FMO DATABASE

FMODB ID: 2R26R

Calculation Name: 3BJ2-B-Xray547

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe | acetyl group

Ligand 3-letter code: HEM | ACE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3BJ2

Chain ID: B

ChEMBL ID:

UniProt ID: D0VWS3

Base Structure: X-ray

Registration Date: 2025-10-04

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	-1311378.604869
FMO2-HF: Nuclear repulsion	1255186.28153
FMO2-HF: Total energy	-56192.323339
FMO2-MP2: Total energy	-56356.511354

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.
-29.533	-21.921	5.746	-3.57	-9.791	-0.036

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 : 0.841 / q_NPA : 0.921

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	-0.001	-0.013	2.484	-3.933	1.198	3.968	-2.701	-6.399	-0.031
4	A	4	THR	0	0.027	-0.007	4.419	3.458	3.521	-0.001	-0.016	-0.046	0.000
79	A	79	ASP	-1	-0.819	-0.867	3.569	-53.103	-52.509	0.020	-0.209	-0.405	-0.001
80	A	80	ASN	0	-0.017	-0.013	4.632	-5.013	-4.957	-0.001	-0.002	-0.053	0.000
81	A	81	ILE	0	0.015	0.026	4.012	3.764	3.912	-0.001	-0.014	-0.134	0.000
132	A	132	LYS	1	0.785	0.902	2.699	41.384	41.911	0.640	-0.175	-0.993	-0.001
133	A	133	PHE	0	0.000	-0.011	5.079	-4.179	-4.075	-0.001	-0.002	-0.101	0.000
136	A	136	VAL	0	-0.047	-0.020	2.405	-2.906	-1.917	1.122	-0.451	-1.660	-0.003
5	A	5	ASP	-1	-0.840	-0.932	7.987	-23.353	-23.353	0.000	0.000	0.000	0.000
6	A	6	PHE	0	0.015	0.017	10.908	0.619	0.619	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.785	-0.867	5.831	-35.280	-35.280	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.804	0.860	5.972	35.722	35.722	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.005	0.013	9.410	1.030	1.030	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.018	-0.005	11.301	1.221	1.221	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.063	-0.027	7.878	1.054	1.054	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.022	0.006	11.304	0.895	0.895	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.885	-0.913	13.951	-13.840	-13.840	0.000	0.000	0.000	0.000
14	A	14	ILE	0	0.030	0.014	12.897	0.910	0.910	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.005	-0.009	12.392	0.690	0.690	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.079	-0.044	16.603	0.927	0.927	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.848	0.906	19.405	14.665	14.665	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.061	-0.005	17.151	0.519	0.519	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.805	-0.889	21.150	-11.202	-11.202	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.054	-0.085	16.937	-0.127	-0.127	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.918	-0.948	21.980	-10.469	-10.469	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.017	-0.011	25.271	0.070	0.070	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.012	-0.002	20.261	0.052	0.052	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.055	0.027	21.473	-0.266	-0.266	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.025	-0.011	22.377	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.012	-0.002	25.132	0.158	0.158	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.028	-0.027	19.405	-0.046	-0.046	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.019	-0.005	22.794	-0.074	-0.074	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.015	0.003	24.145	0.201	0.201	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.927	0.968	24.049	11.357	11.357	0.000	0.000	0.000	0.000
31	A	31	CYS	0	0.030	0.007	22.687	0.010	0.010	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.022	-0.006	24.649	0.256	0.256	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.020	-0.005	28.056	0.419	0.419	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.035	-0.017	25.997	0.254	0.254	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.016	0.009	22.324	0.138	0.138	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.037	0.042	27.057	-0.200	-0.200	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.043	0.016	25.217	0.407	0.407	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.020	-0.033	24.009	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.012	-0.019	26.931	0.071	0.071	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.948	0.979	29.828	10.041	10.041	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.054	-0.019	25.287	0.129	0.129	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.010	-0.005	23.191	-0.184	-0.184	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.029	0.016	29.161	0.270	0.270	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.041	-0.020	32.118	0.445	0.445	0.000	0.000	0.000	0.000
45	A	45	PHE	0	0.002	-0.011	27.227	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.025	0.035	32.961	0.082	0.082	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.038	-0.033	36.577	-0.075	-0.075	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.024	0.013	31.040	-0.137	-0.137	0.000	0.000	0.000	0.000
49	A	49	TYR	0	0.065	0.033	33.908	-0.154	-0.154	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.012	0.015	36.298	-0.077	-0.077	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.079	0.027	34.446	-0.118	-0.118	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.024	0.006	34.744	-0.166	-0.166	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.035	-0.012	36.901	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.023	-0.012	30.587	-0.105	-0.105	0.000	0.000	0.000	0.000
55	A	55	MET	0	-0.032	-0.030	31.591	-0.259	-0.259	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.017	0.030	33.114	-0.031	-0.031	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.055	-0.033	32.712	0.009	0.009	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.050	0.018	31.913	-0.311	-0.311	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.004	0.003	30.481	-0.242	-0.242	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.014	-0.004	27.672	-0.424	-0.424	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.057	0.035	26.876	-0.475	-0.475	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.943	0.990	24.939	11.053	11.053	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.019	-0.019	21.953	-0.089	-0.089	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.065	0.018	22.605	-0.593	-0.593	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.010	0.001	21.502	-0.604	-0.604	0.000	0.000	0.000	0.000
66	A	66	THR	0	-0.065	-0.038	20.811	-0.380	-0.380	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.004	0.009	17.165	-0.702	-0.702	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.002	0.025	16.675	-1.137	-1.137	0.000	0.000	0.000	0.000
69	A	69	HIS	0	0.056	0.018	16.599	-0.863	-0.863	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.023	-0.008	15.839	-0.403	-0.403	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.006	0.010	11.895	-1.364	-1.364	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.778	-0.844	11.880	-18.698	-18.698	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.939	0.963	12.910	16.227	16.227	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.031	0.023	7.997	-1.203	-1.203	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.003	-0.004	8.078	-2.634	-2.634	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.816	0.884	10.187	16.918	16.918	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.040	-0.016	9.239	0.581	0.581	0.000	0.000	0.000	0.000
78	A	78	MET	0	0.040	0.029	5.297	-1.958	-1.958	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.852	0.900	5.939	31.775	31.775	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.014	0.014	7.837	2.840	2.840	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.055	-0.037	9.445	2.813	2.813	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.023	-0.038	10.454	1.692	1.692	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.020	0.031	12.347	0.928	0.928	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.867	-0.949	14.118	-14.832	-14.832	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.070	-0.029	14.082	1.002	1.002	0.000	0.000	0.000	0.000
89	A	89	SER	0	0.022	0.022	13.948	1.058	1.058	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.048	0.029	15.989	0.767	0.767	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.039	-0.018	19.317	0.886	0.886	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.036	-0.057	17.629	1.137	1.137	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.015	-0.001	18.084	0.334	0.334	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.951	-0.975	20.789	-13.560	-13.560	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.906	0.960	23.348	11.947	11.947	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.057	-0.032	22.480	0.555	0.555	0.000	0.000	0.000	0.000
97	A	97	HIS	0	-0.032	0.000	23.853	0.266	0.266	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.033	-0.025	20.587	0.394	0.394	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.862	-0.927	20.906	-14.292	-14.292	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.021	-0.004	16.583	-0.184	-0.184	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.850	-0.908	17.350	-15.301	-15.301	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.074	-0.065	19.132	0.243	0.243	0.000	0.000	0.000	0.000
103	A	103	PHE	0	0.021	0.010	14.936	-0.035	-0.035	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.936	0.991	10.733	21.685	21.685	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.054	0.031	16.223	0.095	0.095	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.015	0.010	16.765	0.382	0.382	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.011	-0.025	13.449	-0.428	-0.428	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.884	-0.936	15.394	-16.542	-16.542	0.000	0.000	0.000	0.000
109	A	109	CYS	0	-0.097	-0.044	17.544	0.766	0.766	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.007	0.005	14.626	0.397	0.397	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.013	-0.018	14.997	-0.053	-0.053	0.000	0.000	0.000	0.000
112	A	112	ILE	0	-0.019	-0.011	17.039	0.486	0.486	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.050	-0.019	20.692	0.570	0.570	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.021	0.006	16.416	0.390	0.390	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.007	-0.001	19.449	0.290	0.290	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.055	-0.029	20.659	0.459	0.459	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.061	-0.036	22.389	0.345	0.345	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.001	0.000	18.268	0.220	0.220	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.040	0.028	22.407	0.235	0.235	0.000	0.000	0.000	0.000
120	A	120	LYS	1	0.909	0.945	22.834	10.607	10.607	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.009	0.004	21.149	-0.100	-0.100	0.000	0.000	0.000	0.000
122	A	122	PHE	0	0.016	0.007	15.165	-0.801	-0.801	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.033	0.015	17.883	0.011	0.011	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.047	0.012	16.773	-0.565	-0.565	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.941	-0.967	14.033	-17.226	-17.226	0.000	0.000	0.000	0.000
126	A	126	VAL	0	0.004	0.002	12.612	-1.576	-1.576	0.000	0.000	0.000	0.000
127	A	127	GLN	0	0.005	0.006	12.654	-0.716	-0.716	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.008	-0.001	10.964	-0.992	-0.992	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.011	0.005	8.074	-2.284	-2.284	0.000	0.000	0.000	0.000
130	A	130	PHE	0	0.030	0.005	7.730	-2.666	-2.666	0.000	0.000	0.000	0.000
131	A	131	GLN	0	0.062	0.027	9.302	-1.318	-1.318	0.000	0.000	0.000	0.000
134	A	134	LEU	0	0.037	0.019	6.226	-1.328	-1.328	0.000	0.000	0.000	0.000
135	A	135	SER	0	-0.080	-0.051	6.706	1.540	1.540	0.000	0.000	0.000	0.000
137	A	137	VAL	0	0.014	0.007	5.590	1.034	1.034	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.005	-0.005	8.390	1.384	1.384	0.000	0.000	0.000	0.000
139	A	139	SER	0	-0.054	-0.022	6.990	2.107	2.107	0.000	0.000	0.000	0.000
140	A	140	ALA	0	-0.019	-0.002	7.762	0.694	0.694	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.013	-0.010	9.683	1.719	1.719	0.000	0.000	0.000	0.000
142	A	142	GLY	0	0.017	0.019	12.585	1.596	1.596	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.960	0.999	14.019	14.632	14.632	0.000	0.000	0.000	0.000
144	A	144	GLN	0	-0.016	-0.013	10.934	-2.342	-2.342	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.036	-0.032	13.709	1.894	1.894	0.000	0.000	0.000	0.000
146	A	146	HIS	-1	-0.852	-0.892	11.383	-23.165	-23.165	0.000	0.000	0.000	0.000

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