FMO DATABASE

FMODB ID: RQR88

Calculation Name: 2C3B-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2C3B

Chain ID: A

ChEMBL ID:

UniProt ID: Q4WHY9

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1298177.409284
FMO2-HF: Nuclear repulsion	1240111.737013
FMO2-HF: Total energy	-58065.672271
FMO2-MP2: Total energy	-58234.473465

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:SER)

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

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.
-59.123	-50.502	6.58	-7.976	-7.224	-0.065

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.819 / q_NPA : 0.897

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	SER	0	0.024	0.049	3.565	-0.967	2.038	-0.018	-1.417	-1.571	-0.004
4	A	3	GLN	0	0.017	0.010	4.422	-7.672	-7.594	-0.001	-0.028	-0.048	0.000
30	A	29	ASP	-1	-0.834	-0.918	2.338	-100.598	-97.297	5.969	-5.435	-3.834	-0.049
31	A	30	LYS	1	0.923	0.955	4.312	30.715	30.849	-0.001	-0.030	-0.103	0.000
41	A	40	ARG	1	0.787	0.839	2.714	68.751	70.795	0.632	-1.063	-1.613	-0.012
148	A	170	GLU	-1	-0.818	-0.909	4.869	-56.507	-56.448	-0.001	-0.003	-0.055	0.000
5	A	4	VAL	0	-0.001	-0.003	6.061	-1.867	-1.867	0.000	0.000	0.000	0.000
6	A	5	PHE	0	-0.055	-0.022	8.449	2.304	2.304	0.000	0.000	0.000	0.000
7	A	6	PHE	0	0.049	0.008	12.255	-0.187	-0.187	0.000	0.000	0.000	0.000
8	A	7	ASP	-1	-0.801	-0.871	15.355	-16.655	-16.655	0.000	0.000	0.000	0.000
9	A	8	VAL	0	-0.011	-0.022	18.561	0.147	0.147	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.908	-0.954	21.233	-11.156	-11.156	0.000	0.000	0.000	0.000
11	A	10	TYR	0	0.002	-0.054	23.670	-0.095	-0.095	0.000	0.000	0.000	0.000
12	A	11	ALA	0	0.064	0.042	27.579	0.070	0.070	0.000	0.000	0.000	0.000
13	A	12	PRO	0	-0.004	-0.012	29.672	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	13	VAL	0	-0.014	-0.018	31.550	0.297	0.297	0.000	0.000	0.000	0.000
15	A	14	GLY	0	-0.026	-0.010	34.292	0.043	0.043	0.000	0.000	0.000	0.000
16	A	15	THR	0	-0.074	-0.034	33.909	0.234	0.234	0.000	0.000	0.000	0.000
17	A	16	ALA	0	-0.019	-0.012	36.091	-0.083	-0.083	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.862	-0.907	34.300	-8.609	-8.609	0.000	0.000	0.000	0.000
19	A	18	THR	0	-0.026	-0.023	29.408	-0.100	-0.100	0.000	0.000	0.000	0.000
20	A	19	LYS	1	0.824	0.891	26.153	11.687	11.687	0.000	0.000	0.000	0.000
21	A	20	VAL	0	0.029	0.005	22.045	-0.195	-0.195	0.000	0.000	0.000	0.000
22	A	21	GLY	0	-0.034	-0.011	22.618	0.237	0.237	0.000	0.000	0.000	0.000
23	A	22	ARG	1	0.795	0.867	15.441	18.196	18.196	0.000	0.000	0.000	0.000
24	A	23	ILE	0	0.007	0.002	15.594	0.560	0.560	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.013	0.001	11.709	-1.075	-1.075	0.000	0.000	0.000	0.000
26	A	25	PHE	0	-0.006	-0.006	10.036	1.413	1.413	0.000	0.000	0.000	0.000
27	A	26	ASN	0	0.006	0.013	8.787	-4.466	-4.466	0.000	0.000	0.000	0.000
28	A	27	LEU	0	-0.005	-0.007	5.375	2.081	2.081	0.000	0.000	0.000	0.000
29	A	28	PHE	0	0.007	0.004	6.065	-4.297	-4.297	0.000	0.000	0.000	0.000
32	A	31	ASP	-1	-0.876	-0.925	6.721	-25.560	-25.560	0.000	0.000	0.000	0.000
33	A	32	VAL	0	-0.013	-0.006	8.567	2.602	2.602	0.000	0.000	0.000	0.000
34	A	33	PRO	0	0.019	0.016	6.276	-0.891	-0.891	0.000	0.000	0.000	0.000
35	A	34	LYS	1	0.925	0.950	7.134	19.374	19.374	0.000	0.000	0.000	0.000
36	A	35	THR	0	0.024	0.021	9.817	0.302	0.302	0.000	0.000	0.000	0.000
37	A	36	ALA	0	0.062	0.041	5.677	0.900	0.900	0.000	0.000	0.000	0.000
38	A	37	LYS	1	0.862	0.947	5.607	29.181	29.181	0.000	0.000	0.000	0.000
39	A	38	ASN	0	0.026	0.008	6.470	1.876	1.876	0.000	0.000	0.000	0.000
40	A	39	PHE	0	0.025	0.022	8.456	1.577	1.577	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.922	-0.984	7.569	-27.305	-27.305	0.000	0.000	0.000	0.000
43	A	42	LEU	0	-0.023	-0.006	10.060	2.344	2.344	0.000	0.000	0.000	0.000
44	A	43	CYS	0	-0.096	-0.011	9.787	1.307	1.307	0.000	0.000	0.000	0.000
45	A	44	LYS	1	0.831	0.899	6.002	43.825	43.825	0.000	0.000	0.000	0.000
46	A	45	ARG	1	0.901	0.978	12.162	21.144	21.144	0.000	0.000	0.000	0.000
47	A	46	PRO	0	0.004	0.004	15.554	0.146	0.146	0.000	0.000	0.000	0.000
48	A	47	ALA	0	0.003	0.003	19.047	-0.318	-0.318	0.000	0.000	0.000	0.000
49	A	48	GLY	0	-0.001	0.006	20.992	0.497	0.497	0.000	0.000	0.000	0.000
50	A	49	GLU	-1	-0.920	-0.961	18.971	-15.297	-15.297	0.000	0.000	0.000	0.000
51	A	50	GLY	0	-0.022	-0.033	16.288	-0.840	-0.840	0.000	0.000	0.000	0.000
52	A	51	TYR	0	-0.020	-0.002	12.212	0.475	0.475	0.000	0.000	0.000	0.000
53	A	52	ARG	1	0.935	1.000	16.852	17.583	17.583	0.000	0.000	0.000	0.000
54	A	53	GLU	-1	-0.827	-0.926	18.634	-12.718	-12.718	0.000	0.000	0.000	0.000
55	A	54	SER	0	-0.037	-0.006	19.267	0.567	0.567	0.000	0.000	0.000	0.000
56	A	55	THR	0	-0.006	-0.022	21.848	0.162	0.162	0.000	0.000	0.000	0.000
57	A	56	PHE	0	0.004	-0.003	18.846	-0.341	-0.341	0.000	0.000	0.000	0.000
58	A	57	HIS	0	-0.052	-0.019	23.638	1.150	1.150	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.874	0.939	25.282	12.309	12.309	0.000	0.000	0.000	0.000
60	A	59	ILE	0	0.025	0.019	25.239	-0.504	-0.504	0.000	0.000	0.000	0.000
61	A	60	ILE	0	-0.091	-0.037	27.168	0.606	0.606	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.005	0.004	28.023	-0.318	-0.318	0.000	0.000	0.000	0.000
63	A	62	ASN	0	-0.038	-0.020	28.190	-0.036	-0.036	0.000	0.000	0.000	0.000
64	A	63	PHE	0	-0.024	0.000	26.746	0.045	0.045	0.000	0.000	0.000	0.000
65	A	64	MET	0	-0.009	0.011	23.620	-0.423	-0.423	0.000	0.000	0.000	0.000
66	A	65	ILE	0	0.068	0.025	21.193	0.549	0.549	0.000	0.000	0.000	0.000
67	A	66	GLN	0	-0.085	-0.050	21.066	-0.053	-0.053	0.000	0.000	0.000	0.000
68	A	67	GLY	0	0.023	-0.004	20.420	0.697	0.697	0.000	0.000	0.000	0.000
69	A	68	GLY	0	-0.042	-0.010	18.592	-0.646	-0.646	0.000	0.000	0.000	0.000
70	A	69	ASP	-2	-1.731	-1.838	19.505	-26.728	-26.728	0.000	0.000	0.000	0.000
71	A	92	SER	0	0.047	0.017	35.555	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	93	ARG	1	1.042	1.017	31.992	9.853	9.853	0.000	0.000	0.000	0.000
73	A	94	LYS	1	0.947	0.967	36.423	7.214	7.214	0.000	0.000	0.000	0.000
74	A	95	HIS	0	-0.004	-0.005	39.290	0.270	0.270	0.000	0.000	0.000	0.000
75	A	96	ASP	-1	-0.705	-0.837	33.725	-9.415	-9.415	0.000	0.000	0.000	0.000
76	A	97	LYS	1	0.915	0.942	36.792	8.323	8.323	0.000	0.000	0.000	0.000
77	A	98	LYS	1	0.886	0.949	38.517	7.290	7.290	0.000	0.000	0.000	0.000
78	A	99	GLY	0	0.034	0.022	39.961	0.168	0.168	0.000	0.000	0.000	0.000
79	A	100	ILE	0	-0.057	0.001	35.431	0.188	0.188	0.000	0.000	0.000	0.000
80	A	101	LEU	0	0.020	0.006	37.517	-0.087	-0.087	0.000	0.000	0.000	0.000
81	A	102	SER	0	-0.047	-0.029	33.933	-0.132	-0.132	0.000	0.000	0.000	0.000
82	A	103	MET	0	0.000	0.041	34.687	0.110	0.110	0.000	0.000	0.000	0.000
83	A	104	ALA	0	0.033	-0.007	29.984	-0.256	-0.256	0.000	0.000	0.000	0.000
84	A	105	ASN	0	-0.063	-0.043	27.739	-0.102	-0.102	0.000	0.000	0.000	0.000
85	A	106	ALA	0	0.038	0.031	29.629	0.084	0.084	0.000	0.000	0.000	0.000
86	A	107	GLY	0	0.029	0.038	32.109	0.230	0.230	0.000	0.000	0.000	0.000
87	A	108	PRO	0	0.013	-0.007	35.147	0.096	0.096	0.000	0.000	0.000	0.000
88	A	109	ASN	0	-0.042	-0.021	38.209	0.257	0.257	0.000	0.000	0.000	0.000
89	A	110	THR	0	0.018	-0.019	37.710	-0.293	-0.293	0.000	0.000	0.000	0.000
90	A	111	ASN	0	-0.029	-0.033	39.025	0.159	0.159	0.000	0.000	0.000	0.000
91	A	112	GLY	0	0.025	0.012	39.575	-0.176	-0.176	0.000	0.000	0.000	0.000
92	A	113	SER	0	-0.006	-0.002	37.769	0.085	0.085	0.000	0.000	0.000	0.000
93	A	114	GLN	0	0.042	0.019	32.379	-0.240	-0.240	0.000	0.000	0.000	0.000
94	A	115	PHE	0	0.009	0.012	36.915	0.191	0.191	0.000	0.000	0.000	0.000
95	A	116	PHE	0	-0.018	0.009	31.560	-0.165	-0.165	0.000	0.000	0.000	0.000
96	A	117	ILE	0	0.030	0.015	35.481	0.116	0.116	0.000	0.000	0.000	0.000
97	A	118	THR	0	-0.013	-0.001	32.645	-0.208	-0.208	0.000	0.000	0.000	0.000
98	A	119	THR	0	0.017	0.012	36.008	0.090	0.090	0.000	0.000	0.000	0.000
99	A	120	ALA	0	-0.005	-0.017	32.880	0.081	0.081	0.000	0.000	0.000	0.000
100	A	121	VAL	0	-0.071	-0.035	30.687	0.012	0.012	0.000	0.000	0.000	0.000
101	A	122	THR	0	0.023	0.013	30.000	-0.308	-0.308	0.000	0.000	0.000	0.000
102	A	123	SER	0	-0.037	-0.043	29.572	-0.305	-0.305	0.000	0.000	0.000	0.000
103	A	124	TRP	0	-0.046	-0.032	22.897	-0.064	-0.064	0.000	0.000	0.000	0.000
104	A	125	LEU	0	-0.020	0.002	23.779	-0.608	-0.608	0.000	0.000	0.000	0.000
105	A	126	ASP	-1	-0.832	-0.924	24.771	-12.463	-12.463	0.000	0.000	0.000	0.000
106	A	127	GLY	0	-0.011	-0.005	24.170	0.216	0.216	0.000	0.000	0.000	0.000
107	A	128	LYS	1	0.891	0.944	22.442	11.424	11.424	0.000	0.000	0.000	0.000
108	A	129	HIS	0	-0.044	-0.017	19.006	-1.081	-1.081	0.000	0.000	0.000	0.000
109	A	130	VAL	0	0.001	-0.001	13.555	-0.184	-0.184	0.000	0.000	0.000	0.000
110	A	131	VAL	0	0.020	0.005	13.719	-0.905	-0.905	0.000	0.000	0.000	0.000
111	A	132	PHE	0	-0.001	-0.019	9.383	-0.629	-0.629	0.000	0.000	0.000	0.000
112	A	133	GLY	0	0.023	0.011	9.046	-4.443	-4.443	0.000	0.000	0.000	0.000
113	A	134	GLU	-1	-0.895	-0.931	10.941	-20.087	-20.087	0.000	0.000	0.000	0.000
114	A	135	VAL	0	-0.018	-0.020	12.714	-1.476	-1.476	0.000	0.000	0.000	0.000
115	A	136	ALA	0	-0.016	-0.005	12.351	0.515	0.515	0.000	0.000	0.000	0.000
116	A	137	ASP	-1	-0.794	-0.864	14.316	-17.263	-17.263	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.784	-0.896	17.811	-13.161	-13.161	0.000	0.000	0.000	0.000
118	A	139	LYS	1	0.936	0.981	20.599	14.170	14.170	0.000	0.000	0.000	0.000
119	A	140	SER	0	-0.029	-0.048	16.836	0.363	0.363	0.000	0.000	0.000	0.000
120	A	141	TYR	0	-0.017	-0.002	19.054	0.363	0.363	0.000	0.000	0.000	0.000
121	A	142	SER	0	-0.005	-0.032	20.984	0.653	0.653	0.000	0.000	0.000	0.000
122	A	143	VAL	0	-0.053	-0.011	21.078	0.548	0.548	0.000	0.000	0.000	0.000
123	A	144	VAL	0	0.016	0.006	19.248	0.312	0.312	0.000	0.000	0.000	0.000
124	A	145	LYS	1	0.802	0.894	22.357	12.438	12.438	0.000	0.000	0.000	0.000
125	A	146	GLU	-1	-0.818	-0.860	25.911	-11.017	-11.017	0.000	0.000	0.000	0.000
126	A	147	ILE	0	-0.004	-0.002	22.206	0.397	0.397	0.000	0.000	0.000	0.000
127	A	148	GLU	-1	-0.793	-0.906	24.540	-12.147	-12.147	0.000	0.000	0.000	0.000
128	A	149	ALA	0	-0.012	-0.001	26.929	0.420	0.420	0.000	0.000	0.000	0.000
129	A	150	LEU	0	-0.003	0.009	27.481	0.495	0.495	0.000	0.000	0.000	0.000
130	A	151	GLY	0	0.031	0.025	29.908	0.190	0.190	0.000	0.000	0.000	0.000
131	A	152	SER	0	-0.026	-0.035	30.699	0.492	0.492	0.000	0.000	0.000	0.000
132	A	153	SER	0	0.064	0.017	32.306	-0.260	-0.260	0.000	0.000	0.000	0.000
133	A	154	SER	0	-0.076	-0.045	34.090	0.014	0.014	0.000	0.000	0.000	0.000
134	A	155	GLY	0	0.022	0.014	29.935	-0.060	-0.060	0.000	0.000	0.000	0.000
135	A	156	SER	0	-0.044	-0.009	29.983	-0.332	-0.332	0.000	0.000	0.000	0.000
136	A	157	VAL	0	0.036	0.027	28.378	0.086	0.086	0.000	0.000	0.000	0.000
137	A	158	ARG	1	0.844	0.903	31.494	9.394	9.394	0.000	0.000	0.000	0.000
138	A	159	SER	0	-0.001	0.019	31.525	0.331	0.331	0.000	0.000	0.000	0.000
139	A	160	ASN	0	0.003	-0.006	33.202	-0.083	-0.083	0.000	0.000	0.000	0.000
140	A	161	THR	0	0.009	0.017	29.077	-0.052	-0.052	0.000	0.000	0.000	0.000
141	A	162	ARG	1	0.837	0.912	27.377	10.665	10.665	0.000	0.000	0.000	0.000
142	A	163	PRO	0	0.002	0.000	24.397	-0.135	-0.135	0.000	0.000	0.000	0.000
143	A	164	LYS	1	0.892	0.944	23.393	11.840	11.840	0.000	0.000	0.000	0.000
144	A	165	ILE	0	-0.012	0.009	16.793	-0.051	-0.051	0.000	0.000	0.000	0.000
145	A	166	VAL	0	0.033	0.022	20.077	-0.129	-0.129	0.000	0.000	0.000	0.000
146	A	167	ASN	0	-0.019	-0.027	16.639	-0.152	-0.152	0.000	0.000	0.000	0.000
147	A	169	GLY	0	0.024	0.014	11.150	0.725	0.725	0.000	0.000	0.000	0.000
149	A	171	LEU	-1	-0.882	-0.930	8.201	-30.947	-30.947	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)