FMO DATABASE

FMODB ID: ZZGJN

Calculation Name: 3H1H-T-Xray547

Preferred Name:

Target Type:

Ligand 3-letter code: CDL | UQ | HEM | HEC | PEE | BOG | FES | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3H1H

Chain ID: T

ChEMBL ID:

UniProt ID: P18946

Base Structure: X-ray

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	79
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-356724.156828
FMO2-HF: Nuclear repulsion	325082.662176
FMO2-HF: Total energy	-31641.494652
FMO2-MP2: Total energy	-31736.731532

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:ILE)

Summations of interaction energy for fragment #1(A:2:ILE)

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.
55.415	59.262	0.185	-1.701	-2.333	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.873 / q_NPA : 0.920

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	PHE	0	0.047	0.023	3.865	5.470	8.137	-0.027	-1.301	-1.340	-0.005
4	A	5	GLY	0	0.015	0.013	4.074	-3.409	-3.146	0.001	-0.046	-0.219	0.000
5	A	6	ASN	0	-0.019	-0.015	2.920	5.343	6.260	0.211	-0.354	-0.774	-0.004
6	A	7	LEU	0	-0.032	0.002	5.975	2.161	2.161	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.060	0.020	8.765	1.847	1.847	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.947	0.982	12.035	16.581	16.581	0.000	0.000	0.000	0.000
9	A	10	VAL	0	0.035	0.017	14.123	1.115	1.115	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.892	0.919	16.178	13.072	13.072	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.028	0.008	19.303	0.075	0.075	0.000	0.000	0.000	0.000
12	A	13	ILE	0	0.032	0.041	19.260	0.459	0.459	0.000	0.000	0.000	0.000
13	A	14	ILE	0	0.006	0.014	20.441	-0.584	-0.584	0.000	0.000	0.000	0.000
14	A	15	THR	0	-0.037	-0.018	20.138	0.063	0.063	0.000	0.000	0.000	0.000
15	A	16	TYR	0	0.056	0.021	22.799	0.063	0.063	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.040	-0.030	22.785	-0.387	-0.387	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.018	0.024	24.841	0.126	0.126	0.000	0.000	0.000	0.000
18	A	19	SER	0	0.052	0.027	25.006	-0.528	-0.528	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.007	-0.022	24.049	0.338	0.338	0.000	0.000	0.000	0.000
20	A	21	PHE	0	-0.022	-0.011	26.134	0.240	0.240	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.917	-0.941	29.392	-9.617	-9.617	0.000	0.000	0.000	0.000
22	A	23	GLN	0	-0.061	-0.026	26.628	0.381	0.381	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.919	0.957	31.862	8.613	8.613	0.000	0.000	0.000	0.000
24	A	25	ALA	0	0.041	0.019	30.076	-0.119	-0.119	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.013	0.007	30.722	-0.197	-0.197	0.000	0.000	0.000	0.000
26	A	27	PRO	0	-0.015	0.002	32.069	0.373	0.373	0.000	0.000	0.000	0.000
27	A	28	ASN	0	0.015	-0.016	35.063	0.137	0.137	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.062	0.042	37.287	0.024	0.024	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.051	0.006	38.730	-0.038	-0.038	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.001	0.001	40.549	0.048	0.048	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.874	-0.930	34.612	-9.133	-9.133	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.007	0.011	35.490	-0.038	-0.038	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.019	0.002	36.526	-0.072	-0.072	0.000	0.000	0.000	0.000
34	A	35	PRO	0	0.025	0.017	39.530	0.019	0.019	0.000	0.000	0.000	0.000
35	A	36	ASN	0	0.027	0.011	34.892	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	37	VAL	0	-0.060	-0.023	35.551	-0.181	-0.181	0.000	0.000	0.000	0.000
37	A	38	TRP	0	0.066	0.033	37.180	-0.062	-0.062	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.924	0.965	32.859	9.284	9.284	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.915	0.955	30.609	9.865	9.865	0.000	0.000	0.000	0.000
40	A	41	PHE	0	0.036	0.030	36.293	-0.049	-0.049	0.000	0.000	0.000	0.000
41	A	42	SER	0	0.022	-0.004	38.820	0.104	0.104	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.086	-0.042	36.606	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	44	GLN	0	0.020	-0.002	34.724	-0.080	-0.080	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.046	0.040	38.294	0.020	0.020	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.022	-0.007	41.671	0.022	0.022	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.847	0.931	36.186	8.700	8.700	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.001	-0.002	36.807	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.015	0.009	39.722	0.068	0.068	0.000	0.000	0.000	0.000
49	A	50	PRO	0	-0.002	0.006	42.951	0.118	0.118	0.000	0.000	0.000	0.000
50	A	51	PRO	0	0.041	0.023	40.986	0.149	0.149	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.005	-0.004	37.744	0.051	0.051	0.000	0.000	0.000	0.000
52	A	53	LEU	0	0.018	0.018	43.898	0.111	0.111	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.021	0.003	47.114	0.145	0.145	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.002	0.000	45.065	0.109	0.109	0.000	0.000	0.000	0.000
55	A	56	TYR	0	0.017	0.010	47.128	0.077	0.077	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.005	0.003	49.034	0.143	0.143	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.012	0.014	48.979	0.123	0.123	0.000	0.000	0.000	0.000
58	A	59	TYR	0	-0.001	0.001	49.321	0.083	0.083	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.016	-0.009	51.381	0.109	0.109	0.000	0.000	0.000	0.000
60	A	61	TRP	0	0.013	0.005	54.393	0.056	0.056	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.038	0.016	54.661	0.095	0.095	0.000	0.000	0.000	0.000
62	A	63	THR	0	-0.040	-0.031	53.773	0.058	0.058	0.000	0.000	0.000	0.000
63	A	64	GLN	0	-0.029	-0.031	56.309	0.035	0.035	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.790	-0.848	59.121	-5.024	-5.024	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.001	-0.004	58.017	0.092	0.092	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.841	-0.912	59.698	-5.234	-5.234	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.786	0.853	62.233	5.063	5.063	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.030	-0.021	61.990	0.099	0.099	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.821	0.916	59.981	5.353	5.353	0.000	0.000	0.000	0.000
70	A	71	ARG	1	0.848	0.934	66.125	4.777	4.777	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.977	0.998	69.116	4.234	4.234	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.003	-0.027	72.484	0.004	0.004	0.000	0.000	0.000	0.000
73	A	74	PRO	0	-0.020	-0.015	74.229	0.026	0.026	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.041	0.023	77.512	0.041	0.041	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.919	-0.937	75.282	-4.299	-4.299	0.000	0.000	0.000	0.000
76	A	77	TYR	0	-0.091	-0.064	76.371	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.958	-0.977	81.483	-3.945	-3.945	0.000	0.000	0.000	0.000
78	A	79	ASN	0	-0.108	-0.050	83.886	0.077	0.077	0.000	0.000	0.000	0.000
79	A	80	ASP	-2	-1.888	-1.923	85.348	-7.380	-7.380	0.000	0.000	0.000	0.000

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