FMO DATABASE

FMODB ID: 2MLZR

Calculation Name: 2DIQ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DIQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Y2W6

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	110
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-762674.732636
FMO2-HF: Nuclear repulsion	721056.673145
FMO2-HF: Total energy	-41618.059491
FMO2-MP2: Total energy	-41739.073221

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.
-134.685	-133.151	0.074	-0.553	-1.055	-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 : 0.901 / q_NPA : 0.941

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	3	SER	0	-0.001	-0.004	3.845	2.264	3.041	-0.003	-0.281	-0.493	0.000
5	A	5	SER	0	-0.054	-0.038	2.936	-11.532	-10.959	0.078	-0.242	-0.410	-0.001
6	A	6	SER	0	0.035	0.011	3.712	6.908	7.018	0.000	-0.028	-0.081	0.000
71	A	71	GLY	0	-0.030	-0.016	4.802	-10.714	-10.640	-0.001	-0.002	-0.071	0.000
4	A	4	GLY	0	0.042	0.038	5.029	6.176	6.176	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.005	0.006	5.395	5.735	5.735	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.859	0.931	6.342	22.479	22.479	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.028	0.019	8.784	1.821	1.821	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.055	0.020	10.921	0.631	0.631	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.041	-0.025	14.212	1.464	1.464	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.040	0.033	9.311	0.981	0.981	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.856	-0.920	13.374	-20.659	-20.659	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.965	0.986	14.438	16.656	16.656	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.018	-0.002	15.556	0.840	0.840	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.041	0.019	13.014	0.589	0.589	0.000	0.000	0.000	0.000
17	A	17	ASN	0	0.005	0.025	16.391	0.809	0.809	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.939	-0.972	19.424	-12.556	-12.556	0.000	0.000	0.000	0.000
19	A	19	MET	0	-0.056	-0.026	17.770	0.346	0.346	0.000	0.000	0.000	0.000
20	A	20	THR	0	0.001	-0.012	18.764	0.358	0.358	0.000	0.000	0.000	0.000
21	A	21	GLN	0	0.019	0.010	21.336	0.377	0.377	0.000	0.000	0.000	0.000
22	A	22	HIS	0	-0.040	0.008	24.215	0.612	0.612	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.014	-0.028	21.730	0.290	0.290	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.939	-0.970	24.066	-12.172	-12.172	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.112	-0.055	25.590	0.518	0.518	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.024	-0.010	27.871	0.457	0.457	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.007	-0.004	29.205	-0.200	-0.200	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.041	-0.023	29.289	-0.275	-0.275	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.906	-0.953	28.999	-9.508	-9.508	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.938	-0.960	29.516	-9.982	-9.982	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.049	-0.024	25.718	0.232	0.232	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.032	-0.026	29.880	0.057	0.057	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.007	0.000	23.750	-0.107	-0.107	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.079	-0.050	25.797	0.604	0.604	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.017	0.012	21.103	-0.446	-0.446	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.023	-0.012	20.334	0.379	0.379	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.847	-0.912	20.622	-13.128	-13.128	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.057	-0.038	17.040	-0.858	-0.858	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.009	-0.008	19.155	0.888	0.888	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.004	0.006	18.552	-1.116	-1.116	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.047	0.015	17.451	0.857	0.857	0.000	0.000	0.000	0.000
42	A	42	PRO	0	0.018	0.024	17.788	-0.926	-0.926	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.010	0.006	12.819	-0.248	-0.248	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.023	0.001	16.958	0.233	0.233	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.024	-0.018	13.995	0.593	0.593	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.051	-0.032	13.492	0.447	0.447	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.005	0.029	16.682	0.508	0.508	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.051	-0.032	16.516	0.262	0.262	0.000	0.000	0.000	0.000
49	A	49	TRP	0	0.001	-0.015	17.504	-0.595	-0.595	0.000	0.000	0.000	0.000
50	A	50	TYR	0	0.001	-0.009	12.250	-1.204	-1.204	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.704	0.810	13.964	20.701	20.701	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.022	-0.007	13.640	-1.886	-1.886	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.913	0.961	15.261	19.051	19.051	0.000	0.000	0.000	0.000
54	A	54	VAL	0	0.001	0.014	17.081	-0.603	-0.603	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.010	-0.007	15.006	0.112	0.112	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.005	-0.011	19.476	0.547	0.547	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.068	-0.029	22.917	0.040	0.040	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.011	0.013	20.341	0.178	0.178	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.970	-0.986	24.396	-10.353	-10.353	0.000	0.000	0.000	0.000
60	A	60	ASN	0	0.031	0.011	24.222	0.385	0.385	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.005	0.001	27.590	0.302	0.302	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.065	-0.031	23.062	-0.228	-0.228	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.003	-0.004	22.446	0.041	0.041	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.875	-0.943	17.571	-18.199	-18.199	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.015	-0.011	16.391	0.333	0.333	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.034	0.013	9.099	-1.603	-1.603	0.000	0.000	0.000	0.000
67	A	67	PHE	0	0.038	0.003	10.001	1.088	1.088	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.041	0.022	9.646	-3.241	-3.241	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.785	-0.869	9.844	-24.059	-24.059	0.000	0.000	0.000	0.000
70	A	70	PHE	0	-0.051	-0.047	6.154	-1.135	-1.135	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.941	-0.958	6.992	-39.268	-39.268	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.020	-0.027	8.646	2.269	2.269	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.003	0.006	12.451	-0.435	-0.435	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.902	-0.946	15.433	-16.342	-16.342	0.000	0.000	0.000	0.000
76	A	76	CYS	0	-0.007	-0.003	19.199	0.343	0.343	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.012	0.015	22.277	0.142	0.142	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.031	0.009	25.350	-0.186	-0.186	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.923	0.984	26.560	10.546	10.546	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.859	-0.955	24.250	-11.615	-11.615	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.025	-0.004	20.929	-0.588	-0.588	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.833	0.913	23.084	12.297	12.297	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.043	0.025	23.436	-0.542	-0.542	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.006	0.015	18.942	0.045	0.045	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.879	0.933	23.110	12.063	12.063	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.029	0.000	23.616	-0.630	-0.630	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.876	-0.927	23.895	-12.691	-12.691	0.000	0.000	0.000	0.000
88	A	88	PHE	0	0.039	0.010	20.272	-0.379	-0.379	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.016	0.004	19.320	-1.025	-1.025	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.047	-0.007	19.867	-0.510	-0.510	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.018	0.011	14.297	-0.087	-0.087	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.050	0.031	14.711	-0.340	-0.340	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.018	0.002	12.782	-0.704	-0.704	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.079	-0.040	8.696	-0.944	-0.944	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.039	-0.008	6.649	-3.629	-3.629	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.025	-0.006	7.992	3.432	3.432	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.922	-0.953	8.299	-25.727	-25.727	0.000	0.000	0.000	0.000
98	A	98	CYS	-1	-0.807	-0.831	10.186	-24.991	-24.991	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.014	-0.022	11.451	0.513	0.513	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.018	0.006	14.011	0.894	0.894	0.000	0.000	0.000	0.000
101	A	101	ALA	0	-0.032	-0.032	17.396	0.029	0.029	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.818	0.866	13.550	21.064	21.064	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.006	-0.003	18.533	0.206	0.206	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.017	0.017	21.367	0.311	0.311	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.030	-0.034	25.054	-0.269	-0.269	0.000	0.000	0.000	0.000
106	A	106	GLY	0	-0.003	0.006	27.257	0.257	0.257	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.022	-0.009	29.788	-0.276	-0.276	0.000	0.000	0.000	0.000
108	A	108	SER	0	0.007	-0.007	29.338	-0.067	-0.067	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.035	-0.013	31.365	0.189	0.189	0.000	0.000	0.000	0.000
110	A	110	GLY	-1	-0.936	-0.953	33.284	-8.656	-8.656	0.000	0.000	0.000	0.000

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