FMO DATABASE

FMODB ID: QK2GY

Calculation Name: 1X4B-A-Other547

Preferred Name: Heterogeneous nuclear ribonucleoproteins A2/B1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1X4B

Chain ID: A

ChEMBL ID: CHEMBL3124741

UniProt ID: P22626

Base Structure: SolutionNMR

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-835259.05332
FMO2-HF: Nuclear repulsion	789766.085944
FMO2-HF: Total energy	-45492.967376
FMO2-MP2: Total energy	-45623.302979

3D Structure

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:1:GLY)

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

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.
13.487	14.403	-0.016	-0.297	-0.604	-0.001

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.916

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	3	SER	0	0.023	0.006	3.812	5.152	6.068	-0.016	-0.297	-0.604	-0.001
4	A	4	GLY	0	0.044	0.027	7.108	0.044	0.044	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.016	-0.008	10.798	0.703	0.703	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.027	-0.008	14.283	0.442	0.442	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.055	0.023	18.017	0.087	0.087	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.034	-0.025	21.632	-0.070	-0.070	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.925	-0.943	25.197	-11.305	-11.305	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.904	0.942	27.447	10.280	10.280	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.005	0.006	30.880	-0.077	-0.077	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.042	-0.022	32.770	0.159	0.159	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.886	-0.927	36.360	-7.818	-7.818	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.020	-0.028	39.340	0.104	0.104	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.001	0.008	40.050	0.024	0.024	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.010	0.014	42.972	0.127	0.127	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.003	0.003	45.906	-0.095	-0.095	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.770	-0.873	48.305	-6.232	-6.232	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.784	0.858	50.150	6.000	6.000	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.898	0.944	44.672	7.140	7.140	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.963	0.988	49.644	5.786	5.786	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.963	0.978	49.395	5.913	5.913	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.829	-0.915	47.520	-6.828	-6.828	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.944	0.954	46.963	6.114	6.114	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.859	-0.910	46.037	-6.842	-6.842	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.010	-0.015	43.344	-0.177	-0.177	0.000	0.000	0.000	0.000
27	A	27	PHE	0	-0.022	-0.015	42.259	-0.172	-0.172	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.842	0.918	41.996	6.809	6.809	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.881	0.963	40.734	7.248	7.248	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.024	0.011	34.810	-0.132	-0.132	0.000	0.000	0.000	0.000
31	A	31	PHE	0	-0.044	-0.017	33.871	0.138	0.138	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.003	-0.004	32.462	-0.297	-0.297	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.013	0.000	31.395	0.232	0.232	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.051	0.030	29.037	-0.237	-0.237	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.036	-0.040	29.970	-0.161	-0.161	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.026	-0.055	30.661	0.297	0.297	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.101	-0.053	31.427	-0.102	-0.102	0.000	0.000	0.000	0.000
38	A	38	GLU	-1	-0.874	-0.927	34.275	-8.545	-8.545	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.059	-0.012	33.815	0.152	0.152	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.031	0.017	36.331	0.050	0.050	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.825	-0.932	39.433	-7.376	-7.376	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.907	-0.950	41.319	-7.222	-7.222	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.004	-0.005	37.366	-0.076	-0.076	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.034	-0.016	35.377	-0.243	-0.243	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.878	0.921	37.404	7.018	7.018	0.000	0.000	0.000	0.000
46	A	46	ASN	0	0.004	0.002	37.121	0.098	0.098	0.000	0.000	0.000	0.000
47	A	47	TYR	0	0.015	0.025	29.228	-0.172	-0.172	0.000	0.000	0.000	0.000
48	A	48	TYR	0	-0.027	-0.064	31.805	-0.080	-0.080	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.851	-0.917	37.209	-7.211	-7.211	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.117	-0.051	33.892	0.170	0.170	0.000	0.000	0.000	0.000
51	A	51	TRP	0	-0.002	0.007	31.609	0.159	0.159	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.032	-0.013	38.224	0.173	0.173	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.929	0.986	41.519	7.152	7.152	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.020	-0.011	39.536	0.056	0.056	0.000	0.000	0.000	0.000
55	A	55	THR	0	-0.083	-0.042	43.855	0.145	0.145	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.883	-0.943	45.656	-6.607	-6.607	0.000	0.000	0.000	0.000
57	A	57	CYS	0	-0.077	-0.042	42.187	-0.210	-0.210	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.034	0.042	42.543	0.102	0.102	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.023	-0.011	38.687	-0.233	-0.233	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.036	-0.012	39.690	0.243	0.243	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.962	0.983	40.071	7.027	7.027	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.864	-0.929	38.526	-8.330	-8.330	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.013	-0.003	41.325	0.146	0.146	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.012	0.018	42.629	0.152	0.152	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.026	-0.003	40.147	0.159	0.159	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.921	0.957	42.929	6.830	6.830	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.945	0.987	40.329	7.614	7.614	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.026	-0.011	37.833	0.107	0.107	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.892	0.950	34.751	8.820	8.820	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.020	0.023	33.671	-0.253	-0.253	0.000	0.000	0.000	0.000
71	A	71	PHE	0	-0.031	-0.027	33.379	-0.277	-0.277	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.059	0.028	35.765	0.254	0.254	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.067	-0.029	37.722	-0.211	-0.211	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.029	0.014	37.327	0.104	0.104	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.027	0.014	40.463	-0.132	-0.132	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.061	0.028	37.341	0.114	0.114	0.000	0.000	0.000	0.000
77	A	77	SER	0	0.008	0.020	43.082	0.179	0.179	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.018	-0.016	44.765	0.193	0.193	0.000	0.000	0.000	0.000
79	A	79	MET	0	-0.012	-0.012	41.509	-0.040	-0.040	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.033	0.024	40.841	-0.182	-0.182	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.817	-0.918	39.235	-7.499	-7.499	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.006	0.012	37.910	-0.228	-0.228	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.905	-0.961	36.316	-8.670	-8.670	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.026	-0.016	34.651	-0.321	-0.321	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.005	0.004	33.408	-0.295	-0.295	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.087	-0.044	32.023	-0.329	-0.329	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.048	-0.025	29.977	-0.435	-0.435	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.010	0.017	29.181	-0.174	-0.174	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.909	0.973	25.031	11.585	11.585	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.014	-0.010	21.602	-0.183	-0.183	0.000	0.000	0.000	0.000
91	A	91	HIS	0	0.053	0.044	24.615	0.294	0.294	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.035	-0.026	25.555	-0.418	-0.418	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.013	0.011	27.436	0.309	0.309	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.802	-0.873	29.803	-10.104	-10.104	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.006	0.021	27.832	-0.115	-0.115	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.817	0.917	25.512	11.198	11.198	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.017	0.000	21.450	0.288	0.288	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.010	0.010	24.877	0.113	0.113	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.878	-0.958	25.527	-12.533	-12.533	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.019	0.010	28.057	0.382	0.382	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.926	0.948	29.996	10.104	10.104	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.975	0.964	29.306	10.318	10.318	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.005	0.027	35.782	0.226	0.226	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.002	-0.014	38.194	0.123	0.123	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.018	-0.005	38.155	-0.188	-0.188	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.870	0.940	35.323	8.391	8.391	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.945	-0.977	36.723	-8.185	-8.185	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.877	-0.931	38.779	-7.222	-7.222	0.000	0.000	0.000	0.000
109	A	109	SER	0	0.025	0.018	41.742	0.185	0.185	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.028	0.010	43.382	0.127	0.127	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.072	-0.036	46.809	-0.032	-0.032	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.039	0.024	49.530	0.083	0.083	0.000	0.000	0.000	0.000
113	A	113	PRO	0	-0.028	-0.008	51.053	-0.055	-0.055	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.012	-0.005	52.293	0.142	0.142	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.070	-0.051	53.255	-0.046	-0.046	0.000	0.000	0.000	0.000
116	A	116	GLY	-1	-0.913	-0.925	55.369	-5.420	-5.420	0.000	0.000	0.000	0.000

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