FMO DATABASE

FMODB ID: 1VQ2Z

Calculation Name: 2CCQ-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CCQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q96IV0

Base Structure: X-ray

Registration Date: 2025-10-11

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-746492.060781
FMO2-HF: Nuclear repulsion	707625.902004
FMO2-HF: Total energy	-38866.158777
FMO2-MP2: Total energy	-38979.724249

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:11:GLY)

Summations of interaction energy for fragment #1(A:11: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.
-205.909	-210.079	43.239	-22.087	-16.98	-0.209

Interaction energy analysis for fragmet #1(A:11:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.878

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	13	ALA	0	-0.034	-0.008	3.516	10.073	11.420	-0.006	-0.615	-0.726	-0.001
4	A	14	SER	0	-0.049	-0.044	3.758	7.531	7.980	0.002	-0.177	-0.274	0.000
5	A	15	PRO	0	0.022	0.001	5.063	-3.990	-3.984	-0.001	-0.006	0.002	0.000
7	A	17	VAL	0	0.004	0.009	2.022	0.763	-0.672	5.977	-3.047	-1.496	-0.009
8	A	18	ALA	0	-0.018	-0.004	4.370	-1.001	-0.867	-0.001	-0.024	-0.108	0.000
11	A	21	CYS	0	-0.070	-0.037	4.245	0.284	0.435	0.006	-0.055	-0.102	0.000
94	A	104	LEU	0	-0.060	-0.038	2.021	-10.168	-9.446	2.327	-1.065	-1.984	-0.014
95	A	105	ILE	0	0.038	0.012	1.997	-33.265	-33.431	8.915	-4.491	-4.258	-0.059
96	A	106	ALA	0	-0.040	-0.027	4.628	1.247	1.307	-0.001	-0.008	-0.051	0.000
97	A	107	ILE	0	-0.083	-0.044	2.476	1.364	1.665	1.650	-0.737	-1.214	-0.007
98	A	108	GLU	-1	-0.845	-0.900	1.853	-117.109	-122.823	24.372	-11.854	-6.804	-0.119
99	A	109	ARG	0	-0.091	-0.038	5.000	3.052	3.027	-0.001	-0.008	0.035	0.000
6	A	16	ALA	0	0.034	0.020	7.578	0.198	0.198	0.000	0.000	0.000	0.000
9	A	19	GLU	-1	-0.823	-0.882	5.629	-20.702	-20.702	0.000	0.000	0.000	0.000
10	A	20	LEU	0	-0.011	0.004	6.145	2.074	2.074	0.000	0.000	0.000	0.000
12	A	22	GLN	0	-0.093	-0.026	6.990	4.822	4.822	0.000	0.000	0.000	0.000
13	A	23	ASN	0	-0.049	-0.047	10.366	4.126	4.126	0.000	0.000	0.000	0.000
14	A	24	THR	0	0.005	0.008	11.812	-0.877	-0.877	0.000	0.000	0.000	0.000
15	A	25	PRO	0	0.058	0.014	12.093	-0.749	-0.749	0.000	0.000	0.000	0.000
16	A	26	GLU	-1	-0.857	-0.926	13.115	-18.205	-18.205	0.000	0.000	0.000	0.000
17	A	27	THR	0	0.008	0.002	14.099	-0.054	-0.054	0.000	0.000	0.000	0.000
18	A	28	PHE	0	0.033	0.024	5.233	0.404	0.404	0.000	0.000	0.000	0.000
19	A	29	LEU	0	-0.002	0.029	10.688	-1.236	-1.236	0.000	0.000	0.000	0.000
20	A	30	GLU	-1	-0.945	-0.968	12.295	-16.347	-16.347	0.000	0.000	0.000	0.000
21	A	31	ALA	0	0.042	0.019	11.650	0.198	0.198	0.000	0.000	0.000	0.000
22	A	32	SER	0	0.028	-0.020	8.437	0.178	0.178	0.000	0.000	0.000	0.000
23	A	33	LYS	1	0.944	0.980	10.074	17.063	17.063	0.000	0.000	0.000	0.000
24	A	34	LEU	0	-0.045	-0.003	13.259	0.877	0.877	0.000	0.000	0.000	0.000
25	A	35	LEU	0	0.027	0.012	9.045	0.781	0.781	0.000	0.000	0.000	0.000
26	A	36	LEU	0	0.010	0.008	8.311	0.492	0.492	0.000	0.000	0.000	0.000
27	A	37	THR	0	-0.077	-0.044	12.102	1.717	1.717	0.000	0.000	0.000	0.000
28	A	38	TYR	0	-0.021	-0.028	14.807	1.249	1.249	0.000	0.000	0.000	0.000
29	A	39	ALA	0	0.054	0.028	12.331	0.941	0.941	0.000	0.000	0.000	0.000
30	A	40	ASP	-1	-0.760	-0.856	13.738	-21.564	-21.564	0.000	0.000	0.000	0.000
31	A	41	ASN	0	-0.054	-0.023	16.102	1.222	1.222	0.000	0.000	0.000	0.000
32	A	42	ILE	0	-0.016	0.004	17.275	0.948	0.948	0.000	0.000	0.000	0.000
33	A	43	LEU	0	-0.013	-0.013	13.536	0.729	0.729	0.000	0.000	0.000	0.000
34	A	44	ARG	1	0.861	0.949	18.184	15.912	15.912	0.000	0.000	0.000	0.000
35	A	45	ASN	0	-0.051	-0.032	21.011	0.550	0.550	0.000	0.000	0.000	0.000
36	A	46	PRO	0	0.083	0.053	21.379	0.291	0.291	0.000	0.000	0.000	0.000
37	A	47	ASN	0	-0.017	-0.021	22.891	-0.200	-0.200	0.000	0.000	0.000	0.000
38	A	48	ASP	-1	-0.857	-0.922	25.504	-10.939	-10.939	0.000	0.000	0.000	0.000
39	A	49	GLU	-1	-0.940	-0.985	24.977	-10.956	-10.956	0.000	0.000	0.000	0.000
40	A	50	LYS	1	0.885	0.955	25.306	11.170	11.170	0.000	0.000	0.000	0.000
41	A	51	TYR	0	-0.026	-0.029	21.200	-0.153	-0.153	0.000	0.000	0.000	0.000
42	A	52	ARG	1	0.805	0.915	20.659	13.212	13.212	0.000	0.000	0.000	0.000
43	A	53	SER	0	-0.009	0.007	21.973	0.035	0.035	0.000	0.000	0.000	0.000
44	A	54	ILE	0	0.009	0.014	17.442	0.311	0.311	0.000	0.000	0.000	0.000
45	A	55	ARG	1	0.885	0.956	21.661	11.163	11.163	0.000	0.000	0.000	0.000
46	A	56	ILE	0	0.086	0.039	21.829	-0.213	-0.213	0.000	0.000	0.000	0.000
47	A	57	GLY	0	0.024	0.002	23.290	-0.132	-0.132	0.000	0.000	0.000	0.000
48	A	58	ASN	0	-0.031	-0.016	22.590	0.154	0.154	0.000	0.000	0.000	0.000
49	A	59	THR	0	0.039	0.029	23.413	-0.461	-0.461	0.000	0.000	0.000	0.000
50	A	60	ALA	0	0.001	0.023	19.961	-0.129	-0.129	0.000	0.000	0.000	0.000
51	A	61	PHE	0	0.069	0.028	17.285	-0.587	-0.587	0.000	0.000	0.000	0.000
52	A	62	SER	0	-0.023	-0.045	19.143	-0.394	-0.394	0.000	0.000	0.000	0.000
53	A	63	THR	0	-0.047	-0.043	21.375	-0.044	-0.044	0.000	0.000	0.000	0.000
54	A	64	ARG	1	0.961	0.984	16.818	15.195	15.195	0.000	0.000	0.000	0.000
55	A	65	LEU	0	-0.028	-0.015	12.973	-1.214	-1.214	0.000	0.000	0.000	0.000
56	A	66	LEU	0	-0.007	0.003	15.789	-0.355	-0.355	0.000	0.000	0.000	0.000
57	A	67	PRO	0	-0.041	-0.008	18.258	0.149	0.149	0.000	0.000	0.000	0.000
58	A	68	VAL	0	-0.023	-0.006	12.538	-0.028	-0.028	0.000	0.000	0.000	0.000
59	A	69	ARG	1	0.873	0.907	12.067	21.917	21.917	0.000	0.000	0.000	0.000
60	A	70	GLY	0	0.082	0.031	9.667	-1.738	-1.738	0.000	0.000	0.000	0.000
61	A	71	ALA	0	0.003	0.011	9.659	-1.961	-1.961	0.000	0.000	0.000	0.000
62	A	72	VAL	0	-0.003	-0.007	11.369	-0.061	-0.061	0.000	0.000	0.000	0.000
63	A	73	GLU	-1	-0.848	-0.930	10.867	-21.620	-21.620	0.000	0.000	0.000	0.000
64	A	74	CYS	0	-0.034	-0.015	7.340	-2.358	-2.358	0.000	0.000	0.000	0.000
65	A	75	LEU	0	-0.014	-0.005	9.374	-0.078	-0.078	0.000	0.000	0.000	0.000
66	A	76	PHE	0	-0.001	0.006	12.743	0.609	0.609	0.000	0.000	0.000	0.000
67	A	77	GLU	-1	-0.779	-0.859	8.004	-34.723	-34.723	0.000	0.000	0.000	0.000
68	A	78	MET	0	-0.099	-0.028	9.151	0.847	0.847	0.000	0.000	0.000	0.000
69	A	79	GLY	0	0.003	0.012	11.928	1.049	1.049	0.000	0.000	0.000	0.000
70	A	80	PHE	0	-0.073	-0.062	14.795	1.400	1.400	0.000	0.000	0.000	0.000
71	A	81	GLU	-1	-0.835	-0.916	17.258	-14.075	-14.075	0.000	0.000	0.000	0.000
72	A	82	GLU	-1	-0.921	-0.973	20.095	-14.276	-14.276	0.000	0.000	0.000	0.000
73	A	83	GLY	0	0.008	0.005	21.682	0.411	0.411	0.000	0.000	0.000	0.000
74	A	84	GLU	-1	-0.942	-0.977	25.100	-10.149	-10.149	0.000	0.000	0.000	0.000
75	A	85	THR	0	-0.017	-0.026	27.252	0.154	0.154	0.000	0.000	0.000	0.000
76	A	86	HIS	0	-0.023	-0.006	23.835	-0.040	-0.040	0.000	0.000	0.000	0.000
77	A	87	LEU	0	0.051	0.051	17.008	0.028	0.028	0.000	0.000	0.000	0.000
78	A	88	ILE	0	-0.027	-0.019	20.924	0.177	0.177	0.000	0.000	0.000	0.000
79	A	89	PHE	0	0.030	0.028	16.238	-0.201	-0.201	0.000	0.000	0.000	0.000
80	A	90	PRO	0	0.022	0.011	19.943	0.794	0.794	0.000	0.000	0.000	0.000
81	A	91	LYS	1	0.954	0.958	22.175	10.373	10.373	0.000	0.000	0.000	0.000
82	A	92	LYS	1	0.847	0.922	22.617	13.223	13.223	0.000	0.000	0.000	0.000
83	A	93	ALA	0	-0.014	0.010	18.467	-0.148	-0.148	0.000	0.000	0.000	0.000
84	A	94	SER	0	-0.022	-0.025	16.844	-0.280	-0.280	0.000	0.000	0.000	0.000
85	A	95	VAL	0	0.057	0.009	16.433	-0.886	-0.886	0.000	0.000	0.000	0.000
86	A	96	GLU	-1	-0.824	-0.891	14.623	-18.397	-18.397	0.000	0.000	0.000	0.000
87	A	97	GLN	0	-0.026	-0.026	10.596	-2.049	-2.049	0.000	0.000	0.000	0.000
88	A	98	LEU	0	0.010	0.008	11.129	-2.454	-2.454	0.000	0.000	0.000	0.000
89	A	99	GLN	0	-0.041	-0.040	10.948	-0.476	-0.476	0.000	0.000	0.000	0.000
90	A	100	LYS	1	0.951	0.984	7.750	28.006	28.006	0.000	0.000	0.000	0.000
91	A	101	ILE	0	-0.014	-0.006	6.399	-6.696	-6.696	0.000	0.000	0.000	0.000
92	A	102	ARG	1	0.811	0.883	6.121	22.066	22.066	0.000	0.000	0.000	0.000
93	A	103	ASP	-1	-0.840	-0.929	6.617	-33.700	-33.700	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:GLY)