FMO DATABASE

FMODB ID: 3KYKL

Calculation Name: 2CFX-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CFX

Chain ID: A

ChEMBL ID:

UniProt ID: P96582

Base Structure: X-ray

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	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1151981.195112
FMO2-HF: Nuclear repulsion	1095374.647081
FMO2-HF: Total energy	-56606.548031
FMO2-MP2: Total energy	-56770.18293

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.
-97.835	-86.592	17.254	-9.415	-19.081	-0.126

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 : 0.775 / q_NPA : 0.909

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	LEU	0	0.080	0.039	2.710	-1.746	2.225	1.066	-1.738	-3.300	-0.012
4	A	4	ASP	-1	-0.854	-0.910	4.779	-27.000	-26.938	0.003	-0.005	-0.060	0.000
7	A	7	ASP	-1	-0.775	-0.880	4.795	-32.750	-32.398	0.007	-0.095	-0.264	0.000
40	A	40	VAL	0	0.028	0.010	4.636	-3.307	-3.197	-0.001	-0.004	-0.105	0.000
42	A	42	GLN	0	-0.007	0.000	2.209	-8.235	-7.623	1.263	-0.268	-1.606	-0.002
43	A	43	LEU	0	-0.008	-0.024	2.144	-9.337	-7.841	4.160	-2.034	-3.622	-0.011
44	A	44	GLU	-1	-0.775	-0.837	2.912	-20.548	-21.808	0.033	1.432	-0.206	-0.001
46	A	46	PHE	0	0.017	-0.013	2.246	-27.013	-20.972	8.787	-6.437	-8.390	-0.098
47	A	47	GLY	0	0.003	0.011	4.341	0.039	0.103	-0.001	-0.009	-0.053	0.000
48	A	48	ILE	0	-0.054	-0.024	2.328	1.673	1.468	1.937	-0.257	-1.475	-0.002
5	A	5	GLN	0	0.060	0.013	7.823	-0.448	-0.448	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.004	0.002	9.374	0.991	0.991	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.020	-0.007	7.047	0.451	0.451	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.042	0.020	9.759	0.917	0.917	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.019	-0.007	7.986	1.016	1.016	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.002	-0.004	6.053	0.728	0.728	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.883	-0.921	9.984	-14.563	-14.563	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.856	-0.940	13.606	-13.202	-13.202	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.046	-0.027	9.774	0.636	0.636	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.923	0.966	12.495	18.675	18.675	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.806	0.897	15.417	15.090	15.090	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.819	-0.888	17.157	-11.796	-11.796	0.000	0.000	0.000	0.000
18	A	18	SER	0	0.003	0.015	15.150	-0.372	-0.372	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.840	0.879	15.825	11.303	11.303	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.059	-0.007	15.769	0.288	0.288	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.016	-0.036	15.751	-0.770	-0.770	0.000	0.000	0.000	0.000
22	A	22	MET	0	0.063	0.011	12.260	-0.291	-0.291	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.920	0.974	15.353	11.867	11.867	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.848	-0.908	18.618	-12.146	-12.146	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.065	0.040	11.431	0.287	0.287	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.035	0.020	15.535	-0.169	-0.169	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.918	0.952	16.372	11.040	11.040	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.898	0.972	17.324	13.324	13.324	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.034	0.006	12.177	0.268	0.268	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.826	0.923	15.476	12.215	12.215	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.017	0.020	11.059	-0.347	-0.347	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.013	0.008	15.574	0.342	0.342	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.060	0.010	15.200	-0.804	-0.804	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.021	0.007	14.183	-0.629	-0.629	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.016	0.013	11.690	-1.779	-1.779	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.021	-0.005	10.363	-1.391	-1.391	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.020	-0.025	9.552	-1.462	-1.462	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.824	-0.894	6.780	-32.310	-32.310	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.829	0.880	5.606	24.385	24.385	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.882	0.926	6.015	22.824	22.824	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.078	-0.042	5.274	-0.766	-0.766	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.044	-0.024	5.909	3.256	3.256	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.954	0.971	7.905	20.606	20.606	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.003	-0.009	10.723	0.546	0.546	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.067	-0.041	10.078	-0.051	-0.051	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.005	-0.016	14.802	0.773	0.773	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.010	-0.005	18.002	0.021	0.021	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.839	-0.906	21.327	-11.866	-11.866	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.009	-0.019	23.284	0.260	0.260	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.812	-0.905	27.020	-8.711	-8.711	0.000	0.000	0.000	0.000
58	A	58	GLN	0	0.090	0.031	27.699	0.435	0.435	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.975	1.004	31.822	7.860	7.860	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.814	0.887	33.870	8.614	8.614	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.036	-0.007	29.914	0.119	0.119	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.005	0.011	34.489	0.065	0.065	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.037	-0.008	32.433	0.124	0.124	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.067	-0.041	35.068	-0.164	-0.164	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.023	0.006	37.418	0.051	0.051	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.033	-0.002	31.940	-0.255	-0.255	0.000	0.000	0.000	0.000
67	A	67	CYS	0	-0.031	0.001	33.750	0.294	0.294	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.015	0.015	29.666	-0.324	-0.324	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.033	-0.021	32.388	0.341	0.341	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.851	-0.912	32.490	-9.189	-9.189	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.010	-0.009	33.385	0.297	0.297	0.000	0.000	0.000	0.000
72	A	72	THR	0	0.007	-0.007	34.068	-0.170	-0.170	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.001	-0.032	33.356	0.215	0.215	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.868	0.940	36.446	7.671	7.671	0.000	0.000	0.000	0.000
75	A	75	ASN	0	-0.017	-0.032	38.912	-0.173	-0.173	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.032	0.025	36.506	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.840	-0.906	35.385	-9.049	-9.049	0.000	0.000	0.000	0.000
78	A	78	TYR	0	-0.019	-0.097	30.525	-0.068	-0.068	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.797	-0.886	28.476	-11.460	-11.460	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.828	0.938	32.186	8.084	8.084	0.000	0.000	0.000	0.000
81	A	81	PHE	0	0.018	0.004	30.807	0.051	0.051	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.835	0.911	25.364	11.708	11.708	0.000	0.000	0.000	0.000
83	A	83	SER	0	-0.006	-0.024	30.092	-0.162	-0.162	0.000	0.000	0.000	0.000
84	A	84	TYR	0	0.009	0.004	31.833	0.108	0.108	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.038	0.019	28.616	0.060	0.060	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.041	-0.029	25.125	0.013	0.013	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.099	-0.049	29.484	0.065	0.065	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.047	-0.017	31.570	0.350	0.350	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.017	0.016	30.574	-0.350	-0.350	0.000	0.000	0.000	0.000
90	A	90	ASN	0	0.011	-0.014	30.205	-0.111	-0.111	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.002	0.011	27.882	0.061	0.061	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.847	-0.893	24.786	-11.264	-11.264	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.002	-0.011	23.404	-0.604	-0.604	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.023	-0.015	24.302	0.588	0.588	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.014	0.006	20.506	-0.800	-0.800	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.871	0.951	24.738	11.312	11.312	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.039	-0.018	25.132	-0.574	-0.574	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.006	-0.006	27.201	0.216	0.216	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.014	-0.007	28.783	-0.030	-0.030	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.009	-0.002	32.363	0.086	0.086	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.009	0.016	33.841	0.216	0.216	0.000	0.000	0.000	0.000
102	A	102	CYS	-1	-0.797	-0.780	31.747	-9.763	-9.763	0.000	0.000	0.000	0.000
103	A	103	TYR	0	0.006	-0.025	27.363	-0.486	-0.486	0.000	0.000	0.000	0.000
104	A	104	MET	0	0.023	0.029	28.039	0.390	0.390	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.018	-0.010	27.698	-0.512	-0.512	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.868	0.938	27.403	10.762	10.762	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.007	0.009	29.534	-0.198	-0.198	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.033	-0.013	28.879	0.261	0.261	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.034	0.003	32.978	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.845	-0.930	36.574	-7.970	-7.970	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.015	-0.023	39.364	0.124	0.124	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.018	-0.009	40.994	-0.129	-0.129	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.917	-0.937	42.829	-6.534	-6.534	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.044	0.029	39.916	-0.031	-0.031	0.000	0.000	0.000	0.000
115	A	115	VAL	0	-0.041	-0.027	37.988	-0.181	-0.181	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.898	-0.946	40.183	-6.707	-6.707	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.875	-0.938	42.386	-6.983	-6.983	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.045	-0.030	34.272	-0.125	-0.125	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.019	-0.012	38.622	-0.104	-0.104	0.000	0.000	0.000	0.000
120	A	120	ASN	0	-0.010	0.002	40.827	-0.030	-0.030	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.904	0.962	37.303	8.185	8.185	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.022	-0.017	36.422	-0.110	-0.110	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.006	0.012	39.116	-0.056	-0.056	0.000	0.000	0.000	0.000
124	A	124	PRO	0	-0.056	-0.028	41.685	0.051	0.051	0.000	0.000	0.000	0.000
125	A	125	TYR	0	-0.047	-0.028	37.224	-0.014	-0.014	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.018	0.001	36.331	-0.181	-0.181	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.069	-0.035	38.457	0.442	0.442	0.000	0.000	0.000	0.000
128	A	128	THR	0	0.010	-0.005	36.593	-0.216	-0.216	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.022	0.023	37.716	0.253	0.253	0.000	0.000	0.000	0.000
130	A	130	THR	0	0.004	-0.003	37.162	-0.314	-0.314	0.000	0.000	0.000	0.000
131	A	131	HIS	0	-0.035	-0.022	35.029	0.344	0.344	0.000	0.000	0.000	0.000
132	A	132	VAL	0	0.024	-0.008	35.987	-0.213	-0.213	0.000	0.000	0.000	0.000
133	A	133	ILE	0	-0.028	-0.011	31.407	0.029	0.029	0.000	0.000	0.000	0.000
134	A	134	PHE	0	-0.024	-0.014	35.700	0.109	0.109	0.000	0.000	0.000	0.000
135	A	135	SER	0	-0.054	-0.029	35.036	0.097	0.097	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.944	-0.970	27.951	-10.325	-10.325	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.038	-0.020	29.915	0.240	0.240	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.875	-0.945	26.091	-11.121	-11.121	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.107	-0.063	24.485	0.009	0.009	0.000	0.000	0.000	0.000
140	A	140	LYS	0	-0.084	-0.011	20.635	-1.081	-1.081	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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