FMO DATABASE

FMODB ID: VR141

Calculation Name: 5JRB-A-Xray372

Preferred Name: DNA repair protein RAD52 homolog

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 5JRB

Chain ID: A

ChEMBL ID: CHEMBL2362978

UniProt ID: P43351

Base Structure: X-ray

Registration Date: 2023-06-20

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	184
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1731236.101834
FMO2-HF: Nuclear repulsion	1658642.875178
FMO2-HF: Total energy	-72593.226656
FMO2-MP2: Total energy	-72802.319405

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:25:CYS)

Summations of interaction energy for fragment #1(A:25:CYS)

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.
-10.041	-14.358	21.498	-8.491	-8.689	-0.052

Interaction energy analysis for fragmet #1(A:25:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.002 / q_NPA : -0.006

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	27	GLY	0	-0.020	-0.017	3.882	0.850	3.176	0.270	-1.065	-1.531	0.002
4	A	28	GLN	0	0.000	0.007	1.886	-11.006	-18.320	21.223	-7.260	-6.649	-0.053
5	A	29	CYS	0	-0.048	-0.009	3.479	0.382	0.953	0.006	-0.151	-0.425	-0.001
6	A	30	GLN	0	0.034	0.006	4.446	0.790	0.890	-0.001	-0.015	-0.084	0.000
7	A	31	TYR	0	-0.001	0.005	8.041	0.074	0.074	0.000	0.000	0.000	0.000
8	A	32	THR	0	-0.019	-0.024	10.958	0.013	0.013	0.000	0.000	0.000	0.000
9	A	33	ALA	0	0.031	0.013	13.255	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	34	GLU	-1	-0.804	-0.902	16.316	-0.275	-0.275	0.000	0.000	0.000	0.000
11	A	35	GLU	-1	-0.790	-0.871	11.703	-0.614	-0.614	0.000	0.000	0.000	0.000
12	A	36	TYR	0	0.025	0.008	15.266	0.032	0.032	0.000	0.000	0.000	0.000
13	A	37	GLN	0	-0.043	-0.022	16.563	0.040	0.040	0.000	0.000	0.000	0.000
14	A	38	ALA	0	-0.009	-0.003	18.932	0.025	0.025	0.000	0.000	0.000	0.000
15	A	39	ILE	0	0.056	0.027	15.005	0.027	0.027	0.000	0.000	0.000	0.000
16	A	40	GLN	0	0.021	0.031	19.124	0.051	0.051	0.000	0.000	0.000	0.000
17	A	41	LYS	1	0.889	0.944	21.017	0.154	0.154	0.000	0.000	0.000	0.000
18	A	42	ALA	0	-0.006	-0.004	21.527	0.017	0.017	0.000	0.000	0.000	0.000
19	A	43	LEU	0	0.049	0.013	18.621	0.022	0.022	0.000	0.000	0.000	0.000
20	A	44	ARG	1	0.877	0.930	23.086	0.200	0.200	0.000	0.000	0.000	0.000
21	A	45	GLN	0	-0.031	-0.002	26.454	0.013	0.013	0.000	0.000	0.000	0.000
22	A	46	ARG	1	0.851	0.907	28.016	0.090	0.090	0.000	0.000	0.000	0.000
23	A	47	LEU	0	0.012	0.023	26.681	0.003	0.003	0.000	0.000	0.000	0.000
24	A	48	GLY	0	0.070	0.060	30.642	0.003	0.003	0.000	0.000	0.000	0.000
25	A	49	PRO	0	-0.005	-0.020	33.227	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	50	GLU	-1	-0.820	-0.912	32.825	-0.047	-0.047	0.000	0.000	0.000	0.000
27	A	51	TYR	0	-0.020	-0.012	26.878	0.002	0.002	0.000	0.000	0.000	0.000
28	A	52	ILE	0	-0.074	-0.027	31.532	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	53	SER	0	0.011	-0.005	34.223	0.004	0.004	0.000	0.000	0.000	0.000
30	A	54	SER	0	-0.072	-0.055	36.097	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	55	ARG	1	0.975	0.994	35.913	0.032	0.032	0.000	0.000	0.000	0.000
32	A	56	MET	0	0.042	0.021	40.454	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	57	ALA	0	0.005	0.012	42.230	0.000	0.000	0.000	0.000	0.000	0.000
34	A	58	GLY	0	0.023	0.003	43.190	0.002	0.002	0.000	0.000	0.000	0.000
35	A	59	GLY	0	0.020	0.019	45.220	0.000	0.000	0.000	0.000	0.000	0.000
36	A	60	GLY	0	-0.005	-0.004	46.342	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	61	GLN	0	0.000	-0.004	44.487	0.001	0.001	0.000	0.000	0.000	0.000
38	A	62	LYS	1	0.911	0.957	42.738	0.035	0.035	0.000	0.000	0.000	0.000
39	A	63	VAL	0	-0.007	-0.007	37.077	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	64	CYS	0	-0.016	-0.018	36.559	0.003	0.003	0.000	0.000	0.000	0.000
41	A	65	TYR	0	-0.067	-0.034	32.178	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	66	ILE	0	0.067	0.044	27.734	0.002	0.002	0.000	0.000	0.000	0.000
43	A	67	GLU	-1	-0.806	-0.866	29.472	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	68	GLY	0	0.067	0.019	25.573	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	69	HIS	0	0.012	-0.007	24.294	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	70	ARG	1	0.837	0.910	24.520	0.031	0.031	0.000	0.000	0.000	0.000
47	A	71	VAL	0	0.022	0.006	22.366	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	72	ILE	0	0.009	0.009	19.313	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	73	ASN	0	-0.006	-0.010	19.748	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	74	LEU	0	-0.025	0.001	20.987	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	75	ALA	0	0.024	0.005	17.358	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	76	ASN	0	-0.033	-0.014	16.268	-0.043	-0.043	0.000	0.000	0.000	0.000
53	A	77	GLU	-1	-0.925	-0.956	16.613	-0.091	-0.091	0.000	0.000	0.000	0.000
54	A	78	MET	0	-0.109	-0.036	18.142	-0.014	-0.014	0.000	0.000	0.000	0.000
55	A	79	PHE	0	-0.006	-0.021	13.071	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	80	GLY	0	0.088	0.057	12.573	-0.062	-0.062	0.000	0.000	0.000	0.000
57	A	81	TYR	0	-0.023	-0.034	11.218	-0.030	-0.030	0.000	0.000	0.000	0.000
58	A	82	ASN	0	-0.016	-0.004	7.402	0.003	0.003	0.000	0.000	0.000	0.000
59	A	83	GLY	0	0.035	0.024	7.985	-0.224	-0.224	0.000	0.000	0.000	0.000
60	A	84	TRP	0	-0.062	-0.047	10.093	-0.102	-0.102	0.000	0.000	0.000	0.000
61	A	85	ALA	0	0.026	0.019	10.137	0.066	0.066	0.000	0.000	0.000	0.000
62	A	86	HIS	0	-0.010	-0.022	12.233	-0.038	-0.038	0.000	0.000	0.000	0.000
63	A	87	SER	0	0.021	0.014	14.279	0.049	0.049	0.000	0.000	0.000	0.000
64	A	88	ILE	0	-0.023	-0.016	16.252	-0.027	-0.027	0.000	0.000	0.000	0.000
65	A	89	THR	0	-0.039	-0.031	18.692	0.023	0.023	0.000	0.000	0.000	0.000
66	A	90	GLN	0	0.016	0.014	19.717	0.013	0.013	0.000	0.000	0.000	0.000
67	A	91	GLN	0	-0.029	-0.003	23.400	0.002	0.002	0.000	0.000	0.000	0.000
68	A	92	ASN	0	-0.038	-0.025	26.410	0.002	0.002	0.000	0.000	0.000	0.000
69	A	93	VAL	0	-0.006	-0.015	30.058	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	94	ASP	-1	-0.772	-0.844	33.284	-0.017	-0.017	0.000	0.000	0.000	0.000
71	A	95	PHE	0	0.022	0.017	35.681	0.000	0.000	0.000	0.000	0.000	0.000
72	A	96	VAL	0	-0.055	-0.052	37.813	0.002	0.002	0.000	0.000	0.000	0.000
73	A	97	ASP	-1	-0.854	-0.904	40.422	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	98	LEU	0	-0.061	-0.045	44.069	0.001	0.001	0.000	0.000	0.000	0.000
75	A	99	ASN	0	0.004	0.005	46.876	0.000	0.000	0.000	0.000	0.000	0.000
76	A	100	ASN	0	-0.005	-0.015	49.728	0.001	0.001	0.000	0.000	0.000	0.000
77	A	101	GLY	0	0.026	0.022	50.860	0.000	0.000	0.000	0.000	0.000	0.000
78	A	102	ALA	0	-0.036	-0.006	46.601	0.001	0.001	0.000	0.000	0.000	0.000
79	A	103	PHE	0	-0.016	-0.026	42.251	0.000	0.000	0.000	0.000	0.000	0.000
80	A	104	TYR	0	-0.013	-0.010	42.295	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	105	VAL	0	-0.035	-0.022	36.264	0.001	0.001	0.000	0.000	0.000	0.000
82	A	106	GLY	0	0.042	0.030	36.150	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	107	VAL	0	-0.052	-0.036	29.936	0.004	0.004	0.000	0.000	0.000	0.000
84	A	108	CYS	0	-0.022	0.001	29.678	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	109	ALA	0	-0.008	-0.025	24.976	0.009	0.009	0.000	0.000	0.000	0.000
86	A	110	PHE	0	0.001	0.000	23.031	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	111	VAL	0	-0.023	-0.012	19.581	0.014	0.014	0.000	0.000	0.000	0.000
88	A	112	ARG	1	0.869	0.950	12.727	0.197	0.197	0.000	0.000	0.000	0.000
89	A	113	VAL	0	-0.002	-0.014	15.671	0.029	0.029	0.000	0.000	0.000	0.000
90	A	114	GLN	0	0.020	0.003	8.485	0.046	0.046	0.000	0.000	0.000	0.000
91	A	115	LEU	0	-0.028	-0.005	10.943	0.061	0.061	0.000	0.000	0.000	0.000
92	A	116	LYS	1	0.837	0.895	6.258	0.926	0.926	0.000	0.000	0.000	0.000
93	A	117	ASP	-1	-0.785	-0.869	5.696	-2.178	-2.178	0.000	0.000	0.000	0.000
94	A	118	GLY	0	-0.008	0.006	7.801	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	119	SER	0	-0.088	-0.056	9.632	0.285	0.285	0.000	0.000	0.000	0.000
96	A	120	TYR	0	-0.006	-0.030	12.988	0.045	0.045	0.000	0.000	0.000	0.000
97	A	121	HIS	0	-0.033	-0.006	15.384	0.017	0.017	0.000	0.000	0.000	0.000
98	A	122	GLU	-1	-0.818	-0.891	18.077	-0.103	-0.103	0.000	0.000	0.000	0.000
99	A	123	ASP	-1	-0.790	-0.859	20.307	-0.101	-0.101	0.000	0.000	0.000	0.000
100	A	124	VAL	0	0.009	0.012	23.636	0.010	0.010	0.000	0.000	0.000	0.000
101	A	125	GLY	0	-0.007	-0.010	26.412	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	126	TYR	0	-0.085	-0.075	27.843	0.006	0.006	0.000	0.000	0.000	0.000
103	A	127	GLY	0	-0.032	-0.009	31.046	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	128	VAL	0	0.009	-0.001	32.643	0.001	0.001	0.000	0.000	0.000	0.000
105	A	129	SER	0	-0.051	-0.019	36.278	0.002	0.002	0.000	0.000	0.000	0.000
106	A	130	GLU	-1	-0.875	-0.938	38.761	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	131	GLY	0	0.009	0.014	42.545	0.000	0.000	0.000	0.000	0.000	0.000
108	A	132	LEU	0	-0.007	-0.004	39.807	0.002	0.002	0.000	0.000	0.000	0.000
109	A	133	ALA	0	0.062	0.031	43.959	0.000	0.000	0.000	0.000	0.000	0.000
110	A	134	SER	0	-0.005	-0.001	41.263	0.002	0.002	0.000	0.000	0.000	0.000
111	A	135	LYS	1	1.012	1.014	39.542	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	136	ALA	0	0.001	0.004	37.460	0.000	0.000	0.000	0.000	0.000	0.000
113	A	137	LEU	0	0.064	0.022	36.245	0.000	0.000	0.000	0.000	0.000	0.000
114	A	138	SER	0	-0.008	-0.005	36.401	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	139	LEU	0	0.013	0.005	34.145	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	140	GLU	-1	-0.882	-0.918	31.939	0.027	0.027	0.000	0.000	0.000	0.000
117	A	141	LYS	1	0.816	0.881	31.490	0.008	0.008	0.000	0.000	0.000	0.000
118	A	142	ALA	0	0.034	0.022	31.887	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	143	ARG	1	0.919	0.937	27.642	-0.031	-0.031	0.000	0.000	0.000	0.000
120	A	144	LYS	1	0.879	0.929	27.178	-0.029	-0.029	0.000	0.000	0.000	0.000
121	A	145	GLU	-1	-0.845	-0.893	27.210	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	146	ALA	0	0.037	0.025	28.458	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	147	VAL	0	0.009	0.004	22.222	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	148	THR	0	-0.026	-0.025	23.764	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	149	ASP	-1	-0.848	-0.921	25.333	-0.063	-0.063	0.000	0.000	0.000	0.000
126	A	150	GLY	0	0.065	0.028	24.333	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	151	LEU	0	-0.014	0.005	18.992	-0.016	-0.016	0.000	0.000	0.000	0.000
128	A	152	LYS	1	0.817	0.892	22.041	0.034	0.034	0.000	0.000	0.000	0.000
129	A	153	ARG	1	0.787	0.884	24.597	0.063	0.063	0.000	0.000	0.000	0.000
130	A	154	ALA	0	0.040	0.027	20.107	-0.011	-0.011	0.000	0.000	0.000	0.000
131	A	155	LEU	0	0.010	0.003	17.700	-0.026	-0.026	0.000	0.000	0.000	0.000
132	A	156	ARG	1	0.822	0.892	21.023	0.100	0.100	0.000	0.000	0.000	0.000
133	A	157	SER	0	-0.032	-0.017	21.884	0.004	0.004	0.000	0.000	0.000	0.000
134	A	158	PHE	0	0.022	0.027	15.957	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	159	GLY	0	0.035	0.012	20.997	-0.010	-0.010	0.000	0.000	0.000	0.000
136	A	160	ASN	0	-0.090	-0.056	24.137	0.016	0.016	0.000	0.000	0.000	0.000
137	A	161	ALA	0	0.001	0.012	23.829	0.012	0.012	0.000	0.000	0.000	0.000
138	A	162	LEU	0	0.041	0.022	19.558	0.005	0.005	0.000	0.000	0.000	0.000
139	A	163	GLY	0	0.033	0.009	24.038	0.008	0.008	0.000	0.000	0.000	0.000
140	A	164	ASN	0	-0.054	-0.015	26.801	0.010	0.010	0.000	0.000	0.000	0.000
141	A	165	CYS	0	-0.032	-0.017	28.436	0.006	0.006	0.000	0.000	0.000	0.000
142	A	166	ILE	0	-0.003	0.005	30.584	0.007	0.007	0.000	0.000	0.000	0.000
143	A	167	LEU	0	-0.003	-0.015	31.189	0.008	0.008	0.000	0.000	0.000	0.000
144	A	168	ASP	-1	-0.752	-0.848	34.152	-0.078	-0.078	0.000	0.000	0.000	0.000
145	A	169	LYS	1	0.929	0.945	35.797	0.067	0.067	0.000	0.000	0.000	0.000
146	A	170	ASP	-1	-0.776	-0.850	38.931	-0.057	-0.057	0.000	0.000	0.000	0.000
147	A	171	TYR	0	-0.021	-0.025	33.265	0.003	0.003	0.000	0.000	0.000	0.000
148	A	172	LEU	0	0.012	0.003	36.585	0.005	0.005	0.000	0.000	0.000	0.000
149	A	173	ARG	1	0.795	0.878	39.179	0.059	0.059	0.000	0.000	0.000	0.000
150	A	174	SER	0	-0.015	-0.021	39.307	0.003	0.003	0.000	0.000	0.000	0.000
151	A	175	LEU	0	0.011	0.003	35.642	0.003	0.003	0.000	0.000	0.000	0.000
152	A	176	ASN	0	-0.094	-0.055	40.035	0.006	0.006	0.000	0.000	0.000	0.000
153	A	177	LYS	1	0.923	0.959	43.235	0.041	0.041	0.000	0.000	0.000	0.000
154	A	178	LEU	0	0.018	0.026	38.920	0.000	0.000	0.000	0.000	0.000	0.000
155	A	179	PRO	0	-0.010	-0.011	43.141	0.001	0.001	0.000	0.000	0.000	0.000
156	A	180	ARG	1	0.888	0.958	38.194	0.034	0.034	0.000	0.000	0.000	0.000
157	A	181	GLN	0	0.048	0.020	39.759	0.003	0.003	0.000	0.000	0.000	0.000
158	A	182	LEU	0	0.021	0.016	42.053	0.001	0.001	0.000	0.000	0.000	0.000
159	A	183	PRO	0	-0.028	-0.014	38.694	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	184	LEU	0	0.000	0.000	33.388	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	185	GLU	-1	-0.899	-0.944	36.652	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	186	VAL	0	-0.008	-0.014	32.294	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	187	ASP	-1	-0.761	-0.844	34.065	0.011	0.011	0.000	0.000	0.000	0.000
164	A	188	LEU	0	0.012	-0.002	32.809	0.002	0.002	0.000	0.000	0.000	0.000
165	A	189	THR	0	-0.081	-0.066	34.332	0.005	0.005	0.000	0.000	0.000	0.000
166	A	190	LYS	1	0.871	0.924	30.332	-0.008	-0.008	0.000	0.000	0.000	0.000
167	A	191	ALA	0	-0.014	0.014	29.631	0.002	0.002	0.000	0.000	0.000	0.000
168	A	192	LYS	1	0.801	0.874	23.278	-0.085	-0.085	0.000	0.000	0.000	0.000
169	A	193	ARG	1	0.886	0.926	28.534	-0.034	-0.034	0.000	0.000	0.000	0.000
170	A	194	GLN	0	0.023	0.017	28.394	0.000	0.000	0.000	0.000	0.000	0.000
171	A	195	ASP	-1	-0.865	-0.931	24.563	0.093	0.093	0.000	0.000	0.000	0.000
172	A	196	LEU	0	-0.007	-0.002	23.725	0.006	0.006	0.000	0.000	0.000	0.000
173	A	197	GLU	-1	-0.824	-0.901	21.023	0.073	0.073	0.000	0.000	0.000	0.000
174	A	198	PRO	0	0.001	-0.003	21.756	0.014	0.014	0.000	0.000	0.000	0.000
175	A	199	SER	0	0.025	0.026	21.144	0.013	0.013	0.000	0.000	0.000	0.000
176	A	200	VAL	0	0.040	0.011	16.127	0.012	0.012	0.000	0.000	0.000	0.000
177	A	201	GLU	-1	-0.832	-0.885	17.561	0.252	0.252	0.000	0.000	0.000	0.000
178	A	202	ALA	0	-0.003	0.002	19.518	0.020	0.020	0.000	0.000	0.000	0.000
179	A	203	ALA	0	-0.014	-0.010	15.864	0.014	0.014	0.000	0.000	0.000	0.000
180	A	204	ARG	1	0.858	0.904	14.654	-0.230	-0.230	0.000	0.000	0.000	0.000
181	A	205	TYR	0	0.029	0.024	15.783	0.047	0.047	0.000	0.000	0.000	0.000
182	A	206	ASN	0	-0.066	-0.039	17.730	-0.004	-0.004	0.000	0.000	0.000	0.000
183	A	207	SER	0	-0.062	-0.031	12.302	0.023	0.023	0.000	0.000	0.000	0.000
184	A	208	CYS	0	-0.064	-0.023	13.375	0.070	0.070	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:25:CYS)