FMO DATABASE

FMODB ID: KK423

Calculation Name: 1WF1-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WF1

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UKM9

Base Structure: SolutionNMR

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	110
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-698817.82836
FMO2-HF: Nuclear repulsion	658079.933137
FMO2-HF: Total energy	-40737.895223
FMO2-MP2: Total energy	-40856.06318

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.
46.038	47.097	-0.015	-0.477	-0.568	-0.002

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 : 0.867 / q_NPA : 0.921

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	0.039	0.019	3.848	1.838	2.897	-0.015	-0.477	-0.568	-0.002
4	A	4	GLY	0	0.027	0.034	7.164	1.059	1.059	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.010	-0.008	10.855	-0.729	-0.729	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.013	0.005	13.856	0.377	0.377	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.001	0.007	15.747	1.178	1.178	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.012	-0.014	16.236	-0.435	-0.435	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.024	-0.005	19.844	0.499	0.499	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.027	0.011	23.117	0.063	0.063	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.938	0.965	26.035	10.940	10.940	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.023	0.027	29.744	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.012	-0.009	32.886	-0.141	-0.141	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.010	0.004	35.456	0.095	0.095	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.019	0.015	38.550	0.009	0.009	0.000	0.000	0.000	0.000
16	A	16	ASN	0	-0.014	-0.022	40.518	0.186	0.186	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.024	0.026	44.166	0.020	0.020	0.000	0.000	0.000	0.000
18	A	18	THR	0	0.001	0.014	46.969	-0.090	-0.090	0.000	0.000	0.000	0.000
19	A	19	ASN	0	0.035	-0.008	46.845	0.045	0.045	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.933	0.962	48.896	5.871	5.871	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.042	0.022	43.444	0.021	0.021	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.900	-0.942	45.691	-6.894	-6.894	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.025	0.004	42.200	-0.121	-0.121	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.952	0.969	41.434	6.546	6.546	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.004	-0.002	40.479	0.029	0.029	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.065	0.044	37.755	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.012	0.000	33.900	-0.127	-0.127	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.012	-0.010	33.615	-0.373	-0.373	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.901	0.971	35.091	7.509	7.509	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.012	0.010	34.684	-0.180	-0.180	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.030	0.016	37.293	0.272	0.272	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.024	-0.019	38.909	-0.180	-0.180	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.093	0.036	40.811	0.252	0.252	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.037	-0.037	42.445	0.062	0.062	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.027	0.034	43.191	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.071	0.024	45.396	0.192	0.192	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.097	-0.031	47.666	0.183	0.183	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.013	-0.003	49.518	0.086	0.086	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.033	-0.016	49.820	0.073	0.073	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.014	0.010	44.481	0.013	0.013	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.975	0.991	47.828	6.053	6.053	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.894	0.928	45.768	6.712	6.712	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.019	-0.007	45.076	-0.150	-0.150	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.825	-0.896	44.586	-6.835	-6.835	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.004	-0.008	40.950	-0.189	-0.189	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.808	-0.911	40.380	-7.555	-7.555	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.022	-0.010	39.744	-0.232	-0.232	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.074	-0.026	37.499	-0.193	-0.193	0.000	0.000	0.000	0.000
49	A	49	PHE	0	0.020	-0.012	35.972	-0.286	-0.286	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.012	-0.008	35.149	-0.314	-0.314	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.927	0.973	32.734	9.024	9.024	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.092	-0.046	29.846	-0.409	-0.409	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.004	-0.001	30.912	-0.291	-0.291	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.934	0.961	33.133	8.003	8.003	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.004	0.016	36.634	-0.101	-0.101	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.031	-0.025	38.458	0.153	0.153	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.028	0.007	40.494	0.205	0.205	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.073	-0.014	42.290	-0.075	-0.075	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.050	-0.038	43.701	0.177	0.177	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.016	0.010	45.945	-0.106	-0.106	0.000	0.000	0.000	0.000
61	A	61	HIS	0	-0.014	0.007	47.727	0.215	0.215	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.938	0.951	49.822	5.788	5.788	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.058	0.024	49.323	0.050	0.050	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.011	0.000	45.103	-0.122	-0.122	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.007	-0.013	43.552	0.156	0.156	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.015	0.020	41.729	-0.141	-0.141	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.010	-0.006	37.931	0.149	0.149	0.000	0.000	0.000	0.000
68	A	68	GLN	0	-0.032	-0.005	38.599	-0.287	-0.287	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.048	0.017	34.185	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.028	0.005	34.345	0.055	0.055	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.014	-0.015	28.565	-0.277	-0.277	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.835	-0.915	29.334	-10.373	-10.373	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.931	0.961	21.534	13.037	13.037	0.000	0.000	0.000	0.000
74	A	74	HIS	0	0.031	0.020	27.661	-0.243	-0.243	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.027	0.023	30.343	0.139	0.139	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.972	0.970	24.963	11.592	11.592	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.022	-0.004	27.270	-0.081	-0.081	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.024	0.002	28.464	0.060	0.060	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.061	-0.028	31.016	0.153	0.153	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.021	-0.029	26.094	0.114	0.114	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.012	0.013	29.752	-0.035	-0.035	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.823	-0.886	30.580	-8.523	-8.523	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.006	-0.004	32.550	0.469	0.469	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.032	0.024	33.050	-0.265	-0.265	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.851	0.934	35.252	8.416	8.416	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.004	0.008	36.706	0.174	0.174	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.015	-0.030	40.307	0.009	0.009	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.050	-0.032	43.324	0.088	0.088	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.028	0.028	45.058	0.134	0.134	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.002	0.008	44.501	-0.080	-0.080	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.013	-0.004	38.097	-0.120	-0.120	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.023	-0.012	38.734	0.130	0.130	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.897	-0.938	38.083	-8.291	-8.291	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.047	-0.029	35.711	0.149	0.149	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.016	-0.005	34.704	-0.435	-0.435	0.000	0.000	0.000	0.000
96	A	96	MET	0	-0.026	-0.010	31.877	-0.103	-0.103	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.011	-0.002	35.018	0.148	0.148	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.024	-0.023	36.941	-0.200	-0.200	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.866	-0.919	38.175	-7.952	-7.952	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.038	-0.017	39.554	0.134	0.134	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.938	0.972	42.367	6.776	6.776	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.002	0.000	45.268	-0.113	-0.113	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.886	-0.955	46.598	-6.151	-6.151	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.870	0.936	46.212	6.398	6.398	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.013	0.006	47.369	0.190	0.190	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.036	0.026	47.500	-0.137	-0.137	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.013	-0.005	45.625	-0.041	-0.041	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.029	-0.021	47.177	0.061	0.061	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.099	-0.060	45.999	-0.161	-0.161	0.000	0.000	0.000	0.000
110	A	110	GLY	-1	-0.887	-0.920	47.959	-6.278	-6.278	0.000	0.000	0.000	0.000

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