FMO DATABASE

FMODB ID: 67K3Z

Calculation Name: 5GVQ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5GVQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q15427

Base Structure: SolutionNMR

Registration Date: 2025-10-04

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	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-719426.306275
FMO2-HF: Nuclear repulsion	679443.172184
FMO2-HF: Total energy	-39983.134091
FMO2-MP2: Total energy	-40099.5488

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.
-60.814	-59.502	-0.004	-0.469	-0.838	-0.002

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 : 0.874 / q_NPA : 0.920

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	3	SER	0	0.067	0.046	3.835	4.164	5.273	-0.003	-0.417	-0.689	-0.002
4	A	4	GLY	0	-0.022	0.006	4.103	6.718	6.921	-0.001	-0.052	-0.149	0.000
5	A	5	SER	0	-0.059	-0.043	5.439	2.428	2.428	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.002	-0.001	7.662	4.518	4.518	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.006	0.019	10.235	-1.666	-1.666	0.000	0.000	0.000	0.000
8	A	8	PRO	0	-0.011	-0.004	12.148	0.179	0.179	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.023	0.008	14.095	1.136	1.136	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.012	-0.009	17.766	-0.158	-0.158	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.980	-0.978	20.762	-13.672	-13.672	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.814	0.898	17.604	15.729	15.729	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.070	0.029	19.654	0.301	0.301	0.000	0.000	0.000	0.000
14	A	14	GLN	0	-0.042	-0.036	21.272	-0.204	-0.204	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.839	-0.888	21.440	-12.838	-12.838	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.037	0.010	16.568	-0.321	-0.321	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.040	-0.028	17.931	-0.494	-0.494	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.003	0.010	19.821	0.463	0.463	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.014	-0.011	22.406	0.191	0.191	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.008	-0.006	23.957	-0.092	-0.092	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.043	0.014	26.961	0.227	0.227	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.016	0.005	30.727	-0.078	-0.078	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.047	-0.014	27.672	0.036	0.036	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.755	-0.868	31.641	-8.569	-8.569	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.935	-0.963	32.641	-8.372	-8.372	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.863	0.926	32.397	8.818	8.818	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.034	-0.016	27.185	-0.338	-0.338	0.000	0.000	0.000	0.000
28	A	28	SER	0	0.022	0.005	27.437	0.129	0.129	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.720	-0.859	24.150	-11.416	-11.416	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.025	0.003	22.056	-0.525	-0.525	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.013	0.025	21.670	-0.464	-0.464	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.004	-0.010	22.343	-0.301	-0.301	0.000	0.000	0.000	0.000
33	A	33	TRP	0	0.007	-0.001	15.150	0.116	0.116	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.945	-0.982	17.508	-15.704	-15.704	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.048	-0.013	18.073	-0.399	-0.399	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.039	-0.002	17.881	-0.078	-0.078	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.003	0.005	12.184	-0.884	-0.884	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.113	-0.057	13.161	-1.076	-1.076	0.000	0.000	0.000	0.000
39	A	39	ALA	0	-0.049	-0.008	14.724	-0.058	-0.058	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.072	0.031	10.572	-1.057	-1.057	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.049	-0.025	8.064	1.079	1.079	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.004	0.009	10.473	0.639	0.639	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.059	-0.032	12.758	-0.712	-0.712	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.043	-0.040	15.055	1.026	1.026	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.019	-0.001	18.878	0.087	0.087	0.000	0.000	0.000	0.000
46	A	46	HIS	0	0.003	0.004	21.878	0.276	0.276	0.000	0.000	0.000	0.000
47	A	47	MET	0	-0.007	0.008	25.663	-0.115	-0.115	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.012	0.013	28.859	0.202	0.202	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.818	0.898	29.567	10.415	10.415	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.770	-0.876	34.934	-7.551	-7.551	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.894	0.945	38.702	7.576	7.576	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.042	-0.017	41.311	0.158	0.158	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.041	-0.043	40.855	0.021	0.021	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.005	0.018	37.975	-0.058	-0.058	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.022	-0.011	36.032	-0.429	-0.429	0.000	0.000	0.000	0.000
56	A	56	HIS	0	0.001	-0.013	32.086	0.029	0.029	0.000	0.000	0.000	0.000
57	A	57	GLN	0	-0.022	-0.022	34.018	0.094	0.094	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.022	0.021	34.079	0.122	0.122	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.079	-0.048	30.403	0.014	0.014	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.003	-0.007	27.428	0.118	0.118	0.000	0.000	0.000	0.000
61	A	61	PHE	0	-0.031	-0.006	24.032	0.173	0.173	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.002	0.006	18.141	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.765	-0.849	17.508	-15.624	-15.624	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.019	0.001	13.202	-0.318	-0.318	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.026	-0.017	8.334	-0.136	-0.136	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.013	0.008	10.692	-0.145	-0.145	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.845	-0.908	13.477	-14.831	-14.831	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.944	-0.974	11.946	-23.623	-23.623	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.866	-0.947	10.703	-27.029	-27.029	0.000	0.000	0.000	0.000
70	A	70	ALA	0	0.010	0.012	13.722	0.899	0.899	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.868	-0.943	17.258	-13.596	-13.596	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.044	-0.020	14.763	1.335	1.335	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.028	0.001	17.046	0.637	0.637	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.046	-0.021	18.572	0.809	0.809	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.886	0.947	20.269	14.914	14.914	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.032	-0.009	17.530	0.486	0.486	0.000	0.000	0.000	0.000
77	A	77	MET	0	-0.004	0.008	19.884	0.483	0.483	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.796	-0.880	23.611	-10.235	-10.235	0.000	0.000	0.000	0.000
79	A	79	MET	0	-0.059	-0.029	26.876	0.193	0.193	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.029	0.035	25.186	0.420	0.420	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.895	0.940	29.131	8.772	8.772	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.064	0.050	26.724	0.102	0.102	0.000	0.000	0.000	0.000
83	A	83	TYR	0	-0.003	-0.019	29.407	0.351	0.351	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.009	0.008	32.446	0.322	0.322	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.823	0.885	33.586	8.842	8.842	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.038	-0.019	32.462	-0.233	-0.233	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.002	0.013	26.109	0.170	0.170	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.793	0.870	28.625	10.426	10.426	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.003	-0.001	23.401	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.037	-0.028	25.874	-0.088	-0.088	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.851	0.912	20.731	14.076	14.076	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.023	-0.010	23.916	0.556	0.556	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.032	-0.023	25.282	0.495	0.495	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.053	-0.024	27.416	0.479	0.479	0.000	0.000	0.000	0.000
95	A	95	HIS	0	0.035	0.024	29.606	0.046	0.046	0.000	0.000	0.000	0.000
96	A	96	ASN	0	0.015	0.002	31.479	-0.392	-0.392	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.921	0.974	30.760	9.683	9.683	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.013	-0.007	32.773	0.230	0.230	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.048	0.032	34.697	0.235	0.235	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.027	-0.050	34.225	-0.410	-0.410	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.015	0.021	34.398	0.266	0.266	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.003	0.012	34.283	-0.184	-0.184	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.022	-0.024	30.241	-0.063	-0.063	0.000	0.000	0.000	0.000
104	A	104	SER	0	-0.049	-0.032	30.939	-0.409	-0.409	0.000	0.000	0.000	0.000
105	A	105	GLY	-1	-0.897	-0.923	33.563	-8.243	-8.243	0.000	0.000	0.000	0.000

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