FMO DATABASE

FMODB ID: RQG18

Calculation Name: 1QC6-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1QC6

Chain ID: A

ChEMBL ID:

UniProt ID: P70429

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	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-930632.597489
FMO2-HF: Nuclear repulsion	885191.261443
FMO2-HF: Total energy	-45441.336046
FMO2-MP2: Total energy	-45572.815089

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:1001:MET)

Summations of interaction energy for fragment #1(A:1001:MET)

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.
-46.437	-41.16	5.11	-4.915	-5.473	-0.045

Interaction energy analysis for fragmet #1(A:1001:MET)

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 : 0.910

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	1003	GLU	-1	-0.836	-0.891	3.158	-63.640	-61.059	0.059	-1.464	-1.176	-0.006
41	A	1041	ASN	0	-0.011	-0.019	2.820	-16.053	-13.797	0.081	-1.204	-1.134	-0.013
42	A	1042	THR	0	0.074	0.017	4.187	-3.757	-3.506	-0.001	-0.055	-0.196	0.000
43	A	1043	ALA	0	-0.109	-0.054	1.894	-1.152	-1.346	4.964	-2.061	-2.708	-0.025
44	A	1044	SER	0	-0.002	-0.007	3.652	6.730	7.113	0.007	-0.131	-0.259	-0.001
4	A	1004	GLN	0	0.011	-0.003	5.847	1.755	1.755	0.000	0.000	0.000	0.000
5	A	1005	SER	0	-0.003	-0.003	7.420	2.217	2.217	0.000	0.000	0.000	0.000
6	A	1006	ILE	0	-0.034	-0.021	11.175	0.251	0.251	0.000	0.000	0.000	0.000
7	A	1007	CYS	0	-0.051	-0.003	13.473	1.711	1.711	0.000	0.000	0.000	0.000
8	A	1008	GLN	0	0.025	0.010	16.083	-0.381	-0.381	0.000	0.000	0.000	0.000
9	A	1009	ALA	0	0.005	0.017	18.694	0.643	0.643	0.000	0.000	0.000	0.000
10	A	1010	ARG	1	0.835	0.886	22.005	10.984	10.984	0.000	0.000	0.000	0.000
11	A	1011	ALA	0	-0.017	-0.013	24.567	0.343	0.343	0.000	0.000	0.000	0.000
12	A	1012	SER	0	0.011	0.003	26.023	-0.136	-0.136	0.000	0.000	0.000	0.000
13	A	1013	VAL	0	-0.005	0.000	23.152	0.069	0.069	0.000	0.000	0.000	0.000
14	A	1014	MET	0	-0.041	-0.029	26.130	0.392	0.392	0.000	0.000	0.000	0.000
15	A	1015	VAL	0	0.034	0.022	26.956	-0.405	-0.405	0.000	0.000	0.000	0.000
16	A	1016	TYR	0	-0.048	-0.024	29.278	0.420	0.420	0.000	0.000	0.000	0.000
17	A	1017	ASP	-1	-0.798	-0.875	32.439	-8.810	-8.810	0.000	0.000	0.000	0.000
18	A	1018	ASP	-1	-0.904	-0.975	34.113	-9.021	-9.021	0.000	0.000	0.000	0.000
19	A	1019	THR	0	-0.073	-0.031	36.589	0.350	0.350	0.000	0.000	0.000	0.000
20	A	1020	SER	0	-0.068	-0.050	38.037	0.257	0.257	0.000	0.000	0.000	0.000
21	A	1021	LYS	1	0.957	0.984	38.966	7.651	7.651	0.000	0.000	0.000	0.000
22	A	1022	LYS	1	0.857	0.937	37.661	8.404	8.404	0.000	0.000	0.000	0.000
23	A	1023	TRP	0	0.044	0.028	29.348	-0.218	-0.218	0.000	0.000	0.000	0.000
24	A	1024	VAL	0	-0.033	-0.020	32.147	0.318	0.318	0.000	0.000	0.000	0.000
25	A	1025	PRO	0	0.023	0.010	30.498	-0.364	-0.364	0.000	0.000	0.000	0.000
26	A	1026	ILE	0	-0.005	-0.017	26.839	0.157	0.157	0.000	0.000	0.000	0.000
27	A	1027	LYS	0	-0.011	-0.018	21.906	0.075	0.075	0.000	0.000	0.000	0.000
28	A	1028	PRO	0	0.016	0.019	27.184	-0.026	-0.026	0.000	0.000	0.000	0.000
29	A	1029	GLY	0	0.074	0.057	28.672	0.269	0.269	0.000	0.000	0.000	0.000
30	A	1030	GLN	0	-0.042	-0.024	31.094	0.063	0.063	0.000	0.000	0.000	0.000
31	A	1031	GLN	0	0.015	0.008	30.570	0.353	0.353	0.000	0.000	0.000	0.000
32	A	1032	GLY	0	-0.009	0.000	31.948	-0.082	-0.082	0.000	0.000	0.000	0.000
33	A	1033	PHE	0	-0.067	-0.032	27.641	-0.112	-0.112	0.000	0.000	0.000	0.000
34	A	1034	SER	-1	-0.700	-0.836	23.114	-12.761	-12.761	0.000	0.000	0.000	0.000
35	A	1035	ARG	1	0.765	0.869	19.532	14.730	14.730	0.000	0.000	0.000	0.000
36	A	1036	ILE	0	0.006	0.000	18.778	-0.594	-0.594	0.000	0.000	0.000	0.000
37	A	1037	ASN	0	0.023	-0.006	14.429	1.280	1.280	0.000	0.000	0.000	0.000
38	A	1038	ILE	0	0.009	0.012	13.341	0.013	0.013	0.000	0.000	0.000	0.000
39	A	1039	TYR	0	0.013	-0.004	9.123	0.223	0.223	0.000	0.000	0.000	0.000
40	A	1040	HIS	0	-0.006	0.000	7.794	-0.077	-0.077	0.000	0.000	0.000	0.000
45	A	1045	SER	0	-0.012	0.010	6.613	5.288	5.288	0.000	0.000	0.000	0.000
46	A	1046	THR	0	0.012	0.024	7.520	4.433	4.433	0.000	0.000	0.000	0.000
47	A	1047	PHE	0	0.065	0.011	8.715	-2.716	-2.716	0.000	0.000	0.000	0.000
48	A	1048	ARG	1	0.860	0.911	10.195	25.668	25.668	0.000	0.000	0.000	0.000
49	A	1049	VAL	0	0.018	0.025	12.694	-0.417	-0.417	0.000	0.000	0.000	0.000
50	A	1050	VAL	0	-0.032	-0.017	12.121	0.107	0.107	0.000	0.000	0.000	0.000
51	A	1051	GLY	0	0.001	0.002	15.393	0.289	0.289	0.000	0.000	0.000	0.000
52	A	1052	VAL	0	-0.019	-0.018	16.915	-0.164	-0.164	0.000	0.000	0.000	0.000
53	A	1053	LYS	0	0.028	0.024	19.845	0.489	0.489	0.000	0.000	0.000	0.000
54	A	1054	LEU	0	-0.077	-0.035	23.155	-0.235	-0.235	0.000	0.000	0.000	0.000
55	A	1055	GLN	0	-0.027	-0.012	24.178	0.537	0.537	0.000	0.000	0.000	0.000
56	A	1056	ASP	-1	-0.836	-0.937	26.066	-11.675	-11.675	0.000	0.000	0.000	0.000
57	A	1057	GLN	0	-0.087	-0.058	20.777	-0.201	-0.201	0.000	0.000	0.000	0.000
58	A	1058	GLN	0	0.006	0.028	20.410	-0.740	-0.740	0.000	0.000	0.000	0.000
59	A	1059	VAL	0	-0.034	-0.026	16.244	-0.147	-0.147	0.000	0.000	0.000	0.000
60	A	1060	VAL	0	0.012	0.020	19.444	0.323	0.323	0.000	0.000	0.000	0.000
61	A	1061	ILE	0	-0.001	0.001	18.567	0.215	0.215	0.000	0.000	0.000	0.000
62	A	1062	ASN	0	0.036	0.012	12.783	-1.619	-1.619	0.000	0.000	0.000	0.000
63	A	1063	TYR	0	0.065	0.044	15.895	-0.149	-0.149	0.000	0.000	0.000	0.000
64	A	1064	SER	0	-0.008	-0.002	13.617	-0.754	-0.754	0.000	0.000	0.000	0.000
65	A	1065	ILE	0	-0.013	-0.007	14.691	1.340	1.340	0.000	0.000	0.000	0.000
66	A	1066	VAL	0	0.013	0.001	15.534	-0.850	-0.850	0.000	0.000	0.000	0.000
67	A	1067	LYS	1	0.949	0.964	17.996	14.994	14.994	0.000	0.000	0.000	0.000
68	A	1068	GLY	0	0.034	0.019	19.389	0.426	0.426	0.000	0.000	0.000	0.000
69	A	1069	LEU	0	-0.066	0.004	19.951	0.695	0.695	0.000	0.000	0.000	0.000
70	A	1070	LYS	1	0.875	0.928	22.720	12.339	12.339	0.000	0.000	0.000	0.000
71	A	1071	TYR	0	0.047	0.017	23.105	0.011	0.011	0.000	0.000	0.000	0.000
72	A	1072	ASN	0	0.009	-0.001	25.202	0.456	0.456	0.000	0.000	0.000	0.000
73	A	1073	GLN	0	0.002	-0.006	27.372	-0.314	-0.314	0.000	0.000	0.000	0.000
74	A	1074	ALA	0	0.021	0.026	29.809	0.289	0.289	0.000	0.000	0.000	0.000
75	A	1075	THR	0	0.036	0.016	32.243	0.273	0.273	0.000	0.000	0.000	0.000
76	A	1076	PRO	0	-0.001	-0.024	31.799	-0.318	-0.318	0.000	0.000	0.000	0.000
77	A	1077	THR	0	-0.007	-0.010	30.602	-0.169	-0.169	0.000	0.000	0.000	0.000
78	A	1078	PHE	0	-0.005	0.021	30.035	-0.283	-0.283	0.000	0.000	0.000	0.000
79	A	1079	HIS	0	-0.010	0.013	26.181	-0.223	-0.223	0.000	0.000	0.000	0.000
80	A	1080	GLN	0	0.008	-0.008	26.688	-0.050	-0.050	0.000	0.000	0.000	0.000
81	A	1081	TRP	0	0.012	-0.005	20.898	-0.274	-0.274	0.000	0.000	0.000	0.000
82	A	1082	ARG	1	0.919	0.983	25.668	10.641	10.641	0.000	0.000	0.000	0.000
83	A	1083	ASP	-1	-0.704	-0.823	22.926	-12.853	-12.853	0.000	0.000	0.000	0.000
84	A	1084	ALA	0	-0.061	-0.050	24.390	-0.060	-0.060	0.000	0.000	0.000	0.000
85	A	1085	ARG	1	0.710	0.805	24.306	12.862	12.862	0.000	0.000	0.000	0.000
86	A	1086	GLN	0	0.019	0.040	26.379	0.519	0.519	0.000	0.000	0.000	0.000
87	A	1087	VAL	0	-0.023	-0.029	27.363	-0.196	-0.196	0.000	0.000	0.000	0.000
88	A	1088	TYR	-1	-0.781	-0.873	24.153	-12.824	-12.824	0.000	0.000	0.000	0.000
89	A	1089	GLY	0	0.016	-0.012	26.241	0.117	0.117	0.000	0.000	0.000	0.000
90	A	1090	LEU	0	-0.045	-0.011	21.798	-0.235	-0.235	0.000	0.000	0.000	0.000
91	A	1091	ASN	0	0.035	0.016	26.471	0.425	0.425	0.000	0.000	0.000	0.000
92	A	1092	PHE	0	0.007	-0.012	23.136	-0.073	-0.073	0.000	0.000	0.000	0.000
93	A	1093	ALA	0	-0.018	-0.004	27.853	0.437	0.437	0.000	0.000	0.000	0.000
94	A	1094	SER	0	-0.058	-0.064	28.662	0.382	0.382	0.000	0.000	0.000	0.000
95	A	1095	LYS	1	1.007	0.985	29.217	9.209	9.209	0.000	0.000	0.000	0.000
96	A	1096	GLU	-1	-0.867	-0.887	26.085	-12.186	-12.186	0.000	0.000	0.000	0.000
97	A	1097	GLU	-1	-0.699	-0.786	24.874	-12.253	-12.253	0.000	0.000	0.000	0.000
98	A	1098	ALA	0	0.033	0.024	24.363	-0.523	-0.523	0.000	0.000	0.000	0.000
99	A	1099	THR	0	-0.050	-0.022	25.496	-0.153	-0.153	0.000	0.000	0.000	0.000
100	A	1100	THR	0	-0.017	-0.039	21.315	-0.491	-0.491	0.000	0.000	0.000	0.000
101	A	1101	PHE	0	0.015	-0.008	18.746	-0.780	-0.780	0.000	0.000	0.000	0.000
102	A	1102	SER	0	-0.063	-0.031	20.779	-0.387	-0.387	0.000	0.000	0.000	0.000
103	A	1103	ASN	0	0.024	0.005	22.397	-0.036	-0.036	0.000	0.000	0.000	0.000
104	A	1104	ALA	0	0.011	0.006	17.021	-0.387	-0.387	0.000	0.000	0.000	0.000
105	A	1105	MET	0	-0.014	-0.004	17.512	-1.034	-1.034	0.000	0.000	0.000	0.000
106	A	1106	LEU	0	0.001	-0.005	18.949	-0.336	-0.336	0.000	0.000	0.000	0.000
107	A	1107	PHE	0	-0.008	0.010	14.137	-0.055	-0.055	0.000	0.000	0.000	0.000
108	A	1108	ALA	0	0.029	0.007	14.522	-0.296	-0.296	0.000	0.000	0.000	0.000
109	A	1109	LEU	0	-0.032	-0.025	15.935	-0.369	-0.369	0.000	0.000	0.000	0.000
110	A	1110	ASN	0	-0.041	-0.026	18.600	0.902	0.902	0.000	0.000	0.000	0.000
111	A	1111	ILE	0	-0.014	0.001	13.223	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	1112	MET	0	-0.130	-0.049	12.420	-0.740	-0.740	0.000	0.000	0.000	0.000
113	A	1113	ASN	-1	-0.922	-0.950	16.775	-14.594	-14.594	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1001:MET)