FMO DATABASE

FMODB ID: 7KGYK

Calculation Name: 1Q7S-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1Q7S

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y3E5

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	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-917271.05075
FMO2-HF: Nuclear repulsion	872380.877429
FMO2-HF: Total energy	-44890.173322
FMO2-MP2: Total energy	-45019.169322

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:63:GLY)

Summations of interaction energy for fragment #1(A:63:GLY)

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.
52.647	54.074	0.044	-0.558	-0.913	-0.003

Interaction energy analysis for fragmet #1(A:63:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.844 / q_NPA : 0.914

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	65	TYR	0	0.011	-0.006	2.723	4.526	5.848	0.046	-0.505	-0.863	-0.003
45	A	107	GLN	0	0.007	0.011	4.229	-11.139	-11.081	-0.001	-0.030	-0.027	0.000
49	A	111	CYS	0	-0.038	0.007	5.451	-3.691	-3.644	-0.001	-0.023	-0.023	0.000
4	A	66	LYS	1	0.804	0.876	6.686	29.130	29.130	0.000	0.000	0.000	0.000
5	A	67	MET	0	-0.009	0.018	10.216	0.976	0.976	0.000	0.000	0.000	0.000
6	A	68	ILE	0	-0.009	-0.003	13.937	0.101	0.101	0.000	0.000	0.000	0.000
7	A	69	LEU	0	-0.035	-0.021	16.540	0.597	0.597	0.000	0.000	0.000	0.000
8	A	70	VAL	0	0.043	0.014	20.253	0.331	0.331	0.000	0.000	0.000	0.000
9	A	71	VAL	0	-0.004	-0.013	22.559	0.513	0.513	0.000	0.000	0.000	0.000
10	A	72	ARG	1	0.842	0.928	26.091	9.886	9.886	0.000	0.000	0.000	0.000
11	A	73	ASN	0	-0.014	-0.014	29.051	0.580	0.580	0.000	0.000	0.000	0.000
12	A	74	ASP	-1	-0.813	-0.912	31.334	-9.225	-9.225	0.000	0.000	0.000	0.000
13	A	75	LEU	0	0.003	0.003	32.439	0.271	0.271	0.000	0.000	0.000	0.000
14	A	76	LYS	1	0.828	0.926	34.674	9.224	9.224	0.000	0.000	0.000	0.000
15	A	77	MET	0	-0.021	0.009	29.778	0.192	0.192	0.000	0.000	0.000	0.000
16	A	78	GLY	0	0.058	0.027	32.857	-0.172	-0.172	0.000	0.000	0.000	0.000
17	A	79	LYS	1	1.001	0.986	30.802	9.113	9.113	0.000	0.000	0.000	0.000
18	A	80	GLY	0	0.021	0.017	30.291	-0.323	-0.323	0.000	0.000	0.000	0.000
19	A	81	LYS	1	0.906	0.955	31.392	9.078	9.078	0.000	0.000	0.000	0.000
20	A	82	VAL	0	0.024	0.013	26.807	-0.229	-0.229	0.000	0.000	0.000	0.000
21	A	83	ALA	0	0.057	0.030	26.552	-0.454	-0.454	0.000	0.000	0.000	0.000
22	A	84	ALA	0	0.021	0.023	26.729	-0.417	-0.417	0.000	0.000	0.000	0.000
23	A	85	GLN	0	0.036	0.026	27.996	-0.309	-0.309	0.000	0.000	0.000	0.000
24	A	86	CYS	0	-0.003	-0.001	23.122	-0.466	-0.466	0.000	0.000	0.000	0.000
25	A	87	SER	0	-0.025	-0.017	23.037	-0.757	-0.757	0.000	0.000	0.000	0.000
26	A	88	HIS	0	-0.027	-0.020	24.069	-0.668	-0.668	0.000	0.000	0.000	0.000
27	A	89	ALA	0	0.010	0.003	22.411	-0.257	-0.257	0.000	0.000	0.000	0.000
28	A	90	ALA	0	0.036	0.004	19.623	-0.614	-0.614	0.000	0.000	0.000	0.000
29	A	91	VAL	0	0.008	0.004	19.767	-0.678	-0.678	0.000	0.000	0.000	0.000
30	A	92	SER	0	-0.025	-0.010	22.006	-0.218	-0.218	0.000	0.000	0.000	0.000
31	A	93	ALA	0	-0.005	0.005	17.634	-0.072	-0.072	0.000	0.000	0.000	0.000
32	A	94	TYR	0	-0.041	-0.033	16.465	-0.154	-0.154	0.000	0.000	0.000	0.000
33	A	95	LYS	1	0.951	0.976	18.385	11.861	11.861	0.000	0.000	0.000	0.000
34	A	96	GLN	0	-0.060	-0.044	19.509	0.273	0.273	0.000	0.000	0.000	0.000
35	A	97	ILE	0	-0.004	0.006	12.542	0.139	0.139	0.000	0.000	0.000	0.000
36	A	98	GLN	0	0.023	0.014	16.177	0.016	0.016	0.000	0.000	0.000	0.000
37	A	99	ARG	1	0.878	0.934	17.725	13.967	13.967	0.000	0.000	0.000	0.000
38	A	100	ARG	1	0.931	0.960	17.684	15.507	15.507	0.000	0.000	0.000	0.000
39	A	101	ASN	0	0.023	0.012	11.337	-0.611	-0.611	0.000	0.000	0.000	0.000
40	A	102	PRO	0	0.070	0.028	12.970	-1.569	-1.569	0.000	0.000	0.000	0.000
41	A	103	GLU	-1	-0.810	-0.880	9.802	-26.133	-26.133	0.000	0.000	0.000	0.000
42	A	104	MET	0	-0.030	-0.003	8.214	-2.537	-2.537	0.000	0.000	0.000	0.000
43	A	105	LEU	0	-0.045	-0.006	9.179	-1.724	-1.724	0.000	0.000	0.000	0.000
44	A	106	LYS	1	0.926	0.947	10.413	21.254	21.254	0.000	0.000	0.000	0.000
46	A	108	TRP	0	-0.020	-0.008	6.713	-2.097	-2.097	0.000	0.000	0.000	0.000
47	A	109	GLU	-1	-0.866	-0.943	8.793	-20.922	-20.922	0.000	0.000	0.000	0.000
48	A	110	TYR	0	-0.025	-0.016	6.896	1.772	1.772	0.000	0.000	0.000	0.000
50	A	112	GLY	0	0.039	0.022	7.626	2.500	2.500	0.000	0.000	0.000	0.000
51	A	113	GLN	0	-0.017	0.001	10.809	3.466	3.466	0.000	0.000	0.000	0.000
52	A	114	PRO	0	0.021	0.031	9.530	2.995	2.995	0.000	0.000	0.000	0.000
53	A	115	LYS	1	0.843	0.891	12.730	19.427	19.427	0.000	0.000	0.000	0.000
54	A	116	VAL	0	0.003	0.010	14.511	0.516	0.516	0.000	0.000	0.000	0.000
55	A	117	VAL	0	0.002	0.008	17.126	0.106	0.106	0.000	0.000	0.000	0.000
56	A	118	VAL	0	0.022	0.014	18.978	0.087	0.087	0.000	0.000	0.000	0.000
57	A	119	LYS	1	0.783	0.886	21.971	12.229	12.229	0.000	0.000	0.000	0.000
58	A	120	ALA	0	0.055	0.036	24.871	-0.248	-0.248	0.000	0.000	0.000	0.000
59	A	121	PRO	0	-0.022	-0.009	26.590	0.234	0.234	0.000	0.000	0.000	0.000
60	A	122	ASP	-1	-0.788	-0.898	29.949	-9.932	-9.932	0.000	0.000	0.000	0.000
61	A	123	GLU	-1	-0.902	-0.972	29.528	-9.942	-9.942	0.000	0.000	0.000	0.000
62	A	124	GLU	-1	-0.912	-0.945	29.881	-10.840	-10.840	0.000	0.000	0.000	0.000
63	A	125	THR	0	0.054	-0.002	25.466	-0.450	-0.450	0.000	0.000	0.000	0.000
64	A	126	LEU	0	-0.047	-0.024	24.992	-0.634	-0.634	0.000	0.000	0.000	0.000
65	A	127	ILE	0	-0.001	0.000	25.210	-0.542	-0.542	0.000	0.000	0.000	0.000
66	A	128	ALA	0	0.035	0.025	25.925	-0.321	-0.321	0.000	0.000	0.000	0.000
67	A	129	LEU	0	-0.028	-0.022	20.507	-0.588	-0.588	0.000	0.000	0.000	0.000
68	A	130	LEU	0	-0.043	-0.015	20.998	-0.851	-0.851	0.000	0.000	0.000	0.000
69	A	131	ALA	0	0.030	0.004	21.992	-0.523	-0.523	0.000	0.000	0.000	0.000
70	A	132	HIS	0	0.002	-0.003	18.368	-0.229	-0.229	0.000	0.000	0.000	0.000
71	A	133	ALA	0	0.032	0.006	17.372	-0.797	-0.797	0.000	0.000	0.000	0.000
72	A	134	LYS	1	0.866	0.936	17.625	14.411	14.411	0.000	0.000	0.000	0.000
73	A	135	MET	0	-0.012	-0.001	19.867	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	136	LEU	0	-0.040	-0.006	14.314	-0.352	-0.352	0.000	0.000	0.000	0.000
75	A	137	GLY	0	-0.008	-0.001	14.651	-1.409	-1.409	0.000	0.000	0.000	0.000
76	A	138	LEU	0	-0.053	-0.015	12.072	-0.855	-0.855	0.000	0.000	0.000	0.000
77	A	139	THR	0	-0.032	-0.018	14.870	1.761	1.761	0.000	0.000	0.000	0.000
78	A	140	VAL	0	0.007	0.004	16.968	-0.412	-0.412	0.000	0.000	0.000	0.000
79	A	141	SER	0	-0.040	-0.024	19.941	0.522	0.522	0.000	0.000	0.000	0.000
80	A	142	LEU	0	0.005	0.018	22.555	-0.161	-0.161	0.000	0.000	0.000	0.000
81	A	143	ILE	0	-0.042	-0.012	25.388	0.289	0.289	0.000	0.000	0.000	0.000
82	A	144	GLN	0	0.042	0.018	28.124	0.391	0.391	0.000	0.000	0.000	0.000
83	A	145	ASP	-1	-0.764	-0.884	31.934	-9.213	-9.213	0.000	0.000	0.000	0.000
84	A	146	ALA	0	0.028	0.026	34.537	0.136	0.136	0.000	0.000	0.000	0.000
85	A	147	GLY	0	-0.010	0.006	37.345	0.268	0.268	0.000	0.000	0.000	0.000
86	A	148	ARG	1	0.858	0.914	37.247	7.932	7.932	0.000	0.000	0.000	0.000
87	A	149	THR	0	0.049	0.018	34.970	-0.166	-0.166	0.000	0.000	0.000	0.000
88	A	150	GLN	0	-0.016	0.005	33.362	-0.362	-0.362	0.000	0.000	0.000	0.000
89	A	151	ILE	0	0.001	0.007	28.097	0.023	0.023	0.000	0.000	0.000	0.000
90	A	152	ALA	0	-0.034	-0.028	32.450	0.213	0.213	0.000	0.000	0.000	0.000
91	A	153	PRO	0	-0.007	-0.009	34.996	-0.135	-0.135	0.000	0.000	0.000	0.000
92	A	154	GLY	0	0.030	0.007	36.121	0.265	0.265	0.000	0.000	0.000	0.000
93	A	155	SER	0	-0.015	0.012	35.072	0.044	0.044	0.000	0.000	0.000	0.000
94	A	156	GLN	0	0.022	0.002	29.970	-0.476	-0.476	0.000	0.000	0.000	0.000
95	A	157	THR	0	-0.027	-0.035	29.909	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	158	VAL	0	0.006	-0.015	23.766	-0.097	-0.097	0.000	0.000	0.000	0.000
97	A	159	LEU	0	-0.007	0.018	21.471	0.168	0.168	0.000	0.000	0.000	0.000
98	A	160	GLY	0	0.007	0.003	20.054	-0.422	-0.422	0.000	0.000	0.000	0.000
99	A	161	ILE	0	0.006	-0.002	15.295	0.317	0.317	0.000	0.000	0.000	0.000
100	A	162	GLY	0	0.032	0.029	13.700	-1.154	-1.154	0.000	0.000	0.000	0.000
101	A	163	PRO	0	-0.047	-0.052	11.441	1.673	1.673	0.000	0.000	0.000	0.000
102	A	164	GLY	0	0.025	0.004	9.931	1.466	1.466	0.000	0.000	0.000	0.000
103	A	165	PRO	0	0.023	0.012	6.273	-1.798	-1.798	0.000	0.000	0.000	0.000
104	A	166	ALA	0	0.012	-0.001	6.166	5.072	5.072	0.000	0.000	0.000	0.000
105	A	167	ASP	-1	-0.820	-0.911	7.002	-32.244	-32.244	0.000	0.000	0.000	0.000
106	A	168	LEU	0	-0.021	-0.020	8.797	3.432	3.432	0.000	0.000	0.000	0.000
107	A	169	ILE	0	0.009	0.006	10.514	2.516	2.516	0.000	0.000	0.000	0.000
108	A	170	ASP	-1	-0.816	-0.875	11.222	-23.035	-23.035	0.000	0.000	0.000	0.000
109	A	171	LYS	1	0.925	0.961	12.994	21.315	21.315	0.000	0.000	0.000	0.000
110	A	172	VAL	0	-0.030	0.003	15.033	1.350	1.350	0.000	0.000	0.000	0.000
111	A	173	THR	0	-0.028	-0.048	15.328	0.903	0.903	0.000	0.000	0.000	0.000
112	A	174	GLY	0	0.026	0.022	15.926	0.397	0.397	0.000	0.000	0.000	0.000
113	A	175	HIS	0	-0.024	-0.003	16.598	-0.115	-0.115	0.000	0.000	0.000	0.000
114	A	176	LEU	0	-0.047	-0.012	19.871	0.886	0.886	0.000	0.000	0.000	0.000
115	A	177	LYS	1	0.939	0.969	21.129	11.465	11.465	0.000	0.000	0.000	0.000
116	A	178	LEU	0	0.077	0.029	18.591	-0.099	-0.099	0.000	0.000	0.000	0.000
117	A	179	TYR	-1	-0.856	-0.923	22.434	-11.569	-11.569	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:63:GLY)