FMO DATABASE

FMODB ID: 7Y9LK

Calculation Name: 2AXI-A-Xray547

Preferred Name: p53-binding protein Mdm-2

Target Type: SINGLE PROTEIN

Ligand Name: 6-chloro-l-tryptophan | 3[n-morpholino]propane sulfonic acid | sulfate ion | d-proline

Ligand 3-letter code: 6CW | MPO | SO4 | DPR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2AXI

Chain ID: A

ChEMBL ID: CHEMBL5023

UniProt ID: Q00987

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	92
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-702757.6583
FMO2-HF: Nuclear repulsion	664600.92753
FMO2-HF: Total energy	-38156.730769
FMO2-MP2: Total energy	-38267.663408

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:23:GLU)

Summations of interaction energy for fragment #1(A:23:GLU)

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.
7.896	10.224	-0.018	-0.903	-1.407	0.001

Interaction energy analysis for fragmet #1(A:23:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.060 / q_NPA : -0.037

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	25	GLU	-1	-0.869	-0.943	3.864	-6.504	-4.269	-0.017	-0.881	-1.337	0.001
29	A	51	LYS	1	0.980	0.987	3.927	9.223	9.316	-0.001	-0.022	-0.070	0.000
4	A	26	THR	0	-0.009	-0.002	5.441	1.460	1.460	0.000	0.000	0.000	0.000
5	A	27	LEU	0	0.054	0.041	8.719	-0.033	-0.033	0.000	0.000	0.000	0.000
6	A	28	VAL	0	-0.024	-0.021	11.595	0.528	0.528	0.000	0.000	0.000	0.000
7	A	29	ARG	1	0.911	0.942	14.165	1.441	1.441	0.000	0.000	0.000	0.000
8	A	30	PRO	0	-0.023	-0.019	16.091	0.143	0.143	0.000	0.000	0.000	0.000
9	A	31	LYS	1	0.895	0.957	18.618	1.218	1.218	0.000	0.000	0.000	0.000
10	A	32	PRO	0	0.027	-0.004	22.088	-0.044	-0.044	0.000	0.000	0.000	0.000
11	A	33	LEU	0	0.041	0.031	23.496	-0.020	-0.020	0.000	0.000	0.000	0.000
12	A	34	LEU	0	0.057	0.025	16.169	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	35	LEU	0	-0.011	-0.003	19.668	-0.075	-0.075	0.000	0.000	0.000	0.000
14	A	36	LYS	1	0.950	0.975	21.503	0.830	0.830	0.000	0.000	0.000	0.000
15	A	37	LEU	0	0.009	0.018	20.023	0.019	0.019	0.000	0.000	0.000	0.000
16	A	38	LEU	0	0.013	0.000	15.630	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	39	LYS	1	0.807	0.903	19.512	1.379	1.379	0.000	0.000	0.000	0.000
18	A	40	SER	0	-0.058	-0.022	22.892	0.090	0.090	0.000	0.000	0.000	0.000
19	A	41	VAL	0	-0.033	-0.008	17.898	0.058	0.058	0.000	0.000	0.000	0.000
20	A	42	GLY	0	0.013	0.016	20.404	-0.065	-0.065	0.000	0.000	0.000	0.000
21	A	43	ALA	0	0.010	0.014	17.440	-0.017	-0.017	0.000	0.000	0.000	0.000
22	A	44	GLN	0	0.017	-0.019	19.363	0.043	0.043	0.000	0.000	0.000	0.000
23	A	45	LYS	1	0.852	0.941	13.119	3.026	3.026	0.000	0.000	0.000	0.000
24	A	46	ASP	-1	-0.783	-0.880	19.719	-1.341	-1.341	0.000	0.000	0.000	0.000
25	A	47	THR	0	-0.063	-0.043	14.857	0.027	0.027	0.000	0.000	0.000	0.000
26	A	48	TYR	0	-0.076	-0.056	12.404	0.054	0.054	0.000	0.000	0.000	0.000
27	A	49	THR	0	0.089	0.059	7.162	-0.380	-0.380	0.000	0.000	0.000	0.000
28	A	50	MET	0	0.007	-0.005	7.572	0.539	0.539	0.000	0.000	0.000	0.000
30	A	52	GLU	-1	-0.827	-0.894	6.599	-2.642	-2.642	0.000	0.000	0.000	0.000
31	A	53	VAL	0	0.007	0.008	10.100	0.679	0.679	0.000	0.000	0.000	0.000
32	A	54	LEU	0	-0.011	-0.004	7.351	0.573	0.573	0.000	0.000	0.000	0.000
33	A	55	PHE	0	-0.020	0.003	9.576	0.506	0.506	0.000	0.000	0.000	0.000
34	A	56	TYR	0	0.035	0.004	11.302	0.506	0.506	0.000	0.000	0.000	0.000
35	A	57	LEU	0	0.017	0.005	14.037	0.338	0.338	0.000	0.000	0.000	0.000
36	A	58	GLY	0	0.008	0.013	13.933	0.262	0.262	0.000	0.000	0.000	0.000
37	A	59	GLN	0	0.024	-0.004	15.170	0.184	0.184	0.000	0.000	0.000	0.000
38	A	60	TYR	0	-0.077	-0.052	17.383	0.166	0.166	0.000	0.000	0.000	0.000
39	A	61	ILE	0	0.005	-0.005	17.163	0.134	0.134	0.000	0.000	0.000	0.000
40	A	62	MET	0	-0.016	-0.001	19.029	0.109	0.109	0.000	0.000	0.000	0.000
41	A	63	THR	0	-0.051	-0.047	20.852	0.108	0.108	0.000	0.000	0.000	0.000
42	A	64	LYS	1	0.898	0.944	23.097	0.830	0.830	0.000	0.000	0.000	0.000
43	A	65	ARG	1	0.936	0.982	24.170	0.534	0.534	0.000	0.000	0.000	0.000
44	A	66	LEU	0	0.000	0.015	22.896	0.038	0.038	0.000	0.000	0.000	0.000
45	A	67	TYR	0	-0.052	-0.013	22.101	0.026	0.026	0.000	0.000	0.000	0.000
46	A	68	ASP	-1	-0.827	-0.912	24.214	-0.173	-0.173	0.000	0.000	0.000	0.000
47	A	69	GLU	-1	-0.909	-0.971	25.962	-0.287	-0.287	0.000	0.000	0.000	0.000
48	A	70	LYS	1	0.913	0.954	27.548	0.147	0.147	0.000	0.000	0.000	0.000
49	A	71	GLN	0	-0.049	-0.016	25.679	0.078	0.078	0.000	0.000	0.000	0.000
50	A	72	GLN	0	0.033	0.015	21.979	0.007	0.007	0.000	0.000	0.000	0.000
51	A	73	HIS	0	-0.031	-0.010	20.118	-0.078	-0.078	0.000	0.000	0.000	0.000
52	A	74	ILE	0	-0.027	-0.008	21.046	-0.031	-0.031	0.000	0.000	0.000	0.000
53	A	75	VAL	0	0.017	0.004	19.884	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	76	TYR	0	0.003	-0.010	23.243	0.026	0.026	0.000	0.000	0.000	0.000
55	A	77	CYS	0	-0.023	-0.016	23.974	-0.026	-0.026	0.000	0.000	0.000	0.000
56	A	78	SER	0	-0.017	-0.006	26.119	-0.015	-0.015	0.000	0.000	0.000	0.000
57	A	79	ASN	0	-0.030	0.003	29.484	0.021	0.021	0.000	0.000	0.000	0.000
58	A	80	ASP	-1	-0.779	-0.867	25.236	-0.763	-0.763	0.000	0.000	0.000	0.000
59	A	81	LEU	0	0.051	0.037	25.722	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	82	LEU	0	-0.024	-0.017	19.501	-0.055	-0.055	0.000	0.000	0.000	0.000
61	A	83	GLY	0	0.012	-0.007	23.181	-0.018	-0.018	0.000	0.000	0.000	0.000
62	A	84	ASP	-1	-0.893	-0.952	25.922	-0.580	-0.580	0.000	0.000	0.000	0.000
63	A	85	LEU	0	-0.102	-0.039	18.314	-0.035	-0.035	0.000	0.000	0.000	0.000
64	A	86	PHE	0	0.007	-0.021	17.081	-0.048	-0.048	0.000	0.000	0.000	0.000
65	A	87	GLY	0	-0.011	0.014	22.583	0.049	0.049	0.000	0.000	0.000	0.000
66	A	88	VAL	0	-0.049	-0.030	24.255	0.066	0.066	0.000	0.000	0.000	0.000
67	A	89	PRO	0	0.053	0.024	26.606	-0.044	-0.044	0.000	0.000	0.000	0.000
68	A	90	SER	0	0.036	-0.004	25.657	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	91	PHE	0	-0.054	-0.020	18.149	0.008	0.008	0.000	0.000	0.000	0.000
70	A	92	SER	0	0.027	0.017	20.978	0.008	0.008	0.000	0.000	0.000	0.000
71	A	93	VAL	0	0.031	0.004	16.133	-0.035	-0.035	0.000	0.000	0.000	0.000
72	A	94	LYS	1	0.972	0.977	15.843	-0.255	-0.255	0.000	0.000	0.000	0.000
73	A	95	GLU	-1	-0.846	-0.912	17.370	-0.188	-0.188	0.000	0.000	0.000	0.000
74	A	96	HIS	0	-0.009	-0.020	12.346	0.024	0.024	0.000	0.000	0.000	0.000
75	A	97	ARG	1	1.002	1.000	14.167	-0.277	-0.277	0.000	0.000	0.000	0.000
76	A	98	LYS	1	0.928	0.992	15.337	0.257	0.257	0.000	0.000	0.000	0.000
77	A	99	ILE	0	0.035	0.027	13.339	-0.102	-0.102	0.000	0.000	0.000	0.000
78	A	100	TYR	0	-0.020	-0.032	6.909	0.487	0.487	0.000	0.000	0.000	0.000
79	A	101	THR	0	-0.063	-0.041	13.506	-0.085	-0.085	0.000	0.000	0.000	0.000
80	A	102	MET	0	-0.033	-0.012	16.793	0.005	0.005	0.000	0.000	0.000	0.000
81	A	103	ILE	0	0.030	0.024	13.136	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	104	TYR	0	0.027	-0.010	9.276	-0.284	-0.284	0.000	0.000	0.000	0.000
83	A	105	ARG	1	0.943	0.975	15.803	0.756	0.756	0.000	0.000	0.000	0.000
84	A	106	ASN	0	-0.041	-0.017	18.638	0.143	0.143	0.000	0.000	0.000	0.000
85	A	107	LEU	0	-0.006	0.004	13.789	-0.072	-0.072	0.000	0.000	0.000	0.000
86	A	108	VAL	0	-0.020	-0.005	18.323	0.172	0.172	0.000	0.000	0.000	0.000
87	A	109	VAL	0	0.020	0.004	13.535	-0.212	-0.212	0.000	0.000	0.000	0.000
88	A	110	VAL	0	-0.041	-0.010	14.991	0.275	0.275	0.000	0.000	0.000	0.000
89	A	111	ASN	0	-0.003	-0.006	15.636	-0.150	-0.150	0.000	0.000	0.000	0.000
90	A	112	GLN	0	-0.049	-0.011	15.229	0.233	0.233	0.000	0.000	0.000	0.000
91	A	113	GLN	0	-0.067	-0.045	10.785	-0.828	-0.828	0.000	0.000	0.000	0.000
92	A	114	GLU	-2	-1.766	-1.879	10.750	-4.116	-4.116	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:23:GLU)