FMO DATABASE

FMODB ID: QM32Y

Calculation Name: 7SYC-A-Xray547

Preferred Name:

Target Type:

Ligand Name: magnesium ion

Ligand 3-letter code: MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7SYC

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-05

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	131
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1145870.997652
FMO2-HF: Nuclear repulsion	1094583.80906
FMO2-HF: Total energy	-51287.188592
FMO2-MP2: Total energy	-51438.593929

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:-1:HIS)

Summations of interaction energy for fragment #1(A:-1:HIS)

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.
-31.638	-30.433	-0.006	-0.473	-0.726	0.001

Interaction energy analysis for fragmet #1(A:-1:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.888 / q_NPA : 0.934

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	1	MET	0	0.036	0.065	3.855	-3.720	-2.515	-0.006	-0.473	-0.726	0.001
4	A	2	LYS	1	0.834	0.908	4.812	51.721	51.721	0.000	0.000	0.000	0.000
5	A	3	LYS	1	0.976	0.974	8.310	22.900	22.900	0.000	0.000	0.000	0.000
6	A	4	LEU	0	0.019	0.023	12.055	0.023	0.023	0.000	0.000	0.000	0.000
7	A	5	GLN	0	0.009	0.013	14.992	0.703	0.703	0.000	0.000	0.000	0.000
8	A	6	ILE	0	0.027	0.023	18.162	-0.126	-0.126	0.000	0.000	0.000	0.000
9	A	7	ALA	0	0.018	0.014	21.423	0.091	0.091	0.000	0.000	0.000	0.000
10	A	8	VAL	0	-0.012	0.002	24.692	0.066	0.066	0.000	0.000	0.000	0.000
11	A	9	GLY	0	0.049	0.012	27.343	0.192	0.192	0.000	0.000	0.000	0.000
12	A	10	ILE	0	-0.041	-0.014	30.885	0.075	0.075	0.000	0.000	0.000	0.000
13	A	11	ILE	0	0.010	0.008	33.206	0.220	0.220	0.000	0.000	0.000	0.000
14	A	12	ARG	1	0.814	0.911	36.222	7.973	7.973	0.000	0.000	0.000	0.000
15	A	13	ASN	0	0.017	-0.001	39.238	0.081	0.081	0.000	0.000	0.000	0.000
16	A	14	PRO	0	0.003	-0.019	42.876	-0.012	-0.012	0.000	0.000	0.000	0.000
17	A	15	GLN	0	-0.028	-0.008	45.764	0.012	0.012	0.000	0.000	0.000	0.000
18	A	16	GLY	0	0.025	0.023	42.802	0.033	0.033	0.000	0.000	0.000	0.000
19	A	17	GLU	-1	-0.944	-0.962	41.253	-7.216	-7.216	0.000	0.000	0.000	0.000
20	A	18	ILE	0	0.007	-0.012	34.690	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	19	PHE	0	-0.002	0.004	35.066	0.063	0.063	0.000	0.000	0.000	0.000
22	A	20	ILE	0	-0.038	-0.015	32.387	-0.292	-0.292	0.000	0.000	0.000	0.000
23	A	21	THR	0	0.065	0.021	29.728	0.276	0.276	0.000	0.000	0.000	0.000
24	A	22	GLN	0	-0.050	-0.033	29.992	0.080	0.080	0.000	0.000	0.000	0.000
25	A	23	ARG	1	0.846	0.914	23.438	12.334	12.334	0.000	0.000	0.000	0.000
26	A	24	ALA	0	0.022	0.011	28.381	0.018	0.018	0.000	0.000	0.000	0.000
27	A	25	ALA	0	-0.007	-0.006	25.239	-0.405	-0.405	0.000	0.000	0.000	0.000
28	A	26	ASP	-1	-0.784	-0.874	21.331	-12.771	-12.771	0.000	0.000	0.000	0.000
29	A	27	ALA	0	-0.012	-0.008	22.936	-0.045	-0.045	0.000	0.000	0.000	0.000
30	A	28	HIS	0	-0.073	-0.029	22.970	0.394	0.394	0.000	0.000	0.000	0.000
31	A	29	MET	0	-0.051	-0.032	27.519	0.342	0.342	0.000	0.000	0.000	0.000
32	A	30	ALA	0	0.007	-0.002	29.235	0.313	0.313	0.000	0.000	0.000	0.000
33	A	31	ASN	0	-0.016	-0.011	29.445	-0.265	-0.265	0.000	0.000	0.000	0.000
34	A	32	LYS	1	0.818	0.895	24.437	11.978	11.978	0.000	0.000	0.000	0.000
35	A	33	LEU	0	0.016	0.010	28.930	0.029	0.029	0.000	0.000	0.000	0.000
36	A	34	GLU	-1	-0.846	-0.929	25.266	-12.412	-12.412	0.000	0.000	0.000	0.000
37	A	35	PHE	0	0.021	0.005	27.896	0.415	0.415	0.000	0.000	0.000	0.000
38	A	36	PRO	0	0.022	0.028	27.827	-0.367	-0.367	0.000	0.000	0.000	0.000
39	A	37	GLY	0	-0.013	-0.019	27.212	0.121	0.121	0.000	0.000	0.000	0.000
40	A	38	GLY	0	0.103	0.050	23.270	-0.279	-0.279	0.000	0.000	0.000	0.000
41	A	39	LYS	1	0.728	0.845	16.910	16.072	16.072	0.000	0.000	0.000	0.000
42	A	40	ILE	0	-0.019	-0.003	20.855	0.526	0.526	0.000	0.000	0.000	0.000
43	A	41	GLU	-1	-0.833	-0.905	20.210	-16.152	-16.152	0.000	0.000	0.000	0.000
44	A	42	SER	0	-0.080	-0.056	19.014	-0.082	-0.082	0.000	0.000	0.000	0.000
45	A	43	ASP	-1	-0.964	-0.981	20.941	-12.396	-12.396	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.788	-0.850	24.421	-11.465	-11.465	0.000	0.000	0.000	0.000
47	A	45	THR	0	-0.026	-0.045	25.151	-0.311	-0.311	0.000	0.000	0.000	0.000
48	A	46	PRO	0	0.010	-0.020	24.811	0.067	0.067	0.000	0.000	0.000	0.000
49	A	47	GLU	-1	-0.817	-0.876	26.684	-9.127	-9.127	0.000	0.000	0.000	0.000
50	A	48	GLN	0	0.027	0.032	28.955	0.026	0.026	0.000	0.000	0.000	0.000
51	A	49	ALA	0	0.029	0.034	25.326	0.126	0.126	0.000	0.000	0.000	0.000
52	A	50	LEU	0	-0.015	-0.005	27.303	0.151	0.151	0.000	0.000	0.000	0.000
53	A	51	ILE	0	-0.034	-0.022	29.525	0.242	0.242	0.000	0.000	0.000	0.000
54	A	52	ARG	1	0.791	0.886	25.040	11.969	11.969	0.000	0.000	0.000	0.000
55	A	53	GLU	-1	-0.809	-0.906	25.409	-11.907	-11.907	0.000	0.000	0.000	0.000
56	A	54	LEU	0	-0.007	-0.005	29.052	0.188	0.188	0.000	0.000	0.000	0.000
57	A	55	GLN	0	-0.020	-0.017	32.276	0.134	0.134	0.000	0.000	0.000	0.000
58	A	56	GLU	-1	-0.974	-0.983	28.631	-10.334	-10.334	0.000	0.000	0.000	0.000
59	A	57	GLU	-1	-0.788	-0.893	26.888	-10.827	-10.827	0.000	0.000	0.000	0.000
60	A	58	VAL	0	-0.042	-0.026	31.532	0.193	0.193	0.000	0.000	0.000	0.000
61	A	59	GLY	0	-0.017	0.000	34.827	0.287	0.287	0.000	0.000	0.000	0.000
62	A	60	ILE	0	-0.045	-0.005	36.192	0.274	0.274	0.000	0.000	0.000	0.000
63	A	61	THR	0	-0.012	-0.005	36.330	-0.255	-0.255	0.000	0.000	0.000	0.000
64	A	62	VAL	0	0.012	0.009	34.082	0.222	0.222	0.000	0.000	0.000	0.000
65	A	63	THR	0	-0.024	-0.013	37.335	0.001	0.001	0.000	0.000	0.000	0.000
66	A	64	THR	0	-0.052	-0.039	38.536	0.138	0.138	0.000	0.000	0.000	0.000
67	A	65	SER	0	-0.055	-0.035	33.845	-0.075	-0.075	0.000	0.000	0.000	0.000
68	A	66	SER	0	0.007	0.002	35.089	0.146	0.146	0.000	0.000	0.000	0.000
69	A	67	LEU	0	-0.044	-0.017	27.948	-0.167	-0.167	0.000	0.000	0.000	0.000
70	A	68	PHE	0	-0.016	-0.001	31.383	0.139	0.139	0.000	0.000	0.000	0.000
71	A	69	ASP	-1	-0.860	-0.948	28.091	-10.907	-10.907	0.000	0.000	0.000	0.000
72	A	70	LYS	1	0.803	0.903	22.234	13.589	13.589	0.000	0.000	0.000	0.000
73	A	71	LEU	0	-0.003	0.028	22.659	-0.186	-0.186	0.000	0.000	0.000	0.000
74	A	72	GLU	-1	-0.891	-0.946	18.503	-15.831	-15.831	0.000	0.000	0.000	0.000
75	A	73	TYR	0	-0.016	-0.014	16.470	0.027	0.027	0.000	0.000	0.000	0.000
76	A	74	GLN	0	-0.039	-0.049	10.171	0.021	0.021	0.000	0.000	0.000	0.000
77	A	75	PHE	0	0.011	0.003	10.457	1.070	1.070	0.000	0.000	0.000	0.000
78	A	76	PRO	0	-0.003	-0.012	8.032	-1.271	-1.271	0.000	0.000	0.000	0.000
79	A	77	ASP	-1	-0.840	-0.900	5.064	-37.930	-37.930	0.000	0.000	0.000	0.000
80	A	78	ARG	1	0.827	0.894	6.010	22.677	22.677	0.000	0.000	0.000	0.000
81	A	79	HIS	0	-0.005	0.010	8.833	0.604	0.604	0.000	0.000	0.000	0.000
82	A	80	ILE	0	0.001	-0.008	12.391	-0.427	-0.427	0.000	0.000	0.000	0.000
83	A	81	THR	0	-0.005	-0.007	15.312	0.648	0.648	0.000	0.000	0.000	0.000
84	A	82	LEU	0	0.004	0.004	18.889	-0.131	-0.131	0.000	0.000	0.000	0.000
85	A	83	TRP	0	-0.004	-0.020	21.940	0.528	0.528	0.000	0.000	0.000	0.000
86	A	84	PHE	0	0.024	0.009	24.342	0.033	0.033	0.000	0.000	0.000	0.000
87	A	85	PHE	0	0.037	0.001	27.499	0.173	0.173	0.000	0.000	0.000	0.000
88	A	86	LEU	0	-0.030	0.013	31.284	0.001	0.001	0.000	0.000	0.000	0.000
89	A	87	VAL	0	-0.009	-0.021	33.935	0.089	0.089	0.000	0.000	0.000	0.000
90	A	88	GLU	-1	-0.756	-0.869	36.642	-7.710	-7.710	0.000	0.000	0.000	0.000
91	A	89	SER	0	-0.049	-0.036	39.867	0.316	0.316	0.000	0.000	0.000	0.000
92	A	90	TRP	0	-0.025	-0.012	39.116	-0.259	-0.259	0.000	0.000	0.000	0.000
93	A	91	GLN	0	-0.031	-0.010	40.861	0.299	0.299	0.000	0.000	0.000	0.000
94	A	92	GLY	0	0.062	0.028	41.088	-0.191	-0.191	0.000	0.000	0.000	0.000
95	A	93	GLU	-1	-0.912	-0.966	42.552	-7.112	-7.112	0.000	0.000	0.000	0.000
96	A	94	PRO	0	-0.028	-0.012	37.389	-0.087	-0.087	0.000	0.000	0.000	0.000
97	A	95	TRP	0	-0.028	-0.006	37.929	0.141	0.141	0.000	0.000	0.000	0.000
98	A	96	GLY	0	0.046	0.023	35.255	-0.220	-0.220	0.000	0.000	0.000	0.000
99	A	97	LYS	1	0.784	0.888	34.863	8.880	8.880	0.000	0.000	0.000	0.000
100	A	98	GLU	-1	-0.925	-0.966	28.962	-10.525	-10.525	0.000	0.000	0.000	0.000
101	A	99	GLY	0	-0.067	-0.027	32.540	-0.119	-0.119	0.000	0.000	0.000	0.000
102	A	100	GLN	0	-0.023	-0.015	30.540	0.190	0.190	0.000	0.000	0.000	0.000
103	A	101	PRO	0	-0.039	-0.029	32.707	0.233	0.233	0.000	0.000	0.000	0.000
104	A	102	GLY	0	0.039	0.007	33.673	-0.321	-0.321	0.000	0.000	0.000	0.000
105	A	103	ARG	1	0.880	0.955	35.866	8.187	8.187	0.000	0.000	0.000	0.000
106	A	104	TRP	0	0.040	0.031	37.845	-0.245	-0.245	0.000	0.000	0.000	0.000
107	A	105	MET	0	-0.068	-0.041	35.494	0.078	0.078	0.000	0.000	0.000	0.000
108	A	106	ALA	0	0.056	0.042	39.606	-0.083	-0.083	0.000	0.000	0.000	0.000
109	A	107	GLY	0	0.078	0.049	38.343	-0.120	-0.120	0.000	0.000	0.000	0.000
110	A	108	PRO	0	0.002	-0.006	38.480	-0.169	-0.169	0.000	0.000	0.000	0.000
111	A	109	THR	0	-0.118	-0.070	40.061	0.108	0.108	0.000	0.000	0.000	0.000
112	A	110	LEU	0	-0.021	0.001	34.116	-0.078	-0.078	0.000	0.000	0.000	0.000
113	A	111	ASP	-1	-0.824	-0.915	34.023	-9.201	-9.201	0.000	0.000	0.000	0.000
114	A	112	PRO	0	0.014	-0.004	30.205	-0.234	-0.234	0.000	0.000	0.000	0.000
115	A	113	ALA	0	-0.041	-0.022	29.352	-0.437	-0.437	0.000	0.000	0.000	0.000
116	A	114	ALA	0	-0.019	0.000	29.775	-0.200	-0.200	0.000	0.000	0.000	0.000
117	A	115	PHE	0	0.039	0.028	27.510	-0.087	-0.087	0.000	0.000	0.000	0.000
118	A	116	PRO	0	-0.025	-0.011	22.464	-0.302	-0.302	0.000	0.000	0.000	0.000
119	A	117	PRO	0	0.045	0.017	21.740	0.062	0.062	0.000	0.000	0.000	0.000
120	A	118	ALA	0	-0.027	-0.008	20.305	0.107	0.107	0.000	0.000	0.000	0.000
121	A	119	ASN	0	0.030	-0.005	22.351	0.123	0.123	0.000	0.000	0.000	0.000
122	A	120	GLU	-1	-0.889	-0.914	25.868	-10.384	-10.384	0.000	0.000	0.000	0.000
123	A	121	PRO	0	0.040	0.019	25.873	0.389	0.389	0.000	0.000	0.000	0.000
124	A	122	VAL	0	0.017	0.008	27.918	0.404	0.404	0.000	0.000	0.000	0.000
125	A	123	ILE	0	-0.018	-0.003	29.803	0.351	0.351	0.000	0.000	0.000	0.000
126	A	124	SER	0	-0.026	-0.046	31.607	0.456	0.456	0.000	0.000	0.000	0.000
127	A	125	LYS	1	0.829	0.923	32.763	9.816	9.816	0.000	0.000	0.000	0.000
128	A	126	LEU	0	-0.010	-0.015	32.962	0.241	0.241	0.000	0.000	0.000	0.000
129	A	127	ILE	0	-0.052	-0.010	35.257	0.245	0.245	0.000	0.000	0.000	0.000
130	A	128	ALA	0	-0.056	-0.032	37.988	0.231	0.231	0.000	0.000	0.000	0.000
131	A	129	GLN	-1	-0.924	-0.950	37.863	-7.499	-7.499	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:HIS)