FMO DATABASE

FMODB ID: KKV33

Calculation Name: 1A34-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A34

Chain ID: A

ChEMBL ID:

UniProt ID: P17574

Base Structure: X-ray

Registration Date: 2025-09-02

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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1203174.683304
FMO2-HF: Nuclear repulsion	1145961.340983
FMO2-HF: Total energy	-57213.342321
FMO2-MP2: Total energy	-57378.385891

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:13:THR)

Summations of interaction energy for fragment #1(A:13:THR)

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.
22.146	24.413	0.013	-1.032	-1.247	-0.003

Interaction energy analysis for fragmet #1(A:13:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.839 / q_NPA : 0.903

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	15	ASP	-1	-0.830	-0.935	3.368	-51.498	-49.353	0.015	-1.021	-1.139	-0.003
4	A	16	ASN	0	-0.053	-0.015	5.351	3.342	3.434	-0.001	-0.009	-0.081	0.000
9	A	21	THR	0	0.004	-0.003	5.589	-0.640	-0.610	-0.001	-0.002	-0.027	0.000
5	A	17	SER	0	-0.056	-0.015	5.632	3.780	3.780	0.000	0.000	0.000	0.000
6	A	18	ASN	0	0.012	0.005	7.679	-0.436	-0.436	0.000	0.000	0.000	0.000
7	A	19	VAL	0	-0.006	0.000	9.410	2.335	2.335	0.000	0.000	0.000	0.000
8	A	20	VAL	0	0.029	0.019	8.261	-3.931	-3.931	0.000	0.000	0.000	0.000
10	A	22	MET	0	-0.017	-0.008	7.929	-0.141	-0.141	0.000	0.000	0.000	0.000
11	A	23	ILE	0	0.015	0.006	5.467	-2.159	-2.159	0.000	0.000	0.000	0.000
12	A	24	ARG	1	0.940	0.963	7.512	28.674	28.674	0.000	0.000	0.000	0.000
13	A	25	ALA	0	0.013	0.013	9.833	-0.280	-0.280	0.000	0.000	0.000	0.000
14	A	26	GLY	0	0.044	0.022	11.737	0.895	0.895	0.000	0.000	0.000	0.000
15	A	27	SER	0	-0.017	-0.012	14.435	0.961	0.961	0.000	0.000	0.000	0.000
16	A	28	TYR	0	0.013	0.007	15.999	-1.115	-1.115	0.000	0.000	0.000	0.000
17	A	29	PRO	0	0.003	0.012	14.923	0.520	0.520	0.000	0.000	0.000	0.000
18	A	30	LYS	1	0.943	0.962	17.054	14.682	14.682	0.000	0.000	0.000	0.000
19	A	31	VAL	0	0.002	-0.001	17.581	-0.857	-0.857	0.000	0.000	0.000	0.000
20	A	32	ASN	0	0.020	-0.005	19.888	0.968	0.968	0.000	0.000	0.000	0.000
21	A	33	PRO	0	0.000	0.014	21.026	-0.638	-0.638	0.000	0.000	0.000	0.000
22	A	34	THR	0	0.014	0.009	22.927	0.049	0.049	0.000	0.000	0.000	0.000
23	A	35	PRO	0	-0.024	-0.001	20.259	0.275	0.275	0.000	0.000	0.000	0.000
24	A	36	THR	0	0.039	0.018	22.880	0.179	0.179	0.000	0.000	0.000	0.000
25	A	37	TRP	0	0.000	-0.007	21.725	-0.556	-0.556	0.000	0.000	0.000	0.000
26	A	38	VAL	0	-0.001	0.003	23.550	0.580	0.580	0.000	0.000	0.000	0.000
27	A	39	ARG	1	0.813	0.901	24.352	11.359	11.359	0.000	0.000	0.000	0.000
28	A	40	ALA	0	0.007	-0.002	26.954	0.318	0.318	0.000	0.000	0.000	0.000
29	A	41	ILE	0	-0.011	-0.002	29.341	-0.252	-0.252	0.000	0.000	0.000	0.000
30	A	42	PRO	0	-0.016	-0.004	31.113	0.259	0.259	0.000	0.000	0.000	0.000
31	A	43	PHE	0	0.039	0.003	34.234	-0.023	-0.023	0.000	0.000	0.000	0.000
32	A	44	GLU	-1	-0.907	-0.951	37.594	-8.089	-8.089	0.000	0.000	0.000	0.000
33	A	45	VAL	0	-0.003	0.010	41.268	0.044	0.044	0.000	0.000	0.000	0.000
34	A	46	SER	0	0.000	-0.011	44.454	0.077	0.077	0.000	0.000	0.000	0.000
35	A	47	VAL	0	-0.013	0.000	47.780	0.048	0.048	0.000	0.000	0.000	0.000
36	A	48	GLN	0	-0.001	-0.006	50.438	0.014	0.014	0.000	0.000	0.000	0.000
37	A	49	SER	0	0.060	0.035	54.280	-0.026	-0.026	0.000	0.000	0.000	0.000
38	A	50	GLY	0	0.017	0.003	56.215	0.089	0.089	0.000	0.000	0.000	0.000
39	A	51	ILE	0	-0.043	-0.022	54.319	0.041	0.041	0.000	0.000	0.000	0.000
40	A	52	ALA	0	-0.025	-0.008	51.801	-0.082	-0.082	0.000	0.000	0.000	0.000
41	A	53	PHE	0	0.010	0.001	45.290	0.044	0.044	0.000	0.000	0.000	0.000
42	A	54	LYS	1	0.893	0.936	47.881	6.183	6.183	0.000	0.000	0.000	0.000
43	A	55	VAL	0	0.013	0.003	41.477	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	56	PRO	0	0.038	0.032	43.308	-0.092	-0.092	0.000	0.000	0.000	0.000
45	A	57	VAL	0	0.024	-0.008	37.851	-0.163	-0.163	0.000	0.000	0.000	0.000
46	A	58	GLY	0	0.014	0.006	38.298	-0.233	-0.233	0.000	0.000	0.000	0.000
47	A	59	SER	0	-0.061	-0.028	38.497	-0.079	-0.079	0.000	0.000	0.000	0.000
48	A	60	LEU	0	-0.027	-0.012	34.256	-0.193	-0.193	0.000	0.000	0.000	0.000
49	A	61	PHE	0	-0.024	0.012	33.255	-0.341	-0.341	0.000	0.000	0.000	0.000
50	A	62	SER	0	0.033	0.005	33.073	0.217	0.217	0.000	0.000	0.000	0.000
51	A	63	ALA	0	0.076	0.052	31.373	-0.328	-0.328	0.000	0.000	0.000	0.000
52	A	64	ASN	0	-0.050	-0.024	30.759	-0.364	-0.364	0.000	0.000	0.000	0.000
53	A	65	PHE	0	-0.029	-0.005	29.801	-0.252	-0.252	0.000	0.000	0.000	0.000
54	A	66	ARG	1	0.948	0.971	24.529	11.827	11.827	0.000	0.000	0.000	0.000
55	A	67	THR	0	-0.004	-0.030	27.439	-0.347	-0.347	0.000	0.000	0.000	0.000
56	A	68	ASP	-1	-0.870	-0.942	30.020	-9.854	-9.854	0.000	0.000	0.000	0.000
57	A	69	SER	0	0.009	0.011	28.428	0.114	0.114	0.000	0.000	0.000	0.000
58	A	70	PHE	0	-0.084	-0.024	25.490	-0.090	-0.090	0.000	0.000	0.000	0.000
59	A	71	THR	0	0.006	0.001	31.536	0.328	0.328	0.000	0.000	0.000	0.000
60	A	72	SER	0	-0.021	-0.001	33.384	0.409	0.409	0.000	0.000	0.000	0.000
61	A	73	VAL	0	0.004	-0.001	31.989	-0.366	-0.366	0.000	0.000	0.000	0.000
62	A	74	THR	0	0.015	0.030	32.173	0.387	0.387	0.000	0.000	0.000	0.000
63	A	75	VAL	0	0.003	-0.004	32.625	-0.320	-0.320	0.000	0.000	0.000	0.000
64	A	76	MET	0	-0.053	-0.026	28.129	0.015	0.015	0.000	0.000	0.000	0.000
65	A	77	SER	0	-0.022	-0.026	33.642	0.097	0.097	0.000	0.000	0.000	0.000
66	A	78	VAL	0	0.028	0.037	35.284	-0.182	-0.182	0.000	0.000	0.000	0.000
67	A	79	ARG	1	0.930	0.970	31.547	9.602	9.602	0.000	0.000	0.000	0.000
68	A	80	ALA	0	0.048	0.027	38.459	-0.078	-0.078	0.000	0.000	0.000	0.000
69	A	81	TRP	0	0.007	-0.009	35.782	-0.022	-0.022	0.000	0.000	0.000	0.000
70	A	82	THR	0	0.016	0.014	42.468	-0.046	-0.046	0.000	0.000	0.000	0.000
71	A	83	GLN	0	0.053	0.022	40.505	-0.168	-0.168	0.000	0.000	0.000	0.000
72	A	84	LEU	0	-0.043	-0.011	44.564	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	85	THR	0	0.051	0.016	48.038	-0.049	-0.049	0.000	0.000	0.000	0.000
74	A	86	PRO	0	0.002	-0.011	50.687	0.017	0.017	0.000	0.000	0.000	0.000
75	A	87	PRO	0	-0.017	-0.003	53.299	0.030	0.030	0.000	0.000	0.000	0.000
76	A	88	VAL	0	0.037	0.018	57.034	-0.034	-0.034	0.000	0.000	0.000	0.000
77	A	89	ASN	0	-0.036	-0.030	59.352	0.075	0.075	0.000	0.000	0.000	0.000
78	A	90	GLU	-1	-0.863	-0.905	56.292	-5.607	-5.607	0.000	0.000	0.000	0.000
79	A	91	TYR	0	0.002	0.009	52.705	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	92	SER	0	-0.001	-0.018	49.226	0.013	0.013	0.000	0.000	0.000	0.000
81	A	93	PHE	0	0.006	0.000	50.214	-0.028	-0.028	0.000	0.000	0.000	0.000
82	A	94	VAL	0	0.005	0.008	45.143	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	95	ARG	1	0.830	0.904	48.315	5.996	5.996	0.000	0.000	0.000	0.000
84	A	96	LEU	0	-0.025	-0.019	41.904	-0.086	-0.086	0.000	0.000	0.000	0.000
85	A	97	LYS	1	0.929	0.968	46.173	6.211	6.211	0.000	0.000	0.000	0.000
86	A	98	PRO	0	-0.035	-0.013	43.703	-0.045	-0.045	0.000	0.000	0.000	0.000
87	A	99	LEU	0	-0.041	-0.005	44.590	0.194	0.194	0.000	0.000	0.000	0.000
88	A	100	PHE	0	-0.002	-0.017	41.436	-0.289	-0.289	0.000	0.000	0.000	0.000
89	A	101	LYS	1	0.820	0.892	40.880	7.807	7.807	0.000	0.000	0.000	0.000
90	A	102	THR	0	-0.030	-0.013	45.388	0.095	0.095	0.000	0.000	0.000	0.000
91	A	103	GLY	0	0.013	0.008	47.707	0.131	0.131	0.000	0.000	0.000	0.000
92	A	104	ASP	-1	-0.896	-0.946	48.537	-6.658	-6.658	0.000	0.000	0.000	0.000
93	A	105	SER	0	-0.025	-0.022	47.468	0.048	0.048	0.000	0.000	0.000	0.000
94	A	106	THR	0	-0.030	-0.022	49.462	0.082	0.082	0.000	0.000	0.000	0.000
95	A	107	GLU	-1	-0.909	-0.937	48.163	-6.426	-6.426	0.000	0.000	0.000	0.000
96	A	108	GLU	-1	-0.858	-0.950	49.127	-6.322	-6.322	0.000	0.000	0.000	0.000
97	A	109	PHE	0	-0.029	-0.013	45.252	0.041	0.041	0.000	0.000	0.000	0.000
98	A	110	GLU	-1	-0.746	-0.844	47.374	-6.106	-6.106	0.000	0.000	0.000	0.000
99	A	111	GLY	0	-0.005	0.012	46.660	-0.068	-0.068	0.000	0.000	0.000	0.000
100	A	112	ARG	1	0.858	0.883	47.702	6.019	6.019	0.000	0.000	0.000	0.000
101	A	113	ALA	0	-0.005	0.012	48.259	-0.117	-0.117	0.000	0.000	0.000	0.000
102	A	114	SER	0	0.015	-0.004	48.987	0.144	0.144	0.000	0.000	0.000	0.000
103	A	115	ASN	0	0.013	-0.007	49.331	0.166	0.166	0.000	0.000	0.000	0.000
104	A	116	ILE	0	0.065	0.028	50.413	-0.113	-0.113	0.000	0.000	0.000	0.000
105	A	117	ASN	0	-0.048	-0.007	49.660	0.005	0.005	0.000	0.000	0.000	0.000
106	A	118	THR	0	-0.067	-0.038	44.935	-0.168	-0.168	0.000	0.000	0.000	0.000
107	A	119	ARG	1	0.878	0.937	41.152	7.742	7.742	0.000	0.000	0.000	0.000
108	A	120	ALA	0	-0.006	0.014	45.483	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	121	SER	0	-0.011	-0.020	41.422	-0.120	-0.120	0.000	0.000	0.000	0.000
110	A	122	VAL	0	-0.010	0.006	42.679	0.070	0.070	0.000	0.000	0.000	0.000
111	A	123	GLY	0	0.018	-0.008	39.761	-0.174	-0.174	0.000	0.000	0.000	0.000
112	A	124	TYR	0	0.029	0.032	39.773	0.136	0.136	0.000	0.000	0.000	0.000
113	A	125	ARG	1	0.964	0.969	34.291	8.628	8.628	0.000	0.000	0.000	0.000
114	A	126	ILE	0	0.045	0.034	36.965	0.218	0.218	0.000	0.000	0.000	0.000
115	A	127	PRO	0	0.003	0.005	36.497	-0.361	-0.361	0.000	0.000	0.000	0.000
116	A	128	THR	0	0.032	-0.014	33.834	0.032	0.032	0.000	0.000	0.000	0.000
117	A	129	ASN	0	0.052	0.023	36.286	-0.194	-0.194	0.000	0.000	0.000	0.000
118	A	130	LEU	0	0.013	0.027	39.185	0.127	0.127	0.000	0.000	0.000	0.000
119	A	131	ARG	1	0.795	0.913	31.255	9.472	9.472	0.000	0.000	0.000	0.000
120	A	132	GLN	0	-0.003	-0.014	35.827	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	133	ASN	0	0.014	0.009	33.542	-0.149	-0.149	0.000	0.000	0.000	0.000
122	A	134	THR	0	-0.071	-0.029	36.772	0.314	0.314	0.000	0.000	0.000	0.000
123	A	135	VAL	0	0.069	0.019	37.135	-0.259	-0.259	0.000	0.000	0.000	0.000
124	A	136	ALA	0	0.021	-0.006	39.261	0.146	0.146	0.000	0.000	0.000	0.000
125	A	137	ALA	0	0.001	0.002	40.529	0.090	0.090	0.000	0.000	0.000	0.000
126	A	138	ASP	-1	-0.763	-0.847	41.643	-7.407	-7.407	0.000	0.000	0.000	0.000
127	A	139	ASN	0	-0.012	-0.026	43.427	-0.038	-0.038	0.000	0.000	0.000	0.000
128	A	140	VAL	0	0.001	0.008	39.249	-0.044	-0.044	0.000	0.000	0.000	0.000
129	A	141	CYS	0	-0.028	-0.018	42.188	-0.005	-0.005	0.000	0.000	0.000	0.000
130	A	142	GLU	-1	-0.770	-0.855	44.803	-6.156	-6.156	0.000	0.000	0.000	0.000
131	A	143	VAL	0	0.019	0.010	44.754	-0.068	-0.068	0.000	0.000	0.000	0.000
132	A	144	ARG	1	0.899	0.958	47.694	6.069	6.069	0.000	0.000	0.000	0.000
133	A	145	SER	0	0.000	-0.024	49.173	-0.121	-0.121	0.000	0.000	0.000	0.000
134	A	146	ASN	0	0.006	-0.007	51.295	-0.045	-0.045	0.000	0.000	0.000	0.000
135	A	147	CYS	0	-0.064	0.019	49.383	0.058	0.058	0.000	0.000	0.000	0.000
136	A	148	ARG	1	0.932	0.944	50.641	5.982	5.982	0.000	0.000	0.000	0.000
137	A	149	GLN	0	0.001	0.005	45.178	-0.130	-0.130	0.000	0.000	0.000	0.000
138	A	150	VAL	0	0.000	0.003	43.232	0.036	0.036	0.000	0.000	0.000	0.000
139	A	151	ALA	0	0.031	0.033	39.235	-0.044	-0.044	0.000	0.000	0.000	0.000
140	A	152	LEU	0	-0.010	-0.013	38.730	0.059	0.059	0.000	0.000	0.000	0.000
141	A	153	VAL	0	-0.013	-0.017	32.553	-0.215	-0.215	0.000	0.000	0.000	0.000
142	A	154	ILE	0	0.004	0.009	34.432	0.060	0.060	0.000	0.000	0.000	0.000
143	A	155	SER	0	-0.011	-0.005	30.370	-0.392	-0.392	0.000	0.000	0.000	0.000
144	A	156	CYS	0	-0.055	-0.029	30.055	0.274	0.274	0.000	0.000	0.000	0.000
145	A	157	CYS	0	-0.002	-0.001	28.069	-0.595	-0.595	0.000	0.000	0.000	0.000
146	A	158	PHE	0	0.024	0.009	27.808	0.360	0.360	0.000	0.000	0.000	0.000
147	A	159	ASN	-1	-0.822	-0.926	27.690	-10.572	-10.572	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:13:THR)