FMO DATABASE

FMODB ID: ZZV7N

Calculation Name: 1X5B-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X5B

Chain ID: A

ChEMBL ID:

UniProt ID: O75886

Base Structure: SolutionNMR

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	163
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1479750.460986
FMO2-HF: Nuclear repulsion	1415964.933614
FMO2-HF: Total energy	-63785.527371
FMO2-MP2: Total energy	-63965.02267

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.
-12.495	-11.17	0.013	-0.759	-0.58	-0.004

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 : 0.864 / q_NPA : 0.919

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	-0.029	-0.006	3.240	-8.037	-6.712	0.013	-0.759	-0.580	-0.004
4	A	4	GLY	0	0.038	0.013	5.773	3.220	3.220	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.013	-0.003	9.599	-0.583	-0.583	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.008	0.015	12.793	0.724	0.724	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.033	0.020	16.502	-0.451	-0.451	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.010	0.001	19.476	-0.072	-0.072	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.009	0.002	21.959	0.345	0.345	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.006	-0.002	25.160	0.176	0.176	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.021	-0.011	27.634	0.449	0.449	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.013	-0.002	30.357	-0.216	-0.216	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.034	0.018	32.984	0.119	0.119	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.028	-0.020	34.673	0.179	0.179	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.007	0.005	38.498	-0.055	-0.055	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.024	0.015	40.546	0.109	0.109	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.839	-0.941	38.906	-7.969	-7.969	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.003	0.018	36.489	-0.060	-0.060	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.810	-0.893	39.924	-7.452	-7.452	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.026	0.013	43.537	0.141	0.141	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.881	-0.914	38.075	-8.395	-8.395	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.813	0.894	41.021	7.833	7.833	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.076	0.051	44.051	0.120	0.120	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.072	-0.058	45.218	0.099	0.099	0.000	0.000	0.000	0.000
25	A	25	ASN	0	0.033	0.011	41.530	-0.149	-0.149	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.927	-0.983	43.149	-7.221	-7.221	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.022	-0.012	40.582	0.096	0.096	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.043	-0.008	46.491	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.002	-0.011	49.436	0.048	0.048	0.000	0.000	0.000	0.000
30	A	30	THR	0	-0.023	-0.014	52.932	0.088	0.088	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.905	-0.966	52.919	-5.813	-5.813	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.917	-0.953	50.571	-6.436	-6.436	0.000	0.000	0.000	0.000
33	A	33	TRP	0	0.030	-0.012	52.704	-0.087	-0.087	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.022	0.000	52.615	0.021	0.021	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.038	0.026	46.224	-0.051	-0.051	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.048	-0.023	50.015	-0.079	-0.079	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.012	-0.003	52.154	0.011	0.011	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.821	-0.891	47.807	-6.837	-6.837	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.055	-0.044	46.777	-0.110	-0.110	0.000	0.000	0.000	0.000
40	A	40	CYS	0	0.034	0.011	49.080	-0.008	-0.008	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.885	-0.939	51.997	-5.963	-5.963	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.816	0.917	44.806	7.074	7.074	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.059	-0.039	49.124	-0.041	-0.041	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.009	0.007	50.527	0.027	0.027	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.042	-0.003	49.786	0.077	0.077	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.048	-0.021	45.704	-0.082	-0.082	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.033	0.014	47.653	0.058	0.058	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.007	-0.016	44.465	0.087	0.087	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.047	0.021	47.039	-0.100	-0.100	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.037	0.023	47.454	-0.105	-0.105	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.804	0.901	46.381	6.765	6.765	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.880	-0.941	41.186	-7.999	-7.999	0.000	0.000	0.000	0.000
53	A	53	CYS	0	0.011	0.021	44.222	-0.076	-0.076	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.043	0.016	46.473	-0.031	-0.031	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.874	0.941	38.956	8.145	8.145	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.003	0.005	42.534	-0.113	-0.113	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.022	-0.001	43.492	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	58	MET	0	0.020	0.005	46.526	0.068	0.068	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.906	0.960	39.954	7.970	7.970	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.793	0.890	40.063	7.735	7.735	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.022	-0.002	45.116	0.079	0.079	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.116	-0.056	45.162	0.170	0.170	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.006	0.008	40.564	-0.238	-0.238	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.915	0.953	40.188	8.085	8.085	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.013	0.019	43.953	0.169	0.169	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.029	-0.004	46.436	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	HIS	0	-0.012	-0.003	48.798	0.091	0.091	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.014	0.010	44.081	0.055	0.055	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.032	0.019	47.314	0.037	0.037	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.014	-0.024	49.305	0.110	0.110	0.000	0.000	0.000	0.000
71	A	71	GLN	0	0.048	0.028	49.285	0.206	0.206	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.011	-0.003	48.190	0.042	0.042	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.051	-0.019	50.113	0.064	0.064	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.033	-0.020	53.596	0.157	0.157	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.026	0.019	48.550	0.077	0.077	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.000	0.005	52.261	0.035	0.035	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.012	-0.003	53.709	0.062	0.062	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.001	0.016	55.304	0.087	0.087	0.000	0.000	0.000	0.000
79	A	79	CYS	0	-0.009	-0.009	52.690	0.029	0.029	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.016	-0.011	55.272	0.042	0.042	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.011	0.016	57.618	0.084	0.084	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.059	-0.044	57.524	0.093	0.093	0.000	0.000	0.000	0.000
83	A	83	CYS	0	-0.041	-0.014	54.342	-0.047	-0.047	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.042	0.035	56.897	0.034	0.034	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.989	0.968	57.999	5.195	5.195	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.013	-0.003	53.635	-0.036	-0.036	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.034	-0.006	50.881	-0.143	-0.143	0.000	0.000	0.000	0.000
88	A	88	HIS	0	-0.041	-0.012	54.721	-0.026	-0.026	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.037	0.010	54.665	0.012	0.012	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.808	-0.887	49.221	-6.653	-6.653	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.021	0.001	53.003	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	92	CYS	0	-0.100	-0.038	55.635	0.045	0.045	0.000	0.000	0.000	0.000
93	A	93	SER	0	0.044	0.027	50.714	0.043	0.043	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.928	0.958	52.922	5.921	5.921	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.866	-0.931	48.637	-6.674	-6.674	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.052	0.033	50.904	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.047	0.017	52.705	0.024	0.024	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.117	-0.073	51.528	0.118	0.118	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.847	-0.937	47.848	-6.854	-6.854	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.008	0.008	51.403	0.028	0.028	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.942	0.963	54.704	5.815	5.815	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.003	0.017	50.608	0.046	0.046	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.041	0.015	50.340	0.036	0.036	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.005	-0.003	52.536	0.053	0.053	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.912	0.945	54.872	5.887	5.887	0.000	0.000	0.000	0.000
106	A	106	ASN	0	0.003	-0.012	49.540	0.089	0.089	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.836	0.932	52.699	5.656	5.656	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.031	0.031	49.743	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	109	HIS	0	0.081	0.016	51.438	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.018	0.023	53.792	0.029	0.029	0.000	0.000	0.000	0.000
111	A	111	LYS	1	1.036	1.012	56.365	5.723	5.723	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.017	0.018	51.745	0.045	0.045	0.000	0.000	0.000	0.000
113	A	113	CYS	0	-0.051	-0.023	54.914	0.015	0.015	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.938	-0.969	57.007	-5.206	-5.206	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.935	0.984	57.026	5.569	5.569	0.000	0.000	0.000	0.000
116	A	116	LEU	0	0.036	0.017	53.905	0.038	0.038	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.849	0.915	57.372	5.330	5.330	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.028	-0.032	60.780	0.055	0.055	0.000	0.000	0.000	0.000
119	A	119	LEU	0	-0.025	0.007	56.485	0.055	0.055	0.000	0.000	0.000	0.000
120	A	120	MET	0	0.009	0.015	58.854	0.004	0.004	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.047	-0.007	61.288	0.061	0.061	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.865	-0.938	62.159	-5.231	-5.231	0.000	0.000	0.000	0.000
123	A	123	TRP	0	0.028	-0.015	56.449	-0.017	-0.017	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.069	-0.050	63.830	0.021	0.021	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.948	-0.979	66.037	-4.600	-4.600	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.909	-0.919	65.330	-4.814	-4.814	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.020	-0.025	61.772	0.014	0.014	0.000	0.000	0.000	0.000
128	A	128	GLN	0	-0.058	-0.035	66.364	0.031	0.031	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.891	0.943	69.071	4.597	4.597	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.887	-0.931	64.173	-5.055	-5.055	0.000	0.000	0.000	0.000
131	A	131	PRO	0	-0.024	-0.014	64.854	-0.028	-0.028	0.000	0.000	0.000	0.000
132	A	132	GLN	0	0.004	-0.021	59.469	-0.087	-0.087	0.000	0.000	0.000	0.000
133	A	133	PHE	0	0.051	0.015	60.210	-0.093	-0.093	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.037	0.030	63.099	0.040	0.040	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.008	0.004	57.791	0.035	0.035	0.000	0.000	0.000	0.000
136	A	136	ILE	0	0.003	0.015	58.356	-0.028	-0.028	0.000	0.000	0.000	0.000
137	A	137	SER	0	0.010	0.005	62.045	0.040	0.040	0.000	0.000	0.000	0.000
138	A	138	ALA	0	-0.020	-0.013	63.854	0.051	0.051	0.000	0.000	0.000	0.000
139	A	139	THR	0	-0.005	-0.018	58.943	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	140	ILE	0	0.012	0.009	62.184	0.007	0.007	0.000	0.000	0.000	0.000
141	A	141	LYS	1	0.926	0.954	64.168	4.722	4.722	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.039	-0.015	63.274	0.009	0.009	0.000	0.000	0.000	0.000
143	A	143	MET	0	-0.026	0.000	58.954	-0.043	-0.043	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.922	0.959	63.646	4.812	4.812	0.000	0.000	0.000	0.000
145	A	145	GLU	-1	-0.952	-0.965	66.909	-4.764	-4.764	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.953	-0.967	62.892	-5.111	-5.111	0.000	0.000	0.000	0.000
147	A	147	GLY	0	-0.008	0.009	65.120	-0.028	-0.028	0.000	0.000	0.000	0.000
148	A	148	ILE	0	-0.114	-0.053	61.003	-0.053	-0.053	0.000	0.000	0.000	0.000
149	A	149	THR	0	0.025	0.008	64.340	0.043	0.043	0.000	0.000	0.000	0.000
150	A	150	PHE	0	0.017	-0.023	61.284	-0.107	-0.107	0.000	0.000	0.000	0.000
151	A	151	PRO	0	0.020	0.027	64.622	0.076	0.076	0.000	0.000	0.000	0.000
152	A	152	PRO	0	0.039	0.014	67.635	-0.008	-0.008	0.000	0.000	0.000	0.000
153	A	153	ALA	0	0.033	0.005	68.259	-0.068	-0.068	0.000	0.000	0.000	0.000
154	A	154	GLY	0	-0.019	-0.005	69.345	0.014	0.014	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.020	0.018	70.462	0.058	0.058	0.000	0.000	0.000	0.000
156	A	156	GLN	0	-0.032	-0.017	74.067	-0.004	-0.004	0.000	0.000	0.000	0.000
157	A	157	THR	0	-0.015	-0.010	75.737	-0.006	-0.006	0.000	0.000	0.000	0.000
158	A	158	SER	0	-0.004	0.003	77.451	0.072	0.072	0.000	0.000	0.000	0.000
159	A	159	GLY	0	0.011	0.005	79.666	-0.038	-0.038	0.000	0.000	0.000	0.000
160	A	160	PRO	0	-0.012	-0.006	80.394	-0.031	-0.031	0.000	0.000	0.000	0.000
161	A	161	SER	0	-0.012	-0.013	80.966	0.038	0.038	0.000	0.000	0.000	0.000
162	A	162	SER	0	-0.038	-0.028	82.781	0.001	0.001	0.000	0.000	0.000	0.000
163	A	163	GLY	-1	-0.928	-0.943	83.954	-3.884	-3.884	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)