FMO DATABASE

FMODB ID: 9L162

Calculation Name: 1XRK-A-Xray547

Preferred Name:

Target Type:

Ligand Name: bleomycin a2 | sulfate ion

Ligand 3-letter code: BLM | SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1XRK

Chain ID: A

ChEMBL ID:

UniProt ID: P17493

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-976985.067312
FMO2-HF: Nuclear repulsion	930361.178966
FMO2-HF: Total energy	-46623.888346
FMO2-MP2: Total energy	-46761.685029

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-126.499	-124.695	-0.015	-0.89	-0.9	-0.003

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.918

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	4	LEU	0	0.067	0.049	3.870	-0.278	1.526	-0.015	-0.890	-0.900	-0.003
4	A	5	THR	0	-0.055	-0.044	6.308	1.068	1.068	0.000	0.000	0.000	0.000
5	A	6	SER	0	0.036	0.029	9.010	2.204	2.204	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.011	-0.015	10.978	-1.612	-1.612	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.032	0.030	13.615	0.587	0.587	0.000	0.000	0.000	0.000
8	A	9	PRO	0	-0.019	-0.002	16.777	-0.104	-0.104	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.026	-0.009	18.998	0.219	0.219	0.000	0.000	0.000	0.000
10	A	11	LEU	0	0.017	0.018	21.611	0.152	0.152	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.018	-0.023	25.369	0.035	0.035	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.059	0.021	27.863	0.239	0.239	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.838	0.913	31.420	8.112	8.112	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.851	-0.914	34.229	-8.230	-8.230	0.000	0.000	0.000	0.000
15	A	16	VAL	0	0.045	0.015	29.221	-0.108	-0.108	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.000	0.007	31.874	-0.158	-0.158	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.940	-0.979	34.357	-8.090	-8.090	0.000	0.000	0.000	0.000
18	A	19	ALA	0	0.018	0.010	30.853	-0.038	-0.038	0.000	0.000	0.000	0.000
19	A	20	VAL	0	0.004	-0.008	29.094	-0.171	-0.171	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.844	-0.858	31.469	-8.170	-8.170	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.059	0.015	32.601	0.048	0.048	0.000	0.000	0.000	0.000
22	A	23	TRP	0	-0.015	-0.045	28.623	-0.119	-0.119	0.000	0.000	0.000	0.000
23	A	24	THR	0	-0.108	-0.077	29.556	-0.094	-0.094	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.847	-0.908	31.906	-8.587	-8.587	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.724	0.836	35.021	8.331	8.331	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.012	0.013	31.462	0.085	0.085	0.000	0.000	0.000	0.000
27	A	28	GLY	0	0.039	0.032	31.670	-0.235	-0.235	0.000	0.000	0.000	0.000
28	A	29	PHE	0	-0.042	-0.018	24.821	-0.319	-0.319	0.000	0.000	0.000	0.000
29	A	30	SER	0	-0.026	-0.017	27.200	0.432	0.432	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.842	0.899	27.168	8.875	8.875	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.055	-0.019	21.354	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.023	-0.012	21.157	-0.033	-0.033	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.021	-0.022	26.157	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.962	-0.970	25.746	-11.274	-11.274	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.978	-0.987	29.575	-8.687	-8.687	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.911	-0.957	27.382	-10.628	-10.628	0.000	0.000	0.000	0.000
37	A	38	PHE	0	0.002	0.000	20.460	-0.430	-0.430	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.029	0.004	25.556	0.259	0.259	0.000	0.000	0.000	0.000
39	A	40	GLY	0	-0.002	0.003	23.045	-0.488	-0.488	0.000	0.000	0.000	0.000
40	A	41	VAL	0	-0.011	-0.002	23.850	0.412	0.412	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.001	-0.014	21.873	-0.514	-0.514	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.813	0.881	24.007	10.734	10.734	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.864	-0.929	24.026	-11.817	-11.817	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.976	-0.983	19.113	-15.159	-15.159	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.053	-0.028	19.032	-0.977	-0.977	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.035	-0.017	18.630	0.652	0.652	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.001	-0.001	19.987	-0.533	-0.533	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.014	-0.021	16.998	0.004	0.004	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.001	0.006	22.402	0.121	0.121	0.000	0.000	0.000	0.000
50	A	51	SER	0	0.000	0.000	24.384	-0.151	-0.151	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.027	0.016	26.434	0.225	0.225	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.064	-0.031	28.456	-0.276	-0.276	0.000	0.000	0.000	0.000
53	A	54	GLN	0	-0.007	-0.011	30.979	0.371	0.371	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.914	-0.959	33.380	-8.638	-8.638	0.000	0.000	0.000	0.000
55	A	56	GLN	0	-0.020	-0.025	33.457	-0.116	-0.116	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.012	0.002	33.024	-0.092	-0.092	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.019	0.018	28.198	-0.178	-0.178	0.000	0.000	0.000	0.000
58	A	59	PRO	0	0.011	0.035	29.678	-0.299	-0.299	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.837	-0.910	30.793	-8.763	-8.763	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.127	-0.072	29.585	0.033	0.033	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.072	-0.028	25.157	-0.532	-0.532	0.000	0.000	0.000	0.000
62	A	63	GLN	0	-0.033	-0.023	25.481	0.405	0.405	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.007	0.001	22.574	-0.587	-0.587	0.000	0.000	0.000	0.000
64	A	65	TRP	0	-0.049	-0.038	22.214	0.424	0.424	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.014	0.004	21.751	-0.729	-0.729	0.000	0.000	0.000	0.000
66	A	67	TRP	0	-0.016	-0.003	20.269	0.397	0.397	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.021	0.013	23.729	-0.081	-0.081	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.849	0.901	23.401	12.895	12.895	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.019	0.010	28.088	0.205	0.205	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.009	-0.011	29.759	0.211	0.211	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.816	-0.905	31.960	-8.717	-8.717	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.966	-0.972	34.073	-8.879	-8.879	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.017	0.016	29.347	0.116	0.116	0.000	0.000	0.000	0.000
74	A	75	TYR	0	0.000	-0.005	33.500	0.121	0.121	0.000	0.000	0.000	0.000
75	A	76	ALA	0	-0.019	0.001	35.942	0.223	0.223	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.829	-0.869	34.102	-9.123	-9.123	0.000	0.000	0.000	0.000
77	A	78	TRP	0	-0.001	-0.032	29.102	0.011	0.011	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.011	-0.034	36.950	0.182	0.182	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.975	-0.969	40.004	-6.901	-6.901	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.088	-0.041	37.889	0.159	0.159	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.025	-0.005	36.140	-0.045	-0.045	0.000	0.000	0.000	0.000
82	A	83	SER	0	-0.006	0.005	39.500	0.110	0.110	0.000	0.000	0.000	0.000
83	A	84	THR	0	0.099	0.042	40.404	-0.132	-0.132	0.000	0.000	0.000	0.000
84	A	85	ASN	0	-0.011	0.009	41.797	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	86	PHE	0	-0.004	-0.005	35.300	0.113	0.113	0.000	0.000	0.000	0.000
86	A	87	ARG	0	0.032	0.049	40.652	0.067	0.067	0.000	0.000	0.000	0.000
87	A	88	ASP	0	-0.110	-0.095	42.790	0.124	0.124	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.011	0.007	42.506	0.126	0.126	0.000	0.000	0.000	0.000
89	A	90	SER	0	0.000	-0.018	42.533	-0.092	-0.092	0.000	0.000	0.000	0.000
90	A	91	GLY	0	0.010	0.022	41.100	-0.081	-0.081	0.000	0.000	0.000	0.000
91	A	92	PRO	0	0.017	0.015	36.336	-0.023	-0.023	0.000	0.000	0.000	0.000
92	A	93	ALA	0	-0.028	-0.014	37.104	0.232	0.232	0.000	0.000	0.000	0.000
93	A	94	MET	0	-0.020	0.000	34.975	-0.243	-0.243	0.000	0.000	0.000	0.000
94	A	95	THR	0	-0.053	-0.038	35.885	0.178	0.178	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.903	-0.950	37.412	-7.509	-7.509	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.029	-0.006	34.600	-0.235	-0.235	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.023	-0.010	34.889	0.265	0.265	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.936	-0.982	34.391	-9.032	-9.032	0.000	0.000	0.000	0.000
99	A	100	GLN	0	0.000	0.015	31.310	0.303	0.303	0.000	0.000	0.000	0.000
100	A	101	PRO	0	-0.055	-0.043	31.465	-0.148	-0.148	0.000	0.000	0.000	0.000
101	A	102	TRP	0	-0.062	-0.042	26.654	-0.062	-0.062	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.015	0.012	27.389	-0.489	-0.489	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.841	0.919	29.570	9.623	9.623	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.729	-0.848	28.868	-11.074	-11.074	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.022	0.026	31.417	0.377	0.377	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.021	-0.008	31.123	-0.419	-0.419	0.000	0.000	0.000	0.000
107	A	108	LEU	0	0.015	-0.002	31.542	0.360	0.360	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.826	0.917	31.699	7.840	7.840	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.753	-0.861	30.641	-9.578	-9.578	0.000	0.000	0.000	0.000
110	A	111	PRO	0	-0.017	-0.021	33.667	0.144	0.144	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.006	0.011	32.206	0.171	0.171	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.024	0.018	33.876	0.082	0.082	0.000	0.000	0.000	0.000
113	A	114	ASN	0	-0.039	-0.028	28.371	-0.356	-0.356	0.000	0.000	0.000	0.000
114	A	115	CYS	0	-0.026	-0.017	29.765	0.192	0.192	0.000	0.000	0.000	0.000
115	A	116	VAL	0	-0.006	-0.005	25.717	-0.424	-0.424	0.000	0.000	0.000	0.000
116	A	117	HIS	1	0.803	0.891	26.845	11.177	11.177	0.000	0.000	0.000	0.000
117	A	118	PHE	0	0.044	0.014	26.456	-0.567	-0.567	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.008	-0.010	24.966	0.434	0.434	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.023	-0.018	26.847	-0.232	-0.232	0.000	0.000	0.000	0.000
120	A	121	GLU	-2	-1.784	-1.859	23.521	-25.218	-25.218	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)