FMO DATABASE

FMODB ID: RQL48

Calculation Name: 1BBH-A-Xray547

Preferred Name:

Target Type:

Ligand Name: heme c

Ligand 3-letter code: HEC

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BBH

Chain ID: A

ChEMBL ID:

UniProt ID: P00154

Base Structure: X-ray

Registration Date: 2025-09-02

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	131
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-985270.538585
FMO2-HF: Nuclear repulsion	936018.725444
FMO2-HF: Total energy	-49251.813141
FMO2-MP2: Total energy	-49392.743476

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:1:ALA)

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

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.
-91.502	-88.562	0.162	-1.799	-1.303	-0.012

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.904

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	3	LEU	0	0.012	0.012	2.892	-19.324	-16.384	0.162	-1.799	-1.303	-0.012
4	A	4	SER	0	-0.017	-0.034	5.755	1.351	1.351	0.000	0.000	0.000	0.000
5	A	5	PRO	0	-0.037	-0.043	6.974	2.170	2.170	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.808	-0.921	10.356	-27.320	-27.320	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.725	-0.830	7.166	-40.177	-40.177	0.000	0.000	0.000	0.000
8	A	8	GLN	0	-0.062	-0.015	8.340	4.218	4.218	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.049	-0.016	12.143	1.961	1.961	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.897	-0.956	13.992	-19.888	-19.888	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.028	-0.033	12.815	1.141	1.141	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.794	0.877	15.432	19.989	19.989	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.071	-0.037	17.858	0.871	0.871	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.050	0.028	18.320	0.898	0.898	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.023	0.013	19.501	0.668	0.668	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.016	-0.017	21.037	0.541	0.541	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.958	-0.965	23.475	-12.184	-12.184	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.104	0.045	23.576	0.674	0.674	0.000	0.000	0.000	0.000
19	A	19	MET	0	-0.015	0.008	24.043	0.619	0.619	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.014	0.017	27.305	0.526	0.526	0.000	0.000	0.000	0.000
21	A	21	TRP	0	0.037	0.012	28.383	0.464	0.464	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.025	-0.032	28.123	0.713	0.713	0.000	0.000	0.000	0.000
23	A	23	MET	0	0.025	0.022	31.351	0.351	0.351	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.007	-0.001	33.139	0.348	0.348	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.817	0.917	31.179	10.487	10.487	0.000	0.000	0.000	0.000
26	A	26	ILE	0	0.016	0.024	34.340	0.271	0.271	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.838	0.893	37.490	8.077	8.077	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.009	-0.012	38.965	0.228	0.228	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.023	-0.026	39.092	0.312	0.312	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.016	-0.008	40.912	0.183	0.183	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.901	-0.914	43.472	-7.413	-7.413	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.025	-0.002	44.741	0.159	0.159	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.966	-0.982	46.255	-6.546	-6.546	0.000	0.000	0.000	0.000
34	A	34	TYR	0	0.011	0.008	42.067	-0.212	-0.212	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.027	-0.019	41.195	0.050	0.050	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.060	0.024	40.760	-0.223	-0.223	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.074	0.043	39.185	-0.187	-0.187	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.055	-0.035	35.764	-0.222	-0.222	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.004	0.005	35.829	-0.347	-0.347	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.881	-0.939	35.915	-8.786	-8.786	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.022	-0.015	32.900	-0.334	-0.334	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.030	-0.016	31.528	-0.420	-0.420	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.029	0.007	31.205	-0.376	-0.376	0.000	0.000	0.000	0.000
44	A	44	ASN	0	0.024	0.012	30.622	-0.312	-0.312	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.046	-0.011	25.989	-0.495	-0.495	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.020	-0.013	26.545	-0.552	-0.552	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.049	0.029	27.411	-0.391	-0.391	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.024	-0.003	24.647	-0.386	-0.386	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.014	-0.018	21.655	-0.670	-0.670	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.003	0.016	22.688	-0.638	-0.638	0.000	0.000	0.000	0.000
51	A	51	ASN	0	-0.086	-0.069	23.991	-0.189	-0.189	0.000	0.000	0.000	0.000
52	A	52	SER	0	-0.084	-0.045	19.272	-0.690	-0.690	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.030	0.021	18.095	-0.981	-0.981	0.000	0.000	0.000	0.000
54	A	54	MET	0	-0.008	-0.007	17.084	-0.852	-0.852	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.007	0.009	17.122	-0.449	-0.449	0.000	0.000	0.000	0.000
56	A	56	ALA	0	-0.004	-0.012	12.668	-0.442	-0.442	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.037	-0.003	12.394	-2.167	-2.167	0.000	0.000	0.000	0.000
58	A	58	TYR	0	-0.014	-0.013	13.917	0.735	0.735	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.073	0.051	11.497	0.606	0.606	0.000	0.000	0.000	0.000
60	A	60	PRO	0	-0.016	-0.023	10.837	0.886	0.886	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.012	0.005	12.336	1.241	1.241	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.029	-0.010	12.502	0.870	0.870	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.783	-0.881	15.123	-16.403	-16.403	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.811	0.888	16.553	18.560	18.560	0.000	0.000	0.000	0.000
65	A	65	ASN	0	0.006	-0.003	17.405	-0.796	-0.796	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.008	0.004	12.651	0.078	0.078	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.024	0.018	16.059	-0.428	-0.428	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.915	-0.958	17.142	-16.133	-16.133	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.009	0.015	15.273	1.059	1.059	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.922	0.949	18.086	13.534	13.534	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.036	0.019	18.659	-0.056	-0.056	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.797	0.875	20.704	12.132	12.132	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.002	0.021	19.938	0.531	0.531	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.849	0.931	23.076	10.650	10.650	0.000	0.000	0.000	0.000
75	A	75	PRO	0	0.028	-0.002	23.315	-0.382	-0.382	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.837	-0.923	24.187	-11.331	-11.331	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.046	0.025	19.886	0.258	0.258	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.006	-0.002	17.097	0.083	0.083	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.048	-0.025	22.268	0.887	0.887	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.023	-0.007	24.968	0.641	0.641	0.000	0.000	0.000	0.000
81	A	81	MET	0	0.034	0.002	19.132	0.204	0.204	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.930	-0.950	24.127	-11.069	-11.069	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.833	-0.884	26.960	-10.072	-10.072	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.004	0.015	23.023	0.144	0.144	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.031	0.008	24.957	-0.063	-0.063	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.785	0.902	25.658	9.711	9.711	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.055	0.014	28.780	0.120	0.120	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.002	0.004	24.797	0.072	0.072	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.911	0.954	26.842	10.934	10.934	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.845	-0.924	28.755	-9.305	-9.305	0.000	0.000	0.000	0.000
91	A	91	PHE	0	-0.007	-0.006	25.940	0.185	0.185	0.000	0.000	0.000	0.000
92	A	92	VAL	0	0.008	0.004	25.951	0.142	0.142	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.005	0.017	29.216	0.186	0.186	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.024	0.019	32.765	0.245	0.245	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.003	-0.011	29.856	0.189	0.189	0.000	0.000	0.000	0.000
96	A	96	ASN	0	0.004	0.005	29.471	-0.151	-0.151	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.038	0.012	32.633	0.266	0.266	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.023	-0.017	33.703	0.232	0.232	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.012	-0.008	32.806	0.179	0.179	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.965	-0.977	34.959	-8.692	-8.692	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.013	-0.014	37.658	0.237	0.237	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.013	0.009	37.124	0.215	0.215	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.005	0.011	37.712	0.149	0.149	0.000	0.000	0.000	0.000
104	A	104	THR	0	-0.091	-0.057	39.643	0.241	0.241	0.000	0.000	0.000	0.000
105	A	105	GLY	0	-0.039	-0.017	42.378	0.195	0.195	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.841	-0.917	43.951	-6.712	-6.712	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.029	0.012	44.501	-0.169	-0.169	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.926	-0.971	44.898	-6.888	-6.888	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.009	-0.002	44.095	-0.102	-0.102	0.000	0.000	0.000	0.000
110	A	110	VAL	0	-0.014	-0.005	39.426	-0.205	-0.205	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.863	0.919	41.013	6.733	6.733	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.041	-0.003	42.352	-0.056	-0.056	0.000	0.000	0.000	0.000
113	A	113	ALA	0	0.067	0.037	38.079	-0.133	-0.133	0.000	0.000	0.000	0.000
114	A	114	PHE	0	-0.029	-0.019	35.661	-0.313	-0.313	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.019	0.012	37.322	-0.190	-0.190	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.888	-0.943	37.687	-8.308	-8.308	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.001	-0.010	31.917	-0.285	-0.285	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.016	0.019	33.302	-0.329	-0.329	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.015	-0.011	34.759	-0.152	-0.152	0.000	0.000	0.000	0.000
120	A	120	ALA	0	0.017	0.016	31.784	-0.129	-0.129	0.000	0.000	0.000	0.000
121	A	121	CYS	0	-0.063	-0.032	30.060	-0.444	-0.444	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.833	0.905	30.705	8.499	8.499	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.024	-0.001	32.802	-0.184	-0.184	0.000	0.000	0.000	0.000
124	A	124	CYS	0	-0.018	0.001	26.355	-0.179	-0.179	0.000	0.000	0.000	0.000
125	A	125	HIS	0	0.020	-0.010	26.718	-0.360	-0.360	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.875	-0.929	29.746	-8.908	-8.908	0.000	0.000	0.000	0.000
127	A	127	LYS	1	0.865	0.945	30.274	10.003	10.003	0.000	0.000	0.000	0.000
128	A	128	TYR	0	-0.032	-0.051	25.771	-0.100	-0.100	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.900	0.960	25.813	10.543	10.543	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.002	0.005	26.839	0.441	0.441	0.000	0.000	0.000	0.000
131	A	131	LYS	0	0.080	0.057	28.147	0.612	0.612	0.000	0.000	0.000	0.000

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