FMO DATABASE

FMODB ID: 15Z3Z

Calculation Name: 2CWP-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CWP

Chain ID: A

ChEMBL ID:

UniProt ID: O58023

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-849710.00613
FMO2-HF: Nuclear repulsion	806562.361186
FMO2-HF: Total energy	-43147.644944
FMO2-MP2: Total energy	-43274.826139

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:4:MET)

Summations of interaction energy for fragment #1(A:4:MET)

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.
-19.935	-18.495	-0.002	-0.456	-0.982	-0.001

Interaction energy analysis for fragmet #1(A:4:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.822 / q_NPA : 0.892

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	6	LEU	0	-0.005	0.010	3.449	1.119	2.559	-0.002	-0.456	-0.982	-0.001
4	A	7	TYR	0	-0.003	-0.003	5.678	5.033	5.033	0.000	0.000	0.000	0.000
5	A	8	ASP	-1	-0.848	-0.926	9.369	-20.502	-20.502	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.032	0.009	12.547	-0.053	-0.053	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.883	-0.945	15.367	-15.494	-15.494	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.867	-0.922	13.398	-19.228	-19.228	0.000	0.000	0.000	0.000
9	A	12	PHE	0	-0.023	-0.013	13.756	0.105	0.105	0.000	0.000	0.000	0.000
10	A	13	TRP	0	0.028	0.008	15.598	0.853	0.853	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.790	0.918	16.495	19.567	19.567	0.000	0.000	0.000	0.000
12	A	15	PHE	0	-0.034	-0.007	15.370	0.803	0.803	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.027	-0.021	19.677	0.292	0.292	0.000	0.000	0.000	0.000
14	A	17	MET	0	0.015	0.008	17.931	0.122	0.122	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.921	0.965	22.724	10.688	10.688	0.000	0.000	0.000	0.000
16	A	19	VAL	0	0.046	0.031	26.163	-0.185	-0.185	0.000	0.000	0.000	0.000
17	A	20	GLY	0	-0.008	-0.001	28.186	0.325	0.325	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.002	-0.011	30.257	-0.105	-0.105	0.000	0.000	0.000	0.000
19	A	22	VAL	0	-0.024	-0.012	31.253	0.097	0.097	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.865	0.943	33.840	8.134	8.134	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.874	0.928	36.188	7.803	7.803	0.000	0.000	0.000	0.000
22	A	25	ALA	0	-0.024	-0.011	33.637	-0.321	-0.321	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.873	-0.917	35.205	-7.589	-7.589	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.895	0.946	33.691	8.689	8.689	0.000	0.000	0.000	0.000
25	A	28	ILE	0	-0.008	0.007	31.943	0.268	0.268	0.000	0.000	0.000	0.000
26	A	29	LYS	1	1.004	0.997	35.594	7.217	7.217	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.906	0.937	37.786	7.678	7.678	0.000	0.000	0.000	0.000
28	A	31	THR	0	-0.012	0.003	32.365	-0.218	-0.218	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.985	0.978	32.074	8.815	8.815	0.000	0.000	0.000	0.000
30	A	33	LYS	1	0.947	0.964	24.608	11.798	11.798	0.000	0.000	0.000	0.000
31	A	34	LEU	0	-0.019	0.014	27.880	-0.181	-0.181	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.033	0.024	29.870	0.418	0.418	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.907	0.960	30.519	8.195	8.195	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.021	0.011	28.644	0.219	0.219	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.036	-0.020	32.734	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	39	VAL	0	0.006	0.008	29.957	0.063	0.063	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.820	-0.905	33.226	-8.327	-8.327	0.000	0.000	0.000	0.000
38	A	41	PHE	0	0.022	-0.009	28.024	-0.260	-0.260	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.042	0.023	33.147	-0.083	-0.083	0.000	0.000	0.000	0.000
40	A	43	ASN	0	-0.073	-0.045	33.628	0.042	0.042	0.000	0.000	0.000	0.000
41	A	44	GLU	-1	-0.901	-0.944	31.400	-9.723	-9.723	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.918	-0.960	35.237	-8.138	-8.138	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.775	0.884	28.732	10.392	10.392	0.000	0.000	0.000	0.000
44	A	47	THR	0	-0.024	-0.010	32.596	0.147	0.147	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.029	-0.002	26.719	-0.255	-0.255	0.000	0.000	0.000	0.000
46	A	49	VAL	0	-0.016	-0.018	28.026	0.314	0.314	0.000	0.000	0.000	0.000
47	A	50	THR	0	0.035	0.021	25.427	-0.570	-0.570	0.000	0.000	0.000	0.000
48	A	51	GLY	0	-0.007	-0.015	24.939	0.474	0.474	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.082	0.043	24.025	-0.200	-0.200	0.000	0.000	0.000	0.000
50	A	53	ALA	0	-0.010	-0.002	26.687	0.188	0.188	0.000	0.000	0.000	0.000
51	A	54	ASP	-1	-0.922	-0.963	26.855	-10.813	-10.813	0.000	0.000	0.000	0.000
52	A	55	GLN	0	-0.034	-0.022	22.944	0.103	0.103	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.021	0.021	26.594	0.036	0.036	0.000	0.000	0.000	0.000
54	A	57	PRO	0	-0.005	0.015	29.663	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	58	PRO	0	-0.012	-0.034	32.835	-0.141	-0.141	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.844	-0.930	34.372	-8.352	-8.352	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.920	-0.960	30.942	-9.487	-9.487	0.000	0.000	0.000	0.000
58	A	61	LEU	0	-0.052	-0.026	28.184	-0.178	-0.178	0.000	0.000	0.000	0.000
59	A	62	GLU	-1	-0.823	-0.927	32.106	-8.043	-8.043	0.000	0.000	0.000	0.000
60	A	63	GLY	0	-0.025	-0.012	35.562	0.031	0.031	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.901	0.960	31.546	8.995	8.995	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.858	0.916	30.515	8.980	8.980	0.000	0.000	0.000	0.000
63	A	66	PHE	0	0.000	0.005	25.942	-0.155	-0.155	0.000	0.000	0.000	0.000
64	A	67	ILE	0	0.061	0.036	21.067	0.192	0.192	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.019	0.006	23.758	-0.166	-0.166	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.011	0.006	19.344	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.001	-0.009	22.561	0.342	0.342	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.025	-0.010	22.430	0.137	0.137	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.025	0.022	19.333	-0.286	-0.286	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.926	0.953	23.059	13.555	13.555	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.057	0.041	25.056	-0.212	-0.212	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.884	0.941	24.363	11.621	11.621	0.000	0.000	0.000	0.000
73	A	76	LYS	1	1.022	1.026	27.986	9.238	9.238	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.045	0.020	24.172	-0.028	-0.028	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.023	-0.023	30.115	0.286	0.286	0.000	0.000	0.000	0.000
76	A	79	GLY	0	-0.061	-0.028	33.266	0.287	0.287	0.000	0.000	0.000	0.000
77	A	80	VAL	0	0.000	0.001	32.926	0.191	0.191	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.908	-0.960	30.931	-10.190	-10.190	0.000	0.000	0.000	0.000
79	A	82	SER	0	-0.005	0.002	26.659	0.223	0.223	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.015	-0.004	28.129	-0.228	-0.228	0.000	0.000	0.000	0.000
81	A	84	GLY	0	0.068	0.027	25.284	0.032	0.032	0.000	0.000	0.000	0.000
82	A	85	MET	0	-0.031	-0.010	17.932	0.116	0.116	0.000	0.000	0.000	0.000
83	A	86	LEU	0	0.016	0.020	23.205	-0.055	-0.055	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.027	-0.016	17.844	-0.512	-0.512	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.041	-0.020	19.366	0.733	0.733	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.025	0.010	18.020	-0.839	-0.839	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.948	-0.990	16.835	-14.883	-14.883	0.000	0.000	0.000	0.000
88	A	91	THR	0	-0.029	-0.019	15.589	-0.681	-0.681	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.898	-0.968	12.232	-17.845	-17.845	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.897	-0.931	14.875	-13.839	-13.839	0.000	0.000	0.000	0.000
91	A	94	GLY	0	-0.015	0.008	17.802	0.641	0.641	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.877	0.963	19.424	12.292	12.292	0.000	0.000	0.000	0.000
93	A	96	VAL	0	-0.010	-0.014	20.152	-0.485	-0.485	0.000	0.000	0.000	0.000
94	A	97	TYR	0	-0.020	-0.023	20.003	0.998	0.998	0.000	0.000	0.000	0.000
95	A	98	LEU	0	0.000	0.002	22.605	-0.441	-0.441	0.000	0.000	0.000	0.000
96	A	99	ILE	0	0.013	0.006	19.316	-0.065	-0.065	0.000	0.000	0.000	0.000
97	A	100	PRO	0	-0.030	-0.010	23.982	0.022	0.022	0.000	0.000	0.000	0.000
98	A	101	VAL	0	-0.025	-0.020	25.943	-0.294	-0.294	0.000	0.000	0.000	0.000
99	A	102	PRO	0	0.006	0.000	27.918	0.275	0.275	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.855	-0.925	31.108	-8.881	-8.881	0.000	0.000	0.000	0.000
101	A	104	GLU	-1	-0.913	-0.954	34.222	-8.767	-8.767	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.039	-0.008	29.268	0.073	0.073	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.010	-0.006	32.623	0.079	0.079	0.000	0.000	0.000	0.000
104	A	107	VAL	0	0.033	0.021	31.964	-0.319	-0.319	0.000	0.000	0.000	0.000
105	A	108	GLY	0	-0.008	-0.006	30.966	0.147	0.147	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.041	-0.013	29.531	-0.193	-0.193	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.810	0.893	21.147	13.690	13.690	0.000	0.000	0.000	0.000
108	A	111	VAL	0	-0.022	-0.014	20.938	0.113	0.113	0.000	0.000	0.000	0.000
109	A	112	TRP	-1	-0.880	-0.946	19.324	-15.360	-15.360	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:4:MET)