FMO DATABASE

FMODB ID: 7N4KK

Calculation Name: 4N0Z-A-Xray547

Preferred Name:

Target Type:

Ligand Name: cisplatin | 3[n-morpholino]propane sulfonic acid | (4s)-2-methyl-2,4-pentanediol

Ligand 3-letter code: CPT | MPO | MPD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4N0Z

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NLB2

Base Structure: X-ray

Registration Date: 2025-10-04

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-842708.463075
FMO2-HF: Nuclear repulsion	800093.787321
FMO2-HF: Total energy	-42614.675755
FMO2-MP2: Total energy	-42737.614012

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:5:SER)

Summations of interaction energy for fragment #1(A:5: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.
65.071	70.376	1.107	-2.385	-4.031	0.009

Interaction energy analysis for fragmet #1(A:5:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.897

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	7	ALA	0	-0.018	0.007	3.403	7.912	10.298	0.018	-1.030	-1.374	0.002
4	A	8	VAL	0	0.053	0.025	2.361	-0.321	1.796	1.085	-1.179	-2.024	0.007
5	A	9	LYS	1	0.845	0.926	3.486	57.361	57.855	0.002	-0.137	-0.360	0.000
53	A	58	ASP	-1	-0.871	-0.932	5.097	-40.090	-40.017	-0.001	-0.002	-0.071	0.000
56	A	61	ASN	0	-0.040	-0.030	3.615	-0.062	0.173	0.003	-0.037	-0.202	0.000
6	A	10	LYS	1	0.946	0.971	6.361	40.119	40.119	0.000	0.000	0.000	0.000
7	A	11	TRP	0	0.013	0.016	7.651	2.238	2.238	0.000	0.000	0.000	0.000
8	A	12	VAL	0	0.010	0.002	8.122	2.321	2.321	0.000	0.000	0.000	0.000
9	A	13	ASN	0	0.022	0.027	10.233	1.380	1.380	0.000	0.000	0.000	0.000
10	A	14	LYS	1	0.905	0.953	12.185	21.965	21.965	0.000	0.000	0.000	0.000
11	A	15	ILE	0	0.026	0.026	12.377	1.481	1.481	0.000	0.000	0.000	0.000
12	A	16	ILE	0	-0.044	-0.024	13.688	1.363	1.363	0.000	0.000	0.000	0.000
13	A	17	GLU	-1	-0.924	-0.965	14.824	-20.403	-20.403	0.000	0.000	0.000	0.000
14	A	18	GLU	-1	-0.961	-0.981	17.160	-16.436	-16.436	0.000	0.000	0.000	0.000
15	A	19	ASN	0	-0.056	-0.027	18.520	1.441	1.441	0.000	0.000	0.000	0.000
16	A	20	ILE	0	0.016	0.016	21.142	-0.363	-0.363	0.000	0.000	0.000	0.000
17	A	21	ILE	0	0.004	0.000	23.319	-0.043	-0.043	0.000	0.000	0.000	0.000
18	A	22	ALA	0	0.042	0.030	17.762	-0.049	-0.049	0.000	0.000	0.000	0.000
19	A	23	VAL	0	-0.020	-0.016	19.364	-0.076	-0.076	0.000	0.000	0.000	0.000
20	A	24	PHE	0	0.009	0.014	12.458	-0.437	-0.437	0.000	0.000	0.000	0.000
21	A	25	ALA	0	0.010	-0.024	16.607	0.641	0.641	0.000	0.000	0.000	0.000
22	A	26	LYS	1	0.864	0.918	16.984	14.294	14.294	0.000	0.000	0.000	0.000
23	A	27	THR	0	-0.005	-0.022	18.985	0.657	0.657	0.000	0.000	0.000	0.000
24	A	28	GLU	-1	-0.939	-0.964	21.821	-11.615	-11.615	0.000	0.000	0.000	0.000
25	A	29	CYS	0	0.009	0.038	21.545	-0.134	-0.134	0.000	0.000	0.000	0.000
26	A	30	PRO	0	0.025	0.000	24.266	0.027	0.027	0.000	0.000	0.000	0.000
27	A	31	TYR	0	0.066	0.019	25.148	0.126	0.126	0.000	0.000	0.000	0.000
28	A	33	ILE	0	0.041	0.024	23.909	0.101	0.101	0.000	0.000	0.000	0.000
29	A	34	LYS	1	0.963	1.000	26.999	10.014	10.014	0.000	0.000	0.000	0.000
30	A	35	ALA	0	0.026	-0.003	24.779	0.243	0.243	0.000	0.000	0.000	0.000
31	A	36	ILE	0	0.013	0.002	22.813	0.138	0.138	0.000	0.000	0.000	0.000
32	A	37	SER	0	-0.028	-0.032	26.577	0.303	0.303	0.000	0.000	0.000	0.000
33	A	38	ILE	0	-0.021	-0.005	29.691	0.279	0.279	0.000	0.000	0.000	0.000
34	A	39	LEU	0	0.002	-0.001	25.012	0.187	0.187	0.000	0.000	0.000	0.000
35	A	40	LYS	1	0.961	0.962	27.326	11.146	11.146	0.000	0.000	0.000	0.000
36	A	41	GLY	0	-0.016	0.014	31.007	0.259	0.259	0.000	0.000	0.000	0.000
37	A	42	TYR	0	-0.062	-0.043	32.042	0.334	0.334	0.000	0.000	0.000	0.000
38	A	43	ASN	0	-0.030	-0.017	33.773	0.041	0.041	0.000	0.000	0.000	0.000
39	A	44	LEU	0	0.033	0.018	28.594	-0.076	-0.076	0.000	0.000	0.000	0.000
40	A	45	ASN	0	0.001	-0.021	28.561	-0.391	-0.391	0.000	0.000	0.000	0.000
41	A	46	SER	0	-0.003	0.000	27.858	-0.186	-0.186	0.000	0.000	0.000	0.000
42	A	47	HIS	0	0.015	0.011	26.123	-0.415	-0.415	0.000	0.000	0.000	0.000
43	A	48	MET	0	-0.089	-0.023	24.044	-0.270	-0.270	0.000	0.000	0.000	0.000
44	A	49	HIS	0	0.004	0.005	16.483	0.796	0.796	0.000	0.000	0.000	0.000
45	A	50	VAL	0	-0.044	-0.037	19.960	-0.049	-0.049	0.000	0.000	0.000	0.000
46	A	51	GLU	-1	-0.833	-0.894	13.536	-18.887	-18.887	0.000	0.000	0.000	0.000
47	A	52	ASN	0	-0.024	-0.032	16.545	-0.377	-0.377	0.000	0.000	0.000	0.000
48	A	53	ILE	0	0.026	-0.003	11.916	-0.462	-0.462	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.756	-0.882	12.602	-16.589	-16.589	0.000	0.000	0.000	0.000
50	A	55	LYS	1	0.868	0.945	15.171	14.086	14.086	0.000	0.000	0.000	0.000
51	A	56	ASN	0	0.053	0.020	8.838	-1.432	-1.432	0.000	0.000	0.000	0.000
52	A	57	PRO	0	0.019	0.020	8.133	0.332	0.332	0.000	0.000	0.000	0.000
54	A	59	MET	0	-0.021	0.016	6.989	-1.856	-1.856	0.000	0.000	0.000	0.000
55	A	60	ALA	0	0.029	0.007	8.838	-0.076	-0.076	0.000	0.000	0.000	0.000
57	A	62	ILE	0	0.025	0.020	5.772	-1.593	-1.593	0.000	0.000	0.000	0.000
58	A	63	GLN	0	-0.026	-0.029	7.877	1.320	1.320	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.025	-0.009	7.353	1.752	1.752	0.000	0.000	0.000	0.000
60	A	65	TYR	0	-0.019	-0.041	6.134	0.043	0.043	0.000	0.000	0.000	0.000
61	A	66	LEU	0	0.043	0.015	8.122	2.767	2.767	0.000	0.000	0.000	0.000
62	A	67	LYS	1	0.901	0.974	11.371	21.872	21.872	0.000	0.000	0.000	0.000
63	A	68	GLU	-1	-0.882	-0.938	6.987	-40.264	-40.264	0.000	0.000	0.000	0.000
64	A	69	LEU	0	-0.012	0.005	10.882	1.755	1.755	0.000	0.000	0.000	0.000
65	A	70	THR	0	-0.025	-0.013	13.293	2.058	2.058	0.000	0.000	0.000	0.000
66	A	71	GLY	0	0.021	0.026	15.381	1.233	1.233	0.000	0.000	0.000	0.000
67	A	72	LYS	1	0.882	0.925	16.872	14.246	14.246	0.000	0.000	0.000	0.000
68	A	73	SER	0	0.062	0.030	13.744	-0.363	-0.363	0.000	0.000	0.000	0.000
69	A	74	SER	0	-0.036	-0.001	14.969	-0.518	-0.518	0.000	0.000	0.000	0.000
70	A	75	VAL	0	0.014	0.029	15.839	-0.093	-0.093	0.000	0.000	0.000	0.000
71	A	76	PRO	0	-0.006	-0.030	18.492	0.623	0.623	0.000	0.000	0.000	0.000
72	A	77	ARG	1	0.807	0.904	15.105	17.070	17.070	0.000	0.000	0.000	0.000
73	A	78	ILE	0	-0.006	0.006	18.236	-0.158	-0.158	0.000	0.000	0.000	0.000
74	A	79	PHE	0	0.030	0.003	14.693	-0.251	-0.251	0.000	0.000	0.000	0.000
75	A	80	ILE	0	0.018	0.007	20.358	0.426	0.426	0.000	0.000	0.000	0.000
76	A	81	ASN	0	0.012	-0.003	22.967	-0.282	-0.282	0.000	0.000	0.000	0.000
77	A	82	LYS	1	0.927	0.960	17.803	15.093	15.093	0.000	0.000	0.000	0.000
78	A	83	ASP	-1	-0.893	-0.914	18.920	-13.930	-13.930	0.000	0.000	0.000	0.000
79	A	84	VAL	0	-0.032	-0.028	17.938	-0.186	-0.186	0.000	0.000	0.000	0.000
80	A	85	VAL	0	-0.032	-0.009	20.594	0.715	0.715	0.000	0.000	0.000	0.000
81	A	86	GLY	0	0.024	0.010	20.891	0.307	0.307	0.000	0.000	0.000	0.000
82	A	87	GLY	0	-0.029	-0.038	21.101	-0.616	-0.616	0.000	0.000	0.000	0.000
83	A	88	CYS	0	-0.066	-0.022	22.911	0.530	0.530	0.000	0.000	0.000	0.000
84	A	89	ASP	-1	-0.854	-0.932	26.074	-10.956	-10.956	0.000	0.000	0.000	0.000
85	A	90	ASP	-1	-0.858	-0.909	23.917	-12.745	-12.745	0.000	0.000	0.000	0.000
86	A	91	LEU	0	0.004	0.001	26.097	0.279	0.279	0.000	0.000	0.000	0.000
87	A	92	VAL	0	-0.013	-0.015	27.857	0.343	0.343	0.000	0.000	0.000	0.000
88	A	93	LYS	1	0.841	0.913	30.235	10.014	10.014	0.000	0.000	0.000	0.000
89	A	94	GLU	-1	-0.753	-0.851	27.850	-11.369	-11.369	0.000	0.000	0.000	0.000
90	A	95	ASN	0	-0.042	-0.018	31.352	0.174	0.174	0.000	0.000	0.000	0.000
91	A	96	ASP	-1	-0.886	-0.938	33.456	-8.715	-8.715	0.000	0.000	0.000	0.000
92	A	97	GLU	-1	-0.856	-0.901	34.473	-9.047	-9.047	0.000	0.000	0.000	0.000
93	A	98	GLY	0	0.000	0.008	36.146	0.071	0.071	0.000	0.000	0.000	0.000
94	A	99	LYS	1	0.884	0.933	28.051	10.964	10.964	0.000	0.000	0.000	0.000
95	A	100	LEU	0	-0.020	-0.014	28.829	-0.257	-0.257	0.000	0.000	0.000	0.000
96	A	101	LYS	1	0.897	0.934	31.688	8.040	8.040	0.000	0.000	0.000	0.000
97	A	102	GLU	-1	-0.843	-0.897	33.249	-9.642	-9.642	0.000	0.000	0.000	0.000
98	A	103	ARG	1	0.764	0.843	24.842	12.258	12.258	0.000	0.000	0.000	0.000
99	A	104	LEU	0	0.007	0.003	29.140	-0.110	-0.110	0.000	0.000	0.000	0.000
100	A	105	GLN	0	-0.028	-0.020	32.090	0.019	0.019	0.000	0.000	0.000	0.000
101	A	106	LYS	1	0.817	0.893	32.110	9.741	9.741	0.000	0.000	0.000	0.000
102	A	107	LEU	0	-0.043	-0.015	27.358	-0.188	-0.188	0.000	0.000	0.000	0.000
103	A	108	GLY	0	-0.006	0.007	31.511	-0.065	-0.065	0.000	0.000	0.000	0.000
104	A	109	LEU	0	-0.060	-0.024	28.577	0.065	0.065	0.000	0.000	0.000	0.000
105	A	110	VAL	0	-0.034	-0.021	33.236	0.120	0.120	0.000	0.000	0.000	0.000
106	A	111	ASN	-1	-0.824	-0.889	36.260	-7.969	-7.969	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:SER)