FMO DATABASE

FMODB ID: Z74KN

Calculation Name: 1X1F-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X1F

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ULZ2

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	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1403204.492902
FMO2-HF: Nuclear repulsion	1344212.041898
FMO2-HF: Total energy	-58992.451004
FMO2-MP2: Total energy	-59167.169478

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.
-17.466	-16.521	-0.016	-0.403	-0.526	-0.001

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 : 0.869 / q_NPA : 0.923

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	-0.003	3.827	1.147	2.092	-0.016	-0.403	-0.526	-0.001
4	A	4	GLY	0	0.032	0.024	6.875	1.135	1.135	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.006	-0.007	10.464	0.753	0.753	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.023	-0.010	13.968	0.003	0.003	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.053	0.026	17.638	0.894	0.894	0.000	0.000	0.000	0.000
8	A	8	GLN	0	-0.053	-0.028	18.453	-0.542	-0.542	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.890	-0.933	16.936	-17.162	-17.162	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.902	0.941	20.245	13.993	13.993	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.043	0.030	22.926	0.619	0.619	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.959	0.979	25.334	9.742	9.742	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.005	-0.005	28.154	0.184	0.184	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.022	-0.017	24.389	-0.381	-0.381	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.044	0.018	27.569	0.093	0.093	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.010	0.023	29.085	0.407	0.407	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.075	-0.040	29.257	-0.339	-0.339	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.001	0.008	25.614	0.075	0.075	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.068	-0.027	29.167	0.375	0.375	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.013	-0.013	29.054	0.197	0.197	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.902	-0.933	23.531	-12.319	-12.319	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.019	-0.004	23.478	0.243	0.243	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.058	-0.021	16.555	-0.415	-0.415	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.026	-0.004	22.143	0.676	0.676	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.043	-0.017	22.852	-0.472	-0.472	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.031	0.016	24.221	0.751	0.751	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.833	0.909	25.792	10.218	10.218	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.975	1.001	26.418	11.652	11.652	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.045	0.012	30.196	-0.167	-0.167	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.001	0.000	29.949	-0.203	-0.203	0.000	0.000	0.000	0.000
31	A	31	TYR	0	-0.056	-0.056	23.265	0.200	0.200	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.943	0.988	26.347	10.166	10.166	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.971	-0.989	25.113	-12.053	-12.053	0.000	0.000	0.000	0.000
34	A	34	TYR	0	-0.024	-0.023	25.227	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.798	-0.867	20.896	-14.620	-14.620	0.000	0.000	0.000	0.000
36	A	36	HIS	0	-0.004	-0.011	17.580	1.027	1.027	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.009	0.004	16.050	-1.657	-1.657	0.000	0.000	0.000	0.000
38	A	38	TRP	0	-0.089	-0.043	17.719	0.525	0.525	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.017	-0.004	19.479	0.038	0.038	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.835	-0.928	22.171	-13.398	-13.398	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.029	0.020	24.822	0.210	0.210	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.923	0.952	23.206	12.809	12.809	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.035	-0.021	29.881	0.073	0.073	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.075	0.028	33.507	0.078	0.078	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.043	-0.035	28.824	0.125	0.125	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.030	-0.005	27.423	-0.169	-0.169	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.017	-0.016	23.376	-0.146	-0.146	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.056	0.024	21.189	-0.057	-0.057	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.006	-0.010	17.128	-0.130	-0.130	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.013	-0.008	12.123	0.605	0.605	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.887	-0.926	11.228	-27.273	-27.273	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.964	0.967	14.121	18.787	18.787	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.936	0.961	10.521	27.588	27.588	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.029	0.003	13.088	-0.736	-0.736	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.050	0.022	14.535	1.046	1.046	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.051	-0.025	17.105	1.124	1.124	0.000	0.000	0.000	0.000
57	A	57	TYR	0	0.012	0.015	17.340	-0.672	-0.672	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.031	-0.023	16.374	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.847	-0.925	18.323	-12.889	-12.889	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.820	0.907	22.012	11.483	11.483	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.019	0.015	25.332	0.237	0.237	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.875	-0.929	28.792	-9.844	-9.844	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.048	-0.023	32.221	0.041	0.041	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.014	0.002	34.792	0.212	0.212	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.934	-0.957	37.301	-7.592	-7.592	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.070	-0.029	36.824	0.033	0.033	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.024	-0.004	39.560	0.215	0.215	0.000	0.000	0.000	0.000
68	A	68	CYS	0	-0.001	-0.022	41.160	0.250	0.250	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.001	0.024	36.261	-0.234	-0.234	0.000	0.000	0.000	0.000
70	A	70	THR	0	-0.018	-0.004	39.187	0.214	0.214	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.846	-0.927	38.720	-8.384	-8.384	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.022	-0.007	37.327	-0.041	-0.041	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.015	-0.003	38.676	-0.206	-0.206	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.047	-0.020	36.725	-0.126	-0.126	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.005	0.001	38.368	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.884	-0.927	33.977	-9.480	-9.480	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.872	0.913	31.965	9.617	9.617	0.000	0.000	0.000	0.000
78	A	78	ASN	0	0.004	0.011	35.900	0.007	0.007	0.000	0.000	0.000	0.000
79	A	79	CYS	0	-0.038	-0.024	32.440	-0.363	-0.363	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.064	0.058	33.981	0.181	0.181	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.927	0.955	32.015	9.314	9.314	0.000	0.000	0.000	0.000
82	A	82	PHE	0	0.040	0.014	32.537	0.309	0.309	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.017	-0.012	34.176	-0.393	-0.393	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.015	-0.008	33.237	0.277	0.277	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.042	0.013	36.245	-0.096	-0.096	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.049	0.026	34.235	0.051	0.051	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.016	0.025	38.967	0.045	0.045	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.860	0.914	37.397	8.414	8.414	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.858	-0.929	32.414	-9.785	-9.785	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.935	-0.959	36.429	-8.200	-8.200	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.036	-0.025	30.303	-0.282	-0.282	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.018	-0.002	31.426	0.038	0.038	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.024	0.010	28.805	-0.430	-0.430	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.894	0.963	27.617	11.786	11.786	0.000	0.000	0.000	0.000
95	A	95	THR	0	0.020	0.008	27.651	-0.367	-0.367	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.927	-0.978	23.331	-13.694	-13.694	0.000	0.000	0.000	0.000
97	A	97	ASN	0	0.004	-0.017	27.174	0.509	0.509	0.000	0.000	0.000	0.000
98	A	98	THR	0	0.035	0.011	30.690	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.939	-0.945	32.077	-9.030	-9.030	0.000	0.000	0.000	0.000
100	A	100	SER	0	0.061	0.023	28.955	0.030	0.030	0.000	0.000	0.000	0.000
101	A	101	GLY	0	-0.027	-0.012	31.001	-0.058	-0.058	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.752	-0.900	33.035	-8.060	-8.060	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.832	-0.902	31.135	-10.189	-10.189	0.000	0.000	0.000	0.000
104	A	104	TRP	0	-0.024	-0.018	25.888	0.281	0.281	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.847	0.923	32.417	8.185	8.185	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.059	0.031	35.798	0.205	0.205	0.000	0.000	0.000	0.000
107	A	107	PHE	0	-0.012	-0.015	32.496	0.214	0.214	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.010	-0.008	31.532	0.029	0.029	0.000	0.000	0.000	0.000
109	A	109	LEU	0	0.009	0.024	35.580	0.112	0.112	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.041	-0.031	37.828	0.233	0.233	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.088	-0.041	34.301	0.136	0.136	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.046	-0.057	37.155	-0.055	-0.055	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.913	-0.952	39.847	-7.112	-7.112	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.111	-0.038	41.292	0.250	0.250	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.011	-0.019	43.061	0.201	0.201	0.000	0.000	0.000	0.000
116	A	116	VAL	0	0.009	-0.003	41.964	-0.211	-0.211	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.022	0.015	40.644	0.210	0.210	0.000	0.000	0.000	0.000
118	A	118	GLN	0	0.035	-0.011	43.615	-0.173	-0.173	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.085	-0.026	45.376	0.159	0.159	0.000	0.000	0.000	0.000
120	A	120	VAL	0	-0.018	0.000	40.843	-0.126	-0.126	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.013	-0.020	40.701	0.235	0.235	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.021	0.006	35.998	-0.050	-0.050	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.050	0.035	37.854	0.240	0.240	0.000	0.000	0.000	0.000
124	A	124	PRO	0	0.052	0.021	40.758	-0.075	-0.075	0.000	0.000	0.000	0.000
125	A	125	GLY	0	-0.025	-0.026	39.382	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	126	GLN	0	-0.090	-0.055	33.193	-0.164	-0.164	0.000	0.000	0.000	0.000
127	A	127	VAL	0	0.064	0.018	37.825	-0.082	-0.082	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.016	0.000	39.353	0.047	0.047	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.964	0.990	31.522	9.888	9.888	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.028	0.025	36.841	-0.101	-0.101	0.000	0.000	0.000	0.000
131	A	131	HIS	0	0.044	0.018	38.862	0.049	0.049	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.935	-0.973	37.520	-8.621	-8.621	0.000	0.000	0.000	0.000
133	A	133	VAL	0	-0.054	-0.023	34.456	-0.056	-0.056	0.000	0.000	0.000	0.000
134	A	134	LEU	0	0.052	0.044	37.136	0.016	0.016	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.983	-1.006	40.427	-7.169	-7.169	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.837	0.924	34.940	8.924	8.924	0.000	0.000	0.000	0.000
137	A	137	GLU	-1	-0.844	-0.933	37.544	-8.212	-8.212	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.958	0.976	39.007	7.187	7.187	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.893	0.945	40.618	7.678	7.678	0.000	0.000	0.000	0.000
140	A	140	ARG	1	0.964	0.983	35.654	8.927	8.927	0.000	0.000	0.000	0.000
141	A	141	ARG	1	0.958	0.972	40.223	7.249	7.249	0.000	0.000	0.000	0.000
142	A	142	ILE	0	-0.046	-0.004	43.453	0.156	0.156	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.955	-0.974	42.069	-7.268	-7.268	0.000	0.000	0.000	0.000
144	A	144	SER	0	-0.069	-0.023	41.167	-0.191	-0.191	0.000	0.000	0.000	0.000
145	A	145	GLY	0	0.013	0.008	42.463	-0.040	-0.040	0.000	0.000	0.000	0.000
146	A	146	PRO	0	0.001	0.001	44.803	-0.070	-0.070	0.000	0.000	0.000	0.000
147	A	147	SER	0	0.015	0.005	44.964	0.120	0.120	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.073	-0.042	46.910	0.061	0.061	0.000	0.000	0.000	0.000
149	A	149	GLY	-1	-0.936	-0.955	47.697	-6.597	-6.597	0.000	0.000	0.000	0.000

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