FMO DATABASE

FMODB ID: 6Z92Z

Calculation Name: 2D88-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2D88

Chain ID: A

ChEMBL ID:

UniProt ID: Q7RTP6

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-959551.74083
FMO2-HF: Nuclear repulsion	911704.441953
FMO2-HF: Total energy	-47847.298876
FMO2-MP2: Total energy	-47981.776378

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.
-8.094	-4.625	0.246	-1.784	-1.931	-0.012

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 : 0.851 / q_NPA : 0.916

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	0.073	0.022	3.820	-2.009	-1.089	-0.012	-0.380	-0.528	0.000
5	A	5	SER	0	-0.088	-0.044	3.230	-4.202	-2.602	0.159	-0.955	-0.804	-0.008
10	A	10	ARG	1	0.987	0.993	3.051	56.987	57.936	0.099	-0.449	-0.599	-0.004
4	A	4	GLY	0	0.038	0.029	6.883	1.416	1.416	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.026	0.020	5.439	1.185	1.185	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.008	-0.007	6.903	-3.127	-3.127	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.001	0.005	5.044	1.155	1.155	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.032	0.014	8.449	0.276	0.276	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.034	0.006	6.970	-5.547	-5.547	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.020	-0.017	8.747	1.575	1.575	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.978	0.974	11.769	23.705	23.705	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.071	0.055	13.822	-0.260	-0.260	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.021	0.026	10.579	0.323	0.323	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.005	0.008	12.058	0.107	0.107	0.000	0.000	0.000	0.000
17	A	17	TRP	0	0.012	-0.003	12.653	0.028	0.028	0.000	0.000	0.000	0.000
18	A	18	CYS	0	0.031	0.012	16.382	0.888	0.888	0.000	0.000	0.000	0.000
19	A	19	GLN	0	-0.091	-0.042	10.475	-0.868	-0.868	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.945	0.973	14.090	18.641	18.641	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.006	0.014	16.781	0.937	0.937	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.062	-0.057	18.081	0.425	0.425	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.906	-0.950	17.528	-16.994	-16.994	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.021	-0.011	19.208	0.799	0.799	0.000	0.000	0.000	0.000
25	A	25	TYR	0	-0.036	-0.026	21.786	0.441	0.441	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.014	0.010	22.252	-0.530	-0.530	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.011	-0.011	22.708	0.174	0.174	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.031	-0.009	19.826	-0.441	-0.441	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.042	-0.025	14.855	-0.433	-0.433	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.048	0.030	15.309	-0.853	-0.853	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.007	-0.019	12.960	-1.464	-1.464	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.905	-0.925	12.449	-23.633	-23.633	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.051	-0.052	14.876	0.618	0.618	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.005	-0.026	17.248	0.518	0.518	0.000	0.000	0.000	0.000
35	A	35	MET	0	-0.004	-0.011	19.194	0.747	0.747	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.010	0.000	17.621	0.328	0.328	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.030	0.001	17.644	0.609	0.609	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.930	0.986	22.221	13.353	13.353	0.000	0.000	0.000	0.000
39	A	39	SER	0	0.007	0.016	24.295	0.692	0.692	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.055	0.023	25.558	0.447	0.447	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.037	0.025	24.865	-0.143	-0.143	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.012	0.006	21.044	-0.019	-0.019	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.008	-0.012	22.980	-0.120	-0.120	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.024	0.000	25.295	0.326	0.326	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.017	0.013	23.650	0.220	0.220	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.083	-0.039	20.765	-0.144	-0.144	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.003	0.004	24.784	0.112	0.112	0.000	0.000	0.000	0.000
48	A	48	HIS	0	0.038	0.040	28.515	-0.192	-0.192	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.883	0.959	22.426	13.691	13.691	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.018	-0.014	23.837	-0.203	-0.203	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.925	0.962	29.130	9.425	9.425	0.000	0.000	0.000	0.000
52	A	52	PRO	0	0.037	0.018	31.847	0.046	0.046	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.937	-0.971	33.054	-8.630	-8.630	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.054	-0.018	33.634	0.144	0.144	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.033	-0.027	30.598	0.069	0.069	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.844	-0.912	32.783	-9.249	-9.249	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.018	-0.041	26.276	-0.155	-0.155	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.981	-0.975	31.291	-9.460	-9.460	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.027	-0.020	33.291	0.139	0.139	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.090	-0.035	31.292	0.157	0.157	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.855	-0.916	31.999	-9.251	-9.251	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.922	-0.985	27.893	-10.498	-10.498	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.039	-0.018	29.441	-0.154	-0.154	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.106	-0.044	32.068	0.296	0.296	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.070	0.041	28.607	-0.079	-0.079	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.836	-0.911	30.864	-8.769	-8.769	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.944	0.964	33.452	8.430	8.430	0.000	0.000	0.000	0.000
68	A	68	ASN	0	0.068	0.027	29.297	-0.056	-0.056	0.000	0.000	0.000	0.000
69	A	69	ASN	0	-0.028	-0.027	27.985	-0.294	-0.294	0.000	0.000	0.000	0.000
70	A	70	GLN	0	0.003	-0.008	30.690	-0.070	-0.070	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.021	0.006	33.789	0.174	0.174	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.055	0.017	29.680	0.099	0.099	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.065	-0.044	29.114	-0.074	-0.074	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.890	-0.926	32.858	-8.099	-8.099	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.022	0.000	33.788	0.090	0.090	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.000	-0.005	31.076	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.974	-0.985	32.989	-8.237	-8.237	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.837	0.906	35.757	8.185	8.185	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.944	-0.961	35.657	-8.104	-8.104	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.062	-0.035	30.143	-0.055	-0.055	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.033	0.035	34.125	-0.051	-0.051	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.099	-0.048	28.558	-0.080	-0.080	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.035	0.019	32.437	0.174	0.174	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.024	-0.009	31.451	-0.427	-0.427	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.024	-0.020	26.755	0.140	0.140	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.045	-0.012	26.870	0.058	0.058	0.000	0.000	0.000	0.000
87	A	87	THR	0	0.068	0.035	32.408	-0.056	-0.056	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.066	0.016	32.151	-0.274	-0.274	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.860	0.922	32.615	8.242	8.242	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.926	-0.959	32.559	-9.282	-9.282	0.000	0.000	0.000	0.000
91	A	91	MET	0	-0.035	-0.022	25.253	-0.223	-0.223	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.027	-0.015	28.452	-0.384	-0.384	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.043	-0.018	30.566	0.012	0.012	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.045	-0.003	27.000	-0.052	-0.052	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.027	0.008	27.094	-0.286	-0.286	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.885	-0.956	19.404	-16.381	-16.381	0.000	0.000	0.000	0.000
97	A	97	PRO	0	0.000	0.024	22.261	0.353	0.353	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.798	-0.905	22.456	-14.086	-14.086	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.960	0.974	14.583	19.897	19.897	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.033	-0.020	19.947	-0.586	-0.586	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.009	0.003	21.638	0.259	0.259	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.015	0.015	20.970	0.472	0.472	0.000	0.000	0.000	0.000
103	A	103	VAL	0	-0.039	-0.019	17.716	-0.232	-0.232	0.000	0.000	0.000	0.000
104	A	104	MET	0	-0.019	0.000	20.622	0.166	0.166	0.000	0.000	0.000	0.000
105	A	105	TYR	0	0.039	0.024	23.870	0.286	0.286	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.028	0.009	19.955	0.188	0.188	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.068	-0.059	21.719	-0.279	-0.279	0.000	0.000	0.000	0.000
108	A	108	GLN	0	-0.033	-0.004	22.947	0.393	0.393	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.063	0.025	24.238	0.237	0.237	0.000	0.000	0.000	0.000
110	A	110	TYR	0	-0.064	-0.025	19.572	-0.102	-0.102	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.910	-1.001	23.013	-12.877	-12.877	0.000	0.000	0.000	0.000
112	A	112	MET	0	-0.019	0.018	25.759	0.361	0.361	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.018	-0.019	24.839	0.260	0.260	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.766	0.897	22.766	12.006	12.006	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.906	-0.946	23.660	-12.006	-12.006	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.009	0.012	26.524	0.592	0.592	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.015	0.009	28.656	-0.130	-0.130	0.000	0.000	0.000	0.000
118	A	118	PRO	0	-0.015	-0.019	29.887	-0.131	-0.131	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.048	-0.017	30.977	0.004	0.004	0.000	0.000	0.000	0.000
120	A	120	SER	0	-0.047	-0.020	29.334	-0.377	-0.377	0.000	0.000	0.000	0.000
121	A	121	GLY	-1	-0.915	-0.945	30.365	-9.450	-9.450	0.000	0.000	0.000	0.000

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