FMO DATABASE

FMODB ID: 1N23Z

Calculation Name: 2IHC-A-Xray372

Preferred Name: Transcription regulator protein BACH1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2IHC

Chain ID: A

ChEMBL ID: CHEMBL4295651

UniProt ID: O14867

Base Structure: X-ray

Registration Date: 2023-09-20

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

DOI:

IFIE MAP

IFIE Diagram

Modeling method

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-965686.106668
FMO2-HF: Nuclear repulsion	917842.292278
FMO2-HF: Total energy	-47843.81439
FMO2-MP2: Total energy	-47982.249081

3D Structure

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:7:SER)

Summations of interaction energy for fragment #1(A:7:SER)

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.
-0.273	2.486	-0.031	-1.452	-1.277	0.005

Interaction energy analysis for fragmet #1(A:7:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.002

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	9	PHE	0	0.002	0.011	3.791	0.057	2.816	-0.031	-1.452	-1.277	0.005
4	A	10	ALA	0	0.018	0.009	6.729	-0.493	-0.493	0.000	0.000	0.000	0.000
5	A	11	TYR	0	-0.027	-0.010	10.054	0.126	0.126	0.000	0.000	0.000	0.000
6	A	12	GLU	-1	-0.904	-0.957	13.155	0.034	0.034	0.000	0.000	0.000	0.000
7	A	13	SER	0	-0.049	-0.017	16.559	0.020	0.020	0.000	0.000	0.000	0.000
8	A	14	SER	0	0.039	0.008	19.633	-0.007	-0.007	0.000	0.000	0.000	0.000
9	A	15	VAL	0	0.019	0.005	22.591	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	16	HIS	0	0.018	0.015	22.107	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	17	SER	0	0.048	0.009	24.136	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	18	THR	0	0.004	-0.002	26.616	0.000	0.000	0.000	0.000	0.000	0.000
13	A	19	ASN	0	0.008	0.007	25.272	0.007	0.007	0.000	0.000	0.000	0.000
14	A	20	VAL	0	-0.001	0.010	26.503	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	21	LEU	0	0.027	0.022	29.412	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	22	LEU	0	0.042	0.031	32.021	0.002	0.002	0.000	0.000	0.000	0.000
17	A	23	SER	0	-0.040	-0.032	31.077	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	24	LEU	0	-0.010	0.003	32.079	0.001	0.001	0.000	0.000	0.000	0.000
19	A	25	ASN	0	0.084	0.042	35.232	0.003	0.003	0.000	0.000	0.000	0.000
20	A	26	ASP	-1	-0.848	-0.914	36.930	-0.052	-0.052	0.000	0.000	0.000	0.000
21	A	27	GLN	0	-0.044	-0.022	33.824	0.002	0.002	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.913	0.945	38.989	0.037	0.037	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.809	0.902	40.199	0.045	0.045	0.000	0.000	0.000	0.000
24	A	30	LYS	1	0.819	0.898	38.129	0.064	0.064	0.000	0.000	0.000	0.000
25	A	31	ASP	-1	-0.813	-0.878	43.535	-0.045	-0.045	0.000	0.000	0.000	0.000
26	A	32	VAL	0	-0.024	-0.008	39.117	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	33	LEU	0	-0.050	-0.045	35.636	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	34	CYS	0	-0.028	0.021	38.898	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	35	ASP	-1	-0.804	-0.884	39.420	-0.056	-0.056	0.000	0.000	0.000	0.000
30	A	36	VAL	0	0.023	0.028	42.634	0.002	0.002	0.000	0.000	0.000	0.000
31	A	37	THR	0	-0.032	-0.018	44.910	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	38	ILE	0	-0.017	-0.004	45.508	0.001	0.001	0.000	0.000	0.000	0.000
33	A	39	PHE	0	-0.021	-0.021	49.174	0.000	0.000	0.000	0.000	0.000	0.000
34	A	40	VAL	0	0.052	0.023	50.722	0.001	0.001	0.000	0.000	0.000	0.000
35	A	41	GLU	-1	-0.774	-0.875	53.848	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	42	GLY	0	-0.030	-0.009	57.136	0.000	0.000	0.000	0.000	0.000	0.000
37	A	43	GLN	0	-0.080	-0.040	54.110	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	44	ARG	1	0.966	0.988	49.865	0.035	0.035	0.000	0.000	0.000	0.000
39	A	45	PHE	0	0.018	0.008	47.236	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	46	ARG	1	0.773	0.880	44.534	0.046	0.046	0.000	0.000	0.000	0.000
41	A	47	ALA	0	0.034	0.007	41.792	0.001	0.001	0.000	0.000	0.000	0.000
42	A	48	HIS	0	0.063	0.051	37.266	0.002	0.002	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.739	0.819	38.765	0.055	0.055	0.000	0.000	0.000	0.000
44	A	50	SER	0	-0.002	-0.010	34.332	0.004	0.004	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.023	0.016	34.642	0.001	0.001	0.000	0.000	0.000	0.000
46	A	52	LEU	0	0.010	0.001	36.555	0.004	0.004	0.000	0.000	0.000	0.000
47	A	53	ALA	0	-0.022	-0.005	37.424	0.003	0.003	0.000	0.000	0.000	0.000
48	A	54	ALA	0	-0.012	-0.003	33.798	0.003	0.003	0.000	0.000	0.000	0.000
49	A	55	CYS	0	-0.043	-0.020	35.680	0.004	0.004	0.000	0.000	0.000	0.000
50	A	56	SER	0	-0.003	-0.012	37.878	0.003	0.003	0.000	0.000	0.000	0.000
51	A	57	SER	0	0.064	0.026	40.660	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	58	TYR	0	-0.007	0.015	42.039	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	59	PHE	0	0.032	-0.012	42.454	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	60	HIS	0	0.031	0.016	37.101	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	61	SER	0	-0.069	-0.048	41.215	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	62	ARG	1	0.872	0.941	44.164	0.020	0.020	0.000	0.000	0.000	0.000
57	A	63	ILE	0	-0.006	0.012	40.354	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	64	VAL	0	-0.030	-0.014	38.548	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	65	GLY	0	-0.007	0.001	40.563	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	66	GLN	0	-0.075	-0.020	43.105	0.001	0.001	0.000	0.000	0.000	0.000
61	A	67	ALA	0	0.056	0.017	40.408	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	68	ASP	-1	-0.863	-0.917	38.473	-0.061	-0.061	0.000	0.000	0.000	0.000
63	A	69	GLY	0	-0.037	-0.014	41.811	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.878	-0.940	44.938	-0.041	-0.041	0.000	0.000	0.000	0.000
65	A	71	LEU	0	-0.025	0.001	43.894	0.002	0.002	0.000	0.000	0.000	0.000
66	A	72	ASN	0	-0.041	-0.042	47.293	0.000	0.000	0.000	0.000	0.000	0.000
67	A	73	ILE	0	0.007	0.004	46.655	0.001	0.001	0.000	0.000	0.000	0.000
68	A	74	THR	0	-0.002	-0.002	50.036	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	75	LEU	0	-0.063	-0.023	48.641	0.000	0.000	0.000	0.000	0.000	0.000
70	A	76	PRO	0	0.013	0.011	52.933	0.000	0.000	0.000	0.000	0.000	0.000
71	A	77	GLU	-1	-0.869	-0.949	55.796	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	78	GLU	-1	-0.902	-0.935	55.306	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.074	-0.033	51.058	0.000	0.000	0.000	0.000	0.000	0.000
74	A	80	THR	0	0.017	-0.008	53.958	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	81	VAL	0	-0.013	-0.032	52.767	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	82	LYS	1	0.783	0.896	51.998	0.008	0.008	0.000	0.000	0.000	0.000
77	A	83	GLY	0	0.026	0.013	51.442	0.001	0.001	0.000	0.000	0.000	0.000
78	A	84	PHE	0	0.025	-0.004	46.393	0.000	0.000	0.000	0.000	0.000	0.000
79	A	85	GLU	-1	-0.858	-0.926	47.261	-0.024	-0.024	0.000	0.000	0.000	0.000
80	A	86	PRO	0	0.006	-0.010	46.313	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	87	LEU	0	0.011	0.017	43.851	0.000	0.000	0.000	0.000	0.000	0.000
82	A	88	ILE	0	-0.033	-0.004	42.486	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	89	GLN	0	-0.033	-0.031	41.678	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	90	PHE	0	-0.021	0.011	37.611	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	91	ALA	0	-0.010	0.004	38.231	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	92	TYR	0	-0.006	-0.036	36.826	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	93	THR	0	-0.092	-0.076	36.466	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	94	ALA	0	-0.027	-0.005	34.378	0.001	0.001	0.000	0.000	0.000	0.000
89	A	95	LYS	1	0.923	0.966	36.503	0.015	0.015	0.000	0.000	0.000	0.000
90	A	96	LEU	0	0.048	0.027	39.598	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	97	ILE	0	-0.061	-0.030	42.927	0.002	0.002	0.000	0.000	0.000	0.000
92	A	98	LEU	0	0.027	0.026	45.870	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	99	SER	0	0.013	-0.015	48.775	0.000	0.000	0.000	0.000	0.000	0.000
94	A	100	LYS	1	0.894	0.944	52.344	0.000	0.000	0.000	0.000	0.000	0.000
95	A	101	GLU	-1	-0.919	-0.959	55.568	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	102	ASN	0	0.041	0.004	49.760	0.001	0.001	0.000	0.000	0.000	0.000
97	A	103	VAL	0	0.019	0.021	50.366	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	104	ASP	-1	-0.828	-0.918	51.784	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	105	GLU	-1	-0.798	-0.874	53.750	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	106	VAL	0	-0.036	-0.025	47.535	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	107	CYS	0	0.013	0.011	48.964	0.000	0.000	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.914	0.966	49.680	0.008	0.008	0.000	0.000	0.000	0.000
103	A	109	CYS	0	-0.041	-0.018	48.398	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	110	VAL	0	0.001	0.001	44.376	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	111	GLU	-1	-0.891	-0.949	46.124	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	112	PHE	0	-0.109	-0.053	48.372	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	113	LEU	0	0.000	-0.011	45.320	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	114	SER	0	-0.026	0.008	43.588	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	115	VAL	0	-0.035	-0.011	40.793	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	116	HIS	0	0.002	0.006	36.764	0.005	0.005	0.000	0.000	0.000	0.000
111	A	117	ASN	0	-0.048	-0.040	33.472	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	118	ILE	0	0.045	0.027	37.231	0.000	0.000	0.000	0.000	0.000	0.000
113	A	119	GLU	-1	-0.867	-0.896	39.813	0.015	0.015	0.000	0.000	0.000	0.000
114	A	120	GLU	-1	-0.802	-0.923	41.384	0.000	0.000	0.000	0.000	0.000	0.000
115	A	121	SER	0	-0.058	-0.059	44.312	0.000	0.000	0.000	0.000	0.000	0.000
116	A	122	CYS	0	-0.114	-0.065	44.092	0.000	0.000	0.000	0.000	0.000	0.000
117	A	123	PHE	0	0.035	0.008	46.181	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	124	GLN	0	0.003	0.008	49.047	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	125	PHE	0	-0.056	-0.021	44.855	0.000	0.000	0.000	0.000	0.000	0.000
120	A	126	LEU	0	-0.046	-0.004	49.541	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:SER)