FMO DATABASE

FMODB ID: 9RRN2

Calculation Name: 2NQB-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2NQB

Chain ID: B

ChEMBL ID:

UniProt ID: P84051

Base Structure: X-ray

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	81
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-472831.506217
FMO2-HF: Nuclear repulsion	441376.235784
FMO2-HF: Total energy	-31455.270434
FMO2-MP2: Total energy	-31548.878697

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:22:LEU)

Summations of interaction energy for fragment #1(A:22:LEU)

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.
78.279	81.301	0.035	-1.609	-1.448	-0.006

Interaction energy analysis for fragmet #1(A:22:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.912 / q_NPA : 0.941

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

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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	24	ASP	-1	-0.762	-0.855	3.294	-46.793	-43.771	0.035	-1.609	-1.448	-0.006
4	A	25	ASN	0	0.000	-0.022	6.182	0.459	0.459	0.000	0.000	0.000	0.000
5	A	26	ILE	0	0.006	0.009	9.147	1.296	1.296	0.000	0.000	0.000	0.000
6	A	27	GLN	0	-0.005	-0.025	8.157	1.819	1.819	0.000	0.000	0.000	0.000
7	A	28	GLY	0	-0.032	-0.008	9.994	0.291	0.291	0.000	0.000	0.000	0.000
8	A	29	ILE	0	0.011	0.020	10.927	2.016	2.016	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.020	0.016	11.714	0.505	0.505	0.000	0.000	0.000	0.000
10	A	31	LYS	1	1.015	1.009	13.973	19.160	19.160	0.000	0.000	0.000	0.000
11	A	32	PRO	0	0.000	-0.022	15.498	1.212	1.212	0.000	0.000	0.000	0.000
12	A	33	ALA	0	-0.015	0.005	17.405	1.049	1.049	0.000	0.000	0.000	0.000
13	A	34	ILE	0	0.069	0.037	16.517	1.002	1.002	0.000	0.000	0.000	0.000
14	A	35	ARG	1	0.893	0.943	19.977	14.832	14.832	0.000	0.000	0.000	0.000
15	A	36	ARG	1	0.969	0.981	18.537	16.079	16.079	0.000	0.000	0.000	0.000
16	A	37	LEU	0	0.013	0.017	21.385	0.607	0.607	0.000	0.000	0.000	0.000
17	A	38	ALA	0	0.040	0.016	24.124	0.568	0.568	0.000	0.000	0.000	0.000
18	A	39	ARG	1	0.810	0.893	25.905	12.033	12.033	0.000	0.000	0.000	0.000
19	A	40	ARG	1	0.964	0.987	27.611	11.523	11.523	0.000	0.000	0.000	0.000
20	A	41	GLY	0	0.023	0.021	28.756	0.331	0.331	0.000	0.000	0.000	0.000
21	A	42	GLY	0	0.036	0.027	30.485	0.212	0.212	0.000	0.000	0.000	0.000
22	A	43	VAL	0	-0.008	0.006	27.429	0.159	0.159	0.000	0.000	0.000	0.000
23	A	44	LYS	1	1.006	1.006	28.814	8.837	8.837	0.000	0.000	0.000	0.000
24	A	45	ARG	1	0.937	0.957	27.945	10.354	10.354	0.000	0.000	0.000	0.000
25	A	46	ILE	0	0.030	0.012	22.494	0.041	0.041	0.000	0.000	0.000	0.000
26	A	47	SER	0	0.025	0.018	23.662	-0.309	-0.309	0.000	0.000	0.000	0.000
27	A	48	GLY	0	0.007	-0.016	19.549	-0.338	-0.338	0.000	0.000	0.000	0.000
28	A	49	LEU	0	0.100	0.046	18.483	-0.925	-0.925	0.000	0.000	0.000	0.000
29	A	50	ILE	0	0.031	0.024	19.918	-0.345	-0.345	0.000	0.000	0.000	0.000
30	A	51	TYR	0	-0.023	-0.009	16.055	0.171	0.171	0.000	0.000	0.000	0.000
31	A	52	GLU	-1	-0.747	-0.853	13.609	-23.719	-23.719	0.000	0.000	0.000	0.000
32	A	53	GLU	-1	-0.898	-0.938	16.980	-13.796	-13.796	0.000	0.000	0.000	0.000
33	A	54	THR	0	-0.051	-0.050	19.692	0.464	0.464	0.000	0.000	0.000	0.000
34	A	55	ARG	1	0.771	0.878	12.222	23.832	23.832	0.000	0.000	0.000	0.000
35	A	56	GLY	0	0.056	0.034	17.652	-0.134	-0.134	0.000	0.000	0.000	0.000
36	A	57	VAL	0	0.024	0.008	19.460	0.335	0.335	0.000	0.000	0.000	0.000
37	A	58	LEU	0	-0.031	-0.019	18.072	0.325	0.325	0.000	0.000	0.000	0.000
38	A	59	LYS	1	0.856	0.911	14.928	17.963	17.963	0.000	0.000	0.000	0.000
39	A	60	VAL	0	0.069	0.038	18.825	0.309	0.309	0.000	0.000	0.000	0.000
40	A	61	PHE	0	-0.038	-0.016	22.278	0.555	0.555	0.000	0.000	0.000	0.000
41	A	62	LEU	0	-0.012	-0.018	18.359	0.358	0.358	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.833	-0.905	18.690	-15.499	-15.499	0.000	0.000	0.000	0.000
43	A	64	ASN	0	-0.004	0.006	21.851	0.375	0.375	0.000	0.000	0.000	0.000
44	A	65	VAL	0	0.013	0.009	25.051	0.349	0.349	0.000	0.000	0.000	0.000
45	A	66	ILE	0	0.001	-0.007	20.065	0.265	0.265	0.000	0.000	0.000	0.000
46	A	67	ARG	1	0.943	0.981	23.979	12.152	12.152	0.000	0.000	0.000	0.000
47	A	68	ASP	-1	-0.785	-0.847	25.683	-9.748	-9.748	0.000	0.000	0.000	0.000
48	A	69	ALA	0	-0.010	-0.007	26.170	0.294	0.294	0.000	0.000	0.000	0.000
49	A	70	VAL	0	-0.003	0.003	23.339	0.168	0.168	0.000	0.000	0.000	0.000
50	A	71	THR	0	0.028	0.007	26.696	0.293	0.293	0.000	0.000	0.000	0.000
51	A	72	TYR	0	-0.037	-0.027	30.013	0.301	0.301	0.000	0.000	0.000	0.000
52	A	73	THR	0	-0.027	-0.027	26.732	0.204	0.204	0.000	0.000	0.000	0.000
53	A	74	GLU	-1	-0.923	-0.967	27.526	-10.512	-10.512	0.000	0.000	0.000	0.000
54	A	75	HIS	0	-0.016	0.005	30.449	0.175	0.175	0.000	0.000	0.000	0.000
55	A	76	ALA	0	-0.061	-0.033	32.916	0.278	0.278	0.000	0.000	0.000	0.000
56	A	77	LYS	1	0.925	0.963	32.444	8.049	8.049	0.000	0.000	0.000	0.000
57	A	78	ARG	1	0.791	0.871	29.386	9.607	9.607	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.969	0.977	25.418	9.926	9.926	0.000	0.000	0.000	0.000
59	A	80	THR	0	0.002	-0.004	24.676	-0.336	-0.336	0.000	0.000	0.000	0.000
60	A	81	VAL	0	0.009	0.024	23.919	0.395	0.395	0.000	0.000	0.000	0.000
61	A	82	THR	0	-0.034	-0.048	26.196	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	83	ALA	0	0.034	0.003	28.682	-0.134	-0.134	0.000	0.000	0.000	0.000
63	A	84	MET	0	0.050	0.035	29.714	0.012	0.012	0.000	0.000	0.000	0.000
64	A	85	ASP	-1	-0.743	-0.799	28.860	-9.799	-9.799	0.000	0.000	0.000	0.000
65	A	86	VAL	0	0.002	-0.004	26.120	-0.063	-0.063	0.000	0.000	0.000	0.000
66	A	87	VAL	0	0.007	0.010	29.061	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	88	TYR	0	-0.021	-0.017	32.568	0.245	0.245	0.000	0.000	0.000	0.000
68	A	89	ALA	0	0.006	0.007	29.186	0.132	0.132	0.000	0.000	0.000	0.000
69	A	90	LEU	0	-0.020	-0.020	27.975	0.020	0.020	0.000	0.000	0.000	0.000
70	A	91	LYS	1	0.910	0.966	31.474	8.296	8.296	0.000	0.000	0.000	0.000
71	A	92	ARG	1	0.873	0.921	32.636	9.361	9.361	0.000	0.000	0.000	0.000
72	A	93	GLN	0	-0.072	-0.043	29.666	-0.067	-0.067	0.000	0.000	0.000	0.000
73	A	94	GLY	0	0.016	0.021	32.841	-0.076	-0.076	0.000	0.000	0.000	0.000
74	A	95	ARG	1	0.839	0.909	30.072	9.996	9.996	0.000	0.000	0.000	0.000
75	A	96	THR	0	0.028	0.005	32.692	-0.226	-0.226	0.000	0.000	0.000	0.000
76	A	97	LEU	0	-0.012	0.014	29.945	-0.024	-0.024	0.000	0.000	0.000	0.000
77	A	98	TYR	0	0.037	0.013	34.007	0.174	0.174	0.000	0.000	0.000	0.000
78	A	99	GLY	0	0.018	-0.001	34.495	-0.223	-0.223	0.000	0.000	0.000	0.000
79	A	100	PHE	0	-0.047	-0.028	28.652	-0.174	-0.174	0.000	0.000	0.000	0.000
80	A	101	GLY	0	0.015	0.009	33.234	-0.093	-0.093	0.000	0.000	0.000	0.000
81	A	102	GLY	-1	-0.910	-0.954	36.275	-8.102	-8.102	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:LEU)