.358	0.358	0.000	0.000	0.000	0.000
51	A	51	SER	0	0.022	0.004	25.099	-0.272	-0.272	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.004	-0.009	20.195	0.034	0.034	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.032	0.021	24.181	-0.029	-0.029	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.007	0.007	26.330	0.432	0.432	0.000	0.000	0.000	0.000
55	A	55	CYS	0	-0.127	-0.050	23.872	0.365	0.365	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.900	-0.947	22.682	-12.830	-12.830	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.028	-0.017	16.677	-0.153	-0.153	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.050	0.025	18.575	-0.432	-0.432	0.000	0.000	0.000	0.000
59	A	59	PRO	0	-0.017	-0.015	14.215	-0.557	-0.557	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.832	-0.907	15.853	-14.068	-14.068	0.000	0.000	0.000	0.000
61	A	61	PRO	0	0.015	0.009	14.372	-0.230	-0.230	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.008	-0.020	15.989	1.510	1.510	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.005	-0.015	16.664	-0.962	-0.962	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.899	-0.931	16.963	-17.666	-17.666	0.000	0.000	0.000	0.000
65	A	65	HIS	1	0.866	0.930	11.643	20.836	20.836	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.014	0.012	11.349	0.745	0.745	0.000	0.000	0.000	0.000
67	A	67	TYR	0	0.019	-0.014	8.302	-2.441	-2.441	0.000	0.000	0.000	0.000
68	A	68	SER	0	-0.020	-0.009	10.648	0.023	0.023	0.000	0.000	0.000	0.000
69	A	69	PHE	0	0.031	0.001	11.384	-0.317	-0.317	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.857	0.930	15.730	13.858	13.858	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.002	0.005	19.264	-0.262	-0.262	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.039	0.017	21.557	0.388	0.388	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.057	0.010	24.875	-0.069	-0.069	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.867	0.926	28.079	10.644	10.644	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.060	0.046	28.990	0.259	0.259	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.941	-0.958	29.039	-9.947	-9.947	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.968	-0.990	24.665	-12.853	-12.853	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.043	-0.012	24.547	0.363	0.363	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.008	-0.006	21.860	0.095	0.095	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.853	0.930	18.471	15.895	15.895	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.016	-0.004	15.263	0.318	0.318	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.849	-0.934	12.711	-20.724	-20.724	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.018	0.031	8.173	0.142	0.142	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.072	0.018	4.848	0.462	0.462	0.000	0.000	0.000	0.000
89	A	89	MET	0	0.036	0.023	5.764	5.093	5.093	0.000	0.000	0.000	0.000
90	A	90	GLY	0	0.003	0.013	7.289	3.326	3.326	0.000	0.000	0.000	0.000
91	A	91	HIS	0	-0.018	-0.013	7.520	3.692	3.692	0.000	0.000	0.000	0.000
92	A	92	TRP	0	0.020	-0.015	9.188	3.914	3.914	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.004	0.003	11.545	2.107	2.107	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.020	0.014	12.689	1.583	1.583	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.022	-0.002	13.242	1.343	1.343	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.009	-0.011	15.017	1.428	1.428	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.004	0.001	16.575	0.988	0.988	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.084	-0.029	18.056	0.755	0.755	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.852	-0.931	19.316	-13.893	-13.893	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.078	-0.048	21.354	0.502	0.502	0.000	0.000	0.000	0.000
101	A	101	GLY	0	-0.024	-0.019	23.235	0.318	0.318	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.022	0.026	23.960	-0.100	-0.100	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.012	-0.005	26.832	0.286	0.286	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.025	-0.007	30.443	-0.078	-0.078	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.047	-0.045	31.693	0.330	0.330	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.045	-0.026	28.295	-0.294	-0.294	0.000	0.000	0.000	0.000
107	A	107	GLY	-1	-0.920	-0.932	28.657	-10.467	-10.467	0.000	0.000	0.000	0.000

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