FMO DATABASE

FMODB ID: LQYZ9

Calculation Name: 1NGR-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1NGR

Chain ID: A

ChEMBL ID:

UniProt ID: P07174

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-570022.892758
FMO2-HF: Nuclear repulsion	537049.637204
FMO2-HF: Total energy	-32973.255554
FMO2-MP2: Total energy	-33070.066561

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:334:GLY)

Summations of interaction energy for fragment #1(A:334: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.
-181.176	-179.908	22.509	-13.299	-10.476	-0.15

Interaction energy analysis for fragmet #1(A:334:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.796 / q_NPA : 0.888

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	336	LEU	0	0.060	0.027	3.853	-4.198	-3.548	-0.011	-0.265	-0.374	0.000
62	A	395	THR	0	-0.054	-0.071	2.048	-3.175	-0.377	3.071	-2.823	-3.045	-0.035
63	A	396	LEU	0	-0.009	-0.007	4.209	6.012	6.217	-0.001	-0.041	-0.163	0.000
64	A	397	ASP	-1	-0.750	-0.864	1.889	-132.060	-134.499	19.451	-10.160	-6.852	-0.115
65	A	398	ALA	0	0.022	0.025	4.343	6.568	6.622	-0.001	-0.010	-0.042	0.000
4	A	337	TYR	0	0.027	0.018	6.412	3.008	3.008	0.000	0.000	0.000	0.000
5	A	338	SER	0	-0.006	-0.018	8.517	1.765	1.765	0.000	0.000	0.000	0.000
6	A	339	SER	0	-0.054	-0.028	8.502	3.371	3.371	0.000	0.000	0.000	0.000
7	A	340	LEU	0	-0.013	0.008	10.450	1.505	1.505	0.000	0.000	0.000	0.000
8	A	341	PRO	0	-0.006	-0.007	12.423	0.652	0.652	0.000	0.000	0.000	0.000
9	A	342	LEU	0	0.010	0.006	15.860	1.343	1.343	0.000	0.000	0.000	0.000
10	A	343	THR	0	0.070	0.002	17.185	-0.840	-0.840	0.000	0.000	0.000	0.000
11	A	344	LYS	1	0.802	0.902	14.979	17.387	17.387	0.000	0.000	0.000	0.000
12	A	345	ARG	1	0.835	0.909	10.096	24.426	24.426	0.000	0.000	0.000	0.000
13	A	346	GLU	-1	-0.746	-0.843	16.357	-13.700	-13.700	0.000	0.000	0.000	0.000
14	A	347	GLU	-1	-0.848	-0.908	18.331	-15.567	-15.567	0.000	0.000	0.000	0.000
15	A	348	VAL	0	0.011	-0.004	14.081	-0.201	-0.201	0.000	0.000	0.000	0.000
16	A	349	GLU	-1	-0.830	-0.917	17.421	-14.314	-14.314	0.000	0.000	0.000	0.000
17	A	350	LYS	1	0.720	0.858	19.686	15.828	15.828	0.000	0.000	0.000	0.000
18	A	351	LEU	0	-0.016	0.013	16.015	0.353	0.353	0.000	0.000	0.000	0.000
19	A	352	LEU	0	-0.037	-0.011	14.165	0.261	0.261	0.000	0.000	0.000	0.000
20	A	353	ASN	0	0.037	-0.005	18.749	0.948	0.948	0.000	0.000	0.000	0.000
21	A	354	GLY	0	0.020	0.007	22.369	-0.311	-0.311	0.000	0.000	0.000	0.000
22	A	355	ASP	-1	-0.808	-0.907	23.693	-12.378	-12.378	0.000	0.000	0.000	0.000
23	A	356	THR	0	-0.015	-0.015	19.034	-0.351	-0.351	0.000	0.000	0.000	0.000
24	A	357	TRP	0	-0.022	-0.001	18.280	-0.893	-0.893	0.000	0.000	0.000	0.000
25	A	358	ARG	1	0.844	0.908	18.716	11.843	11.843	0.000	0.000	0.000	0.000
26	A	359	HIS	0	-0.037	-0.030	20.443	-0.397	-0.397	0.000	0.000	0.000	0.000
27	A	360	LEU	0	0.013	-0.001	12.997	-0.383	-0.383	0.000	0.000	0.000	0.000
28	A	361	ALA	0	0.017	-0.001	15.708	-0.978	-0.978	0.000	0.000	0.000	0.000
29	A	362	GLY	0	0.021	0.015	16.836	-0.282	-0.282	0.000	0.000	0.000	0.000
30	A	363	GLU	-1	-0.868	-0.922	15.196	-18.747	-18.747	0.000	0.000	0.000	0.000
31	A	364	LEU	0	-0.082	-0.034	10.576	-1.820	-1.820	0.000	0.000	0.000	0.000
32	A	365	GLY	0	0.000	0.006	13.294	-0.915	-0.915	0.000	0.000	0.000	0.000
33	A	366	TYR	0	-0.027	-0.009	15.192	0.265	0.265	0.000	0.000	0.000	0.000
34	A	367	GLN	0	-0.013	-0.025	18.265	0.050	0.050	0.000	0.000	0.000	0.000
35	A	368	PRO	0	0.021	0.003	21.966	-0.150	-0.150	0.000	0.000	0.000	0.000
36	A	369	GLU	-1	-0.811	-0.909	24.106	-12.081	-12.081	0.000	0.000	0.000	0.000
37	A	370	HIS	0	0.016	0.009	20.701	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	371	ILE	0	-0.048	0.001	20.193	-0.035	-0.035	0.000	0.000	0.000	0.000
39	A	372	ASP	-1	-0.825	-0.916	22.393	-10.987	-10.987	0.000	0.000	0.000	0.000
40	A	373	SER	0	-0.047	-0.024	24.066	0.569	0.569	0.000	0.000	0.000	0.000
41	A	374	PHE	0	0.067	0.018	18.054	0.093	0.093	0.000	0.000	0.000	0.000
42	A	375	THR	0	-0.070	-0.035	23.050	0.004	0.004	0.000	0.000	0.000	0.000
43	A	376	HIS	1	0.773	0.882	25.719	11.241	11.241	0.000	0.000	0.000	0.000
44	A	377	GLU	-1	-0.846	-0.894	22.914	-13.372	-13.372	0.000	0.000	0.000	0.000
45	A	378	ALA	0	-0.031	-0.016	25.649	-0.038	-0.038	0.000	0.000	0.000	0.000
46	A	379	CYS	0	0.019	-0.006	23.630	0.336	0.336	0.000	0.000	0.000	0.000
47	A	380	PRO	0	0.035	0.042	21.659	-0.525	-0.525	0.000	0.000	0.000	0.000
48	A	381	VAL	0	0.016	0.004	17.072	-0.693	-0.693	0.000	0.000	0.000	0.000
49	A	382	ARG	1	0.779	0.867	17.702	12.877	12.877	0.000	0.000	0.000	0.000
50	A	383	ALA	0	0.034	0.022	18.589	-0.693	-0.693	0.000	0.000	0.000	0.000
51	A	384	LEU	0	-0.003	0.018	15.222	-0.626	-0.626	0.000	0.000	0.000	0.000
52	A	385	LEU	0	-0.017	-0.022	12.478	-1.504	-1.504	0.000	0.000	0.000	0.000
53	A	386	ALA	0	-0.037	-0.008	13.738	-1.425	-1.425	0.000	0.000	0.000	0.000
54	A	387	SER	0	-0.024	-0.022	15.425	-0.331	-0.331	0.000	0.000	0.000	0.000
55	A	388	TRP	0	0.015	0.008	7.406	-1.624	-1.624	0.000	0.000	0.000	0.000
56	A	389	GLY	0	-0.021	-0.010	10.478	-2.164	-2.164	0.000	0.000	0.000	0.000
57	A	390	ALA	0	0.012	0.017	11.565	-0.459	-0.459	0.000	0.000	0.000	0.000
58	A	391	GLN	0	-0.051	-0.023	11.229	2.302	2.302	0.000	0.000	0.000	0.000
59	A	392	ASP	-1	-0.873	-0.933	9.258	-35.425	-35.425	0.000	0.000	0.000	0.000
60	A	393	SER	0	-0.027	-0.021	5.836	-2.738	-2.738	0.000	0.000	0.000	0.000
61	A	394	ALA	0	0.013	0.025	5.523	-5.669	-5.669	0.000	0.000	0.000	0.000
66	A	399	LEU	0	0.015	0.007	5.886	6.183	6.183	0.000	0.000	0.000	0.000
67	A	400	LEU	0	-0.019	0.002	7.347	3.518	3.518	0.000	0.000	0.000	0.000
68	A	401	ALA	0	-0.009	-0.007	8.090	3.387	3.387	0.000	0.000	0.000	0.000
69	A	402	ALA	0	-0.023	-0.008	9.883	2.875	2.875	0.000	0.000	0.000	0.000
70	A	403	LEU	0	0.013	-0.004	12.072	2.132	2.132	0.000	0.000	0.000	0.000
71	A	404	ARG	1	0.760	0.840	11.761	24.671	24.671	0.000	0.000	0.000	0.000
72	A	405	ARG	1	0.810	0.905	12.272	23.124	23.124	0.000	0.000	0.000	0.000
73	A	406	ILE	0	-0.022	-0.006	15.777	1.189	1.189	0.000	0.000	0.000	0.000
74	A	407	GLN	0	-0.042	-0.025	17.862	1.296	1.296	0.000	0.000	0.000	0.000
75	A	408	ARG	1	0.852	0.928	17.932	15.119	15.119	0.000	0.000	0.000	0.000
76	A	409	ALA	0	0.012	-0.012	16.075	-0.946	-0.946	0.000	0.000	0.000	0.000
77	A	410	ASP	-1	-0.836	-0.903	16.771	-15.993	-15.993	0.000	0.000	0.000	0.000
78	A	411	ILE	0	-0.008	-0.005	15.293	-0.094	-0.094	0.000	0.000	0.000	0.000
79	A	412	VAL	0	-0.051	-0.021	11.255	-1.165	-1.165	0.000	0.000	0.000	0.000
80	A	413	GLU	-1	-0.754	-0.862	12.686	-22.599	-22.599	0.000	0.000	0.000	0.000
81	A	414	SER	0	-0.045	-0.029	14.985	-0.179	-0.179	0.000	0.000	0.000	0.000
82	A	415	LEU	0	-0.002	-0.022	10.817	-0.614	-0.614	0.000	0.000	0.000	0.000
83	A	416	CYS	0	-0.076	-0.019	10.489	-2.518	-2.518	0.000	0.000	0.000	0.000
84	A	417	SER	0	-0.098	-0.063	11.573	-0.119	-0.119	0.000	0.000	0.000	0.000
85	A	418	GLU	-2	-1.649	-1.755	13.988	-31.397	-31.397	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:334:GLY)