FMO DATABASE

FMODB ID: 55NRZ

Calculation Name: 2B0R-A-Xray547

Preferred Name:

Target Type:

Ligand Name: unknown atom or ion

Ligand 3-letter code: UNX

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2B0R

Chain ID: A

ChEMBL ID:

UniProt ID: Q5CS32

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	164
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1561545.70225
FMO2-HF: Nuclear repulsion	1496590.670812
FMO2-HF: Total energy	-64955.031438
FMO2-MP2: Total energy	-65140.83047

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:35:ARG)

Summations of interaction energy for fragment #1(A:35:ARG)

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.
-402.942	-401.455	38.138	-18.031	-21.596	-0.216

Interaction energy analysis for fragmet #1(A:35:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.642 / q_NPA : 1.811

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	37	VAL	0	0.023	0.030	3.166	-5.941	-3.061	0.116	-1.095	-1.901	-0.004
4	A	38	VAL	0	-0.022	-0.003	4.518	9.624	9.801	-0.001	-0.018	-0.158	0.000
47	A	81	GLN	0	0.020	-0.029	3.619	-6.259	-5.810	-0.001	-0.224	-0.224	0.000
64	A	98	ASN	0	-0.010	-0.013	1.871	-24.751	-28.250	9.174	-2.514	-3.161	-0.031
65	A	99	CYS	0	-0.028	-0.024	3.648	6.148	6.239	0.000	0.112	-0.204	0.000
66	A	100	VAL	0	0.015	-0.012	2.541	-12.764	-10.739	1.258	-0.750	-2.534	-0.005
83	A	117	ASN	0	-0.033	-0.013	1.970	-28.399	-27.922	5.567	-2.728	-3.316	-0.033
84	A	118	CYS	0	-0.020	0.019	2.012	-36.963	-34.933	5.346	-3.732	-3.645	-0.055
85	A	119	ASP	-1	-0.791	-0.886	1.693	-146.453	-149.760	16.682	-7.067	-6.308	-0.088
86	A	120	ASP	-1	-0.885	-0.941	4.625	-60.466	-60.447	-0.001	-0.011	-0.008	0.000
103	A	137	SER	0	0.011	0.001	4.969	-13.533	-13.445	-0.001	-0.003	-0.083	0.000
104	A	138	ASN	0	-0.019	-0.010	4.645	14.897	14.954	-0.001	-0.001	-0.054	0.000
5	A	39	THR	0	-0.010	0.000	6.469	-0.763	-0.763	0.000	0.000	0.000	0.000
6	A	40	ASN	0	0.001	-0.027	9.118	-1.643	-1.643	0.000	0.000	0.000	0.000
7	A	41	GLY	0	-0.014	-0.003	11.710	3.013	3.013	0.000	0.000	0.000	0.000
8	A	42	SER	0	-0.014	-0.015	14.230	-1.373	-1.373	0.000	0.000	0.000	0.000
9	A	43	PRO	0	0.004	0.020	14.877	-0.707	-0.707	0.000	0.000	0.000	0.000
10	A	44	LYS	1	0.833	0.930	15.543	35.189	35.189	0.000	0.000	0.000	0.000
11	A	45	VAL	0	0.024	0.005	16.485	-1.743	-1.743	0.000	0.000	0.000	0.000
12	A	46	GLU	-1	-0.885	-0.927	19.140	-23.486	-23.486	0.000	0.000	0.000	0.000
13	A	47	LEU	0	-0.014	0.006	20.330	-0.970	-0.970	0.000	0.000	0.000	0.000
14	A	48	GLN	0	0.030	0.016	20.413	0.287	0.287	0.000	0.000	0.000	0.000
15	A	49	LYS	1	0.937	0.961	22.381	21.091	21.091	0.000	0.000	0.000	0.000
16	A	50	ASP	-1	-0.929	-0.979	23.827	-22.216	-22.216	0.000	0.000	0.000	0.000
17	A	51	THR	0	-0.035	-0.017	17.865	-0.272	-0.272	0.000	0.000	0.000	0.000
18	A	52	TYR	0	-0.015	-0.036	19.863	-0.066	-0.066	0.000	0.000	0.000	0.000
19	A	53	LEU	0	-0.017	-0.016	15.729	-1.665	-1.665	0.000	0.000	0.000	0.000
20	A	54	VAL	0	0.017	0.000	14.381	0.937	0.937	0.000	0.000	0.000	0.000
21	A	55	GLU	-1	-0.804	-0.898	11.660	-41.957	-41.957	0.000	0.000	0.000	0.000
22	A	56	ASN	0	0.011	0.000	10.415	-0.870	-0.870	0.000	0.000	0.000	0.000
23	A	57	HIS	0	0.008	0.000	11.416	1.528	1.528	0.000	0.000	0.000	0.000
24	A	58	VAL	0	0.014	-0.007	9.500	-4.320	-4.320	0.000	0.000	0.000	0.000
25	A	59	ASN	0	-0.041	-0.022	9.896	0.280	0.280	0.000	0.000	0.000	0.000
26	A	60	CYS	0	-0.038	0.000	12.591	2.313	2.313	0.000	0.000	0.000	0.000
27	A	61	ALA	0	0.014	0.006	15.970	-0.471	-0.471	0.000	0.000	0.000	0.000
28	A	62	ASP	-1	-0.904	-0.939	18.063	-26.683	-26.683	0.000	0.000	0.000	0.000
29	A	63	PRO	0	-0.067	-0.043	19.014	-1.726	-1.726	0.000	0.000	0.000	0.000
30	A	64	ILE	0	0.006	0.000	16.409	1.627	1.627	0.000	0.000	0.000	0.000
31	A	65	THR	0	-0.002	-0.005	19.089	-0.756	-0.756	0.000	0.000	0.000	0.000
32	A	66	LEU	0	-0.037	-0.010	20.187	0.576	0.576	0.000	0.000	0.000	0.000
33	A	67	SER	0	0.066	0.023	22.459	-0.113	-0.113	0.000	0.000	0.000	0.000
34	A	68	GLU	-1	-0.898	-0.908	25.454	-21.151	-21.151	0.000	0.000	0.000	0.000
35	A	69	GLY	0	0.041	0.020	25.214	-0.943	-0.943	0.000	0.000	0.000	0.000
36	A	70	SER	0	-0.033	-0.039	26.377	0.887	0.887	0.000	0.000	0.000	0.000
37	A	71	ILE	0	0.046	0.008	26.194	-0.621	-0.621	0.000	0.000	0.000	0.000
38	A	72	LYS	1	0.895	0.945	27.079	18.038	18.038	0.000	0.000	0.000	0.000
39	A	73	ASN	0	0.032	0.041	23.826	0.290	0.290	0.000	0.000	0.000	0.000
40	A	74	LYS	1	0.940	0.982	19.232	25.302	25.302	0.000	0.000	0.000	0.000
41	A	75	VAL	0	0.034	0.022	16.167	0.329	0.329	0.000	0.000	0.000	0.000
42	A	76	SER	0	-0.028	-0.016	13.634	-0.577	-0.577	0.000	0.000	0.000	0.000
43	A	77	VAL	0	-0.001	0.013	10.999	0.582	0.582	0.000	0.000	0.000	0.000
44	A	78	ARG	1	0.845	0.899	8.455	46.063	46.063	0.000	0.000	0.000	0.000
45	A	79	CYS	0	-0.035	0.005	5.775	1.891	1.891	0.000	0.000	0.000	0.000
46	A	80	SER	0	0.034	0.003	6.858	4.876	4.876	0.000	0.000	0.000	0.000
48	A	82	ASN	0	-0.059	-0.013	7.165	0.941	0.941	0.000	0.000	0.000	0.000
49	A	83	SER	0	0.059	0.022	9.792	5.353	5.353	0.000	0.000	0.000	0.000
50	A	84	ARG	1	0.942	0.973	13.315	30.923	30.923	0.000	0.000	0.000	0.000
51	A	85	ILE	0	-0.009	0.000	12.809	0.921	0.921	0.000	0.000	0.000	0.000
52	A	86	ILE	0	-0.004	-0.005	16.867	0.055	0.055	0.000	0.000	0.000	0.000
53	A	87	VAL	0	-0.016	-0.004	18.742	0.087	0.087	0.000	0.000	0.000	0.000
54	A	88	GLU	-1	-0.864	-0.940	21.504	-22.794	-22.794	0.000	0.000	0.000	0.000
55	A	89	GLN	0	-0.032	-0.005	25.023	1.144	1.144	0.000	0.000	0.000	0.000
56	A	90	LYS	1	0.904	0.969	24.401	20.492	20.492	0.000	0.000	0.000	0.000
57	A	91	VAL	0	0.002	0.004	20.804	0.646	0.646	0.000	0.000	0.000	0.000
58	A	92	ASN	0	0.006	-0.005	23.094	-0.511	-0.511	0.000	0.000	0.000	0.000
59	A	93	SER	0	-0.005	-0.014	18.892	0.043	0.043	0.000	0.000	0.000	0.000
60	A	94	ILE	0	-0.007	-0.005	14.772	0.202	0.202	0.000	0.000	0.000	0.000
61	A	95	PHE	0	0.000	0.015	10.425	-0.963	-0.963	0.000	0.000	0.000	0.000
62	A	96	ILE	0	0.004	-0.005	8.551	0.225	0.225	0.000	0.000	0.000	0.000
63	A	97	GLU	-1	-0.799	-0.899	5.776	-57.686	-57.686	0.000	0.000	0.000	0.000
67	A	101	GLY	0	0.062	0.048	5.432	5.934	5.934	0.000	0.000	0.000	0.000
68	A	102	CYS	0	-0.114	-0.040	7.791	5.781	5.781	0.000	0.000	0.000	0.000
69	A	103	ILE	0	-0.010	-0.010	10.790	1.349	1.349	0.000	0.000	0.000	0.000
70	A	104	PHE	0	0.029	0.001	10.413	1.316	1.316	0.000	0.000	0.000	0.000
71	A	105	LEU	0	-0.031	-0.005	15.790	0.715	0.715	0.000	0.000	0.000	0.000
72	A	106	VAL	0	0.007	-0.005	17.795	0.172	0.172	0.000	0.000	0.000	0.000
73	A	107	ASN	0	-0.014	0.002	20.687	0.681	0.681	0.000	0.000	0.000	0.000
74	A	108	GLY	0	0.055	0.011	22.601	0.200	0.200	0.000	0.000	0.000	0.000
75	A	109	VAL	0	-0.062	-0.026	19.772	-0.202	-0.202	0.000	0.000	0.000	0.000
76	A	110	ILE	0	-0.074	-0.041	23.157	0.897	0.897	0.000	0.000	0.000	0.000
77	A	111	SER	0	-0.017	-0.016	22.467	0.226	0.226	0.000	0.000	0.000	0.000
78	A	112	SER	0	0.023	0.007	17.937	0.280	0.280	0.000	0.000	0.000	0.000
79	A	113	ILE	0	-0.008	-0.001	14.102	0.060	0.060	0.000	0.000	0.000	0.000
80	A	114	GLU	-1	-0.948	-0.978	12.496	-35.026	-35.026	0.000	0.000	0.000	0.000
81	A	115	ILE	0	-0.006	-0.003	7.537	-1.368	-1.368	0.000	0.000	0.000	0.000
82	A	116	VAL	0	0.048	0.018	6.883	0.093	0.093	0.000	0.000	0.000	0.000
87	A	121	ILE	0	-0.042	-0.001	6.847	1.830	1.830	0.000	0.000	0.000	0.000
88	A	122	LYS	1	0.944	0.979	10.037	47.892	47.892	0.000	0.000	0.000	0.000
89	A	123	LEU	0	0.027	0.016	13.859	-0.279	-0.279	0.000	0.000	0.000	0.000
90	A	124	GLN	0	-0.007	0.000	15.531	1.605	1.605	0.000	0.000	0.000	0.000
91	A	125	MET	0	-0.033	0.018	19.358	0.236	0.236	0.000	0.000	0.000	0.000
92	A	126	THR	0	-0.011	-0.017	21.782	0.448	0.448	0.000	0.000	0.000	0.000
93	A	127	GLY	0	0.056	0.036	25.236	0.948	0.948	0.000	0.000	0.000	0.000
94	A	128	ILE	0	-0.032	-0.020	25.254	-0.779	-0.779	0.000	0.000	0.000	0.000
95	A	129	VAL	0	0.039	0.006	19.317	-0.306	-0.306	0.000	0.000	0.000	0.000
96	A	130	PRO	0	-0.043	-0.004	22.778	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	131	THR	0	0.026	0.021	19.046	0.304	0.304	0.000	0.000	0.000	0.000
98	A	132	ILE	0	-0.015	-0.017	14.692	-0.639	-0.639	0.000	0.000	0.000	0.000
99	A	133	SER	0	-0.012	0.006	14.359	0.745	0.745	0.000	0.000	0.000	0.000
100	A	134	LEU	0	0.028	0.018	10.671	-2.239	-2.239	0.000	0.000	0.000	0.000
101	A	135	ASP	-1	-0.703	-0.830	9.537	-44.017	-44.017	0.000	0.000	0.000	0.000
102	A	136	LYS	1	0.768	0.871	6.344	42.462	42.462	0.000	0.000	0.000	0.000
105	A	139	LYS	1	0.850	0.919	7.222	48.456	48.456	0.000	0.000	0.000	0.000
106	A	140	VAL	0	0.000	0.009	8.807	-1.581	-1.581	0.000	0.000	0.000	0.000
107	A	141	ASN	0	0.004	0.020	11.237	1.407	1.407	0.000	0.000	0.000	0.000
108	A	142	ILE	0	0.011	-0.003	14.630	-0.473	-0.473	0.000	0.000	0.000	0.000
109	A	143	TYR	0	-0.009	-0.012	16.618	0.364	0.364	0.000	0.000	0.000	0.000
110	A	144	THR	0	0.004	-0.024	20.206	0.485	0.485	0.000	0.000	0.000	0.000
111	A	145	SER	0	0.045	0.019	22.888	0.616	0.616	0.000	0.000	0.000	0.000
112	A	146	LYS	1	0.821	0.882	25.907	20.312	20.312	0.000	0.000	0.000	0.000
113	A	147	GLU	-1	-0.909	-0.962	28.941	-19.628	-19.628	0.000	0.000	0.000	0.000
114	A	148	GLY	0	-0.005	-0.009	25.261	0.283	0.283	0.000	0.000	0.000	0.000
115	A	149	LYS	1	0.895	0.949	24.479	19.767	19.767	0.000	0.000	0.000	0.000
116	A	150	ASN	0	-0.031	-0.022	25.479	-0.544	-0.544	0.000	0.000	0.000	0.000
117	A	151	VAL	0	0.009	0.021	20.288	0.166	0.166	0.000	0.000	0.000	0.000
118	A	152	GLU	-1	-0.870	-0.915	22.043	-23.408	-23.408	0.000	0.000	0.000	0.000
119	A	153	VAL	0	-0.015	-0.015	16.092	-0.980	-0.980	0.000	0.000	0.000	0.000
120	A	154	TYR	0	-0.067	-0.042	17.126	0.332	0.332	0.000	0.000	0.000	0.000
121	A	155	SER	0	0.008	-0.006	13.830	-1.497	-1.497	0.000	0.000	0.000	0.000
122	A	156	SER	0	-0.010	-0.024	12.322	2.376	2.376	0.000	0.000	0.000	0.000
123	A	157	LYS	1	0.862	0.927	10.609	38.576	38.576	0.000	0.000	0.000	0.000
124	A	158	SER	0	0.047	0.019	9.369	-5.693	-5.693	0.000	0.000	0.000	0.000
125	A	159	SER	0	-0.003	-0.006	9.280	3.321	3.321	0.000	0.000	0.000	0.000
126	A	160	GLU	-1	-0.908	-0.963	10.471	-55.708	-55.708	0.000	0.000	0.000	0.000
127	A	161	MET	0	-0.048	0.000	11.947	-1.483	-1.483	0.000	0.000	0.000	0.000
128	A	162	ASN	0	0.010	-0.006	13.774	3.828	3.828	0.000	0.000	0.000	0.000
129	A	163	LEU	0	0.017	0.015	16.787	-0.843	-0.843	0.000	0.000	0.000	0.000
130	A	164	LEU	0	-0.029	-0.009	18.096	0.757	0.757	0.000	0.000	0.000	0.000
131	A	165	PHE	0	-0.004	-0.004	21.806	0.245	0.245	0.000	0.000	0.000	0.000
132	A	166	PRO	0	0.000	0.022	25.377	0.358	0.358	0.000	0.000	0.000	0.000
133	A	167	GLY	0	0.014	-0.002	27.500	0.751	0.751	0.000	0.000	0.000	0.000
134	A	168	GLU	-1	-0.986	-0.995	30.481	-16.917	-16.917	0.000	0.000	0.000	0.000
135	A	169	GLU	-1	-0.937	-0.952	32.916	-17.578	-17.578	0.000	0.000	0.000	0.000
136	A	170	GLU	-1	-0.978	-0.995	29.602	-21.261	-21.261	0.000	0.000	0.000	0.000
137	A	171	GLY	0	-0.030	-0.021	26.563	-0.021	-0.021	0.000	0.000	0.000	0.000
138	A	172	ASP	-1	-0.874	-0.917	26.374	-21.327	-21.327	0.000	0.000	0.000	0.000
139	A	173	TRP	0	-0.048	-0.042	23.554	-0.504	-0.504	0.000	0.000	0.000	0.000
140	A	174	LYS	1	0.940	0.975	25.509	21.162	21.162	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.880	-0.951	19.191	-32.029	-32.029	0.000	0.000	0.000	0.000
142	A	176	LEU	0	-0.067	-0.043	21.447	1.442	1.442	0.000	0.000	0.000	0.000
143	A	177	ALA	0	0.056	0.039	18.587	-0.936	-0.936	0.000	0.000	0.000	0.000
144	A	178	ILE	0	-0.026	-0.021	16.075	1.577	1.577	0.000	0.000	0.000	0.000
145	A	179	PRO	0	-0.029	-0.006	17.549	-1.131	-1.131	0.000	0.000	0.000	0.000
146	A	180	GLU	-1	-0.812	-0.921	14.493	-40.110	-40.110	0.000	0.000	0.000	0.000
147	A	181	GLN	0	-0.043	-0.011	16.819	0.289	0.289	0.000	0.000	0.000	0.000
148	A	182	PHE	0	0.005	0.000	18.490	0.950	0.950	0.000	0.000	0.000	0.000
149	A	183	VAL	0	-0.002	0.013	22.758	-0.127	-0.127	0.000	0.000	0.000	0.000
150	A	184	THR	0	-0.012	-0.027	25.674	0.082	0.082	0.000	0.000	0.000	0.000
151	A	185	LYS	1	0.926	0.956	27.763	17.686	17.686	0.000	0.000	0.000	0.000
152	A	186	TYR	0	-0.008	0.009	31.454	-0.314	-0.314	0.000	0.000	0.000	0.000
153	A	187	ASN	0	-0.037	-0.030	33.777	0.619	0.619	0.000	0.000	0.000	0.000
154	A	188	GLU	-1	-0.843	-0.950	36.590	-15.291	-15.291	0.000	0.000	0.000	0.000
155	A	189	SER	0	-0.018	-0.034	39.848	0.203	0.203	0.000	0.000	0.000	0.000
156	A	190	LYS	0	-0.008	0.022	37.862	0.292	0.292	0.000	0.000	0.000	0.000
157	A	191	GLY	0	-0.001	0.027	38.231	-0.088	-0.088	0.000	0.000	0.000	0.000
158	A	192	LYS	1	0.831	0.897	33.079	16.239	16.239	0.000	0.000	0.000	0.000
159	A	193	LEU	0	0.005	0.007	27.983	0.178	0.178	0.000	0.000	0.000	0.000
160	A	194	GLU	-1	-0.866	-0.911	30.325	-17.221	-17.221	0.000	0.000	0.000	0.000
161	A	195	SER	0	-0.031	-0.036	25.704	-0.572	-0.572	0.000	0.000	0.000	0.000
162	A	196	MET	0	-0.025	0.011	26.992	0.597	0.597	0.000	0.000	0.000	0.000
163	A	197	VAL	0	0.004	-0.002	23.107	-0.672	-0.672	0.000	0.000	0.000	0.000
164	A	198	SER	-1	-0.934	-0.965	23.269	-22.262	-22.262	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:35:ARG)