FMO DATABASE

FMODB ID: JKJG9

Calculation Name: 1X0H-A-Other549

Preferred Name: Ras GTPase-activating-like protein IQGAP1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X0H

Chain ID: A

ChEMBL ID: CHEMBL4295763

UniProt ID: P46940

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-838706.150742
FMO2-HF: Nuclear repulsion	794756.074727
FMO2-HF: Total energy	-43950.076015
FMO2-MP2: Total energy	-44077.831463

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: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.
-23.806	-22.463	-0.01	-0.542	-0.789	-0.002

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 : 0.862 / q_NPA : 0.913

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	3	SER	0	0.006	0.001	3.674	5.249	6.381	-0.009	-0.457	-0.665	-0.002
4	A	4	GLY	0	0.017	0.007	4.034	-7.310	-7.099	-0.001	-0.085	-0.124	0.000
5	A	5	SER	0	-0.031	-0.001	5.909	2.550	2.550	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.026	0.009	7.283	1.059	1.059	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.018	0.020	9.810	1.411	1.411	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.023	-0.022	13.428	0.343	0.343	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.041	0.032	16.497	0.059	0.059	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.002	0.002	18.217	0.150	0.150	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.920	0.963	20.413	13.626	13.626	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.025	0.009	22.299	-0.367	-0.367	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.003	0.003	26.294	0.161	0.161	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.074	0.034	30.027	-0.139	-0.139	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.038	0.022	32.688	0.033	0.033	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.903	0.954	27.374	10.764	10.764	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.022	0.011	27.129	-0.280	-0.280	0.000	0.000	0.000	0.000
18	A	18	HIS	0	-0.022	0.000	30.530	0.114	0.114	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.937	-0.970	32.119	-9.030	-9.030	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.809	0.908	25.930	11.587	11.587	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.052	0.037	31.624	-0.020	-0.020	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.049	-0.018	28.736	0.080	0.080	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.039	-0.022	32.102	0.089	0.089	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.005	0.000	34.018	0.116	0.116	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.906	-0.969	37.744	-7.333	-7.333	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.035	-0.036	36.237	-0.212	-0.212	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.782	-0.858	40.321	-7.073	-7.073	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.876	-0.948	42.063	-7.410	-7.410	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.092	-0.025	38.876	0.031	0.031	0.000	0.000	0.000	0.000
30	A	30	GLN	0	0.068	0.033	42.125	-0.093	-0.093	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.088	0.043	39.292	-0.161	-0.161	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.020	-0.015	39.385	-0.196	-0.196	0.000	0.000	0.000	0.000
33	A	33	GLN	0	0.038	0.007	40.209	-0.049	-0.049	0.000	0.000	0.000	0.000
34	A	34	PHE	0	0.005	0.011	35.592	-0.259	-0.259	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.929	0.953	34.623	7.874	7.874	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.053	-0.021	34.613	-0.065	-0.065	0.000	0.000	0.000	0.000
37	A	37	VAL	0	0.049	0.033	33.322	0.068	0.068	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.062	-0.036	26.801	-0.245	-0.245	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.045	0.024	28.064	0.190	0.190	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.881	-0.950	23.947	-12.816	-12.816	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.002	0.002	22.626	0.355	0.355	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.042	0.011	20.564	-0.838	-0.838	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.044	-0.008	16.133	0.451	0.451	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.007	-0.015	18.639	-0.075	-0.075	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.959	-0.975	13.997	-22.210	-22.210	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.892	-0.948	16.484	-14.880	-14.880	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.067	-0.046	18.420	-0.599	-0.599	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.013	-0.001	20.177	0.570	0.570	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.853	-0.912	23.003	-11.756	-11.756	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.007	-0.001	19.879	-0.998	-0.998	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.813	-0.885	23.299	-12.609	-12.609	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.055	-0.041	24.824	-0.327	-0.327	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.904	0.954	27.109	12.182	12.182	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.024	0.005	28.900	-0.199	-0.199	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.910	0.954	28.638	10.676	10.676	0.000	0.000	0.000	0.000
56	A	56	PHE	0	-0.028	-0.024	31.097	0.107	0.107	0.000	0.000	0.000	0.000
57	A	57	MET	0	0.032	0.003	34.854	0.074	0.074	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.044	-0.001	32.075	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.013	0.001	32.025	0.087	0.087	0.000	0.000	0.000	0.000
60	A	60	GLN	0	-0.001	-0.016	29.263	-0.451	-0.451	0.000	0.000	0.000	0.000
61	A	61	MET	0	-0.043	-0.017	31.541	0.024	0.024	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.927	-0.958	31.091	-9.740	-9.740	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.084	-0.057	26.935	0.190	0.190	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.032	0.020	29.754	-0.033	-0.033	0.000	0.000	0.000	0.000
65	A	65	MET	0	0.016	0.018	26.741	-0.230	-0.230	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.044	-0.023	27.416	0.474	0.474	0.000	0.000	0.000	0.000
67	A	67	HIS	0	0.104	0.046	26.648	-0.599	-0.599	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.046	-0.049	25.172	0.265	0.265	0.000	0.000	0.000	0.000
69	A	69	GLN	0	-0.006	-0.009	27.602	0.414	0.414	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.842	-0.927	30.598	-9.558	-9.558	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.041	-0.023	28.077	0.272	0.272	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.007	-0.001	29.033	0.220	0.220	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.059	-0.030	32.832	0.384	0.384	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.010	0.005	35.021	0.248	0.248	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.059	-0.039	32.218	0.070	0.070	0.000	0.000	0.000	0.000
76	A	76	TYR	0	-0.055	-0.019	36.388	0.159	0.159	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.887	-0.931	38.612	-7.566	-7.566	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.008	0.009	40.003	0.217	0.217	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.032	-0.010	39.404	0.102	0.102	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.002	-0.009	37.562	-0.252	-0.252	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.055	-0.028	37.083	-0.225	-0.225	0.000	0.000	0.000	0.000
82	A	82	MET	0	0.049	0.029	31.434	0.110	0.110	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.780	0.885	36.761	7.337	7.337	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.016	0.007	32.008	-0.121	-0.121	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.024	-0.034	31.995	0.166	0.166	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.838	-0.917	37.972	-7.271	-7.271	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.867	0.937	39.722	7.626	7.626	0.000	0.000	0.000	0.000
88	A	88	ALA	0	-0.005	0.005	35.905	0.082	0.082	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.875	0.937	37.689	7.619	7.619	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.005	-0.004	31.192	-0.106	-0.106	0.000	0.000	0.000	0.000
91	A	91	ASN	0	0.055	0.027	34.007	0.112	0.112	0.000	0.000	0.000	0.000
92	A	92	VAL	0	0.053	0.026	32.661	-0.399	-0.399	0.000	0.000	0.000	0.000
93	A	93	ASN	0	0.033	0.011	31.603	-0.494	-0.494	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.050	-0.021	30.550	-0.272	-0.272	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.009	0.000	27.437	-0.466	-0.466	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.041	0.031	26.844	-0.594	-0.594	0.000	0.000	0.000	0.000
97	A	97	PHE	0	-0.008	0.002	25.671	-0.634	-0.634	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.047	-0.024	23.823	-0.530	-0.530	0.000	0.000	0.000	0.000
99	A	99	LEU	0	0.032	0.006	22.338	-0.813	-0.813	0.000	0.000	0.000	0.000
100	A	100	ASN	0	0.048	0.022	20.984	-0.633	-0.633	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.935	0.972	19.566	13.385	13.385	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.809	0.919	18.430	14.915	14.915	0.000	0.000	0.000	0.000
103	A	103	PHE	0	0.028	0.005	16.969	-0.825	-0.825	0.000	0.000	0.000	0.000
104	A	104	TYR	0	-0.020	0.001	16.608	-1.027	-1.027	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.005	0.006	14.258	0.334	0.334	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.888	0.955	12.261	18.442	18.442	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.024	-0.020	7.718	-0.506	-0.506	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.002	0.002	8.066	-3.840	-3.840	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.051	-0.019	10.380	0.963	0.963	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.014	-0.030	13.200	0.250	0.250	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.087	-0.059	16.716	0.410	0.410	0.000	0.000	0.000	0.000
112	A	112	GLY	-1	-0.845	-0.873	18.923	-13.913	-13.913	0.000	0.000	0.000	0.000

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