FMO DATABASE

FMODB ID: 19YMZ

Calculation Name: 2KWL-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KWL

Chain ID: A

ChEMBL ID:

UniProt ID: O51647

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	84
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-550476.965124
FMO2-HF: Nuclear repulsion	516832.684695
FMO2-HF: Total energy	-33644.280429
FMO2-MP2: Total energy	-33743.275853

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.
-189.6	-188.833	0.003	-0.408	-0.361	-0.001

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 : 0.819 / q_NPA : 0.896

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

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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	GLY	0	0.023	0.028	3.852	-6.479	-5.712	0.003	-0.408	-0.361	-0.001
4	A	4	SER	0	-0.026	-0.030	6.624	-3.182	-3.182	0.000	0.000	0.000	0.000
5	A	5	MET	0	-0.017	0.000	8.474	0.744	0.744	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.838	-0.905	11.992	-19.708	-19.708	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.013	-0.004	13.511	-0.518	-0.518	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.940	-0.980	10.006	-31.120	-31.120	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.845	-0.919	13.049	-22.626	-22.626	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.050	-0.022	14.740	1.254	1.254	0.000	0.000	0.000	0.000
11	A	11	PHE	0	0.031	-0.007	13.138	0.812	0.812	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.000	0.007	14.222	0.902	0.902	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.978	0.977	16.373	15.906	15.906	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.036	-0.026	18.853	0.887	0.887	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.872	0.937	19.143	15.328	15.328	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.003	0.006	18.693	0.744	0.744	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.040	-0.003	20.580	0.513	0.513	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.029	0.018	23.824	0.394	0.394	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.049	-0.035	21.601	0.282	0.282	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.909	-0.931	23.687	-11.016	-11.016	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.099	-0.073	26.256	0.250	0.250	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.041	-0.022	25.415	0.281	0.281	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.960	-0.964	24.394	-12.582	-12.582	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.856	0.942	22.714	12.082	12.082	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.925	0.955	17.049	16.153	16.153	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.834	-0.923	14.909	-19.554	-19.554	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.956	-0.983	13.540	-22.696	-22.696	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.962	-0.970	15.958	-14.613	-14.613	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.053	-0.021	17.307	1.027	1.027	0.000	0.000	0.000	0.000
30	A	30	THR	0	-0.001	-0.011	19.416	-0.178	-0.178	0.000	0.000	0.000	0.000
31	A	31	THR	0	0.038	0.010	22.201	0.382	0.382	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.955	-0.992	25.551	-10.981	-10.981	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.030	0.003	23.663	0.365	0.365	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.956	0.956	26.657	10.355	10.355	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.048	-0.006	27.728	-0.237	-0.237	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.015	0.000	29.758	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.933	-0.933	27.340	-10.688	-10.688	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.888	-0.938	23.318	-13.901	-13.901	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.008	-0.006	26.057	-0.161	-0.161	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.019	-0.012	28.696	0.160	0.160	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.010	0.004	31.828	0.359	0.359	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.824	-0.922	33.233	-8.944	-8.944	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.079	-0.051	34.429	0.023	0.023	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.048	-0.022	35.389	0.040	0.040	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.856	-0.925	36.369	-8.337	-8.337	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.062	-0.038	31.121	-0.138	-0.138	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.007	0.011	34.035	-0.115	-0.115	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.905	-0.968	36.239	-7.958	-7.958	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.063	-0.009	30.057	-0.113	-0.113	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.018	-0.025	31.310	-0.250	-0.250	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.029	0.009	32.502	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.011	-0.027	35.738	0.046	0.046	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.051	-0.019	27.702	-0.191	-0.191	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.798	-0.897	31.711	-9.240	-9.240	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.956	-0.981	32.970	-8.212	-8.212	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.073	-0.029	31.967	0.117	0.117	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.120	-0.070	27.380	-0.462	-0.462	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.955	-0.953	31.515	-9.234	-9.234	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.874	-0.930	29.863	-10.628	-10.628	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.889	0.939	33.496	8.589	8.589	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.067	0.034	30.196	-0.172	-0.172	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.072	-0.049	33.003	-0.088	-0.088	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-1.011	-1.016	34.722	-8.370	-8.370	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.036	-0.018	29.814	0.008	0.008	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.737	-0.874	28.183	-10.856	-10.856	0.000	0.000	0.000	0.000
66	A	66	ALA	0	-0.047	-0.009	29.309	-0.245	-0.245	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.085	-0.038	27.243	0.001	0.001	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-1.023	-1.011	24.833	-12.206	-12.206	0.000	0.000	0.000	0.000
69	A	69	PHE	0	-0.014	-0.018	26.354	-0.439	-0.439	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.970	-0.955	27.053	-9.903	-9.903	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.101	-0.052	25.214	0.151	0.151	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.038	0.011	23.945	-0.142	-0.142	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.021	0.002	20.932	-0.483	-0.483	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.746	-0.858	20.837	-13.262	-13.262	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.004	0.003	22.982	-0.256	-0.256	0.000	0.000	0.000	0.000
76	A	76	VAL	0	-0.018	-0.006	18.179	-0.284	-0.284	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.022	-0.029	18.015	-0.129	-0.129	0.000	0.000	0.000	0.000
78	A	78	PHE	0	-0.015	-0.011	19.327	-0.356	-0.356	0.000	0.000	0.000	0.000
79	A	79	ILE	0	0.015	0.010	22.172	0.014	0.014	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.777	0.888	13.350	21.453	21.453	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.871	0.945	18.541	13.230	13.230	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.787	0.879	19.934	11.904	11.904	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.874	0.964	21.794	14.024	14.024	0.000	0.000	0.000	0.000
84	A	84	GLY	-1	-0.873	-0.943	18.237	-17.125	-17.125	0.000	0.000	0.000	0.000

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