FMO DATABASE

FMODB ID: VZ7J1

Calculation Name: 1WJ5-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WJ5

Chain ID: A

ChEMBL ID:

UniProt ID: Q8K2X3

Base Structure: SolutionNMR

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-883092.397502
FMO2-HF: Nuclear repulsion	837676.94567
FMO2-HF: Total energy	-45415.451832
FMO2-MP2: Total energy	-45549.47458

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.
-18.171	-17.447	-0.001	-0.384	-0.338	-0.001

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 : 0.856 / q_NPA : 0.916

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	0.026	0.020	3.844	-4.163	-3.439	-0.001	-0.384	-0.338	-0.001
4	A	4	GLY	0	0.028	0.023	6.784	2.448	2.448	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.044	-0.043	9.139	1.979	1.979	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.005	0.003	12.829	0.609	0.609	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.061	0.049	14.893	0.707	0.707	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.046	-0.031	17.923	-0.720	-0.720	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.862	0.918	20.391	14.670	14.670	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.785	-0.882	22.747	-13.349	-13.349	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.043	-0.010	23.632	-0.833	-0.833	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.036	-0.027	23.036	0.366	0.366	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.760	-0.885	25.889	-11.583	-11.583	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.018	0.000	28.740	-0.164	-0.164	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.020	0.039	29.266	0.005	0.005	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.051	0.020	25.300	-0.228	-0.228	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.045	-0.024	25.123	-0.452	-0.452	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.030	-0.046	27.171	0.010	0.010	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.004	-0.002	24.203	0.058	0.058	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.023	-0.003	21.756	-0.282	-0.282	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.010	-0.013	24.743	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.004	0.000	27.003	0.097	0.097	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.794	-0.873	22.496	-13.621	-13.621	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.956	0.964	23.839	12.978	12.978	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.028	0.019	27.228	0.238	0.238	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.876	0.936	22.675	13.872	13.872	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.953	-0.982	23.510	-13.291	-13.291	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.020	0.000	27.617	0.247	0.247	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.001	-0.003	31.180	0.273	0.273	0.000	0.000	0.000	0.000
30	A	30	GLN	0	-0.023	-0.005	26.234	0.182	0.182	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.946	-0.965	30.175	-10.259	-10.259	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.874	0.935	31.509	9.420	9.420	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.828	0.926	30.334	10.543	10.543	0.000	0.000	0.000	0.000
34	A	34	MET	0	0.004	0.014	35.329	0.336	0.336	0.000	0.000	0.000	0.000
35	A	35	GLN	0	0.034	-0.003	35.952	-0.264	-0.264	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.029	-0.021	38.279	0.056	0.056	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.003	0.010	34.999	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.114	0.050	40.164	0.014	0.014	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.028	-0.029	37.476	-0.089	-0.089	0.000	0.000	0.000	0.000
40	A	40	GLN	0	0.006	-0.007	38.917	-0.099	-0.099	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.870	-0.936	39.967	-7.422	-7.422	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.054	-0.021	34.207	-0.138	-0.138	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.804	-0.911	36.682	-8.490	-8.490	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.045	-0.024	38.861	0.035	0.035	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.017	0.006	34.058	-0.030	-0.030	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.831	-0.918	35.223	-8.732	-8.732	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.053	-0.031	30.497	-0.146	-0.146	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.053	-0.013	30.255	-0.464	-0.464	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.057	0.028	32.157	-0.178	-0.178	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.032	-0.016	31.117	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.098	-0.052	25.779	-0.393	-0.393	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.011	-0.004	30.040	-0.035	-0.035	0.000	0.000	0.000	0.000
53	A	53	SER	0	0.021	0.003	32.949	0.299	0.299	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.866	0.955	26.232	11.673	11.673	0.000	0.000	0.000	0.000
55	A	55	PRO	0	-0.003	0.006	30.016	0.166	0.166	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.015	0.001	29.577	-0.401	-0.401	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.028	0.002	29.707	0.087	0.087	0.000	0.000	0.000	0.000
58	A	58	HIS	0	0.003	-0.004	32.383	0.115	0.115	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.003	-0.010	35.989	-0.086	-0.086	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.007	0.000	39.028	0.102	0.102	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.016	0.018	42.239	-0.065	-0.065	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.005	-0.004	42.804	0.070	0.070	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.905	-0.951	42.862	-7.418	-7.418	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.053	-0.039	44.727	0.206	0.206	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.007	-0.002	46.449	0.168	0.168	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.978	-0.992	46.941	-6.777	-6.777	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.029	0.004	45.213	-0.106	-0.106	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.904	0.937	48.453	6.072	6.072	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.791	-0.893	46.890	-6.835	-6.835	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.118	-0.062	48.071	0.072	0.072	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.028	0.028	45.256	-0.086	-0.086	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.047	-0.029	38.662	-0.033	-0.033	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.067	0.033	40.541	-0.118	-0.118	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.076	0.038	40.552	-0.127	-0.127	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.022	-0.003	36.399	-0.102	-0.102	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.082	0.057	36.209	-0.218	-0.218	0.000	0.000	0.000	0.000
77	A	77	GLN	0	0.058	0.033	36.782	-0.106	-0.106	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.798	0.913	37.329	7.759	7.759	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.028	0.025	31.558	-0.138	-0.138	0.000	0.000	0.000	0.000
80	A	80	PHE	0	0.061	-0.007	33.446	-0.278	-0.278	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.906	0.954	35.051	7.955	7.955	0.000	0.000	0.000	0.000
82	A	82	ASN	0	0.002	0.002	33.253	0.137	0.137	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.000	0.004	30.788	-0.227	-0.227	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.004	-0.004	31.310	-0.274	-0.274	0.000	0.000	0.000	0.000
85	A	85	GLN	0	-0.012	-0.002	33.748	-0.265	-0.265	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.050	0.012	27.601	-0.134	-0.134	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.064	-0.021	28.452	-0.320	-0.320	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.027	-0.010	30.722	0.163	0.163	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.968	-0.970	29.840	-10.183	-10.183	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.797	0.881	24.157	12.651	12.651	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.002	0.018	28.201	-0.231	-0.231	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.048	-0.023	26.039	0.019	0.019	0.000	0.000	0.000	0.000
93	A	93	VAL	0	-0.016	-0.029	30.482	0.189	0.189	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.007	-0.003	34.074	0.018	0.018	0.000	0.000	0.000	0.000
95	A	95	GLN	0	0.026	0.011	37.252	0.172	0.172	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.892	0.958	40.803	7.004	7.004	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.869	-0.925	43.768	-6.663	-6.663	0.000	0.000	0.000	0.000
98	A	98	SER	0	0.016	-0.007	44.579	-0.174	-0.174	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.015	-0.005	44.585	0.194	0.194	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.029	-0.022	42.859	-0.093	-0.093	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.924	-0.939	43.139	-7.042	-7.042	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.845	0.915	43.629	7.005	7.005	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.050	-0.003	41.286	-0.117	-0.117	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.045	0.014	37.147	-0.088	-0.088	0.000	0.000	0.000	0.000
105	A	105	TYR	0	0.000	-0.007	38.744	0.047	0.047	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.027	-0.014	32.576	-0.229	-0.229	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.005	-0.006	30.728	0.003	0.003	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.049	-0.036	31.899	0.034	0.034	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.863	0.944	29.256	9.992	9.992	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.802	-0.885	31.960	-8.247	-8.247	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.820	0.906	35.242	7.853	7.853	0.000	0.000	0.000	0.000
112	A	112	ASP	-1	-0.774	-0.873	34.579	-9.199	-9.199	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.047	-0.022	38.036	0.205	0.205	0.000	0.000	0.000	0.000
114	A	114	GLN	0	-0.012	-0.005	38.473	-0.195	-0.195	0.000	0.000	0.000	0.000
115	A	115	SER	0	0.022	0.002	36.297	0.157	0.157	0.000	0.000	0.000	0.000
116	A	116	GLY	0	-0.009	-0.006	38.509	0.063	0.063	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.017	-0.009	41.202	0.132	0.132	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.014	-0.013	43.880	0.119	0.119	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.024	-0.014	46.856	0.022	0.022	0.000	0.000	0.000	0.000
120	A	120	GLY	-1	-0.949	-0.953	49.346	-6.209	-6.209	0.000	0.000	0.000	0.000

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