FMO DATABASE

FMODB ID: 1VJ9Z

Calculation Name: 3CAD-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3CAD

Chain ID: A

ChEMBL ID:

UniProt ID: Q60654

Base Structure: X-ray

Registration Date: 2025-10-06

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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1100560.986785
FMO2-HF: Nuclear repulsion	1048612.595493
FMO2-HF: Total energy	-51948.391292
FMO2-MP2: Total energy	-52093.991595

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:140:GLU)

Summations of interaction energy for fragment #1(A:140:GLU)

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.
8.093	9.987	3.429	-1.8	-3.523	0.013

Interaction energy analysis for fragmet #1(A:140:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / q_NPA : -0.006

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	142	TYR	0	0.045	0.032	3.878	3.972	5.778	-0.021	-0.860	-0.925	-0.001
5	A	144	PHE	0	0.016	-0.001	2.343	4.978	5.066	3.450	-0.940	-2.598	0.014
4	A	143	TRP	0	0.033	0.017	5.964	1.082	1.082	0.000	0.000	0.000	0.000
6	A	145	CYS	0	-0.029	-0.010	6.380	-2.351	-2.351	0.000	0.000	0.000	0.000
7	A	146	TYR	0	0.052	0.030	8.666	1.119	1.119	0.000	0.000	0.000	0.000
8	A	147	GLY	0	-0.012	0.000	11.449	-0.609	-0.609	0.000	0.000	0.000	0.000
9	A	148	ILE	0	0.046	0.031	14.586	0.093	0.093	0.000	0.000	0.000	0.000
10	A	149	LYS	1	0.774	0.872	14.536	-2.327	-2.327	0.000	0.000	0.000	0.000
11	A	151	TYR	0	-0.043	-0.064	9.736	-0.807	-0.807	0.000	0.000	0.000	0.000
12	A	152	TYR	0	0.014	0.004	9.576	1.059	1.059	0.000	0.000	0.000	0.000
13	A	153	PHE	0	-0.011	-0.009	8.326	-0.210	-0.210	0.000	0.000	0.000	0.000
14	A	154	ASP	-1	-0.836	-0.938	10.524	-0.944	-0.944	0.000	0.000	0.000	0.000
15	A	155	MET	0	-0.012	-0.019	8.807	0.245	0.245	0.000	0.000	0.000	0.000
16	A	156	ASP	-1	-0.913	-0.939	12.382	-1.281	-1.281	0.000	0.000	0.000	0.000
17	A	157	ARG	1	0.757	0.844	15.886	1.094	1.094	0.000	0.000	0.000	0.000
18	A	158	LYS	1	0.951	0.972	17.841	0.243	0.243	0.000	0.000	0.000	0.000
19	A	159	THR	0	0.058	0.038	20.881	0.036	0.036	0.000	0.000	0.000	0.000
20	A	160	TRP	0	0.022	0.007	22.805	0.008	0.008	0.000	0.000	0.000	0.000
21	A	161	SER	0	0.011	-0.007	23.859	0.051	0.051	0.000	0.000	0.000	0.000
22	A	162	GLY	0	0.018	0.006	23.945	0.035	0.035	0.000	0.000	0.000	0.000
23	A	163	CYS	0	-0.024	0.015	15.091	0.165	0.165	0.000	0.000	0.000	0.000
24	A	164	LYS	1	0.899	0.959	21.065	-0.338	-0.338	0.000	0.000	0.000	0.000
25	A	165	GLN	0	-0.002	-0.020	23.253	0.113	0.113	0.000	0.000	0.000	0.000
26	A	166	THR	0	0.032	-0.006	19.065	-0.013	-0.013	0.000	0.000	0.000	0.000
27	A	167	CYS	0	-0.070	-0.023	14.508	-0.098	-0.098	0.000	0.000	0.000	0.000
28	A	168	GLN	0	-0.008	-0.005	20.140	0.093	0.093	0.000	0.000	0.000	0.000
29	A	169	ILE	0	-0.026	0.002	22.505	0.013	0.013	0.000	0.000	0.000	0.000
30	A	170	SER	0	0.000	0.008	18.896	0.031	0.031	0.000	0.000	0.000	0.000
31	A	171	SER	0	0.012	0.009	19.587	0.132	0.132	0.000	0.000	0.000	0.000
32	A	172	LEU	0	-0.034	-0.012	15.172	0.145	0.145	0.000	0.000	0.000	0.000
33	A	173	SER	0	-0.046	-0.021	18.798	-0.157	-0.157	0.000	0.000	0.000	0.000
34	A	174	LEU	0	0.001	0.000	18.629	0.180	0.180	0.000	0.000	0.000	0.000
35	A	175	LEU	0	-0.022	-0.009	14.817	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	176	LYS	1	0.885	0.955	18.475	-1.185	-1.185	0.000	0.000	0.000	0.000
37	A	177	ILE	0	0.009	0.011	17.657	0.177	0.177	0.000	0.000	0.000	0.000
38	A	178	ASP	-1	-0.747	-0.877	19.972	1.343	1.343	0.000	0.000	0.000	0.000
39	A	179	ASN	0	-0.040	-0.050	20.022	-0.067	-0.067	0.000	0.000	0.000	0.000
40	A	180	GLU	-1	-0.818	-0.924	20.383	1.107	1.107	0.000	0.000	0.000	0.000
41	A	181	ASP	-1	-0.929	-0.962	17.955	1.685	1.685	0.000	0.000	0.000	0.000
42	A	182	GLU	-1	-0.756	-0.809	15.506	2.418	2.418	0.000	0.000	0.000	0.000
43	A	183	LEU	0	0.026	0.006	15.078	0.217	0.217	0.000	0.000	0.000	0.000
44	A	184	LYS	1	0.916	0.953	15.656	-1.213	-1.213	0.000	0.000	0.000	0.000
45	A	185	PHE	0	0.017	-0.010	10.988	-0.111	-0.111	0.000	0.000	0.000	0.000
46	A	186	LEU	0	-0.011	0.000	10.872	0.510	0.510	0.000	0.000	0.000	0.000
47	A	187	GLN	0	-0.031	-0.030	11.463	-0.054	-0.054	0.000	0.000	0.000	0.000
48	A	188	ASN	0	-0.104	-0.031	10.211	-0.107	-0.107	0.000	0.000	0.000	0.000
49	A	189	LEU	0	0.029	0.014	5.313	-0.149	-0.149	0.000	0.000	0.000	0.000
50	A	190	ALA	0	-0.007	0.017	7.646	-0.153	-0.153	0.000	0.000	0.000	0.000
51	A	191	PRO	0	-0.009	-0.001	9.185	-0.623	-0.623	0.000	0.000	0.000	0.000
52	A	192	SER	0	-0.012	-0.027	10.261	0.478	0.478	0.000	0.000	0.000	0.000
53	A	193	ASP	-1	-0.829	-0.883	13.117	-0.756	-0.756	0.000	0.000	0.000	0.000
54	A	194	ILE	0	0.001	0.019	14.466	0.178	0.178	0.000	0.000	0.000	0.000
55	A	195	SER	0	0.031	-0.003	14.686	0.004	0.004	0.000	0.000	0.000	0.000
56	A	196	TRP	0	-0.062	-0.030	16.799	0.146	0.146	0.000	0.000	0.000	0.000
57	A	197	ILE	0	0.020	0.002	17.438	0.137	0.137	0.000	0.000	0.000	0.000
58	A	198	GLY	0	-0.001	0.008	19.897	-0.120	-0.120	0.000	0.000	0.000	0.000
59	A	199	PHE	0	-0.007	-0.016	22.634	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	200	SER	0	0.001	-0.007	25.318	-0.040	-0.040	0.000	0.000	0.000	0.000
61	A	201	TYR	0	-0.013	-0.004	28.421	0.015	0.015	0.000	0.000	0.000	0.000
62	A	202	ASP	-1	-0.794	-0.870	32.223	0.314	0.314	0.000	0.000	0.000	0.000
63	A	203	ASN	0	0.049	0.000	34.198	0.008	0.008	0.000	0.000	0.000	0.000
64	A	204	LYS	1	0.903	0.946	37.433	-0.269	-0.269	0.000	0.000	0.000	0.000
65	A	205	LYS	1	0.834	0.895	32.782	-0.427	-0.427	0.000	0.000	0.000	0.000
66	A	206	LYS	1	0.868	0.958	38.128	-0.201	-0.201	0.000	0.000	0.000	0.000
67	A	207	ASP	-1	-0.796	-0.886	34.711	0.320	0.320	0.000	0.000	0.000	0.000
68	A	208	TRP	0	-0.044	-0.031	28.512	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	209	ALA	0	-0.027	-0.015	30.130	0.022	0.022	0.000	0.000	0.000	0.000
70	A	210	TRP	0	0.043	0.030	21.892	0.029	0.029	0.000	0.000	0.000	0.000
71	A	211	ILE	0	-0.045	-0.034	22.773	-0.041	-0.041	0.000	0.000	0.000	0.000
72	A	212	ASP	-1	-0.892	-0.954	25.185	0.862	0.862	0.000	0.000	0.000	0.000
73	A	213	ASN	0	-0.070	-0.041	27.215	-0.027	-0.027	0.000	0.000	0.000	0.000
74	A	214	GLY	0	0.061	0.055	28.827	-0.044	-0.044	0.000	0.000	0.000	0.000
75	A	215	PRO	0	-0.020	-0.028	28.375	0.029	0.029	0.000	0.000	0.000	0.000
76	A	216	SER	0	-0.047	-0.017	24.261	0.036	0.036	0.000	0.000	0.000	0.000
77	A	217	LYS	1	0.892	0.959	24.854	-0.891	-0.891	0.000	0.000	0.000	0.000
78	A	218	LEU	0	0.017	-0.001	21.762	-0.038	-0.038	0.000	0.000	0.000	0.000
79	A	219	ALA	0	0.022	0.028	25.371	-0.061	-0.061	0.000	0.000	0.000	0.000
80	A	220	LEU	0	0.041	0.025	26.871	0.006	0.006	0.000	0.000	0.000	0.000
81	A	221	ASN	0	-0.013	-0.016	27.973	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	222	THR	0	0.001	-0.003	30.473	-0.045	-0.045	0.000	0.000	0.000	0.000
83	A	223	THR	0	0.046	0.015	31.894	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	224	LYS	1	0.852	0.929	27.798	-0.268	-0.268	0.000	0.000	0.000	0.000
85	A	225	TYR	0	-0.055	-0.009	26.168	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	226	ASN	0	0.036	0.003	32.233	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	227	ILE	0	0.028	-0.007	33.651	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	228	ARG	1	0.898	0.965	35.790	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	229	ASP	-1	-0.813	-0.899	29.827	0.018	0.018	0.000	0.000	0.000	0.000
90	A	230	GLY	0	0.020	0.008	31.469	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	231	LEU	0	0.012	-0.001	30.408	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	232	CYS	0	-0.061	-0.006	25.765	0.033	0.033	0.000	0.000	0.000	0.000
93	A	233	MET	0	-0.003	0.019	23.557	-0.051	-0.051	0.000	0.000	0.000	0.000
94	A	234	SER	0	-0.053	-0.020	20.484	0.014	0.014	0.000	0.000	0.000	0.000
95	A	235	LEU	0	-0.002	-0.011	15.254	0.067	0.067	0.000	0.000	0.000	0.000
96	A	236	SER	0	-0.019	-0.023	17.170	-0.105	-0.105	0.000	0.000	0.000	0.000
97	A	237	LYS	1	1.016	0.992	14.362	0.353	0.353	0.000	0.000	0.000	0.000
98	A	238	THR	0	-0.043	0.002	16.181	0.060	0.060	0.000	0.000	0.000	0.000
99	A	239	ARG	1	0.948	0.972	19.723	-0.154	-0.154	0.000	0.000	0.000	0.000
100	A	240	LEU	0	0.038	0.037	19.969	-0.064	-0.064	0.000	0.000	0.000	0.000
101	A	241	ASP	-1	-0.851	-0.919	22.463	0.179	0.179	0.000	0.000	0.000	0.000
102	A	242	ASN	0	-0.016	-0.036	24.438	0.044	0.044	0.000	0.000	0.000	0.000
103	A	243	GLY	0	0.006	0.015	26.728	-0.031	-0.031	0.000	0.000	0.000	0.000
104	A	244	ASP	-1	-0.902	-0.962	26.783	-0.069	-0.069	0.000	0.000	0.000	0.000
105	A	246	GLY	0	0.027	0.013	26.298	0.000	0.000	0.000	0.000	0.000	0.000
106	A	247	LYS	1	0.945	0.975	24.109	0.073	0.073	0.000	0.000	0.000	0.000
107	A	248	SER	0	-0.019	-0.016	21.331	0.059	0.059	0.000	0.000	0.000	0.000
108	A	249	TYR	0	-0.007	-0.009	17.905	-0.117	-0.117	0.000	0.000	0.000	0.000
109	A	250	ILE	0	0.027	0.047	11.520	0.050	0.050	0.000	0.000	0.000	0.000
110	A	252	ILE	0	0.009	0.015	12.272	0.083	0.083	0.000	0.000	0.000	0.000
111	A	254	GLY	0	0.044	0.011	14.099	0.405	0.405	0.000	0.000	0.000	0.000
112	A	255	LYS	1	0.863	0.930	15.205	-1.650	-1.650	0.000	0.000	0.000	0.000
113	A	256	ARG	1	0.916	0.930	15.884	-1.189	-1.189	0.000	0.000	0.000	0.000
114	A	257	LEU	0	-0.027	-0.010	14.329	-0.144	-0.144	0.000	0.000	0.000	0.000
115	A	258	ASP	-1	-0.802	-0.887	17.603	1.496	1.496	0.000	0.000	0.000	0.000
116	A	259	LYS	1	0.791	0.876	20.384	-1.406	-1.406	0.000	0.000	0.000	0.000
117	A	260	PHE	0	0.027	0.008	17.488	0.139	0.139	0.000	0.000	0.000	0.000
118	A	261	PRO	0	-0.074	-0.033	14.607	-0.111	-0.111	0.000	0.000	0.000	0.000
119	A	262	HIS	-1	-0.897	-0.932	17.176	1.343	1.343	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:140:GLU)