FMO DATABASE

FMODB ID: G8VR1

Calculation Name: 1B34-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1B34

Chain ID: A

ChEMBL ID:

UniProt ID: P62314

Base Structure: X-ray

Registration Date: 2025-09-02

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	80
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-513765.38273
FMO2-HF: Nuclear repulsion	482149.948794
FMO2-HF: Total energy	-31615.433935
FMO2-MP2: Total energy	-31707.441882

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:2:LYS)

Summations of interaction energy for fragment #1(A:2: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.
63.812	68.085	1.376	-2.161	-3.486	-0.019

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.829 / q_NPA : 1.899

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	4	VAL	0	0.067	0.030	2.380	-0.973	1.772	1.348	-1.686	-2.407	-0.016
4	A	5	ARG	1	0.935	0.959	3.007	89.615	90.970	0.029	-0.452	-0.931	-0.003
5	A	6	PHE	0	0.027	0.033	4.764	7.151	7.324	-0.001	-0.023	-0.148	0.000
6	A	7	LEU	0	0.032	0.003	6.939	5.813	5.813	0.000	0.000	0.000	0.000
7	A	8	MET	0	-0.069	-0.036	5.395	4.468	4.468	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.855	0.933	7.461	63.163	63.163	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.001	0.017	11.027	2.821	2.821	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.024	-0.006	13.520	1.915	1.915	0.000	0.000	0.000	0.000
11	A	12	HIS	0	-0.016	-0.029	15.992	0.966	0.966	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.854	-0.915	15.995	-30.858	-30.858	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.041	-0.016	18.719	0.585	0.585	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.014	0.015	16.400	-0.532	-0.532	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.007	-0.004	19.847	2.016	2.016	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.005	0.008	16.498	-1.286	-1.286	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.806	-0.860	19.170	-24.239	-24.239	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.014	0.000	18.994	-1.682	-1.682	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.877	0.923	15.797	33.851	33.851	0.000	0.000	0.000	0.000
20	A	21	ASN	0	-0.010	0.012	21.409	0.043	0.043	0.000	0.000	0.000	0.000
21	A	22	GLY	0	0.000	0.011	23.803	1.007	1.007	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.018	-0.016	24.866	0.959	0.959	0.000	0.000	0.000	0.000
23	A	24	GLN	0	0.000	-0.004	23.678	-0.989	-0.989	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.002	0.000	21.919	1.071	1.071	0.000	0.000	0.000	0.000
25	A	26	HIS	0	-0.027	-0.015	22.202	-0.795	-0.795	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.080	0.036	22.618	0.901	0.901	0.000	0.000	0.000	0.000
27	A	28	THR	0	-0.038	-0.013	21.167	-0.764	-0.764	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.011	-0.003	14.457	0.516	0.516	0.000	0.000	0.000	0.000
29	A	30	THR	0	-0.076	-0.052	18.223	0.542	0.542	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.048	0.012	14.845	-0.260	-0.260	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.023	-0.004	10.099	0.892	0.892	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.758	-0.854	10.788	-42.248	-42.248	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.028	-0.009	5.760	-3.569	-3.569	0.000	0.000	0.000	0.000
34	A	35	SER	0	-0.082	-0.034	7.503	-4.066	-4.066	0.000	0.000	0.000	0.000
35	A	36	MET	0	-0.031	-0.029	8.327	0.612	0.612	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.044	-0.031	10.553	3.429	3.429	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.013	-0.004	13.606	-1.912	-1.912	0.000	0.000	0.000	0.000
38	A	39	HIS	0	0.032	0.037	15.345	2.998	2.998	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.020	0.020	18.390	-0.717	-0.717	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.997	0.983	20.836	24.932	24.932	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.017	-0.011	24.157	-0.424	-0.424	0.000	0.000	0.000	0.000
42	A	43	VAL	0	-0.029	0.000	23.974	-0.456	-0.456	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.997	1.009	26.378	20.905	20.905	0.000	0.000	0.000	0.000
44	A	45	MET	0	-0.011	-0.005	26.528	-1.057	-1.057	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.014	0.002	27.578	1.027	1.027	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.015	0.009	28.228	-0.665	-0.665	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.914	0.939	26.756	22.299	22.299	0.000	0.000	0.000	0.000
48	A	49	ASN	0	-0.027	-0.014	31.141	0.178	0.178	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.949	0.980	33.832	17.524	17.524	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.886	-0.931	34.229	-16.107	-16.107	0.000	0.000	0.000	0.000
51	A	52	PRO	0	-0.089	-0.049	31.769	-0.363	-0.363	0.000	0.000	0.000	0.000
52	A	53	VAL	0	0.039	0.017	30.765	0.441	0.441	0.000	0.000	0.000	0.000
53	A	54	GLN	0	0.008	0.003	30.341	-1.165	-1.165	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.009	-0.012	27.535	0.358	0.358	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.899	-0.938	28.756	-18.818	-18.818	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.035	-0.033	24.386	-0.763	-0.763	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.002	0.006	22.955	0.633	0.633	0.000	0.000	0.000	0.000
58	A	59	SER	0	-0.032	-0.015	19.288	-1.147	-1.147	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.010	0.004	17.884	0.962	0.962	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.990	0.989	16.816	25.223	25.223	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.088	0.048	13.115	0.498	0.498	0.000	0.000	0.000	0.000
62	A	63	ASN	0	-0.026	-0.025	14.064	-0.090	-0.090	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.006	-0.012	15.844	1.183	1.183	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.016	0.030	14.003	1.510	1.510	0.000	0.000	0.000	0.000
65	A	66	ARG	1	0.807	0.894	16.059	26.641	26.641	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.047	-0.054	14.827	-1.878	-1.878	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.033	0.003	11.985	1.189	1.189	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.010	-0.003	15.982	-1.047	-1.047	0.000	0.000	0.000	0.000
69	A	70	LEU	0	-0.006	-0.016	12.589	0.101	0.101	0.000	0.000	0.000	0.000
70	A	71	PRO	0	0.021	0.008	16.916	1.010	1.010	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.894	-0.937	18.652	-27.695	-27.695	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.026	-0.015	20.441	0.045	0.045	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.020	-0.006	13.808	-0.640	-0.640	0.000	0.000	0.000	0.000
74	A	75	PRO	0	0.022	0.024	15.475	-0.248	-0.248	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.015	-0.021	12.250	-2.971	-2.971	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.862	-0.936	11.003	-44.092	-44.092	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.033	0.009	11.107	-2.728	-2.728	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.075	-0.027	9.898	-2.103	-2.103	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.118	-0.066	5.979	-8.887	-8.887	0.000	0.000	0.000	0.000
80	A	81	VAL	-1	-0.945	-0.937	7.292	-59.947	-59.947	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)