FMO DATABASE

FMODB ID: NLQNQ

Calculation Name: 4HWD-D-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4HWD

Chain ID: D

ChEMBL ID:

UniProt ID: Q0WPX7

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-589683.167064
FMO2-HF: Nuclear repulsion	554590.508816
FMO2-HF: Total energy	-35092.658247
FMO2-MP2: Total energy	-35193.624551

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:133:GLY)

Summations of interaction energy for fragment #1(A:133: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.
18.619	21.217	4.111	-3.206	-3.503	-0.038

Interaction energy analysis for fragmet #1(A:133:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.894 / q_NPA : 0.938

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	135	GLY	0	0.060	0.046	3.876	5.791	6.468	-0.002	-0.254	-0.421	-0.001
4	A	136	SER	0	0.036	-0.003	2.044	-16.127	-15.332	4.095	-2.475	-2.415	-0.035
5	A	137	SER	0	0.007	0.005	2.946	4.976	5.976	0.019	-0.468	-0.551	-0.002
6	A	138	SER	0	0.011	-0.016	5.179	8.982	9.108	-0.001	-0.009	-0.116	0.000
7	A	139	LYS	1	0.784	0.890	6.724	32.246	32.246	0.000	0.000	0.000	0.000
8	A	140	ALA	0	0.058	0.035	7.241	3.690	3.690	0.000	0.000	0.000	0.000
9	A	141	ILE	0	0.042	0.021	8.935	3.297	3.297	0.000	0.000	0.000	0.000
10	A	142	SER	0	-0.044	0.006	11.114	3.366	3.366	0.000	0.000	0.000	0.000
11	A	143	ASP	-1	-0.811	-0.899	10.856	-25.383	-25.383	0.000	0.000	0.000	0.000
12	A	144	ILE	0	0.006	0.011	12.143	1.677	1.677	0.000	0.000	0.000	0.000
13	A	145	SER	0	-0.053	-0.054	14.931	1.735	1.735	0.000	0.000	0.000	0.000
14	A	146	PHE	0	0.027	0.019	16.843	1.335	1.335	0.000	0.000	0.000	0.000
15	A	147	GLN	0	0.008	0.001	18.003	0.941	0.941	0.000	0.000	0.000	0.000
16	A	148	VAL	0	0.002	-0.007	18.399	0.948	0.948	0.000	0.000	0.000	0.000
17	A	149	GLU	-1	-0.946	-0.971	20.949	-13.876	-13.876	0.000	0.000	0.000	0.000
18	A	150	ARG	1	0.910	0.961	21.865	14.039	14.039	0.000	0.000	0.000	0.000
19	A	151	LEU	0	-0.033	-0.009	21.902	0.563	0.563	0.000	0.000	0.000	0.000
20	A	152	ALA	0	0.025	0.016	25.187	0.552	0.552	0.000	0.000	0.000	0.000
21	A	153	GLY	0	-0.006	0.002	27.097	0.510	0.510	0.000	0.000	0.000	0.000
22	A	154	GLN	0	-0.033	-0.013	28.606	0.375	0.375	0.000	0.000	0.000	0.000
23	A	155	LEU	0	0.021	0.008	28.525	0.348	0.348	0.000	0.000	0.000	0.000
24	A	156	SER	0	-0.002	0.004	30.967	0.484	0.484	0.000	0.000	0.000	0.000
25	A	157	ALA	0	0.005	0.011	33.112	0.358	0.358	0.000	0.000	0.000	0.000
26	A	158	PHE	0	0.009	-0.008	32.100	0.280	0.280	0.000	0.000	0.000	0.000
27	A	159	ASP	-1	-0.889	-0.942	34.959	-8.542	-8.542	0.000	0.000	0.000	0.000
28	A	160	THR	0	-0.062	-0.045	36.738	0.362	0.362	0.000	0.000	0.000	0.000
29	A	161	VAL	0	-0.018	-0.001	38.891	0.285	0.285	0.000	0.000	0.000	0.000
30	A	162	ILE	0	0.056	0.034	37.467	0.249	0.249	0.000	0.000	0.000	0.000
31	A	163	GLY	0	-0.027	-0.010	40.611	0.208	0.208	0.000	0.000	0.000	0.000
32	A	164	LYS	1	0.839	0.904	42.140	7.634	7.634	0.000	0.000	0.000	0.000
33	A	165	GLY	0	-0.004	0.014	44.791	0.161	0.161	0.000	0.000	0.000	0.000
34	A	166	GLY	0	-0.008	0.011	44.257	0.126	0.126	0.000	0.000	0.000	0.000
35	A	167	LYS	1	0.871	0.921	43.115	7.282	7.282	0.000	0.000	0.000	0.000
36	A	168	VAL	0	-0.001	-0.004	36.671	-0.050	-0.050	0.000	0.000	0.000	0.000
37	A	169	GLU	-1	-0.875	-0.928	38.733	-8.199	-8.199	0.000	0.000	0.000	0.000
38	A	170	GLU	-1	-0.751	-0.889	37.114	-8.895	-8.895	0.000	0.000	0.000	0.000
39	A	171	LYS	1	0.935	0.959	34.973	8.514	8.514	0.000	0.000	0.000	0.000
40	A	172	ASN	0	-0.018	-0.011	33.379	-0.473	-0.473	0.000	0.000	0.000	0.000
41	A	173	LEU	0	-0.003	0.005	32.093	-0.395	-0.395	0.000	0.000	0.000	0.000
42	A	174	GLU	-1	-0.889	-0.937	31.249	-9.553	-9.553	0.000	0.000	0.000	0.000
43	A	175	ASN	0	-0.036	-0.032	29.298	-0.158	-0.158	0.000	0.000	0.000	0.000
44	A	176	LEU	0	-0.008	-0.001	26.970	-0.512	-0.512	0.000	0.000	0.000	0.000
45	A	177	MET	0	0.022	0.020	26.508	-0.724	-0.724	0.000	0.000	0.000	0.000
46	A	178	GLU	-1	-0.897	-0.935	23.246	-14.191	-14.191	0.000	0.000	0.000	0.000
47	A	179	MET	0	0.019	0.002	23.000	-0.738	-0.738	0.000	0.000	0.000	0.000
48	A	180	LEU	0	-0.010	-0.012	21.611	-0.952	-0.952	0.000	0.000	0.000	0.000
49	A	181	MET	0	0.041	0.018	20.970	-0.877	-0.877	0.000	0.000	0.000	0.000
50	A	182	ASN	0	-0.076	-0.036	18.797	-1.889	-1.889	0.000	0.000	0.000	0.000
51	A	183	GLN	0	-0.002	-0.019	16.906	-2.197	-2.197	0.000	0.000	0.000	0.000
52	A	184	LEU	0	0.015	0.016	15.979	-1.334	-1.334	0.000	0.000	0.000	0.000
53	A	185	VAL	0	0.021	0.003	16.051	-1.028	-1.028	0.000	0.000	0.000	0.000
54	A	186	LYS	1	0.871	0.944	13.229	17.681	17.681	0.000	0.000	0.000	0.000
55	A	187	LEU	0	-0.038	-0.020	11.584	-2.646	-2.646	0.000	0.000	0.000	0.000
56	A	188	ASP	-1	-0.878	-0.943	11.479	-21.772	-21.772	0.000	0.000	0.000	0.000
57	A	189	ALA	0	-0.047	-0.007	10.894	-0.535	-0.535	0.000	0.000	0.000	0.000
58	A	190	ILE	0	-0.095	-0.032	6.172	-4.782	-4.782	0.000	0.000	0.000	0.000
59	A	191	SER	0	-0.004	0.005	5.742	0.323	0.323	0.000	0.000	0.000	0.000
60	A	192	GLY	0	0.004	-0.020	5.525	-7.988	-7.988	0.000	0.000	0.000	0.000
61	A	193	ASP	-1	-0.890	-0.962	7.384	-24.303	-24.303	0.000	0.000	0.000	0.000
62	A	194	GLY	0	0.024	0.007	10.060	-1.189	-1.189	0.000	0.000	0.000	0.000
63	A	195	ASP	-1	-0.816	-0.910	12.403	-22.019	-22.019	0.000	0.000	0.000	0.000
64	A	196	VAL	0	-0.011	0.017	7.130	0.507	0.507	0.000	0.000	0.000	0.000
65	A	197	LYS	1	1.000	0.999	10.477	20.806	20.806	0.000	0.000	0.000	0.000
66	A	198	LEU	0	-0.055	-0.010	12.703	1.694	1.694	0.000	0.000	0.000	0.000
67	A	199	LYS	1	0.864	0.896	13.238	22.694	22.694	0.000	0.000	0.000	0.000
68	A	200	LYS	1	0.875	0.935	11.772	22.784	22.784	0.000	0.000	0.000	0.000
69	A	201	LYS	1	0.917	0.956	13.890	15.941	15.941	0.000	0.000	0.000	0.000
70	A	202	MET	0	-0.019	-0.005	17.159	0.943	0.943	0.000	0.000	0.000	0.000
71	A	203	GLN	0	0.019	-0.006	16.036	1.847	1.847	0.000	0.000	0.000	0.000
72	A	204	GLU	-1	-0.762	-0.882	16.992	-17.078	-17.078	0.000	0.000	0.000	0.000
73	A	205	GLU	-1	-0.928	-0.938	18.790	-13.096	-13.096	0.000	0.000	0.000	0.000
74	A	206	ARG	1	0.898	0.954	21.249	14.919	14.919	0.000	0.000	0.000	0.000
75	A	207	LEU	0	0.010	0.001	18.392	0.555	0.555	0.000	0.000	0.000	0.000
76	A	208	HIS	1	0.831	0.922	20.735	15.065	15.065	0.000	0.000	0.000	0.000
77	A	209	LYS	1	1.055	1.037	24.574	11.412	11.412	0.000	0.000	0.000	0.000
78	A	210	TYR	0	-0.055	-0.045	23.956	0.302	0.302	0.000	0.000	0.000	0.000
79	A	211	VAL	0	0.024	0.014	24.737	0.283	0.283	0.000	0.000	0.000	0.000
80	A	212	GLU	-1	-0.867	-0.940	27.510	-10.976	-10.976	0.000	0.000	0.000	0.000
81	A	213	ALA	0	-0.043	-0.029	30.081	0.405	0.405	0.000	0.000	0.000	0.000
82	A	214	LEU	0	-0.016	-0.007	28.933	0.328	0.328	0.000	0.000	0.000	0.000
83	A	215	ASP	-1	-0.869	-0.941	31.059	-10.028	-10.028	0.000	0.000	0.000	0.000
84	A	216	LEU	0	-0.040	-0.027	33.471	0.367	0.367	0.000	0.000	0.000	0.000
85	A	217	LEU	0	-0.045	-0.017	33.693	0.305	0.305	0.000	0.000	0.000	0.000
86	A	218	LYS	1	0.870	0.932	33.227	9.538	9.538	0.000	0.000	0.000	0.000
87	A	219	ILE	0	-0.004	0.008	37.047	0.249	0.249	0.000	0.000	0.000	0.000
88	A	220	LYS	1	0.846	0.929	39.351	7.876	7.876	0.000	0.000	0.000	0.000
89	A	221	ASN	0	-0.053	-0.032	39.377	0.318	0.318	0.000	0.000	0.000	0.000
90	A	222	SER	-1	-0.950	-0.958	40.574	-7.332	-7.332	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:133:GLY)