FMO DATABASE

FMODB ID: Z71LN

Calculation Name: 1KLP-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1KLP

Chain ID: A

ChEMBL ID:

UniProt ID: P9WQF3

Base Structure: SolutionNMR

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-836290.026904
FMO2-HF: Nuclear repulsion	792392.398724
FMO2-HF: Total energy	-43897.62818
FMO2-MP2: Total energy	-44026.038286

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:MET)

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

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.
-348.933	-346.224	0.056	-1.448	-1.316	-0.01

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.768 / q_NPA : 0.867

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	VAL	0	0.067	0.051	3.114	-18.328	-15.771	0.057	-1.438	-1.175	-0.010
4	A	4	THR	0	0.033	0.014	4.603	8.710	8.862	-0.001	-0.010	-0.141	0.000
5	A	5	GLN	0	0.071	0.025	6.306	2.658	2.658	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.948	-0.991	8.446	-28.277	-28.277	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.988	-0.981	5.061	-47.467	-47.467	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.003	-0.002	8.196	2.876	2.876	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.021	0.005	11.320	2.194	2.194	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.003	-0.009	11.304	1.448	1.448	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.043	0.024	10.868	1.270	1.270	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.014	-0.008	11.792	1.428	1.428	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.007	0.006	14.545	1.351	1.351	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.971	-0.986	13.982	-20.449	-20.449	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.032	-0.008	14.377	0.991	0.991	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.006	-0.012	17.996	0.978	0.978	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.962	-0.947	20.073	-13.218	-13.218	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.933	-0.972	19.420	-15.356	-15.356	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.082	-0.028	21.720	0.747	0.747	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.055	-0.063	23.665	0.640	0.640	0.000	0.000	0.000	0.000
21	A	21	GLY	0	-0.035	-0.002	24.813	0.552	0.552	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.064	-0.025	23.712	0.252	0.252	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.906	-0.959	22.829	-12.947	-12.947	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.015	0.002	18.029	-0.326	-0.326	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.029	-0.049	18.593	-0.868	-0.868	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.875	-0.929	19.984	-12.354	-12.354	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.021	0.022	17.068	0.342	0.342	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.015	-0.031	18.124	-1.058	-1.058	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.020	-0.035	16.224	0.091	0.091	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.901	-0.928	18.140	-13.299	-13.299	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.816	0.939	20.938	14.022	14.022	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.018	-0.027	22.117	-0.500	-0.500	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.054	0.026	21.145	0.592	0.592	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.001	-0.012	24.323	0.102	0.102	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.956	-0.994	27.949	-10.392	-10.392	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.883	-0.952	25.306	-12.444	-12.444	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.002	-0.003	22.110	0.046	0.046	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.944	-0.954	26.346	-9.681	-9.681	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.075	-0.040	25.954	0.352	0.352	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.857	-0.938	29.268	-10.242	-10.242	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.046	-0.038	27.113	-0.422	-0.422	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.049	-0.030	27.074	-0.298	-0.298	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.015	0.016	25.601	-0.225	-0.225	0.000	0.000	0.000	0.000
44	A	44	MET	0	0.006	0.008	20.301	-0.587	-0.587	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.007	0.017	22.327	-0.685	-0.685	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.899	-0.957	22.810	-12.567	-12.567	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.013	-0.007	18.345	-0.709	-0.709	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.005	0.025	18.150	-1.231	-1.231	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.011	-0.007	18.225	-0.882	-0.882	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.010	-0.008	17.733	-0.075	-0.075	0.000	0.000	0.000	0.000
51	A	51	THR	0	0.006	-0.007	12.867	-1.643	-1.643	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.907	-0.990	13.863	-19.373	-19.373	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-1.018	-0.993	16.063	-16.986	-16.986	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.812	0.899	13.113	18.451	18.451	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.043	-0.015	5.882	-5.318	-5.318	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.000	0.017	10.885	-0.968	-0.968	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.082	-0.038	10.983	-0.538	-0.538	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.842	0.916	11.977	24.946	24.946	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.055	0.030	15.707	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	60	PRO	0	0.001	0.016	19.056	0.535	0.535	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.870	-0.952	22.652	-11.997	-11.997	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-1.069	-1.030	25.687	-11.474	-11.474	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.864	-0.936	20.483	-15.255	-15.255	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.028	-0.025	21.364	0.027	0.027	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.031	-0.018	23.619	0.236	0.236	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.063	-0.025	25.423	0.419	0.419	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.045	-0.004	19.262	-0.082	-0.082	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.886	0.959	22.934	11.985	11.985	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.027	-0.026	21.525	0.154	0.154	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.052	0.040	15.938	-0.505	-0.505	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.005	-0.001	16.667	-1.050	-1.050	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.821	-0.920	16.933	-15.836	-15.836	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.026	-0.002	15.842	-0.540	-0.540	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.041	-0.017	11.640	-1.138	-1.138	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.041	-0.026	13.422	-1.403	-1.403	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.011	0.009	15.183	-0.568	-0.568	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.005	0.014	11.119	-0.367	-0.367	0.000	0.000	0.000	0.000
78	A	78	GLN	0	-0.048	-0.059	8.846	2.192	2.192	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.747	0.877	11.667	21.412	21.412	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.001	0.009	14.917	1.038	1.038	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.962	-0.959	9.378	-27.693	-27.693	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.978	-0.998	10.269	-21.450	-21.450	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.905	-0.939	6.872	-44.326	-44.326	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.034	-0.036	10.374	1.867	1.867	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.008	0.012	13.309	0.700	0.700	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.958	-0.984	16.743	-14.880	-14.880	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.010	-0.012	18.198	0.816	0.816	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.068	0.027	15.963	-0.700	-0.700	0.000	0.000	0.000	0.000
89	A	89	GLN	0	0.013	0.019	9.234	0.435	0.435	0.000	0.000	0.000	0.000
90	A	90	ALA	0	0.028	0.001	14.954	0.116	0.116	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.054	0.010	18.608	0.940	0.940	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.941	0.955	20.165	14.323	14.323	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.031	-0.011	23.715	0.575	0.575	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.913	0.949	26.241	10.611	10.611	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.040	0.021	22.059	-0.067	-0.067	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.908	-0.955	24.936	-10.443	-10.443	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.091	-0.041	27.487	0.210	0.210	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.861	-0.932	21.446	-15.030	-15.030	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.039	-0.034	25.086	0.331	0.331	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.028	0.005	21.647	0.011	0.011	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.842	-0.922	23.174	-11.668	-11.668	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.087	-0.062	25.497	-0.139	-0.139	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.029	0.028	27.347	0.302	0.302	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.020	-0.010	30.750	0.109	0.109	0.000	0.000	0.000	0.000
105	A	105	ASN	0	-0.038	-0.028	33.153	0.410	0.410	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.044	-0.013	36.302	-0.020	-0.020	0.000	0.000	0.000	0.000
107	A	107	GLN	0	0.076	0.038	33.286	0.007	0.007	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.040	-0.035	38.245	0.225	0.225	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.889	0.941	39.894	7.705	7.705	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.058	0.044	35.701	-0.015	-0.015	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.972	-0.985	39.608	-7.136	-7.136	0.000	0.000	0.000	0.000
112	A	112	ALA	0	0.001	-0.007	39.612	-0.218	-0.218	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.947	-0.956	38.897	-8.035	-8.035	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.063	-0.046	41.897	0.160	0.160	0.000	0.000	0.000	0.000
115	A	115	LYS	0	0.023	0.026	43.641	-0.046	-0.046	0.000	0.000	0.000	0.000

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