FMO DATABASE

FMODB ID: 3K1VL

Calculation Name: 1X5O-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X5O

Chain ID: A

ChEMBL ID:

UniProt ID: P29558

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-776472.173466
FMO2-HF: Nuclear repulsion	733155.450221
FMO2-HF: Total energy	-43316.723245
FMO2-MP2: Total energy	-43439.340303

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.
-21.626	-18.945	0.139	-1.264	-1.555	-0.009

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 : 0.875 / q_NPA : 0.922

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	-0.033	-0.004	2.913	-4.352	-1.835	0.140	-1.247	-1.410	-0.009
4	A	4	GLY	0	0.061	0.044	4.282	3.478	3.642	-0.001	-0.017	-0.145	0.000
5	A	5	SER	0	-0.017	-0.025	7.468	2.234	2.234	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.010	0.005	10.663	0.425	0.425	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.021	0.024	14.233	1.104	1.104	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.020	-0.021	16.338	0.169	0.169	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.969	0.994	19.583	16.183	16.183	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.019	0.000	21.407	0.224	0.224	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.009	-0.012	25.223	-0.083	-0.083	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.034	0.010	28.056	0.214	0.214	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.039	-0.005	28.414	0.189	0.189	0.000	0.000	0.000	0.000
14	A	14	GLN	0	-0.013	-0.004	31.430	0.343	0.343	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.046	0.016	33.362	-0.080	-0.080	0.000	0.000	0.000	0.000
16	A	16	GLN	0	0.002	0.005	35.440	-0.037	-0.037	0.000	0.000	0.000	0.000
17	A	17	MET	0	0.015	0.013	35.034	-0.058	-0.058	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.002	0.004	37.460	0.087	0.087	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.906	0.935	37.794	8.098	8.098	0.000	0.000	0.000	0.000
20	A	20	GLN	0	0.025	0.021	37.962	-0.177	-0.177	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.039	-0.017	31.609	-0.194	-0.194	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.836	-0.907	35.652	-8.171	-8.171	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.057	-0.045	34.010	-0.333	-0.333	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.818	-0.873	31.461	-9.907	-9.907	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.033	-0.012	29.907	-0.395	-0.395	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.000	-0.042	29.726	-0.324	-0.324	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.014	-0.004	24.238	-0.482	-0.482	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.036	0.017	23.193	0.068	0.068	0.000	0.000	0.000	0.000
29	A	29	TYR	0	-0.019	-0.023	16.960	-0.018	-0.018	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.039	0.016	17.258	-0.120	-0.120	0.000	0.000	0.000	0.000
31	A	31	SER	0	-0.044	-0.044	13.735	-0.442	-0.442	0.000	0.000	0.000	0.000
32	A	32	ASN	0	0.003	0.010	10.513	1.038	1.038	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.025	0.007	11.537	0.242	0.242	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.022	0.009	8.916	-3.107	-3.107	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.001	-0.024	4.974	1.524	1.524	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.042	-0.025	9.195	1.869	1.869	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.021	0.016	11.800	1.147	1.147	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.839	-0.919	14.438	-16.588	-16.588	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.872	-0.959	17.875	-14.526	-14.526	0.000	0.000	0.000	0.000
40	A	40	GLN	0	0.002	0.016	20.837	0.651	0.651	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.865	-0.934	17.783	-15.023	-15.023	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.049	-0.032	18.383	0.110	0.110	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.884	-0.946	20.294	-11.197	-11.197	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.070	-0.052	22.156	1.052	1.052	0.000	0.000	0.000	0.000
45	A	45	MET	0	-0.046	0.001	19.024	0.109	0.109	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.009	-0.007	22.865	0.279	0.279	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.966	0.986	25.500	11.607	11.607	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.075	-0.025	26.575	0.441	0.441	0.000	0.000	0.000	0.000
49	A	49	PHE	0	-0.035	-0.004	24.941	0.160	0.160	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.008	-0.029	29.434	0.421	0.421	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.014	0.022	30.637	-0.350	-0.350	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.001	-0.004	26.256	-0.070	-0.070	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.050	-0.016	29.551	0.219	0.219	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.020	-0.017	27.797	0.021	0.021	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.015	0.013	22.511	-0.126	-0.126	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.974	0.988	20.842	13.789	13.789	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.056	0.028	15.095	-0.339	-0.339	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.056	-0.018	15.474	0.626	0.626	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.868	0.921	14.710	15.114	15.114	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.801	-0.901	11.480	-24.720	-24.720	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.000	-0.013	14.537	0.558	0.558	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.022	-0.003	14.081	1.346	1.346	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.017	0.018	16.063	0.551	0.551	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.031	-0.018	9.561	0.322	0.322	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.031	0.025	11.266	0.577	0.577	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.830	0.893	10.245	20.002	20.002	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.038	0.029	9.802	-0.917	-0.917	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.037	-0.023	10.680	0.772	0.772	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.002	-0.008	14.346	0.090	0.090	0.000	0.000	0.000	0.000
70	A	70	PHE	0	-0.055	-0.014	17.665	0.111	0.111	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.039	0.008	21.356	0.037	0.037	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.933	0.990	24.151	10.325	10.325	0.000	0.000	0.000	0.000
73	A	73	MET	0	0.020	0.011	27.522	-0.048	-0.048	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.861	-0.955	29.811	-8.998	-8.998	0.000	0.000	0.000	0.000
75	A	75	SER	0	0.015	-0.001	32.981	0.235	0.235	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.048	0.007	32.243	-0.315	-0.315	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.903	-0.943	32.479	-8.836	-8.836	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.844	0.935	30.700	9.358	9.358	0.000	0.000	0.000	0.000
79	A	79	CYS	0	-0.065	-0.019	28.243	-0.355	-0.355	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.904	-0.946	27.895	-9.984	-9.984	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.013	0.000	28.774	-0.278	-0.278	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.004	-0.004	24.084	-0.301	-0.301	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.024	-0.017	24.028	-0.564	-0.564	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.019	-0.015	24.236	-0.414	-0.414	0.000	0.000	0.000	0.000
85	A	85	HIS	0	-0.024	-0.001	24.938	-0.232	-0.232	0.000	0.000	0.000	0.000
86	A	86	PHE	0	-0.009	-0.048	19.704	-0.577	-0.577	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.052	-0.005	19.526	-1.527	-1.527	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.043	0.032	17.893	0.463	0.463	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.893	0.956	18.813	14.052	14.052	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.016	0.003	12.685	-0.707	-0.707	0.000	0.000	0.000	0.000
91	A	91	ILE	0	-0.005	0.006	15.352	1.048	1.048	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.920	0.949	15.610	13.684	13.684	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.026	0.012	13.034	-0.136	-0.136	0.000	0.000	0.000	0.000
94	A	94	PRO	0	0.045	0.027	16.354	0.596	0.596	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.002	-0.007	17.313	-0.888	-0.888	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.020	0.008	17.028	0.452	0.452	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.024	-0.004	12.404	-1.160	-1.160	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.034	-0.014	9.322	0.377	0.377	0.000	0.000	0.000	0.000
99	A	99	ALA	0	0.021	0.012	10.867	-0.800	-0.800	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.009	-0.003	8.713	-2.834	-2.834	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.022	-0.009	6.854	0.290	0.290	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-1.008	-0.985	6.977	-34.932	-34.932	0.000	0.000	0.000	0.000
103	A	103	PRO	0	-0.019	0.000	10.269	0.569	0.569	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.010	-0.007	13.219	-1.146	-1.146	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.011	0.000	15.288	1.000	1.000	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.003	-0.008	16.852	0.095	0.095	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.925	0.981	19.680	15.932	15.932	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.089	0.036	23.106	-0.242	-0.242	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.072	-0.024	23.451	-0.439	-0.439	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.023	0.015	25.106	0.415	0.415	0.000	0.000	0.000	0.000
111	A	111	PRO	0	0.025	0.025	27.138	-0.377	-0.377	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.041	-0.040	25.952	-0.406	-0.406	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.123	-0.072	28.239	-0.151	-0.151	0.000	0.000	0.000	0.000
114	A	114	GLY	-1	-0.877	-0.913	30.891	-9.335	-9.335	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)