FMO DATABASE

FMODB ID: 7KZ8K

Calculation Name: 3I6X-A-Xray547

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: 3I6X

Chain ID: A

ChEMBL ID: CHEMBL4295763

UniProt ID: P46940

Base Structure: X-ray

Registration Date: 2025-10-05

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	164
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1783725.948978
FMO2-HF: Nuclear repulsion	1714860.682345
FMO2-HF: Total energy	-68865.266633
FMO2-MP2: Total energy	-69063.034491

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:28:ALA)

Summations of interaction energy for fragment #1(A:28: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.
-59.764	-56.231	0.027	-1.428	-2.133	-0.006

Interaction energy analysis for fragmet #1(A:28:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.844 / q_NPA : 0.904

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	30	GLU	-1	-0.846	-0.923	3.285	-45.386	-42.992	0.013	-1.021	-1.386	-0.004
4	A	31	MET	0	-0.052	-0.025	3.431	5.660	6.624	0.015	-0.392	-0.588	-0.002
5	A	32	ASP	-1	-0.851	-0.920	4.801	-23.254	-23.079	-0.001	-0.015	-0.159	0.000
6	A	33	GLU	-1	-0.760	-0.865	7.413	-23.997	-23.997	0.000	0.000	0.000	0.000
7	A	34	ARG	1	0.885	0.941	6.768	38.836	38.836	0.000	0.000	0.000	0.000
8	A	35	ARG	1	0.873	0.947	8.631	31.861	31.861	0.000	0.000	0.000	0.000
9	A	36	ARG	1	0.836	0.916	10.502	28.306	28.306	0.000	0.000	0.000	0.000
10	A	37	GLN	0	0.000	-0.004	11.704	0.533	0.533	0.000	0.000	0.000	0.000
11	A	38	ASN	0	-0.085	-0.059	12.678	-0.277	-0.277	0.000	0.000	0.000	0.000
12	A	39	VAL	0	0.031	0.021	14.508	1.394	1.394	0.000	0.000	0.000	0.000
13	A	40	ALA	0	0.032	0.027	16.500	1.175	1.175	0.000	0.000	0.000	0.000
14	A	41	TYR	0	-0.001	-0.014	17.428	0.863	0.863	0.000	0.000	0.000	0.000
15	A	42	GLU	-1	-0.864	-0.934	16.997	-17.425	-17.425	0.000	0.000	0.000	0.000
16	A	43	TYR	0	-0.071	-0.073	20.534	0.991	0.991	0.000	0.000	0.000	0.000
17	A	44	LEU	0	0.025	0.018	21.244	0.698	0.698	0.000	0.000	0.000	0.000
18	A	45	CYS	0	-0.043	-0.006	22.198	0.660	0.660	0.000	0.000	0.000	0.000
19	A	46	HIS	1	0.831	0.890	23.278	13.316	13.316	0.000	0.000	0.000	0.000
20	A	47	LEU	0	0.036	0.027	25.897	0.589	0.589	0.000	0.000	0.000	0.000
21	A	48	GLU	-1	-0.763	-0.875	27.928	-9.789	-9.789	0.000	0.000	0.000	0.000
22	A	49	GLU	-1	-0.809	-0.895	27.168	-11.302	-11.302	0.000	0.000	0.000	0.000
23	A	50	ALA	0	-0.019	-0.012	30.888	0.412	0.412	0.000	0.000	0.000	0.000
24	A	51	LYS	1	0.793	0.890	32.462	9.363	9.363	0.000	0.000	0.000	0.000
25	A	52	ARG	1	0.860	0.914	30.942	10.296	10.296	0.000	0.000	0.000	0.000
26	A	53	TRP	0	-0.029	-0.002	35.188	0.248	0.248	0.000	0.000	0.000	0.000
27	A	54	MET	0	0.007	0.002	36.919	0.214	0.214	0.000	0.000	0.000	0.000
28	A	55	GLU	-1	-0.770	-0.865	37.222	-8.380	-8.380	0.000	0.000	0.000	0.000
29	A	56	ALA	0	-0.054	-0.027	39.631	0.247	0.247	0.000	0.000	0.000	0.000
30	A	57	CYS	0	-0.078	-0.035	40.697	0.203	0.203	0.000	0.000	0.000	0.000
31	A	58	LEU	0	-0.066	-0.037	42.055	0.217	0.217	0.000	0.000	0.000	0.000
32	A	59	GLY	0	-0.029	-0.003	44.135	0.179	0.179	0.000	0.000	0.000	0.000
33	A	60	GLU	-1	-0.874	-0.925	43.695	-6.926	-6.926	0.000	0.000	0.000	0.000
34	A	61	ASP	-1	-0.899	-0.943	40.477	-7.882	-7.882	0.000	0.000	0.000	0.000
35	A	62	LEU	0	-0.044	-0.032	36.804	0.099	0.099	0.000	0.000	0.000	0.000
36	A	63	PRO	0	0.001	0.001	35.194	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	64	PRO	0	0.043	0.020	32.545	-0.092	-0.092	0.000	0.000	0.000	0.000
38	A	65	THR	0	0.025	0.013	28.207	-0.063	-0.063	0.000	0.000	0.000	0.000
39	A	66	THR	0	-0.019	-0.032	26.893	-0.128	-0.128	0.000	0.000	0.000	0.000
40	A	67	GLU	-1	-0.909	-0.955	28.600	-9.531	-9.531	0.000	0.000	0.000	0.000
41	A	68	LEU	0	-0.054	-0.015	31.158	0.307	0.307	0.000	0.000	0.000	0.000
42	A	69	GLU	-1	-0.790	-0.885	27.881	-11.267	-11.267	0.000	0.000	0.000	0.000
43	A	70	GLU	-1	-0.787	-0.867	31.927	-9.145	-9.145	0.000	0.000	0.000	0.000
44	A	71	GLY	0	0.006	-0.003	34.209	0.306	0.306	0.000	0.000	0.000	0.000
45	A	72	LEU	0	0.012	0.000	34.024	0.302	0.302	0.000	0.000	0.000	0.000
46	A	73	ARG	1	0.790	0.875	34.529	9.243	9.243	0.000	0.000	0.000	0.000
47	A	74	ASN	0	-0.024	-0.026	38.125	0.170	0.170	0.000	0.000	0.000	0.000
48	A	75	GLY	0	0.062	0.017	40.578	0.243	0.243	0.000	0.000	0.000	0.000
49	A	76	VAL	0	-0.071	-0.019	41.963	0.099	0.099	0.000	0.000	0.000	0.000
50	A	77	TYR	0	0.032	0.006	40.001	0.104	0.104	0.000	0.000	0.000	0.000
51	A	78	LEU	0	0.022	0.026	37.532	0.040	0.040	0.000	0.000	0.000	0.000
52	A	79	ALA	0	0.002	-0.002	41.644	0.106	0.106	0.000	0.000	0.000	0.000
53	A	80	LYS	1	0.769	0.868	44.709	7.107	7.107	0.000	0.000	0.000	0.000
54	A	81	LEU	0	0.015	0.018	39.779	0.116	0.116	0.000	0.000	0.000	0.000
55	A	82	GLY	0	0.035	0.002	43.990	0.061	0.061	0.000	0.000	0.000	0.000
56	A	83	ASN	0	-0.114	-0.080	45.924	0.134	0.134	0.000	0.000	0.000	0.000
57	A	84	PHE	0	0.013	0.005	43.896	0.095	0.095	0.000	0.000	0.000	0.000
58	A	85	PHE	0	0.016	0.006	42.750	0.067	0.067	0.000	0.000	0.000	0.000
59	A	86	SER	0	0.024	0.010	47.270	0.088	0.088	0.000	0.000	0.000	0.000
60	A	87	PRO	0	0.022	0.013	49.774	0.065	0.065	0.000	0.000	0.000	0.000
61	A	88	LYS	1	0.717	0.848	52.663	6.045	6.045	0.000	0.000	0.000	0.000
62	A	89	VAL	0	-0.046	-0.012	50.443	0.100	0.100	0.000	0.000	0.000	0.000
63	A	90	VAL	0	0.016	0.027	47.916	0.046	0.046	0.000	0.000	0.000	0.000
64	A	91	SER	0	0.018	0.009	51.282	0.061	0.061	0.000	0.000	0.000	0.000
65	A	92	LEU	0	0.093	0.031	49.802	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	93	LYS	1	0.887	0.933	52.616	5.403	5.403	0.000	0.000	0.000	0.000
67	A	94	LYS	1	0.937	0.965	53.626	5.811	5.811	0.000	0.000	0.000	0.000
68	A	95	ILE	0	0.033	0.061	47.820	-0.038	-0.038	0.000	0.000	0.000	0.000
69	A	96	TYR	0	0.014	0.002	48.170	0.196	0.196	0.000	0.000	0.000	0.000
70	A	97	ASP	-1	-0.731	-0.866	47.086	-6.956	-6.956	0.000	0.000	0.000	0.000
71	A	98	ARG	1	0.932	0.982	47.819	6.054	6.054	0.000	0.000	0.000	0.000
72	A	99	GLU	-1	-0.852	-0.935	47.973	-6.505	-6.505	0.000	0.000	0.000	0.000
73	A	100	GLN	0	-0.014	-0.008	42.362	-0.191	-0.191	0.000	0.000	0.000	0.000
74	A	101	THR	0	0.005	0.005	46.420	-0.109	-0.109	0.000	0.000	0.000	0.000
75	A	102	ARG	1	0.833	0.908	48.183	6.485	6.485	0.000	0.000	0.000	0.000
76	A	103	TYR	0	0.031	0.005	38.301	0.061	0.061	0.000	0.000	0.000	0.000
77	A	104	LYS	1	0.900	0.951	44.069	6.917	6.917	0.000	0.000	0.000	0.000
78	A	105	ALA	0	-0.019	0.014	45.232	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	106	THR	0	-0.078	-0.059	45.725	0.102	0.102	0.000	0.000	0.000	0.000
80	A	107	GLY	0	0.071	0.056	42.196	0.032	0.032	0.000	0.000	0.000	0.000
81	A	108	LEU	0	0.005	0.011	38.803	0.165	0.165	0.000	0.000	0.000	0.000
82	A	109	HIS	0	0.013	0.005	42.947	0.060	0.060	0.000	0.000	0.000	0.000
83	A	110	PHE	0	0.079	0.043	45.788	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	111	ARG	1	0.937	0.963	46.878	6.092	6.092	0.000	0.000	0.000	0.000
85	A	112	HIS	0	-0.029	-0.033	44.042	0.029	0.029	0.000	0.000	0.000	0.000
86	A	113	THR	0	-0.003	-0.006	43.789	-0.159	-0.159	0.000	0.000	0.000	0.000
87	A	114	ASP	-1	-0.905	-0.948	44.900	-6.532	-6.532	0.000	0.000	0.000	0.000
88	A	115	ASN	0	-0.070	-0.038	44.830	0.161	0.161	0.000	0.000	0.000	0.000
89	A	116	VAL	0	0.034	0.018	40.345	-0.048	-0.048	0.000	0.000	0.000	0.000
90	A	117	ILE	0	-0.004	0.006	43.169	-0.054	-0.054	0.000	0.000	0.000	0.000
91	A	118	GLN	0	-0.040	-0.038	45.793	0.064	0.064	0.000	0.000	0.000	0.000
92	A	119	TRP	0	0.021	-0.002	36.994	0.024	0.024	0.000	0.000	0.000	0.000
93	A	120	LEU	0	0.034	0.014	40.052	-0.021	-0.021	0.000	0.000	0.000	0.000
94	A	121	ASN	0	-0.051	-0.038	43.877	0.089	0.089	0.000	0.000	0.000	0.000
95	A	122	ALA	0	-0.012	0.004	45.647	0.090	0.090	0.000	0.000	0.000	0.000
96	A	123	MET	0	-0.003	-0.008	38.420	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	124	ASP	-1	-0.886	-0.919	44.228	-6.884	-6.884	0.000	0.000	0.000	0.000
98	A	125	GLU	-1	-0.796	-0.874	46.496	-6.050	-6.050	0.000	0.000	0.000	0.000
99	A	126	ILE	0	-0.033	-0.004	43.362	0.073	0.073	0.000	0.000	0.000	0.000
100	A	127	GLY	0	0.013	0.019	46.166	-0.043	-0.043	0.000	0.000	0.000	0.000
101	A	128	LEU	0	-0.007	0.012	38.798	-0.115	-0.115	0.000	0.000	0.000	0.000
102	A	129	PRO	0	-0.011	-0.016	38.682	0.029	0.029	0.000	0.000	0.000	0.000
103	A	130	LYS	1	0.900	0.923	38.941	6.932	6.932	0.000	0.000	0.000	0.000
104	A	131	ILE	0	-0.053	-0.008	33.695	-0.074	-0.074	0.000	0.000	0.000	0.000
105	A	132	PHE	0	0.011	-0.007	33.085	-0.254	-0.254	0.000	0.000	0.000	0.000
106	A	133	TYR	0	0.001	-0.010	34.890	-0.078	-0.078	0.000	0.000	0.000	0.000
107	A	134	PRO	0	-0.008	-0.003	34.531	-0.150	-0.150	0.000	0.000	0.000	0.000
108	A	135	GLU	-1	-0.881	-0.945	35.925	-8.559	-8.559	0.000	0.000	0.000	0.000
109	A	136	THR	0	0.010	-0.020	37.555	-0.132	-0.132	0.000	0.000	0.000	0.000
110	A	137	THR	0	-0.044	-0.036	36.984	-0.127	-0.127	0.000	0.000	0.000	0.000
111	A	138	ASP	-1	-0.800	-0.887	33.425	-9.758	-9.758	0.000	0.000	0.000	0.000
112	A	139	ILE	0	0.030	0.004	33.612	-0.242	-0.242	0.000	0.000	0.000	0.000
113	A	140	TYR	0	-0.006	-0.002	35.936	0.018	0.018	0.000	0.000	0.000	0.000
114	A	141	ASP	-1	-0.857	-0.915	36.377	-8.349	-8.349	0.000	0.000	0.000	0.000
115	A	142	ARG	1	0.785	0.868	28.338	10.710	10.710	0.000	0.000	0.000	0.000
116	A	143	LYS	1	0.828	0.925	31.245	9.135	9.135	0.000	0.000	0.000	0.000
117	A	144	ASN	0	0.008	-0.013	28.573	-0.507	-0.507	0.000	0.000	0.000	0.000
118	A	145	MET	0	0.021	0.039	29.765	0.297	0.297	0.000	0.000	0.000	0.000
119	A	146	PRO	0	0.083	0.044	25.760	0.250	0.250	0.000	0.000	0.000	0.000
120	A	147	ARG	1	0.841	0.931	28.140	9.577	9.577	0.000	0.000	0.000	0.000
121	A	148	CYS	0	-0.039	-0.011	30.745	0.370	0.370	0.000	0.000	0.000	0.000
122	A	149	ILE	0	0.046	0.028	28.811	0.283	0.283	0.000	0.000	0.000	0.000
123	A	150	TYR	0	-0.003	-0.013	23.687	0.051	0.051	0.000	0.000	0.000	0.000
124	A	151	CYS	0	-0.061	-0.001	30.580	0.284	0.284	0.000	0.000	0.000	0.000
125	A	152	ILE	0	0.000	0.000	33.639	0.292	0.292	0.000	0.000	0.000	0.000
126	A	153	HIS	0	-0.041	-0.020	29.662	0.269	0.269	0.000	0.000	0.000	0.000
127	A	154	ALA	0	-0.028	-0.011	33.137	0.171	0.171	0.000	0.000	0.000	0.000
128	A	155	LEU	0	-0.011	-0.009	35.080	0.245	0.245	0.000	0.000	0.000	0.000
129	A	156	SER	0	0.024	0.016	35.721	0.213	0.213	0.000	0.000	0.000	0.000
130	A	157	LEU	0	-0.013	-0.009	34.476	0.215	0.215	0.000	0.000	0.000	0.000
131	A	158	TYR	0	-0.064	-0.054	37.435	0.148	0.148	0.000	0.000	0.000	0.000
132	A	159	LEU	0	0.039	0.000	40.491	0.213	0.213	0.000	0.000	0.000	0.000
133	A	160	PHE	0	-0.039	-0.001	38.975	0.164	0.164	0.000	0.000	0.000	0.000
134	A	161	LYS	1	0.877	0.930	39.065	8.224	8.224	0.000	0.000	0.000	0.000
135	A	162	LEU	0	-0.010	0.007	42.977	0.167	0.167	0.000	0.000	0.000	0.000
136	A	163	GLY	0	-0.039	-0.011	45.114	0.176	0.176	0.000	0.000	0.000	0.000
137	A	164	LEU	0	-0.038	-0.021	45.570	0.103	0.103	0.000	0.000	0.000	0.000
138	A	165	ALA	0	0.011	0.007	42.138	0.036	0.036	0.000	0.000	0.000	0.000
139	A	166	PRO	0	0.000	0.007	40.636	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	167	GLN	0	-0.018	-0.012	36.051	-0.099	-0.099	0.000	0.000	0.000	0.000
141	A	168	ILE	0	-0.004	0.011	32.286	0.063	0.063	0.000	0.000	0.000	0.000
142	A	169	GLN	0	-0.001	-0.008	32.402	-0.210	-0.210	0.000	0.000	0.000	0.000
143	A	170	ASP	-1	-0.818	-0.903	26.961	-11.851	-11.851	0.000	0.000	0.000	0.000
144	A	171	LEU	0	-0.038	-0.045	27.669	0.251	0.251	0.000	0.000	0.000	0.000
145	A	172	TYR	0	0.000	0.028	17.436	-0.129	-0.129	0.000	0.000	0.000	0.000
146	A	173	GLY	0	0.015	0.008	22.434	-0.555	-0.555	0.000	0.000	0.000	0.000
147	A	174	LYS	1	0.744	0.865	23.475	11.141	11.141	0.000	0.000	0.000	0.000
148	A	175	VAL	0	-0.017	-0.010	25.099	0.572	0.572	0.000	0.000	0.000	0.000
149	A	176	ASP	-1	-0.895	-0.920	22.174	-14.198	-14.198	0.000	0.000	0.000	0.000
150	A	177	PHE	0	-0.020	-0.029	22.364	0.578	0.578	0.000	0.000	0.000	0.000
151	A	178	THR	0	-0.044	-0.052	22.170	-0.571	-0.571	0.000	0.000	0.000	0.000
152	A	179	GLU	-1	-0.923	-0.977	16.820	-18.551	-18.551	0.000	0.000	0.000	0.000
153	A	180	GLU	-1	-0.883	-0.924	19.310	-13.993	-13.993	0.000	0.000	0.000	0.000
154	A	181	GLU	-1	-0.787	-0.855	21.884	-12.205	-12.205	0.000	0.000	0.000	0.000
155	A	182	ILE	0	-0.035	-0.017	16.615	-0.193	-0.193	0.000	0.000	0.000	0.000
156	A	183	ASN	0	0.014	-0.006	16.126	-1.559	-1.559	0.000	0.000	0.000	0.000
157	A	184	ASN	0	-0.022	-0.016	18.635	-0.253	-0.253	0.000	0.000	0.000	0.000
158	A	185	MET	0	-0.013	-0.001	21.011	0.200	0.200	0.000	0.000	0.000	0.000
159	A	186	LYS	1	0.790	0.881	13.071	22.511	22.511	0.000	0.000	0.000	0.000
160	A	187	THR	0	0.021	0.007	18.287	-0.097	-0.097	0.000	0.000	0.000	0.000
161	A	188	GLU	-1	-0.881	-0.916	20.141	-11.758	-11.758	0.000	0.000	0.000	0.000
162	A	189	LEU	0	-0.095	-0.050	20.013	0.499	0.499	0.000	0.000	0.000	0.000
163	A	190	GLU	-1	-0.929	-0.967	15.829	-20.666	-20.666	0.000	0.000	0.000	0.000
164	A	191	LYS	0	-0.031	-0.006	20.385	0.424	0.424	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:ALA)