FMO DATABASE

FMODB ID: M87KZ

Calculation Name: 1A9W-E-Xray547

Preferred Name: Hemoglobin alpha subunit

Target Type: SINGLE PROTEIN

Ligand Name: protoporphyrin ix containing fe | carbon monoxide

Ligand 3-letter code: HEM | CMO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A9W

Chain ID: E

ChEMBL ID: CHEMBL2887

UniProt ID: P69905

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1296072.626803
FMO2-HF: Nuclear repulsion	1240740.676677
FMO2-HF: Total energy	-55331.950127
FMO2-MP2: Total energy	-55494.922119

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.
3.618	9.678	2.949	-3.041	-5.964	-0.027

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 : 0.840 / q_NPA : 0.915

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	PHE	0	0.007	-0.007	2.672	-4.390	-0.194	1.242	-2.249	-3.189	-0.022
4	A	4	THR	0	0.025	-0.010	5.360	3.602	3.654	-0.001	-0.003	-0.047	0.000
79	A	79	ASP	-1	-0.848	-0.898	5.079	-44.384	-44.387	-0.001	-0.008	0.012	0.000
81	A	81	LEU	0	0.069	0.043	4.035	4.354	4.510	0.000	-0.015	-0.141	0.000
132	A	132	LYS	1	0.811	0.934	2.625	40.390	41.167	0.523	-0.231	-1.069	-0.001
133	A	133	LEU	0	-0.005	-0.005	3.915	-6.503	-6.203	0.001	-0.100	-0.201	-0.001
135	A	135	SER	0	-0.033	-0.026	4.652	1.192	1.244	-0.001	-0.002	-0.048	0.000
136	A	136	ALA	0	-0.049	-0.029	2.365	-2.092	-1.879	1.179	-0.376	-1.016	-0.003
137	A	137	VAL	0	0.011	0.001	4.019	0.230	0.323	0.005	-0.018	-0.079	0.000
139	A	139	ILE	0	0.005	-0.002	3.849	0.499	0.723	0.002	-0.039	-0.186	0.000
5	A	5	ALA	0	0.036	0.001	8.530	-0.224	-0.224	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.888	-0.938	11.900	-17.867	-17.867	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.774	-0.868	6.433	-34.762	-34.762	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.847	0.898	7.552	33.080	33.080	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.012	0.026	10.252	1.118	1.118	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.025	0.024	12.422	1.055	1.055	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.008	0.002	9.031	0.883	0.883	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.013	-0.028	12.399	1.064	1.064	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.042	-0.025	14.678	1.419	1.419	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.007	0.006	16.270	0.750	0.750	0.000	0.000	0.000	0.000
15	A	15	TRP	0	-0.006	-0.007	15.201	0.419	0.419	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.045	-0.039	17.301	0.655	0.655	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.807	0.904	20.200	13.641	13.641	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.020	0.011	18.735	0.228	0.228	0.000	0.000	0.000	0.000
19	A	19	ASN	0	0.028	0.004	22.239	0.092	0.092	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.030	0.000	21.051	-0.136	-0.136	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.890	-0.937	23.090	-11.045	-11.045	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.838	-0.936	25.701	-10.579	-10.579	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.028	0.024	21.336	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.037	0.015	21.072	-0.457	-0.457	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.038	-0.017	22.113	-0.067	-0.067	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.848	-0.915	23.335	-11.371	-11.371	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.012	0.009	19.037	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.026	-0.012	21.076	-0.100	-0.100	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.032	-0.002	22.709	0.230	0.230	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.888	0.927	22.513	11.928	11.928	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.023	0.001	19.144	0.036	0.036	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.007	0.001	22.308	0.256	0.256	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.025	-0.007	25.874	0.427	0.427	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.033	-0.013	22.968	0.284	0.284	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.024	0.017	19.754	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.028	0.027	24.484	-0.151	-0.151	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.029	0.009	22.120	0.451	0.451	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.018	-0.027	21.858	0.060	0.060	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.008	-0.024	24.873	0.163	0.163	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.949	0.987	27.746	10.889	10.889	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.043	-0.020	24.033	0.127	0.127	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.026	-0.020	22.517	-0.122	-0.122	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.879	-0.910	28.359	-8.836	-8.836	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.056	0.015	30.889	0.211	0.211	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.066	-0.042	26.883	0.122	0.122	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.028	0.033	32.417	0.167	0.167	0.000	0.000	0.000	0.000
47	A	47	ASN	0	0.024	0.018	35.275	-0.109	-0.109	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.043	0.012	29.932	-0.179	-0.179	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.016	-0.023	33.304	-0.083	-0.083	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.044	0.022	34.715	0.114	0.114	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.063	0.020	31.275	-0.107	-0.107	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.021	0.010	32.296	-0.215	-0.215	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.032	0.004	35.005	0.015	0.015	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.016	0.004	28.450	-0.072	-0.072	0.000	0.000	0.000	0.000
55	A	55	LEU	0	0.035	0.014	27.708	-0.201	-0.201	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.031	0.024	30.972	0.013	0.013	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.032	-0.026	31.396	-0.065	-0.065	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.023	-0.003	31.373	-0.312	-0.312	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.877	0.942	30.420	9.261	9.261	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.018	0.022	26.430	-0.406	-0.406	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.872	0.927	26.208	9.012	9.012	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.011	0.003	26.592	-0.338	-0.338	0.000	0.000	0.000	0.000
63	A	63	HIS	0	-0.008	-0.016	22.144	0.033	0.033	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.065	0.028	22.425	-0.619	-0.619	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.811	0.908	21.640	10.263	10.263	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.927	0.982	21.846	11.364	11.364	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.006	0.005	17.367	-0.719	-0.719	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.037	0.027	17.102	-1.115	-1.115	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.008	-0.015	17.174	-0.690	-0.690	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.068	-0.040	15.253	-0.839	-0.839	0.000	0.000	0.000	0.000
71	A	71	PHE	0	0.040	0.004	10.802	-1.704	-1.704	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.038	0.023	12.760	-1.267	-1.267	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.905	-0.948	14.076	-18.778	-18.778	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.002	-0.006	8.850	-1.407	-1.407	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.004	-0.004	9.396	-2.616	-2.616	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.842	0.917	10.968	17.862	17.862	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.039	-0.019	9.990	1.015	1.015	0.000	0.000	0.000	0.000
78	A	78	MET	0	-0.003	0.003	5.870	-3.932	-3.932	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.062	-0.043	5.709	-6.684	-6.684	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.832	0.937	6.957	37.455	37.455	0.000	0.000	0.000	0.000
83	A	83	PRO	0	0.032	0.008	8.632	2.956	2.956	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.016	0.008	10.708	2.550	2.550	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.057	0.002	9.722	1.864	1.864	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.002	0.016	12.553	1.275	1.275	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.917	0.949	14.469	20.432	20.432	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.006	0.003	15.048	0.957	0.957	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.033	-0.017	13.831	0.506	0.506	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.903	-0.952	15.737	-14.126	-14.126	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.034	-0.014	19.340	0.766	0.766	0.000	0.000	0.000	0.000
92	A	92	HIS	0	-0.050	-0.061	17.270	1.170	1.170	0.000	0.000	0.000	0.000
93	A	93	CYS	0	0.002	0.029	18.620	0.382	0.382	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.773	-0.871	20.307	-13.931	-13.931	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.878	0.938	23.303	11.888	11.888	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.067	-0.034	21.708	0.653	0.653	0.000	0.000	0.000	0.000
97	A	97	HIS	0	-0.011	0.011	22.999	0.281	0.281	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.032	-0.010	19.098	0.348	0.348	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.825	-0.921	19.123	-16.386	-16.386	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.067	0.026	14.177	-0.166	-0.166	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.834	-0.886	14.615	-19.169	-19.169	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.034	-0.041	15.973	0.301	0.301	0.000	0.000	0.000	0.000
103	A	103	PHE	0	0.012	0.008	12.541	0.109	0.109	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.862	0.918	11.474	19.452	19.452	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.045	0.000	13.073	0.184	0.184	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.022	0.010	15.555	0.434	0.434	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.030	0.006	12.078	0.187	0.187	0.000	0.000	0.000	0.000
108	A	108	ASN	0	0.007	-0.015	13.022	-0.713	-0.713	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.021	-0.006	14.877	0.643	0.643	0.000	0.000	0.000	0.000
110	A	110	MET	0	-0.016	0.000	13.996	0.706	0.706	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.010	-0.001	12.500	0.340	0.340	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.004	0.006	15.315	0.708	0.708	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.031	-0.007	18.826	0.629	0.629	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.002	0.010	14.637	0.596	0.596	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.021	0.009	18.778	0.512	0.512	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.090	-0.056	20.404	0.688	0.688	0.000	0.000	0.000	0.000
117	A	117	HIS	0	-0.056	-0.027	21.882	0.510	0.510	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.021	0.014	19.683	0.237	0.237	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.019	0.020	22.811	0.309	0.309	0.000	0.000	0.000	0.000
120	A	120	LYS	1	0.922	0.952	22.768	10.080	10.080	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.823	-0.903	20.792	-13.164	-13.164	0.000	0.000	0.000	0.000
122	A	122	PHE	0	-0.014	-0.010	14.610	-0.870	-0.870	0.000	0.000	0.000	0.000
123	A	123	THR	0	-0.023	-0.028	18.153	-0.041	-0.041	0.000	0.000	0.000	0.000
124	A	124	PRO	0	0.046	0.011	16.483	-0.811	-0.811	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.835	-0.898	13.900	-16.617	-16.617	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.007	0.002	12.743	-1.753	-1.753	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.036	-0.016	12.828	-0.801	-0.801	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.002	-0.002	10.015	-1.492	-1.492	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.006	0.006	8.300	-2.869	-2.869	0.000	0.000	0.000	0.000
130	A	130	TRP	0	0.041	0.011	7.858	-3.444	-3.444	0.000	0.000	0.000	0.000
131	A	131	GLN	0	0.024	0.011	8.838	0.245	0.245	0.000	0.000	0.000	0.000
134	A	134	VAL	0	0.003	0.009	5.908	-1.091	-1.091	0.000	0.000	0.000	0.000
138	A	138	ALA	0	0.004	0.009	7.600	1.829	1.829	0.000	0.000	0.000	0.000
140	A	140	ALA	0	-0.058	-0.033	6.918	-0.758	-0.758	0.000	0.000	0.000	0.000
141	A	141	LEU	0	0.008	0.002	8.413	2.093	2.093	0.000	0.000	0.000	0.000
142	A	142	ALA	0	0.005	0.036	11.166	1.706	1.706	0.000	0.000	0.000	0.000
143	A	143	HIS	0	-0.002	0.000	10.763	-3.799	-3.799	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.793	0.869	12.597	15.959	15.959	0.000	0.000	0.000	0.000
145	A	145	TYR	-1	-0.898	-0.947	14.520	-19.718	-19.718	0.000	0.000	0.000	0.000

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