FMO DATABASE

FMODB ID: MR49Z

Calculation Name: 1NQ3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1NQ3

Chain ID: A

ChEMBL ID:

UniProt ID: P80601

Base Structure: X-ray

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1035531.456543
FMO2-HF: Nuclear repulsion	987482.598192
FMO2-HF: Total energy	-48048.858351
FMO2-MP2: Total energy	-48190.951259

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:3:SER)

Summations of interaction energy for fragment #1(A:3:SER)

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.
4.526	5.978	-0.016	-0.607	-0.828	-0.001

Interaction energy analysis for fragmet #1(A:3:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.838 / q_NPA : 0.907

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	5	VAL	0	0.038	0.031	3.849	4.057	5.509	-0.016	-0.607	-0.828	-0.001
4	A	6	ARG	1	0.982	0.986	6.209	26.807	26.807	0.000	0.000	0.000	0.000
5	A	7	ARG	1	0.905	0.953	8.799	22.395	22.395	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.024	0.013	11.930	0.208	0.208	0.000	0.000	0.000	0.000
7	A	9	ILE	0	-0.018	0.005	15.461	-0.023	-0.023	0.000	0.000	0.000	0.000
8	A	10	SER	0	0.008	-0.003	18.446	0.622	0.622	0.000	0.000	0.000	0.000
9	A	11	THR	0	-0.019	-0.029	21.382	-0.095	-0.095	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.001	0.002	24.629	0.188	0.188	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.922	0.966	27.770	10.523	10.523	0.000	0.000	0.000	0.000
12	A	14	ALA	0	0.067	0.044	26.978	0.174	0.174	0.000	0.000	0.000	0.000
13	A	15	PRO	0	-0.011	0.015	28.817	-0.078	-0.078	0.000	0.000	0.000	0.000
14	A	16	ALA	0	0.014	0.015	27.089	-0.415	-0.415	0.000	0.000	0.000	0.000
15	A	17	ALA	0	-0.014	-0.010	23.795	0.176	0.176	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.026	-0.001	25.625	-0.164	-0.164	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.040	0.007	26.289	0.345	0.345	0.000	0.000	0.000	0.000
18	A	20	PRO	0	-0.036	-0.005	23.187	-0.361	-0.361	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.002	0.000	21.479	-0.314	-0.314	0.000	0.000	0.000	0.000
20	A	22	SER	0	-0.008	-0.013	19.073	-0.383	-0.383	0.000	0.000	0.000	0.000
21	A	23	GLN	0	0.016	0.008	21.065	-0.333	-0.333	0.000	0.000	0.000	0.000
22	A	24	ALA	0	0.067	0.033	19.389	0.256	0.256	0.000	0.000	0.000	0.000
23	A	25	VAL	0	-0.056	-0.019	13.545	-0.439	-0.439	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.013	0.027	11.977	0.235	0.235	0.000	0.000	0.000	0.000
25	A	27	VAL	0	-0.018	-0.033	8.467	-1.449	-1.449	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.932	-0.964	8.395	-34.044	-34.044	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.886	0.927	9.271	22.368	22.368	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.015	0.008	12.814	2.341	2.341	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.029	-0.020	14.384	-0.944	-0.944	0.000	0.000	0.000	0.000
30	A	32	TYR	0	0.023	0.007	14.239	1.091	1.091	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.005	-0.018	18.852	-0.217	-0.217	0.000	0.000	0.000	0.000
32	A	34	SER	0	-0.009	-0.020	22.163	0.212	0.212	0.000	0.000	0.000	0.000
33	A	35	GLY	0	0.017	0.021	24.098	0.197	0.197	0.000	0.000	0.000	0.000
34	A	36	GLN	0	-0.071	-0.039	26.437	0.368	0.368	0.000	0.000	0.000	0.000
35	A	37	LEU	0	0.070	0.023	29.896	0.242	0.242	0.000	0.000	0.000	0.000
36	A	38	GLY	0	0.037	0.024	33.343	-0.137	-0.137	0.000	0.000	0.000	0.000
37	A	39	MET	0	-0.065	-0.019	32.383	0.255	0.255	0.000	0.000	0.000	0.000
38	A	40	ASP	-1	-0.762	-0.879	34.266	-8.657	-8.657	0.000	0.000	0.000	0.000
39	A	41	PRO	0	-0.035	-0.025	31.381	-0.109	-0.109	0.000	0.000	0.000	0.000
40	A	42	ALA	0	-0.020	-0.008	32.371	-0.192	-0.192	0.000	0.000	0.000	0.000
41	A	43	SER	0	-0.041	-0.030	34.657	0.047	0.047	0.000	0.000	0.000	0.000
42	A	44	GLY	0	0.044	0.025	34.358	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	45	GLN	0	-0.060	-0.028	35.138	0.082	0.082	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.019	-0.007	37.522	-0.179	-0.179	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.020	0.017	39.136	0.191	0.191	0.000	0.000	0.000	0.000
46	A	48	PRO	0	-0.008	-0.002	40.882	0.070	0.070	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.034	0.003	44.380	-0.035	-0.035	0.000	0.000	0.000	0.000
48	A	50	GLY	0	-0.003	0.013	43.861	0.085	0.085	0.000	0.000	0.000	0.000
49	A	51	VAL	0	0.049	0.004	40.556	-0.132	-0.132	0.000	0.000	0.000	0.000
50	A	52	VAL	0	0.026	0.019	40.620	-0.200	-0.200	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.793	-0.879	40.825	-7.615	-7.615	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.818	-0.924	38.196	-8.139	-8.139	0.000	0.000	0.000	0.000
53	A	55	ALA	0	0.032	0.013	36.554	-0.296	-0.296	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.862	0.911	35.734	7.348	7.348	0.000	0.000	0.000	0.000
55	A	57	GLN	0	-0.017	0.016	33.640	-0.038	-0.038	0.000	0.000	0.000	0.000
56	A	58	ALA	0	0.004	0.006	32.503	-0.298	-0.298	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.007	-0.010	31.053	-0.434	-0.434	0.000	0.000	0.000	0.000
58	A	60	THR	0	-0.015	-0.026	30.950	-0.287	-0.287	0.000	0.000	0.000	0.000
59	A	61	ASN	0	-0.012	-0.007	29.366	-0.233	-0.233	0.000	0.000	0.000	0.000
60	A	62	ILE	0	-0.007	-0.011	26.169	-0.445	-0.445	0.000	0.000	0.000	0.000
61	A	63	GLY	0	0.027	0.016	26.176	-0.478	-0.478	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.901	-0.970	26.872	-11.002	-11.002	0.000	0.000	0.000	0.000
63	A	65	ILE	0	-0.032	-0.010	21.986	-0.477	-0.477	0.000	0.000	0.000	0.000
64	A	66	LEU	0	-0.029	-0.016	22.117	-0.791	-0.791	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.965	0.994	22.303	10.684	10.684	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.059	-0.028	21.654	-0.270	-0.270	0.000	0.000	0.000	0.000
67	A	69	ALA	0	-0.033	-0.012	18.211	-0.750	-0.750	0.000	0.000	0.000	0.000
68	A	70	GLY	0	-0.029	-0.001	18.613	-0.875	-0.875	0.000	0.000	0.000	0.000
69	A	71	CYS	0	-0.103	-0.045	19.788	-0.552	-0.552	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.783	-0.872	22.649	-11.455	-11.455	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.024	-0.009	25.290	-0.406	-0.406	0.000	0.000	0.000	0.000
72	A	74	THR	0	-0.070	-0.051	26.687	-0.115	-0.115	0.000	0.000	0.000	0.000
73	A	75	ASN	0	0.004	-0.001	21.044	0.125	0.125	0.000	0.000	0.000	0.000
74	A	76	VAL	0	-0.037	-0.013	22.296	-0.698	-0.698	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.029	0.016	20.589	0.336	0.336	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.876	0.940	23.536	12.394	12.394	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.018	0.008	25.207	-0.218	-0.218	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.050	-0.028	27.423	0.141	0.141	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.021	-0.006	29.581	-0.036	-0.036	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.022	0.018	30.526	0.213	0.213	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.027	0.004	34.444	0.050	0.050	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.031	0.014	38.212	0.001	0.001	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.870	-0.931	40.878	-6.755	-6.755	0.000	0.000	0.000	0.000
84	A	86	ILE	0	0.018	0.008	40.685	-0.156	-0.156	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.074	-0.056	42.938	0.002	0.002	0.000	0.000	0.000	0.000
86	A	88	ASP	-1	-0.847	-0.923	42.460	-7.176	-7.176	0.000	0.000	0.000	0.000
87	A	89	PHE	0	-0.020	-0.016	37.348	-0.149	-0.149	0.000	0.000	0.000	0.000
88	A	90	SER	0	0.016	-0.001	41.018	-0.190	-0.190	0.000	0.000	0.000	0.000
89	A	91	ALA	0	0.051	0.031	42.945	-0.063	-0.063	0.000	0.000	0.000	0.000
90	A	92	VAL	0	0.025	0.014	37.166	-0.109	-0.109	0.000	0.000	0.000	0.000
91	A	93	ASN	0	0.000	0.004	38.345	-0.451	-0.451	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.840	-0.906	39.420	-7.441	-7.441	0.000	0.000	0.000	0.000
93	A	95	VAL	0	0.013	0.018	37.607	0.014	0.014	0.000	0.000	0.000	0.000
94	A	96	TYR	0	0.019	-0.007	30.590	-0.092	-0.092	0.000	0.000	0.000	0.000
95	A	97	LYS	1	0.770	0.855	35.550	7.380	7.380	0.000	0.000	0.000	0.000
96	A	98	GLN	0	-0.051	-0.016	37.765	0.216	0.216	0.000	0.000	0.000	0.000
97	A	99	TYR	0	-0.033	-0.011	32.539	0.080	0.080	0.000	0.000	0.000	0.000
98	A	100	PHE	0	-0.031	-0.016	28.770	-0.376	-0.376	0.000	0.000	0.000	0.000
99	A	101	GLN	0	0.013	0.006	33.407	0.405	0.405	0.000	0.000	0.000	0.000
100	A	102	SER	0	-0.012	-0.012	32.950	0.154	0.154	0.000	0.000	0.000	0.000
101	A	103	SER	0	-0.016	-0.011	28.761	-0.223	-0.223	0.000	0.000	0.000	0.000
102	A	104	PHE	0	0.007	0.011	29.070	-0.336	-0.336	0.000	0.000	0.000	0.000
103	A	105	PRO	0	0.005	0.021	27.203	-0.134	-0.134	0.000	0.000	0.000	0.000
104	A	106	ALA	0	0.016	0.019	26.640	0.438	0.438	0.000	0.000	0.000	0.000
105	A	107	ARG	1	0.870	0.919	28.427	8.946	8.946	0.000	0.000	0.000	0.000
106	A	108	ALA	0	-0.014	0.004	30.710	0.195	0.195	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.001	-0.011	32.274	-0.125	-0.125	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.004	0.003	31.221	0.097	0.097	0.000	0.000	0.000	0.000
109	A	111	GLN	0	0.013	0.022	36.895	-0.051	-0.051	0.000	0.000	0.000	0.000
110	A	112	VAL	0	-0.009	-0.011	34.514	-0.088	-0.088	0.000	0.000	0.000	0.000
111	A	113	ALA	0	-0.015	-0.013	37.985	0.162	0.162	0.000	0.000	0.000	0.000
112	A	114	ALA	0	-0.007	-0.008	38.438	0.203	0.203	0.000	0.000	0.000	0.000
113	A	115	LEU	0	0.000	0.024	34.213	-0.252	-0.252	0.000	0.000	0.000	0.000
114	A	116	PRO	0	0.028	0.006	32.452	0.274	0.274	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.810	0.874	34.482	8.888	8.888	0.000	0.000	0.000	0.000
116	A	118	GLY	0	0.014	0.025	38.415	0.171	0.171	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.034	0.000	37.936	0.153	0.153	0.000	0.000	0.000	0.000
118	A	120	ARG	1	0.875	0.925	39.001	7.354	7.354	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.000	-0.008	35.479	0.014	0.014	0.000	0.000	0.000	0.000
120	A	122	GLU	-1	-0.890	-0.949	30.179	-10.159	-10.159	0.000	0.000	0.000	0.000
121	A	123	ILE	0	-0.032	-0.012	29.456	0.051	0.051	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.873	-0.925	25.351	-12.121	-12.121	0.000	0.000	0.000	0.000
123	A	125	ALA	0	-0.022	-0.022	24.631	0.276	0.276	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.015	-0.004	18.932	-0.569	-0.569	0.000	0.000	0.000	0.000
125	A	127	ALA	0	0.016	0.012	19.963	0.636	0.636	0.000	0.000	0.000	0.000
126	A	128	VAL	0	0.000	0.003	16.213	-1.125	-1.125	0.000	0.000	0.000	0.000
127	A	129	GLN	0	-0.001	-0.008	14.702	-0.371	-0.371	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.024	0.038	17.288	-0.571	-0.571	0.000	0.000	0.000	0.000
129	A	131	PRO	0	-0.008	-0.016	17.464	-0.867	-0.867	0.000	0.000	0.000	0.000
130	A	132	LEU	0	0.003	-0.015	19.191	-0.981	-0.981	0.000	0.000	0.000	0.000
131	A	133	THR	0	-0.034	-0.017	21.654	0.331	0.331	0.000	0.000	0.000	0.000
132	A	134	THR	0	-0.023	-0.006	24.270	-0.461	-0.461	0.000	0.000	0.000	0.000
133	A	135	ALA	-1	-0.914	-0.941	26.927	-10.532	-10.532	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:SER)