FMO DATABASE

FMODB ID: Z92JN

Calculation Name: 1MUP-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-(sec-butyl)thiazole | cadmium ion

Ligand 3-letter code: TZL | CD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1MUP

Chain ID: A

ChEMBL ID:

UniProt ID: P02762

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	156
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1640428.816622
FMO2-HF: Nuclear repulsion	1576264.702423
FMO2-HF: Total energy	-64164.114199
FMO2-MP2: Total energy	-64349.694387

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:5:GLU)

Summations of interaction energy for fragment #1(A:5: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.
-160.472	-152.979	24.733	-16.247	-15.977	-0.022

Interaction energy analysis for fragmet #1(A:5:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.079 / q_NPA : -0.046

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	7	ALA	0	-0.012	-0.001	3.234	8.572	10.769	0.088	-0.962	-1.324	-0.003
4	A	8	SER	0	0.018	0.007	4.953	-2.721	-2.718	-0.001	-0.005	0.003	0.000
9	A	13	ASN	0	0.010	-0.001	4.298	-4.489	-4.252	-0.001	-0.034	-0.202	0.000
10	A	14	PHE	0	0.019	0.024	5.171	6.145	6.198	-0.001	-0.002	-0.050	0.000
14	A	18	LYS	1	0.860	0.927	1.794	-64.285	-66.781	11.549	-5.019	-4.034	0.066
96	A	100	ASP	-1	-0.802	-0.903	2.406	-29.902	-28.584	0.404	-0.620	-1.101	-0.003
97	A	101	TYR	0	-0.013	0.001	1.875	-33.931	-32.348	10.722	-6.082	-6.222	-0.041
98	A	102	ASP	-1	-0.897	-0.959	2.398	-49.578	-45.055	1.974	-3.522	-2.975	-0.041
99	A	103	ASN	0	-0.045	-0.019	5.121	7.138	7.213	-0.001	-0.001	-0.072	0.000
5	A	9	SER	0	-0.005	-0.017	8.766	1.593	1.593	0.000	0.000	0.000	0.000
6	A	10	THR	0	-0.012	0.000	10.929	0.495	0.495	0.000	0.000	0.000	0.000
7	A	11	GLY	0	-0.016	0.000	9.303	0.003	0.003	0.000	0.000	0.000	0.000
8	A	12	ARG	1	0.912	0.939	10.304	-4.176	-4.176	0.000	0.000	0.000	0.000
11	A	15	ASN	0	0.010	0.002	5.402	-3.598	-3.598	0.000	0.000	0.000	0.000
12	A	16	VAL	0	0.049	0.011	7.040	-1.342	-1.342	0.000	0.000	0.000	0.000
13	A	17	GLU	-1	-0.893	-0.945	9.373	3.811	3.811	0.000	0.000	0.000	0.000
15	A	19	ILE	0	-0.018	-0.012	7.910	-2.942	-2.942	0.000	0.000	0.000	0.000
16	A	20	ASN	0	0.032	0.029	9.928	-0.877	-0.877	0.000	0.000	0.000	0.000
17	A	21	GLY	0	0.042	0.037	11.865	-0.745	-0.745	0.000	0.000	0.000	0.000
18	A	22	GLU	-1	-0.875	-0.941	14.471	-2.868	-2.868	0.000	0.000	0.000	0.000
19	A	23	TRP	0	-0.075	-0.038	7.573	-1.092	-1.092	0.000	0.000	0.000	0.000
20	A	24	HIS	1	0.871	0.951	14.375	3.613	3.613	0.000	0.000	0.000	0.000
21	A	25	THR	0	0.019	-0.004	15.707	-0.435	-0.435	0.000	0.000	0.000	0.000
22	A	26	ILE	0	-0.055	0.002	14.546	0.126	0.126	0.000	0.000	0.000	0.000
23	A	27	ILE	0	0.016	0.003	17.779	0.183	0.183	0.000	0.000	0.000	0.000
24	A	28	LEU	0	-0.017	0.013	18.866	-0.092	-0.092	0.000	0.000	0.000	0.000
25	A	29	ALA	0	0.026	0.015	21.524	0.035	0.035	0.000	0.000	0.000	0.000
26	A	30	SER	0	-0.010	-0.014	23.169	0.066	0.066	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.821	-0.915	25.884	-0.745	-0.745	0.000	0.000	0.000	0.000
28	A	32	LYS	1	0.807	0.914	28.777	0.508	0.508	0.000	0.000	0.000	0.000
29	A	33	ARG	1	0.847	0.889	29.527	1.022	1.022	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.878	-0.937	30.336	-0.633	-0.633	0.000	0.000	0.000	0.000
31	A	35	LYS	1	0.880	0.952	29.186	0.537	0.537	0.000	0.000	0.000	0.000
32	A	36	ILE	0	0.005	0.000	24.260	-0.015	-0.015	0.000	0.000	0.000	0.000
33	A	37	GLU	-1	-0.813	-0.888	27.648	-1.007	-1.007	0.000	0.000	0.000	0.000
34	A	38	ASP	-1	-0.872	-0.930	30.398	-1.058	-1.058	0.000	0.000	0.000	0.000
35	A	39	ASN	0	-0.002	-0.012	31.960	0.004	0.004	0.000	0.000	0.000	0.000
36	A	40	GLY	0	0.033	0.034	30.996	0.072	0.072	0.000	0.000	0.000	0.000
37	A	41	ASN	0	-0.068	-0.054	30.199	-0.085	-0.085	0.000	0.000	0.000	0.000
38	A	42	PHE	0	0.008	0.011	25.261	0.024	0.024	0.000	0.000	0.000	0.000
39	A	43	ARG	1	0.834	0.938	24.863	1.064	1.064	0.000	0.000	0.000	0.000
40	A	44	LEU	0	-0.032	-0.004	23.215	0.060	0.060	0.000	0.000	0.000	0.000
41	A	45	PHE	0	0.015	0.011	21.589	-0.216	-0.216	0.000	0.000	0.000	0.000
42	A	46	LEU	0	-0.030	-0.020	15.528	0.142	0.142	0.000	0.000	0.000	0.000
43	A	47	GLU	-1	-0.812	-0.847	18.999	-1.367	-1.367	0.000	0.000	0.000	0.000
44	A	48	GLN	0	-0.020	-0.028	16.468	-0.115	-0.115	0.000	0.000	0.000	0.000
45	A	49	ILE	0	-0.022	0.010	13.132	0.243	0.243	0.000	0.000	0.000	0.000
46	A	50	HIS	0	-0.007	0.001	15.829	-0.122	-0.122	0.000	0.000	0.000	0.000
47	A	51	VAL	0	-0.031	-0.020	12.922	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	52	LEU	0	-0.009	-0.002	16.279	0.016	0.016	0.000	0.000	0.000	0.000
49	A	53	GLU	-1	-0.909	-0.963	17.607	1.954	1.954	0.000	0.000	0.000	0.000
50	A	54	ASN	0	-0.072	-0.043	18.161	0.325	0.325	0.000	0.000	0.000	0.000
51	A	55	SER	0	-0.007	-0.012	19.354	-0.092	-0.092	0.000	0.000	0.000	0.000
52	A	56	LEU	0	-0.022	-0.009	14.915	0.138	0.138	0.000	0.000	0.000	0.000
53	A	57	VAL	0	-0.015	0.000	18.997	-0.139	-0.139	0.000	0.000	0.000	0.000
54	A	58	LEU	0	-0.006	0.009	17.736	-0.124	-0.124	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.954	0.974	20.178	0.458	0.458	0.000	0.000	0.000	0.000
56	A	60	PHE	0	0.068	0.008	20.460	-0.218	-0.218	0.000	0.000	0.000	0.000
57	A	61	HIS	1	0.865	0.935	23.077	1.490	1.490	0.000	0.000	0.000	0.000
58	A	62	THR	0	0.002	-0.003	25.334	-0.117	-0.117	0.000	0.000	0.000	0.000
59	A	63	VAL	0	0.035	-0.001	27.319	0.001	0.001	0.000	0.000	0.000	0.000
60	A	64	ARG	1	0.778	0.890	30.006	0.832	0.832	0.000	0.000	0.000	0.000
61	A	65	ASP	-1	-0.884	-0.941	33.650	-0.728	-0.728	0.000	0.000	0.000	0.000
62	A	66	GLU	-1	-0.955	-0.982	32.060	-0.953	-0.953	0.000	0.000	0.000	0.000
63	A	67	GLU	-1	-0.968	-0.954	32.264	-0.646	-0.646	0.000	0.000	0.000	0.000
64	A	161	CYS	-1	-0.903	-0.946	24.732	-1.266	-1.266	0.000	0.000	0.000	0.000
65	A	69	SER	0	-0.004	-0.002	30.300	0.067	0.067	0.000	0.000	0.000	0.000
66	A	70	GLU	0	-0.062	-0.065	25.351	-0.026	-0.026	0.000	0.000	0.000	0.000
67	A	71	LEU	0	0.010	0.004	26.086	0.086	0.086	0.000	0.000	0.000	0.000
68	A	72	SER	0	-0.060	-0.042	24.901	-0.055	-0.055	0.000	0.000	0.000	0.000
69	A	73	MET	0	-0.033	0.004	23.577	0.055	0.055	0.000	0.000	0.000	0.000
70	A	74	VAL	0	0.006	0.000	23.610	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	75	ALA	0	0.008	0.012	20.817	-0.048	-0.048	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.816	-0.886	21.112	0.780	0.780	0.000	0.000	0.000	0.000
73	A	77	LYS	1	0.872	0.937	16.782	-2.163	-2.163	0.000	0.000	0.000	0.000
74	A	78	THR	0	-0.017	-0.026	20.572	0.016	0.016	0.000	0.000	0.000	0.000
75	A	79	GLU	-1	-0.950	-0.982	21.084	1.226	1.226	0.000	0.000	0.000	0.000
76	A	80	LYS	1	0.815	0.921	17.935	-0.745	-0.745	0.000	0.000	0.000	0.000
77	A	81	ALA	0	0.007	-0.017	15.386	0.046	0.046	0.000	0.000	0.000	0.000
78	A	82	GLY	0	0.000	-0.021	13.933	-0.216	-0.216	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.843	-0.867	14.680	0.277	0.277	0.000	0.000	0.000	0.000
80	A	84	TYR	0	0.001	0.005	14.293	0.314	0.314	0.000	0.000	0.000	0.000
81	A	85	SER	0	-0.009	-0.001	20.266	-0.158	-0.158	0.000	0.000	0.000	0.000
82	A	86	VAL	0	0.031	0.000	23.604	0.041	0.041	0.000	0.000	0.000	0.000
83	A	87	THR	0	0.003	0.008	25.919	-0.049	-0.049	0.000	0.000	0.000	0.000
84	A	88	TYR	0	-0.047	-0.038	27.516	0.004	0.004	0.000	0.000	0.000	0.000
85	A	89	ASP	-1	-0.777	-0.892	29.595	-0.428	-0.428	0.000	0.000	0.000	0.000
86	A	90	GLY	0	0.036	0.023	31.913	-0.018	-0.018	0.000	0.000	0.000	0.000
87	A	91	PHE	0	-0.008	0.003	27.117	0.016	0.016	0.000	0.000	0.000	0.000
88	A	92	ASN	0	-0.011	-0.014	25.013	-0.128	-0.128	0.000	0.000	0.000	0.000
89	A	93	THR	0	0.048	0.028	22.678	0.084	0.084	0.000	0.000	0.000	0.000
90	A	94	PHE	0	-0.003	-0.004	17.035	-0.160	-0.160	0.000	0.000	0.000	0.000
91	A	95	THR	0	0.000	-0.003	15.258	0.289	0.289	0.000	0.000	0.000	0.000
92	A	96	ILE	0	0.030	0.011	10.284	-0.315	-0.315	0.000	0.000	0.000	0.000
93	A	97	PRO	0	0.000	0.014	11.341	0.319	0.319	0.000	0.000	0.000	0.000
94	A	98	LYS	1	0.821	0.904	7.518	4.511	4.511	0.000	0.000	0.000	0.000
95	A	99	THR	0	0.079	0.055	5.995	-0.960	-0.960	0.000	0.000	0.000	0.000
100	A	104	PHE	0	0.007	-0.006	6.037	3.721	3.721	0.000	0.000	0.000	0.000
101	A	105	LEU	0	-0.007	-0.004	7.181	-1.970	-1.970	0.000	0.000	0.000	0.000
102	A	106	MET	0	-0.033	-0.003	9.797	0.910	0.910	0.000	0.000	0.000	0.000
103	A	107	ALA	0	-0.004	-0.011	12.639	0.360	0.360	0.000	0.000	0.000	0.000
104	A	108	HIS	0	-0.047	-0.037	15.264	-0.058	-0.058	0.000	0.000	0.000	0.000
105	A	109	LEU	0	0.012	0.005	18.436	0.225	0.225	0.000	0.000	0.000	0.000
106	A	110	ILE	0	0.008	0.009	21.622	-0.082	-0.082	0.000	0.000	0.000	0.000
107	A	111	ASN	0	-0.044	-0.027	25.088	0.095	0.095	0.000	0.000	0.000	0.000
108	A	112	GLU	-1	-0.902	-0.959	28.163	0.032	0.032	0.000	0.000	0.000	0.000
109	A	113	LYS	1	0.850	0.911	31.182	0.302	0.302	0.000	0.000	0.000	0.000
110	A	114	ASP	-1	-0.893	-0.949	34.553	-0.158	-0.158	0.000	0.000	0.000	0.000
111	A	115	GLY	0	-0.043	-0.017	36.739	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.896	-0.934	34.099	-0.409	-0.409	0.000	0.000	0.000	0.000
113	A	117	THR	0	-0.023	-0.029	29.749	0.043	0.043	0.000	0.000	0.000	0.000
114	A	118	PHE	0	-0.037	-0.016	26.939	-0.028	-0.028	0.000	0.000	0.000	0.000
115	A	119	GLN	0	0.051	0.035	23.242	-0.011	-0.011	0.000	0.000	0.000	0.000
116	A	120	LEU	0	-0.007	-0.002	21.130	-0.053	-0.053	0.000	0.000	0.000	0.000
117	A	121	MET	0	-0.038	-0.015	17.559	0.079	0.079	0.000	0.000	0.000	0.000
118	A	122	GLY	0	0.028	0.013	17.643	0.082	0.082	0.000	0.000	0.000	0.000
119	A	123	LEU	0	-0.038	-0.004	12.186	-0.316	-0.316	0.000	0.000	0.000	0.000
120	A	124	TYR	0	0.021	-0.003	12.832	0.492	0.492	0.000	0.000	0.000	0.000
121	A	125	GLY	0	0.041	0.011	11.248	-1.165	-1.165	0.000	0.000	0.000	0.000
122	A	126	ARG	1	0.774	0.867	8.115	6.424	6.424	0.000	0.000	0.000	0.000
123	A	127	GLU	-1	-0.875	-0.929	11.631	-3.489	-3.489	0.000	0.000	0.000	0.000
124	A	128	PRO	0	-0.045	-0.044	14.425	-0.069	-0.069	0.000	0.000	0.000	0.000
125	A	129	ASP	-1	-0.761	-0.882	16.222	-3.062	-3.062	0.000	0.000	0.000	0.000
126	A	130	LEU	0	-0.037	-0.013	10.948	-0.677	-0.677	0.000	0.000	0.000	0.000
127	A	131	SER	0	0.032	0.011	12.947	0.481	0.481	0.000	0.000	0.000	0.000
128	A	132	SER	0	0.053	0.002	14.644	-0.083	-0.083	0.000	0.000	0.000	0.000
129	A	133	ASP	-1	-0.889	-0.933	13.359	-4.338	-4.338	0.000	0.000	0.000	0.000
130	A	134	ILE	0	-0.033	-0.015	9.362	-0.010	-0.010	0.000	0.000	0.000	0.000
131	A	135	LYS	1	0.806	0.892	12.787	3.646	3.646	0.000	0.000	0.000	0.000
132	A	136	GLU	-1	-0.776	-0.849	16.264	-2.063	-2.063	0.000	0.000	0.000	0.000
133	A	137	ARG	1	0.793	0.862	7.967	8.570	8.570	0.000	0.000	0.000	0.000
134	A	138	PHE	0	0.013	-0.010	14.656	0.203	0.203	0.000	0.000	0.000	0.000
135	A	139	ALA	0	0.024	0.020	15.908	0.396	0.396	0.000	0.000	0.000	0.000
136	A	140	GLN	0	-0.004	-0.014	18.127	0.267	0.267	0.000	0.000	0.000	0.000
137	A	141	LEU	0	-0.005	0.008	14.484	0.255	0.255	0.000	0.000	0.000	0.000
138	A	142	CYS	0	-0.036	-0.021	18.229	0.320	0.320	0.000	0.000	0.000	0.000
139	A	143	GLU	-1	-0.875	-0.924	21.025	-1.222	-1.222	0.000	0.000	0.000	0.000
140	A	144	GLU	-1	-1.003	-0.998	19.130	-1.210	-1.210	0.000	0.000	0.000	0.000
141	A	145	HIS	1	0.779	0.877	18.309	1.372	1.372	0.000	0.000	0.000	0.000
142	A	146	GLY	0	0.007	0.011	23.263	0.107	0.107	0.000	0.000	0.000	0.000
143	A	147	ILE	0	-0.045	-0.016	22.651	0.043	0.043	0.000	0.000	0.000	0.000
144	A	148	LEU	0	0.033	0.021	25.177	-0.119	-0.119	0.000	0.000	0.000	0.000
145	A	149	ARG	1	0.845	0.859	22.189	1.898	1.898	0.000	0.000	0.000	0.000
146	A	150	GLU	-1	-0.938	-0.958	26.501	-0.990	-0.990	0.000	0.000	0.000	0.000
147	A	151	ASN	0	-0.031	-0.016	27.282	0.046	0.046	0.000	0.000	0.000	0.000
148	A	152	ILE	0	-0.028	-0.013	21.727	-0.055	-0.055	0.000	0.000	0.000	0.000
149	A	153	ILE	0	-0.005	0.001	23.902	0.065	0.065	0.000	0.000	0.000	0.000
150	A	154	ASP	-1	-0.800	-0.870	20.957	-2.897	-2.897	0.000	0.000	0.000	0.000
151	A	155	LEU	0	0.021	-0.007	21.397	0.192	0.192	0.000	0.000	0.000	0.000
152	A	156	SER	0	-0.012	-0.025	19.311	0.126	0.126	0.000	0.000	0.000	0.000
153	A	157	ASN	0	-0.095	-0.053	20.616	0.038	0.038	0.000	0.000	0.000	0.000
154	A	158	ALA	0	0.005	0.006	23.923	0.146	0.146	0.000	0.000	0.000	0.000
155	A	159	ASN	0	-0.082	-0.052	19.535	0.238	0.238	0.000	0.000	0.000	0.000
156	A	160	ARG	1	0.792	0.890	21.442	2.289	2.289	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLU)