FMO DATABASE

FMODB ID: KK5L3

Calculation Name: 1V4L-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V4L

Chain ID: A

ChEMBL ID:

UniProt ID: Q6TPH0

Base Structure: X-ray

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1214971.056839
FMO2-HF: Nuclear repulsion	1158544.368839
FMO2-HF: Total energy	-56426.687999
FMO2-MP2: Total energy	-56587.294636

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:ASP)

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

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.
-12.948	-10.973	-0.021	-0.895	-1.059	-0.001

Interaction energy analysis for fragmet #1(A:1:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.110 / q_NPA : -0.059

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	ASP	-1	-0.883	-0.921	3.840	-1.557	0.418	-0.021	-0.895	-1.059	-0.001
4	A	4	CYS	0	-0.085	-0.064	6.677	-0.757	-0.757	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.009	0.023	10.104	0.543	0.543	0.000	0.000	0.000	0.000
6	A	6	PRO	0	0.038	0.010	13.738	0.116	0.116	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.003	-0.004	15.202	-0.022	-0.022	0.000	0.000	0.000	0.000
8	A	8	TRP	0	-0.044	-0.029	13.253	0.062	0.062	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.054	-0.026	11.264	0.211	0.211	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.035	0.017	6.538	-0.118	-0.118	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.009	-0.010	8.508	1.027	1.027	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.868	-0.929	8.272	-3.234	-3.234	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.866	0.935	6.342	1.925	1.925	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.017	-0.039	7.871	-0.110	-0.110	0.000	0.000	0.000	0.000
15	A	16	TYR	0	-0.042	-0.054	11.241	0.179	0.179	0.000	0.000	0.000	0.000
16	A	17	GLN	0	0.006	0.004	14.554	0.179	0.179	0.000	0.000	0.000	0.000
17	A	18	ALA	0	-0.022	-0.010	17.522	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	PHE	0	0.026	0.019	20.655	0.036	0.036	0.000	0.000	0.000	0.000
19	A	20	SER	0	0.014	-0.012	23.986	0.043	0.043	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.883	-0.952	26.631	-0.257	-0.257	0.000	0.000	0.000	0.000
21	A	22	PRO	0	-0.053	-0.025	29.477	-0.033	-0.033	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.965	0.999	28.682	0.395	0.395	0.000	0.000	0.000	0.000
23	A	24	ASN	0	-0.001	0.030	31.798	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	25	TRP	0	0.049	-0.017	27.209	-0.019	-0.019	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.918	-0.962	29.665	-0.446	-0.446	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.855	-0.929	30.743	-0.409	-0.409	0.000	0.000	0.000	0.000
27	A	28	ALA	0	-0.061	-0.034	27.075	-0.032	-0.032	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.819	-0.918	24.605	-0.881	-0.881	0.000	0.000	0.000	0.000
29	A	30	SER	0	0.017	-0.006	26.049	-0.060	-0.060	0.000	0.000	0.000	0.000
30	A	31	PHE	0	-0.017	-0.018	24.189	-0.036	-0.036	0.000	0.000	0.000	0.000
31	A	32	CYS	0	-0.104	-0.005	19.607	-0.109	-0.109	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.821	-0.890	22.107	-0.981	-0.981	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.973	-0.989	24.155	-0.687	-0.687	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.000	0.005	21.973	-0.023	-0.023	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.005	-0.006	15.643	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.868	0.937	19.084	1.136	1.136	0.000	0.000	0.000	0.000
37	A	38	THR	0	0.011	-0.005	15.294	0.187	0.187	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.083	-0.054	18.167	-0.033	-0.033	0.000	0.000	0.000	0.000
39	A	40	HIS	1	0.829	0.903	19.033	1.256	1.256	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.014	-0.005	20.134	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.070	-0.026	17.636	-0.053	-0.053	0.000	0.000	0.000	0.000
42	A	43	SER	0	0.006	0.003	18.505	0.097	0.097	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.050	-0.030	18.270	-0.037	-0.037	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.772	-0.863	15.846	-1.469	-1.469	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.024	-0.016	16.232	0.103	0.103	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.005	-0.009	18.808	0.003	0.003	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.047	0.032	15.928	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.747	-0.824	14.992	-1.074	-1.074	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.030	0.007	15.903	-0.015	-0.015	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.861	-0.935	17.546	0.319	0.319	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.039	0.026	12.162	0.051	0.051	0.000	0.000	0.000	0.000
52	A	53	VAL	0	0.001	-0.006	15.949	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	54	ALA	0	-0.005	0.000	18.207	0.019	0.019	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.031	-0.029	16.757	0.009	0.009	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.011	0.004	15.128	0.043	0.043	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.017	-0.019	18.326	-0.015	-0.015	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.060	-0.029	21.998	0.009	0.009	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.898	-0.919	18.900	0.348	0.348	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.880	0.914	16.883	-0.196	-0.196	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.025	0.006	21.743	-0.029	-0.029	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.952	0.966	24.836	-0.139	-0.139	0.000	0.000	0.000	0.000
62	A	63	THR	0	0.020	0.019	27.307	0.016	0.016	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.029	-0.016	30.077	0.001	0.001	0.000	0.000	0.000	0.000
64	A	65	PHE	0	0.030	0.007	27.129	-0.024	-0.024	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.006	0.004	32.353	0.017	0.017	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.030	-0.025	30.605	0.023	0.023	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.041	0.033	24.378	0.004	0.004	0.000	0.000	0.000	0.000
68	A	69	TRP	0	-0.051	-0.032	26.747	0.003	0.003	0.000	0.000	0.000	0.000
69	A	70	ILE	0	0.027	0.012	22.877	-0.022	-0.022	0.000	0.000	0.000	0.000
70	A	71	GLY	0	0.071	0.042	23.375	0.022	0.022	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.050	-0.003	24.635	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.880	0.925	27.148	0.557	0.557	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.020	-0.006	30.740	-0.018	-0.018	0.000	0.000	0.000	0.000
74	A	75	GLN	0	0.036	0.007	31.272	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.003	-0.013	35.386	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.876	0.943	37.844	0.359	0.359	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.740	-0.857	41.918	-0.271	-0.271	0.000	0.000	0.000	0.000
78	A	79	GLN	0	-0.054	-0.019	42.574	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	80	GLN	0	-0.070	-0.044	42.111	0.004	0.004	0.000	0.000	0.000	0.000
80	A	81	CYS	0	-0.019	-0.001	38.613	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.910	0.957	42.120	0.158	0.158	0.000	0.000	0.000	0.000
82	A	83	SER	0	0.021	-0.010	45.320	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.857	-0.895	47.930	-0.168	-0.168	0.000	0.000	0.000	0.000
84	A	85	TRP	0	-0.019	-0.017	49.580	0.001	0.001	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.056	-0.033	52.298	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.898	-0.960	53.382	-0.099	-0.099	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.018	-0.013	54.068	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.009	0.030	54.843	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.039	0.011	52.677	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.028	-0.007	49.197	0.005	0.005	0.000	0.000	0.000	0.000
91	A	92	ASN	0	-0.053	-0.029	51.123	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	TYR	0	-0.037	-0.032	53.008	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.753	-0.858	46.559	-0.198	-0.198	0.000	0.000	0.000	0.000
94	A	95	ASN	0	0.019	0.001	50.392	0.003	0.003	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.022	0.003	44.485	0.008	0.008	0.000	0.000	0.000	0.000
96	A	97	TYR	0	0.046	0.014	46.526	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	98	LYS	1	1.015	0.998	42.773	0.218	0.218	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.018	-0.010	42.120	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.027	-0.015	41.767	0.008	0.008	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.039	-0.016	41.455	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.901	0.943	37.114	0.128	0.128	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.848	0.911	35.820	0.278	0.278	0.000	0.000	0.000	0.000
103	A	104	CYS	0	0.016	0.026	31.342	-0.028	-0.028	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.036	0.008	28.607	0.045	0.045	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.004	0.012	27.646	-0.033	-0.033	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.036	0.039	22.706	0.030	0.030	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.931	0.967	27.420	0.044	0.044	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.948	0.986	28.652	-0.028	-0.028	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.011	-0.012	31.333	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.040	-0.026	29.525	0.005	0.005	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.854	-0.935	26.030	0.272	0.272	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.075	-0.033	24.364	0.008	0.008	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.904	0.944	20.873	-0.331	-0.331	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.024	-0.002	24.616	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	116	TRP	0	0.013	-0.001	22.906	-0.014	-0.014	0.000	0.000	0.000	0.000
116	A	117	PHE	0	-0.017	-0.016	28.474	0.014	0.014	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.015	-0.001	31.579	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.025	-0.028	33.104	0.031	0.031	0.000	0.000	0.000	0.000
119	A	120	TYR	0	0.003	0.014	35.430	-0.023	-0.023	0.000	0.000	0.000	0.000
120	A	122	GLY	0	0.045	0.015	34.657	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	123	ARG	1	0.818	0.905	35.209	0.168	0.168	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.881	-0.934	33.976	-0.218	-0.218	0.000	0.000	0.000	0.000
123	A	125	ASN	0	-0.089	-0.060	30.644	0.061	0.061	0.000	0.000	0.000	0.000
124	A	126	PRO	0	0.049	0.037	27.095	-0.026	-0.026	0.000	0.000	0.000	0.000
125	A	127	PHE	0	-0.026	-0.008	23.834	0.008	0.008	0.000	0.000	0.000	0.000
126	A	128	VAL	0	0.021	0.013	18.709	0.016	0.016	0.000	0.000	0.000	0.000
127	A	130	LYS	1	0.820	0.898	14.589	1.523	1.523	0.000	0.000	0.000	0.000
128	A	131	TYR	0	0.057	0.033	12.040	0.183	0.183	0.000	0.000	0.000	0.000
129	A	132	THR	0	-0.009	-0.010	11.977	-0.134	-0.134	0.000	0.000	0.000	0.000
130	A	133	PRO	0	-0.017	-0.003	8.386	0.555	0.555	0.000	0.000	0.000	0.000
131	A	134	GLU	-1	-0.951	-0.966	10.615	-2.989	-2.989	0.000	0.000	0.000	0.000
132	A	135	CYS	-1	-0.985	-0.988	6.745	-8.385	-8.385	0.000	0.000	0.000	0.000

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