FMO DATABASE

FMODB ID: 9L212

Calculation Name: 1IT2-A-Xray547

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe

Ligand 3-letter code: HEM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1IT2

Chain ID: A

ChEMBL ID:

UniProt ID: Q7SID0

Base Structure: X-ray

Registration Date: 2025-10-03

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	-1448256.141813
FMO2-HF: Nuclear repulsion	1390093.870409
FMO2-HF: Total energy	-58162.271404
FMO2-MP2: Total energy	-58334.692039

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:PRO)

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

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.
-98.007	-96.036	21.126	-13.224	-9.874	-0.14

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.792 / q_NPA : 0.854

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	ILE	0	-0.016	-0.006	3.647	1.667	3.347	0.001	-0.693	-0.989	-0.001
115	A	115	LYS	1	0.929	0.960	4.522	36.748	36.811	-0.001	-0.004	-0.058	0.000
129	A	129	ALA	0	0.034	0.004	4.515	-2.330	-2.274	-0.001	-0.006	-0.049	0.000
132	A	132	GLU	-1	-0.818	-0.888	1.750	-130.874	-130.702	21.127	-12.521	-8.778	-0.139
4	A	4	ASP	-1	-0.791	-0.905	5.772	-25.205	-25.205	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.026	0.012	9.408	3.440	3.440	0.000	0.000	0.000	0.000
6	A	6	GLY	0	0.014	0.014	10.343	-1.994	-1.994	0.000	0.000	0.000	0.000
7	A	7	PRO	0	-0.006	-0.004	12.013	0.827	0.827	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.023	0.007	11.908	-2.031	-2.031	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.017	-0.008	8.146	0.851	0.851	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.039	0.020	10.866	1.022	1.022	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.028	-0.013	11.438	-1.632	-1.632	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.004	-0.029	13.493	1.979	1.979	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.834	-0.934	15.534	-15.956	-15.956	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.037	-0.016	15.757	0.335	0.335	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.760	-0.850	10.656	-27.436	-27.436	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.906	0.947	13.280	16.431	16.431	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.931	0.972	16.253	15.139	15.139	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.010	-0.004	13.145	0.836	0.836	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.016	0.001	11.834	0.489	0.489	0.000	0.000	0.000	0.000
20	A	20	ASN	0	0.016	-0.011	14.636	0.302	0.302	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.886	0.951	17.341	16.778	16.778	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.009	0.013	13.201	0.798	0.798	0.000	0.000	0.000	0.000
23	A	23	TRP	0	0.034	0.000	15.624	0.117	0.117	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.008	0.001	18.127	0.467	0.467	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.927	0.972	18.448	16.780	16.780	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.017	-0.006	16.365	0.397	0.397	0.000	0.000	0.000	0.000
27	A	27	TYR	0	0.014	-0.001	19.800	0.591	0.591	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.866	0.920	22.161	12.619	12.619	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.860	-0.916	23.524	-11.835	-11.835	0.000	0.000	0.000	0.000
30	A	30	TYR	0	0.010	0.014	21.886	-0.352	-0.352	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.926	-0.943	22.387	-11.253	-11.253	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.002	-0.008	23.316	0.144	0.144	0.000	0.000	0.000	0.000
33	A	33	TYR	0	0.023	0.001	17.569	-0.361	-0.361	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.044	-0.028	18.673	-0.662	-0.662	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.012	0.012	19.455	-0.449	-0.449	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.016	0.004	18.993	0.293	0.293	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.011	0.009	14.149	-0.448	-0.448	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.000	0.008	16.267	-0.568	-0.568	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.000	-0.005	18.522	0.148	0.148	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.892	0.932	11.977	21.742	21.742	0.000	0.000	0.000	0.000
41	A	41	PHE	0	0.026	0.017	13.799	-0.199	-0.199	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.011	-0.005	16.103	0.171	0.171	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.892	0.945	19.004	13.307	13.307	0.000	0.000	0.000	0.000
44	A	44	CYS	0	-0.072	-0.026	14.648	0.073	0.073	0.000	0.000	0.000	0.000
45	A	45	PHE	0	0.006	0.005	11.564	-0.056	-0.056	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.030	0.021	17.756	0.440	0.440	0.000	0.000	0.000	0.000
47	A	47	GLN	0	0.030	0.007	18.147	0.557	0.557	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.015	0.011	17.896	0.269	0.269	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.069	-0.040	20.017	-0.056	-0.056	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.018	-0.013	23.225	0.444	0.444	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.037	-0.012	20.611	0.319	0.319	0.000	0.000	0.000	0.000
52	A	52	PHE	0	0.008	0.009	19.043	-0.096	-0.096	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.042	0.010	24.997	0.370	0.370	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.859	0.934	28.499	10.475	10.475	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.045	0.024	23.086	0.238	0.238	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.045	-0.011	27.403	0.021	0.021	0.000	0.000	0.000	0.000
57	A	57	THR	0	0.001	0.001	28.421	-0.102	-0.102	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.834	0.931	29.761	10.110	10.110	0.000	0.000	0.000	0.000
59	A	59	LYS	1	1.015	1.003	29.011	9.982	9.982	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.050	-0.035	29.599	0.398	0.398	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.033	0.004	30.455	0.021	0.021	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.011	0.008	25.130	0.166	0.166	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.858	-0.936	26.447	-11.017	-11.017	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.012	-0.002	27.356	-0.136	-0.136	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.862	-0.918	28.573	-9.881	-9.881	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.016	-0.005	28.897	-0.363	-0.363	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.789	-0.900	28.887	-10.414	-10.414	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.031	-0.003	23.750	-0.434	-0.434	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.959	0.973	24.307	9.761	9.761	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.015	0.016	25.286	-0.298	-0.298	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.031	-0.019	21.788	-0.021	-0.021	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.006	-0.001	20.582	-0.665	-0.665	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.034	0.015	20.655	-0.693	-0.693	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.000	0.002	22.763	-0.189	-0.189	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.032	-0.006	16.610	-0.317	-0.317	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.012	-0.004	17.927	-0.764	-0.764	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.006	-0.006	19.163	-0.540	-0.540	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.854	0.937	19.328	14.658	14.658	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.008	0.001	14.923	-0.323	-0.323	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.028	0.017	17.437	-0.457	-0.457	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.885	-0.934	20.178	-13.284	-13.284	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.005	0.024	15.991	0.183	0.183	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.003	-0.011	15.222	-0.295	-0.295	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.057	-0.034	18.397	0.146	0.146	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.017	-0.030	20.652	0.575	0.575	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.064	-0.011	16.019	-0.681	-0.681	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.869	-0.918	18.695	-15.171	-15.171	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.037	-0.003	21.488	0.163	0.163	0.000	0.000	0.000	0.000
89	A	89	GLN	0	0.027	0.009	18.066	-1.184	-1.184	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.871	-0.948	20.457	-13.461	-13.461	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.889	-0.963	23.470	-12.326	-12.326	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.005	0.014	16.681	-0.236	-0.236	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.017	-0.019	18.185	-0.334	-0.334	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.906	0.955	20.481	11.337	11.337	0.000	0.000	0.000	0.000
95	A	95	SER	0	0.011	0.007	21.869	-0.067	-0.067	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.019	0.003	16.363	0.129	0.129	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.959	0.988	20.291	13.446	13.446	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.955	-0.959	21.852	-11.418	-11.418	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.012	-0.003	20.236	0.228	0.228	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.019	-0.013	18.738	0.208	0.208	0.000	0.000	0.000	0.000
101	A	101	GLN	0	0.064	0.022	20.786	0.228	0.228	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.945	0.991	24.172	11.483	11.483	0.000	0.000	0.000	0.000
103	A	103	HIS	0	-0.014	-0.029	20.591	0.190	0.190	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.834	0.930	22.292	13.254	13.254	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.061	-0.052	23.428	0.493	0.493	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.061	-0.022	26.900	0.419	0.419	0.000	0.000	0.000	0.000
107	A	107	PHE	0	-0.053	-0.043	23.451	0.371	0.371	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.908	0.972	25.035	10.763	10.763	0.000	0.000	0.000	0.000
109	A	109	VAL	0	0.021	0.022	18.980	0.049	0.049	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.835	-0.911	17.360	-16.318	-16.318	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.002	-0.005	15.550	-0.789	-0.789	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.004	0.000	11.843	-1.452	-1.452	0.000	0.000	0.000	0.000
113	A	113	TRP	0	0.015	-0.006	12.067	-1.883	-1.883	0.000	0.000	0.000	0.000
114	A	114	PHE	0	0.007	0.017	12.676	-0.814	-0.814	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.846	-0.897	8.299	-32.989	-32.989	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.010	-0.003	10.315	-0.387	-0.387	0.000	0.000	0.000	0.000
118	A	118	SER	0	0.017	-0.013	8.722	0.602	0.602	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.034	-0.027	6.263	-3.938	-3.938	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.024	0.004	7.250	0.003	0.003	0.000	0.000	0.000	0.000
121	A	121	PHE	0	0.020	0.020	10.689	1.465	1.465	0.000	0.000	0.000	0.000
122	A	122	VAL	0	0.009	-0.003	6.438	1.620	1.620	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.023	-0.021	8.413	2.205	2.205	0.000	0.000	0.000	0.000
124	A	124	THR	0	-0.033	-0.027	9.796	2.112	2.112	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.076	-0.034	11.696	1.678	1.678	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.952	-0.959	11.851	-20.577	-20.577	0.000	0.000	0.000	0.000
127	A	127	GLY	0	-0.027	-0.007	9.919	0.412	0.412	0.000	0.000	0.000	0.000
128	A	128	GLY	0	0.054	0.023	7.668	-2.607	-2.607	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.888	-0.942	5.475	-32.413	-32.413	0.000	0.000	0.000	0.000
131	A	131	PHE	0	0.022	0.007	8.265	1.684	1.684	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.834	0.924	5.442	29.923	29.923	0.000	0.000	0.000	0.000
134	A	134	LEU	0	0.016	0.004	6.948	2.428	2.428	0.000	0.000	0.000	0.000
135	A	135	PHE	0	0.033	-0.008	7.915	2.163	2.163	0.000	0.000	0.000	0.000
136	A	136	SER	0	0.008	0.001	5.693	-0.666	-0.666	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.029	-0.002	8.218	2.833	2.833	0.000	0.000	0.000	0.000
138	A	138	ILE	0	0.006	0.002	11.586	1.972	1.972	0.000	0.000	0.000	0.000
139	A	139	CYS	0	-0.054	-0.020	9.593	1.535	1.535	0.000	0.000	0.000	0.000
140	A	140	ILE	0	-0.009	0.001	9.885	1.666	1.666	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.032	-0.008	12.760	1.828	1.828	0.000	0.000	0.000	0.000
142	A	142	LEU	0	-0.009	0.009	14.851	1.378	1.378	0.000	0.000	0.000	0.000
143	A	143	ARG	1	0.867	0.926	11.119	23.528	23.528	0.000	0.000	0.000	0.000
144	A	144	SER	0	-0.088	-0.051	15.764	1.164	1.164	0.000	0.000	0.000	0.000
145	A	145	ALA	0	-0.022	0.000	18.173	0.614	0.614	0.000	0.000	0.000	0.000
146	A	146	TYR	-1	-0.920	-0.959	18.277	-13.508	-13.508	0.000	0.000	0.000	0.000

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