FMO DATABASE

FMODB ID: J2129

Calculation Name: 4ZC3-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 4ZC3

Chain ID: A

ChEMBL ID:

UniProt ID: P68928

Base Structure: X-ray

Registration Date: 2025-07-10

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-299460.46601
FMO2-HF: Nuclear repulsion	277600.290649
FMO2-HF: Total energy	-21860.175362
FMO2-MP2: Total energy	-21924.417681

3D Structure

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:6:LEU)

Summations of interaction energy for fragment #1(A:6:LEU)

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.
-6.183	-4.012	-0.001	-1.068	-1.106	0.004

Interaction energy analysis for fragmet #1(A:6:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.078 / q_NPA : 0.001

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].
4	A	7	SER	0	-0.063	0.054	4.550	-0.695	-0.465	-0.001	-0.115	-0.114	0.000
5	A	8	PRO	0	0.050	-0.069	3.853	-2.273	-0.844	-0.007	-0.862	-0.561	0.005
6	A	9	LYS	0	0.148	0.032	6.606	-0.181	-0.181	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.750	1.022	8.157	-0.637	-0.637	0.000	0.000	0.000	0.000
8	A	10	GLN	0	0.132	-0.075	4.785	-0.657	-0.607	-0.002	-0.005	-0.044	0.000
9	A	10	GLN	0	-0.130	0.064	3.990	2.273	2.421	0.001	-0.034	-0.116	0.000
10	A	11	GLU	0	0.020	-0.134	5.070	0.309	0.309	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.838	-0.749	3.909	-7.240	-7.024	0.008	-0.020	-0.204	-0.001
12	A	12	ARG	0	0.134	-0.070	6.115	0.007	0.007	0.000	0.000	0.000	0.000
13	A	12	ARG	1	0.755	1.011	9.948	0.225	0.225	0.000	0.000	0.000	0.000
14	A	13	PHE	0	0.124	-0.061	8.713	-0.087	-0.087	0.000	0.000	0.000	0.000
15	A	13	PHE	0	-0.135	0.062	8.469	0.091	0.091	0.000	0.000	0.000	0.000
16	A	14	ILE	0	0.096	-0.091	8.370	0.113	0.113	0.000	0.000	0.000	0.000
17	A	14	ILE	0	-0.109	0.080	5.807	0.006	0.006	0.000	0.000	0.000	0.000
18	A	15	GLU	0	0.084	-0.101	9.735	0.033	0.033	0.000	0.000	0.000	0.000
19	A	15	GLU	-1	-0.906	-0.779	10.616	-0.871	-0.871	0.000	0.000	0.000	0.000
20	A	16	GLU	0	0.091	-0.094	12.103	0.012	0.012	0.000	0.000	0.000	0.000
21	A	16	GLU	-1	-0.896	-0.790	13.267	-0.139	-0.139	0.000	0.000	0.000	0.000
22	A	17	TYR	0	0.134	-0.052	12.950	0.043	0.043	0.000	0.000	0.000	0.000
23	A	17	TYR	0	-0.096	0.077	12.990	0.028	0.028	0.000	0.000	0.000	0.000
24	A	18	PHE	0	-0.007	-0.091	14.338	0.053	0.053	0.000	0.000	0.000	0.000
25	A	18	PHE	0	-0.093	0.064	12.523	-0.014	-0.014	0.000	0.000	0.000	0.000
26	A	19	ILE	0	0.132	-0.067	16.059	0.018	0.018	0.000	0.000	0.000	0.000
27	A	19	ILE	0	-0.107	0.084	15.547	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	20	ASN	0	0.015	-0.044	17.598	0.006	0.006	0.000	0.000	0.000	0.000
29	A	20	ASN	0	-0.201	-0.030	17.023	0.027	0.027	0.000	0.000	0.000	0.000
30	A	21	ASP	0	0.158	-0.069	19.492	0.038	0.038	0.000	0.000	0.000	0.000
31	A	21	ASP	-1	-0.959	-0.862	22.343	-0.062	-0.062	0.000	0.000	0.000	0.000
32	A	22	MET	0	0.116	-0.078	17.529	0.022	0.022	0.000	0.000	0.000	0.000
33	A	22	MET	0	-0.116	0.089	17.109	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	23	ASN	0	0.167	-0.064	18.615	0.045	0.045	0.000	0.000	0.000	0.000
35	A	23	ASN	0	-0.115	0.074	20.328	0.027	0.027	0.000	0.000	0.000	0.000
36	A	24	ALA	0	0.130	-0.114	15.795	-0.028	-0.028	0.000	0.000	0.000	0.000
37	A	24	ALA	0	-0.045	0.123	15.455	0.012	0.012	0.000	0.000	0.000	0.000
38	A	25	THR	0	0.011	-0.070	15.952	0.058	0.058	0.000	0.000	0.000	0.000
39	A	25	THR	0	-0.028	0.053	20.010	0.011	0.011	0.000	0.000	0.000	0.000
40	A	26	LYS	0	0.063	-0.111	18.094	0.035	0.035	0.000	0.000	0.000	0.000
41	A	26	LYS	1	0.806	1.032	19.596	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	27	ALA	0	0.111	-0.079	14.808	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	27	ALA	0	-0.055	0.149	13.858	0.003	0.003	0.000	0.000	0.000	0.000
44	A	28	ALA	0	0.088	-0.108	13.527	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	28	ALA	0	-0.100	0.098	14.407	0.018	0.018	0.000	0.000	0.000	0.000
46	A	29	ILE	0	0.070	-0.094	14.591	0.051	0.051	0.000	0.000	0.000	0.000
47	A	29	ILE	0	-0.102	0.073	18.968	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	30	ALA	0	0.016	-0.122	16.740	0.023	0.023	0.000	0.000	0.000	0.000
49	A	30	ALA	0	-0.030	0.137	16.086	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	31	ALA	0	0.035	-0.131	12.070	-0.099	-0.099	0.000	0.000	0.000	0.000
51	A	31	ALA	0	-0.066	0.116	11.120	0.025	0.025	0.000	0.000	0.000	0.000
52	A	32	GLY	0	-0.004	-0.100	12.678	0.059	0.059	0.000	0.000	0.000	0.000
53	A	33	TYR	0	0.014	-0.017	14.683	0.065	0.065	0.000	0.000	0.000	0.000
54	A	33	TYR	0	-0.066	0.104	9.194	0.008	0.008	0.000	0.000	0.000	0.000
55	A	34	SER	0	0.109	-0.070	15.338	-0.075	-0.075	0.000	0.000	0.000	0.000
56	A	34	SER	0	-0.043	0.071	18.853	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	35	LYS	0	0.135	-0.080	18.878	0.034	0.034	0.000	0.000	0.000	0.000
58	A	35	LYS	1	0.907	1.092	21.380	-0.159	-0.159	0.000	0.000	0.000	0.000
59	A	36	ASN	0	0.052	-0.081	21.197	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	36	ASN	0	-0.090	0.077	23.095	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	37	SER	0	0.021	-0.077	18.922	-0.028	-0.028	0.000	0.000	0.000	0.000
62	A	37	SER	0	-0.002	0.071	18.199	0.014	0.014	0.000	0.000	0.000	0.000
63	A	38	ALA	0	0.057	-0.094	17.010	0.082	0.082	0.000	0.000	0.000	0.000
64	A	38	ALA	0	-0.053	0.118	18.038	-0.013	-0.013	0.000	0.000	0.000	0.000
65	A	39	SER	0	0.050	-0.059	17.163	0.036	0.036	0.000	0.000	0.000	0.000
66	A	39	SER	0	0.004	0.075	20.783	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	40	ALA	0	0.097	-0.114	18.414	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	40	ALA	0	-0.082	0.117	18.973	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	41	ILE	0	0.094	-0.088	14.623	0.037	0.037	0.000	0.000	0.000	0.000
70	A	41	ILE	0	-0.111	0.092	12.562	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	42	GLY	0	0.019	-0.103	13.373	0.102	0.102	0.000	0.000	0.000	0.000
72	A	43	ALA	0	0.095	0.000	14.053	0.019	0.019	0.000	0.000	0.000	0.000
73	A	43	ALA	0	-0.070	0.110	17.547	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	44	GLU	0	0.077	-0.119	13.942	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	44	GLU	-1	-0.952	-0.821	12.263	1.507	1.507	0.000	0.000	0.000	0.000
76	A	45	ASN	0	0.027	-0.094	9.973	0.140	0.140	0.000	0.000	0.000	0.000
77	A	45	ASN	0	-0.083	0.068	8.750	0.448	0.448	0.000	0.000	0.000	0.000
78	A	46	LEU	0	0.163	-0.070	10.097	0.119	0.119	0.000	0.000	0.000	0.000
79	A	46	LEU	0	-0.098	0.111	13.299	-0.017	-0.017	0.000	0.000	0.000	0.000
80	A	47	GLN	0	-0.021	-0.141	12.536	-0.092	-0.092	0.000	0.000	0.000	0.000
81	A	47	GLN	0	-0.065	0.108	14.586	0.022	0.022	0.000	0.000	0.000	0.000
82	A	48	LYS	0	0.140	-0.090	9.127	-0.140	-0.140	0.000	0.000	0.000	0.000
83	A	48	LYS	1	0.734	1.012	7.562	-2.178	-2.178	0.000	0.000	0.000	0.000
84	A	49	PRO	0	0.035	-0.077	9.668	-0.051	-0.051	0.000	0.000	0.000	0.000
85	A	50	ALA	0	0.137	0.009	5.832	-0.644	-0.644	0.000	0.000	0.000	0.000
86	A	50	ALA	0	-0.078	0.103	4.976	0.349	0.349	0.000	0.000	0.000	0.000
87	A	51	ILE	0	0.006	-0.134	6.564	-0.564	-0.564	0.000	0.000	0.000	0.000
88	A	51	ILE	0	-0.093	0.110	4.833	0.145	0.145	0.000	0.000	0.000	0.000
89	A	52	ARG	0	0.184	-0.073	7.345	-0.373	-0.373	0.000	0.000	0.000	0.000
90	A	52	ARG	1	0.734	0.989	11.431	-0.046	-0.046	0.000	0.000	0.000	0.000
91	A	53	ALA	0	0.119	-0.085	9.808	-0.106	-0.106	0.000	0.000	0.000	0.000
92	A	53	ALA	0	-0.086	0.103	8.916	-0.012	-0.012	0.000	0.000	0.000	0.000
93	A	54	ARG	0	0.043	-0.106	7.539	-0.128	-0.128	0.000	0.000	0.000	0.000
94	A	54	ARG	1	0.743	0.969	4.178	4.259	4.357	0.000	-0.032	-0.067	0.000
95	A	55	ILE	0	0.119	-0.069	8.913	-0.170	-0.170	0.000	0.000	0.000	0.000
96	A	55	ILE	0	-0.126	0.067	10.205	0.025	0.025	0.000	0.000	0.000	0.000
97	A	56	ASP	0	0.133	-0.082	11.767	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	56	ASP	-1	-0.887	-0.772	13.450	-0.067	-0.067	0.000	0.000	0.000	0.000
99	A	57	ALA	0	0.078	-0.110	11.606	0.095	0.095	0.000	0.000	0.000	0.000
100	A	57	ALA	0	-0.108	0.094	10.825	-0.057	-0.057	0.000	0.000	0.000	0.000
101	A	58	ARG	0	0.095	-0.085	12.379	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	58	ARG	1	0.742	0.977	11.525	0.803	0.803	0.000	0.000	0.000	0.000
103	A	59	LEU	0	0.053	-0.119	13.796	0.014	0.014	0.000	0.000	0.000	0.000
104	A	59	LEU	0	-0.092	0.084	16.038	0.017	0.017	0.000	0.000	0.000	0.000
105	A	60	LYS	0	0.107	-0.044	16.307	0.051	0.051	0.000	0.000	0.000	0.000
106	A	60	LYS	1	0.734	0.986	14.550	0.715	0.715	0.000	0.000	0.000	0.000
107	A	61	GLU	0	0.008	-0.147	16.273	0.059	0.059	0.000	0.000	0.000	0.000
108	A	61	GLU	-1	-0.947	-0.842	13.465	-0.939	-0.939	0.000	0.000	0.000	0.000
109	A	62	ILE	0	-0.084	-0.118	17.626	0.046	0.046	0.000	0.000	0.000	0.000
110	A	62	ILE	0	-0.002	0.016	17.562	0.007	0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:LEU)