FMO DATABASE

FMODB ID: QK26Y

Calculation Name: 1X9F-A-Xray547

Preferred Name:

Target Type:

Ligand Name: protoporphyrin ix containing fe | phosphate ion | carbon monoxide

Ligand 3-letter code: HEM | PO4 | CMO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X9F

Chain ID: A

ChEMBL ID:

UniProt ID: P02218

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	-1470918.038776
FMO2-HF: Nuclear repulsion	1411398.448721
FMO2-HF: Total energy	-59519.590055
FMO2-MP2: Total energy	-59695.015403

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:5:ASP)

Summations of interaction energy for fragment #1(A:5:ASP)

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.
-9.47	-7.711	2.112	-1.979	-1.894	0

Interaction energy analysis for fragmet #1(A:5:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.053 / q_NPA : -0.040

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	7	CYS	0	-0.059	-0.008	3.655	-5.513	-3.660	0.002	-0.979	-0.877	0.002
133	A	137	ARG	1	0.832	0.903	2.142	11.715	11.621	2.110	-1.000	-1.017	-0.002
4	A	8	SER	0	0.012	-0.008	6.397	1.908	1.908	0.000	0.000	0.000	0.000
5	A	9	TYR	0	-0.063	-0.048	7.911	0.684	0.684	0.000	0.000	0.000	0.000
6	A	10	GLU	-1	-0.857	-0.916	10.303	-3.370	-3.370	0.000	0.000	0.000	0.000
7	A	11	ASP	-1	-0.736	-0.847	6.224	-9.737	-9.737	0.000	0.000	0.000	0.000
8	A	12	ARG	1	0.893	0.922	9.936	2.445	2.445	0.000	0.000	0.000	0.000
9	A	13	ARG	1	0.943	0.980	12.503	2.291	2.291	0.000	0.000	0.000	0.000
10	A	14	GLU	-1	-0.831	-0.910	12.629	-2.498	-2.498	0.000	0.000	0.000	0.000
11	A	15	ILE	0	-0.036	-0.016	9.810	0.318	0.318	0.000	0.000	0.000	0.000
12	A	16	ARG	1	0.822	0.900	14.261	1.431	1.431	0.000	0.000	0.000	0.000
13	A	17	HIS	0	0.019	0.020	17.544	0.272	0.272	0.000	0.000	0.000	0.000
14	A	18	ILE	0	-0.001	0.001	15.098	0.127	0.127	0.000	0.000	0.000	0.000
15	A	19	TRP	0	0.000	-0.028	17.376	0.163	0.163	0.000	0.000	0.000	0.000
16	A	20	ASP	-1	-0.928	-0.958	19.178	-0.814	-0.814	0.000	0.000	0.000	0.000
17	A	21	ASP	-1	-0.895	-0.935	21.750	-0.919	-0.919	0.000	0.000	0.000	0.000
18	A	22	VAL	0	-0.059	-0.019	19.600	0.087	0.087	0.000	0.000	0.000	0.000
19	A	23	TRP	0	-0.072	-0.038	22.589	0.119	0.119	0.000	0.000	0.000	0.000
20	A	24	SER	0	0.080	0.039	24.282	0.038	0.038	0.000	0.000	0.000	0.000
21	A	25	SER	0	-0.057	-0.038	27.606	0.029	0.029	0.000	0.000	0.000	0.000
22	A	26	SER	0	0.017	0.011	30.305	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	27	PHE	0	0.017	0.016	32.447	0.030	0.030	0.000	0.000	0.000	0.000
24	A	28	THR	0	0.016	-0.008	30.562	-0.023	-0.023	0.000	0.000	0.000	0.000
25	A	29	ASP	-1	-0.855	-0.920	30.156	-0.304	-0.304	0.000	0.000	0.000	0.000
26	A	30	ARG	1	0.897	0.945	24.900	0.702	0.702	0.000	0.000	0.000	0.000
27	A	31	ARG	1	0.896	0.950	25.470	0.331	0.331	0.000	0.000	0.000	0.000
28	A	32	VAL	0	-0.009	-0.009	25.893	0.005	0.005	0.000	0.000	0.000	0.000
29	A	33	ALA	0	0.002	0.001	27.742	0.012	0.012	0.000	0.000	0.000	0.000
30	A	34	ILE	0	0.019	0.013	21.655	0.001	0.001	0.000	0.000	0.000	0.000
31	A	35	VAL	0	0.011	-0.004	21.967	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	36	ARG	1	0.808	0.897	23.874	0.240	0.240	0.000	0.000	0.000	0.000
33	A	37	ALA	0	0.042	0.026	24.271	0.031	0.031	0.000	0.000	0.000	0.000
34	A	38	VAL	0	-0.007	-0.002	18.894	0.009	0.009	0.000	0.000	0.000	0.000
35	A	39	PHE	0	-0.001	-0.011	21.301	0.056	0.056	0.000	0.000	0.000	0.000
36	A	40	ASP	-1	-0.885	-0.951	23.543	-0.144	-0.144	0.000	0.000	0.000	0.000
37	A	41	ASP	-1	-0.814	-0.874	19.741	-0.403	-0.403	0.000	0.000	0.000	0.000
38	A	42	LEU	0	0.018	0.007	18.764	0.051	0.051	0.000	0.000	0.000	0.000
39	A	43	PHE	0	-0.031	-0.032	21.329	0.065	0.065	0.000	0.000	0.000	0.000
40	A	44	LYS	1	0.938	0.980	23.960	0.252	0.252	0.000	0.000	0.000	0.000
41	A	45	HIS	0	-0.091	-0.045	20.153	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	46	TYR	0	-0.034	-0.003	16.095	0.132	0.132	0.000	0.000	0.000	0.000
43	A	47	PRO	0	0.040	0.037	22.433	0.020	0.020	0.000	0.000	0.000	0.000
44	A	48	THR	0	-0.009	-0.008	25.110	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	49	SER	0	-0.011	-0.008	22.633	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	50	LYS	1	0.908	0.958	24.732	0.015	0.015	0.000	0.000	0.000	0.000
47	A	51	ALA	0	0.071	0.027	27.691	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	52	LEU	0	-0.058	-0.016	24.101	0.006	0.006	0.000	0.000	0.000	0.000
49	A	53	PHE	0	-0.041	-0.028	23.257	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	54	GLU	-1	-0.846	-0.919	29.394	0.122	0.122	0.000	0.000	0.000	0.000
51	A	55	ARG	1	0.904	0.956	32.285	-0.135	-0.135	0.000	0.000	0.000	0.000
52	A	56	VAL	0	-0.100	-0.062	29.308	-0.008	-0.008	0.000	0.000	0.000	0.000
53	A	57	LYS	1	0.894	0.957	32.771	-0.032	-0.032	0.000	0.000	0.000	0.000
54	A	58	ILE	0	-0.052	-0.024	29.633	-0.025	-0.025	0.000	0.000	0.000	0.000
55	A	59	ASP	-1	-0.870	-0.936	32.584	0.014	0.014	0.000	0.000	0.000	0.000
56	A	60	GLU	-1	-0.842	-0.918	36.165	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	61	PRO	0	0.028	0.026	33.101	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	62	GLU	-1	-0.787	-0.902	33.773	-0.206	-0.206	0.000	0.000	0.000	0.000
59	A	63	SER	0	-0.031	-0.018	36.005	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.024	0.026	36.212	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	65	GLU	-1	-0.847	-0.926	35.024	-0.030	-0.030	0.000	0.000	0.000	0.000
62	A	66	PHE	0	0.041	0.043	28.404	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	67	LYS	1	0.885	0.934	30.720	0.143	0.143	0.000	0.000	0.000	0.000
64	A	68	SER	0	-0.039	-0.034	30.716	-0.014	-0.014	0.000	0.000	0.000	0.000
65	A	69	HIS	0	-0.012	-0.012	25.532	0.001	0.001	0.000	0.000	0.000	0.000
66	A	70	LEU	0	0.009	0.013	26.303	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	71	VAL	0	0.008	-0.001	25.917	-0.042	-0.042	0.000	0.000	0.000	0.000
68	A	72	ARG	1	0.885	0.947	26.738	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	73	VAL	0	-0.008	0.009	21.160	0.001	0.001	0.000	0.000	0.000	0.000
70	A	74	ALA	0	0.023	0.019	21.894	-0.046	-0.046	0.000	0.000	0.000	0.000
71	A	75	ASN	0	0.000	-0.026	22.442	-0.068	-0.068	0.000	0.000	0.000	0.000
72	A	76	GLY	0	0.009	0.012	22.271	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	77	LEU	0	-0.004	0.007	15.589	0.008	0.008	0.000	0.000	0.000	0.000
74	A	78	LYS	1	0.901	0.968	18.729	0.612	0.612	0.000	0.000	0.000	0.000
75	A	79	LEU	0	-0.013	-0.003	20.879	-0.048	-0.048	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.013	-0.008	15.468	0.001	0.001	0.000	0.000	0.000	0.000
77	A	81	ILE	0	-0.010	-0.007	14.621	-0.097	-0.097	0.000	0.000	0.000	0.000
78	A	82	ASN	0	-0.031	-0.035	17.236	-0.111	-0.111	0.000	0.000	0.000	0.000
79	A	83	LEU	0	0.029	0.022	18.781	0.052	0.052	0.000	0.000	0.000	0.000
80	A	84	LEU	0	-0.052	-0.016	12.743	0.015	0.015	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.770	-0.872	15.656	-1.236	-1.236	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.890	-0.922	18.362	-0.269	-0.269	0.000	0.000	0.000	0.000
83	A	87	THR	0	-0.022	-0.024	15.549	0.132	0.132	0.000	0.000	0.000	0.000
84	A	88	LEU	0	0.030	0.011	17.708	0.164	0.164	0.000	0.000	0.000	0.000
85	A	89	VAL	0	0.030	0.017	20.340	0.096	0.096	0.000	0.000	0.000	0.000
86	A	90	LEU	0	-0.015	-0.004	14.190	0.079	0.079	0.000	0.000	0.000	0.000
87	A	91	GLN	0	-0.064	-0.034	16.639	0.194	0.194	0.000	0.000	0.000	0.000
88	A	92	SER	0	-0.019	0.005	17.906	0.144	0.144	0.000	0.000	0.000	0.000
89	A	93	HIS	0	0.056	0.020	19.790	0.078	0.078	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.032	-0.022	13.155	0.026	0.026	0.000	0.000	0.000	0.000
91	A	95	GLY	0	-0.029	-0.018	17.787	0.142	0.142	0.000	0.000	0.000	0.000
92	A	96	HIS	0	0.057	0.038	19.735	0.037	0.037	0.000	0.000	0.000	0.000
93	A	97	LEU	0	-0.006	-0.012	17.827	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	98	ALA	0	-0.007	0.012	17.921	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	99	ASP	-1	-0.858	-0.926	19.510	0.722	0.722	0.000	0.000	0.000	0.000
96	A	100	GLN	0	-0.061	-0.042	23.211	-0.049	-0.049	0.000	0.000	0.000	0.000
97	A	101	HIS	0	-0.075	-0.051	20.487	-0.110	-0.110	0.000	0.000	0.000	0.000
98	A	102	ILE	0	0.047	0.031	20.230	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	103	GLN	0	-0.064	-0.024	23.466	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	104	ARG	1	0.831	0.918	24.684	-0.388	-0.388	0.000	0.000	0.000	0.000
101	A	105	LYS	1	1.039	1.012	25.068	-0.406	-0.406	0.000	0.000	0.000	0.000
102	A	106	GLY	0	0.011	0.003	25.123	-0.053	-0.053	0.000	0.000	0.000	0.000
103	A	107	VAL	0	-0.001	0.000	19.864	-0.021	-0.021	0.000	0.000	0.000	0.000
104	A	108	THR	0	0.073	0.046	19.647	0.073	0.073	0.000	0.000	0.000	0.000
105	A	109	LYS	1	0.879	0.914	12.917	-2.292	-2.292	0.000	0.000	0.000	0.000
106	A	110	GLU	-1	-0.845	-0.895	14.686	0.752	0.752	0.000	0.000	0.000	0.000
107	A	111	TYR	0	0.006	-0.016	16.273	-0.109	-0.109	0.000	0.000	0.000	0.000
108	A	112	PHE	0	0.022	0.002	13.773	-0.140	-0.140	0.000	0.000	0.000	0.000
109	A	113	ARG	1	0.814	0.906	11.527	-0.975	-0.975	0.000	0.000	0.000	0.000
110	A	114	GLY	0	0.046	0.013	13.093	-0.267	-0.267	0.000	0.000	0.000	0.000
111	A	115	ILE	0	-0.013	-0.009	14.964	-0.173	-0.173	0.000	0.000	0.000	0.000
112	A	116	GLY	0	0.016	0.006	11.802	-0.183	-0.183	0.000	0.000	0.000	0.000
113	A	117	GLU	-1	-0.868	-0.939	12.746	-0.282	-0.282	0.000	0.000	0.000	0.000
114	A	118	ALA	0	0.019	0.021	14.077	-0.168	-0.168	0.000	0.000	0.000	0.000
115	A	119	PHE	0	-0.015	-0.025	14.653	-0.065	-0.065	0.000	0.000	0.000	0.000
116	A	120	ALA	0	-0.030	-0.011	11.988	-0.127	-0.127	0.000	0.000	0.000	0.000
117	A	121	ARG	1	0.816	0.885	13.938	0.392	0.392	0.000	0.000	0.000	0.000
118	A	122	VAL	0	0.002	0.007	17.328	0.031	0.031	0.000	0.000	0.000	0.000
119	A	123	LEU	0	0.007	0.005	15.003	0.040	0.040	0.000	0.000	0.000	0.000
120	A	124	PRO	0	-0.019	-0.013	16.261	0.021	0.021	0.000	0.000	0.000	0.000
121	A	125	GLN	0	-0.073	-0.038	18.801	0.113	0.113	0.000	0.000	0.000	0.000
122	A	126	VAL	0	-0.054	-0.024	21.133	0.087	0.087	0.000	0.000	0.000	0.000
123	A	127	LEU	0	-0.031	-0.011	18.485	0.054	0.054	0.000	0.000	0.000	0.000
124	A	128	SER	0	0.031	0.014	20.633	-0.070	-0.070	0.000	0.000	0.000	0.000
125	A	129	CYS	0	-0.037	-0.034	19.254	0.003	0.003	0.000	0.000	0.000	0.000
126	A	130	PHE	0	0.061	0.042	13.635	-0.203	-0.203	0.000	0.000	0.000	0.000
127	A	131	ASN	0	0.003	-0.004	11.069	-0.529	-0.529	0.000	0.000	0.000	0.000
128	A	132	VAL	0	0.019	-0.004	11.164	-0.315	-0.315	0.000	0.000	0.000	0.000
129	A	133	ASP	-1	-0.895	-0.946	7.796	-6.991	-6.991	0.000	0.000	0.000	0.000
130	A	134	ALA	0	-0.016	-0.010	6.580	-1.680	-1.680	0.000	0.000	0.000	0.000
131	A	135	TRP	0	0.022	0.005	7.690	-0.299	-0.299	0.000	0.000	0.000	0.000
132	A	136	ASN	0	0.017	0.005	6.514	0.940	0.940	0.000	0.000	0.000	0.000
134	A	139	PHE	0	0.031	0.025	7.842	1.198	1.198	0.000	0.000	0.000	0.000
135	A	140	HIS	0	0.005	-0.006	5.064	1.301	1.301	0.000	0.000	0.000	0.000
136	A	141	ARG	1	0.942	0.979	6.560	0.327	0.327	0.000	0.000	0.000	0.000
137	A	142	LEU	0	-0.030	-0.021	7.615	0.633	0.633	0.000	0.000	0.000	0.000
138	A	143	VAL	0	0.042	0.015	10.011	0.363	0.363	0.000	0.000	0.000	0.000
139	A	144	ALA	0	-0.015	0.004	7.889	0.232	0.232	0.000	0.000	0.000	0.000
140	A	145	ARG	1	0.891	0.951	10.033	-1.165	-1.165	0.000	0.000	0.000	0.000
141	A	146	ILE	0	-0.008	0.002	13.186	-0.063	-0.063	0.000	0.000	0.000	0.000
142	A	147	ALA	0	0.059	0.012	13.297	-0.050	-0.050	0.000	0.000	0.000	0.000
143	A	148	LYS	1	0.787	0.891	13.643	-1.659	-1.659	0.000	0.000	0.000	0.000
144	A	149	ASP	-1	-0.820	-0.916	14.573	1.750	1.750	0.000	0.000	0.000	0.000
145	A	150	LEU	0	-0.018	-0.001	17.381	-0.123	-0.123	0.000	0.000	0.000	0.000
146	A	151	PRO	-1	-0.957	-0.952	17.207	1.069	1.069	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ASP)