FMO DATABASE

FMODB ID: 2JL3R

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	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	183
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2015421.290736
FMO2-HF: Nuclear repulsion	1943040.422507
FMO2-HF: Total energy	-72380.868229
FMO2-MP2: Total energy	-72594.472863

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.
-2.287	4.311	3.036	-3.358	-6.275	0.003

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 : 0.103 / q_NPA : 0.053

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	0.004	0.009	2.419	-3.808	0.378	0.851	-2.066	-2.970	0.005
4	A	64	LEU	0	0.018	0.029	2.280	-1.330	0.630	2.185	-1.186	-2.959	-0.002
5	A	65	LEU	0	0.073	0.042	4.153	0.799	1.251	0.000	-0.106	-0.346	0.000
6	A	66	SER	0	-0.068	-0.036	6.226	0.675	0.675	0.000	0.000	0.000	0.000
7	A	67	LYS	1	0.845	0.902	7.800	1.004	1.004	0.000	0.000	0.000	0.000
8	A	68	ARG	1	0.795	0.878	9.015	0.486	0.486	0.000	0.000	0.000	0.000
9	A	69	ILE	0	-0.024	-0.003	5.932	0.194	0.194	0.000	0.000	0.000	0.000
10	A	70	ILE	0	0.018	0.008	5.705	-0.536	-0.536	0.000	0.000	0.000	0.000
11	A	71	PHE	0	-0.041	-0.028	5.403	0.041	0.041	0.000	0.000	0.000	0.000
12	A	72	LEU	0	0.023	0.032	6.942	0.452	0.452	0.000	0.000	0.000	0.000
13	A	73	SER	0	-0.014	-0.012	8.655	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	74	SER	0	0.000	-0.009	10.341	0.036	0.036	0.000	0.000	0.000	0.000
15	A	75	PRO	0	0.018	0.035	12.968	-0.040	-0.040	0.000	0.000	0.000	0.000
16	A	76	ILE	0	-0.014	-0.002	14.099	0.076	0.076	0.000	0.000	0.000	0.000
17	A	77	TYR	0	0.005	-0.023	13.360	-0.038	-0.038	0.000	0.000	0.000	0.000
18	A	78	PRO	0	0.023	0.003	14.574	0.028	0.028	0.000	0.000	0.000	0.000
19	A	79	HIS	0	0.063	0.039	10.144	-0.104	-0.104	0.000	0.000	0.000	0.000
20	A	80	ILE	0	-0.030	-0.005	9.568	0.051	0.051	0.000	0.000	0.000	0.000
21	A	81	SER	0	-0.012	-0.036	11.032	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	82	GLU	-1	-0.852	-0.917	12.002	0.295	0.295	0.000	0.000	0.000	0.000
23	A	83	GLN	0	-0.012	-0.004	7.409	0.165	0.165	0.000	0.000	0.000	0.000
24	A	84	ILE	0	-0.023	0.001	8.817	-0.106	-0.106	0.000	0.000	0.000	0.000
25	A	85	ILE	0	0.031	0.013	10.466	-0.104	-0.104	0.000	0.000	0.000	0.000
26	A	86	SER	0	-0.027	-0.023	9.887	-0.059	-0.059	0.000	0.000	0.000	0.000
27	A	87	GLN	0	-0.056	-0.045	5.325	-0.391	-0.391	0.000	0.000	0.000	0.000
28	A	88	LEU	0	0.008	0.004	9.131	-0.097	-0.097	0.000	0.000	0.000	0.000
29	A	89	LEU	0	0.010	0.009	12.525	-0.026	-0.026	0.000	0.000	0.000	0.000
30	A	90	TYR	0	0.000	-0.003	9.390	0.006	0.006	0.000	0.000	0.000	0.000
31	A	91	LEU	0	0.010	0.005	8.822	-0.030	-0.030	0.000	0.000	0.000	0.000
32	A	92	GLU	-1	-0.711	-0.817	12.667	-0.134	-0.134	0.000	0.000	0.000	0.000
33	A	93	TYR	0	-0.044	-0.026	15.395	0.030	0.030	0.000	0.000	0.000	0.000
34	A	94	GLU	-1	-0.829	-0.861	13.008	-0.390	-0.390	0.000	0.000	0.000	0.000
35	A	95	SER	0	-0.027	-0.050	15.502	0.025	0.025	0.000	0.000	0.000	0.000
36	A	96	LYS	1	0.774	0.885	17.574	0.132	0.132	0.000	0.000	0.000	0.000
37	A	97	ARG	1	0.979	0.986	20.375	0.116	0.116	0.000	0.000	0.000	0.000
38	A	98	LYS	1	0.840	0.924	14.979	0.362	0.362	0.000	0.000	0.000	0.000
39	A	99	PRO	0	0.011	0.009	16.131	-0.025	-0.025	0.000	0.000	0.000	0.000
40	A	100	ILE	0	-0.003	0.014	10.824	-0.059	-0.059	0.000	0.000	0.000	0.000
41	A	101	HIS	0	0.003	0.015	10.532	0.106	0.106	0.000	0.000	0.000	0.000
42	A	102	LEU	0	0.051	0.023	9.653	-0.089	-0.089	0.000	0.000	0.000	0.000
43	A	103	TYR	0	0.013	-0.003	9.146	0.062	0.062	0.000	0.000	0.000	0.000
44	A	104	ILE	0	-0.011	-0.008	10.465	0.091	0.091	0.000	0.000	0.000	0.000
45	A	105	ASN	0	-0.039	-0.024	12.618	-0.047	-0.047	0.000	0.000	0.000	0.000
46	A	106	SER	0	-0.019	-0.028	13.979	0.038	0.038	0.000	0.000	0.000	0.000
47	A	107	THR	0	-0.012	-0.037	15.823	-0.027	-0.027	0.000	0.000	0.000	0.000
48	A	108	GLY	0	0.038	0.028	17.771	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	109	ASP	-1	-0.795	-0.876	18.346	0.171	0.171	0.000	0.000	0.000	0.000
50	A	110	ILE	0	-0.007	0.000	20.418	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	111	ASP	-1	-0.772	-0.878	19.090	0.266	0.266	0.000	0.000	0.000	0.000
52	A	112	ASN	0	-0.021	-0.018	21.710	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	113	ASN	0	-0.004	0.003	24.658	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	114	LYS	1	0.869	0.934	24.488	-0.131	-0.131	0.000	0.000	0.000	0.000
55	A	115	ILE	0	0.039	0.023	23.956	0.009	0.009	0.000	0.000	0.000	0.000
56	A	116	ILE	0	-0.049	-0.017	18.019	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	117	ASN	0	0.002	-0.034	17.659	0.001	0.001	0.000	0.000	0.000	0.000
58	A	118	LEU	0	-0.016	-0.013	20.818	-0.012	-0.012	0.000	0.000	0.000	0.000
59	A	119	ASN	0	0.051	0.041	21.463	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	120	GLY	0	0.052	0.025	20.282	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	121	ILE	0	-0.004	-0.003	21.091	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	122	THR	0	0.034	0.005	23.162	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	123	ASP	-1	-0.811	-0.856	17.962	0.161	0.161	0.000	0.000	0.000	0.000
64	A	124	VAL	0	-0.017	-0.021	18.712	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	125	ILE	0	-0.029	-0.009	19.768	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	126	SER	0	-0.012	-0.017	19.405	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	127	ILE	0	-0.043	-0.017	14.909	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	128	VAL	0	-0.008	-0.013	17.730	-0.022	-0.022	0.000	0.000	0.000	0.000
69	A	129	ASP	-1	-0.814	-0.872	20.412	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	130	VAL	0	-0.017	-0.013	16.219	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	131	ILE	0	-0.042	-0.024	15.803	-0.020	-0.020	0.000	0.000	0.000	0.000
72	A	132	ASN	0	-0.076	-0.052	19.108	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	133	TYR	0	-0.105	-0.062	21.514	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	134	ILE	0	-0.067	-0.017	16.531	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	135	SER	0	-0.037	-0.026	20.514	0.006	0.006	0.000	0.000	0.000	0.000
76	A	136	SER	0	-0.056	-0.049	16.783	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	137	ASP	-1	-0.748	-0.847	18.369	-0.104	-0.104	0.000	0.000	0.000	0.000
78	A	138	VAL	0	0.001	-0.001	14.871	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	139	TYR	0	-0.045	-0.022	15.245	0.024	0.024	0.000	0.000	0.000	0.000
80	A	140	THR	0	-0.002	-0.014	14.422	-0.027	-0.027	0.000	0.000	0.000	0.000
81	A	141	TYR	0	-0.012	-0.014	13.138	0.006	0.006	0.000	0.000	0.000	0.000
82	A	142	CYS	0	-0.010	0.008	14.237	0.033	0.033	0.000	0.000	0.000	0.000
83	A	143	LEU	0	-0.005	-0.018	11.718	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	144	GLY	0	0.009	0.006	15.585	0.012	0.012	0.000	0.000	0.000	0.000
85	A	145	LYS	1	0.909	0.981	17.118	-0.216	-0.216	0.000	0.000	0.000	0.000
86	A	146	ALA	0	0.073	0.032	17.092	0.020	0.020	0.000	0.000	0.000	0.000
87	A	147	TYR	0	-0.005	0.002	19.137	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	148	GLY	0	0.091	0.049	20.838	0.015	0.015	0.000	0.000	0.000	0.000
89	A	149	ILE	0	-0.015	-0.004	18.922	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	150	ALA	0	0.027	0.012	16.984	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	151	CYS	0	-0.037	0.009	18.342	-0.017	-0.017	0.000	0.000	0.000	0.000
92	A	152	ILE	0	0.016	0.015	21.216	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	153	LEU	0	0.000	0.023	14.068	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	154	ALA	0	0.028	0.003	17.500	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	155	SER	0	-0.020	0.002	18.415	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	156	SER	0	-0.016	-0.032	19.442	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	157	GLY	0	-0.012	0.009	18.649	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	158	LYS	1	0.796	0.882	19.290	0.101	0.101	0.000	0.000	0.000	0.000
99	A	159	LYS	1	0.822	0.887	21.723	0.016	0.016	0.000	0.000	0.000	0.000
100	A	160	GLY	0	0.008	0.006	24.773	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	161	TYR	0	-0.061	-0.038	19.771	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	162	ARG	1	0.741	0.859	19.090	0.008	0.008	0.000	0.000	0.000	0.000
103	A	163	PHE	0	0.025	0.006	17.908	0.004	0.004	0.000	0.000	0.000	0.000
104	A	164	SER	0	0.034	0.005	18.792	0.017	0.017	0.000	0.000	0.000	0.000
105	A	165	LEU	0	-0.010	0.004	16.499	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	166	LYS	1	1.010	1.004	20.198	0.011	0.011	0.000	0.000	0.000	0.000
107	A	167	ASN	0	-0.010	-0.015	22.382	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	168	SER	0	-0.057	-0.029	18.872	0.012	0.012	0.000	0.000	0.000	0.000
109	A	169	SER	0	-0.031	-0.005	21.421	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	170	PHE	0	0.010	-0.020	20.272	0.015	0.015	0.000	0.000	0.000	0.000
111	A	171	CYS	0	-0.056	-0.024	23.461	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	172	LEU	0	-0.008	0.008	24.634	0.007	0.007	0.000	0.000	0.000	0.000
113	A	173	ASN	0	0.052	0.008	25.036	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	174	GLN	0	0.035	0.033	28.501	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	175	SER	0	-0.016	-0.019	30.994	0.006	0.006	0.000	0.000	0.000	0.000
116	A	176	TYR	0	-0.095	-0.082	24.226	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	177	SER	0	-0.010	-0.021	29.955	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	178	ILE	0	-0.003	0.008	26.478	0.000	0.000	0.000	0.000	0.000	0.000
119	A	179	ILE	0	0.011	0.010	29.910	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	180	PRO	0	-0.008	-0.008	28.106	0.002	0.002	0.000	0.000	0.000	0.000
121	A	181	PHE	0	0.000	0.005	30.547	-0.005	-0.005	0.000	0.000	0.000	0.000
122	A	182	ASN	0	-0.020	-0.010	30.386	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	183	GLN	0	0.048	0.023	33.566	0.002	0.002	0.000	0.000	0.000	0.000
124	A	184	ALA	0	0.023	0.023	34.635	0.000	0.000	0.000	0.000	0.000	0.000
125	A	185	THR	0	-0.009	-0.017	35.919	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	186	ASN	0	0.008	0.006	37.524	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	187	ILE	0	0.097	0.045	37.785	0.001	0.001	0.000	0.000	0.000	0.000
128	A	188	GLU	-1	-0.854	-0.899	39.011	0.027	0.027	0.000	0.000	0.000	0.000
129	A	189	ILE	0	-0.020	-0.022	35.035	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	190	GLN	0	0.080	0.040	33.095	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	191	ASN	0	-0.036	-0.031	34.803	0.002	0.002	0.000	0.000	0.000	0.000
132	A	192	LYS	1	0.890	0.936	36.730	-0.027	-0.027	0.000	0.000	0.000	0.000
133	A	193	GLU	-1	-0.908	-0.940	29.964	0.055	0.055	0.000	0.000	0.000	0.000
134	A	194	ILE	0	-0.002	0.003	31.955	0.001	0.001	0.000	0.000	0.000	0.000
135	A	195	MET	0	0.002	0.001	32.817	0.000	0.000	0.000	0.000	0.000	0.000
136	A	196	ASN	0	-0.058	-0.042	32.454	-0.004	-0.004	0.000	0.000	0.000	0.000
137	A	197	THR	0	-0.025	-0.012	27.409	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	198	LYS	1	0.861	0.914	29.547	-0.051	-0.051	0.000	0.000	0.000	0.000
139	A	199	LYS	1	0.829	0.896	31.897	-0.020	-0.020	0.000	0.000	0.000	0.000
140	A	200	LYS	1	0.988	0.987	27.830	-0.034	-0.034	0.000	0.000	0.000	0.000
141	A	201	VAL	0	0.014	0.015	26.387	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	202	ILE	0	0.038	0.025	28.303	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	203	GLU	-1	-0.820	-0.874	30.825	0.012	0.012	0.000	0.000	0.000	0.000
144	A	204	ILE	0	-0.008	-0.004	24.290	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	205	ILE	0	0.034	0.016	26.504	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	206	SER	0	-0.003	-0.005	28.136	-0.004	-0.004	0.000	0.000	0.000	0.000
147	A	207	LYS	1	0.915	0.975	24.741	0.007	0.007	0.000	0.000	0.000	0.000
148	A	208	ASN	0	-0.043	-0.039	23.471	-0.012	-0.012	0.000	0.000	0.000	0.000
149	A	209	THR	0	-0.016	-0.015	27.005	-0.003	-0.003	0.000	0.000	0.000	0.000
150	A	210	GLU	-1	-0.850	-0.882	29.443	-0.018	-0.018	0.000	0.000	0.000	0.000
151	A	211	LYS	1	0.823	0.903	31.729	-0.007	-0.007	0.000	0.000	0.000	0.000
152	A	212	ASP	-1	-0.874	-0.927	34.867	0.006	0.006	0.000	0.000	0.000	0.000
153	A	213	THR	0	0.020	-0.003	34.487	0.002	0.002	0.000	0.000	0.000	0.000
154	A	214	ASN	0	-0.015	-0.003	36.307	0.002	0.002	0.000	0.000	0.000	0.000
155	A	215	VAL	0	0.055	0.026	36.299	0.002	0.002	0.000	0.000	0.000	0.000
156	A	216	ILE	0	-0.013	-0.005	31.580	0.003	0.003	0.000	0.000	0.000	0.000
157	A	217	SER	0	0.009	-0.012	34.121	0.004	0.004	0.000	0.000	0.000	0.000
158	A	218	ASN	0	-0.078	-0.039	36.037	0.001	0.001	0.000	0.000	0.000	0.000
159	A	219	VAL	0	-0.001	0.002	32.787	0.002	0.002	0.000	0.000	0.000	0.000
160	A	220	LEU	0	0.014	0.018	29.553	0.003	0.003	0.000	0.000	0.000	0.000
161	A	221	GLU	-1	-0.850	-0.904	33.445	0.033	0.033	0.000	0.000	0.000	0.000
162	A	222	ARG	1	0.796	0.886	34.868	-0.034	-0.034	0.000	0.000	0.000	0.000
163	A	223	ASP	-1	-0.791	-0.870	30.174	0.070	0.070	0.000	0.000	0.000	0.000
164	A	224	LYS	1	0.796	0.888	30.402	-0.035	-0.035	0.000	0.000	0.000	0.000
165	A	225	TYR	0	-0.003	-0.028	26.719	0.005	0.005	0.000	0.000	0.000	0.000
166	A	226	PHE	0	0.003	0.003	26.623	-0.007	-0.007	0.000	0.000	0.000	0.000
167	A	227	ASN	0	0.042	0.021	26.077	0.004	0.004	0.000	0.000	0.000	0.000
168	A	228	ALA	0	0.053	0.013	23.951	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	229	ASP	-1	-0.883	-0.945	25.355	-0.004	-0.004	0.000	0.000	0.000	0.000
170	A	230	GLU	-1	-0.825	-0.905	28.852	0.026	0.026	0.000	0.000	0.000	0.000
171	A	231	ALA	0	-0.026	-0.007	24.800	0.000	0.000	0.000	0.000	0.000	0.000
172	A	232	VAL	0	-0.005	0.002	26.106	-0.003	-0.003	0.000	0.000	0.000	0.000
173	A	233	ASP	-1	-0.937	-0.954	28.018	0.002	0.002	0.000	0.000	0.000	0.000
174	A	234	PHE	0	0.014	-0.013	29.382	-0.001	-0.001	0.000	0.000	0.000	0.000
175	A	235	LYS	1	0.870	0.931	28.216	0.010	0.010	0.000	0.000	0.000	0.000
176	A	236	LEU	0	-0.018	-0.009	24.435	-0.001	-0.001	0.000	0.000	0.000	0.000
177	A	237	ILE	0	-0.052	-0.030	20.462	0.001	0.001	0.000	0.000	0.000	0.000
178	A	238	ASP	-1	-0.788	-0.863	23.436	-0.036	-0.036	0.000	0.000	0.000	0.000
179	A	239	HIS	0	-0.017	-0.007	23.199	0.003	0.003	0.000	0.000	0.000	0.000
180	A	240	ILE	0	0.006	-0.001	22.866	0.003	0.003	0.000	0.000	0.000	0.000
181	A	241	LEU	0	-0.064	-0.027	17.439	-0.008	-0.008	0.000	0.000	0.000	0.000
182	A	242	GLU	-1	-0.923	-0.966	21.820	-0.033	-0.033	0.000	0.000	0.000	0.000
183	A	243	LYS	1	0.935	0.973	21.399	0.065	0.065	0.000	0.000	0.000	0.000

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