FMO DATABASE

FMODB ID: 9Q5Y2

Calculation Name: 2CJ4-A-Xray549

Preferred Name:

Target Type:

Ligand Name: sulfate ion | acetate ion

Ligand 3-letter code: SO4 | ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CJ4

Chain ID: A

ChEMBL ID:

UniProt ID: O49908

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1273165.53136
FMO2-HF: Nuclear repulsion	1217454.506339
FMO2-HF: Total energy	-55711.025022
FMO2-MP2: Total energy	-55871.959487

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:4:ASN)

Summations of interaction energy for fragment #1(A:4:ASN)

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.
-46.762	-38.686	4.941	-4.957	-8.057	-0.025

Interaction energy analysis for fragmet #1(A:4:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.896 / q_NPA : 0.938

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	6	LEU	0	0.020	0.015	3.166	5.051	7.016	0.036	-0.757	-1.244	-0.001
4	A	7	VAL	0	-0.005	0.023	1.934	2.308	3.468	4.039	-2.116	-3.083	-0.022
5	A	8	GLU	-1	-0.874	-0.948	3.626	-45.631	-44.576	0.006	-0.391	-0.670	-0.001
22	A	25	LEU	0	-0.017	-0.015	2.887	-2.885	-1.625	0.236	-0.402	-1.093	0.000
27	A	30	SER	0	0.002	-0.005	4.888	-2.700	-2.732	-0.001	-0.016	0.050	0.000
28	A	31	ALA	0	-0.073	-0.030	2.716	-15.054	-12.765	0.622	-1.199	-1.712	0.000
29	A	32	THR	0	-0.060	-0.044	3.769	-8.625	-8.246	0.003	-0.076	-0.305	-0.001
6	A	9	THR	0	-0.059	-0.048	5.685	8.520	8.520	0.000	0.000	0.000	0.000
7	A	10	THR	0	0.018	0.008	6.513	5.599	5.599	0.000	0.000	0.000	0.000
8	A	11	CYS	0	-0.070	-0.100	7.377	2.037	2.037	0.000	0.000	0.000	0.000
9	A	12	LYS	1	0.894	0.951	9.356	27.683	27.683	0.000	0.000	0.000	0.000
10	A	13	ASN	0	-0.083	-0.031	11.461	3.479	3.479	0.000	0.000	0.000	0.000
11	A	14	THR	0	-0.001	-0.010	11.931	1.467	1.467	0.000	0.000	0.000	0.000
12	A	15	PRO	0	-0.008	-0.015	14.564	0.132	0.132	0.000	0.000	0.000	0.000
13	A	16	ASN	0	-0.018	-0.008	15.258	-0.115	-0.115	0.000	0.000	0.000	0.000
14	A	17	TYR	0	0.025	0.022	8.744	-1.295	-1.295	0.000	0.000	0.000	0.000
15	A	18	GLN	0	0.062	0.009	10.515	-3.069	-3.069	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.048	-0.003	11.861	-0.798	-0.798	0.000	0.000	0.000	0.000
17	A	20	CYS	-1	-0.706	-0.762	10.236	-29.194	-29.194	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.066	0.015	5.658	-2.260	-2.260	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.914	0.962	7.682	17.895	17.895	0.000	0.000	0.000	0.000
20	A	23	THR	0	-0.057	-0.032	10.348	0.863	0.863	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.009	0.000	6.835	-0.391	-0.391	0.000	0.000	0.000	0.000
23	A	26	SER	0	-0.087	-0.046	6.415	1.451	1.451	0.000	0.000	0.000	0.000
24	A	27	ASP	-1	-0.802	-0.881	8.467	-22.282	-22.282	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.950	0.968	7.110	20.668	20.668	0.000	0.000	0.000	0.000
26	A	29	ARG	1	0.781	0.860	7.274	19.544	19.544	0.000	0.000	0.000	0.000
30	A	33	GLY	0	0.048	0.045	5.599	4.406	4.406	0.000	0.000	0.000	0.000
31	A	34	ASP	-1	-0.829	-0.895	6.159	-29.918	-29.918	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.029	-0.011	8.159	-1.137	-1.137	0.000	0.000	0.000	0.000
33	A	36	THR	0	0.065	0.043	9.319	0.842	0.842	0.000	0.000	0.000	0.000
34	A	37	THR	0	-0.035	-0.035	8.869	1.297	1.297	0.000	0.000	0.000	0.000
35	A	38	LEU	0	-0.065	-0.038	4.853	-0.193	-0.193	0.000	0.000	0.000	0.000
36	A	39	ALA	0	0.033	0.018	8.958	1.276	1.276	0.000	0.000	0.000	0.000
37	A	40	LEU	0	0.024	0.011	12.586	1.235	1.235	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.056	-0.014	8.600	0.770	0.770	0.000	0.000	0.000	0.000
39	A	42	MET	0	-0.004	0.013	11.764	1.541	1.541	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.023	0.008	13.915	1.319	1.319	0.000	0.000	0.000	0.000
41	A	44	ASP	-1	-0.810	-0.890	15.727	-16.724	-16.724	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.039	-0.016	15.037	0.998	0.998	0.000	0.000	0.000	0.000
43	A	46	ILE	0	-0.007	-0.004	17.141	1.019	1.019	0.000	0.000	0.000	0.000
44	A	47	LYS	1	0.960	0.973	19.759	13.579	13.579	0.000	0.000	0.000	0.000
45	A	48	ALA	0	-0.014	-0.007	19.517	0.803	0.803	0.000	0.000	0.000	0.000
46	A	49	LYS	1	0.881	0.938	20.174	15.021	15.021	0.000	0.000	0.000	0.000
47	A	50	ALA	0	0.071	0.035	22.680	0.664	0.664	0.000	0.000	0.000	0.000
48	A	51	ASN	0	-0.003	-0.001	24.843	0.329	0.329	0.000	0.000	0.000	0.000
49	A	52	GLN	0	0.036	0.024	23.983	0.038	0.038	0.000	0.000	0.000	0.000
50	A	53	ALA	0	0.013	0.017	26.738	0.491	0.491	0.000	0.000	0.000	0.000
51	A	54	ALA	0	0.038	0.018	28.757	0.462	0.462	0.000	0.000	0.000	0.000
52	A	55	VAL	0	-0.004	-0.002	29.915	0.449	0.449	0.000	0.000	0.000	0.000
53	A	56	THR	0	-0.073	-0.038	29.988	0.422	0.422	0.000	0.000	0.000	0.000
54	A	57	ILE	0	0.025	0.010	31.953	0.377	0.377	0.000	0.000	0.000	0.000
55	A	58	SER	0	-0.021	-0.010	34.704	0.417	0.417	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.983	0.997	32.727	9.649	9.649	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.012	0.002	35.144	0.262	0.262	0.000	0.000	0.000	0.000
58	A	61	ARG	1	0.899	0.947	38.539	8.238	8.238	0.000	0.000	0.000	0.000
59	A	62	HIS	0	-0.049	-0.023	39.755	0.338	0.338	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.056	-0.030	40.216	0.127	0.127	0.000	0.000	0.000	0.000
61	A	64	ASN	0	-0.042	-0.014	42.754	0.102	0.102	0.000	0.000	0.000	0.000
62	A	65	PRO	0	0.016	0.022	41.837	0.025	0.025	0.000	0.000	0.000	0.000
63	A	66	PRO	0	0.037	0.012	42.610	0.173	0.173	0.000	0.000	0.000	0.000
64	A	67	ALA	0	0.033	0.016	44.707	-0.112	-0.112	0.000	0.000	0.000	0.000
65	A	68	ALA	0	0.020	0.006	45.148	-0.038	-0.038	0.000	0.000	0.000	0.000
66	A	69	TRP	0	0.049	0.007	39.288	-0.149	-0.149	0.000	0.000	0.000	0.000
67	A	70	LYS	1	0.947	0.982	41.315	6.653	6.653	0.000	0.000	0.000	0.000
68	A	71	GLY	0	0.000	0.001	42.763	-0.043	-0.043	0.000	0.000	0.000	0.000
69	A	72	PRO	0	0.058	0.032	38.452	-0.114	-0.114	0.000	0.000	0.000	0.000
70	A	73	LEU	0	0.043	0.015	36.547	-0.225	-0.225	0.000	0.000	0.000	0.000
71	A	74	LYS	1	0.907	0.957	37.684	7.090	7.090	0.000	0.000	0.000	0.000
72	A	75	ASN	0	0.027	0.009	38.165	-0.040	-0.040	0.000	0.000	0.000	0.000
73	A	76	CYS	0	-0.069	-0.002	31.237	0.148	0.148	0.000	0.000	0.000	0.000
74	A	77	ALA	0	-0.037	-0.022	33.400	-0.252	-0.252	0.000	0.000	0.000	0.000
75	A	78	PHE	0	-0.046	-0.012	34.523	-0.097	-0.097	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.023	0.001	31.519	-0.136	-0.136	0.000	0.000	0.000	0.000
77	A	80	TYR	0	0.051	-0.014	26.433	-0.432	-0.432	0.000	0.000	0.000	0.000
78	A	81	LYS	1	0.941	0.977	29.693	8.409	8.409	0.000	0.000	0.000	0.000
79	A	82	VAL	0	0.045	0.045	30.258	-0.093	-0.093	0.000	0.000	0.000	0.000
80	A	83	ILE	0	0.018	0.023	25.006	-0.318	-0.318	0.000	0.000	0.000	0.000
81	A	84	LEU	0	-0.081	-0.050	25.540	-0.280	-0.280	0.000	0.000	0.000	0.000
82	A	85	THR	0	-0.138	-0.092	27.559	0.025	0.025	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.013	0.019	29.034	0.156	0.156	0.000	0.000	0.000	0.000
84	A	87	SER	0	0.026	0.004	25.872	-0.217	-0.217	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.014	-0.002	21.157	-0.443	-0.443	0.000	0.000	0.000	0.000
86	A	89	PRO	0	-0.033	-0.026	22.380	-0.498	-0.498	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.889	-0.931	24.015	-11.561	-11.561	0.000	0.000	0.000	0.000
88	A	91	ALA	0	0.023	0.004	19.741	-0.255	-0.255	0.000	0.000	0.000	0.000
89	A	92	ILE	0	-0.009	-0.005	19.270	-0.602	-0.602	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.881	-0.934	20.316	-11.693	-11.693	0.000	0.000	0.000	0.000
91	A	94	ALA	0	-0.019	-0.012	21.737	-0.059	-0.059	0.000	0.000	0.000	0.000
92	A	95	LEU	0	-0.011	-0.012	15.489	-0.287	-0.287	0.000	0.000	0.000	0.000
93	A	96	THR	0	-0.091	-0.053	17.764	-0.698	-0.698	0.000	0.000	0.000	0.000
94	A	97	LYS	1	0.803	0.902	19.422	11.586	11.586	0.000	0.000	0.000	0.000
95	A	98	GLY	0	-0.004	0.008	21.948	0.691	0.691	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.849	-0.914	22.544	-12.628	-12.628	0.000	0.000	0.000	0.000
97	A	100	PRO	0	0.046	0.015	18.766	0.130	0.130	0.000	0.000	0.000	0.000
98	A	101	LYS	1	0.857	0.920	20.752	11.354	11.354	0.000	0.000	0.000	0.000
99	A	102	PHE	0	0.031	0.003	23.509	0.131	0.131	0.000	0.000	0.000	0.000
100	A	103	ALA	0	0.002	0.006	19.201	0.024	0.024	0.000	0.000	0.000	0.000
101	A	104	GLU	-1	-0.840	-0.923	19.974	-15.065	-15.065	0.000	0.000	0.000	0.000
102	A	105	ASP	-1	-0.836	-0.909	21.755	-11.247	-11.247	0.000	0.000	0.000	0.000
103	A	106	GLY	0	0.053	0.029	24.053	0.247	0.247	0.000	0.000	0.000	0.000
104	A	107	MET	0	-0.056	-0.028	18.640	-0.363	-0.363	0.000	0.000	0.000	0.000
105	A	108	VAL	0	-0.032	-0.020	21.973	0.043	0.043	0.000	0.000	0.000	0.000
106	A	109	GLY	0	0.026	0.020	24.799	0.316	0.316	0.000	0.000	0.000	0.000
107	A	110	SER	0	-0.012	-0.037	22.391	0.196	0.196	0.000	0.000	0.000	0.000
108	A	111	SER	0	-0.060	-0.056	23.211	0.273	0.273	0.000	0.000	0.000	0.000
109	A	112	GLY	0	0.021	0.023	24.873	0.230	0.230	0.000	0.000	0.000	0.000
110	A	113	ASP	-1	-0.839	-0.936	28.581	-9.986	-9.986	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.034	-0.011	26.250	0.312	0.312	0.000	0.000	0.000	0.000
112	A	115	GLN	0	-0.083	-0.046	28.221	-0.231	-0.231	0.000	0.000	0.000	0.000
113	A	116	GLU	-1	-0.830	-0.920	29.646	-8.547	-8.547	0.000	0.000	0.000	0.000
114	A	118	GLU	-1	-0.729	-0.819	30.434	-9.770	-9.770	0.000	0.000	0.000	0.000
115	A	119	GLU	-1	-0.882	-0.928	32.556	-9.210	-9.210	0.000	0.000	0.000	0.000
116	A	120	TYR	0	-0.079	-0.043	35.192	0.328	0.328	0.000	0.000	0.000	0.000
117	A	121	PHE	0	-0.044	-0.039	34.963	0.302	0.302	0.000	0.000	0.000	0.000
118	A	122	LYS	1	1.004	1.007	37.413	7.973	7.973	0.000	0.000	0.000	0.000
119	A	123	GLY	0	-0.038	-0.016	38.332	0.211	0.211	0.000	0.000	0.000	0.000
120	A	124	SER	0	-0.042	-0.011	39.702	0.255	0.255	0.000	0.000	0.000	0.000
121	A	125	LYS	1	0.935	0.966	34.392	8.723	8.723	0.000	0.000	0.000	0.000
122	A	126	SER	0	0.021	-0.017	32.511	0.154	0.154	0.000	0.000	0.000	0.000
123	A	127	PRO	0	-0.067	-0.034	34.170	-0.171	-0.171	0.000	0.000	0.000	0.000
124	A	128	PHE	0	-0.023	-0.035	29.925	-0.024	-0.024	0.000	0.000	0.000	0.000
125	A	129	SER	0	0.000	-0.010	29.166	-0.476	-0.476	0.000	0.000	0.000	0.000
126	A	130	ALA	0	0.019	0.004	25.408	-0.267	-0.267	0.000	0.000	0.000	0.000
127	A	131	LEU	0	-0.075	-0.030	24.465	-0.558	-0.558	0.000	0.000	0.000	0.000
128	A	132	ASN	0	0.063	0.027	24.811	-0.543	-0.543	0.000	0.000	0.000	0.000
129	A	133	ILE	0	0.048	0.030	23.117	-0.245	-0.245	0.000	0.000	0.000	0.000
130	A	134	ALA	0	-0.012	-0.002	20.693	-0.466	-0.466	0.000	0.000	0.000	0.000
131	A	135	VAL	0	0.020	0.003	20.392	-0.697	-0.697	0.000	0.000	0.000	0.000
132	A	136	HIS	1	0.856	0.945	21.763	12.189	12.189	0.000	0.000	0.000	0.000
133	A	137	GLU	-1	-0.878	-0.956	18.972	-15.156	-15.156	0.000	0.000	0.000	0.000
134	A	138	LEU	0	-0.019	-0.017	15.504	-0.666	-0.666	0.000	0.000	0.000	0.000
135	A	139	SER	0	0.010	0.011	17.301	-0.641	-0.641	0.000	0.000	0.000	0.000
136	A	140	ASP	-1	-0.808	-0.864	19.163	-13.732	-13.732	0.000	0.000	0.000	0.000
137	A	141	VAL	0	-0.042	-0.028	13.224	-0.252	-0.252	0.000	0.000	0.000	0.000
138	A	142	GLY	0	0.023	0.000	14.791	-0.888	-0.888	0.000	0.000	0.000	0.000
139	A	143	ARG	1	0.839	0.916	15.743	13.141	13.141	0.000	0.000	0.000	0.000
140	A	144	ALA	0	-0.068	-0.024	15.302	0.077	0.077	0.000	0.000	0.000	0.000
141	A	145	ILE	0	-0.021	-0.010	10.350	-0.740	-0.740	0.000	0.000	0.000	0.000
142	A	146	VAL	0	0.043	0.012	13.010	-0.456	-0.456	0.000	0.000	0.000	0.000
143	A	147	ARG	1	0.926	0.964	15.806	16.242	16.242	0.000	0.000	0.000	0.000
144	A	148	ASN	0	-0.110	-0.055	12.733	0.348	0.348	0.000	0.000	0.000	0.000
145	A	149	LEU	0	-0.077	-0.040	12.965	-0.462	-0.462	0.000	0.000	0.000	0.000
146	A	150	LEU	-1	-0.951	-0.949	16.585	-13.685	-13.685	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)