FMO DATABASE

FMODB ID: QLYGY

Calculation Name: 1V5Q-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V5Q

Chain ID: A

ChEMBL ID:

UniProt ID: Q925T6

Base Structure: SolutionNMR

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-776521.346947
FMO2-HF: Nuclear repulsion	732583.601823
FMO2-HF: Total energy	-43937.745124
FMO2-MP2: Total energy	-44065.827414

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.
-176.731	-173.908	0.2	-1.69	-1.333	-0.017

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 : 0.842 / q_NPA : 0.908

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	3	SER	0	-0.008	-0.006	2.735	-20.825	-18.059	0.201	-1.687	-1.281	-0.017
4	A	4	GLY	0	0.037	0.027	5.339	5.646	5.703	-0.001	-0.003	-0.052	0.000
5	A	5	SER	0	-0.036	-0.035	7.910	-3.267	-3.267	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.031	0.031	7.300	-1.421	-1.421	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.022	-0.007	9.677	1.633	1.633	0.000	0.000	0.000	0.000
8	A	8	ALA	0	-0.034	0.002	12.785	-0.296	-0.296	0.000	0.000	0.000	0.000
9	A	9	GLY	0	-0.014	-0.006	12.341	0.543	0.543	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.033	-0.018	13.227	-0.243	-0.243	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.030	-0.021	11.952	-1.127	-1.127	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.031	0.038	15.296	0.671	0.671	0.000	0.000	0.000	0.000
13	A	13	HIS	0	-0.035	-0.014	17.318	-1.009	-1.009	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.035	-0.035	18.198	0.231	0.231	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.909	-0.957	20.782	-11.153	-11.153	0.000	0.000	0.000	0.000
16	A	16	THR	0	-0.018	-0.007	24.027	-0.220	-0.220	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.053	-0.028	26.195	0.506	0.506	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.859	-0.918	29.342	-8.940	-8.940	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.027	-0.019	30.629	0.249	0.249	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.022	0.017	33.381	0.127	0.127	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.019	0.003	34.994	0.154	0.154	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.025	-0.035	38.603	0.117	0.117	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.032	-0.004	42.279	-0.032	-0.032	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.819	-0.907	43.238	-6.894	-6.894	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.062	-0.038	45.169	0.014	0.014	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.066	-0.031	46.607	0.137	0.137	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.008	-0.012	42.227	-0.049	-0.049	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.014	0.001	41.588	-0.198	-0.198	0.000	0.000	0.000	0.000
29	A	29	PHE	0	0.029	-0.004	37.070	-0.004	-0.004	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.007	0.007	37.726	-0.087	-0.087	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.048	0.019	31.750	-0.160	-0.160	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.009	-0.004	31.894	-0.018	-0.018	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.023	0.024	27.920	-0.270	-0.270	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.017	-0.018	21.831	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.051	0.006	24.739	-0.347	-0.347	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.077	-0.037	25.823	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	37	VAL	0	0.007	0.007	27.754	0.053	0.053	0.000	0.000	0.000	0.000
38	A	38	PHE	0	-0.029	-0.019	29.261	0.256	0.256	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.015	0.011	24.943	-0.405	-0.405	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.067	-0.036	24.148	0.503	0.503	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.957	-0.982	23.198	-12.942	-12.942	0.000	0.000	0.000	0.000
42	A	42	THR	0	0.084	0.071	21.214	0.161	0.161	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.032	0.024	22.959	0.282	0.282	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.128	-0.072	18.856	-0.423	-0.423	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.030	-0.020	17.927	-0.907	-0.907	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.077	0.047	17.834	0.594	0.594	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.001	-0.004	20.840	-0.027	-0.027	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.007	0.008	19.656	0.224	0.224	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.007	0.004	23.964	0.440	0.440	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.067	-0.027	26.933	-0.249	-0.249	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.044	-0.036	28.391	0.067	0.067	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.054	0.035	30.604	-0.050	-0.050	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.895	-0.950	34.107	-8.571	-8.571	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.021	0.018	37.849	0.015	0.015	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.973	-0.995	39.761	-7.017	-7.017	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.017	-0.005	38.131	0.110	0.110	0.000	0.000	0.000	0.000
57	A	57	PRO	0	-0.049	-0.022	39.543	-0.050	-0.050	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.049	0.018	34.583	-0.087	-0.087	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.887	-0.946	34.865	-9.459	-9.459	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.817	0.905	36.794	7.265	7.265	0.000	0.000	0.000	0.000
61	A	61	CYS	0	-0.068	-0.030	35.951	0.141	0.141	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.002	0.005	34.549	-0.051	-0.051	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.076	-0.044	31.634	-0.245	-0.245	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.026	0.013	29.643	-0.274	-0.274	0.000	0.000	0.000	0.000
65	A	65	GLN	0	-0.012	-0.012	25.422	0.475	0.475	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.025	-0.016	26.818	-0.173	-0.173	0.000	0.000	0.000	0.000
67	A	67	GLY	0	-0.019	-0.019	23.555	-0.362	-0.362	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.851	-0.923	22.423	-12.467	-12.467	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.882	0.938	19.903	14.406	14.406	0.000	0.000	0.000	0.000
70	A	70	VAL	0	-0.036	-0.008	22.108	0.173	0.173	0.000	0.000	0.000	0.000
71	A	71	MET	0	0.007	0.009	19.038	-0.531	-0.531	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.044	0.018	23.799	0.077	0.077	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.017	-0.006	27.375	0.142	0.142	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.001	-0.023	30.783	0.089	0.089	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.018	0.023	30.761	0.244	0.244	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.035	-0.012	29.508	-0.103	-0.103	0.000	0.000	0.000	0.000
77	A	77	PRO	0	0.035	0.023	25.338	-0.166	-0.166	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.021	-0.014	23.837	0.234	0.234	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.979	-1.012	20.171	-15.618	-15.618	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.926	-0.962	23.253	-11.695	-11.695	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.062	-0.037	25.889	0.114	0.114	0.000	0.000	0.000	0.000
82	A	82	THR	0	-0.029	-0.021	27.445	-0.338	-0.338	0.000	0.000	0.000	0.000
83	A	83	PHE	0	0.005	-0.004	28.268	0.105	0.105	0.000	0.000	0.000	0.000
84	A	84	GLU	-1	-0.924	-0.968	29.542	-8.965	-8.965	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.890	-0.913	31.272	-9.508	-9.508	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.081	0.038	29.338	0.206	0.206	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.028	-0.018	31.476	0.446	0.446	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.034	-0.040	34.150	0.486	0.486	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.036	0.033	31.653	0.259	0.259	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.019	0.036	33.051	0.215	0.215	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.891	0.945	36.491	8.242	8.242	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.884	-0.937	38.775	-7.614	-7.614	0.000	0.000	0.000	0.000
93	A	93	SER	0	0.036	0.001	37.363	0.166	0.166	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.059	-0.052	39.958	0.103	0.103	0.000	0.000	0.000	0.000
95	A	95	ILE	0	-0.085	-0.023	42.929	0.235	0.235	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.073	-0.036	41.550	0.180	0.180	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.040	-0.028	43.935	0.045	0.045	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.861	0.924	39.956	7.552	7.552	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.033	0.038	34.481	0.001	0.001	0.000	0.000	0.000	0.000
100	A	100	THR	0	-0.038	-0.020	33.037	0.119	0.119	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.029	-0.020	29.878	-0.142	-0.142	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.904	-0.944	26.508	-11.020	-11.020	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.014	-0.008	24.986	-0.484	-0.484	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.826	-0.907	18.796	-15.609	-15.609	0.000	0.000	0.000	0.000
105	A	105	PHE	0	-0.101	-0.073	22.053	-0.132	-0.132	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.832	-0.918	18.450	-16.401	-16.401	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.024	-0.002	21.374	0.820	0.820	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.035	-0.020	22.745	-0.468	-0.468	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.885	-0.946	19.639	-15.541	-15.541	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.049	-0.032	24.222	0.408	0.408	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.017	-0.005	21.794	-0.236	-0.236	0.000	0.000	0.000	0.000
112	A	112	ILE	0	-0.020	-0.009	24.844	0.520	0.520	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.010	0.011	25.430	-0.510	-0.510	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.005	-0.006	24.768	0.280	0.280	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.015	-0.006	26.770	0.308	0.308	0.000	0.000	0.000	0.000
116	A	116	GLY	0	0.035	0.000	29.713	-0.208	-0.208	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.072	-0.040	31.213	0.500	0.500	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.025	0.016	31.331	-0.312	-0.312	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.006	0.014	29.213	0.219	0.219	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.015	-0.018	32.191	0.114	0.114	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.046	-0.034	35.474	-0.157	-0.157	0.000	0.000	0.000	0.000
122	A	122	GLY	-1	-0.926	-0.937	36.717	-8.271	-8.271	0.000	0.000	0.000	0.000

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