FMO DATABASE

FMODB ID: VV761

Calculation Name: 2CWQ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CWQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SMF5

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-913115.384406
FMO2-HF: Nuclear repulsion	865779.24839
FMO2-HF: Total energy	-47336.136015
FMO2-MP2: Total energy	-47473.335766

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:-9:SER)

Summations of interaction energy for fragment #1(A:-9:SER)

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.
19.092	21.505	10.059	-6.588	-5.882	-0.069

Interaction energy analysis for fragmet #1(A:-9:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.823 / q_NPA : 0.902

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

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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	LEU	0	-0.027	-0.001	3.749	-7.027	-5.433	-0.007	-0.879	-0.707	-0.001
6	A	-4	ARG	1	0.892	0.933	4.698	53.662	53.754	-0.001	-0.003	-0.088	0.000
57	A	48	GLU	-1	-0.842	-0.931	1.910	-99.035	-99.551	9.862	-5.200	-4.146	-0.065
58	A	49	LYS	1	0.916	0.963	3.600	29.265	29.671	0.004	-0.155	-0.255	-0.001
63	A	54	GLU	-1	-0.789	-0.906	2.660	-46.918	-46.324	0.202	-0.221	-0.575	-0.002
89	A	80	ARG	1	0.864	0.931	4.154	48.033	48.276	-0.001	-0.130	-0.111	0.000
4	A	-6	VAL	0	0.044	0.027	5.850	3.379	3.379	0.000	0.000	0.000	0.000
5	A	-5	PRO	0	0.004	0.006	5.027	-6.590	-6.590	0.000	0.000	0.000	0.000
7	A	-3	GLY	0	0.048	0.021	7.475	2.410	2.410	0.000	0.000	0.000	0.000
8	A	-2	SER	0	-0.030	-0.021	8.711	2.492	2.492	0.000	0.000	0.000	0.000
9	A	-1	HIS	0	0.033	0.013	11.179	0.405	0.405	0.000	0.000	0.000	0.000
10	A	1	MET	0	-0.039	-0.021	13.938	1.409	1.409	0.000	0.000	0.000	0.000
11	A	2	ASP	-1	-0.810	-0.895	13.656	-20.940	-20.940	0.000	0.000	0.000	0.000
12	A	3	ARG	1	0.913	0.946	16.457	15.283	15.283	0.000	0.000	0.000	0.000
13	A	4	THR	0	-0.009	-0.020	18.326	0.474	0.474	0.000	0.000	0.000	0.000
14	A	5	HIS	0	0.082	0.030	16.886	-0.968	-0.968	0.000	0.000	0.000	0.000
15	A	6	GLU	-1	-0.880	-0.906	15.633	-16.861	-16.861	0.000	0.000	0.000	0.000
16	A	7	ARG	1	0.835	0.914	9.224	25.730	25.730	0.000	0.000	0.000	0.000
17	A	8	VAL	0	-0.017	-0.007	10.864	-2.565	-2.565	0.000	0.000	0.000	0.000
18	A	9	LEU	0	0.013	0.005	12.057	-0.935	-0.935	0.000	0.000	0.000	0.000
19	A	10	GLN	0	0.062	0.018	12.921	-0.380	-0.380	0.000	0.000	0.000	0.000
20	A	11	ALA	0	0.025	0.027	7.879	-0.793	-0.793	0.000	0.000	0.000	0.000
21	A	12	MET	0	-0.007	-0.002	9.591	-1.383	-1.383	0.000	0.000	0.000	0.000
22	A	13	ALA	0	0.012	-0.002	11.712	0.388	0.388	0.000	0.000	0.000	0.000
23	A	14	GLU	-1	-0.967	-0.967	8.772	-30.361	-30.361	0.000	0.000	0.000	0.000
24	A	15	ASN	0	-0.048	-0.037	6.357	-2.545	-2.545	0.000	0.000	0.000	0.000
25	A	16	LEU	0	-0.039	-0.015	9.251	0.323	0.323	0.000	0.000	0.000	0.000
26	A	17	GLY	0	-0.010	0.000	12.722	1.251	1.251	0.000	0.000	0.000	0.000
27	A	18	GLU	-1	-0.890	-0.951	15.333	-15.203	-15.203	0.000	0.000	0.000	0.000
28	A	19	GLY	0	-0.044	-0.018	16.317	0.926	0.926	0.000	0.000	0.000	0.000
29	A	20	LEU	0	-0.013	-0.008	15.145	-0.174	-0.174	0.000	0.000	0.000	0.000
30	A	21	PRO	0	-0.003	-0.003	16.859	1.116	1.116	0.000	0.000	0.000	0.000
31	A	22	ARG	1	1.009	0.994	19.926	11.109	11.109	0.000	0.000	0.000	0.000
32	A	23	ALA	0	0.024	0.011	21.627	0.304	0.304	0.000	0.000	0.000	0.000
33	A	24	ILE	0	0.019	0.013	15.943	0.131	0.131	0.000	0.000	0.000	0.000
34	A	25	PRO	0	0.040	0.005	19.373	0.011	0.011	0.000	0.000	0.000	0.000
35	A	26	LEU	0	0.011	0.011	21.326	0.377	0.377	0.000	0.000	0.000	0.000
36	A	27	LEU	0	-0.002	0.002	19.844	0.365	0.365	0.000	0.000	0.000	0.000
37	A	28	ALA	0	-0.009	-0.015	19.275	0.100	0.100	0.000	0.000	0.000	0.000
38	A	29	GLU	-1	-0.922	-0.957	21.118	-10.999	-10.999	0.000	0.000	0.000	0.000
39	A	30	LYS	1	0.879	0.945	24.871	11.056	11.056	0.000	0.000	0.000	0.000
40	A	31	ALA	0	-0.015	-0.004	24.223	0.380	0.380	0.000	0.000	0.000	0.000
41	A	32	PRO	0	0.061	0.042	20.881	-0.597	-0.597	0.000	0.000	0.000	0.000
42	A	33	GLY	0	0.024	0.001	19.671	-0.848	-0.848	0.000	0.000	0.000	0.000
43	A	34	LEU	0	0.013	0.006	20.189	-0.478	-0.478	0.000	0.000	0.000	0.000
44	A	35	LEU	0	-0.013	-0.001	15.528	-0.659	-0.659	0.000	0.000	0.000	0.000
45	A	36	LEU	0	0.000	0.003	15.182	-1.450	-1.450	0.000	0.000	0.000	0.000
46	A	37	GLU	-1	-0.772	-0.844	15.542	-17.353	-17.353	0.000	0.000	0.000	0.000
47	A	38	HIS	0	-0.008	0.006	13.991	0.036	0.036	0.000	0.000	0.000	0.000
48	A	39	GLY	0	0.042	0.020	12.097	-1.165	-1.165	0.000	0.000	0.000	0.000
49	A	40	ARG	1	0.810	0.870	11.817	15.103	15.103	0.000	0.000	0.000	0.000
50	A	41	SER	0	-0.051	-0.030	13.912	-0.363	-0.363	0.000	0.000	0.000	0.000
51	A	42	TRP	0	0.049	0.004	8.374	0.611	0.611	0.000	0.000	0.000	0.000
52	A	43	THR	0	-0.047	-0.051	7.894	-0.891	-0.891	0.000	0.000	0.000	0.000
53	A	44	TYR	0	-0.046	-0.013	10.150	-0.530	-0.530	0.000	0.000	0.000	0.000
54	A	45	ALA	0	0.013	0.011	13.249	0.329	0.329	0.000	0.000	0.000	0.000
55	A	46	MET	0	-0.086	-0.031	8.271	-0.339	-0.339	0.000	0.000	0.000	0.000
56	A	47	PRO	0	0.078	0.047	7.729	-4.563	-4.563	0.000	0.000	0.000	0.000
59	A	50	GLY	0	0.053	0.025	6.360	2.649	2.649	0.000	0.000	0.000	0.000
60	A	51	ALA	0	0.005	0.004	8.865	-0.597	-0.597	0.000	0.000	0.000	0.000
61	A	52	LEU	0	0.031	0.029	9.590	0.993	0.993	0.000	0.000	0.000	0.000
62	A	53	ASP	-1	-0.792	-0.874	6.205	-31.004	-31.004	0.000	0.000	0.000	0.000
64	A	55	LYS	1	0.982	1.014	5.778	23.576	23.576	0.000	0.000	0.000	0.000
65	A	56	THR	0	-0.008	-0.030	8.775	2.573	2.573	0.000	0.000	0.000	0.000
66	A	57	ARG	1	0.780	0.883	5.857	39.717	39.717	0.000	0.000	0.000	0.000
67	A	58	THR	0	-0.002	-0.020	8.283	1.498	1.498	0.000	0.000	0.000	0.000
68	A	59	LEU	0	-0.030	-0.018	10.913	1.625	1.625	0.000	0.000	0.000	0.000
69	A	60	ILE	0	0.024	0.021	13.571	1.418	1.418	0.000	0.000	0.000	0.000
70	A	61	LEU	0	0.007	-0.002	11.758	1.162	1.162	0.000	0.000	0.000	0.000
71	A	62	LEU	0	-0.025	-0.009	14.973	1.015	1.015	0.000	0.000	0.000	0.000
72	A	63	GLY	0	0.035	0.012	16.791	0.986	0.986	0.000	0.000	0.000	0.000
73	A	64	ILE	0	0.023	0.009	17.706	0.835	0.835	0.000	0.000	0.000	0.000
74	A	65	ALA	0	-0.029	0.008	18.852	0.743	0.743	0.000	0.000	0.000	0.000
75	A	66	LEU	0	-0.031	-0.028	20.423	0.692	0.692	0.000	0.000	0.000	0.000
76	A	67	ALA	0	-0.016	0.001	22.804	0.584	0.584	0.000	0.000	0.000	0.000
77	A	68	THR	0	-0.064	-0.062	22.924	0.429	0.429	0.000	0.000	0.000	0.000
78	A	69	GLY	0	0.041	0.041	25.217	0.341	0.341	0.000	0.000	0.000	0.000
79	A	70	SER	0	0.009	0.009	21.768	0.205	0.205	0.000	0.000	0.000	0.000
80	A	71	GLU	-1	-0.873	-0.953	22.025	-12.277	-12.277	0.000	0.000	0.000	0.000
81	A	72	ALA	0	-0.023	-0.015	21.127	-0.533	-0.533	0.000	0.000	0.000	0.000
82	A	73	CYS	0	-0.017	-0.006	18.056	-0.729	-0.729	0.000	0.000	0.000	0.000
83	A	74	VAL	0	0.041	0.025	17.370	-1.081	-1.081	0.000	0.000	0.000	0.000
84	A	75	LYS	1	0.897	0.951	18.169	13.795	13.795	0.000	0.000	0.000	0.000
85	A	76	ALA	0	0.025	0.021	14.967	-0.671	-0.671	0.000	0.000	0.000	0.000
86	A	77	MET	0	-0.004	-0.004	11.994	-2.112	-2.112	0.000	0.000	0.000	0.000
87	A	78	ALA	0	0.037	0.022	13.508	-0.975	-0.975	0.000	0.000	0.000	0.000
88	A	79	HIS	0	-0.068	-0.043	14.393	0.173	0.173	0.000	0.000	0.000	0.000
90	A	81	ALA	0	0.015	-0.001	9.859	-2.105	-2.105	0.000	0.000	0.000	0.000
91	A	82	LYS	1	0.942	0.974	11.503	16.480	16.480	0.000	0.000	0.000	0.000
92	A	83	ARG	1	0.873	0.930	9.407	23.720	23.720	0.000	0.000	0.000	0.000
93	A	84	LEU	0	-0.046	-0.013	4.840	-2.504	-2.504	0.000	0.000	0.000	0.000
94	A	85	GLY	0	0.007	0.019	8.462	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	86	LEU	0	-0.056	-0.029	9.062	1.042	1.042	0.000	0.000	0.000	0.000
96	A	87	SER	0	0.011	0.004	12.587	0.931	0.931	0.000	0.000	0.000	0.000
97	A	88	LYS	1	1.015	0.994	16.180	12.273	12.273	0.000	0.000	0.000	0.000
98	A	89	GLU	-1	-0.886	-0.941	19.324	-12.561	-12.561	0.000	0.000	0.000	0.000
99	A	90	ALA	0	0.020	0.018	15.795	0.249	0.249	0.000	0.000	0.000	0.000
100	A	91	LEU	0	-0.006	0.011	14.762	-0.099	-0.099	0.000	0.000	0.000	0.000
101	A	92	LEU	0	0.017	-0.005	18.189	0.418	0.418	0.000	0.000	0.000	0.000
102	A	93	GLU	-1	-0.896	-0.945	19.832	-12.522	-12.522	0.000	0.000	0.000	0.000
103	A	94	THR	0	0.010	-0.008	17.023	0.119	0.119	0.000	0.000	0.000	0.000
104	A	95	LEU	0	-0.010	0.002	19.715	0.284	0.284	0.000	0.000	0.000	0.000
105	A	96	LYS	1	0.850	0.924	22.710	12.467	12.467	0.000	0.000	0.000	0.000
106	A	97	ILE	0	0.016	0.009	20.573	0.432	0.432	0.000	0.000	0.000	0.000
107	A	98	ALA	0	0.012	0.009	21.989	0.287	0.287	0.000	0.000	0.000	0.000
108	A	99	ARG	1	0.947	0.969	23.829	10.287	10.287	0.000	0.000	0.000	0.000
109	A	100	GLN	0	-0.032	-0.021	26.906	0.376	0.376	0.000	0.000	0.000	0.000
110	A	101	ALA	0	-0.016	-0.004	25.035	0.296	0.296	0.000	0.000	0.000	0.000
111	A	102	GLN	0	0.033	0.013	27.152	0.246	0.246	0.000	0.000	0.000	0.000
112	A	103	ALA	0	-0.013	0.000	29.529	0.338	0.338	0.000	0.000	0.000	0.000
113	A	104	ASN	0	0.015	-0.001	28.616	0.504	0.504	0.000	0.000	0.000	0.000
114	A	105	ALA	0	0.005	0.009	30.052	0.228	0.228	0.000	0.000	0.000	0.000
115	A	106	VAL	0	-0.024	-0.012	32.043	0.237	0.237	0.000	0.000	0.000	0.000
116	A	107	LEU	0	0.000	-0.005	35.065	0.240	0.240	0.000	0.000	0.000	0.000
117	A	108	GLY	0	-0.019	-0.003	34.788	0.182	0.182	0.000	0.000	0.000	0.000
118	A	109	HIS	0	-0.025	-0.025	33.105	0.299	0.299	0.000	0.000	0.000	0.000
119	A	110	ALA	0	0.002	0.009	37.648	0.200	0.200	0.000	0.000	0.000	0.000
120	A	111	ALA	0	0.021	0.017	40.234	0.206	0.206	0.000	0.000	0.000	0.000
121	A	112	PRO	0	0.001	-0.016	41.641	0.161	0.161	0.000	0.000	0.000	0.000
122	A	113	LEU	0	-0.039	-0.004	44.236	0.142	0.142	0.000	0.000	0.000	0.000
123	A	114	LEU	0	-0.027	-0.031	41.716	0.109	0.109	0.000	0.000	0.000	0.000
124	A	115	GLU	-1	-0.947	-0.967	45.957	-6.611	-6.611	0.000	0.000	0.000	0.000
125	A	116	VAL	0	-0.117	-0.052	48.231	0.135	0.135	0.000	0.000	0.000	0.000
126	A	117	LEU	-1	-0.978	-0.965	47.430	-5.952	-5.952	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-9:SER)