FMO DATABASE

FMODB ID: Z74NN

Calculation Name: 1WF7-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1WF7

Chain ID: A

ChEMBL ID:

UniProt ID: Q8CI51

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	103
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-591267.614738
FMO2-HF: Nuclear repulsion	554568.636429
FMO2-HF: Total energy	-36698.978309
FMO2-MP2: Total energy	-36804.017334

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.
35.678	36.784	0.007	-0.581	-0.531	-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 : 0.881 / q_NPA : 0.930

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	-0.020	-0.031	3.492	-7.070	-5.964	0.007	-0.581	-0.531	-0.002
4	A	4	GLY	0	0.047	0.023	5.681	2.612	2.612	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.029	-0.018	9.411	2.113	2.113	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.004	0.012	11.616	0.153	0.153	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.039	0.014	13.881	-1.041	-1.041	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.026	-0.009	15.253	1.047	1.047	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.004	0.005	16.805	-0.859	-0.859	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.002	-0.013	18.296	0.934	0.934	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.031	-0.005	20.561	-0.476	-0.476	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.078	0.025	23.223	0.419	0.419	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.021	-0.027	26.232	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.016	0.016	29.615	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.099	0.040	31.776	0.241	0.241	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.061	-0.008	30.744	-0.288	-0.288	0.000	0.000	0.000	0.000
17	A	17	TRP	0	0.044	0.018	25.558	-0.400	-0.400	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.024	-0.027	26.005	-0.368	-0.368	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.013	0.014	24.143	-0.158	-0.158	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.955	0.983	26.230	10.248	10.248	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.056	0.035	25.961	-0.476	-0.476	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.032	-0.005	27.431	0.158	0.158	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.068	0.015	28.979	-0.390	-0.390	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.009	-0.006	30.959	0.154	0.154	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.938	0.950	32.065	9.340	9.340	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.925	-0.957	34.695	-8.321	-8.321	0.000	0.000	0.000	0.000
27	A	27	PHE	0	-0.002	0.002	33.783	0.075	0.075	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.031	-0.005	34.994	-0.159	-0.159	0.000	0.000	0.000	0.000
29	A	29	MET	0	-0.002	0.042	28.748	-0.066	-0.066	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.024	0.005	25.827	0.107	0.107	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.005	0.002	27.166	0.090	0.090	0.000	0.000	0.000	0.000
32	A	32	THR	0	0.001	-0.003	23.512	-0.516	-0.516	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.021	-0.005	21.169	0.698	0.698	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.028	0.009	24.206	-0.161	-0.161	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.005	-0.020	26.231	0.233	0.233	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.038	-0.028	21.042	-0.064	-0.064	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.940	0.991	25.252	11.215	11.215	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.846	-0.919	24.607	-12.557	-12.557	0.000	0.000	0.000	0.000
39	A	39	GLY	0	-0.013	-0.011	21.920	0.248	0.248	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.032	-0.014	23.000	0.188	0.188	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.918	0.960	21.798	11.387	11.387	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.030	0.012	20.111	-0.651	-0.651	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.025	0.018	18.401	-1.217	-1.217	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.019	-0.016	17.222	-0.560	-0.560	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.014	0.001	15.869	-0.958	-0.958	0.000	0.000	0.000	0.000
46	A	46	HIS	0	-0.034	-0.011	11.693	-2.145	-2.145	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.026	-0.003	14.514	-0.839	-0.839	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.852	0.906	11.421	24.871	24.871	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.019	0.006	18.492	0.338	0.338	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.006	0.004	20.694	-0.435	-0.435	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.844	-0.911	17.302	-19.123	-19.123	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.006	-0.015	19.771	0.877	0.877	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.016	-0.017	20.678	-0.737	-0.737	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.037	-0.016	19.288	0.559	0.559	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.018	-0.014	23.158	0.389	0.389	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.009	-0.002	24.154	-0.516	-0.516	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.811	-0.913	26.351	-10.240	-10.240	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.004	0.007	26.032	0.331	0.331	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.036	-0.014	27.032	0.048	0.048	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.027	-0.010	27.228	-0.451	-0.451	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.027	-0.017	26.405	0.446	0.446	0.000	0.000	0.000	0.000
62	A	62	GLN	0	0.032	0.024	25.058	0.430	0.430	0.000	0.000	0.000	0.000
63	A	63	GLY	0	-0.016	-0.008	29.230	0.258	0.258	0.000	0.000	0.000	0.000
64	A	64	MET	0	-0.018	0.012	30.313	0.403	0.403	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.037	0.010	32.740	-0.215	-0.215	0.000	0.000	0.000	0.000
66	A	66	HIS	0	0.027	0.000	31.590	0.066	0.066	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.004	0.000	33.918	-0.154	-0.154	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.906	-0.952	34.638	-8.931	-8.931	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.031	0.012	29.980	-0.122	-0.122	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.028	-0.024	31.328	-0.297	-0.297	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.022	-0.014	33.132	0.075	0.075	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.869	0.934	31.031	10.052	10.052	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.016	-0.017	28.153	-0.099	-0.099	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.898	0.941	31.073	8.690	8.690	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.009	0.025	34.184	0.220	0.220	0.000	0.000	0.000	0.000
76	A	76	CYS	0	-0.059	0.001	29.866	-0.094	-0.094	0.000	0.000	0.000	0.000
77	A	77	THR	0	0.009	0.001	31.970	-0.099	-0.099	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.034	0.020	31.199	0.041	0.041	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.037	-0.039	25.690	-0.353	-0.353	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.008	0.001	25.376	0.316	0.316	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.028	0.023	22.580	-0.438	-0.438	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.005	0.005	21.850	0.789	0.789	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.015	0.010	18.608	-1.015	-1.015	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.008	0.011	16.683	0.793	0.793	0.000	0.000	0.000	0.000
85	A	85	GLN	0	-0.007	-0.011	17.076	-0.576	-0.576	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.899	0.965	12.451	19.308	19.308	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.038	0.009	14.326	1.290	1.290	0.000	0.000	0.000	0.000
88	A	88	SER	0	0.011	0.007	13.715	-0.490	-0.490	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.015	0.014	8.589	-1.875	-1.875	0.000	0.000	0.000	0.000
90	A	90	ALA	0	0.007	0.003	9.776	1.815	1.815	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.039	-0.031	7.989	-1.385	-1.385	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.951	0.977	10.082	20.793	20.793	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.012	-0.010	11.464	-0.386	-0.386	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.906	-0.949	13.436	-14.677	-14.677	0.000	0.000	0.000	0.000
95	A	95	PRO	0	-0.033	-0.005	17.121	-0.235	-0.235	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.038	0.016	18.815	0.654	0.654	0.000	0.000	0.000	0.000
97	A	97	SER	0	0.009	0.008	21.135	0.189	0.189	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.046	-0.043	24.716	0.156	0.156	0.000	0.000	0.000	0.000
99	A	99	GLY	0	0.000	0.009	27.817	-0.076	-0.076	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.024	-0.006	31.167	-0.062	-0.062	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.007	0.000	33.722	0.010	0.010	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.033	-0.013	36.933	-0.051	-0.051	0.000	0.000	0.000	0.000
103	A	103	GLY	-1	-0.933	-0.959	40.485	-7.199	-7.199	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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