FMO DATABASE

FMODB ID: K2VZ3

Calculation Name: 2DSR-G-Xray540

Preferred Name: Insulin-like growth factor binding protein 4

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2DSR

Chain ID: G

ChEMBL ID: CHEMBL2310

UniProt ID: P22692

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-472874.719937
FMO2-HF: Nuclear repulsion	440927.483577
FMO2-HF: Total energy	-31947.236361
FMO2-MP2: Total energy	-32036.214278

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(G:151:GLY)

Summations of interaction energy for fragment #1(G:151: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.
-0.244	4.934	2.616	-3.537	-4.254	-0.019

Interaction energy analysis for fragmet #1(G:151:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.066 / q_NPA : 0.031

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	G	152	SER	0	-0.026	0.055	4.534	0.330	0.568	-0.001	-0.085	-0.152	0.000
4	G	153	CYS	0	0.191	-0.088	3.754	-0.543	1.041	-0.002	-0.845	-0.736	0.003
5	G	153	CYS	0	-0.254	0.233	5.020	0.197	0.197	0.000	0.000	0.000	0.000
6	G	154	GLN	0	0.137	-0.084	3.687	1.357	1.547	0.005	-0.030	-0.166	0.000
7	G	154	GLN	0	-0.089	0.096	2.892	-1.235	-0.369	0.112	-0.426	-0.552	0.000
8	G	155	SER	0	-0.012	-0.106	4.556	1.252	1.398	-0.002	-0.033	-0.111	0.000
9	G	155	SER	0	-0.064	0.066	3.787	0.871	1.010	-0.001	-0.069	-0.069	0.000
10	G	156	GLU	0	0.082	-0.101	6.054	0.806	0.806	0.000	0.000	0.000	0.000
11	G	156	GLU	-1	-0.902	-0.794	7.796	-1.426	-1.426	0.000	0.000	0.000	0.000
12	G	157	LEU	0	0.083	-0.089	7.994	0.494	0.494	0.000	0.000	0.000	0.000
13	G	157	LEU	0	-0.089	0.089	7.846	-0.018	-0.018	0.000	0.000	0.000	0.000
14	G	158	HIS	0	0.083	-0.085	8.509	0.376	0.376	0.000	0.000	0.000	0.000
15	G	158	HIS	0	-0.085	0.087	8.656	-0.067	-0.067	0.000	0.000	0.000	0.000
16	G	159	ARG	0	0.173	-0.074	10.185	0.263	0.263	0.000	0.000	0.000	0.000
17	G	159	ARG	1	0.697	0.980	11.155	1.173	1.173	0.000	0.000	0.000	0.000
18	G	160	ALA	0	0.070	-0.123	12.239	0.174	0.174	0.000	0.000	0.000	0.000
19	G	160	ALA	0	-0.064	0.120	13.048	-0.007	-0.007	0.000	0.000	0.000	0.000
20	G	161	LEU	0	0.025	-0.115	13.288	0.137	0.137	0.000	0.000	0.000	0.000
21	G	161	LEU	0	-0.076	0.095	12.089	0.010	0.010	0.000	0.000	0.000	0.000
22	G	162	GLU	0	0.126	-0.082	14.289	0.118	0.118	0.000	0.000	0.000	0.000
23	G	162	GLU	-1	-0.950	-0.812	14.146	-0.803	-0.803	0.000	0.000	0.000	0.000
24	G	163	ARG	0	0.091	-0.092	16.040	0.082	0.082	0.000	0.000	0.000	0.000
25	G	163	ARG	1	0.757	1.002	15.972	0.660	0.660	0.000	0.000	0.000	0.000
26	G	164	LEU	0	0.066	-0.113	17.917	0.067	0.067	0.000	0.000	0.000	0.000
27	G	164	LEU	0	-0.104	0.101	16.746	0.005	0.005	0.000	0.000	0.000	0.000
28	G	165	ALA	0	0.131	-0.087	18.954	0.054	0.054	0.000	0.000	0.000	0.000
29	G	165	ALA	0	-0.080	0.108	19.159	-0.003	-0.003	0.000	0.000	0.000	0.000
30	G	166	ALA	0	0.052	-0.105	20.693	0.042	0.042	0.000	0.000	0.000	0.000
31	G	166	ALA	0	-0.088	0.101	20.965	-0.003	-0.003	0.000	0.000	0.000	0.000
32	G	167	SER	0	-0.025	-0.082	22.494	0.022	0.022	0.000	0.000	0.000	0.000
33	G	167	SER	0	-0.045	0.041	26.001	-0.006	-0.006	0.000	0.000	0.000	0.000
34	G	168	GLN	0	0.018	-0.096	24.894	-0.022	-0.022	0.000	0.000	0.000	0.000
35	G	168	GLN	0	-0.055	0.097	24.821	0.021	0.021	0.000	0.000	0.000	0.000
36	G	169	SER	0	0.069	-0.077	27.328	0.008	0.008	0.000	0.000	0.000	0.000
37	G	169	SER	0	-0.030	0.085	28.056	0.003	0.003	0.000	0.000	0.000	0.000
38	G	170	ARG	0	0.012	-0.101	23.877	0.016	0.016	0.000	0.000	0.000	0.000
39	G	170	ARG	1	0.748	0.976	22.364	0.342	0.342	0.000	0.000	0.000	0.000
40	G	171	THR	0	-0.022	-0.109	25.338	0.011	0.011	0.000	0.000	0.000	0.000
41	G	171	THR	0	-0.013	0.058	26.777	0.003	0.003	0.000	0.000	0.000	0.000
42	G	172	HIS	0	0.103	-0.077	23.890	-0.031	-0.031	0.000	0.000	0.000	0.000
43	G	172	HIS	0	-0.051	0.097	24.017	-0.011	-0.011	0.000	0.000	0.000	0.000
44	G	173	GLU	0	0.126	-0.113	24.017	-0.022	-0.022	0.000	0.000	0.000	0.000
45	G	173	GLU	-1	-0.981	-0.828	27.249	-0.204	-0.204	0.000	0.000	0.000	0.000
46	G	174	ASP	0	0.046	-0.111	23.481	-0.015	-0.015	0.000	0.000	0.000	0.000
47	G	174	ASP	-1	-0.810	-0.770	22.807	-0.292	-0.292	0.000	0.000	0.000	0.000
48	G	175	LEU	0	0.028	-0.103	19.825	-0.043	-0.043	0.000	0.000	0.000	0.000
49	G	175	LEU	0	-0.083	0.102	18.690	-0.002	-0.002	0.000	0.000	0.000	0.000
50	G	176	TYR	0	0.093	-0.085	19.636	-0.048	-0.048	0.000	0.000	0.000	0.000
51	G	176	TYR	0	-0.090	0.083	23.363	0.008	0.008	0.000	0.000	0.000	0.000
52	G	177	ILE	0	-0.007	-0.113	20.957	-0.023	-0.023	0.000	0.000	0.000	0.000
53	G	177	ILE	0	-0.092	0.093	22.555	0.003	0.003	0.000	0.000	0.000	0.000
54	G	178	ILE	0	0.000	-0.117	18.396	-0.020	-0.020	0.000	0.000	0.000	0.000
55	G	178	ILE	0	-0.076	0.092	17.025	-0.005	-0.005	0.000	0.000	0.000	0.000
56	G	179	PRO	0	0.011	-0.096	15.833	-0.021	-0.021	0.000	0.000	0.000	0.000
57	G	180	ILE	0	0.114	-0.008	13.286	-0.138	-0.138	0.000	0.000	0.000	0.000
58	G	180	ILE	0	-0.087	0.113	12.518	0.002	0.002	0.000	0.000	0.000	0.000
59	G	181	PRO	0	-0.056	-0.113	9.431	0.089	0.089	0.000	0.000	0.000	0.000
60	G	182	ASN	0	0.228	0.075	11.008	-0.075	-0.075	0.000	0.000	0.000	0.000
61	G	182	ASN	0	-0.198	0.035	12.913	0.026	0.026	0.000	0.000	0.000	0.000
62	G	183	CYS	0	0.077	-0.135	7.319	0.156	0.156	0.000	0.000	0.000	0.000
63	G	184	ASP	0	0.071	-0.068	7.288	0.131	0.131	0.000	0.000	0.000	0.000
64	G	184	ASP	-1	-0.891	-0.819	6.163	0.693	0.693	0.000	0.000	0.000	0.000
65	G	185	ARG	0	0.139	-0.064	6.736	-0.289	-0.289	0.000	0.000	0.000	0.000
66	G	185	ARG	1	0.857	1.052	9.425	-0.465	-0.465	0.000	0.000	0.000	0.000
67	G	186	ASN	0	0.022	-0.098	5.629	-0.239	-0.239	0.000	0.000	0.000	0.000
68	G	186	ASN	0	-0.175	0.025	6.106	0.106	0.106	0.000	0.000	0.000	0.000
69	G	187	GLY	0	0.083	-0.074	2.126	2.943	3.580	1.202	-0.901	-0.937	-0.005
70	G	188	ASN	0	0.081	0.038	2.793	-4.901	-4.226	1.180	-0.843	-1.011	-0.015
71	G	188	ASN	0	-0.135	0.048	3.250	-1.147	-0.449	0.121	-0.287	-0.531	-0.002
72	G	189	PHE	0	0.095	-0.113	3.998	-0.182	-0.177	0.002	-0.018	0.011	0.000
73	G	189	PHE	0	-0.043	0.133	6.469	-0.081	-0.081	0.000	0.000	0.000	0.000
74	G	190	HIS	0	0.044	-0.121	7.569	0.286	0.286	0.000	0.000	0.000	0.000
75	G	190	HIS	0	-0.095	0.108	11.404	0.087	0.087	0.000	0.000	0.000	0.000
76	G	191	PRO	0	-0.031	-0.121	10.870	-0.074	-0.074	0.000	0.000	0.000	0.000
77	G	192	LYS	0	0.197	0.062	13.300	-0.008	-0.008	0.000	0.000	0.000	0.000
78	G	192	LYS	1	0.668	0.958	16.538	0.131	0.131	0.000	0.000	0.000	0.000
79	G	193	GLN	0	0.030	-0.137	14.580	-0.005	-0.005	0.000	0.000	0.000	0.000
80	G	193	GLN	0	-0.086	0.094	10.902	-0.071	-0.071	0.000	0.000	0.000	0.000
81	G	194	CYS	0	0.040	-0.112	15.329	0.048	0.048	0.000	0.000	0.000	0.000
82	G	194	CYS	0	-0.231	0.166	18.992	0.018	0.018	0.000	0.000	0.000	0.000
83	G	195	HIS	0	0.130	-0.054	17.914	-0.062	-0.062	0.000	0.000	0.000	0.000
84	G	195	HIS	0	-0.040	0.113	20.464	0.025	0.025	0.000	0.000	0.000	0.000
85	G	196	PRO	0	-0.018	-0.095	19.697	0.021	0.021	0.000	0.000	0.000	0.000
86	G	197	ALA	0	0.116	0.011	21.630	0.008	0.008	0.000	0.000	0.000	0.000
87	G	197	ALA	0	-0.103	0.080	25.303	0.003	0.003	0.000	0.000	0.000	0.000
88	G	198	LEU	0	-0.022	-0.133	25.261	-0.013	-0.013	0.000	0.000	0.000	0.000
89	G	198	LEU	0	-0.007	0.128	25.860	0.000	0.000	0.000	0.000	0.000	0.000
90	G	199	ASP	0	0.081	-0.098	28.157	0.006	0.006	0.000	0.000	0.000	0.000
91	G	199	ASP	-1	-0.978	-0.817	31.905	-0.162	-0.162	0.000	0.000	0.000	0.000
92	G	200	GLY	0	0.017	-0.118	31.280	0.009	0.009	0.000	0.000	0.000	0.000
93	G	201	GLN	0	0.018	-0.035	30.041	0.010	0.010	0.000	0.000	0.000	0.000
94	G	201	GLN	0	-0.082	0.109	30.024	0.002	0.002	0.000	0.000	0.000	0.000
95	G	202	ARG	0	0.126	-0.081	26.095	-0.016	-0.016	0.000	0.000	0.000	0.000
96	G	202	ARG	1	0.835	1.047	21.654	0.178	0.178	0.000	0.000	0.000	0.000
97	G	203	GLY	0	0.017	-0.075	23.242	0.009	0.009	0.000	0.000	0.000	0.000
98	G	204	LYS	0	0.059	0.002	23.520	0.004	0.004	0.000	0.000	0.000	0.000
99	G	204	LYS	1	0.769	1.012	24.747	0.141	0.141	0.000	0.000	0.000	0.000
100	G	205	CYS	0	0.037	-0.124	20.060	-0.033	-0.033	0.000	0.000	0.000	0.000
101	G	206	TRP	0	0.127	-0.100	18.618	0.037	0.037	0.000	0.000	0.000	0.000
102	G	206	TRP	0	-0.047	0.113	15.418	0.018	0.018	0.000	0.000	0.000	0.000
103	G	207	CYS	0	0.136	-0.096	16.565	-0.035	-0.035	0.000	0.000	0.000	0.000
104	G	207	CYS	0	-0.239	0.181	17.019	-0.003	-0.003	0.000	0.000	0.000	0.000
105	G	208	VAL	0	0.014	-0.110	12.844	0.021	0.021	0.000	0.000	0.000	0.000
106	G	208	VAL	0	-0.022	0.113	11.353	-0.017	-0.017	0.000	0.000	0.000	0.000
107	G	209	ASP	0	0.106	-0.093	11.770	0.071	0.071	0.000	0.000	0.000	0.000
108	G	209	ASP	-1	-0.863	-0.801	9.895	-0.111	-0.111	0.000	0.000	0.000	0.000
109	G	210	ARG	0	0.040	-0.090	9.003	-0.216	-0.216	0.000	0.000	0.000	0.000
110	G	210	ARG	1	0.876	1.059	8.660	-0.131	-0.131	0.000	0.000	0.000	0.000
111	G	211	LYS	0	0.151	-0.059	5.684	-0.125	-0.125	0.000	0.000	0.000	0.000
112	G	211	LYS	1	0.858	1.071	5.870	-0.542	-0.542	0.000	0.000	0.000	0.000
113	G	212	THR	0	-0.044	-0.094	5.696	-0.564	-0.564	0.000	0.000	0.000	0.000
114	G	212	THR	0	-0.073	0.050	9.018	0.037	0.037	0.000	0.000	0.000	0.000
115	G	213	GLY	0	0.079	-0.086	8.347	-0.071	-0.071	0.000	0.000	0.000	0.000
116	G	214	VAL	0	0.098	-0.013	10.145	0.026	0.026	0.000	0.000	0.000	0.000
117	G	214	VAL	0	-0.084	0.117	12.440	0.006	0.006	0.000	0.000	0.000	0.000
118	G	215	LYS	0	0.114	-0.076	13.571	0.033	0.033	0.000	0.000	0.000	0.000
119	G	215	LYS	1	0.740	1.008	17.252	0.212	0.212	0.000	0.000	0.000	0.000
120	G	216	LEU	0	0.031	-0.131	16.421	0.010	0.010	0.000	0.000	0.000	0.000
121	G	216	LEU	0	-0.074	0.119	15.238	0.008	0.008	0.000	0.000	0.000	0.000
122	G	217	PRO	0	-0.054	-0.120	18.031	-0.010	-0.010	0.000	0.000	0.000	0.000
123	G	218	GLY	0	0.053	0.014	21.896	0.016	0.016	0.000	0.000	0.000	0.000
124	G	219	GLY	0	0.034	0.027	23.710	-0.015	-0.015	0.000	0.000	0.000	0.000
125	G	220	LEU	0	0.047	-0.006	23.260	-0.017	-0.017	0.000	0.000	0.000	0.000
126	G	220	LEU	0	-0.078	0.105	22.166	-0.003	-0.003	0.000	0.000	0.000	0.000
127	G	221	GLU	0	0.068	-0.105	23.584	0.002	0.002	0.000	0.000	0.000	0.000
128	G	221	GLU	-1	-0.851	-0.772	24.844	-0.123	-0.123	0.000	0.000	0.000	0.000
129	G	222	PRO	0	0.098	-0.084	23.637	-0.022	-0.022	0.000	0.000	0.000	0.000
130	G	223	LYS	0	0.157	0.020	21.968	0.009	0.009	0.000	0.000	0.000	0.000
131	G	223	LYS	1	0.857	1.066	20.021	0.115	0.115	0.000	0.000	0.000	0.000
132	G	224	GLY	0	-0.108	-0.167	22.606	0.005	0.005	0.000	0.000	0.000	0.000
133	G	225	GLU	0	0.080	0.014	25.435	0.014	0.014	0.000	0.000	0.000	0.000
134	G	225	GLU	-1	-0.943	-0.834	27.062	-0.094	-0.094	0.000	0.000	0.000	0.000
135	G	226	LEU	0	0.162	-0.082	22.692	0.015	0.015	0.000	0.000	0.000	0.000
136	G	226	LEU	0	-0.148	0.098	20.122	-0.004	-0.004	0.000	0.000	0.000	0.000
137	G	227	ASP	0	0.018	-0.119	21.217	-0.009	-0.009	0.000	0.000	0.000	0.000
138	G	227	ASP	-1	-0.861	-0.790	20.844	-0.017	-0.017	0.000	0.000	0.000	0.000
139	G	228	CYS	0	0.002	-0.114	17.762	-0.006	-0.006	0.000	0.000	0.000	0.000
140	G	229	HIS	0	0.005	-0.094	17.730	0.004	0.004	0.000	0.000	0.000	0.000
141	G	229	HIS	0	0.039	0.014	16.687	0.026	0.026	0.000	0.000	0.000	0.000

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