FMO DATABASE

FMODB ID: 372GL

Calculation Name: 3BRT-B-Xray540

Preferred Name: Inhibitor of nuclear factor kappa B kinase alpha subunit

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3BRT

Chain ID: B

ChEMBL ID: CHEMBL3476

UniProt ID: O15111

Base Structure: X-ray

Registration Date: 2025-07-11

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-282216.845195
FMO2-HF: Nuclear repulsion	255416.9521
FMO2-HF: Total energy	-26799.893095
FMO2-MP2: Total energy	-26875.425115

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(B:49:GLU)

Summations of interaction energy for fragment #1(B:49:GLU)

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.
0.186	1.723	0.138	0.04	-1.716	0

Interaction energy analysis for fragmet #1(B:49:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.125 / q_NPA : 0.003

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].
4	B	50	THR	0	-0.032	0.040	4.255	0.953	1.240	0.000	-0.131	-0.157	0.000
5	B	51	LEU	0	0.156	-0.065	3.742	-0.031	1.288	0.000	-0.684	-0.635	0.003
6	B	51	LEU	0	-0.063	0.123	4.901	-0.052	-0.008	-0.001	-0.007	-0.036	0.000
7	B	52	GLN	0	0.080	-0.092	3.874	1.600	1.727	-0.002	-0.011	-0.114	0.000
8	B	52	GLN	0	-0.010	0.102	3.372	-3.017	-3.459	0.144	0.924	-0.626	-0.003
9	B	53	ARG	0	0.111	-0.064	4.465	0.810	0.936	-0.002	-0.027	-0.097	0.000
10	B	53	ARG	1	0.863	1.059	4.324	-1.387	-1.311	-0.001	-0.024	-0.051	0.000
11	B	54	CYS	0	0.073	-0.157	5.901	0.522	0.522	0.000	0.000	0.000	0.000
12	B	54	CYS	0	-0.125	0.107	7.838	0.155	0.155	0.000	0.000	0.000	0.000
13	B	55	LEU	0	0.107	-0.070	8.536	0.404	0.404	0.000	0.000	0.000	0.000
14	B	55	LEU	0	-0.093	0.108	8.072	-0.007	-0.007	0.000	0.000	0.000	0.000
15	B	56	GLU	0	0.061	-0.092	8.893	0.163	0.163	0.000	0.000	0.000	0.000
16	B	56	GLU	-1	-0.969	-0.875	8.571	-0.974	-0.974	0.000	0.000	0.000	0.000
17	B	57	GLU	0	0.120	-0.107	10.291	0.107	0.107	0.000	0.000	0.000	0.000
18	B	57	GLU	-1	-0.989	-0.829	11.006	0.069	0.069	0.000	0.000	0.000	0.000
19	B	58	ASN	0	0.083	-0.098	12.271	0.122	0.122	0.000	0.000	0.000	0.000
20	B	58	ASN	0	-0.108	0.084	13.256	-0.045	-0.045	0.000	0.000	0.000	0.000
21	B	59	GLN	0	0.057	-0.113	13.799	0.084	0.084	0.000	0.000	0.000	0.000
22	B	59	GLN	0	-0.063	0.118	14.412	0.041	0.041	0.000	0.000	0.000	0.000
23	B	60	GLU	0	0.076	-0.106	14.662	0.024	0.024	0.000	0.000	0.000	0.000
24	B	60	GLU	-1	-0.974	-0.850	13.807	-0.050	-0.050	0.000	0.000	0.000	0.000
25	B	61	LEU	0	0.063	-0.116	16.296	0.050	0.050	0.000	0.000	0.000	0.000
26	B	61	LEU	0	-0.090	0.112	15.814	0.000	0.000	0.000	0.000	0.000	0.000
27	B	62	ARG	0	0.032	-0.101	17.984	0.041	0.041	0.000	0.000	0.000	0.000
28	B	62	ARG	1	0.772	1.005	17.498	0.438	0.438	0.000	0.000	0.000	0.000
29	B	63	ASP	0	0.037	-0.160	19.318	0.012	0.012	0.000	0.000	0.000	0.000
30	B	63	ASP	-1	-0.919	-0.809	18.653	-0.304	-0.304	0.000	0.000	0.000	0.000
31	B	64	ALA	0	0.074	-0.094	20.599	0.016	0.016	0.000	0.000	0.000	0.000
32	B	64	ALA	0	-0.055	0.113	21.031	0.006	0.006	0.000	0.000	0.000	0.000
33	B	65	ILE	0	0.021	-0.129	22.394	0.023	0.023	0.000	0.000	0.000	0.000
34	B	65	ILE	0	-0.079	0.121	23.055	-0.002	-0.002	0.000	0.000	0.000	0.000
35	B	66	ARG	0	0.069	-0.106	23.982	0.014	0.014	0.000	0.000	0.000	0.000
36	B	66	ARG	1	0.861	1.056	20.217	0.312	0.312	0.000	0.000	0.000	0.000
37	B	67	GLN	0	0.075	-0.078	25.346	0.004	0.004	0.000	0.000	0.000	0.000
38	B	67	GLN	0	-0.069	0.111	25.628	0.009	0.009	0.000	0.000	0.000	0.000
39	B	68	SER	0	0.142	-0.077	26.669	0.007	0.007	0.000	0.000	0.000	0.000
40	B	68	SER	0	-0.057	0.089	27.199	0.004	0.004	0.000	0.000	0.000	0.000
41	B	69	ASN	0	0.078	-0.091	28.285	0.012	0.012	0.000	0.000	0.000	0.000
42	B	69	ASN	0	-0.146	0.060	28.253	0.010	0.010	0.000	0.000	0.000	0.000
43	B	70	GLN	0	0.097	-0.101	29.846	0.006	0.006	0.000	0.000	0.000	0.000
44	B	70	GLN	0	-0.089	0.125	30.623	-0.012	-0.012	0.000	0.000	0.000	0.000
45	B	71	ILE	0	0.034	-0.105	31.333	0.002	0.002	0.000	0.000	0.000	0.000
46	B	71	ILE	0	-0.065	0.095	29.915	0.002	0.002	0.000	0.000	0.000	0.000
47	B	72	LEU	0	0.091	-0.086	32.699	0.007	0.007	0.000	0.000	0.000	0.000
48	B	72	LEU	0	-0.052	0.105	31.687	0.000	0.000	0.000	0.000	0.000	0.000
49	B	73	ARG	0	0.114	-0.009	34.223	0.005	0.005	0.000	0.000	0.000	0.000
50	B	73	ARG	1	0.844	1.030	31.922	0.106	0.106	0.000	0.000	0.000	0.000
51	B	74	GLU	0	0.075	-0.117	35.907	0.002	0.002	0.000	0.000	0.000	0.000
52	B	74	GLU	-1	-0.914	-0.848	36.535	-0.056	-0.056	0.000	0.000	0.000	0.000
53	B	75	ARG	0	0.029	-0.122	37.088	0.003	0.003	0.000	0.000	0.000	0.000
54	B	75	ARG	1	0.684	0.962	36.344	0.040	0.040	0.000	0.000	0.000	0.000
55	B	76	CYS	0	0.116	-0.179	38.547	0.006	0.006	0.000	0.000	0.000	0.000
56	B	76	CYS	0	-0.094	0.112	37.804	0.001	0.001	0.000	0.000	0.000	0.000
57	B	77	GLU	0	0.099	-0.078	40.398	0.004	0.004	0.000	0.000	0.000	0.000
58	B	77	GLU	-1	-1.005	-0.808	41.224	-0.062	-0.062	0.000	0.000	0.000	0.000
59	B	78	GLU	0	0.106	-0.104	41.807	0.001	0.001	0.000	0.000	0.000	0.000
60	B	78	GLU	-1	-0.938	-0.782	41.480	-0.031	-0.031	0.000	0.000	0.000	0.000
61	B	79	LEU	0	0.092	-0.179	42.864	0.003	0.003	0.000	0.000	0.000	0.000
62	B	79	LEU	0	-0.139	0.157	41.705	0.001	0.001	0.000	0.000	0.000	0.000
63	B	80	LEU	0	0.123	-0.116	44.534	0.004	0.004	0.000	0.000	0.000	0.000
64	B	80	LEU	0	-0.138	0.110	44.766	0.000	0.000	0.000	0.000	0.000	0.000
65	B	81	HIS	0	0.048	-0.128	46.426	0.002	0.002	0.000	0.000	0.000	0.000
66	B	81	HIS	0	-0.155	0.069	45.605	-0.001	-0.001	0.000	0.000	0.000	0.000
67	B	82	PHE	0	0.152	-0.064	47.614	0.001	0.001	0.000	0.000	0.000	0.000
68	B	82	PHE	0	-0.084	0.095	47.625	0.001	0.001	0.000	0.000	0.000	0.000
69	B	83	GLN	0	0.081	-0.151	48.748	0.003	0.003	0.000	0.000	0.000	0.000
70	B	83	GLN	0	-0.098	0.102	47.151	-0.001	-0.001	0.000	0.000	0.000	0.000
71	B	84	ALA	0	0.043	-0.086	50.532	0.003	0.003	0.000	0.000	0.000	0.000
72	B	84	ALA	0	-0.041	0.121	51.916	-0.001	-0.001	0.000	0.000	0.000	0.000
73	B	85	SER	0	0.145	-0.125	52.349	0.001	0.001	0.000	0.000	0.000	0.000
74	B	85	SER	0	0.009	0.125	52.739	0.000	0.000	0.000	0.000	0.000	0.000
75	B	86	GLN	0	-0.006	-0.076	53.122	0.001	0.001	0.000	0.000	0.000	0.000
76	B	86	GLN	0	-0.143	0.084	52.167	0.000	0.000	0.000	0.000	0.000	0.000
77	B	87	ARG	0	0.060	-0.107	54.753	0.002	0.002	0.000	0.000	0.000	0.000
78	B	87	ARG	1	0.848	1.057	55.522	0.021	0.021	0.000	0.000	0.000	0.000
79	B	88	GLU	0	0.095	-0.120	56.754	0.002	0.002	0.000	0.000	0.000	0.000
80	B	88	GLU	-1	-1.005	-0.829	56.118	-0.026	-0.026	0.000	0.000	0.000	0.000
81	B	89	GLU	0	0.132	-0.119	57.965	0.000	0.000	0.000	0.000	0.000	0.000
82	B	89	GLU	-1	-1.009	-0.828	57.932	-0.011	-0.011	0.000	0.000	0.000	0.000
83	B	90	LYS	0	0.125	-0.105	58.955	0.001	0.001	0.000	0.000	0.000	0.000
84	B	90	LYS	1	0.831	1.071	58.846	0.008	0.008	0.000	0.000	0.000	0.000
85	B	91	GLU	0	-0.009	-0.158	60.704	0.002	0.002	0.000	0.000	0.000	0.000
86	B	91	GLU	-1	-0.979	-0.823	60.427	-0.020	-0.020	0.000	0.000	0.000	0.000
87	B	92	PHE	0	0.081	-0.105	62.434	0.001	0.001	0.000	0.000	0.000	0.000
88	B	92	PHE	0	-0.085	0.126	62.776	0.000	0.000	0.000	0.000	0.000	0.000
89	B	93	LEU	0	0.119	-0.130	63.377	0.000	0.000	0.000	0.000	0.000	0.000
90	B	93	LEU	0	-0.088	0.123	61.700	0.000	0.000	0.000	0.000	0.000	0.000
91	B	94	MET	0	0.082	-0.131	64.658	0.001	0.001	0.000	0.000	0.000	0.000
92	B	94	MET	0	-0.123	0.098	62.258	0.000	0.000	0.000	0.000	0.000	0.000
93	B	95	CYS	0	0.140	-0.112	66.535	0.001	0.001	0.000	0.000	0.000	0.000
94	B	95	CYS	0	-0.141	0.123	67.786	0.000	0.000	0.000	0.000	0.000	0.000
95	B	96	LYS	0	0.055	-0.163	68.249	0.000	0.000	0.000	0.000	0.000	0.000
96	B	96	LYS	1	0.905	1.103	67.830	0.012	0.012	0.000	0.000	0.000	0.000
97	B	97	PHE	0	0.069	-0.059	68.979	0.000	0.000	0.000	0.000	0.000	0.000
98	B	97	PHE	0	-0.138	0.114	66.152	0.000	0.000	0.000	0.000	0.000	0.000
99	B	98	GLN	0	0.052	-0.118	70.540	0.001	0.001	0.000	0.000	0.000	0.000
100	B	98	GLN	0	-0.081	0.073	69.483	0.000	0.000	0.000	0.000	0.000	0.000
101	B	99	GLU	0	0.067	-0.128	72.572	0.000	0.000	0.000	0.000	0.000	0.000
102	B	99	GLU	-1	-0.981	-0.856	72.550	-0.011	-0.011	0.000	0.000	0.000	0.000
103	B	100	ALA	0	0.085	-0.104	73.581	0.000	0.000	0.000	0.000	0.000	0.000
104	B	100	ALA	0	-0.075	0.119	73.494	0.000	0.000	0.000	0.000	0.000	0.000
105	B	101	ARG	0	0.077	-0.101	74.602	0.001	0.001	0.000	0.000	0.000	0.000
106	B	101	ARG	1	0.834	1.065	73.730	0.003	0.003	0.000	0.000	0.000	0.000
107	B	102	LYS	0	0.138	-0.046	76.358	0.001	0.001	0.000	0.000	0.000	0.000
108	B	102	LYS	1	0.846	1.038	76.039	0.008	0.008	0.000	0.000	0.000	0.000
109	B	103	LEU	0	0.068	-0.102	78.246	0.000	0.000	0.000	0.000	0.000	0.000
110	B	103	LEU	0	-0.121	0.099	78.390	0.000	0.000	0.000	0.000	0.000	0.000
111	B	104	VAL	0	0.108	-0.118	79.153	0.000	0.000	0.000	0.000	0.000	0.000
112	B	104	VAL	0	-0.104	0.112	78.277	0.000	0.000	0.000	0.000	0.000	0.000
113	B	105	GLU	0	0.061	-0.097	80.504	0.001	0.001	0.000	0.000	0.000	0.000
114	B	105	GLU	-1	-0.942	-0.884	79.071	-0.004	-0.004	0.000	0.000	0.000	0.000
115	B	106	ARG	0	0.020	-0.123	82.451	0.000	0.000	0.000	0.000	0.000	0.000
116	B	106	ARG	1	0.844	1.062	81.660	0.007	0.007	0.000	0.000	0.000	0.000
117	B	107	LEU	0	0.014	-0.103	84.094	0.000	0.000	0.000	0.000	0.000	0.000
118	B	107	LEU	0	-0.093	0.093	82.839	0.000	0.000	0.000	0.000	0.000	0.000
119	B	108	GLY	0	0.009	-0.097	85.409	0.000	0.000	0.000	0.000	0.000	0.000
120	B	109	LEU	0	-0.068	-0.022	87.265	0.001	0.001	0.000	0.000	0.000	0.000
121	B	109	LEU	0	0.011	0.019	87.107	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(B:49:GLU)