FMO DATABASE

FMODB ID: 8Q7RY

Calculation Name: 2KVI-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KVI

Chain ID: A

ChEMBL ID:

UniProt ID: P38996

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	77
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-496693.879547
FMO2-HF: Nuclear repulsion	465725.973092
FMO2-HF: Total energy	-30967.906455
FMO2-MP2: Total energy	-31057.831857

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:PRO)

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

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.
-96.287	-93.184	18.574	-11.843	-9.833	-0.118

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.770 / q_NPA : 0.860

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	0.037	0.024	3.882	3.441	5.088	-0.013	-0.726	-0.908	-0.001
31	A	31	MET	0	-0.035	-0.020	3.521	-4.047	-3.828	0.003	-0.070	-0.153	0.000
45	A	45	ASP	-1	-0.786	-0.877	1.720	-139.419	-139.680	18.498	-10.563	-7.673	-0.115
46	A	46	ASN	0	0.009	-0.010	2.716	16.139	17.419	0.087	-0.441	-0.925	-0.002
47	A	47	PRO	0	0.016	0.000	4.082	4.574	4.762	0.000	-0.038	-0.150	0.000
76	A	76	ALA	0	-0.027	-0.022	4.764	-2.348	-2.318	-0.001	-0.005	-0.024	0.000
4	A	4	ARG	1	0.884	0.930	5.818	23.776	23.776	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.069	0.062	9.629	0.877	0.877	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.029	-0.018	12.234	0.627	0.627	0.000	0.000	0.000	0.000
7	A	7	ILE	0	0.065	0.021	16.018	0.207	0.207	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.002	-0.011	19.189	0.190	0.190	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.037	-0.037	22.929	0.161	0.161	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.065	0.043	21.342	0.298	0.298	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.058	-0.022	21.415	0.232	0.232	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.015	0.002	23.642	0.087	0.087	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.927	0.978	26.885	11.101	11.101	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.024	-0.023	25.892	-0.363	-0.363	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.051	0.035	20.627	-0.086	-0.086	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.015	-0.015	21.356	0.229	0.229	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.967	0.962	15.270	19.016	19.016	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.847	-0.913	16.646	-15.650	-15.650	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.852	-0.911	18.560	-14.243	-14.243	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.044	0.012	14.759	-0.162	-0.162	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.003	0.010	11.765	-0.910	-0.910	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.834	0.908	15.060	13.496	13.496	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.026	0.006	17.757	0.229	0.229	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.051	0.003	13.324	-0.078	-0.078	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.036	-0.025	12.830	-1.116	-1.116	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.066	-0.026	13.316	-1.043	-1.043	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.045	-0.026	14.449	0.055	0.055	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.012	-0.031	10.340	-1.027	-1.027	0.000	0.000	0.000	0.000
29	A	29	HIS	0	-0.004	-0.018	5.985	-2.125	-2.125	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.025	0.004	7.550	-0.752	-0.752	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.086	-0.032	8.162	1.298	1.298	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.026	0.008	11.614	-0.184	-0.184	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.038	-0.023	14.840	1.177	1.177	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.041	0.029	17.684	-0.078	-0.078	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.955	0.973	20.611	13.779	13.779	0.000	0.000	0.000	0.000
37	A	37	ASN	0	0.017	0.015	23.855	0.119	0.119	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.039	0.021	25.858	-0.209	-0.209	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.016	-0.022	21.555	0.056	0.056	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.015	0.004	19.549	0.218	0.218	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.056	-0.017	15.480	-0.202	-0.202	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.025	0.008	11.484	0.407	0.407	0.000	0.000	0.000	0.000
43	A	43	GLN	0	0.006	0.005	8.679	-0.407	-0.407	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.050	0.010	6.820	0.993	0.993	0.000	0.000	0.000	0.000
48	A	48	GLN	0	-0.011	-0.001	6.810	4.243	4.243	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.058	0.044	7.237	3.051	3.051	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.051	-0.017	7.611	1.690	1.690	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.852	0.907	10.125	23.498	23.498	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.783	-0.877	12.380	-21.146	-21.146	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.020	-0.006	12.900	1.230	1.230	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.043	-0.030	14.380	1.403	1.403	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.907	-0.969	16.374	-16.496	-16.496	0.000	0.000	0.000	0.000
56	A	56	CYS	0	-0.059	-0.017	17.787	1.162	1.162	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.893	-0.923	18.587	-14.237	-14.237	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.096	-0.045	19.951	0.880	0.880	0.000	0.000	0.000	0.000
59	A	59	GLN	0	-0.050	-0.043	20.740	0.837	0.837	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.896	-0.931	20.258	-14.501	-14.501	0.000	0.000	0.000	0.000
61	A	61	MET	0	-0.020	-0.010	21.525	0.302	0.302	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.020	0.006	22.322	-0.029	-0.029	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.054	-0.004	23.976	0.564	0.564	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.045	0.017	27.609	-0.099	-0.099	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.905	0.933	28.794	9.329	9.329	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.907	0.986	28.845	10.230	10.230	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.026	0.022	23.760	0.073	0.073	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.038	-0.010	21.306	0.133	0.133	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.032	0.021	17.477	-0.237	-0.237	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.882	-0.922	15.103	-17.199	-17.199	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.046	0.028	10.666	-1.149	-1.149	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.015	-0.025	11.130	0.779	0.779	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.006	-0.003	7.153	-4.066	-4.066	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.063	-0.038	6.297	1.994	1.994	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.047	0.027	6.341	-3.187	-3.187	0.000	0.000	0.000	0.000
77	A	77	ARG	0	0.101	0.057	5.949	6.328	6.328	0.000	0.000	0.000	0.000

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