FMO DATABASE

FMODB ID: G5L41

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	OptAll
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	-966737.812849
FMO2-HF: Nuclear repulsion	918893.702406
FMO2-HF: Total energy	-47844.110443
FMO2-MP2: Total energy	-47982.574924

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.
0.538	2.713	-0.016	-1.166	-0.992	0.004

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 : 0.010 / q_NPA : 0.004

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

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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	-0.004	0.001	3.882	0.914	3.089	-0.016	-1.166	-0.992	0.004
4	A	10	ALA	0	0.010	0.006	6.608	-0.485	-0.485	0.000	0.000	0.000	0.000
5	A	11	TYR	0	0.007	-0.001	10.359	0.113	0.113	0.000	0.000	0.000	0.000
6	A	12	GLU	-1	-0.906	-0.944	13.579	0.006	0.006	0.000	0.000	0.000	0.000
7	A	13	SER	0	-0.041	-0.024	16.959	0.020	0.020	0.000	0.000	0.000	0.000
8	A	14	SER	0	0.021	0.002	19.751	-0.011	-0.011	0.000	0.000	0.000	0.000
9	A	15	VAL	0	0.016	0.009	22.672	0.002	0.002	0.000	0.000	0.000	0.000
10	A	16	HIS	0	0.015	0.014	22.205	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	17	SER	0	0.063	0.024	24.255	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	18	THR	0	0.022	0.008	26.810	0.000	0.000	0.000	0.000	0.000	0.000
13	A	19	ASN	0	0.021	0.010	25.300	0.007	0.007	0.000	0.000	0.000	0.000
14	A	20	VAL	0	-0.014	0.009	26.678	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	21	LEU	0	0.016	0.018	29.417	0.000	0.000	0.000	0.000	0.000	0.000
16	A	22	LEU	0	0.027	0.011	32.098	0.003	0.003	0.000	0.000	0.000	0.000
17	A	23	SER	0	-0.037	-0.034	30.906	0.000	0.000	0.000	0.000	0.000	0.000
18	A	24	LEU	0	-0.022	-0.005	32.288	0.000	0.000	0.000	0.000	0.000	0.000
19	A	25	ASN	0	0.071	0.042	35.397	0.004	0.004	0.000	0.000	0.000	0.000
20	A	26	ASP	-1	-0.851	-0.915	36.754	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	27	GLN	0	-0.021	-0.009	34.083	0.002	0.002	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.911	0.939	39.063	0.043	0.043	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.806	0.894	40.076	0.052	0.052	0.000	0.000	0.000	0.000
24	A	30	LYS	1	0.805	0.892	38.640	0.068	0.068	0.000	0.000	0.000	0.000
25	A	31	ASP	-1	-0.769	-0.859	44.145	-0.050	-0.050	0.000	0.000	0.000	0.000
26	A	32	VAL	0	-0.018	0.003	39.165	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	33	LEU	0	-0.040	-0.040	35.909	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	34	CYS	0	-0.038	0.020	39.496	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	35	ASP	-1	-0.783	-0.872	39.448	-0.064	-0.064	0.000	0.000	0.000	0.000
30	A	36	VAL	0	0.007	0.020	42.632	0.002	0.002	0.000	0.000	0.000	0.000
31	A	37	THR	0	-0.027	-0.012	45.066	0.000	0.000	0.000	0.000	0.000	0.000
32	A	38	ILE	0	-0.020	-0.001	45.801	0.001	0.001	0.000	0.000	0.000	0.000
33	A	39	PHE	0	-0.016	-0.014	49.589	0.000	0.000	0.000	0.000	0.000	0.000
34	A	40	VAL	0	0.055	0.028	51.175	0.001	0.001	0.000	0.000	0.000	0.000
35	A	41	GLU	-1	-0.789	-0.884	54.366	-0.019	-0.019	0.000	0.000	0.000	0.000
36	A	42	GLY	0	-0.020	0.000	57.770	0.000	0.000	0.000	0.000	0.000	0.000
37	A	43	GLN	0	-0.070	-0.036	54.867	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	44	ARG	1	0.903	0.955	49.566	0.041	0.041	0.000	0.000	0.000	0.000
39	A	45	PHE	0	0.024	0.011	47.909	0.000	0.000	0.000	0.000	0.000	0.000
40	A	46	ARG	1	0.762	0.845	44.880	0.051	0.051	0.000	0.000	0.000	0.000
41	A	47	ALA	0	0.026	0.008	41.746	0.001	0.001	0.000	0.000	0.000	0.000
42	A	48	HIS	0	0.058	0.047	37.554	0.002	0.002	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.759	0.825	39.109	0.062	0.062	0.000	0.000	0.000	0.000
44	A	50	SER	0	0.009	0.004	34.582	0.004	0.004	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.014	0.011	34.898	0.001	0.001	0.000	0.000	0.000	0.000
46	A	52	LEU	0	0.027	0.010	36.792	0.004	0.004	0.000	0.000	0.000	0.000
47	A	53	ALA	0	-0.011	-0.004	38.077	0.003	0.003	0.000	0.000	0.000	0.000
48	A	54	ALA	0	-0.013	-0.011	34.191	0.003	0.003	0.000	0.000	0.000	0.000
49	A	55	CYS	0	-0.046	-0.004	36.126	0.004	0.004	0.000	0.000	0.000	0.000
50	A	56	SER	0	-0.001	-0.010	38.458	0.004	0.004	0.000	0.000	0.000	0.000
51	A	57	SER	0	0.063	0.017	40.854	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	58	TYR	0	-0.017	0.027	42.388	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	59	PHE	0	0.044	-0.003	42.832	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	60	HIS	0	0.056	0.022	37.986	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	61	SER	0	-0.064	-0.042	41.744	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	62	ARG	1	0.840	0.921	44.863	0.029	0.029	0.000	0.000	0.000	0.000
57	A	63	ILE	0	-0.019	0.002	40.495	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	64	VAL	0	-0.041	-0.021	39.099	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	65	GLY	0	-0.003	0.004	41.160	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	66	GLN	0	-0.071	-0.029	43.935	0.001	0.001	0.000	0.000	0.000	0.000
61	A	67	ALA	0	0.039	0.018	41.445	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	68	ASP	-1	-0.871	-0.924	39.145	-0.068	-0.068	0.000	0.000	0.000	0.000
63	A	69	GLY	0	-0.018	0.004	42.339	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.853	-0.928	45.502	-0.047	-0.047	0.000	0.000	0.000	0.000
65	A	71	LEU	0	-0.044	-0.015	44.995	0.002	0.002	0.000	0.000	0.000	0.000
66	A	72	ASN	0	-0.038	-0.039	48.236	0.001	0.001	0.000	0.000	0.000	0.000
67	A	73	ILE	0	-0.009	-0.005	47.195	0.001	0.001	0.000	0.000	0.000	0.000
68	A	74	THR	0	-0.007	-0.010	50.540	0.000	0.000	0.000	0.000	0.000	0.000
69	A	75	LEU	0	-0.053	-0.013	49.308	0.000	0.000	0.000	0.000	0.000	0.000
70	A	76	PRO	0	0.014	0.013	53.547	0.000	0.000	0.000	0.000	0.000	0.000
71	A	77	GLU	-1	-0.876	-0.954	56.374	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	78	GLU	-1	-0.918	-0.946	55.716	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.061	-0.027	51.418	0.000	0.000	0.000	0.000	0.000	0.000
74	A	80	THR	0	0.013	-0.013	54.548	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	81	VAL	0	-0.025	-0.037	52.619	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	82	LYS	1	0.787	0.893	52.077	0.012	0.012	0.000	0.000	0.000	0.000
77	A	83	GLY	0	0.040	0.018	51.574	0.001	0.001	0.000	0.000	0.000	0.000
78	A	84	PHE	0	0.036	0.002	46.850	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	85	GLU	-1	-0.837	-0.907	47.490	-0.030	-0.030	0.000	0.000	0.000	0.000
80	A	86	PRO	0	-0.032	-0.023	46.296	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	87	LEU	0	0.018	0.013	44.157	0.000	0.000	0.000	0.000	0.000	0.000
82	A	88	ILE	0	-0.024	-0.003	42.806	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	89	GLN	0	-0.033	-0.029	42.028	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	90	PHE	0	-0.017	0.021	38.247	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	91	ALA	0	0.010	-0.005	38.452	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	92	TYR	0	-0.019	-0.034	36.997	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	93	THR	0	-0.093	-0.087	36.380	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	94	ALA	0	-0.022	0.006	34.432	0.002	0.002	0.000	0.000	0.000	0.000
89	A	95	LYS	1	0.924	0.962	36.522	0.022	0.022	0.000	0.000	0.000	0.000
90	A	96	LEU	0	0.041	0.039	39.581	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	97	ILE	0	-0.052	-0.033	42.935	0.002	0.002	0.000	0.000	0.000	0.000
92	A	98	LEU	0	0.006	0.009	45.933	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	99	SER	0	0.020	-0.009	49.000	0.001	0.001	0.000	0.000	0.000	0.000
94	A	100	LYS	1	0.831	0.889	52.612	0.004	0.004	0.000	0.000	0.000	0.000
95	A	101	GLU	-1	-0.897	-0.950	55.634	-0.012	-0.012	0.000	0.000	0.000	0.000
96	A	102	ASN	0	0.051	0.016	49.923	0.001	0.001	0.000	0.000	0.000	0.000
97	A	103	VAL	0	-0.006	0.013	50.382	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	104	ASP	-1	-0.806	-0.882	51.989	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	105	GLU	-1	-0.778	-0.860	54.222	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	106	VAL	0	-0.022	-0.016	47.831	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	107	CYS	0	0.011	0.011	49.388	0.000	0.000	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.896	0.953	50.217	0.013	0.013	0.000	0.000	0.000	0.000
103	A	109	CYS	0	-0.040	-0.022	48.678	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	110	VAL	0	-0.021	-0.007	44.925	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	111	GLU	-1	-0.885	-0.949	46.767	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	112	PHE	0	-0.062	-0.024	48.660	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	113	LEU	0	-0.008	-0.024	45.665	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	114	SER	0	-0.016	0.004	44.318	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	115	VAL	0	-0.062	-0.018	41.480	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	116	HIS	0	-0.006	0.000	37.193	0.005	0.005	0.000	0.000	0.000	0.000
111	A	117	ASN	0	-0.049	-0.049	33.539	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	118	ILE	0	0.037	0.037	37.615	0.001	0.001	0.000	0.000	0.000	0.000
113	A	119	GLU	-1	-0.862	-0.898	40.322	0.008	0.008	0.000	0.000	0.000	0.000
114	A	120	GLU	-1	-0.788	-0.915	41.972	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	121	SER	0	-0.052	-0.051	44.798	0.000	0.000	0.000	0.000	0.000	0.000
116	A	122	CYS	0	-0.125	-0.075	44.174	0.000	0.000	0.000	0.000	0.000	0.000
117	A	123	PHE	0	0.034	0.008	46.315	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	124	GLN	0	0.000	0.009	49.479	0.000	0.000	0.000	0.000	0.000	0.000
119	A	125	PHE	0	-0.039	-0.017	44.973	0.001	0.001	0.000	0.000	0.000	0.000
120	A	126	LEU	0	-0.055	-0.002	49.929	-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)