FMO DATABASE

FMODB ID: NZR2Q

Calculation Name: 2IKK-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2IKK

Chain ID: A

ChEMBL ID:

UniProt ID: O32152

Base Structure: X-ray

Registration Date: 2025-10-04

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	156
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1553224.446361
FMO2-HF: Nuclear repulsion	1491242.973393
FMO2-HF: Total energy	-61981.472968
FMO2-MP2: Total energy	-62163.584404

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:83:GLY)

Summations of interaction energy for fragment #1(A:83: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.
-165.918	-164.284	4.15	-3.133	-2.65	-0.025

Interaction energy analysis for fragmet #1(A:83:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.820 / q_NPA : 0.892

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	85	GLU	-1	-0.801	-0.873	3.846	-36.281	-35.583	-0.008	-0.257	-0.433	-0.001
4	A	86	ASN	0	-0.054	-0.045	4.899	-5.547	-5.350	-0.001	-0.012	-0.183	0.000
152	A	234	THR	0	-0.087	-0.032	2.435	-16.229	-15.457	4.160	-2.840	-2.092	-0.024
153	A	235	PHE	0	0.048	0.027	4.745	2.691	2.658	-0.001	-0.024	0.058	0.000
5	A	87	LEU	0	0.027	0.020	5.948	4.426	4.426	0.000	0.000	0.000	0.000
6	A	88	TYR	0	0.007	0.001	8.041	-0.508	-0.508	0.000	0.000	0.000	0.000
7	A	89	PHE	0	0.036	0.017	10.680	2.129	2.129	0.000	0.000	0.000	0.000
8	A	90	GLN	0	-0.020	-0.012	13.170	0.447	0.447	0.000	0.000	0.000	0.000
9	A	91	SER	0	0.000	0.012	14.453	1.262	1.262	0.000	0.000	0.000	0.000
10	A	92	ASN	0	-0.026	-0.016	17.231	0.245	0.245	0.000	0.000	0.000	0.000
11	A	93	ALA	0	-0.026	-0.025	20.117	0.400	0.400	0.000	0.000	0.000	0.000
12	A	94	SER	0	0.013	0.005	17.715	-0.805	-0.805	0.000	0.000	0.000	0.000
13	A	95	THR	0	-0.028	-0.009	19.816	0.844	0.844	0.000	0.000	0.000	0.000
14	A	96	GLY	0	0.102	0.049	20.120	-0.798	-0.798	0.000	0.000	0.000	0.000
15	A	97	LYS	1	0.810	0.895	21.409	12.715	12.715	0.000	0.000	0.000	0.000
16	A	98	LYS	1	0.834	0.934	21.714	11.710	11.710	0.000	0.000	0.000	0.000
17	A	99	PRO	0	0.019	-0.007	19.752	0.132	0.132	0.000	0.000	0.000	0.000
18	A	100	LYS	0	-0.015	0.004	13.454	0.432	0.432	0.000	0.000	0.000	0.000
19	A	101	HIS	0	0.028	0.015	19.286	-0.124	-0.124	0.000	0.000	0.000	0.000
20	A	102	HIS	0	-0.004	-0.006	21.472	0.360	0.360	0.000	0.000	0.000	0.000
21	A	103	VAL	0	-0.033	-0.022	24.248	-0.343	-0.343	0.000	0.000	0.000	0.000
22	A	104	LEU	0	-0.053	-0.012	24.228	0.403	0.403	0.000	0.000	0.000	0.000
23	A	105	SER	0	0.007	0.006	27.864	0.227	0.227	0.000	0.000	0.000	0.000
24	A	106	HIS	0	-0.016	-0.020	29.889	-0.280	-0.280	0.000	0.000	0.000	0.000
25	A	107	ASP	-1	-0.873	-0.914	32.507	-8.688	-8.688	0.000	0.000	0.000	0.000
26	A	108	ILE	0	-0.059	-0.024	34.782	-0.142	-0.142	0.000	0.000	0.000	0.000
27	A	109	ILE	0	-0.005	0.000	33.069	0.200	0.200	0.000	0.000	0.000	0.000
28	A	110	PRO	0	0.010	-0.001	37.400	0.004	0.004	0.000	0.000	0.000	0.000
29	A	111	ALA	0	-0.023	0.001	35.381	-0.233	-0.233	0.000	0.000	0.000	0.000
30	A	112	SER	0	0.046	0.021	32.504	0.181	0.181	0.000	0.000	0.000	0.000
31	A	113	LYS	1	0.986	0.980	34.740	7.793	7.793	0.000	0.000	0.000	0.000
32	A	114	PRO	0	0.069	0.040	30.141	0.043	0.043	0.000	0.000	0.000	0.000
33	A	115	ILE	0	0.018	0.007	28.770	-0.205	-0.205	0.000	0.000	0.000	0.000
34	A	116	ALA	0	-0.004	-0.010	32.058	0.003	0.003	0.000	0.000	0.000	0.000
35	A	117	GLU	-1	-0.955	-0.982	33.450	-8.945	-8.945	0.000	0.000	0.000	0.000
36	A	118	LYS	1	0.786	0.872	25.774	11.742	11.742	0.000	0.000	0.000	0.000
37	A	119	LEU	0	-0.029	-0.024	30.719	-0.108	-0.108	0.000	0.000	0.000	0.000
38	A	120	GLN	0	-0.039	-0.008	33.316	0.376	0.376	0.000	0.000	0.000	0.000
39	A	121	ILE	0	-0.040	0.000	35.871	0.228	0.228	0.000	0.000	0.000	0.000
40	A	122	GLN	0	0.004	0.000	38.712	0.059	0.059	0.000	0.000	0.000	0.000
41	A	123	PRO	0	0.007	-0.001	39.775	-0.172	-0.172	0.000	0.000	0.000	0.000
42	A	124	GLU	-1	-0.937	-0.965	39.717	-7.634	-7.634	0.000	0.000	0.000	0.000
43	A	125	SER	0	-0.014	-0.019	38.672	0.116	0.116	0.000	0.000	0.000	0.000
44	A	126	PRO	0	0.001	0.016	38.511	-0.210	-0.210	0.000	0.000	0.000	0.000
45	A	127	VAL	0	-0.001	-0.014	33.703	-0.095	-0.095	0.000	0.000	0.000	0.000
46	A	128	VAL	0	-0.005	-0.001	32.537	0.072	0.072	0.000	0.000	0.000	0.000
47	A	129	GLU	-1	-0.847	-0.923	29.492	-10.614	-10.614	0.000	0.000	0.000	0.000
48	A	130	LEU	0	-0.022	-0.013	26.633	0.131	0.131	0.000	0.000	0.000	0.000
49	A	131	LYS	1	0.846	0.921	25.843	10.549	10.549	0.000	0.000	0.000	0.000
50	A	132	ARG	1	0.778	0.852	22.730	13.232	13.232	0.000	0.000	0.000	0.000
51	A	133	ILE	0	0.019	0.022	19.010	-0.272	-0.272	0.000	0.000	0.000	0.000
52	A	134	LEU	0	-0.029	-0.014	15.098	0.594	0.594	0.000	0.000	0.000	0.000
53	A	135	TYR	0	0.004	-0.008	16.205	-0.749	-0.749	0.000	0.000	0.000	0.000
54	A	136	ASN	0	-0.047	-0.030	10.784	0.537	0.537	0.000	0.000	0.000	0.000
55	A	137	ASP	-1	-0.843	-0.917	13.938	-20.523	-20.523	0.000	0.000	0.000	0.000
56	A	138	ASP	-1	-0.954	-0.981	16.493	-14.438	-14.438	0.000	0.000	0.000	0.000
57	A	139	GLN	0	-0.002	0.006	11.133	-0.307	-0.307	0.000	0.000	0.000	0.000
58	A	140	PRO	0	-0.026	-0.004	15.591	-0.596	-0.596	0.000	0.000	0.000	0.000
59	A	141	LEU	0	0.008	0.012	10.287	-1.130	-1.130	0.000	0.000	0.000	0.000
60	A	142	THR	0	-0.098	-0.066	13.176	-0.779	-0.779	0.000	0.000	0.000	0.000
61	A	143	PHE	0	0.024	0.029	15.785	0.777	0.777	0.000	0.000	0.000	0.000
62	A	144	GLU	-1	-0.782	-0.864	19.230	-14.128	-14.128	0.000	0.000	0.000	0.000
63	A	145	VAL	0	0.017	0.016	21.344	0.558	0.558	0.000	0.000	0.000	0.000
64	A	146	THR	0	-0.030	-0.023	24.019	-0.304	-0.304	0.000	0.000	0.000	0.000
65	A	147	HIS	0	-0.021	-0.021	26.321	0.184	0.184	0.000	0.000	0.000	0.000
66	A	148	TYR	0	0.018	-0.010	27.176	-0.152	-0.152	0.000	0.000	0.000	0.000
67	A	149	PRO	0	0.046	0.032	32.341	0.183	0.183	0.000	0.000	0.000	0.000
68	A	150	LEU	0	0.008	-0.002	35.808	0.070	0.070	0.000	0.000	0.000	0.000
69	A	151	ASP	-1	-0.924	-0.967	38.694	-7.423	-7.423	0.000	0.000	0.000	0.000
70	A	152	LEU	0	-0.067	-0.025	35.848	0.105	0.105	0.000	0.000	0.000	0.000
71	A	153	PHE	0	-0.069	-0.036	34.089	-0.024	-0.024	0.000	0.000	0.000	0.000
72	A	154	PRO	0	0.051	0.031	37.578	-0.080	-0.080	0.000	0.000	0.000	0.000
73	A	155	GLY	0	0.051	0.031	39.902	0.035	0.035	0.000	0.000	0.000	0.000
74	A	156	ILE	0	-0.027	0.010	32.415	-0.076	-0.076	0.000	0.000	0.000	0.000
75	A	157	ASP	-1	-0.811	-0.934	34.714	-8.478	-8.478	0.000	0.000	0.000	0.000
76	A	158	THR	0	-0.079	-0.052	35.745	-0.053	-0.053	0.000	0.000	0.000	0.000
77	A	159	PHE	0	-0.036	-0.021	34.521	0.046	0.046	0.000	0.000	0.000	0.000
78	A	160	ILE	0	-0.040	-0.007	30.243	-0.350	-0.350	0.000	0.000	0.000	0.000
79	A	161	ALA	0	0.026	0.008	31.388	0.180	0.180	0.000	0.000	0.000	0.000
80	A	162	ASP	-1	-0.751	-0.892	27.426	-11.784	-11.784	0.000	0.000	0.000	0.000
81	A	163	GLY	0	-0.024	0.001	25.751	0.149	0.149	0.000	0.000	0.000	0.000
82	A	164	VAL	0	-0.032	0.002	26.841	-0.043	-0.043	0.000	0.000	0.000	0.000
83	A	165	SER	0	-0.046	-0.022	26.036	-0.536	-0.536	0.000	0.000	0.000	0.000
84	A	166	MET	0	0.072	0.022	26.663	0.378	0.378	0.000	0.000	0.000	0.000
85	A	167	HIS	0	0.028	0.026	23.446	0.324	0.324	0.000	0.000	0.000	0.000
86	A	168	ASP	-1	-0.870	-0.926	28.176	-10.547	-10.547	0.000	0.000	0.000	0.000
87	A	169	ILE	0	-0.022	0.001	30.639	0.400	0.400	0.000	0.000	0.000	0.000
88	A	170	LEU	0	0.012	0.012	28.968	0.304	0.304	0.000	0.000	0.000	0.000
89	A	171	LYS	1	0.975	1.001	31.055	10.107	10.107	0.000	0.000	0.000	0.000
90	A	172	GLN	0	-0.046	-0.039	33.496	0.153	0.153	0.000	0.000	0.000	0.000
91	A	173	GLN	0	-0.012	0.009	35.827	0.464	0.464	0.000	0.000	0.000	0.000
92	A	174	TYR	0	-0.002	-0.025	35.339	0.109	0.109	0.000	0.000	0.000	0.000
93	A	175	LYS	1	0.800	0.906	36.772	8.121	8.121	0.000	0.000	0.000	0.000
94	A	176	VAL	0	0.023	0.020	32.146	0.014	0.014	0.000	0.000	0.000	0.000
95	A	177	VAL	0	-0.028	-0.025	29.447	-0.214	-0.214	0.000	0.000	0.000	0.000
96	A	178	PRO	0	0.001	0.005	26.346	0.208	0.208	0.000	0.000	0.000	0.000
97	A	179	THR	0	-0.051	-0.037	28.045	-0.043	-0.043	0.000	0.000	0.000	0.000
98	A	180	HIS	0	-0.034	-0.003	25.724	-0.400	-0.400	0.000	0.000	0.000	0.000
99	A	181	ASN	0	-0.004	-0.014	21.246	-0.377	-0.377	0.000	0.000	0.000	0.000
100	A	182	THR	0	0.009	0.027	23.284	-0.474	-0.474	0.000	0.000	0.000	0.000
101	A	183	LYS	1	0.894	0.919	17.172	15.783	15.783	0.000	0.000	0.000	0.000
102	A	184	LEU	0	-0.006	0.013	20.034	-0.108	-0.108	0.000	0.000	0.000	0.000
103	A	185	LEU	0	-0.022	-0.008	12.296	-0.297	-0.297	0.000	0.000	0.000	0.000
104	A	186	ASN	0	-0.030	-0.008	16.830	0.309	0.309	0.000	0.000	0.000	0.000
105	A	187	VAL	0	-0.010	-0.011	13.979	-1.247	-1.247	0.000	0.000	0.000	0.000
106	A	188	VAL	0	-0.003	0.010	16.676	1.003	1.003	0.000	0.000	0.000	0.000
107	A	189	TYR	0	-0.028	-0.022	17.982	-0.685	-0.685	0.000	0.000	0.000	0.000
108	A	190	ALA	0	0.010	0.018	19.260	0.620	0.620	0.000	0.000	0.000	0.000
109	A	191	GLN	0	0.018	0.005	21.059	0.842	0.842	0.000	0.000	0.000	0.000
110	A	192	GLN	0	0.007	0.009	24.242	-0.206	-0.206	0.000	0.000	0.000	0.000
111	A	193	GLU	-1	-0.843	-0.908	25.367	-11.365	-11.365	0.000	0.000	0.000	0.000
112	A	194	GLU	-1	-0.804	-0.915	20.320	-13.251	-13.251	0.000	0.000	0.000	0.000
113	A	195	SER	0	-0.011	-0.027	20.835	-0.428	-0.428	0.000	0.000	0.000	0.000
114	A	196	LYS	1	0.905	0.957	21.861	10.980	10.980	0.000	0.000	0.000	0.000
115	A	197	TYR	0	-0.032	-0.029	22.144	0.126	0.126	0.000	0.000	0.000	0.000
116	A	198	LEU	0	0.007	-0.009	16.168	-0.550	-0.550	0.000	0.000	0.000	0.000
117	A	199	ASP	-1	-0.951	-0.950	17.421	-17.078	-17.078	0.000	0.000	0.000	0.000
118	A	200	CYS	0	-0.072	-0.008	17.209	-1.097	-1.097	0.000	0.000	0.000	0.000
119	A	201	ASP	-1	-0.864	-0.918	18.962	-13.650	-13.650	0.000	0.000	0.000	0.000
120	A	202	ILE	0	-0.072	-0.053	20.811	-0.201	-0.201	0.000	0.000	0.000	0.000
121	A	203	GLY	0	-0.025	-0.017	22.037	0.217	0.217	0.000	0.000	0.000	0.000
122	A	204	ASP	-1	-0.793	-0.885	16.748	-17.935	-17.935	0.000	0.000	0.000	0.000
123	A	205	ALA	0	-0.020	-0.010	14.557	0.369	0.369	0.000	0.000	0.000	0.000
124	A	206	LEU	0	0.000	0.010	14.244	-1.540	-1.540	0.000	0.000	0.000	0.000
125	A	207	PHE	0	-0.005	-0.005	8.403	0.644	0.644	0.000	0.000	0.000	0.000
126	A	208	GLU	-1	-0.873	-0.952	13.949	-13.897	-13.897	0.000	0.000	0.000	0.000
127	A	209	ILE	0	-0.050	-0.027	14.745	-0.421	-0.421	0.000	0.000	0.000	0.000
128	A	210	ASP	-1	-0.799	-0.863	17.864	-12.020	-12.020	0.000	0.000	0.000	0.000
129	A	211	LYS	1	0.896	0.941	20.201	13.696	13.696	0.000	0.000	0.000	0.000
130	A	212	THR	0	0.038	0.016	22.257	0.540	0.540	0.000	0.000	0.000	0.000
131	A	213	ALA	0	-0.038	-0.018	25.219	-0.279	-0.279	0.000	0.000	0.000	0.000
132	A	214	PHE	0	0.050	0.018	26.662	0.264	0.264	0.000	0.000	0.000	0.000
133	A	215	THR	0	0.002	-0.009	29.439	-0.126	-0.126	0.000	0.000	0.000	0.000
134	A	216	SER	0	0.018	-0.010	32.242	-0.040	-0.040	0.000	0.000	0.000	0.000
135	A	217	ASN	0	-0.061	-0.045	35.317	0.085	0.085	0.000	0.000	0.000	0.000
136	A	218	ASP	-1	-0.866	-0.907	32.016	-9.590	-9.590	0.000	0.000	0.000	0.000
137	A	219	GLN	0	-0.003	0.010	34.201	0.171	0.171	0.000	0.000	0.000	0.000
138	A	220	PRO	0	0.005	0.012	31.215	-0.270	-0.270	0.000	0.000	0.000	0.000
139	A	221	ILE	0	-0.058	-0.032	29.147	0.297	0.297	0.000	0.000	0.000	0.000
140	A	222	TYR	0	0.015	-0.013	24.202	-0.128	-0.128	0.000	0.000	0.000	0.000
141	A	223	CYS	0	-0.073	-0.014	26.237	-0.205	-0.205	0.000	0.000	0.000	0.000
142	A	224	SER	0	0.022	-0.018	22.339	0.243	0.243	0.000	0.000	0.000	0.000
143	A	225	LEU	0	0.015	0.024	21.655	-0.186	-0.186	0.000	0.000	0.000	0.000
144	A	226	PHE	0	-0.057	-0.025	16.976	0.183	0.183	0.000	0.000	0.000	0.000
145	A	227	LEU	0	0.033	0.018	16.875	-0.469	-0.469	0.000	0.000	0.000	0.000
146	A	228	MET	0	0.028	0.004	11.623	0.357	0.357	0.000	0.000	0.000	0.000
147	A	229	HIS	0	0.027	-0.007	12.480	-1.628	-1.628	0.000	0.000	0.000	0.000
148	A	230	THR	0	-0.025	-0.033	10.101	-2.353	-2.353	0.000	0.000	0.000	0.000
149	A	231	ASN	0	-0.061	-0.030	8.174	-3.685	-3.685	0.000	0.000	0.000	0.000
150	A	232	ARG	1	0.788	0.879	7.721	18.876	18.876	0.000	0.000	0.000	0.000
151	A	233	VAL	0	0.016	0.018	6.301	-0.300	-0.300	0.000	0.000	0.000	0.000
154	A	236	THR	0	-0.033	-0.019	6.721	-2.228	-2.228	0.000	0.000	0.000	0.000
155	A	237	ILE	0	-0.008	-0.014	8.967	2.342	2.342	0.000	0.000	0.000	0.000
156	A	238	ASN	-1	-0.928	-0.953	11.932	-21.313	-21.313	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:83:GLY)