FMO DATABASE

FMODB ID: 8G36Y

Calculation Name: 2CWJ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CWJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9YBU8

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-893548.743194
FMO2-HF: Nuclear repulsion	849689.078021
FMO2-HF: Total energy	-43859.665173
FMO2-MP2: Total energy	-43988.265328

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:4:ALA)

Summations of interaction energy for fragment #1(A:4:ALA)

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.
-112.507	-110.217	2.174	-1.324	-3.138	-0.015

Interaction energy analysis for fragmet #1(A:4:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.878 / q_NPA : 0.933

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	6	LYS	1	0.907	0.962	3.439	65.713	66.848	0.000	-0.492	-0.642	0.000
28	A	31	PRO	0	-0.081	-0.046	1.964	-4.329	-4.724	2.103	-0.229	-1.479	-0.009
29	A	32	GLU	-1	-1.015	-1.016	2.785	-70.819	-69.502	0.074	-0.562	-0.829	-0.006
30	A	33	THR	0	-0.022	-0.015	4.973	6.362	6.421	-0.001	-0.004	-0.053	0.000
51	A	54	ALA	0	0.026	0.018	4.456	-0.341	-0.280	-0.001	-0.011	-0.049	0.000
52	A	55	ILE	0	-0.069	-0.037	4.117	-1.355	-1.242	-0.001	-0.026	-0.086	0.000
4	A	7	PRO	0	0.022	0.033	6.610	1.528	1.528	0.000	0.000	0.000	0.000
5	A	8	VAL	0	0.001	0.006	9.951	0.226	0.226	0.000	0.000	0.000	0.000
6	A	9	GLY	0	0.032	0.008	13.039	1.388	1.388	0.000	0.000	0.000	0.000
7	A	10	PRO	0	-0.046	-0.032	15.768	-0.484	-0.484	0.000	0.000	0.000	0.000
8	A	11	TYR	0	0.009	0.019	11.022	0.569	0.569	0.000	0.000	0.000	0.000
9	A	12	SER	0	0.035	0.014	11.719	-1.208	-1.208	0.000	0.000	0.000	0.000
10	A	13	GLN	0	-0.017	-0.015	5.253	1.672	1.672	0.000	0.000	0.000	0.000
11	A	14	ALA	0	0.046	0.022	9.860	-0.076	-0.076	0.000	0.000	0.000	0.000
12	A	15	VAL	0	-0.058	-0.021	11.615	-0.056	-0.056	0.000	0.000	0.000	0.000
13	A	16	GLU	-1	-0.842	-0.923	14.829	-15.975	-15.975	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.048	-0.031	16.642	0.713	0.713	0.000	0.000	0.000	0.000
15	A	18	GLY	0	-0.011	-0.003	20.358	0.255	0.255	0.000	0.000	0.000	0.000
16	A	19	CYS	0	-0.018	-0.009	21.579	-0.120	-0.120	0.000	0.000	0.000	0.000
17	A	20	PHE	0	-0.030	-0.019	19.923	0.323	0.323	0.000	0.000	0.000	0.000
18	A	21	MET	0	0.039	0.039	11.295	-0.586	-0.586	0.000	0.000	0.000	0.000
19	A	22	PHE	0	-0.037	-0.017	16.403	0.270	0.270	0.000	0.000	0.000	0.000
20	A	23	VAL	0	-0.010	-0.007	11.164	-0.960	-0.960	0.000	0.000	0.000	0.000
21	A	24	SER	0	-0.001	-0.030	12.387	1.464	1.464	0.000	0.000	0.000	0.000
22	A	25	GLY	0	0.011	0.003	12.708	-1.014	-1.014	0.000	0.000	0.000	0.000
23	A	26	GLN	0	-0.037	-0.033	8.114	-0.204	-0.204	0.000	0.000	0.000	0.000
24	A	27	ILE	0	0.062	0.016	10.664	1.569	1.569	0.000	0.000	0.000	0.000
25	A	28	PRO	0	-0.045	-0.001	9.690	-3.408	-3.408	0.000	0.000	0.000	0.000
26	A	29	ILE	0	0.000	0.004	7.806	1.416	1.416	0.000	0.000	0.000	0.000
27	A	30	ASN	0	0.116	0.067	6.977	-8.159	-8.159	0.000	0.000	0.000	0.000
31	A	34	GLY	0	-0.055	-0.017	7.388	3.136	3.136	0.000	0.000	0.000	0.000
32	A	35	ALA	0	0.015	0.015	9.121	2.665	2.665	0.000	0.000	0.000	0.000
33	A	36	LEU	0	-0.025	-0.020	10.683	-2.282	-2.282	0.000	0.000	0.000	0.000
34	A	37	GLU	-1	-0.878	-0.962	9.920	-29.834	-29.834	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.890	-0.944	13.233	-15.260	-15.260	0.000	0.000	0.000	0.000
36	A	39	GLY	0	-0.028	-0.007	16.362	-0.370	-0.370	0.000	0.000	0.000	0.000
37	A	40	GLY	0	0.003	0.003	18.153	0.812	0.812	0.000	0.000	0.000	0.000
38	A	41	PHE	0	-0.041	-0.026	19.582	0.548	0.548	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.873	0.924	18.562	13.287	13.287	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.851	-0.925	15.733	-16.776	-16.776	0.000	0.000	0.000	0.000
41	A	44	SER	0	0.036	0.005	13.998	-1.177	-1.177	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.004	-0.006	13.853	-1.177	-1.177	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.901	0.963	13.101	21.399	21.399	0.000	0.000	0.000	0.000
44	A	47	ARG	1	0.925	0.965	4.837	40.552	40.552	0.000	0.000	0.000	0.000
45	A	48	ALA	0	-0.025	-0.017	9.395	-2.706	-2.706	0.000	0.000	0.000	0.000
46	A	49	LEU	0	0.009	0.016	10.718	-0.704	-0.704	0.000	0.000	0.000	0.000
47	A	50	ASP	-1	-0.837	-0.906	8.331	-25.946	-25.946	0.000	0.000	0.000	0.000
48	A	51	ASN	0	-0.092	-0.068	5.808	-7.765	-7.765	0.000	0.000	0.000	0.000
49	A	52	LEU	0	-0.003	0.011	6.856	-2.162	-2.162	0.000	0.000	0.000	0.000
50	A	53	LYS	1	0.922	0.957	8.932	21.986	21.986	0.000	0.000	0.000	0.000
53	A	56	VAL	0	-0.034	-0.011	6.532	1.943	1.943	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.907	-0.956	8.779	-25.767	-25.767	0.000	0.000	0.000	0.000
55	A	58	GLY	0	-0.052	-0.025	7.262	0.813	0.813	0.000	0.000	0.000	0.000
56	A	59	ALA	0	-0.059	-0.031	8.139	1.183	1.183	0.000	0.000	0.000	0.000
57	A	60	GLY	0	-0.018	0.000	11.324	1.576	1.576	0.000	0.000	0.000	0.000
58	A	61	TYR	0	0.019	-0.012	12.728	0.947	0.947	0.000	0.000	0.000	0.000
59	A	62	SER	0	0.031	0.018	13.494	-1.445	-1.445	0.000	0.000	0.000	0.000
60	A	63	MET	0	0.007	-0.004	12.976	-0.168	-0.168	0.000	0.000	0.000	0.000
61	A	64	ASP	-1	-0.969	-0.992	15.980	-14.693	-14.693	0.000	0.000	0.000	0.000
62	A	65	ASP	-1	-0.801	-0.879	18.462	-13.320	-13.320	0.000	0.000	0.000	0.000
63	A	66	ILE	0	-0.058	-0.012	14.507	0.311	0.311	0.000	0.000	0.000	0.000
64	A	67	VAL	0	0.023	0.009	19.046	0.575	0.575	0.000	0.000	0.000	0.000
65	A	68	LYS	1	0.784	0.880	20.619	13.443	13.443	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.033	0.019	17.456	-0.705	-0.705	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.027	-0.033	19.008	1.194	1.194	0.000	0.000	0.000	0.000
68	A	71	VAL	0	-0.006	0.006	18.462	-0.765	-0.765	0.000	0.000	0.000	0.000
69	A	72	TYR	0	-0.035	-0.038	18.925	1.288	1.288	0.000	0.000	0.000	0.000
70	A	73	ILE	0	0.017	-0.001	19.980	-0.797	-0.797	0.000	0.000	0.000	0.000
71	A	74	THR	0	-0.028	-0.017	21.303	0.648	0.648	0.000	0.000	0.000	0.000
72	A	75	ASP	-1	-0.831	-0.895	23.737	-11.231	-11.231	0.000	0.000	0.000	0.000
73	A	76	ILE	0	0.009	0.006	25.986	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	77	SER	0	0.018	0.004	28.400	-0.075	-0.075	0.000	0.000	0.000	0.000
75	A	78	ARG	1	0.868	0.937	23.250	12.438	12.438	0.000	0.000	0.000	0.000
76	A	79	PHE	0	0.009	0.007	23.937	-0.436	-0.436	0.000	0.000	0.000	0.000
77	A	80	SER	0	-0.037	-0.028	25.152	-0.210	-0.210	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.849	-0.943	22.917	-12.885	-12.885	0.000	0.000	0.000	0.000
79	A	82	PHE	0	0.021	0.010	17.891	-0.442	-0.442	0.000	0.000	0.000	0.000
80	A	83	ASN	0	-0.007	-0.026	20.891	-0.672	-0.672	0.000	0.000	0.000	0.000
81	A	84	GLU	-1	-0.919	-0.939	22.933	-13.090	-13.090	0.000	0.000	0.000	0.000
82	A	85	VAL	0	0.048	0.024	16.672	-0.086	-0.086	0.000	0.000	0.000	0.000
83	A	86	TYR	0	0.019	0.006	18.269	-0.639	-0.639	0.000	0.000	0.000	0.000
84	A	87	ARG	1	0.869	0.933	19.004	12.935	12.935	0.000	0.000	0.000	0.000
85	A	88	GLU	-1	-0.930	-0.963	17.577	-15.590	-15.590	0.000	0.000	0.000	0.000
86	A	89	TYR	0	-0.125	-0.087	11.853	-0.392	-0.392	0.000	0.000	0.000	0.000
87	A	90	PHE	0	0.027	0.022	16.327	-0.222	-0.222	0.000	0.000	0.000	0.000
88	A	91	ASN	0	0.013	0.007	19.565	0.135	0.135	0.000	0.000	0.000	0.000
89	A	92	ARG	1	0.928	0.965	22.674	10.484	10.484	0.000	0.000	0.000	0.000
90	A	93	PRO	0	0.022	0.002	25.110	0.161	0.161	0.000	0.000	0.000	0.000
91	A	94	TYR	0	0.000	-0.011	22.428	0.051	0.051	0.000	0.000	0.000	0.000
92	A	95	PRO	0	0.022	0.051	19.949	0.539	0.539	0.000	0.000	0.000	0.000
93	A	96	ALA	0	0.013	-0.002	23.006	0.199	0.199	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.914	0.979	21.559	12.144	12.144	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.053	-0.020	23.540	0.552	0.552	0.000	0.000	0.000	0.000
96	A	99	VAL	0	0.008	-0.011	23.009	-0.607	-0.607	0.000	0.000	0.000	0.000
97	A	100	VAL	0	-0.017	0.000	24.311	0.581	0.581	0.000	0.000	0.000	0.000
98	A	101	GLY	0	0.026	0.025	24.835	-0.457	-0.457	0.000	0.000	0.000	0.000
99	A	102	VAL	0	-0.019	-0.017	22.820	0.354	0.354	0.000	0.000	0.000	0.000
100	A	103	ALA	0	-0.015	-0.013	25.891	0.417	0.417	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.024	-0.014	24.322	0.052	0.052	0.000	0.000	0.000	0.000
102	A	105	LEU	0	0.015	0.025	18.444	0.041	0.041	0.000	0.000	0.000	0.000
103	A	106	PRO	0	0.028	0.016	16.424	0.294	0.294	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.034	-0.030	13.896	-0.577	-0.577	0.000	0.000	0.000	0.000
105	A	108	GLY	0	0.004	0.013	18.074	0.056	0.056	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.017	0.006	15.878	0.174	0.174	0.000	0.000	0.000	0.000
107	A	110	PRO	0	0.032	0.000	16.777	0.675	0.675	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.043	-0.022	15.332	0.871	0.871	0.000	0.000	0.000	0.000
109	A	112	GLU	-1	-0.856	-0.933	14.942	-19.232	-19.232	0.000	0.000	0.000	0.000
110	A	113	VAL	0	-0.051	-0.025	13.503	1.325	1.325	0.000	0.000	0.000	0.000
111	A	114	GLU	-1	-0.813	-0.867	14.230	-16.284	-16.284	0.000	0.000	0.000	0.000
112	A	115	ALA	0	-0.054	-0.038	15.005	0.671	0.671	0.000	0.000	0.000	0.000
113	A	116	VAL	0	-0.016	-0.003	16.240	-0.351	-0.351	0.000	0.000	0.000	0.000
114	A	117	LEU	0	-0.041	-0.006	13.937	0.361	0.361	0.000	0.000	0.000	0.000
115	A	118	TYR	0	-0.090	-0.063	18.616	0.240	0.240	0.000	0.000	0.000	0.000
116	A	119	THR	-1	-0.858	-0.904	17.216	-13.631	-13.631	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ALA)