FMO DATABASE

FMODB ID: NZQJQ

Calculation Name: 1USZ-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | chloride ion

Ligand 3-letter code: SO4 | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1USZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q57254

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	-1158905.727318
FMO2-HF: Nuclear repulsion	1106151.321836
FMO2-HF: Total energy	-52754.405483
FMO2-MP2: Total energy	-52908.855674

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
-110.991	-106.133	17.177	-13.026	-9.011	-0.122

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.799 / q_NPA : 0.893

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	2	PHE	0	0.032	0.013	3.825	2.570	3.550	-0.015	-0.386	-0.580	-0.001
97	A	96	ASP	-1	-0.904	-0.970	2.759	-84.120	-80.883	0.206	-2.115	-1.328	-0.024
102	A	101	TYR	0	0.005	-0.022	4.760	1.259	1.339	-0.001	-0.005	-0.074	0.000
138	A	137	TRP	0	0.016	0.007	2.146	-13.927	-12.914	6.618	-3.422	-4.209	-0.048
139	A	138	ALA	0	-0.022	-0.001	4.294	6.245	6.342	-0.001	-0.049	-0.047	0.000
140	A	139	LYS	0	0.071	0.048	2.029	-29.598	-30.147	10.370	-7.049	-2.773	-0.049
4	A	3	THR	0	-0.021	-0.004	6.814	2.461	2.461	0.000	0.000	0.000	0.000
5	A	4	PRO	0	-0.008	-0.011	9.807	1.241	1.241	0.000	0.000	0.000	0.000
6	A	5	SER	0	-0.030	-0.023	13.056	0.941	0.941	0.000	0.000	0.000	0.000
7	A	6	GLY	0	0.014	0.006	15.076	0.132	0.132	0.000	0.000	0.000	0.000
8	A	7	THR	0	-0.003	0.009	17.697	-0.073	-0.073	0.000	0.000	0.000	0.000
9	A	8	THR	0	0.014	-0.003	18.746	-0.809	-0.809	0.000	0.000	0.000	0.000
10	A	9	GLY	0	0.009	0.017	20.081	0.903	0.903	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.005	-0.025	21.155	-0.280	-0.280	0.000	0.000	0.000	0.000
12	A	11	THR	0	-0.003	0.006	22.332	0.437	0.437	0.000	0.000	0.000	0.000
13	A	12	LYS	1	0.939	0.968	24.449	11.185	11.185	0.000	0.000	0.000	0.000
14	A	13	LEU	0	-0.001	-0.005	27.599	0.167	0.167	0.000	0.000	0.000	0.000
15	A	14	THR	0	0.004	0.007	29.943	-0.123	-0.123	0.000	0.000	0.000	0.000
16	A	15	VAL	0	-0.010	0.007	30.977	0.160	0.160	0.000	0.000	0.000	0.000
17	A	16	THR	0	-0.024	-0.022	33.809	0.250	0.250	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.769	-0.894	37.613	-8.192	-8.192	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.871	-0.950	40.437	-7.880	-7.880	0.000	0.000	0.000	0.000
20	A	19	CYS	0	-0.037	-0.011	42.422	0.125	0.125	0.000	0.000	0.000	0.000
21	A	20	GLN	0	0.004	0.013	38.020	0.021	0.021	0.000	0.000	0.000	0.000
22	A	21	VAL	0	0.011	-0.002	42.298	0.153	0.153	0.000	0.000	0.000	0.000
23	A	22	ARG	1	0.851	0.921	37.295	8.183	8.183	0.000	0.000	0.000	0.000
24	A	23	VAL	0	0.022	0.008	41.351	0.201	0.201	0.000	0.000	0.000	0.000
25	A	24	GLY	0	-0.013	0.000	40.911	-0.184	-0.184	0.000	0.000	0.000	0.000
26	A	25	ASP	-1	-0.872	-0.941	37.947	-8.141	-8.141	0.000	0.000	0.000	0.000
27	A	26	LEU	0	-0.056	-0.015	36.136	-0.092	-0.092	0.000	0.000	0.000	0.000
28	A	27	THR	0	0.015	0.002	33.526	-0.255	-0.255	0.000	0.000	0.000	0.000
29	A	28	VAL	0	-0.011	-0.005	29.916	0.284	0.284	0.000	0.000	0.000	0.000
30	A	29	ALA	0	0.033	0.023	32.995	-0.086	-0.086	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.874	0.936	31.352	9.548	9.548	0.000	0.000	0.000	0.000
32	A	31	THR	0	-0.020	0.010	34.862	-0.104	-0.104	0.000	0.000	0.000	0.000
33	A	32	ARG	1	0.881	0.923	34.978	8.286	8.286	0.000	0.000	0.000	0.000
34	A	33	GLY	0	0.046	0.022	35.118	-0.208	-0.208	0.000	0.000	0.000	0.000
35	A	34	GLN	0	-0.017	-0.010	34.778	-0.100	-0.100	0.000	0.000	0.000	0.000
36	A	35	LEU	0	-0.017	0.009	29.877	-0.271	-0.271	0.000	0.000	0.000	0.000
37	A	36	THR	0	0.028	-0.001	31.481	-0.016	-0.016	0.000	0.000	0.000	0.000
38	A	37	ASP	-1	-0.851	-0.935	26.915	-12.020	-12.020	0.000	0.000	0.000	0.000
39	A	38	ALA	0	-0.024	-0.012	26.435	0.333	0.333	0.000	0.000	0.000	0.000
40	A	39	ALA	0	-0.005	0.018	27.511	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	40	PRO	0	-0.018	-0.008	27.443	-0.434	-0.434	0.000	0.000	0.000	0.000
42	A	41	ILE	0	0.001	-0.003	25.837	0.410	0.410	0.000	0.000	0.000	0.000
43	A	42	GLY	0	0.006	0.004	26.211	0.464	0.464	0.000	0.000	0.000	0.000
44	A	43	PRO	0	-0.039	-0.019	24.667	-0.442	-0.442	0.000	0.000	0.000	0.000
45	A	44	VAL	0	0.022	0.008	20.494	0.168	0.168	0.000	0.000	0.000	0.000
46	A	45	THR	0	0.000	-0.002	22.249	-0.335	-0.335	0.000	0.000	0.000	0.000
47	A	46	VAL	0	-0.009	-0.006	17.481	-0.450	-0.450	0.000	0.000	0.000	0.000
48	A	47	GLN	0	-0.010	-0.022	20.510	0.821	0.821	0.000	0.000	0.000	0.000
49	A	48	ALA	0	-0.003	0.017	16.539	-0.193	-0.193	0.000	0.000	0.000	0.000
50	A	49	LEU	0	0.027	0.003	18.404	0.826	0.826	0.000	0.000	0.000	0.000
51	A	50	GLY	0	0.034	0.022	18.353	-0.634	-0.634	0.000	0.000	0.000	0.000
52	A	51	CYS	0	-0.034	-0.017	14.510	-0.887	-0.887	0.000	0.000	0.000	0.000
53	A	52	ASN	0	-0.001	-0.009	15.330	-0.761	-0.761	0.000	0.000	0.000	0.000
54	A	53	ALA	0	0.036	0.029	15.019	0.223	0.223	0.000	0.000	0.000	0.000
55	A	54	ARG	1	0.906	0.954	10.510	21.742	21.742	0.000	0.000	0.000	0.000
56	A	55	GLN	0	-0.022	-0.005	7.779	-0.113	-0.113	0.000	0.000	0.000	0.000
57	A	56	VAL	0	0.030	0.017	9.626	-1.837	-1.837	0.000	0.000	0.000	0.000
58	A	57	ALA	0	-0.003	-0.008	8.705	-1.704	-1.704	0.000	0.000	0.000	0.000
59	A	58	LEU	0	0.002	0.008	10.763	1.840	1.840	0.000	0.000	0.000	0.000
60	A	59	LYS	1	0.862	0.944	9.632	25.605	25.605	0.000	0.000	0.000	0.000
61	A	60	ALA	0	0.033	0.029	12.058	1.822	1.822	0.000	0.000	0.000	0.000
62	A	61	ASP	-1	-0.808	-0.905	13.788	-19.043	-19.043	0.000	0.000	0.000	0.000
63	A	62	THR	0	-0.047	-0.047	14.884	-0.921	-0.921	0.000	0.000	0.000	0.000
64	A	63	ASP	-1	-0.895	-0.934	16.039	-15.974	-15.974	0.000	0.000	0.000	0.000
65	A	64	ASN	0	-0.010	-0.018	17.440	0.739	0.739	0.000	0.000	0.000	0.000
66	A	65	PHE	0	-0.039	-0.006	11.269	-0.790	-0.790	0.000	0.000	0.000	0.000
67	A	66	GLU	-1	-0.904	-0.960	15.010	-16.529	-16.529	0.000	0.000	0.000	0.000
68	A	67	GLN	0	-0.031	-0.023	13.867	-1.013	-1.013	0.000	0.000	0.000	0.000
69	A	68	GLY	0	-0.007	0.011	11.997	0.356	0.356	0.000	0.000	0.000	0.000
70	A	69	LYS	1	0.823	0.892	12.987	16.687	16.687	0.000	0.000	0.000	0.000
71	A	70	PHE	0	0.017	0.005	11.788	-0.591	-0.591	0.000	0.000	0.000	0.000
72	A	71	PHE	0	0.013	-0.014	16.955	0.858	0.858	0.000	0.000	0.000	0.000
73	A	72	LEU	0	-0.009	0.006	20.359	-0.371	-0.371	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.008	0.007	22.601	0.276	0.276	0.000	0.000	0.000	0.000
75	A	74	SER	0	0.008	0.005	24.404	0.267	0.267	0.000	0.000	0.000	0.000
76	A	75	ASP	-1	-0.818	-0.908	27.662	-10.656	-10.656	0.000	0.000	0.000	0.000
77	A	76	ASN	0	-0.093	-0.063	29.841	-0.259	-0.259	0.000	0.000	0.000	0.000
78	A	77	ASN	0	-0.049	-0.028	25.817	-0.241	-0.241	0.000	0.000	0.000	0.000
79	A	78	ARG	1	0.926	0.972	26.175	9.801	9.801	0.000	0.000	0.000	0.000
80	A	79	ASP	-1	-0.849	-0.915	26.682	-10.660	-10.660	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.875	0.954	20.514	14.646	14.646	0.000	0.000	0.000	0.000
82	A	81	LEU	0	-0.002	0.012	24.692	0.425	0.425	0.000	0.000	0.000	0.000
83	A	82	TYR	0	0.001	-0.010	19.791	-0.337	-0.337	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.016	-0.016	19.812	0.646	0.646	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.065	-0.031	18.822	-1.602	-1.602	0.000	0.000	0.000	0.000
86	A	85	ILE	0	-0.004	0.001	15.404	0.802	0.802	0.000	0.000	0.000	0.000
87	A	86	ARG	1	0.922	0.961	17.147	12.858	12.858	0.000	0.000	0.000	0.000
88	A	87	PRO	0	0.015	0.016	17.126	0.628	0.628	0.000	0.000	0.000	0.000
89	A	88	MET	0	-0.041	-0.009	19.964	0.312	0.312	0.000	0.000	0.000	0.000
90	A	89	ASP	-1	-0.789	-0.856	20.666	-14.872	-14.872	0.000	0.000	0.000	0.000
91	A	90	ASN	0	-0.015	-0.024	22.029	-0.210	-0.210	0.000	0.000	0.000	0.000
92	A	91	SER	0	-0.089	-0.049	17.553	-0.848	-0.848	0.000	0.000	0.000	0.000
93	A	92	ALA	0	0.043	0.024	15.233	-0.073	-0.073	0.000	0.000	0.000	0.000
94	A	93	TRP	0	-0.015	-0.025	12.041	-1.227	-1.227	0.000	0.000	0.000	0.000
95	A	94	THR	0	-0.018	0.007	7.104	2.383	2.383	0.000	0.000	0.000	0.000
96	A	95	THR	0	0.002	0.002	9.039	-0.181	-0.181	0.000	0.000	0.000	0.000
98	A	97	ASN	0	0.019	0.002	6.147	3.171	3.171	0.000	0.000	0.000	0.000
99	A	98	GLY	0	0.064	0.029	7.899	0.535	0.535	0.000	0.000	0.000	0.000
100	A	99	VAL	0	-0.070	-0.037	6.549	2.445	2.445	0.000	0.000	0.000	0.000
101	A	100	PHE	0	0.031	0.018	8.396	-1.704	-1.704	0.000	0.000	0.000	0.000
103	A	102	LYS	1	0.925	0.993	9.561	19.733	19.733	0.000	0.000	0.000	0.000
104	A	103	ASN	0	-0.024	-0.037	9.939	-0.803	-0.803	0.000	0.000	0.000	0.000
105	A	104	ASP	-1	-0.879	-0.943	10.843	-21.265	-21.265	0.000	0.000	0.000	0.000
106	A	105	VAL	0	-0.065	-0.036	11.719	-0.387	-0.387	0.000	0.000	0.000	0.000
107	A	106	GLY	0	0.038	0.017	13.624	1.196	1.196	0.000	0.000	0.000	0.000
108	A	107	SER	0	-0.094	-0.044	16.141	-0.980	-0.980	0.000	0.000	0.000	0.000
109	A	108	TRP	0	-0.008	-0.017	17.015	0.494	0.494	0.000	0.000	0.000	0.000
110	A	109	GLY	0	0.037	0.009	18.911	-0.349	-0.349	0.000	0.000	0.000	0.000
111	A	110	GLY	0	0.015	0.020	21.309	0.262	0.262	0.000	0.000	0.000	0.000
112	A	111	THR	0	-0.071	-0.044	22.856	0.343	0.343	0.000	0.000	0.000	0.000
113	A	112	ILE	0	0.016	0.021	17.137	-0.203	-0.203	0.000	0.000	0.000	0.000
114	A	113	GLY	0	0.021	-0.003	20.746	0.651	0.651	0.000	0.000	0.000	0.000
115	A	114	ILE	0	-0.021	-0.005	20.013	-0.774	-0.774	0.000	0.000	0.000	0.000
116	A	115	TYR	0	0.008	-0.008	22.498	0.927	0.927	0.000	0.000	0.000	0.000
117	A	116	VAL	0	0.005	0.007	23.274	-0.627	-0.627	0.000	0.000	0.000	0.000
118	A	117	ASP	-1	-0.843	-0.889	21.001	-14.930	-14.930	0.000	0.000	0.000	0.000
119	A	118	GLY	0	0.063	0.033	23.910	0.018	0.018	0.000	0.000	0.000	0.000
120	A	119	GLN	0	-0.051	-0.031	26.948	0.265	0.265	0.000	0.000	0.000	0.000
121	A	120	GLN	0	0.004	0.004	25.041	-0.047	-0.047	0.000	0.000	0.000	0.000
122	A	121	THR	0	0.005	0.012	30.363	0.025	0.025	0.000	0.000	0.000	0.000
123	A	122	ASN	0	-0.019	-0.014	33.281	0.428	0.428	0.000	0.000	0.000	0.000
124	A	123	THR	0	-0.039	-0.023	29.826	-0.028	-0.028	0.000	0.000	0.000	0.000
125	A	124	PRO	0	0.003	0.009	31.354	0.300	0.300	0.000	0.000	0.000	0.000
126	A	125	PRO	0	-0.008	-0.011	33.242	-0.258	-0.258	0.000	0.000	0.000	0.000
127	A	126	GLY	0	0.033	0.027	33.479	0.045	0.045	0.000	0.000	0.000	0.000
128	A	127	ASN	0	-0.056	-0.032	31.425	0.105	0.105	0.000	0.000	0.000	0.000
129	A	128	TYR	0	-0.021	-0.019	26.697	-0.296	-0.296	0.000	0.000	0.000	0.000
130	A	129	THR	0	0.019	-0.010	23.649	0.255	0.255	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.010	0.014	17.639	-0.353	-0.353	0.000	0.000	0.000	0.000
132	A	131	THR	0	-0.043	-0.016	19.178	0.633	0.633	0.000	0.000	0.000	0.000
133	A	132	LEU	0	-0.013	-0.014	15.513	-1.134	-1.134	0.000	0.000	0.000	0.000
134	A	133	THR	0	0.032	0.022	15.196	1.365	1.365	0.000	0.000	0.000	0.000
135	A	134	GLY	0	0.008	0.014	14.277	-1.648	-1.648	0.000	0.000	0.000	0.000
136	A	135	GLY	0	0.005	-0.009	12.405	0.260	0.260	0.000	0.000	0.000	0.000
137	A	136	TYR	0	0.013	0.003	8.744	1.328	1.328	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:0:GLY)