FMO DATABASE

FMODB ID: 2MG6R

Calculation Name: 3BCQ-B-Xray547

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe | oxygen molecule

Ligand 3-letter code: HEM | OXY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3BCQ

Chain ID: B

ChEMBL ID:

UniProt ID: D0VWS2

Base Structure: X-ray

Registration Date: 2025-10-05

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1305491.273808
FMO2-HF: Nuclear repulsion	1249391.673135
FMO2-HF: Total energy	-56099.600673
FMO2-MP2: Total energy	-56262.580488

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:VAL)

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

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.
21.088	27.292	1.677	-2.094	-5.787	-0.013

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

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 : 0.907

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	TRP	0	-0.060	-0.024	2.490	3.429	7.129	1.055	-1.305	-3.449	-0.009
4	A	4	SER	0	0.023	-0.008	4.918	2.631	2.680	-0.001	-0.004	-0.044	0.000
79	A	79	ASP	-1	-0.784	-0.845	3.560	-54.205	-53.560	0.027	-0.254	-0.418	-0.001
80	A	80	ASN	0	-0.035	-0.027	3.876	-10.039	-9.667	0.005	-0.168	-0.209	-0.001
81	A	81	ILE	0	0.035	0.030	4.383	4.834	4.969	-0.001	-0.006	-0.128	0.000
133	A	133	LYS	1	0.855	0.915	3.083	41.315	41.740	0.051	-0.076	-0.400	0.000
137	A	137	VAL	0	-0.019	-0.010	2.643	-1.865	-0.987	0.541	-0.281	-1.139	-0.002
5	A	5	THR	0	0.000	-0.017	8.372	-0.221	-0.221	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.045	0.039	11.401	0.989	0.989	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.701	-0.815	5.918	-35.376	-35.376	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.816	0.868	6.302	39.009	39.009	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.025	-0.024	10.218	1.467	1.467	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.031	0.025	12.223	1.195	1.195	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.011	-0.001	8.955	1.162	1.162	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.008	-0.007	12.359	1.114	1.114	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.025	-0.008	14.615	1.177	1.177	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.025	0.020	14.723	1.037	1.037	0.000	0.000	0.000	0.000
15	A	15	TRP	0	0.047	0.001	14.672	0.744	0.744	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.014	0.001	16.802	0.636	0.636	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.819	0.896	19.380	14.580	14.580	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.054	-0.010	18.118	0.564	0.564	0.000	0.000	0.000	0.000
19	A	19	SER	0	0.028	0.029	21.362	0.022	0.022	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.054	0.009	20.231	0.006	0.006	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.893	-0.965	22.821	-10.944	-10.944	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.836	-0.888	25.457	-10.478	-10.478	0.000	0.000	0.000	0.000
23	A	23	ILE	0	0.011	-0.008	20.339	0.068	0.068	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.044	0.015	21.709	-0.162	-0.162	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.032	-0.014	22.668	0.010	0.010	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.015	0.022	25.726	0.336	0.336	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.025	0.012	20.956	0.151	0.151	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.011	0.002	22.650	-0.060	-0.060	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.001	-0.026	24.055	0.298	0.298	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.912	0.953	24.090	11.085	11.085	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.043	0.026	21.254	0.214	0.214	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.034	-0.022	24.939	0.257	0.257	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.027	-0.009	28.131	0.392	0.392	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.041	-0.019	26.372	0.252	0.252	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.012	0.013	22.690	0.124	0.124	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.041	0.025	27.273	-0.164	-0.164	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.042	0.012	25.056	0.361	0.361	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.009	-0.007	24.149	-0.038	-0.038	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.046	-0.037	26.904	0.037	0.037	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.944	0.983	29.585	9.613	9.613	0.000	0.000	0.000	0.000
41	A	41	HIS	0	-0.009	-0.002	24.750	0.289	0.289	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.015	-0.012	22.994	-0.120	-0.120	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.029	0.014	28.949	0.242	0.242	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.020	0.000	31.437	0.252	0.252	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.030	-0.036	26.515	0.021	0.021	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.028	0.026	32.662	0.095	0.095	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.009	0.005	35.670	0.043	0.043	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.042	0.009	30.886	-0.113	-0.113	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.004	0.000	34.640	-0.091	-0.091	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.060	0.030	36.587	0.146	0.146	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.058	0.014	34.052	-0.110	-0.110	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.008	0.015	34.723	-0.141	-0.141	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.035	-0.011	36.841	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.041	-0.013	30.508	-0.100	-0.100	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.021	-0.004	31.622	-0.384	-0.384	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.004	0.017	33.026	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.034	-0.023	32.424	-0.030	-0.030	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.044	0.018	31.918	-0.315	-0.315	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.916	0.966	29.632	9.441	9.441	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.021	0.010	27.739	-0.384	-0.384	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.035	0.019	26.955	-0.443	-0.443	0.000	0.000	0.000	0.000
62	A	62	HIS	0	0.004	-0.002	26.580	-0.280	-0.280	0.000	0.000	0.000	0.000
63	A	63	HIS	0	0.019	0.001	21.821	-0.108	-0.108	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.063	0.024	22.681	-0.575	-0.575	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.879	0.944	21.665	10.156	10.156	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.028	-0.010	20.744	-0.523	-0.523	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.008	0.000	17.403	-0.756	-0.756	0.000	0.000	0.000	0.000
68	A	68	MET	0	-0.015	0.012	16.837	-1.059	-1.059	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.042	0.022	16.850	-0.729	-0.729	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.003	-0.001	15.443	-0.648	-0.648	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.009	0.025	12.215	-1.510	-1.510	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.825	-0.901	12.372	-17.073	-17.073	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.846	0.907	12.920	17.558	17.558	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.018	0.016	8.447	-1.168	-1.168	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.013	-0.008	8.824	-2.380	-2.380	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.830	0.901	10.269	16.211	16.211	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.056	-0.029	8.931	0.280	0.280	0.000	0.000	0.000	0.000
78	A	78	MET	0	0.037	0.016	5.212	-2.653	-2.653	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.937	0.982	5.680	32.497	32.497	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.016	0.018	7.569	3.111	3.111	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.031	0.032	9.430	2.618	2.618	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.001	-0.034	9.904	2.166	2.166	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.002	0.012	11.872	1.870	1.870	0.000	0.000	0.000	0.000
87	A	87	SER	0	0.011	-0.012	13.792	0.666	0.666	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.031	-0.010	13.862	1.084	1.084	0.000	0.000	0.000	0.000
89	A	89	SER	0	0.019	0.023	13.363	1.069	1.069	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.008	0.015	15.383	0.778	0.778	0.000	0.000	0.000	0.000
91	A	91	MET	0	-0.038	-0.019	18.861	0.762	0.762	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.010	-0.037	17.370	1.126	1.126	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.019	-0.013	17.378	0.274	0.274	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.886	-0.936	19.906	-12.905	-12.905	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.896	0.961	22.835	11.986	11.986	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.054	-0.038	21.931	0.494	0.494	0.000	0.000	0.000	0.000
97	A	97	HIS	0	-0.017	0.014	23.306	0.242	0.242	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.052	-0.024	20.375	0.335	0.335	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.857	-0.930	20.332	-13.960	-13.960	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.056	0.014	16.171	0.008	0.008	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.861	-0.921	16.848	-15.216	-15.216	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.053	-0.052	18.669	0.510	0.510	0.000	0.000	0.000	0.000
103	A	103	PHE	0	0.000	-0.001	14.635	0.160	0.160	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.856	0.935	12.905	17.267	17.267	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.029	0.018	15.906	0.142	0.142	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.008	-0.001	17.479	0.417	0.417	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.030	0.012	13.473	0.163	0.163	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.821	-0.896	15.482	-16.072	-16.072	0.000	0.000	0.000	0.000
109	A	109	CYS	0	-0.053	-0.030	17.619	0.730	0.730	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.007	-0.003	16.308	0.533	0.533	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.024	-0.011	15.677	0.002	0.002	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.009	0.003	17.854	0.430	0.430	0.000	0.000	0.000	0.000
113	A	113	CYS	0	-0.059	-0.022	21.553	0.663	0.663	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.013	0.009	18.029	0.397	0.397	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.010	0.009	20.420	0.377	0.377	0.000	0.000	0.000	0.000
116	A	116	MET	0	-0.073	-0.047	21.911	0.442	0.442	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.809	0.903	24.078	11.192	11.192	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.039	-0.023	19.623	0.162	0.162	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.044	0.031	24.237	0.235	0.235	0.000	0.000	0.000	0.000
120	A	120	PRO	0	0.002	-0.025	23.859	-0.441	-0.441	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.007	0.008	23.737	-0.167	-0.167	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.012	0.009	22.089	-0.295	-0.295	0.000	0.000	0.000	0.000
123	A	123	PHE	0	-0.058	-0.030	16.443	-0.847	-0.847	0.000	0.000	0.000	0.000
124	A	124	THR	0	0.031	0.031	17.916	0.278	0.278	0.000	0.000	0.000	0.000
125	A	125	PRO	0	0.034	0.005	17.559	-0.757	-0.757	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.829	-0.917	14.612	-16.740	-16.740	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.040	-0.025	13.129	-1.492	-1.492	0.000	0.000	0.000	0.000
128	A	128	GLN	0	-0.024	-0.010	13.428	-0.591	-0.591	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.964	-0.973	9.313	-25.390	-25.390	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.064	0.028	8.704	-1.874	-1.874	0.000	0.000	0.000	0.000
131	A	131	TRP	0	-0.001	-0.025	8.704	-2.354	-2.354	0.000	0.000	0.000	0.000
132	A	132	GLN	0	0.006	0.016	10.295	-0.955	-0.955	0.000	0.000	0.000	0.000
134	A	134	PHE	0	-0.025	-0.031	5.458	-3.091	-3.091	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.002	-0.008	7.163	-0.834	-0.834	0.000	0.000	0.000	0.000
136	A	136	ALA	0	0.010	0.015	6.591	0.569	0.569	0.000	0.000	0.000	0.000
138	A	138	VAL	0	0.003	-0.004	5.610	1.078	1.078	0.000	0.000	0.000	0.000
139	A	139	VAL	0	-0.008	-0.004	8.607	1.297	1.297	0.000	0.000	0.000	0.000
140	A	140	ALA	0	-0.018	-0.003	7.317	1.349	1.349	0.000	0.000	0.000	0.000
141	A	141	ALA	0	-0.017	-0.006	7.297	0.676	0.676	0.000	0.000	0.000	0.000
142	A	142	LEU	0	-0.031	-0.022	9.269	1.330	1.330	0.000	0.000	0.000	0.000
143	A	143	SER	0	-0.024	-0.021	12.284	1.915	1.915	0.000	0.000	0.000	0.000
144	A	144	ARG	1	0.885	0.949	13.407	14.193	14.193	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.032	-0.028	8.208	-1.611	-1.611	0.000	0.000	0.000	0.000
146	A	146	HIS	-1	-0.897	-0.931	13.916	-19.426	-19.426	0.000	0.000	0.000	0.000

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