FMO DATABASE

FMODB ID: 9R8N2

Calculation Name: 1WG7-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WG7

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BZ29

Base Structure: SolutionNMR

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	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1318773.645287
FMO2-HF: Nuclear repulsion	1259319.789978
FMO2-HF: Total energy	-59453.85531
FMO2-MP2: Total energy	-59624.148621

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:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-41.833	-40.466	-0.017	-0.682	-0.668	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.918

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	3	SER	0	0.028	0.001	3.846	7.788	9.155	-0.017	-0.682	-0.668	-0.004
4	A	4	GLY	0	0.045	0.029	5.999	-1.480	-1.480	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.041	-0.012	7.590	-2.316	-2.316	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.023	-0.016	9.245	1.578	1.578	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.001	0.012	10.953	1.543	1.543	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.003	-0.003	13.010	-0.389	-0.389	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.002	-0.010	16.371	0.158	0.158	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.026	-0.024	19.854	-0.176	-0.176	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.063	0.072	19.686	0.170	0.170	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.032	-0.003	23.747	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.009	0.002	27.274	0.331	0.331	0.000	0.000	0.000	0.000
14	A	14	GLN	0	-0.035	-0.031	31.065	0.021	0.021	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.877	0.937	34.400	7.767	7.767	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.026	0.022	36.691	-0.122	-0.122	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.065	0.028	37.886	-0.147	-0.147	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.059	-0.013	39.359	0.276	0.276	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.028	0.014	39.799	-0.188	-0.188	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.899	0.943	41.606	6.854	6.854	0.000	0.000	0.000	0.000
21	A	21	HIS	0	0.030	0.026	42.133	-0.295	-0.295	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.044	0.017	44.282	0.186	0.186	0.000	0.000	0.000	0.000
23	A	23	TRP	0	-0.066	-0.039	45.690	-0.216	-0.216	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.025	0.028	44.701	0.173	0.173	0.000	0.000	0.000	0.000
25	A	25	TYR	0	-0.043	-0.038	47.219	-0.051	-0.051	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.921	0.976	39.825	7.915	7.915	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.011	-0.013	45.684	0.122	0.122	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.094	-0.062	43.825	-0.275	-0.275	0.000	0.000	0.000	0.000
29	A	29	MET	0	0.031	0.039	44.220	-0.091	-0.091	0.000	0.000	0.000	0.000
30	A	30	ASN	0	-0.071	-0.042	45.245	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.045	0.032	47.940	0.061	0.061	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.042	0.029	50.989	0.112	0.112	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.066	0.016	52.692	-0.110	-0.110	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.048	0.002	53.518	-0.080	-0.080	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.017	-0.004	48.798	-0.072	-0.072	0.000	0.000	0.000	0.000
36	A	36	THR	0	0.025	0.016	49.017	-0.197	-0.197	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.030	-0.017	48.804	-0.110	-0.110	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.930	0.959	46.907	6.778	6.778	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.022	-0.007	49.324	-0.045	-0.045	0.000	0.000	0.000	0.000
40	A	40	PHE	0	0.020	0.015	49.551	-0.085	-0.085	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.976	0.998	46.808	6.634	6.634	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.798	0.904	47.358	6.072	6.072	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.885	0.933	42.036	7.241	7.241	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.052	0.047	41.709	0.115	0.115	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.020	-0.026	41.251	-0.237	-0.237	0.000	0.000	0.000	0.000
46	A	46	HIS	0	0.029	0.001	36.882	0.035	0.035	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.053	-0.020	37.387	-0.163	-0.163	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.027	-0.012	32.143	0.159	0.159	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.021	0.021	31.837	0.145	0.145	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.064	-0.043	27.683	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.062	0.033	26.234	0.241	0.241	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.890	-0.961	25.298	-12.588	-12.588	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.087	0.061	27.192	0.222	0.222	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.036	0.029	28.422	0.437	0.437	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.044	-0.061	31.352	0.109	0.109	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.054	0.018	29.997	0.034	0.034	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.051	-0.009	33.895	0.223	0.223	0.000	0.000	0.000	0.000
58	A	58	ASN	0	0.056	0.021	32.312	-0.120	-0.120	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.006	0.011	36.313	0.302	0.302	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.057	0.028	34.197	-0.100	-0.100	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.828	0.909	39.723	7.989	7.989	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.839	-0.943	42.348	-7.128	-7.128	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.826	-0.908	42.370	-6.831	-6.831	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.867	0.947	41.461	7.107	7.107	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.050	0.013	37.435	-0.109	-0.109	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.024	0.003	34.446	-0.072	-0.072	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.955	0.975	32.824	8.239	8.239	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.840	-0.922	29.467	-10.679	-10.679	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.076	-0.028	32.160	0.354	0.354	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.811	0.890	34.714	8.326	8.326	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.036	0.012	33.939	-0.036	-0.036	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.014	0.002	31.359	0.063	0.063	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.035	-0.018	33.679	-0.027	-0.027	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.080	0.032	29.687	0.088	0.088	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.017	-0.022	32.715	0.159	0.159	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.850	-0.924	29.625	-10.152	-10.152	0.000	0.000	0.000	0.000
77	A	77	SER	0	0.008	0.017	31.130	0.009	0.009	0.000	0.000	0.000	0.000
78	A	78	CYS	0	-0.107	-0.052	33.541	0.265	0.265	0.000	0.000	0.000	0.000
79	A	79	MET	0	0.002	0.005	37.240	0.073	0.073	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.032	0.008	39.715	0.134	0.134	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.060	-0.019	43.031	-0.040	-0.040	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.013	0.002	45.423	0.151	0.151	0.000	0.000	0.000	0.000
83	A	83	GLN	0	0.048	0.008	48.495	0.053	0.053	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.047	-0.030	49.282	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.018	0.007	52.690	0.182	0.182	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.944	0.948	55.574	5.579	5.579	0.000	0.000	0.000	0.000
87	A	87	VAL	0	-0.022	0.007	51.928	0.069	0.069	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.987	0.975	54.752	5.718	5.718	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.986	0.994	55.721	5.183	5.183	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.050	0.036	54.574	0.013	0.013	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.008	-0.009	51.457	-0.118	-0.118	0.000	0.000	0.000	0.000
92	A	92	PHE	0	0.021	-0.002	45.710	0.111	0.111	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.781	-0.866	44.935	-7.048	-7.048	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.020	0.000	41.010	0.036	0.036	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.873	0.921	41.491	6.942	6.942	0.000	0.000	0.000	0.000
96	A	96	MET	0	0.023	0.025	34.297	-0.109	-0.109	0.000	0.000	0.000	0.000
97	A	97	GLN	0	0.060	0.018	31.213	0.363	0.363	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.955	-0.961	31.445	-10.205	-10.205	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.883	0.928	33.997	8.441	8.441	0.000	0.000	0.000	0.000
100	A	100	SER	0	0.023	0.012	36.965	0.154	0.154	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.027	-0.042	38.798	0.028	0.028	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.011	0.006	35.594	0.090	0.090	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.017	-0.009	42.408	0.117	0.117	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.018	0.016	42.777	-0.073	-0.073	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.001	-0.003	46.839	0.147	0.147	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.026	0.024	49.887	-0.102	-0.102	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.792	-0.891	51.964	-5.788	-5.788	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.051	-0.039	54.833	0.173	0.173	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.942	-0.968	54.858	-5.486	-5.486	0.000	0.000	0.000	0.000
110	A	110	VAL	0	0.113	0.062	54.069	-0.103	-0.103	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.904	-0.961	51.044	-6.258	-6.258	0.000	0.000	0.000	0.000
112	A	112	MET	0	-0.066	-0.020	50.027	-0.143	-0.143	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.924	-0.968	50.113	-5.978	-5.978	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.864	-0.915	49.118	-6.441	-6.441	0.000	0.000	0.000	0.000
115	A	115	TRP	0	0.007	-0.010	41.971	-0.191	-0.191	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.026	-0.011	45.473	-0.152	-0.152	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.013	-0.010	46.360	-0.103	-0.103	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.045	-0.028	42.254	-0.105	-0.105	0.000	0.000	0.000	0.000
119	A	119	LEU	0	0.004	0.008	40.243	-0.174	-0.174	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.052	0.009	41.518	-0.250	-0.250	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.931	0.981	42.713	6.822	6.822	0.000	0.000	0.000	0.000
122	A	122	ILE	0	0.024	0.017	36.671	-0.071	-0.071	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.049	-0.023	38.022	-0.139	-0.139	0.000	0.000	0.000	0.000
124	A	124	GLN	0	-0.020	-0.012	38.796	-0.049	-0.049	0.000	0.000	0.000	0.000
125	A	125	LEU	0	0.000	-0.016	38.649	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	126	ASN	0	0.038	0.034	34.526	-0.262	-0.262	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.034	-0.002	34.694	-0.221	-0.221	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.980	-0.998	36.319	-7.661	-7.661	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.030	0.017	33.417	-0.063	-0.063	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.053	0.034	31.405	-0.247	-0.247	0.000	0.000	0.000	0.000
131	A	131	MET	0	-0.105	-0.066	31.801	-0.251	-0.251	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.053	-0.032	33.865	-0.113	-0.113	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.845	-0.924	28.312	-10.680	-10.680	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.900	0.968	28.626	9.779	9.779	0.000	0.000	0.000	0.000
135	A	135	ARG	1	0.808	0.890	29.645	8.974	8.974	0.000	0.000	0.000	0.000
136	A	136	ASN	0	-0.023	-0.007	29.853	0.535	0.535	0.000	0.000	0.000	0.000
137	A	137	GLY	0	0.016	0.021	26.547	-0.205	-0.205	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.957	-0.979	26.399	-10.886	-10.886	0.000	0.000	0.000	0.000
139	A	139	SER	0	-0.053	-0.024	25.787	0.422	0.422	0.000	0.000	0.000	0.000
140	A	140	HIS	0	-0.030	-0.017	24.052	-0.447	-0.447	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.861	-0.932	25.192	-10.789	-10.789	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-1.019	-1.001	24.378	-11.293	-11.293	0.000	0.000	0.000	0.000
143	A	143	ASP	-1	-0.941	-0.951	21.302	-13.762	-13.762	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.929	-0.971	20.806	-14.942	-14.942	0.000	0.000	0.000	0.000
145	A	145	SER	0	-0.070	-0.052	23.736	0.744	0.744	0.000	0.000	0.000	0.000
146	A	146	GLY	0	-0.060	-0.016	24.381	-0.262	-0.262	0.000	0.000	0.000	0.000
147	A	147	PRO	0	0.041	0.037	20.697	-0.163	-0.163	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.011	-0.030	20.342	-0.627	-0.627	0.000	0.000	0.000	0.000
149	A	149	SER	0	-0.091	-0.054	22.459	0.430	0.430	0.000	0.000	0.000	0.000
150	A	150	GLY	-1	-0.934	-0.939	23.982	-12.885	-12.885	0.000	0.000	0.000	0.000

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