FMO DATABASE

FMODB ID: RL9G8

Calculation Name: 1V60-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V60

Chain ID: A

ChEMBL ID:

UniProt ID: Q9D8S9

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-811115.468465
FMO2-HF: Nuclear repulsion	766089.42736
FMO2-HF: Total energy	-45026.041105
FMO2-MP2: Total energy	-45156.123979

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:6:GLY)

Summations of interaction energy for fragment #1(A:6: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.
3.1	4.059	-0.013	-0.35	-0.596	-0.001

Interaction energy analysis for fragmet #1(A:6:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.866 / 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	8	SER	0	0.070	0.028	3.827	3.075	4.034	-0.013	-0.350	-0.596	-0.001
4	A	9	GLY	0	0.022	0.015	6.794	0.568	0.568	0.000	0.000	0.000	0.000
5	A	10	SER	0	-0.042	-0.014	5.678	2.807	2.807	0.000	0.000	0.000	0.000
6	A	11	SER	0	0.006	0.002	8.413	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	12	GLY	0	0.023	0.017	9.678	-0.120	-0.120	0.000	0.000	0.000	0.000
8	A	13	MET	0	0.024	-0.006	10.308	2.252	2.252	0.000	0.000	0.000	0.000
9	A	14	ALA	0	-0.007	0.003	12.565	-0.802	-0.802	0.000	0.000	0.000	0.000
10	A	15	THR	0	-0.036	-0.019	13.811	0.342	0.342	0.000	0.000	0.000	0.000
11	A	16	ARG	1	0.995	0.993	15.453	16.278	16.278	0.000	0.000	0.000	0.000
12	A	17	SER	0	-0.004	0.004	17.416	0.566	0.566	0.000	0.000	0.000	0.000
13	A	18	CYS	0	-0.026	-0.015	20.562	-0.396	-0.396	0.000	0.000	0.000	0.000
14	A	19	VAL	0	-0.026	-0.015	22.792	0.329	0.329	0.000	0.000	0.000	0.000
15	A	20	SER	0	0.064	0.037	26.546	-0.031	-0.031	0.000	0.000	0.000	0.000
16	A	21	ARG	1	0.936	0.961	28.929	9.789	9.789	0.000	0.000	0.000	0.000
17	A	22	GLY	0	0.017	0.014	32.600	0.017	0.017	0.000	0.000	0.000	0.000
18	A	23	SER	0	-0.016	-0.001	34.823	0.123	0.123	0.000	0.000	0.000	0.000
19	A	24	ALA	0	-0.017	-0.020	30.580	-0.289	-0.289	0.000	0.000	0.000	0.000
20	A	25	GLY	0	0.055	0.022	31.171	0.238	0.238	0.000	0.000	0.000	0.000
21	A	26	SER	0	-0.060	-0.019	27.245	0.061	0.061	0.000	0.000	0.000	0.000
22	A	27	ALA	0	0.004	0.002	26.075	-0.179	-0.179	0.000	0.000	0.000	0.000
23	A	28	ALA	0	0.011	0.008	28.128	0.333	0.333	0.000	0.000	0.000	0.000
24	A	29	ALA	0	0.007	0.012	30.164	-0.236	-0.236	0.000	0.000	0.000	0.000
25	A	30	GLY	0	0.074	0.040	31.193	-0.119	-0.119	0.000	0.000	0.000	0.000
26	A	31	PRO	0	-0.058	-0.034	29.845	-0.023	-0.023	0.000	0.000	0.000	0.000
27	A	32	VAL	0	0.039	0.025	31.467	0.063	0.063	0.000	0.000	0.000	0.000
28	A	33	GLU	-1	-0.808	-0.927	34.514	-8.761	-8.761	0.000	0.000	0.000	0.000
29	A	34	ALA	0	-0.004	-0.008	31.185	0.105	0.105	0.000	0.000	0.000	0.000
30	A	35	ALA	0	0.015	0.013	33.191	0.048	0.048	0.000	0.000	0.000	0.000
31	A	36	ILE	0	0.013	0.002	34.957	0.200	0.200	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.896	0.955	34.357	9.074	9.074	0.000	0.000	0.000	0.000
33	A	38	ALA	0	0.033	0.017	33.159	0.148	0.148	0.000	0.000	0.000	0.000
34	A	39	LYS	1	0.933	0.974	35.207	8.293	8.293	0.000	0.000	0.000	0.000
35	A	40	LEU	0	0.017	0.009	38.083	0.174	0.174	0.000	0.000	0.000	0.000
36	A	41	GLU	-1	-0.889	-0.970	34.712	-8.932	-8.932	0.000	0.000	0.000	0.000
37	A	42	GLN	0	-0.065	-0.032	35.114	0.129	0.129	0.000	0.000	0.000	0.000
38	A	43	ALA	0	-0.041	-0.013	39.162	0.149	0.149	0.000	0.000	0.000	0.000
39	A	44	LEU	0	-0.085	-0.054	42.241	0.263	0.263	0.000	0.000	0.000	0.000
40	A	45	SER	0	-0.020	0.004	40.943	0.151	0.151	0.000	0.000	0.000	0.000
41	A	46	PRO	0	-0.086	-0.038	40.963	0.144	0.144	0.000	0.000	0.000	0.000
42	A	47	GLU	-1	-0.911	-0.953	41.681	-7.289	-7.289	0.000	0.000	0.000	0.000
43	A	48	VAL	0	-0.024	-0.016	41.219	-0.144	-0.144	0.000	0.000	0.000	0.000
44	A	49	LEU	0	-0.001	0.000	38.732	0.194	0.194	0.000	0.000	0.000	0.000
45	A	50	GLU	-1	-0.848	-0.907	38.117	-8.666	-8.666	0.000	0.000	0.000	0.000
46	A	51	LEU	0	-0.060	-0.032	37.281	0.208	0.208	0.000	0.000	0.000	0.000
47	A	52	ARG	1	0.860	0.928	36.483	8.241	8.241	0.000	0.000	0.000	0.000
48	A	53	ASN	0	0.014	0.006	37.110	0.267	0.267	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.828	-0.916	39.002	-7.369	-7.369	0.000	0.000	0.000	0.000
50	A	55	SER	0	-0.046	-0.020	40.599	0.009	0.009	0.000	0.000	0.000	0.000
51	A	56	GLY	0	0.041	0.023	42.566	-0.024	-0.024	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.028	-0.014	45.856	0.077	0.077	0.000	0.000	0.000	0.000
53	A	58	HIS	0	-0.023	-0.007	45.559	0.220	0.220	0.000	0.000	0.000	0.000
54	A	59	ALA	0	0.008	-0.002	48.191	-0.109	-0.109	0.000	0.000	0.000	0.000
55	A	60	VAL	0	-0.008	0.002	44.142	0.042	0.042	0.000	0.000	0.000	0.000
56	A	61	PRO	0	0.002	0.006	41.081	-0.051	-0.051	0.000	0.000	0.000	0.000
57	A	62	ALA	0	0.045	0.024	37.425	-0.016	-0.016	0.000	0.000	0.000	0.000
58	A	63	GLY	0	0.042	0.012	36.341	-0.093	-0.093	0.000	0.000	0.000	0.000
59	A	64	SER	0	-0.038	-0.022	37.206	0.001	0.001	0.000	0.000	0.000	0.000
60	A	65	GLU	-1	-0.897	-0.955	35.001	-8.865	-8.865	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.009	-0.001	39.578	0.022	0.022	0.000	0.000	0.000	0.000
62	A	67	HIS	0	-0.002	-0.008	42.953	0.085	0.085	0.000	0.000	0.000	0.000
63	A	68	PHE	0	-0.006	0.003	37.427	-0.144	-0.144	0.000	0.000	0.000	0.000
64	A	69	ARG	1	0.904	0.968	42.375	6.886	6.886	0.000	0.000	0.000	0.000
65	A	70	VAL	0	0.035	0.032	41.030	-0.169	-0.169	0.000	0.000	0.000	0.000
66	A	71	ALA	0	-0.024	-0.016	42.787	0.243	0.243	0.000	0.000	0.000	0.000
67	A	72	VAL	0	0.006	0.008	43.114	-0.166	-0.166	0.000	0.000	0.000	0.000
68	A	73	VAL	0	0.006	0.016	44.703	0.216	0.216	0.000	0.000	0.000	0.000
69	A	74	SER	0	0.064	0.015	45.868	-0.060	-0.060	0.000	0.000	0.000	0.000
70	A	75	SER	0	0.023	0.004	47.785	0.101	0.101	0.000	0.000	0.000	0.000
71	A	76	ARG	1	0.955	0.980	47.670	6.536	6.536	0.000	0.000	0.000	0.000
72	A	77	PHE	0	0.021	-0.012	47.639	0.114	0.114	0.000	0.000	0.000	0.000
73	A	78	GLU	-1	-0.915	-0.958	53.002	-5.738	-5.738	0.000	0.000	0.000	0.000
74	A	79	GLY	0	-0.023	-0.003	55.675	0.059	0.059	0.000	0.000	0.000	0.000
75	A	80	MET	0	-0.045	-0.003	53.730	0.114	0.114	0.000	0.000	0.000	0.000
76	A	81	SER	0	0.056	0.028	57.509	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	82	PRO	0	0.017	-0.001	55.947	-0.112	-0.112	0.000	0.000	0.000	0.000
78	A	83	LEU	0	0.063	0.023	54.871	-0.112	-0.112	0.000	0.000	0.000	0.000
79	A	84	GLN	0	-0.003	-0.012	54.609	-0.029	-0.029	0.000	0.000	0.000	0.000
80	A	85	ARG	1	0.834	0.923	51.726	5.734	5.734	0.000	0.000	0.000	0.000
81	A	86	HIS	0	0.011	0.013	50.116	-0.137	-0.137	0.000	0.000	0.000	0.000
82	A	87	ARG	1	0.975	0.995	49.727	5.836	5.836	0.000	0.000	0.000	0.000
83	A	88	LEU	0	0.016	0.001	48.706	-0.048	-0.048	0.000	0.000	0.000	0.000
84	A	89	VAL	0	0.000	0.005	44.491	-0.128	-0.128	0.000	0.000	0.000	0.000
85	A	90	HIS	0	0.006	-0.011	45.543	-0.081	-0.081	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.960	-0.955	47.290	-6.298	-6.298	0.000	0.000	0.000	0.000
87	A	92	ALA	0	-0.012	-0.001	42.886	-0.100	-0.100	0.000	0.000	0.000	0.000
88	A	93	LEU	0	-0.061	-0.040	39.373	-0.232	-0.232	0.000	0.000	0.000	0.000
89	A	94	SER	0	0.006	-0.017	43.207	0.088	0.088	0.000	0.000	0.000	0.000
90	A	95	GLU	-1	-0.962	-0.985	41.408	-7.572	-7.572	0.000	0.000	0.000	0.000
91	A	96	GLU	-1	-0.927	-0.971	38.782	-8.205	-8.205	0.000	0.000	0.000	0.000
92	A	97	LEU	0	-0.025	-0.023	42.360	0.028	0.028	0.000	0.000	0.000	0.000
93	A	98	ALA	0	-0.053	-0.008	45.623	0.166	0.166	0.000	0.000	0.000	0.000
94	A	99	GLY	0	0.059	0.022	42.881	-0.033	-0.033	0.000	0.000	0.000	0.000
95	A	100	PRO	0	-0.089	-0.017	39.083	0.083	0.083	0.000	0.000	0.000	0.000
96	A	101	VAL	0	-0.017	-0.011	41.240	0.053	0.053	0.000	0.000	0.000	0.000
97	A	102	HIS	0	-0.041	-0.025	43.602	0.203	0.203	0.000	0.000	0.000	0.000
98	A	103	ALA	0	-0.034	-0.020	46.763	0.177	0.177	0.000	0.000	0.000	0.000
99	A	104	LEU	0	0.029	0.020	42.797	-0.117	-0.117	0.000	0.000	0.000	0.000
100	A	105	ALA	0	-0.036	-0.010	46.573	0.119	0.119	0.000	0.000	0.000	0.000
101	A	106	ILE	0	0.009	0.002	45.900	-0.095	-0.095	0.000	0.000	0.000	0.000
102	A	107	GLN	0	-0.010	-0.015	47.130	0.254	0.254	0.000	0.000	0.000	0.000
103	A	108	ALA	0	0.019	0.021	47.822	-0.111	-0.111	0.000	0.000	0.000	0.000
104	A	109	LYS	1	0.910	0.957	49.162	6.514	6.514	0.000	0.000	0.000	0.000
105	A	110	THR	0	0.075	0.036	49.785	-0.105	-0.105	0.000	0.000	0.000	0.000
106	A	111	PRO	0	0.056	0.014	48.418	0.014	0.014	0.000	0.000	0.000	0.000
107	A	112	ALA	0	-0.005	0.010	50.118	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	113	GLN	0	0.022	-0.009	53.517	0.021	0.021	0.000	0.000	0.000	0.000
109	A	114	TRP	0	0.020	0.015	44.454	0.046	0.046	0.000	0.000	0.000	0.000
110	A	115	ARG	1	0.926	0.954	48.701	6.360	6.360	0.000	0.000	0.000	0.000
111	A	116	GLU	-1	-0.949	-0.951	51.484	-5.602	-5.602	0.000	0.000	0.000	0.000
112	A	117	ASN	0	-0.038	-0.020	51.715	0.075	0.075	0.000	0.000	0.000	0.000
113	A	118	PRO	0	-0.029	-0.011	46.936	-0.043	-0.043	0.000	0.000	0.000	0.000
114	A	119	GLN	0	-0.039	-0.011	46.856	-0.130	-0.130	0.000	0.000	0.000	0.000
115	A	120	LEU	0	-0.047	-0.032	44.002	0.084	0.084	0.000	0.000	0.000	0.000
116	A	121	ASP	-1	-0.881	-0.934	47.790	-6.305	-6.305	0.000	0.000	0.000	0.000
117	A	122	ILE	0	-0.128	-0.080	42.093	0.075	0.075	0.000	0.000	0.000	0.000
118	A	123	SER	0	0.056	0.014	44.203	0.024	0.024	0.000	0.000	0.000	0.000
119	A	124	PRO	0	-0.023	0.000	46.339	0.061	0.061	0.000	0.000	0.000	0.000
120	A	125	PRO	0	0.009	0.007	46.861	-0.150	-0.150	0.000	0.000	0.000	0.000
121	A	126	CYS	0	-0.082	-0.045	45.789	0.093	0.093	0.000	0.000	0.000	0.000
122	A	127	LEU	0	-0.014	-0.014	42.669	-0.169	-0.169	0.000	0.000	0.000	0.000
123	A	128	GLY	-1	-0.934	-0.950	41.538	-7.622	-7.622	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:GLY)