FMO DATABASE

FMODB ID: 55NLZ

Calculation Name: 2DH7-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DH7

Chain ID: A

ChEMBL ID:

UniProt ID: Q01085

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	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-683683.456508
FMO2-HF: Nuclear repulsion	644717.256383
FMO2-HF: Total energy	-38966.200125
FMO2-MP2: Total energy	-39080.638911

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:82:GLY)

Summations of interaction energy for fragment #1(A:82: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.
77.082	78.208	-0.005	-0.44	-0.68	-0.001

Interaction energy analysis for fragmet #1(A:82:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.919

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	84	SER	0	0.016	0.015	3.831	1.263	2.111	-0.006	-0.335	-0.507	0.000
59	A	140	TYR	0	-0.048	-0.031	3.842	-3.087	-2.809	0.001	-0.105	-0.173	-0.001
4	A	85	GLY	0	0.025	0.000	6.805	0.233	0.233	0.000	0.000	0.000	0.000
5	A	86	SER	0	0.031	0.021	9.944	1.064	1.064	0.000	0.000	0.000	0.000
6	A	87	SER	0	-0.005	-0.004	12.856	-1.103	-1.103	0.000	0.000	0.000	0.000
7	A	88	GLY	0	0.008	0.014	13.953	1.226	1.226	0.000	0.000	0.000	0.000
8	A	89	GLN	0	-0.036	-0.014	15.699	-0.474	-0.474	0.000	0.000	0.000	0.000
9	A	90	LYS	1	0.949	0.976	17.373	13.818	13.818	0.000	0.000	0.000	0.000
10	A	91	LYS	1	0.923	0.940	20.513	12.331	12.331	0.000	0.000	0.000	0.000
11	A	92	ASP	-1	-0.864	-0.918	21.341	-14.200	-14.200	0.000	0.000	0.000	0.000
12	A	93	THR	0	-0.015	-0.001	19.785	0.264	0.264	0.000	0.000	0.000	0.000
13	A	94	SER	0	0.003	-0.001	22.693	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	95	ASN	0	-0.025	-0.020	24.621	0.148	0.148	0.000	0.000	0.000	0.000
15	A	96	HIS	0	0.009	0.012	21.986	-0.275	-0.275	0.000	0.000	0.000	0.000
16	A	97	PHE	0	0.036	0.013	21.589	-0.510	-0.510	0.000	0.000	0.000	0.000
17	A	98	HIS	0	-0.040	-0.023	16.031	-0.122	-0.122	0.000	0.000	0.000	0.000
18	A	99	VAL	0	0.007	0.003	17.274	-0.303	-0.303	0.000	0.000	0.000	0.000
19	A	100	PHE	0	-0.029	-0.016	9.215	-0.838	-0.838	0.000	0.000	0.000	0.000
20	A	101	VAL	0	0.019	0.003	13.209	1.322	1.322	0.000	0.000	0.000	0.000
21	A	102	GLY	0	0.006	-0.014	12.262	-2.230	-2.230	0.000	0.000	0.000	0.000
22	A	103	ASP	-1	-0.867	-0.930	12.907	-19.463	-19.463	0.000	0.000	0.000	0.000
23	A	104	LEU	0	-0.029	-0.001	12.597	1.350	1.350	0.000	0.000	0.000	0.000
24	A	105	SER	0	0.056	0.024	14.142	-1.082	-1.082	0.000	0.000	0.000	0.000
25	A	106	PRO	0	-0.077	-0.046	15.490	-0.262	-0.262	0.000	0.000	0.000	0.000
26	A	107	GLU	-1	-0.913	-0.960	16.521	-13.993	-13.993	0.000	0.000	0.000	0.000
27	A	108	ILE	0	0.009	0.034	16.488	0.338	0.338	0.000	0.000	0.000	0.000
28	A	109	THR	0	0.007	-0.027	17.275	-0.913	-0.913	0.000	0.000	0.000	0.000
29	A	110	THR	0	-0.021	-0.038	16.499	-0.434	-0.434	0.000	0.000	0.000	0.000
30	A	111	GLU	-1	-0.902	-0.945	18.319	-12.631	-12.631	0.000	0.000	0.000	0.000
31	A	112	ASP	-1	-0.778	-0.861	20.823	-13.200	-13.200	0.000	0.000	0.000	0.000
32	A	113	ILE	0	-0.038	-0.017	15.844	0.171	0.171	0.000	0.000	0.000	0.000
33	A	114	LYS	1	0.910	0.945	19.826	14.670	14.670	0.000	0.000	0.000	0.000
34	A	115	SER	0	0.016	0.000	22.424	0.471	0.471	0.000	0.000	0.000	0.000
35	A	116	ALA	0	0.012	0.005	22.737	0.380	0.380	0.000	0.000	0.000	0.000
36	A	117	PHE	0	-0.009	-0.023	19.219	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	118	ALA	0	0.006	0.003	23.805	0.184	0.184	0.000	0.000	0.000	0.000
38	A	119	PRO	0	-0.038	-0.016	26.745	0.312	0.312	0.000	0.000	0.000	0.000
39	A	120	PHE	0	-0.008	0.007	24.593	0.190	0.190	0.000	0.000	0.000	0.000
40	A	121	GLY	0	0.074	0.039	27.895	0.212	0.212	0.000	0.000	0.000	0.000
41	A	122	LYS	1	0.860	0.932	26.564	11.113	11.113	0.000	0.000	0.000	0.000
42	A	123	ILE	0	0.040	0.022	21.240	-0.302	-0.302	0.000	0.000	0.000	0.000
43	A	124	SER	0	-0.073	-0.024	22.225	0.754	0.754	0.000	0.000	0.000	0.000
44	A	125	ASP	-1	-0.870	-0.933	17.764	-15.181	-15.181	0.000	0.000	0.000	0.000
45	A	126	ALA	0	0.014	-0.004	16.807	-0.365	-0.365	0.000	0.000	0.000	0.000
46	A	127	ARG	1	0.872	0.942	10.081	25.759	25.759	0.000	0.000	0.000	0.000
47	A	128	VAL	0	0.054	0.033	12.664	-0.953	-0.953	0.000	0.000	0.000	0.000
48	A	129	VAL	0	-0.062	-0.029	6.155	0.132	0.132	0.000	0.000	0.000	0.000
49	A	130	LYS	1	0.928	0.977	9.303	17.192	17.192	0.000	0.000	0.000	0.000
50	A	131	ASP	-1	-0.840	-0.932	8.250	-33.756	-33.756	0.000	0.000	0.000	0.000
51	A	132	MET	0	-0.033	-0.012	9.102	2.546	2.546	0.000	0.000	0.000	0.000
52	A	133	ALA	0	0.010	0.024	10.898	1.579	1.579	0.000	0.000	0.000	0.000
53	A	134	THR	0	0.000	-0.022	12.315	1.108	1.108	0.000	0.000	0.000	0.000
54	A	135	GLY	0	0.039	0.036	13.336	1.189	1.189	0.000	0.000	0.000	0.000
55	A	136	LYS	1	0.911	0.954	13.461	20.637	20.637	0.000	0.000	0.000	0.000
56	A	137	SER	0	-0.035	-0.036	11.899	-2.424	-2.424	0.000	0.000	0.000	0.000
57	A	138	LYS	1	0.837	0.901	5.348	39.577	39.577	0.000	0.000	0.000	0.000
58	A	139	GLY	0	0.038	0.040	9.263	-1.434	-1.434	0.000	0.000	0.000	0.000
60	A	141	GLY	0	0.022	0.002	9.951	-0.277	-0.277	0.000	0.000	0.000	0.000
61	A	142	PHE	0	-0.030	-0.012	8.265	-0.802	-0.802	0.000	0.000	0.000	0.000
62	A	143	VAL	0	0.045	0.022	13.722	0.647	0.647	0.000	0.000	0.000	0.000
63	A	144	SER	0	0.004	0.021	17.547	-0.218	-0.218	0.000	0.000	0.000	0.000
64	A	145	PHE	0	0.018	0.007	19.667	0.305	0.305	0.000	0.000	0.000	0.000
65	A	146	TYR	0	-0.011	-0.029	23.358	-0.146	-0.146	0.000	0.000	0.000	0.000
66	A	147	ASN	0	-0.002	-0.002	26.409	0.189	0.189	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.847	0.932	24.925	11.706	11.706	0.000	0.000	0.000	0.000
68	A	149	LEU	0	0.060	0.031	26.440	-0.301	-0.301	0.000	0.000	0.000	0.000
69	A	150	ASP	-1	-0.822	-0.906	26.930	-10.843	-10.843	0.000	0.000	0.000	0.000
70	A	151	ALA	0	0.003	-0.001	22.444	-0.285	-0.285	0.000	0.000	0.000	0.000
71	A	152	GLU	-1	-0.872	-0.940	23.708	-12.056	-12.056	0.000	0.000	0.000	0.000
72	A	153	ASN	0	-0.012	-0.001	25.881	0.009	0.009	0.000	0.000	0.000	0.000
73	A	154	ALA	0	0.031	0.015	22.743	-0.036	-0.036	0.000	0.000	0.000	0.000
74	A	155	ILE	0	-0.046	-0.033	20.279	-0.397	-0.397	0.000	0.000	0.000	0.000
75	A	156	VAL	0	0.011	0.015	22.573	-0.297	-0.297	0.000	0.000	0.000	0.000
76	A	157	HIS	0	-0.001	0.009	25.603	-0.016	-0.016	0.000	0.000	0.000	0.000
77	A	158	MET	0	-0.010	-0.016	21.577	0.245	0.245	0.000	0.000	0.000	0.000
78	A	159	GLY	0	0.005	0.017	21.102	-0.641	-0.641	0.000	0.000	0.000	0.000
79	A	160	GLY	0	-0.023	-0.003	21.049	0.526	0.526	0.000	0.000	0.000	0.000
80	A	161	GLN	0	-0.025	-0.005	22.349	0.543	0.543	0.000	0.000	0.000	0.000
81	A	162	TRP	0	0.016	-0.006	22.513	-0.925	-0.925	0.000	0.000	0.000	0.000
82	A	163	LEU	0	-0.033	0.002	20.073	0.295	0.295	0.000	0.000	0.000	0.000
83	A	164	GLY	0	0.110	0.037	21.789	0.439	0.439	0.000	0.000	0.000	0.000
84	A	165	GLY	0	-0.033	0.000	21.139	-0.782	-0.782	0.000	0.000	0.000	0.000
85	A	166	ARG	1	0.886	0.928	18.724	15.491	15.491	0.000	0.000	0.000	0.000
86	A	167	GLN	0	-0.032	-0.015	20.659	0.060	0.060	0.000	0.000	0.000	0.000
87	A	168	ILE	0	-0.020	0.005	17.639	-0.895	-0.895	0.000	0.000	0.000	0.000
88	A	169	ARG	1	0.962	0.977	15.436	17.722	17.722	0.000	0.000	0.000	0.000
89	A	170	THR	0	-0.026	-0.022	16.740	-0.757	-0.757	0.000	0.000	0.000	0.000
90	A	171	ASN	0	-0.032	-0.012	14.136	1.061	1.061	0.000	0.000	0.000	0.000
91	A	172	TRP	0	0.042	0.017	16.791	-0.403	-0.403	0.000	0.000	0.000	0.000
92	A	173	ALA	0	-0.021	-0.007	13.350	-0.695	-0.695	0.000	0.000	0.000	0.000
93	A	174	THR	0	-0.030	-0.008	14.214	-0.680	-0.680	0.000	0.000	0.000	0.000
94	A	175	ARG	1	0.974	0.990	14.466	20.098	20.098	0.000	0.000	0.000	0.000
95	A	176	LYS	1	0.977	0.976	17.121	13.682	13.682	0.000	0.000	0.000	0.000
96	A	177	PRO	0	0.007	0.012	20.346	-0.462	-0.462	0.000	0.000	0.000	0.000
97	A	178	PRO	0	0.009	0.005	21.771	0.294	0.294	0.000	0.000	0.000	0.000
98	A	179	ALA	0	0.017	0.007	24.568	0.095	0.095	0.000	0.000	0.000	0.000
99	A	180	PRO	0	0.001	0.004	28.261	-0.088	-0.088	0.000	0.000	0.000	0.000
100	A	181	SER	0	-0.011	-0.015	30.501	0.210	0.210	0.000	0.000	0.000	0.000
101	A	182	GLY	0	0.025	0.012	33.555	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	183	PRO	0	-0.032	-0.007	35.501	0.193	0.193	0.000	0.000	0.000	0.000
103	A	184	SER	0	-0.026	-0.023	38.375	0.132	0.132	0.000	0.000	0.000	0.000
104	A	185	SER	0	-0.030	-0.026	41.969	-0.095	-0.095	0.000	0.000	0.000	0.000
105	A	186	GLY	-1	-0.918	-0.933	44.179	-6.683	-6.683	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:82:GLY)