FMO DATABASE

FMODB ID: GVRZ1

Calculation Name: 2KL4-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KL4

Chain ID: A

ChEMBL ID:

UniProt ID: Q9KB96

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-999273.887238
FMO2-HF: Nuclear repulsion	951845.325915
FMO2-HF: Total energy	-47428.561322
FMO2-MP2: Total energy	-47566.973944

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.
-215.568	-208.66	3.421	-5.76	-4.568	-0.06

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 : 0.869 / q_NPA : 0.927

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	HIS	0	0.029	-0.004	3.404	-0.164	0.821	0.006	-0.539	-0.452	-0.001
38	A	38	GLU	-1	-0.866	-0.934	2.407	-128.587	-122.763	3.416	-5.208	-4.032	-0.059
39	A	39	PRO	0	-0.042	-0.023	4.050	8.751	8.850	-0.001	-0.013	-0.084	0.000
4	A	4	MET	0	0.019	0.017	5.655	6.952	6.952	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.894	-0.933	7.730	-32.606	-32.606	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.018	0.017	7.710	2.777	2.777	0.000	0.000	0.000	0.000
7	A	7	PHE	0	0.005	-0.002	8.225	2.778	2.778	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.007	0.005	12.238	2.296	2.296	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.939	-0.959	13.930	-18.518	-18.518	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.075	0.014	14.012	1.792	1.792	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.007	-0.003	14.595	1.211	1.211	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.817	0.909	16.937	19.115	19.115	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.021	0.021	20.574	0.732	0.732	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.063	-0.021	19.824	0.585	0.585	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.915	-0.956	23.501	-11.258	-11.258	0.000	0.000	0.000	0.000
16	A	16	HIS	0	-0.062	-0.035	26.067	0.509	0.509	0.000	0.000	0.000	0.000
17	A	17	PRO	0	0.068	0.034	25.179	-0.318	-0.318	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.890	-0.951	25.290	-11.205	-11.205	0.000	0.000	0.000	0.000
19	A	19	HIS	1	0.807	0.889	25.597	11.438	11.438	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.882	0.950	19.275	15.056	15.056	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.788	-0.885	19.863	-15.391	-15.391	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.948	0.977	19.104	12.046	12.046	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.024	-0.029	16.749	-0.203	-0.203	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.962	-0.982	14.523	-20.451	-20.451	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.877	-0.909	13.803	-17.568	-17.568	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.000	0.008	14.236	-1.273	-1.273	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.048	-0.020	11.047	-1.201	-1.201	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.013	-0.019	9.527	-2.829	-2.829	0.000	0.000	0.000	0.000
29	A	29	TRP	0	0.045	0.012	9.862	-2.182	-2.182	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.022	-0.008	9.450	0.037	0.037	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.017	-0.008	5.561	-1.067	-1.067	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.042	-0.011	6.427	-4.100	-4.100	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.062	-0.034	9.091	1.454	1.454	0.000	0.000	0.000	0.000
34	A	34	PHE	0	-0.019	-0.009	9.971	1.602	1.602	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.012	0.008	6.005	-1.433	-1.433	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.014	-0.011	5.778	-6.672	-6.672	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.055	-0.014	7.682	2.086	2.086	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.006	-0.019	6.988	2.752	2.752	0.000	0.000	0.000	0.000
41	A	41	MET	0	0.017	0.028	10.314	1.680	1.680	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.974	0.982	13.186	18.919	18.919	0.000	0.000	0.000	0.000
43	A	43	TRP	0	-0.015	-0.008	16.301	0.481	0.481	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.031	-0.009	18.365	0.591	0.591	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.048	-0.021	17.683	0.411	0.411	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.013	-0.002	13.667	-0.956	-0.956	0.000	0.000	0.000	0.000
47	A	47	MET	0	-0.012	0.006	12.320	1.893	1.893	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.014	-0.011	7.681	-2.282	-2.282	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.023	-0.003	9.103	3.266	3.266	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.056	0.038	9.129	-5.094	-5.094	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.015	0.005	9.736	4.004	4.004	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.009	0.012	11.185	1.827	1.827	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.050	-0.029	12.963	1.398	1.398	0.000	0.000	0.000	0.000
54	A	54	PHE	0	-0.041	-0.045	13.767	-1.578	-1.578	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.044	0.025	14.605	0.517	0.517	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.010	0.005	12.432	0.245	0.245	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.005	0.015	14.490	-1.242	-1.242	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.017	0.004	13.943	1.012	1.012	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.014	-0.026	18.214	-0.090	-0.090	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.024	0.027	20.180	0.326	0.326	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.005	-0.005	22.529	0.134	0.134	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.926	0.949	26.260	11.217	11.217	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.022	-0.025	29.297	0.186	0.186	0.000	0.000	0.000	0.000
64	A	64	HIS	0	0.051	0.029	27.208	0.055	0.055	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.010	0.025	19.396	-0.146	-0.146	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.023	-0.002	22.902	0.469	0.469	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.022	-0.006	18.435	-0.826	-0.826	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.016	-0.003	19.526	0.981	0.981	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.014	0.023	17.658	-0.883	-0.883	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.795	-0.890	18.720	-16.286	-16.286	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.922	-0.967	21.092	-11.687	-11.687	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.051	0.031	23.040	0.424	0.424	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.035	-0.013	23.170	0.341	0.341	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.086	-0.042	23.673	0.313	0.313	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.058	-0.020	26.866	0.583	0.583	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.004	-0.005	26.948	0.619	0.619	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.014	0.004	24.456	0.216	0.216	0.000	0.000	0.000	0.000
78	A	78	ALA	0	0.022	0.011	27.760	0.048	0.048	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.882	-0.936	29.419	-9.036	-9.036	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.030	0.019	29.050	0.212	0.212	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.030	-0.020	25.234	-0.019	-0.019	0.000	0.000	0.000	0.000
82	A	82	ALA	0	-0.008	0.002	29.443	0.119	0.119	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.101	-0.058	33.090	0.378	0.378	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.048	-0.012	29.875	0.131	0.131	0.000	0.000	0.000	0.000
85	A	85	GLY	0	-0.001	0.014	31.833	-0.039	-0.039	0.000	0.000	0.000	0.000
86	A	86	TYR	0	-0.098	-0.074	27.992	-0.085	-0.085	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.007	-0.016	30.766	0.203	0.203	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.015	0.000	28.615	-0.462	-0.462	0.000	0.000	0.000	0.000
89	A	89	THR	0	-0.073	-0.027	28.080	0.392	0.392	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.990	0.967	29.978	9.263	9.263	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.031	0.026	26.760	-0.073	-0.073	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.007	0.006	23.394	-0.535	-0.535	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.064	0.023	21.087	0.796	0.796	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.918	0.953	24.675	9.994	9.994	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.036	0.036	23.723	0.384	0.384	0.000	0.000	0.000	0.000
96	A	96	PRO	0	-0.047	-0.028	26.651	-0.268	-0.268	0.000	0.000	0.000	0.000
97	A	97	TRP	0	0.022	-0.011	21.988	0.002	0.002	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.065	-0.026	27.773	-0.200	-0.200	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.809	-0.885	28.835	-10.131	-10.131	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.026	0.003	25.485	-0.484	-0.484	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.020	0.005	20.118	0.205	0.205	0.000	0.000	0.000	0.000
102	A	102	HIS	0	0.041	0.026	22.903	-0.643	-0.643	0.000	0.000	0.000	0.000
103	A	103	TYR	0	0.003	-0.030	17.054	-0.426	-0.426	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.935	-0.962	19.701	-13.114	-13.114	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.007	-0.013	22.089	-0.180	-0.180	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.035	-0.022	17.235	-0.095	-0.095	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.939	0.981	17.363	16.411	16.411	0.000	0.000	0.000	0.000
108	A	108	GLN	0	-0.009	0.008	18.367	-0.498	-0.498	0.000	0.000	0.000	0.000
109	A	109	MET	0	-0.032	0.018	20.262	0.032	0.032	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.015	0.005	13.732	0.049	0.049	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.856	-0.955	15.602	-18.929	-18.929	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.033	0.000	17.446	0.123	0.123	0.000	0.000	0.000	0.000
113	A	113	ASN	0	-0.016	-0.037	18.579	0.329	0.329	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.018	-0.017	12.849	-0.363	-0.363	0.000	0.000	0.000	0.000
115	A	115	GLN	0	-0.051	-0.022	17.081	0.698	0.698	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.971	-0.977	19.650	-12.471	-12.471	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.751	0.867	18.787	15.889	15.889	0.000	0.000	0.000	0.000
118	A	118	GLU	-2	-1.915	-1.935	18.791	-31.156	-31.156	0.000	0.000	0.000	0.000

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