FMO DATABASE

FMODB ID: VQ861

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	OptH
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
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-965646.165671
FMO2-HF: Nuclear repulsion	917802.880943
FMO2-HF: Total energy	-47843.284728
FMO2-MP2: Total energy	-47981.691485

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.
0.204	2.186	-0.031	-0.929	-1.022	0

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 : -0.038 / q_NPA : -0.035

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].
3	A	9	PHE	0	0.000	0.010	3.791	0.044	2.026	-0.031	-0.929	-1.022
4	A	10	ALA	0	0.021	0.009	6.430	-0.401	-0.401	0.000	0.000	0.000
5	A	11	TYR	0	-0.030	-0.008	9.927	0.008	0.008	0.000	0.000	0.000
6	A	12	GLU	-1	-0.908	-0.960	12.876	0.451	0.451	0.000	0.000	0.000
7	A	13	SER	0	-0.036	-0.010	16.320	-0.017	-0.017	0.000	0.000	0.000
8	A	14	SER	0	0.032	0.003	19.357	-0.001	-0.001	0.000	0.000	0.000
9	A	15	VAL	0	0.046	0.022	22.369	-0.010	-0.010	0.000	0.000	0.000
10	A	16	HIS	0	-0.005	-0.001	21.768	-0.016	-0.016	0.000	0.000	0.000
11	A	17	SER	0	0.005	-0.008	23.803	-0.012	-0.012	0.000	0.000	0.000
12	A	18	THR	0	0.050	0.020	26.355	-0.005	-0.005	0.000	0.000	0.000
13	A	19	ASN	0	0.006	0.004	25.210	-0.007	-0.007	0.000	0.000	0.000
14	A	20	VAL	0	-0.005	0.004	26.295	-0.009	-0.009	0.000	0.000	0.000
15	A	21	LEU	0	0.038	0.022	29.096	-0.006	-0.006	0.000	0.000	0.000
16	A	22	LEU	0	0.029	0.019	31.504	-0.005	-0.005	0.000	0.000	0.000
17	A	23	SER	0	-0.030	-0.015	30.898	-0.007	-0.007	0.000	0.000	0.000
18	A	24	LEU	0	-0.012	0.001	32.067	-0.004	-0.004	0.000	0.000	0.000
19	A	25	ASN	0	0.068	0.026	35.015	-0.003	-0.003	0.000	0.000	0.000
20	A	26	ASP	-1	-0.883	-0.936	36.370	0.000	0.000	0.000	0.000	0.000
21	A	27	GLN	0	-0.043	-0.017	33.744	-0.001	-0.001	0.000	0.000	0.000
22	A	28	ARG	1	0.933	0.973	38.708	-0.028	-0.028	0.000	0.000	0.000
23	A	29	LYS	1	0.880	0.944	39.842	-0.017	-0.017	0.000	0.000	0.000
24	A	30	LYS	1	0.808	0.896	37.636	0.001	0.001	0.000	0.000	0.000
25	A	31	ASP	-1	-0.859	-0.911	43.243	0.007	0.007	0.000	0.000	0.000
26	A	32	VAL	0	-0.024	-0.002	38.852	-0.002	-0.002	0.000	0.000	0.000
27	A	33	LEU	0	-0.054	-0.048	35.396	0.002	0.002	0.000	0.000	0.000
28	A	34	CYS	0	-0.034	0.019	38.776	0.004	0.004	0.000	0.000	0.000
29	A	35	ASP	-1	-0.812	-0.899	39.135	0.025	0.025	0.000	0.000	0.000
30	A	36	VAL	0	-0.001	0.020	42.459	0.001	0.001	0.000	0.000	0.000
31	A	37	THR	0	-0.020	-0.010	44.889	-0.002	-0.002	0.000	0.000	0.000
32	A	38	ILE	0	-0.024	-0.005	45.618	0.001	0.001	0.000	0.000	0.000
33	A	39	PHE	0	-0.041	-0.027	49.174	-0.002	-0.002	0.000	0.000	0.000
34	A	40	VAL	0	0.061	0.022	50.650	0.001	0.001	0.000	0.000	0.000
35	A	41	GLU	-1	-0.800	-0.902	53.837	0.022	0.022	0.000	0.000	0.000
36	A	42	GLY	0	-0.042	-0.012	57.122	-0.001	-0.001	0.000	0.000	0.000
37	A	43	GLN	0	-0.038	-0.024	53.720	-0.001	-0.001	0.000	0.000	0.000
38	A	44	ARG	1	0.956	0.979	50.305	-0.011	-0.011	0.000	0.000	0.000
39	A	45	PHE	0	0.031	0.014	47.111	-0.001	-0.001	0.000	0.000	0.000
40	A	46	ARG	1	0.837	0.908	45.054	-0.012	-0.012	0.000	0.000	0.000
41	A	47	ALA	0	0.021	-0.003	41.731	0.001	0.001	0.000	0.000	0.000
42	A	48	HIS	0	0.085	0.072	37.006	0.000	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.773	0.862	39.105	-0.023	-0.023	0.000	0.000	0.000
44	A	50	SER	0	0.000	-0.007	34.421	0.003	0.003	0.000	0.000	0.000
45	A	51	VAL	0	0.030	0.015	34.519	0.006	0.006	0.000	0.000	0.000
46	A	52	LEU	0	0.011	0.004	36.555	0.004	0.004	0.000	0.000	0.000
47	A	53	ALA	0	-0.034	-0.011	37.522	0.002	0.002	0.000	0.000	0.000
48	A	54	ALA	0	-0.005	0.000	33.798	0.004	0.004	0.000	0.000	0.000
49	A	55	CYS	0	-0.049	-0.023	35.674	0.005	0.005	0.000	0.000	0.000
50	A	56	SER	0	-0.016	-0.046	37.870	-0.001	-0.001	0.000	0.000	0.000
51	A	57	SER	0	0.073	0.040	40.771	0.000	0.000	0.000	0.000	0.000
52	A	58	TYR	0	-0.015	0.011	42.036	-0.002	-0.002	0.000	0.000	0.000
53	A	59	PHE	0	0.013	-0.016	42.424	-0.003	-0.003	0.000	0.000	0.000
54	A	60	HIS	0	0.025	0.014	37.014	-0.002	-0.002	0.000	0.000	0.000
55	A	61	SER	0	-0.068	-0.048	41.407	-0.001	-0.001	0.000	0.000	0.000
56	A	62	ARG	1	0.902	0.954	44.459	-0.042	-0.042	0.000	0.000	0.000
57	A	63	ILE	0	-0.006	0.013	40.674	-0.003	-0.003	0.000	0.000	0.000
58	A	64	VAL	0	-0.029	-0.016	38.966	-0.002	-0.002	0.000	0.000	0.000
59	A	65	GLY	0	-0.006	0.001	40.825	0.001	0.001	0.000	0.000	0.000
60	A	66	GLN	0	-0.066	-0.015	43.371	-0.001	-0.001	0.000	0.000	0.000
61	A	67	ALA	0	0.036	0.002	40.566	-0.002	-0.002	0.000	0.000	0.000
62	A	68	ASP	-1	-0.891	-0.942	38.895	0.028	0.028	0.000	0.000	0.000
63	A	69	GLY	0	-0.031	-0.004	41.816	-0.004	-0.004	0.000	0.000	0.000
64	A	70	GLU	-1	-0.923	-0.966	45.102	0.017	0.017	0.000	0.000	0.000
65	A	71	LEU	0	-0.010	0.007	44.094	0.002	0.002	0.000	0.000	0.000
66	A	72	ASN	0	0.015	-0.004	47.312	-0.001	-0.001	0.000	0.000	0.000
67	A	73	ILE	0	-0.009	-0.008	46.923	0.001	0.001	0.000	0.000	0.000
68	A	74	THR	0	-0.011	-0.007	50.163	-0.001	-0.001	0.000	0.000	0.000
69	A	75	LEU	0	-0.059	-0.027	48.821	0.002	0.002	0.000	0.000	0.000
70	A	76	PRO	0	0.025	0.018	52.926	-0.002	-0.002	0.000	0.000	0.000
71	A	77	GLU	-1	-0.868	-0.945	55.787	0.026	0.026	0.000	0.000	0.000
72	A	78	GLU	-1	-0.901	-0.947	55.241	0.035	0.035	0.000	0.000	0.000
73	A	79	VAL	0	-0.077	-0.026	51.036	0.001	0.001	0.000	0.000	0.000
74	A	80	THR	0	0.027	-0.004	53.947	-0.001	-0.001	0.000	0.000	0.000
75	A	81	VAL	0	-0.005	-0.013	52.532	0.002	0.002	0.000	0.000	0.000
76	A	82	LYS	1	0.795	0.906	51.892	-0.026	-0.026	0.000	0.000	0.000
77	A	83	GLY	0	0.029	0.012	51.426	0.001	0.001	0.000	0.000	0.000
78	A	84	PHE	0	0.020	-0.002	46.313	0.002	0.002	0.000	0.000	0.000
79	A	85	GLU	-1	-0.891	-0.953	47.247	0.028	0.028	0.000	0.000	0.000
80	A	86	PRO	0	0.007	-0.004	46.090	0.001	0.001	0.000	0.000	0.000
81	A	87	LEU	0	0.012	0.017	43.837	0.003	0.003	0.000	0.000	0.000
82	A	88	ILE	0	-0.026	0.002	42.472	0.003	0.003	0.000	0.000	0.000
83	A	89	GLN	0	-0.042	-0.046	41.545	-0.001	-0.001	0.000	0.000	0.000
84	A	90	PHE	0	-0.022	0.022	37.710	0.000	0.000	0.000	0.000	0.000
85	A	91	ALA	0	-0.011	0.001	38.147	0.003	0.003	0.000	0.000	0.000
86	A	92	TYR	0	-0.015	-0.054	36.726	0.003	0.003	0.000	0.000	0.000
87	A	93	THR	0	-0.110	-0.093	36.151	-0.002	-0.002	0.000	0.000	0.000
88	A	94	ALA	0	-0.018	0.004	34.139	0.002	0.002	0.000	0.000	0.000
89	A	95	LYS	1	0.924	0.967	36.295	-0.036	-0.036	0.000	0.000	0.000
90	A	96	LEU	0	0.049	0.024	39.360	-0.003	-0.003	0.000	0.000	0.000
91	A	97	ILE	0	-0.069	-0.032	42.730	0.001	0.001	0.000	0.000	0.000
92	A	98	LEU	0	0.014	0.023	45.642	-0.002	-0.002	0.000	0.000	0.000
93	A	99	SER	0	-0.002	-0.015	48.569	-0.002	-0.002	0.000	0.000	0.000
94	A	100	LYS	1	0.910	0.942	52.140	-0.033	-0.033	0.000	0.000	0.000
95	A	101	GLU	-1	-0.926	-0.965	55.382	0.023	0.023	0.000	0.000	0.000
96	A	102	ASN	0	0.059	0.010	49.719	0.001	0.001	0.000	0.000	0.000
97	A	103	VAL	0	0.022	0.014	50.493	0.001	0.001	0.000	0.000	0.000
98	A	104	ASP	-1	-0.848	-0.919	51.770	0.037	0.037	0.000	0.000	0.000
99	A	105	GLU	-1	-0.828	-0.885	53.737	0.029	0.029	0.000	0.000	0.000
100	A	106	VAL	0	-0.033	-0.026	47.482	0.001	0.001	0.000	0.000	0.000
101	A	107	CYS	0	0.026	0.012	48.947	0.002	0.002	0.000	0.000	0.000
102	A	108	LYS	1	0.886	0.968	49.669	-0.037	-0.037	0.000	0.000	0.000
103	A	109	CYS	0	-0.044	-0.026	48.380	0.000	0.000	0.000	0.000	0.000
104	A	110	VAL	0	-0.005	0.001	44.351	0.001	0.001	0.000	0.000	0.000
105	A	111	GLU	-1	-0.876	-0.943	46.115	0.050	0.050	0.000	0.000	0.000
106	A	112	PHE	0	-0.104	-0.053	48.365	0.001	0.001	0.000	0.000	0.000
107	A	113	LEU	0	0.009	-0.003	45.286	0.000	0.000	0.000	0.000	0.000
108	A	114	SER	0	-0.021	0.033	43.440	0.003	0.003	0.000	0.000	0.000
109	A	115	VAL	0	-0.036	-0.013	40.980	0.002	0.002	0.000	0.000	0.000
110	A	116	HIS	0	0.001	-0.002	36.673	0.001	0.001	0.000	0.000	0.000
111	A	117	ASN	0	-0.063	-0.044	33.706	-0.004	-0.004	0.000	0.000	0.000
112	A	118	ILE	0	0.052	0.024	37.220	-0.001	-0.001	0.000	0.000	0.000
113	A	119	GLU	-1	-0.875	-0.895	39.822	0.078	0.078	0.000	0.000	0.000
114	A	120	GLU	-1	-0.808	-0.926	41.370	0.057	0.057	0.000	0.000	0.000
115	A	121	SER	0	-0.071	-0.067	44.285	-0.004	-0.004	0.000	0.000	0.000
116	A	122	CYS	0	-0.104	-0.051	44.075	-0.003	-0.003	0.000	0.000	0.000
117	A	123	PHE	0	0.045	0.005	45.999	-0.004	-0.004	0.000	0.000	0.000
118	A	124	GLN	0	-0.020	-0.008	49.031	-0.002	-0.002	0.000	0.000	0.000
119	A	125	PHE	0	-0.061	-0.023	45.003	-0.001	-0.001	0.000	0.000	0.000
120	A	126	LEU	0	0.026	0.033	49.057	-0.004	-0.004	0.000	0.000	0.000

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