FMO DATABASE

FMODB ID: N6YNQ

Calculation Name: 1NLQ-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1NLQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q27415

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-777947.056937
FMO2-HF: Nuclear repulsion	737849.97285
FMO2-HF: Total energy	-40097.084087
FMO2-MP2: Total energy	-40217.214502

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:GLU)

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

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.
-210.32	-212.833	40.307	-20.288	-17.507	-0.126

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.730 / q_NPA : 0.802

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	SER	0	-0.049	-0.013	3.617	6.298	8.223	-0.054	-0.708	-1.164	-0.003
102	A	104	ILE	0	0.015	-0.006	2.663	-5.514	-4.271	0.110	-0.488	-0.865	-0.003
103	A	105	LYS	1	0.827	0.908	2.337	38.718	39.998	4.936	-2.370	-3.846	0.032
104	A	106	ASP	-1	-0.803	-0.862	1.542	-108.037	-116.432	35.270	-16.163	-10.712	-0.148
105	A	107	ASP	-2	-1.883	-1.924	3.466	-86.767	-85.333	0.045	-0.559	-0.920	-0.004
4	A	6	PHE	0	0.012	0.011	7.226	-0.980	-0.980	0.000	0.000	0.000	0.000
5	A	7	TYR	0	0.029	0.015	9.577	0.287	0.287	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.042	0.006	12.091	0.476	0.476	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.038	0.005	15.689	0.409	0.409	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.018	-0.029	18.763	0.251	0.251	0.000	0.000	0.000	0.000
9	A	11	LEU	0	-0.013	0.017	22.486	0.011	0.011	0.000	0.000	0.000	0.000
10	A	12	THR	0	-0.020	-0.050	25.266	0.006	0.006	0.000	0.000	0.000	0.000
11	A	13	ALA	0	0.034	0.011	29.065	-0.065	-0.065	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.906	-0.934	31.827	-9.532	-9.532	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.029	-0.013	25.856	-0.056	-0.056	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.805	-0.876	26.887	-11.094	-11.094	0.000	0.000	0.000	0.000
15	A	17	SER	0	0.003	-0.004	24.517	-0.420	-0.420	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.018	0.001	18.508	-0.034	-0.034	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.044	-0.027	17.494	0.031	0.031	0.000	0.000	0.000	0.000
18	A	20	TRP	0	-0.082	-0.033	8.499	0.188	0.188	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.747	-0.902	13.817	-16.779	-16.779	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.058	-0.018	7.495	0.349	0.349	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.862	-0.916	8.870	-24.371	-24.371	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.933	-0.976	11.895	-14.136	-14.136	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.977	-0.968	14.148	-16.079	-16.079	0.000	0.000	0.000	0.000
24	A	26	TYR	0	-0.031	-0.026	10.607	0.479	0.479	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.043	0.003	10.657	-1.413	-1.413	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.819	0.898	5.136	28.800	28.800	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.126	0.059	6.663	-3.562	-3.562	0.000	0.000	0.000	0.000
28	A	30	GLN	0	-0.078	-0.033	5.780	-3.397	-3.397	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.827	0.877	6.593	33.122	33.122	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.045	0.000	7.674	-3.292	-3.292	0.000	0.000	0.000	0.000
31	A	33	VAL	0	0.027	0.002	8.258	1.283	1.283	0.000	0.000	0.000	0.000
32	A	34	ILE	0	-0.025	-0.012	10.849	-0.502	-0.502	0.000	0.000	0.000	0.000
33	A	35	LYS	1	0.838	0.905	10.522	25.791	25.791	0.000	0.000	0.000	0.000
34	A	36	GLN	0	-0.025	-0.027	14.470	1.590	1.590	0.000	0.000	0.000	0.000
35	A	37	ILE	0	-0.011	0.003	17.691	-0.377	-0.377	0.000	0.000	0.000	0.000
36	A	38	LEU	0	-0.016	-0.006	20.523	0.540	0.540	0.000	0.000	0.000	0.000
37	A	39	LEU	0	-0.004	0.014	23.049	0.001	0.001	0.000	0.000	0.000	0.000
38	A	40	GLY	0	0.044	0.012	26.622	0.078	0.078	0.000	0.000	0.000	0.000
39	A	41	ALA	0	-0.037	-0.030	27.590	0.296	0.296	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.896	-0.946	30.713	-9.117	-9.117	0.000	0.000	0.000	0.000
41	A	43	ALA	0	-0.053	-0.010	30.623	0.216	0.216	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.835	0.899	32.680	9.480	9.480	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.848	-0.942	35.808	-8.806	-8.806	0.000	0.000	0.000	0.000
44	A	46	ASN	0	-0.086	-0.059	36.676	0.191	0.191	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.798	-0.874	33.847	-9.174	-9.174	0.000	0.000	0.000	0.000
46	A	48	PHE	0	-0.014	-0.021	32.887	-0.170	-0.170	0.000	0.000	0.000	0.000
47	A	49	ASN	0	-0.035	-0.041	29.068	-0.058	-0.058	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.023	-0.017	28.434	-0.124	-0.124	0.000	0.000	0.000	0.000
49	A	51	VAL	0	0.007	0.012	22.298	0.088	0.088	0.000	0.000	0.000	0.000
50	A	52	GLU	-1	-0.849	-0.919	24.996	-11.337	-11.337	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.023	-0.008	19.045	-0.363	-0.363	0.000	0.000	0.000	0.000
52	A	54	ASN	0	-0.005	-0.016	22.117	0.806	0.806	0.000	0.000	0.000	0.000
53	A	55	THR	0	-0.008	-0.021	18.181	-1.082	-1.082	0.000	0.000	0.000	0.000
54	A	56	PRO	0	0.006	-0.001	20.647	0.252	0.252	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.825	0.931	15.234	18.983	18.983	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.864	-0.937	19.179	-15.470	-15.470	0.000	0.000	0.000	0.000
57	A	59	SER	0	-0.075	-0.042	22.451	0.552	0.552	0.000	0.000	0.000	0.000
58	A	60	VAL	0	-0.025	0.002	21.821	0.422	0.422	0.000	0.000	0.000	0.000
59	A	61	GLN	0	-0.012	-0.015	24.281	0.101	0.101	0.000	0.000	0.000	0.000
60	A	62	ILE	0	-0.005	0.001	23.823	0.442	0.442	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.026	-0.018	24.824	-0.442	-0.442	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.004	0.009	19.534	-0.098	-0.098	0.000	0.000	0.000	0.000
63	A	65	ALA	0	-0.003	-0.002	22.873	-0.311	-0.311	0.000	0.000	0.000	0.000
64	A	66	VAL	0	-0.032	-0.006	24.818	0.345	0.345	0.000	0.000	0.000	0.000
65	A	67	LEU	0	0.006	0.004	24.488	-0.104	-0.104	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.809	0.912	28.971	9.052	9.052	0.000	0.000	0.000	0.000
67	A	69	ALA	0	-0.001	0.023	32.210	-0.110	-0.110	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.088	0.045	33.322	0.238	0.238	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.929	-0.947	33.134	-9.104	-9.104	0.000	0.000	0.000	0.000
70	A	72	THR	0	-0.022	-0.009	27.746	-0.191	-0.191	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.893	0.939	26.919	10.267	10.267	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.030	-0.009	22.799	-0.256	-0.256	0.000	0.000	0.000	0.000
73	A	75	VAL	0	0.012	0.015	21.780	0.410	0.410	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.004	-0.017	18.602	-1.000	-1.000	0.000	0.000	0.000	0.000
75	A	77	PRO	0	-0.033	-0.014	17.890	0.147	0.147	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.828	-0.895	13.438	-22.285	-22.285	0.000	0.000	0.000	0.000
77	A	79	VAL	0	0.002	0.025	15.323	-0.172	-0.172	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.851	-0.916	11.042	-27.564	-27.564	0.000	0.000	0.000	0.000
79	A	81	PHE	0	0.011	0.000	12.379	1.745	1.745	0.000	0.000	0.000	0.000
80	A	82	TYR	0	0.036	0.021	9.807	-2.338	-2.338	0.000	0.000	0.000	0.000
81	A	83	GLU	-1	-0.824	-0.897	10.486	-20.606	-20.606	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.005	-0.025	12.216	1.595	1.595	0.000	0.000	0.000	0.000
83	A	85	LYS	1	0.851	0.948	14.292	14.049	14.049	0.000	0.000	0.000	0.000
84	A	86	VAL	0	-0.004	0.001	14.998	0.738	0.738	0.000	0.000	0.000	0.000
85	A	87	THR	0	-0.038	-0.021	17.504	0.094	0.094	0.000	0.000	0.000	0.000
86	A	88	PHE	0	0.009	0.006	16.170	0.415	0.415	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.869	0.912	21.880	10.787	10.787	0.000	0.000	0.000	0.000
88	A	90	LEU	0	-0.040	-0.009	25.619	-0.066	-0.066	0.000	0.000	0.000	0.000
89	A	91	ILE	0	-0.004	-0.003	27.848	0.375	0.375	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.912	0.951	30.736	9.214	9.214	0.000	0.000	0.000	0.000
91	A	93	GLY	0	0.030	0.029	31.230	-0.296	-0.296	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.022	-0.023	32.491	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.012	0.033	29.049	-0.148	-0.148	0.000	0.000	0.000	0.000
94	A	96	PRO	0	-0.009	-0.002	26.617	0.406	0.406	0.000	0.000	0.000	0.000
95	A	97	VAL	0	-0.009	-0.014	23.377	0.111	0.111	0.000	0.000	0.000	0.000
96	A	98	TYR	0	-0.019	-0.004	20.475	-0.038	-0.038	0.000	0.000	0.000	0.000
97	A	99	ILE	0	0.018	0.015	16.454	0.110	0.110	0.000	0.000	0.000	0.000
98	A	100	HIS	0	0.021	0.001	14.942	-0.444	-0.444	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.025	0.001	11.703	0.584	0.584	0.000	0.000	0.000	0.000
100	A	102	HIS	0	-0.068	-0.029	5.657	5.004	5.004	0.000	0.000	0.000	0.000
101	A	103	ASN	0	0.031	0.008	7.057	1.162	1.162	0.000	0.000	0.000	0.000

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