FMO DATABASE

FMODB ID: 86J1Y

Calculation Name: 2XC7-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2XC7

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H814

Base Structure: SolutionNMR

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-758663.555685
FMO2-HF: Nuclear repulsion	717301.770941
FMO2-HF: Total energy	-41361.784744
FMO2-MP2: Total energy	-41482.507785

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.
-103.467	-104.051	15.59	-8.776	-6.228	-0.09

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 : 0.785 / q_NPA : 0.869

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

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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	MET	0	-0.022	-0.002	3.833	9.962	12.491	-0.026	-1.277	-1.225	-0.007
4	A	4	ALA	0	0.043	0.014	4.682	5.110	5.179	-0.001	-0.005	-0.062	0.000
5	A	5	GLU	-1	-0.786	-0.882	1.821	-118.667	-121.844	15.618	-7.492	-4.949	-0.083
6	A	6	ASP	-1	-0.839	-0.911	5.357	-27.737	-27.742	-0.001	-0.002	0.008	0.000
7	A	7	SER	0	-0.001	0.002	8.653	3.898	3.898	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.059	0.004	10.362	-0.641	-0.641	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.929	-0.948	13.614	-19.243	-19.243	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.959	0.983	7.155	32.632	32.632	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.041	-0.017	11.030	0.628	0.628	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.015	0.008	12.986	1.133	1.133	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.918	-0.948	14.310	-19.078	-19.078	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.847	-0.929	10.952	-24.423	-24.423	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.026	-0.026	14.343	0.938	0.938	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.056	-0.041	17.283	1.210	1.210	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.001	0.002	15.898	0.987	0.987	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.919	0.960	13.696	20.648	20.648	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.050	-0.018	18.331	0.639	0.639	0.000	0.000	0.000	0.000
20	A	20	GLN	0	-0.063	-0.030	21.506	1.108	1.108	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.798	-0.901	22.609	-11.613	-11.613	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.027	-0.008	24.384	-0.095	-0.095	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.746	0.859	27.242	10.665	10.665	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.947	0.952	21.942	13.340	13.340	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.840	-0.897	23.037	-12.453	-12.453	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.037	-0.006	24.481	-0.265	-0.265	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.015	-0.012	20.261	-0.167	-0.167	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.034	0.007	19.723	-0.686	-0.686	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.745	0.856	20.756	10.728	10.728	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.028	0.014	20.772	0.085	0.085	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.021	-0.001	16.064	-0.113	-0.113	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.907	0.955	18.906	12.460	12.460	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.014	0.011	21.142	0.129	0.129	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.014	-0.008	19.494	0.142	0.142	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.004	0.006	18.528	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.003	-0.017	12.054	1.679	1.679	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.907	0.933	11.914	20.798	20.798	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.882	0.945	13.477	15.033	15.033	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.054	0.032	15.848	0.702	0.702	0.000	0.000	0.000	0.000
40	A	40	ILE	0	0.026	0.005	9.656	0.100	0.100	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.834	-0.915	13.721	-19.394	-19.394	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.003	0.010	16.308	0.657	0.657	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.010	-0.003	13.164	0.562	0.562	0.000	0.000	0.000	0.000
44	A	44	MET	0	-0.061	-0.011	14.503	-0.035	-0.035	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.767	-0.884	17.016	-12.478	-12.478	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.018	-0.041	19.716	0.580	0.580	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.019	-0.003	19.180	0.577	0.577	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.918	-0.939	21.175	-12.068	-12.068	0.000	0.000	0.000	0.000
49	A	49	VAL	0	0.014	-0.004	23.688	0.690	0.690	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.897	-0.924	23.044	-11.367	-11.367	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.037	-0.015	25.102	0.280	0.280	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.021	-0.016	27.046	0.708	0.708	0.000	0.000	0.000	0.000
53	A	53	GLY	0	-0.010	0.015	28.952	0.361	0.361	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.006	-0.004	30.153	0.284	0.284	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.053	-0.039	29.237	-0.320	-0.320	0.000	0.000	0.000	0.000
56	A	56	PHE	0	-0.008	-0.001	31.538	0.274	0.274	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.007	0.010	31.265	-0.161	-0.161	0.000	0.000	0.000	0.000
58	A	58	MET	0	0.045	0.002	33.803	0.269	0.269	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.011	0.018	36.454	0.278	0.278	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.014	0.016	37.733	0.222	0.222	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.034	-0.020	38.618	0.015	0.015	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.918	0.956	35.136	8.611	8.611	0.000	0.000	0.000	0.000
63	A	63	ARG	1	1.004	0.992	34.347	8.229	8.229	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.800	0.868	26.848	11.029	11.029	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.007	0.022	29.791	-0.208	-0.208	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.096	0.039	24.822	-0.088	-0.088	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.081	0.041	24.315	-0.295	-0.295	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.031	-0.023	25.378	-0.063	-0.063	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.006	-0.004	24.854	0.176	0.176	0.000	0.000	0.000	0.000
70	A	70	PHE	0	0.086	0.032	18.595	0.048	0.048	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.031	-0.019	23.589	0.093	0.093	0.000	0.000	0.000	0.000
72	A	72	ASN	0	0.004	-0.010	26.604	0.578	0.578	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.044	0.040	21.201	0.293	0.293	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.025	-0.011	23.742	0.050	0.050	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.790	0.890	26.522	10.718	10.718	0.000	0.000	0.000	0.000
76	A	76	ASN	0	-0.068	-0.037	25.411	0.609	0.609	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.001	0.022	23.064	-0.089	-0.089	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.022	0.009	23.528	0.367	0.367	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.062	-0.034	23.856	0.176	0.176	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.038	-0.021	22.026	-0.379	-0.379	0.000	0.000	0.000	0.000
81	A	81	SER	0	0.033	0.017	26.436	0.218	0.218	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.870	-0.949	29.892	-9.245	-9.245	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.834	-0.899	32.111	-8.908	-8.908	0.000	0.000	0.000	0.000
84	A	84	GLN	0	0.015	-0.006	27.313	-0.142	-0.142	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.039	-0.001	26.993	-0.207	-0.207	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.831	0.897	29.535	9.005	9.005	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.934	-0.976	30.061	-10.291	-10.291	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.003	0.006	24.796	-0.055	-0.055	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.005	-0.030	27.566	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.073	-0.015	30.218	0.228	0.228	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.019	0.028	32.987	0.350	0.350	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.791	-0.876	31.177	-9.961	-9.961	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.013	-0.009	31.774	-0.248	-0.248	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.019	0.007	34.175	0.210	0.210	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.937	0.970	36.853	7.751	7.751	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.939	-0.971	39.472	-7.875	-7.875	0.000	0.000	0.000	0.000
97	A	97	TYR	0	0.023	0.005	42.998	-0.095	-0.095	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.849	-0.932	46.043	-6.846	-6.846	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.050	-0.027	44.590	0.164	0.164	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.935	0.959	47.359	6.697	6.697	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.917	0.968	50.990	6.157	6.157	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.030	0.015	50.034	-0.022	-0.022	0.000	0.000	0.000	0.000
103	A	103	ALA	0	-0.058	-0.024	51.254	0.124	0.124	0.000	0.000	0.000	0.000
104	A	104	ARG	0	0.058	0.044	51.455	0.174	0.174	0.000	0.000	0.000	0.000

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