FMO DATABASE

FMODB ID: MV91Z

Calculation Name: 4GM2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GM2

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IL98

Base Structure: X-ray

Registration Date: 2023-06-22

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

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	183
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2005078.849863
FMO2-HF: Nuclear repulsion	1932699.272482
FMO2-HF: Total energy	-72379.577381
FMO2-MP2: Total energy	-72593.105546

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:61:PRO)

Summations of interaction energy for fragment #1(A:61:PRO)

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.
-5.543	1.88	3.174	-3.873	-6.725	0.007

Interaction energy analysis for fragmet #1(A:61:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.082 / q_NPA : 0.036

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	63	LEU	0	0.039	0.016	2.370	-4.874	-0.012	0.805	-2.342	-3.325	0.006
4	A	64	LEU	0	0.018	0.016	2.070	-2.296	-0.262	2.366	-1.395	-3.006	0.001
5	A	65	LEU	0	0.069	0.043	3.840	0.414	0.941	0.003	-0.136	-0.394	0.000
6	A	66	SER	0	-0.065	-0.031	5.808	0.578	0.578	0.000	0.000	0.000	0.000
7	A	67	LYS	1	0.897	0.947	7.408	0.654	0.654	0.000	0.000	0.000	0.000
8	A	68	ARG	1	0.812	0.905	8.796	0.451	0.451	0.000	0.000	0.000	0.000
9	A	69	ILE	0	-0.038	-0.009	6.183	0.182	0.182	0.000	0.000	0.000	0.000
10	A	70	ILE	0	0.028	0.024	5.637	-0.501	-0.501	0.000	0.000	0.000	0.000
11	A	71	PHE	0	-0.037	-0.027	5.268	0.127	0.127	0.000	0.000	0.000	0.000
12	A	72	LEU	0	0.007	0.017	6.952	0.360	0.360	0.000	0.000	0.000	0.000
13	A	73	SER	0	-0.033	-0.023	7.811	-0.086	-0.086	0.000	0.000	0.000	0.000
14	A	74	SER	0	0.041	0.016	10.489	0.048	0.048	0.000	0.000	0.000	0.000
15	A	75	PRO	0	0.021	0.033	12.957	-0.035	-0.035	0.000	0.000	0.000	0.000
16	A	76	ILE	0	0.003	-0.008	14.140	0.048	0.048	0.000	0.000	0.000	0.000
17	A	77	TYR	0	0.032	0.010	13.345	-0.029	-0.029	0.000	0.000	0.000	0.000
18	A	78	PRO	0	0.044	0.013	14.838	0.007	0.007	0.000	0.000	0.000	0.000
19	A	79	HIS	0	0.074	0.034	10.410	-0.069	-0.069	0.000	0.000	0.000	0.000
20	A	80	ILE	0	-0.046	-0.008	9.405	0.017	0.017	0.000	0.000	0.000	0.000
21	A	81	SER	0	-0.015	-0.027	11.082	-0.027	-0.027	0.000	0.000	0.000	0.000
22	A	82	GLU	-1	-0.901	-0.941	12.466	0.093	0.093	0.000	0.000	0.000	0.000
23	A	83	GLN	0	-0.009	-0.010	7.131	0.086	0.086	0.000	0.000	0.000	0.000
24	A	84	ILE	0	-0.009	-0.002	9.113	-0.121	-0.121	0.000	0.000	0.000	0.000
25	A	85	ILE	0	0.048	0.025	10.706	-0.081	-0.081	0.000	0.000	0.000	0.000
26	A	86	SER	0	-0.017	-0.005	10.211	-0.037	-0.037	0.000	0.000	0.000	0.000
27	A	87	GLN	0	-0.028	-0.022	5.723	-0.388	-0.388	0.000	0.000	0.000	0.000
28	A	88	LEU	0	-0.002	0.001	9.547	-0.058	-0.058	0.000	0.000	0.000	0.000
29	A	89	LEU	0	-0.002	0.000	12.898	-0.006	-0.006	0.000	0.000	0.000	0.000
30	A	90	TYR	0	-0.005	-0.003	10.080	-0.026	-0.026	0.000	0.000	0.000	0.000
31	A	91	LEU	0	0.019	0.000	9.032	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	92	GLU	-1	-0.748	-0.849	12.926	-0.129	-0.129	0.000	0.000	0.000	0.000
33	A	93	TYR	0	-0.076	-0.048	16.053	0.029	0.029	0.000	0.000	0.000	0.000
34	A	94	GLU	-1	-0.984	-0.966	13.311	-0.272	-0.272	0.000	0.000	0.000	0.000
35	A	95	SER	0	-0.073	-0.051	16.182	0.019	0.019	0.000	0.000	0.000	0.000
36	A	96	LYS	1	0.891	0.963	17.547	0.108	0.108	0.000	0.000	0.000	0.000
37	A	97	ARG	1	1.008	1.006	19.933	0.107	0.107	0.000	0.000	0.000	0.000
38	A	98	LYS	1	0.967	0.983	16.019	0.265	0.265	0.000	0.000	0.000	0.000
39	A	99	PRO	0	0.025	0.015	16.372	-0.023	-0.023	0.000	0.000	0.000	0.000
40	A	100	ILE	0	-0.010	0.004	11.032	-0.047	-0.047	0.000	0.000	0.000	0.000
41	A	101	HIS	0	0.021	0.043	10.733	0.083	0.083	0.000	0.000	0.000	0.000
42	A	102	LEU	0	0.050	0.022	9.906	-0.085	-0.085	0.000	0.000	0.000	0.000
43	A	103	TYR	0	-0.015	-0.014	9.216	0.044	0.044	0.000	0.000	0.000	0.000
44	A	104	ILE	0	0.003	-0.011	10.501	0.060	0.060	0.000	0.000	0.000	0.000
45	A	105	ASN	0	-0.028	-0.013	12.519	-0.044	-0.044	0.000	0.000	0.000	0.000
46	A	106	SER	0	-0.005	-0.020	13.692	0.038	0.038	0.000	0.000	0.000	0.000
47	A	107	THR	0	-0.021	-0.034	15.704	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	108	GLY	0	0.022	0.016	17.794	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	109	ASP	-1	-0.820	-0.912	18.310	0.107	0.107	0.000	0.000	0.000	0.000
50	A	110	ILE	0	-0.008	0.009	20.626	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	111	ASP	-1	-0.866	-0.961	19.646	0.195	0.195	0.000	0.000	0.000	0.000
52	A	112	ASN	0	-0.016	0.000	21.693	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	113	ASN	0	-0.025	-0.018	24.802	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	114	LYS	1	0.920	0.972	24.551	-0.086	-0.086	0.000	0.000	0.000	0.000
55	A	115	ILE	0	0.045	0.023	23.785	0.009	0.009	0.000	0.000	0.000	0.000
56	A	116	ILE	0	-0.055	-0.017	17.772	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	117	ASN	0	-0.030	-0.044	17.879	0.001	0.001	0.000	0.000	0.000	0.000
58	A	118	LEU	0	-0.010	-0.008	21.045	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	119	ASN	0	0.008	0.010	22.034	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	120	GLY	0	0.076	0.044	20.334	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	121	ILE	0	0.002	-0.008	21.052	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	122	THR	0	0.053	0.014	23.030	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	123	ASP	-1	-0.814	-0.889	18.122	0.073	0.073	0.000	0.000	0.000	0.000
64	A	124	VAL	0	-0.046	-0.033	18.480	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	125	ILE	0	-0.026	-0.017	19.861	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	126	SER	0	0.027	0.010	19.760	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	127	ILE	0	-0.042	-0.012	15.242	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	128	VAL	0	-0.028	-0.014	18.127	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	129	ASP	-1	-0.886	-0.940	20.516	-0.028	-0.028	0.000	0.000	0.000	0.000
70	A	130	VAL	0	-0.042	-0.025	16.561	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	131	ILE	0	-0.065	-0.036	16.131	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	132	ASN	0	-0.037	-0.022	19.066	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	133	TYR	0	-0.076	-0.016	22.044	0.001	0.001	0.000	0.000	0.000	0.000
74	A	134	ILE	0	-0.071	-0.021	16.552	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	135	SER	0	-0.082	-0.069	20.795	0.004	0.004	0.000	0.000	0.000	0.000
76	A	136	SER	0	-0.052	-0.032	16.858	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	137	ASP	-1	-0.861	-0.920	18.657	-0.107	-0.107	0.000	0.000	0.000	0.000
78	A	138	VAL	0	0.023	0.003	14.733	-0.030	-0.030	0.000	0.000	0.000	0.000
79	A	139	TYR	0	-0.039	-0.018	15.564	0.025	0.025	0.000	0.000	0.000	0.000
80	A	140	THR	0	-0.004	-0.019	14.640	-0.025	-0.025	0.000	0.000	0.000	0.000
81	A	141	TYR	0	-0.017	-0.029	13.422	0.013	0.013	0.000	0.000	0.000	0.000
82	A	142	CYS	0	-0.026	0.011	14.337	0.021	0.021	0.000	0.000	0.000	0.000
83	A	143	LEU	0	-0.004	-0.040	11.519	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	144	GLY	0	0.009	0.006	15.471	0.011	0.011	0.000	0.000	0.000	0.000
85	A	145	LYS	1	0.934	0.991	17.144	-0.147	-0.147	0.000	0.000	0.000	0.000
86	A	146	ALA	0	0.070	0.032	17.144	0.014	0.014	0.000	0.000	0.000	0.000
87	A	147	TYR	0	0.001	-0.004	19.127	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	148	GLY	0	0.079	0.036	20.865	0.010	0.010	0.000	0.000	0.000	0.000
89	A	149	ILE	0	0.018	0.004	19.098	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	150	ALA	0	0.032	0.010	17.074	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	151	CYS	0	-0.057	0.000	18.504	-0.015	-0.015	0.000	0.000	0.000	0.000
92	A	152	ILE	0	0.040	0.021	21.246	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	153	LEU	0	-0.016	0.010	14.438	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	154	ALA	0	0.038	0.013	17.727	-0.018	-0.018	0.000	0.000	0.000	0.000
95	A	155	SER	0	-0.029	0.013	18.658	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	156	SER	0	0.004	-0.030	19.853	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	157	GLY	0	-0.010	0.017	19.036	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	158	LYS	1	0.879	0.950	19.689	0.096	0.096	0.000	0.000	0.000	0.000
99	A	159	LYS	1	0.890	0.948	22.001	0.033	0.033	0.000	0.000	0.000	0.000
100	A	160	GLY	0	-0.014	-0.004	24.944	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	161	TYR	0	-0.067	-0.051	19.842	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	162	ARG	1	0.786	0.921	19.345	0.024	0.024	0.000	0.000	0.000	0.000
103	A	163	PHE	0	0.031	0.011	17.862	0.008	0.008	0.000	0.000	0.000	0.000
104	A	164	SER	0	0.035	0.002	18.921	0.010	0.010	0.000	0.000	0.000	0.000
105	A	165	LEU	0	-0.032	0.012	16.194	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	166	LYS	1	1.012	0.991	20.286	0.009	0.009	0.000	0.000	0.000	0.000
107	A	167	ASN	0	-0.038	-0.023	22.413	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	168	SER	0	-0.036	-0.008	19.086	0.010	0.010	0.000	0.000	0.000	0.000
109	A	169	SER	0	-0.025	-0.003	21.420	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	170	PHE	0	0.004	-0.022	20.268	0.007	0.007	0.000	0.000	0.000	0.000
111	A	171	CYS	0	-0.030	-0.001	23.656	0.000	0.000	0.000	0.000	0.000	0.000
112	A	172	LEU	0	-0.010	-0.003	24.719	0.003	0.003	0.000	0.000	0.000	0.000
113	A	173	ASN	0	0.032	0.007	25.058	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	174	GLN	0	0.007	0.013	28.733	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	175	SER	0	-0.035	-0.038	31.241	0.003	0.003	0.000	0.000	0.000	0.000
116	A	176	TYR	0	-0.073	-0.037	24.773	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	177	SER	0	-0.012	-0.019	30.324	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	178	ILE	0	0.015	0.017	26.560	0.000	0.000	0.000	0.000	0.000	0.000
119	A	179	ILE	0	-0.006	0.004	30.180	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	180	PRO	0	-0.011	-0.010	28.567	0.002	0.002	0.000	0.000	0.000	0.000
121	A	181	PHE	0	0.001	0.003	30.711	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	182	ASN	0	-0.030	-0.019	30.478	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	183	GLN	0	0.040	0.022	33.840	0.000	0.000	0.000	0.000	0.000	0.000
124	A	184	ALA	0	0.027	0.026	34.701	0.000	0.000	0.000	0.000	0.000	0.000
125	A	185	THR	0	0.004	-0.010	36.063	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	186	ASN	0	0.007	0.008	37.782	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	187	ILE	0	0.095	0.042	37.984	0.000	0.000	0.000	0.000	0.000	0.000
128	A	188	GLU	-1	-0.862	-0.921	39.295	0.011	0.011	0.000	0.000	0.000	0.000
129	A	189	ILE	0	-0.021	-0.028	35.372	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	190	GLN	0	0.071	0.036	33.969	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	191	ASN	0	0.004	-0.013	35.264	0.002	0.002	0.000	0.000	0.000	0.000
132	A	192	LYS	1	0.866	0.932	37.466	-0.011	-0.011	0.000	0.000	0.000	0.000
133	A	193	GLU	-1	-0.936	-0.959	29.662	0.025	0.025	0.000	0.000	0.000	0.000
134	A	194	ILE	0	-0.004	0.009	32.492	0.000	0.000	0.000	0.000	0.000	0.000
135	A	195	MET	0	-0.016	-0.010	33.489	0.000	0.000	0.000	0.000	0.000	0.000
136	A	196	ASN	0	-0.003	-0.004	33.087	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	197	THR	0	-0.032	-0.020	27.954	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	198	LYS	1	0.919	0.950	30.120	-0.026	-0.026	0.000	0.000	0.000	0.000
139	A	199	LYS	1	0.886	0.929	32.454	0.000	0.000	0.000	0.000	0.000	0.000
140	A	200	LYS	1	0.979	0.982	28.600	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	201	VAL	0	0.014	0.019	26.860	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	202	ILE	0	0.034	0.017	28.622	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	203	GLU	-1	-0.856	-0.898	30.797	-0.007	-0.007	0.000	0.000	0.000	0.000
144	A	204	ILE	0	-0.007	-0.003	24.486	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	205	ILE	0	0.014	0.010	26.542	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	206	SER	0	0.000	-0.005	28.302	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	207	LYS	1	0.970	0.998	26.497	0.029	0.029	0.000	0.000	0.000	0.000
148	A	208	ASN	0	-0.070	-0.051	23.901	-0.007	-0.007	0.000	0.000	0.000	0.000
149	A	209	THR	0	-0.028	-0.025	27.442	-0.002	-0.002	0.000	0.000	0.000	0.000
150	A	210	GLU	-1	-0.971	-0.983	29.811	-0.025	-0.025	0.000	0.000	0.000	0.000
151	A	211	LYS	1	0.870	0.945	32.533	0.008	0.008	0.000	0.000	0.000	0.000
152	A	212	ASP	-1	-0.843	-0.921	34.906	-0.006	-0.006	0.000	0.000	0.000	0.000
153	A	213	THR	0	0.031	-0.006	34.737	0.001	0.001	0.000	0.000	0.000	0.000
154	A	214	ASN	0	-0.036	-0.017	36.676	0.002	0.002	0.000	0.000	0.000	0.000
155	A	215	VAL	0	0.040	0.024	36.359	0.002	0.002	0.000	0.000	0.000	0.000
156	A	216	ILE	0	0.002	0.001	31.724	0.002	0.002	0.000	0.000	0.000	0.000
157	A	217	SER	0	0.013	-0.011	34.304	0.003	0.003	0.000	0.000	0.000	0.000
158	A	218	ASN	0	-0.057	-0.013	36.347	0.001	0.001	0.000	0.000	0.000	0.000
159	A	219	VAL	0	-0.032	-0.012	32.704	0.002	0.002	0.000	0.000	0.000	0.000
160	A	220	LEU	0	-0.028	0.008	29.974	0.003	0.003	0.000	0.000	0.000	0.000
161	A	221	GLU	-1	-0.908	-0.951	33.745	0.017	0.017	0.000	0.000	0.000	0.000
162	A	222	ARG	1	0.855	0.911	35.163	-0.020	-0.020	0.000	0.000	0.000	0.000
163	A	223	ASP	-1	-0.801	-0.873	31.021	0.040	0.040	0.000	0.000	0.000	0.000
164	A	224	LYS	1	0.898	0.956	30.570	-0.015	-0.015	0.000	0.000	0.000	0.000
165	A	225	TYR	0	-0.007	-0.024	26.888	0.002	0.002	0.000	0.000	0.000	0.000
166	A	226	PHE	0	0.001	0.008	26.563	-0.004	-0.004	0.000	0.000	0.000	0.000
167	A	227	ASN	0	0.059	0.036	26.305	0.002	0.002	0.000	0.000	0.000	0.000
168	A	228	ALA	0	0.050	-0.003	24.273	-0.002	-0.002	0.000	0.000	0.000	0.000
169	A	229	ASP	-1	-0.857	-0.931	25.702	-0.009	-0.009	0.000	0.000	0.000	0.000
170	A	230	GLU	-1	-0.892	-0.955	29.237	0.011	0.011	0.000	0.000	0.000	0.000
171	A	231	ALA	0	-0.056	-0.028	25.231	0.000	0.000	0.000	0.000	0.000	0.000
172	A	232	VAL	0	-0.005	-0.004	26.362	-0.003	-0.003	0.000	0.000	0.000	0.000
173	A	233	ASP	-1	-0.942	-0.955	28.186	-0.008	-0.008	0.000	0.000	0.000	0.000
174	A	234	PHE	0	-0.072	-0.046	29.338	0.000	0.000	0.000	0.000	0.000	0.000
175	A	235	LYS	1	0.956	0.972	28.695	0.016	0.016	0.000	0.000	0.000	0.000
176	A	236	LEU	0	-0.043	-0.024	24.582	-0.002	-0.002	0.000	0.000	0.000	0.000
177	A	237	ILE	0	-0.041	-0.027	20.917	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	238	ASP	-1	-0.798	-0.876	23.620	-0.044	-0.044	0.000	0.000	0.000	0.000
179	A	239	HIS	0	-0.005	-0.005	23.493	0.005	0.005	0.000	0.000	0.000	0.000
180	A	240	ILE	0	0.003	-0.001	22.948	-0.001	-0.001	0.000	0.000	0.000	0.000
181	A	241	LEU	0	-0.054	-0.026	17.779	-0.004	-0.004	0.000	0.000	0.000	0.000
182	A	242	GLU	-1	-0.932	-0.964	22.059	-0.029	-0.029	0.000	0.000	0.000	0.000
183	A	243	LYS	1	0.935	0.971	21.231	0.040	0.040	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:61:PRO)