FMO DATABASE

FMODB ID: 3M25L

Calculation Name: 6LMJ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6LMJ

Chain ID: A

ChEMBL ID:

UniProt ID: P68742

Base Structure: X-ray

Registration Date: 2025-10-06

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-582301.572729
FMO2-HF: Nuclear repulsion	544569.076917
FMO2-HF: Total energy	-37732.495812
FMO2-MP2: Total energy	-37845.135958

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:12:LYS)

Summations of interaction energy for fragment #1(A:12:LYS)

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.
131.367	132.895	0.041	-0.742	-0.827	-0.003

Interaction energy analysis for fragmet #1(A:12:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.825 / q_NPA : 1.902

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	14	THR	0	-0.006	-0.012	3.427	-5.831	-4.303	0.041	-0.742	-0.827	-0.003
4	A	15	ILE	0	0.014	0.026	6.253	3.911	3.911	0.000	0.000	0.000	0.000
5	A	16	THR	0	-0.028	-0.045	9.133	4.479	4.479	0.000	0.000	0.000	0.000
6	A	17	LYS	1	0.969	0.963	12.335	32.056	32.056	0.000	0.000	0.000	0.000
7	A	18	GLN	0	0.039	0.032	15.523	1.424	1.424	0.000	0.000	0.000	0.000
8	A	19	GLU	-1	-0.792	-0.862	10.344	-49.343	-49.343	0.000	0.000	0.000	0.000
9	A	20	LEU	0	0.027	0.013	13.692	0.678	0.678	0.000	0.000	0.000	0.000
10	A	21	TYR	0	-0.019	-0.017	14.694	0.976	0.976	0.000	0.000	0.000	0.000
11	A	22	SER	0	-0.013	-0.009	16.243	1.932	1.932	0.000	0.000	0.000	0.000
12	A	23	LEU	0	0.015	0.014	11.330	0.662	0.662	0.000	0.000	0.000	0.000
13	A	24	VAL	0	0.029	0.012	16.041	0.998	0.998	0.000	0.000	0.000	0.000
14	A	25	ALA	0	-0.042	0.001	18.934	1.251	1.251	0.000	0.000	0.000	0.000
15	A	26	ALA	0	-0.009	-0.005	18.336	1.040	1.040	0.000	0.000	0.000	0.000
16	A	27	ASP	-1	-0.948	-0.964	18.386	-28.597	-28.597	0.000	0.000	0.000	0.000
17	A	28	THR	0	-0.031	-0.052	20.405	1.414	1.414	0.000	0.000	0.000	0.000
18	A	29	GLN	0	-0.013	0.008	23.273	1.173	1.173	0.000	0.000	0.000	0.000
19	A	30	LEU	0	-0.020	0.006	24.522	1.285	1.285	0.000	0.000	0.000	0.000
20	A	31	ASN	0	0.030	-0.002	24.705	-1.480	-1.480	0.000	0.000	0.000	0.000
21	A	32	LYS	1	0.951	0.964	19.189	29.441	29.441	0.000	0.000	0.000	0.000
22	A	33	ALA	0	-0.004	0.001	23.775	-0.101	-0.101	0.000	0.000	0.000	0.000
23	A	34	LEU	0	-0.042	-0.021	26.812	0.545	0.545	0.000	0.000	0.000	0.000
24	A	35	ILE	0	0.039	0.026	21.003	0.238	0.238	0.000	0.000	0.000	0.000
25	A	36	GLU	-1	-0.817	-0.926	22.299	-26.409	-26.409	0.000	0.000	0.000	0.000
26	A	37	ARG	1	0.928	0.985	24.525	19.224	19.224	0.000	0.000	0.000	0.000
27	A	38	ILE	0	0.026	0.013	26.246	0.589	0.589	0.000	0.000	0.000	0.000
28	A	39	PHE	0	0.024	0.005	20.486	0.292	0.292	0.000	0.000	0.000	0.000
29	A	40	THR	0	-0.020	-0.020	24.778	0.088	0.088	0.000	0.000	0.000	0.000
30	A	41	SER	0	-0.052	-0.023	27.168	0.725	0.725	0.000	0.000	0.000	0.000
31	A	42	GLN	0	0.051	0.018	22.844	0.572	0.572	0.000	0.000	0.000	0.000
32	A	43	GLN	0	-0.012	-0.005	24.290	-0.267	-0.267	0.000	0.000	0.000	0.000
33	A	44	LYS	1	0.930	0.966	27.192	18.329	18.329	0.000	0.000	0.000	0.000
34	A	45	ILE	0	0.014	0.004	30.782	0.519	0.519	0.000	0.000	0.000	0.000
35	A	46	ILE	0	0.027	0.017	25.356	0.437	0.437	0.000	0.000	0.000	0.000
36	A	47	GLN	0	0.013	0.012	29.419	0.981	0.981	0.000	0.000	0.000	0.000
37	A	48	ASN	0	-0.007	-0.012	31.038	0.663	0.663	0.000	0.000	0.000	0.000
38	A	49	ALA	0	0.069	0.043	32.474	0.442	0.442	0.000	0.000	0.000	0.000
39	A	50	LEU	0	0.002	0.000	28.333	0.284	0.284	0.000	0.000	0.000	0.000
40	A	51	LYS	1	0.879	0.929	33.027	18.103	18.103	0.000	0.000	0.000	0.000
41	A	52	HIS	1	0.832	0.921	35.739	16.315	16.315	0.000	0.000	0.000	0.000
42	A	53	ASN	0	-0.033	-0.009	36.166	0.164	0.164	0.000	0.000	0.000	0.000
43	A	54	GLN	0	0.029	0.027	35.480	0.325	0.325	0.000	0.000	0.000	0.000
44	A	55	GLU	-1	-0.845	-0.919	31.856	-18.854	-18.854	0.000	0.000	0.000	0.000
45	A	56	VAL	0	0.004	0.001	28.492	0.352	0.352	0.000	0.000	0.000	0.000
46	A	57	ILE	0	-0.004	-0.011	26.590	-0.588	-0.588	0.000	0.000	0.000	0.000
47	A	58	ILE	0	-0.008	0.013	22.114	0.525	0.525	0.000	0.000	0.000	0.000
48	A	59	PRO	0	0.067	0.040	22.650	-0.446	-0.446	0.000	0.000	0.000	0.000
49	A	60	PRO	0	0.009	-0.006	17.811	-0.227	-0.227	0.000	0.000	0.000	0.000
50	A	61	GLY	0	0.048	0.017	21.127	0.355	0.355	0.000	0.000	0.000	0.000
51	A	62	ILE	0	-0.025	-0.011	18.516	-0.090	-0.090	0.000	0.000	0.000	0.000
52	A	63	LYS	1	0.849	0.920	22.997	19.772	19.772	0.000	0.000	0.000	0.000
53	A	64	PHE	0	-0.003	-0.012	22.376	-0.683	-0.683	0.000	0.000	0.000	0.000
54	A	65	THR	0	-0.002	-0.009	27.155	0.845	0.845	0.000	0.000	0.000	0.000
55	A	66	VAL	0	0.009	0.000	29.229	-0.579	-0.579	0.000	0.000	0.000	0.000
56	A	67	VAL	0	0.009	0.009	29.857	0.446	0.446	0.000	0.000	0.000	0.000
57	A	68	THR	0	0.020	-0.002	32.743	0.056	0.056	0.000	0.000	0.000	0.000
58	A	69	VAL	0	-0.057	-0.020	29.995	-0.213	-0.213	0.000	0.000	0.000	0.000
59	A	70	LYS	1	1.041	1.008	32.874	16.445	16.445	0.000	0.000	0.000	0.000
60	A	71	ALA	0	0.013	0.010	33.925	-0.485	-0.485	0.000	0.000	0.000	0.000
61	A	72	LYS	1	0.906	0.950	29.508	19.532	19.532	0.000	0.000	0.000	0.000
62	A	73	PRO	0	0.052	0.031	34.614	-0.067	-0.067	0.000	0.000	0.000	0.000
63	A	74	ALA	0	0.003	-0.001	34.138	-0.541	-0.541	0.000	0.000	0.000	0.000
64	A	75	ARG	1	0.932	0.959	28.090	19.898	19.898	0.000	0.000	0.000	0.000
65	A	76	GLN	0	0.053	0.032	33.174	-0.409	-0.409	0.000	0.000	0.000	0.000
66	A	77	GLY	0	-0.014	-0.002	29.894	-0.105	-0.105	0.000	0.000	0.000	0.000
67	A	78	HIS	0	0.003	-0.004	29.337	0.216	0.216	0.000	0.000	0.000	0.000
68	A	79	ASN	0	0.009	0.012	24.698	-1.212	-1.212	0.000	0.000	0.000	0.000
69	A	80	PRO	0	0.047	0.008	24.395	0.296	0.296	0.000	0.000	0.000	0.000
70	A	81	ALA	0	-0.006	0.010	22.889	0.159	0.159	0.000	0.000	0.000	0.000
71	A	82	THR	0	-0.056	-0.028	25.016	0.336	0.336	0.000	0.000	0.000	0.000
72	A	83	GLY	0	0.043	0.029	28.107	0.566	0.566	0.000	0.000	0.000	0.000
73	A	84	GLU	-1	-0.927	-0.967	29.697	-18.074	-18.074	0.000	0.000	0.000	0.000
74	A	85	PRO	0	-0.034	-0.009	30.780	-0.512	-0.512	0.000	0.000	0.000	0.000
75	A	86	ILE	0	0.006	0.006	27.207	0.120	0.120	0.000	0.000	0.000	0.000
76	A	87	GLN	0	0.033	0.005	31.505	-0.027	-0.027	0.000	0.000	0.000	0.000
77	A	88	ILE	0	-0.066	-0.022	27.909	-0.506	-0.506	0.000	0.000	0.000	0.000
78	A	89	LYS	1	0.974	0.972	31.182	19.109	19.109	0.000	0.000	0.000	0.000
79	A	90	ALA	0	0.025	0.017	32.614	-0.413	-0.413	0.000	0.000	0.000	0.000
80	A	91	LYS	1	0.882	0.950	28.690	19.458	19.458	0.000	0.000	0.000	0.000
81	A	92	PRO	0	0.049	0.025	33.807	0.023	0.023	0.000	0.000	0.000	0.000
82	A	93	GLU	-1	-0.877	-0.945	34.597	-16.300	-16.300	0.000	0.000	0.000	0.000
83	A	94	HIS	0	-0.058	-0.047	29.237	-0.161	-0.161	0.000	0.000	0.000	0.000
84	A	95	LYS	1	0.975	0.990	33.495	16.312	16.312	0.000	0.000	0.000	0.000
85	A	96	ALA	0	-0.007	0.006	28.012	-0.366	-0.366	0.000	0.000	0.000	0.000
86	A	97	VAL	0	0.027	0.023	25.497	0.440	0.440	0.000	0.000	0.000	0.000
87	A	98	LYS	1	0.940	0.968	24.790	22.369	22.369	0.000	0.000	0.000	0.000
88	A	99	ILE	0	0.028	0.025	19.368	0.658	0.658	0.000	0.000	0.000	0.000
89	A	100	ARG	1	0.909	0.947	23.276	22.122	22.122	0.000	0.000	0.000	0.000
90	A	101	ALA	0	0.049	0.038	19.564	0.338	0.338	0.000	0.000	0.000	0.000
91	A	102	LEU	0	-0.036	-0.029	21.641	0.878	0.878	0.000	0.000	0.000	0.000
92	A	103	LYS	1	0.909	0.930	22.468	23.197	23.197	0.000	0.000	0.000	0.000
93	A	104	PRO	0	0.036	0.016	22.333	-0.742	-0.742	0.000	0.000	0.000	0.000
94	A	105	VAL	0	-0.027	-0.004	17.374	-0.860	-0.860	0.000	0.000	0.000	0.000
95	A	106	HIS	0	-0.023	-0.028	17.673	-0.915	-0.915	0.000	0.000	0.000	0.000
96	A	107	ASP	-1	-0.801	-0.885	18.363	-26.217	-26.217	0.000	0.000	0.000	0.000
97	A	108	MET	0	-0.078	-0.033	15.248	0.254	0.254	0.000	0.000	0.000	0.000
98	A	109	LEU	0	-0.085	-0.039	12.600	-2.510	-2.510	0.000	0.000	0.000	0.000
99	A	110	ASN	-1	-0.919	-0.929	15.950	-31.135	-31.135	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:LYS)