FMO DATABASE

FMODB ID: L6LL9

Calculation Name: 2O6P-A-Xray549

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe

Ligand 3-letter code: HEM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2O6P

Chain ID: A

ChEMBL ID:

UniProt ID: Q8KQR1

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1047990.880757
FMO2-HF: Nuclear repulsion	999409.686802
FMO2-HF: Total energy	-48581.193955
FMO2-MP2: Total energy	-48725.703256

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:28:GLY)

Summations of interaction energy for fragment #1(A:28:GLY)

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.
-70.888	-69.751	16.867	-10.014	-7.99	-0.116

Interaction energy analysis for fragmet #1(A:28:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.851 / q_NPA : 0.927

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	30	ASP	-1	-0.808	-0.893	3.810	-43.349	-42.498	-0.013	-0.304	-0.534	-0.001
118	A	145	PRO	0	-0.005	0.016	4.364	1.770	1.837	-0.001	-0.018	-0.048	0.000
120	A	147	ASP	-1	-0.839	-0.910	1.793	-114.396	-115.857	16.243	-8.437	-6.345	-0.104
121	A	148	VAL	0	-0.041	-0.020	2.707	-14.022	-12.340	0.639	-1.242	-1.079	-0.011
122	A	149	ALA	0	0.025	0.023	4.589	5.818	5.816	-0.001	-0.013	0.016	0.000
4	A	31	SER	0	-0.063	-0.031	6.305	6.256	6.256	0.000	0.000	0.000	0.000
5	A	32	GLY	0	0.039	0.026	8.023	-3.062	-3.062	0.000	0.000	0.000	0.000
6	A	33	THR	0	-0.052	-0.027	9.536	2.107	2.107	0.000	0.000	0.000	0.000
7	A	34	LEU	0	-0.003	0.005	9.926	-2.296	-2.296	0.000	0.000	0.000	0.000
8	A	35	ASN	0	0.056	0.028	11.964	2.194	2.194	0.000	0.000	0.000	0.000
9	A	36	TYR	0	-0.078	-0.065	14.691	-0.542	-0.542	0.000	0.000	0.000	0.000
10	A	37	GLU	-1	-0.814	-0.886	17.352	-12.476	-12.476	0.000	0.000	0.000	0.000
11	A	38	VAL	0	-0.007	-0.004	21.019	-0.319	-0.319	0.000	0.000	0.000	0.000
12	A	39	TYR	0	-0.002	-0.001	22.293	0.136	0.136	0.000	0.000	0.000	0.000
13	A	40	LYS	1	0.986	0.985	26.205	9.155	9.155	0.000	0.000	0.000	0.000
14	A	41	TYR	0	-0.042	-0.016	28.061	0.018	0.018	0.000	0.000	0.000	0.000
15	A	42	ASN	0	-0.016	-0.008	27.596	0.042	0.042	0.000	0.000	0.000	0.000
16	A	43	THR	0	-0.026	-0.007	28.308	0.139	0.139	0.000	0.000	0.000	0.000
17	A	44	ASN	0	-0.034	-0.023	25.161	-1.007	-1.007	0.000	0.000	0.000	0.000
18	A	45	ASP	-1	-0.830	-0.902	26.759	-10.191	-10.191	0.000	0.000	0.000	0.000
19	A	46	THR	0	-0.030	-0.038	26.279	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	47	SER	0	-0.036	-0.012	27.433	0.589	0.589	0.000	0.000	0.000	0.000
21	A	48	ILE	0	0.043	0.016	29.371	-0.117	-0.117	0.000	0.000	0.000	0.000
22	A	49	ALA	0	0.015	-0.004	28.700	0.049	0.049	0.000	0.000	0.000	0.000
23	A	50	ASN	0	0.033	0.011	24.276	-0.718	-0.718	0.000	0.000	0.000	0.000
24	A	51	ASP	-1	-0.862	-0.930	25.898	-11.018	-11.018	0.000	0.000	0.000	0.000
25	A	52	TYR	0	-0.045	-0.009	28.253	0.088	0.088	0.000	0.000	0.000	0.000
26	A	53	PHE	0	-0.005	0.000	22.780	-0.222	-0.222	0.000	0.000	0.000	0.000
27	A	54	ASN	0	0.008	0.012	22.770	0.183	0.183	0.000	0.000	0.000	0.000
28	A	55	LYS	1	0.816	0.938	19.344	12.747	12.747	0.000	0.000	0.000	0.000
29	A	56	PRO	0	-0.006	0.002	14.929	0.434	0.434	0.000	0.000	0.000	0.000
30	A	57	ALA	0	0.014	0.013	15.811	0.775	0.775	0.000	0.000	0.000	0.000
31	A	58	LYS	1	0.959	0.964	13.460	18.772	18.772	0.000	0.000	0.000	0.000
32	A	59	TYR	0	-0.031	-0.022	5.641	2.706	2.706	0.000	0.000	0.000	0.000
33	A	60	ILE	0	-0.011	-0.019	10.639	-1.046	-1.046	0.000	0.000	0.000	0.000
34	A	61	LYS	1	0.838	0.934	7.912	33.229	33.229	0.000	0.000	0.000	0.000
35	A	62	LYS	1	0.825	0.898	10.407	17.503	17.503	0.000	0.000	0.000	0.000
36	A	63	ASN	0	-0.015	-0.019	13.672	0.171	0.171	0.000	0.000	0.000	0.000
37	A	64	GLY	0	0.032	0.025	13.315	0.860	0.860	0.000	0.000	0.000	0.000
38	A	65	LYS	1	0.865	0.934	13.866	15.619	15.619	0.000	0.000	0.000	0.000
39	A	66	LEU	0	0.014	0.014	8.624	-1.203	-1.203	0.000	0.000	0.000	0.000
40	A	67	TYR	0	-0.006	-0.005	12.240	2.027	2.027	0.000	0.000	0.000	0.000
41	A	68	VAL	0	0.011	0.008	13.004	-1.559	-1.559	0.000	0.000	0.000	0.000
42	A	69	GLN	0	-0.060	-0.056	15.119	0.956	0.956	0.000	0.000	0.000	0.000
43	A	70	ILE	0	0.000	-0.001	17.442	-0.462	-0.462	0.000	0.000	0.000	0.000
44	A	71	THR	0	-0.004	-0.009	19.761	0.297	0.297	0.000	0.000	0.000	0.000
45	A	72	VAL	0	0.000	0.002	22.548	-0.109	-0.109	0.000	0.000	0.000	0.000
46	A	73	ASN	0	0.003	-0.005	25.840	0.606	0.606	0.000	0.000	0.000	0.000
47	A	74	HIS	1	0.901	0.944	28.986	9.423	9.423	0.000	0.000	0.000	0.000
48	A	75	SER	0	-0.021	-0.007	30.352	0.095	0.095	0.000	0.000	0.000	0.000
49	A	76	HIS	1	0.770	0.830	31.659	8.476	8.476	0.000	0.000	0.000	0.000
50	A	77	TRP	0	-0.041	-0.025	34.567	0.111	0.111	0.000	0.000	0.000	0.000
51	A	78	ILE	0	0.005	0.019	28.838	0.094	0.094	0.000	0.000	0.000	0.000
52	A	79	THR	0	0.017	0.004	32.361	-0.203	-0.203	0.000	0.000	0.000	0.000
53	A	80	GLY	0	0.012	0.020	30.902	0.051	0.051	0.000	0.000	0.000	0.000
54	A	81	MET	0	-0.004	0.011	24.287	-0.056	-0.056	0.000	0.000	0.000	0.000
55	A	82	SER	0	-0.037	-0.025	25.348	0.023	0.023	0.000	0.000	0.000	0.000
56	A	83	ILE	0	0.037	0.020	19.617	0.015	0.015	0.000	0.000	0.000	0.000
57	A	84	GLU	-1	-0.778	-0.863	18.618	-16.308	-16.308	0.000	0.000	0.000	0.000
58	A	85	GLY	0	-0.019	0.001	22.556	0.035	0.035	0.000	0.000	0.000	0.000
59	A	86	HIS	1	0.886	0.950	20.820	14.324	14.324	0.000	0.000	0.000	0.000
60	A	87	LYS	1	1.002	0.982	24.377	9.796	9.796	0.000	0.000	0.000	0.000
61	A	88	GLU	-1	-0.749	-0.827	24.120	-11.557	-11.557	0.000	0.000	0.000	0.000
62	A	89	ASN	0	-0.010	0.011	21.755	0.978	0.978	0.000	0.000	0.000	0.000
63	A	90	ILE	0	-0.033	-0.027	23.484	-0.407	-0.407	0.000	0.000	0.000	0.000
64	A	91	ILE	0	0.018	0.021	19.733	0.274	0.274	0.000	0.000	0.000	0.000
65	A	92	SER	0	0.004	0.000	23.858	0.169	0.169	0.000	0.000	0.000	0.000
66	A	93	LYS	1	0.960	0.970	26.026	10.149	10.149	0.000	0.000	0.000	0.000
67	A	94	ASN	0	0.020	0.013	28.445	0.340	0.340	0.000	0.000	0.000	0.000
68	A	95	THR	0	0.032	0.004	30.430	-0.031	-0.031	0.000	0.000	0.000	0.000
69	A	96	ALA	0	0.027	0.020	33.802	0.168	0.168	0.000	0.000	0.000	0.000
70	A	97	LYS	1	0.847	0.911	27.230	11.307	11.307	0.000	0.000	0.000	0.000
71	A	98	ASP	-1	-0.769	-0.851	31.919	-9.251	-9.251	0.000	0.000	0.000	0.000
72	A	99	GLU	-1	-0.800	-0.885	27.240	-11.689	-11.689	0.000	0.000	0.000	0.000
73	A	100	ARG	1	0.677	0.794	26.606	10.933	10.933	0.000	0.000	0.000	0.000
74	A	101	THR	0	-0.008	0.014	20.558	-0.410	-0.410	0.000	0.000	0.000	0.000
75	A	102	SER	0	-0.037	-0.037	22.465	0.316	0.316	0.000	0.000	0.000	0.000
76	A	103	GLU	-1	-0.818	-0.884	17.656	-17.307	-17.307	0.000	0.000	0.000	0.000
77	A	104	PHE	0	0.012	-0.005	18.459	0.945	0.945	0.000	0.000	0.000	0.000
78	A	105	GLU	-1	-0.852	-0.905	17.011	-16.365	-16.365	0.000	0.000	0.000	0.000
79	A	106	VAL	0	-0.054	-0.039	13.813	0.899	0.899	0.000	0.000	0.000	0.000
80	A	107	SER	0	-0.043	-0.060	14.725	-1.324	-1.324	0.000	0.000	0.000	0.000
81	A	108	LYS	1	0.892	0.952	11.734	16.189	16.189	0.000	0.000	0.000	0.000
82	A	109	LEU	0	0.051	0.026	7.241	1.394	1.394	0.000	0.000	0.000	0.000
83	A	110	ASN	0	-0.067	-0.046	10.454	1.893	1.893	0.000	0.000	0.000	0.000
84	A	111	GLY	0	0.071	0.041	12.370	0.462	0.462	0.000	0.000	0.000	0.000
85	A	112	LYS	1	0.839	0.903	16.068	13.080	13.080	0.000	0.000	0.000	0.000
86	A	113	ILE	0	-0.023	-0.010	15.997	-0.212	-0.212	0.000	0.000	0.000	0.000
87	A	114	ASP	-1	-0.770	-0.861	20.393	-11.584	-11.584	0.000	0.000	0.000	0.000
88	A	115	GLY	0	-0.013	-0.021	23.526	-0.392	-0.392	0.000	0.000	0.000	0.000
89	A	116	LYS	1	0.866	0.933	25.320	10.523	10.523	0.000	0.000	0.000	0.000
90	A	117	ILE	0	-0.025	-0.006	27.838	-0.338	-0.338	0.000	0.000	0.000	0.000
91	A	118	ASP	-1	-0.841	-0.887	30.020	-9.056	-9.056	0.000	0.000	0.000	0.000
92	A	119	VAL	0	-0.016	-0.023	33.011	-0.156	-0.156	0.000	0.000	0.000	0.000
93	A	120	TYR	0	0.033	0.014	35.390	0.262	0.262	0.000	0.000	0.000	0.000
94	A	121	ILE	0	-0.012	-0.011	37.305	-0.096	-0.096	0.000	0.000	0.000	0.000
95	A	122	ASP	-1	-0.882	-0.950	40.584	-6.720	-6.720	0.000	0.000	0.000	0.000
96	A	123	GLU	-1	-0.765	-0.848	40.700	-7.858	-7.858	0.000	0.000	0.000	0.000
97	A	124	LYS	1	0.907	0.953	44.809	6.315	6.315	0.000	0.000	0.000	0.000
98	A	125	VAL	0	0.059	0.033	42.234	-0.137	-0.137	0.000	0.000	0.000	0.000
99	A	126	ASN	0	0.013	-0.002	44.293	0.124	0.124	0.000	0.000	0.000	0.000
100	A	127	GLY	0	-0.003	-0.003	47.008	0.154	0.154	0.000	0.000	0.000	0.000
101	A	128	LYS	1	0.930	0.965	48.751	6.322	6.322	0.000	0.000	0.000	0.000
102	A	129	PRO	0	0.005	-0.004	47.902	-0.146	-0.146	0.000	0.000	0.000	0.000
103	A	130	PHE	0	-0.010	0.004	40.777	0.065	0.065	0.000	0.000	0.000	0.000
104	A	131	LYS	1	0.859	0.940	43.077	7.195	7.195	0.000	0.000	0.000	0.000
105	A	132	TYR	0	0.000	0.007	36.766	-0.080	-0.080	0.000	0.000	0.000	0.000
106	A	133	ASP	-1	-0.867	-0.936	40.107	-7.737	-7.737	0.000	0.000	0.000	0.000
107	A	134	HIS	0	0.002	0.013	37.193	0.013	0.013	0.000	0.000	0.000	0.000
108	A	135	HIS	1	0.811	0.871	34.967	8.219	8.219	0.000	0.000	0.000	0.000
109	A	136	TYR	0	-0.008	-0.002	32.170	0.129	0.129	0.000	0.000	0.000	0.000
110	A	137	ASN	0	-0.002	0.005	29.876	-0.358	-0.358	0.000	0.000	0.000	0.000
111	A	138	ILE	0	-0.013	-0.015	25.533	0.228	0.228	0.000	0.000	0.000	0.000
112	A	139	THR	0	0.028	-0.005	23.344	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	140	TYR	0	-0.006	0.007	19.568	0.128	0.128	0.000	0.000	0.000	0.000
114	A	141	LYS	1	0.912	0.941	17.524	16.441	16.441	0.000	0.000	0.000	0.000
115	A	142	PHE	0	0.027	0.008	13.861	0.058	0.058	0.000	0.000	0.000	0.000
116	A	143	ASN	0	-0.038	-0.020	13.040	0.522	0.522	0.000	0.000	0.000	0.000
117	A	144	GLY	0	0.061	0.030	9.620	-0.260	-0.260	0.000	0.000	0.000	0.000
119	A	146	THR	0	0.014	-0.014	6.303	0.813	0.813	0.000	0.000	0.000	0.000
123	A	150	GLY	-1	-0.831	-0.911	8.157	-27.422	-27.422	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:GLY)