FMO DATABASE

FMODB ID: 7YL2K

Calculation Name: 2C06-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2C06

Chain ID: A

ChEMBL ID:

UniProt ID: P13976

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	110
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-811448.972198
FMO2-HF: Nuclear repulsion	769695.694984
FMO2-HF: Total energy	-41753.277214
FMO2-MP2: Total energy	-41874.388577

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:MET)

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

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.
80.655	89.429	10.462	-8.476	-10.757	-0.066

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.815 / q_NPA : 0.904

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	ARG	1	0.906	0.936	3.805	28.541	30.073	-0.028	-0.643	-0.861	0.000
5	A	5	GLU	-1	-0.795	-0.877	2.046	-90.109	-89.414	7.764	-5.062	-3.397	-0.050
7	A	7	TRP	0	-0.058	-0.039	2.466	-6.528	-3.399	1.214	-1.607	-2.736	-0.016
27	A	27	ILE	0	-0.041	-0.017	3.226	0.661	1.408	0.039	-0.152	-0.634	-0.001
31	A	31	ALA	0	0.071	0.024	3.771	0.401	0.669	0.000	-0.062	-0.206	0.000
32	A	32	ALA	0	0.002	0.000	4.784	1.106	1.261	-0.001	-0.009	-0.144	0.000
34	A	34	ASN	0	0.024	0.018	2.911	6.347	7.352	1.429	-0.755	-1.679	0.001
35	A	35	ARG	1	0.960	0.983	4.857	28.833	29.131	0.003	-0.032	-0.270	0.000
38	A	38	ARG	1	0.842	0.936	5.189	25.078	25.186	-0.001	-0.011	-0.095	0.000
40	A	40	PRO	0	-0.030	-0.003	3.970	0.205	0.721	0.041	-0.106	-0.450	0.000
41	A	41	VAL	0	0.057	0.022	6.225	1.292	1.298	-0.001	-0.003	-0.001	0.000
82	A	82	MET	0	-0.023	-0.015	3.688	-1.274	-1.039	0.004	-0.034	-0.205	0.000
83	A	83	LYS	1	0.785	0.888	5.086	24.245	24.325	-0.001	0.000	-0.079	0.000
4	A	4	GLY	0	0.086	0.041	6.983	0.929	0.929	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.009	-0.005	5.969	0.936	0.936	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.002	0.014	7.835	2.270	2.270	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.002	-0.006	8.638	-1.154	-1.154	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.031	0.000	10.726	0.985	0.985	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.040	0.019	12.937	-0.676	-0.676	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.777	-0.853	14.887	-13.459	-13.459	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.040	-0.034	16.096	-0.764	-0.764	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.041	-0.035	19.256	-0.182	-0.182	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.005	-0.001	21.561	0.417	0.417	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.006	-0.009	24.883	-0.186	-0.186	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.008	0.002	26.078	0.234	0.234	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.786	-0.872	19.867	-13.458	-13.458	0.000	0.000	0.000	0.000
19	A	19	GLN	0	-0.006	0.012	18.342	0.238	0.238	0.000	0.000	0.000	0.000
20	A	20	GLN	0	-0.025	-0.015	18.674	-0.562	-0.562	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.013	-0.001	19.547	0.063	0.063	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.032	-0.026	14.311	-0.675	-0.675	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.832	0.914	14.241	16.476	16.476	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.022	0.000	11.684	-1.327	-1.327	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.000	0.009	8.403	1.485	1.485	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.011	0.010	8.726	-2.908	-2.908	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.078	0.036	6.241	-0.044	-0.044	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.012	0.008	6.536	1.726	1.726	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.022	0.015	6.491	-4.653	-4.653	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.061	0.026	7.352	1.847	1.847	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.035	-0.010	6.034	1.852	1.852	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.049	0.013	8.439	1.428	1.428	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.039	0.016	5.723	-0.847	-0.847	0.000	0.000	0.000	0.000
42	A	42	VAL	0	-0.026	-0.022	7.377	-2.470	-2.470	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.020	0.017	9.949	1.682	1.682	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.029	0.013	12.506	-1.351	-1.351	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.022	0.029	14.070	0.508	0.508	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.015	-0.021	16.609	0.038	0.038	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.052	0.028	20.423	-0.255	-0.255	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.031	0.009	23.686	-0.189	-0.189	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.019	-0.009	25.191	0.306	0.306	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.046	-0.010	28.942	-0.139	-0.139	0.000	0.000	0.000	0.000
51	A	51	PHE	0	0.056	0.026	26.434	0.061	0.061	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.001	0.020	22.453	-0.087	-0.087	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.921	0.947	22.975	10.650	10.650	0.000	0.000	0.000	0.000
54	A	54	THR	0	0.001	-0.007	23.103	0.212	0.212	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.038	-0.015	24.429	0.607	0.607	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.030	0.019	25.417	-0.118	-0.118	0.000	0.000	0.000	0.000
57	A	57	PHE	0	0.056	0.022	22.044	-0.219	-0.219	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.032	-0.005	20.765	-0.794	-0.794	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.027	-0.017	17.330	0.522	0.522	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.062	-0.064	20.398	0.215	0.215	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.050	-0.022	15.605	-1.015	-1.015	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.931	-0.967	19.405	-13.141	-13.141	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.034	0.022	22.227	0.190	0.190	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.078	-0.047	16.945	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.012	0.010	18.878	-0.447	-0.447	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.033	-0.008	14.744	-0.648	-0.648	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.960	0.966	15.564	18.803	18.803	0.000	0.000	0.000	0.000
68	A	68	THR	0	-0.091	-0.082	13.902	0.574	0.574	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.009	0.006	16.402	0.373	0.373	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.009	-0.005	19.641	0.104	0.104	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.001	0.006	19.864	0.104	0.104	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.016	0.017	14.312	-0.184	-0.184	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.817	0.907	17.013	14.303	14.303	0.000	0.000	0.000	0.000
74	A	74	CYS	0	-0.039	-0.019	17.051	-1.121	-1.121	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.763	-0.876	18.389	-13.031	-13.031	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.042	-0.015	19.984	0.287	0.287	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.024	-0.007	15.421	-0.751	-0.751	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.913	0.935	14.719	15.743	15.743	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.022	-0.009	9.799	-1.018	-1.018	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.025	0.004	9.328	1.127	1.127	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.801	-0.902	9.101	-22.386	-22.386	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.044	0.022	7.770	0.124	0.124	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.854	0.925	9.683	18.299	18.299	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.029	0.021	7.269	0.276	0.276	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.035	0.017	5.512	1.691	1.691	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.845	0.913	6.477	21.138	21.138	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.896	0.944	4.838	45.821	45.821	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.006	0.006	7.579	2.741	2.741	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.765	-0.862	9.431	-20.926	-20.926	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.806	0.890	7.622	27.679	27.679	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.036	0.039	9.306	2.282	2.282	0.000	0.000	0.000	0.000
94	A	94	PRO	0	0.049	0.017	11.626	-1.720	-1.720	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.846	-0.932	11.813	-25.528	-25.528	0.000	0.000	0.000	0.000
96	A	96	THR	0	0.024	0.009	14.730	0.082	0.082	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.016	0.008	14.510	0.547	0.547	0.000	0.000	0.000	0.000
98	A	98	MET	0	-0.024	0.004	10.998	-1.159	-1.159	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.033	-0.025	13.998	0.729	0.729	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.682	-0.823	17.460	-13.559	-13.559	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.002	-0.002	13.085	0.496	0.496	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.062	-0.040	13.372	0.237	0.237	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.008	0.020	16.661	0.535	0.535	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.844	0.913	18.921	14.095	14.095	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.000	0.003	14.131	0.307	0.307	0.000	0.000	0.000	0.000
106	A	106	SER	0	0.039	0.020	18.798	0.161	0.161	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.030	-0.037	21.811	0.450	0.450	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.028	-0.011	19.156	0.315	0.315	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.105	-0.037	20.316	-0.087	-0.087	0.000	0.000	0.000	0.000
110	A	110	THR	-1	-0.922	-0.944	24.362	-10.180	-10.180	0.000	0.000	0.000	0.000

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