FMO DATABASE

FMODB ID: Q548Y

Calculation Name: 1CCR-A-Xray547

Preferred Name:

Target Type:

Ligand Name: heme c | n-trimethyllysine | acetyl group

Ligand 3-letter code: HEC | M3L | ACE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CCR

Chain ID: A

ChEMBL ID:

UniProt ID: Q0DI31

Base Structure: X-ray

Registration Date: 2025-10-06

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	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-857517.312224
FMO2-HF: Nuclear repulsion	814771.605309
FMO2-HF: Total energy	-42745.706915
FMO2-MP2: Total energy	-42869.86398

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:ALA)

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

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.
-37.592	-35.816	18.155	-11.738	-8.193	-0.132

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.762 / q_NPA : 0.871

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	0.051	0.004	3.755	-8.059	-6.630	-0.014	-0.810	-0.606	0.000
5	A	5	GLU	-1	-0.856	-0.909	1.739	-127.015	-127.201	18.168	-10.798	-7.183	-0.132
6	A	6	ALA	0	-0.067	-0.018	4.500	-1.185	-1.088	-0.001	-0.004	-0.092	0.000
73	A	73	TYR	0	-0.037	-0.020	3.051	4.881	5.269	0.003	-0.122	-0.269	0.000
96	A	96	PRO	0	0.034	0.011	4.400	2.467	2.515	-0.001	-0.004	-0.043	0.000
4	A	4	SER	0	0.014	0.004	6.175	2.388	2.388	0.000	0.000	0.000	0.000
7	A	7	PRO	0	-0.022	-0.016	6.115	3.500	3.500	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.029	0.024	9.339	0.215	0.215	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.015	0.013	12.706	0.092	0.092	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.003	-0.016	13.773	1.901	1.901	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.096	0.045	17.234	-0.093	-0.093	0.000	0.000	0.000	0.000
12	A	12	LYS	1	1.016	0.999	19.474	12.819	12.819	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.069	-0.034	17.243	0.540	0.540	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.039	0.009	17.213	0.052	0.052	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.785	-0.874	17.990	-12.065	-12.065	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.890	0.951	20.803	14.845	14.845	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.015	0.020	14.982	0.319	0.319	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.073	0.028	19.097	0.199	0.199	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.841	0.894	20.898	12.496	12.496	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.058	-0.043	21.634	0.206	0.206	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.872	0.950	16.406	17.967	17.967	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.047	-0.011	19.463	-0.583	-0.583	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.041	0.025	22.174	0.392	0.392	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.006	0.010	25.597	0.324	0.324	0.000	0.000	0.000	0.000
25	A	25	CYS	0	-0.062	-0.035	24.526	0.511	0.511	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.002	-0.002	22.645	-0.319	-0.319	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.023	-0.027	26.026	0.027	0.027	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.008	0.000	23.753	-0.400	-0.400	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.815	-0.891	26.595	-10.639	-10.639	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.893	0.928	30.039	10.532	10.532	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.018	0.010	32.014	0.254	0.254	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.021	-0.002	31.856	0.232	0.232	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.031	0.024	33.776	0.014	0.014	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.011	-0.002	30.687	-0.617	-0.617	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.906	0.950	29.014	10.999	10.999	0.000	0.000	0.000	0.000
36	A	36	GLN	0	0.028	0.020	27.859	0.122	0.122	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.012	0.014	25.891	-0.085	-0.085	0.000	0.000	0.000	0.000
38	A	38	PRO	0	-0.025	-0.009	24.893	0.382	0.382	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.019	-0.019	26.168	-0.725	-0.725	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.048	-0.033	21.093	-0.195	-0.195	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.004	0.002	24.189	-0.127	-0.127	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.019	0.011	25.751	0.188	0.188	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.056	-0.024	18.680	-0.051	-0.051	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.003	-0.013	15.992	-0.618	-0.618	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.067	0.052	20.069	0.779	0.779	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.802	0.888	21.855	12.944	12.944	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.029	0.001	21.596	-0.435	-0.435	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.039	-0.015	20.595	0.304	0.304	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.006	-0.020	22.667	0.469	0.469	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.005	-0.010	25.922	0.611	0.611	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.022	0.001	26.916	0.227	0.227	0.000	0.000	0.000	0.000
52	A	52	PRO	0	0.053	0.029	29.136	0.149	0.149	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.053	0.018	32.966	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	TYR	0	-0.053	-0.035	27.431	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.015	0.013	31.133	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	56	TYR	0	0.029	0.025	24.534	0.072	0.072	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.037	-0.031	24.917	0.326	0.326	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.036	0.002	27.530	-0.127	-0.127	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.042	0.034	22.445	-0.055	-0.055	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.878	-0.956	22.156	-14.399	-14.399	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.910	0.969	23.268	10.466	10.466	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.019	-0.018	24.861	0.097	0.097	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.028	-0.011	17.020	0.097	0.097	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.012	0.010	20.388	-0.538	-0.538	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.006	-0.002	16.315	-0.325	-0.325	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.029	0.022	18.896	0.475	0.475	0.000	0.000	0.000	0.000
67	A	67	TRP	0	-0.023	-0.010	14.913	-1.848	-1.848	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.763	-0.893	15.399	-16.243	-16.243	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.817	-0.898	11.790	-21.977	-21.977	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.005	-0.013	9.734	-3.044	-3.044	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.031	-0.001	9.934	-2.295	-2.295	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.029	0.014	12.459	-0.187	-0.187	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.880	-0.931	6.441	-45.685	-45.685	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.008	-0.013	8.640	1.352	1.352	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.015	-0.020	11.577	1.145	1.145	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.021	0.018	6.022	0.771	0.771	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.064	-0.067	10.094	2.360	2.360	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.095	0.060	12.835	0.164	0.164	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.934	0.972	15.604	14.295	14.295	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.903	0.954	12.883	20.958	20.958	0.000	0.000	0.000	0.000
82	A	82	TYR	0	0.039	0.038	11.063	-0.341	-0.341	0.000	0.000	0.000	0.000
83	A	83	ILE	0	0.013	0.006	14.231	0.543	0.543	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.028	0.012	17.200	0.680	0.680	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.041	0.023	19.927	0.511	0.511	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.016	0.007	19.269	0.858	0.858	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.885	0.934	22.397	10.873	10.873	0.000	0.000	0.000	0.000
88	A	88	MET	0	0.005	0.021	18.257	0.280	0.280	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.018	-0.019	21.362	-0.456	-0.456	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.047	0.020	15.488	0.095	0.095	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.002	-0.002	17.108	-0.513	-0.513	0.000	0.000	0.000	0.000
92	A	92	GLY	0	-0.002	0.007	13.489	-1.004	-1.004	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.063	-0.024	11.893	0.847	0.847	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.909	0.952	10.078	20.753	20.753	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.962	0.973	8.263	23.335	23.335	0.000	0.000	0.000	0.000
97	A	97	GLN	0	0.004	-0.010	6.684	0.518	0.518	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.836	-0.939	10.159	-20.891	-20.891	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.832	0.919	5.257	44.022	44.022	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.088	0.047	9.111	1.380	1.380	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.804	-0.890	10.832	-19.295	-19.295	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.033	-0.019	14.050	1.332	1.332	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.009	0.005	10.907	1.102	1.102	0.000	0.000	0.000	0.000
104	A	104	SER	0	-0.010	-0.023	14.174	0.887	0.887	0.000	0.000	0.000	0.000
105	A	105	TYR	0	-0.026	-0.017	16.469	1.021	1.021	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.017	-0.006	17.266	0.686	0.686	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.828	0.919	15.041	20.488	20.488	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.936	-0.954	20.115	-11.913	-11.913	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.009	-0.010	22.814	0.410	0.410	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.110	-0.067	21.959	0.279	0.279	0.000	0.000	0.000	0.000
111	A	111	SER	-1	-0.864	-0.912	24.482	-11.062	-11.062	0.000	0.000	0.000	0.000

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