FMO DATABASE

FMODB ID: 53LZZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1728343.256163
FMO2-HF: Nuclear repulsion	1655751.265252
FMO2-HF: Total energy	-72591.990911
FMO2-MP2: Total energy	-72801.167539

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.
-7.953	-6.984	11.713	-5.561	-7.12	-0.026

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 : 0.016 / q_NPA : 0.013

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	-0.031	-0.021	3.819	0.190	2.838	0.240	-1.310	-1.578	0.003
4	A	28	GLN	0	-0.015	-0.003	1.977	-8.210	-10.416	11.469	-4.160	-5.104	-0.029
5	A	29	CYS	0	-0.038	-0.012	3.284	-0.021	0.438	0.005	-0.083	-0.380	0.000
6	A	30	GLN	0	0.018	0.002	4.672	0.661	0.729	-0.001	-0.008	-0.058	0.000
7	A	31	TYR	0	-0.013	-0.002	8.360	0.062	0.062	0.000	0.000	0.000	0.000
8	A	32	THR	0	0.040	0.021	11.045	0.026	0.026	0.000	0.000	0.000	0.000
9	A	33	ALA	0	0.041	0.021	13.143	0.002	0.002	0.000	0.000	0.000	0.000
10	A	34	GLU	-1	-0.873	-0.951	16.429	-0.238	-0.238	0.000	0.000	0.000	0.000
11	A	35	GLU	-1	-0.811	-0.894	11.725	-0.527	-0.527	0.000	0.000	0.000	0.000
12	A	36	TYR	0	0.006	0.001	15.319	0.025	0.025	0.000	0.000	0.000	0.000
13	A	37	GLN	0	-0.025	-0.016	16.347	0.030	0.030	0.000	0.000	0.000	0.000
14	A	38	ALA	0	-0.016	-0.014	18.951	0.023	0.023	0.000	0.000	0.000	0.000
15	A	39	ILE	0	0.063	0.034	14.837	0.027	0.027	0.000	0.000	0.000	0.000
16	A	40	GLN	0	-0.030	0.001	19.029	0.048	0.048	0.000	0.000	0.000	0.000
17	A	41	LYS	1	0.906	0.941	20.983	0.150	0.150	0.000	0.000	0.000	0.000
18	A	42	ALA	0	-0.007	-0.001	21.555	0.018	0.018	0.000	0.000	0.000	0.000
19	A	43	LEU	0	0.065	0.021	18.947	0.019	0.019	0.000	0.000	0.000	0.000
20	A	44	ARG	1	0.917	0.973	23.225	0.187	0.187	0.000	0.000	0.000	0.000
21	A	45	GLN	0	-0.044	-0.004	25.938	0.004	0.004	0.000	0.000	0.000	0.000
22	A	46	ARG	1	0.942	0.969	28.205	0.090	0.090	0.000	0.000	0.000	0.000
23	A	47	LEU	0	0.013	0.011	26.994	0.003	0.003	0.000	0.000	0.000	0.000
24	A	48	GLY	0	0.055	0.053	31.039	0.004	0.004	0.000	0.000	0.000	0.000
25	A	49	PRO	0	-0.009	-0.016	33.486	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	50	GLU	-1	-0.835	-0.917	32.694	-0.048	-0.048	0.000	0.000	0.000	0.000
27	A	51	TYR	0	-0.054	-0.034	26.461	0.002	0.002	0.000	0.000	0.000	0.000
28	A	52	ILE	0	-0.084	-0.030	31.660	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	53	SER	0	0.008	0.008	34.310	0.006	0.006	0.000	0.000	0.000	0.000
30	A	54	SER	0	-0.051	-0.037	36.115	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	55	ARG	1	0.996	0.992	36.688	0.038	0.038	0.000	0.000	0.000	0.000
32	A	56	MET	0	0.036	0.014	40.535	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	57	ALA	0	-0.005	0.010	42.145	0.000	0.000	0.000	0.000	0.000	0.000
34	A	58	GLY	0	0.039	0.012	43.263	0.002	0.002	0.000	0.000	0.000	0.000
35	A	59	GLY	0	0.019	0.016	45.555	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	60	GLY	0	-0.016	-0.009	46.488	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	61	GLN	0	-0.026	-0.011	44.466	0.001	0.001	0.000	0.000	0.000	0.000
38	A	62	LYS	1	0.972	0.996	42.647	0.038	0.038	0.000	0.000	0.000	0.000
39	A	63	VAL	0	-0.002	0.000	37.264	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	64	CYS	0	-0.028	-0.026	36.480	0.003	0.003	0.000	0.000	0.000	0.000
41	A	65	TYR	0	-0.057	-0.022	32.181	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	66	ILE	0	0.076	0.053	27.863	0.002	0.002	0.000	0.000	0.000	0.000
43	A	67	GLU	-1	-0.853	-0.944	29.801	-0.033	-0.033	0.000	0.000	0.000	0.000
44	A	68	GLY	0	0.056	0.014	26.068	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	69	HIS	0	0.004	0.000	24.651	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	70	ARG	1	0.952	0.986	24.555	0.039	0.039	0.000	0.000	0.000	0.000
47	A	71	VAL	0	0.029	0.011	22.130	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	72	ILE	0	0.015	0.014	19.335	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	73	ASN	0	-0.021	-0.009	19.706	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	74	LEU	0	-0.029	-0.009	20.757	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	75	ALA	0	0.032	0.014	17.252	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	76	ASN	0	0.004	0.004	15.844	-0.053	-0.053	0.000	0.000	0.000	0.000
53	A	77	GLU	-1	-0.941	-0.959	16.333	-0.089	-0.089	0.000	0.000	0.000	0.000
54	A	78	MET	0	-0.098	-0.030	18.033	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	79	PHE	0	-0.005	-0.020	13.128	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	80	GLY	0	0.080	0.053	12.451	-0.072	-0.072	0.000	0.000	0.000	0.000
57	A	81	TYR	0	-0.002	-0.015	10.340	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	82	ASN	0	-0.041	-0.016	6.563	-0.042	-0.042	0.000	0.000	0.000	0.000
59	A	83	GLY	0	0.029	0.014	7.903	-0.256	-0.256	0.000	0.000	0.000	0.000
60	A	84	TRP	0	-0.086	-0.068	10.171	-0.090	-0.090	0.000	0.000	0.000	0.000
61	A	85	ALA	0	0.020	0.018	10.125	0.054	0.054	0.000	0.000	0.000	0.000
62	A	86	HIS	0	0.008	-0.016	12.273	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	87	SER	0	-0.018	0.010	14.494	0.041	0.041	0.000	0.000	0.000	0.000
64	A	88	ILE	0	0.007	-0.011	16.296	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	89	THR	0	-0.022	0.000	19.224	0.017	0.017	0.000	0.000	0.000	0.000
66	A	90	GLN	0	0.003	-0.001	20.335	0.018	0.018	0.000	0.000	0.000	0.000
67	A	91	GLN	0	-0.009	0.015	23.947	0.000	0.000	0.000	0.000	0.000	0.000
68	A	92	ASN	0	-0.024	-0.012	26.833	0.001	0.001	0.000	0.000	0.000	0.000
69	A	93	VAL	0	-0.031	-0.025	30.489	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	94	ASP	-1	-0.809	-0.872	33.605	-0.029	-0.029	0.000	0.000	0.000	0.000
71	A	95	PHE	0	-0.006	-0.007	36.055	0.001	0.001	0.000	0.000	0.000	0.000
72	A	96	VAL	0	-0.071	-0.052	38.116	0.001	0.001	0.000	0.000	0.000	0.000
73	A	97	ASP	-1	-0.856	-0.909	40.561	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	98	LEU	0	-0.060	-0.044	44.179	0.000	0.000	0.000	0.000	0.000	0.000
75	A	99	ASN	0	0.023	0.009	46.830	0.001	0.001	0.000	0.000	0.000	0.000
76	A	100	ASN	0	-0.018	-0.019	49.667	0.000	0.000	0.000	0.000	0.000	0.000
77	A	101	GLY	0	0.011	0.008	50.323	0.000	0.000	0.000	0.000	0.000	0.000
78	A	102	ALA	0	-0.009	0.019	46.377	0.001	0.001	0.000	0.000	0.000	0.000
79	A	103	PHE	0	-0.041	-0.036	42.004	0.000	0.000	0.000	0.000	0.000	0.000
80	A	104	TYR	0	-0.019	-0.009	42.043	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	105	VAL	0	-0.025	-0.018	35.983	0.001	0.001	0.000	0.000	0.000	0.000
82	A	106	GLY	0	0.053	0.041	36.154	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	107	VAL	0	-0.061	-0.033	29.965	0.003	0.003	0.000	0.000	0.000	0.000
84	A	108	CYS	0	0.045	0.042	29.817	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	109	ALA	0	-0.023	-0.030	24.810	0.008	0.008	0.000	0.000	0.000	0.000
86	A	110	PHE	0	0.010	0.013	23.247	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	111	VAL	0	-0.007	0.008	19.483	0.009	0.009	0.000	0.000	0.000	0.000
88	A	112	ARG	1	0.992	0.994	12.263	0.236	0.236	0.000	0.000	0.000	0.000
89	A	113	VAL	0	-0.031	-0.027	15.638	0.012	0.012	0.000	0.000	0.000	0.000
90	A	114	GLN	0	-0.022	-0.013	8.052	0.134	0.134	0.000	0.000	0.000	0.000
91	A	115	LEU	0	-0.016	0.003	11.409	0.025	0.025	0.000	0.000	0.000	0.000
92	A	116	LYS	1	0.904	0.932	6.179	0.864	0.864	0.000	0.000	0.000	0.000
93	A	117	ASP	-1	-0.802	-0.863	6.105	-1.805	-1.805	0.000	0.000	0.000	0.000
94	A	118	GLY	0	-0.005	0.008	8.232	0.072	0.072	0.000	0.000	0.000	0.000
95	A	119	SER	0	-0.073	-0.075	10.156	0.234	0.234	0.000	0.000	0.000	0.000
96	A	120	TYR	0	-0.047	-0.040	13.355	0.024	0.024	0.000	0.000	0.000	0.000
97	A	121	HIS	0	-0.021	-0.002	15.606	0.022	0.022	0.000	0.000	0.000	0.000
98	A	122	GLU	-1	-0.895	-0.952	18.684	-0.111	-0.111	0.000	0.000	0.000	0.000
99	A	123	ASP	-1	-0.820	-0.885	20.667	-0.112	-0.112	0.000	0.000	0.000	0.000
100	A	124	VAL	0	-0.006	-0.007	24.074	0.007	0.007	0.000	0.000	0.000	0.000
101	A	125	GLY	0	-0.020	-0.013	26.776	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	126	TYR	0	-0.103	-0.090	28.094	0.006	0.006	0.000	0.000	0.000	0.000
103	A	127	GLY	0	-0.026	-0.013	31.281	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	128	VAL	0	0.022	0.002	32.631	0.002	0.002	0.000	0.000	0.000	0.000
105	A	129	SER	0	-0.044	-0.025	36.326	0.001	0.001	0.000	0.000	0.000	0.000
106	A	130	GLU	-1	-0.931	-0.964	38.568	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	131	GLY	0	0.030	0.012	42.312	0.000	0.000	0.000	0.000	0.000	0.000
108	A	132	LEU	0	-0.030	-0.010	39.617	0.002	0.002	0.000	0.000	0.000	0.000
109	A	133	ALA	0	0.107	0.053	43.788	0.000	0.000	0.000	0.000	0.000	0.000
110	A	134	SER	0	-0.018	0.005	41.039	0.001	0.001	0.000	0.000	0.000	0.000
111	A	135	LYS	1	1.030	1.018	39.531	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	136	ALA	0	-0.017	-0.006	37.584	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	137	LEU	0	0.041	0.007	36.454	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	138	SER	0	-0.004	-0.006	36.603	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	139	LEU	0	0.017	0.002	34.287	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	140	GLU	-1	-0.866	-0.909	31.638	0.009	0.009	0.000	0.000	0.000	0.000
117	A	141	LYS	1	0.835	0.908	31.580	0.017	0.017	0.000	0.000	0.000	0.000
118	A	142	ALA	0	0.039	0.024	32.219	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	143	ARG	1	0.932	0.944	28.760	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	144	LYS	1	0.874	0.918	27.264	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	145	GLU	-1	-0.842	-0.902	27.379	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	146	ALA	0	0.045	0.028	28.403	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	147	VAL	0	-0.006	-0.001	22.297	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	148	THR	0	-0.027	-0.012	24.010	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	149	ASP	-1	-0.882	-0.936	25.293	-0.072	-0.072	0.000	0.000	0.000	0.000
126	A	150	GLY	0	0.073	0.026	24.713	-0.009	-0.009	0.000	0.000	0.000	0.000
127	A	151	LEU	0	-0.038	-0.012	18.867	-0.015	-0.015	0.000	0.000	0.000	0.000
128	A	152	LYS	1	0.854	0.920	22.219	0.047	0.047	0.000	0.000	0.000	0.000
129	A	153	ARG	1	0.811	0.900	24.755	0.078	0.078	0.000	0.000	0.000	0.000
130	A	154	ALA	0	0.040	0.039	20.285	-0.009	-0.009	0.000	0.000	0.000	0.000
131	A	155	LEU	0	0.019	0.002	17.739	-0.021	-0.021	0.000	0.000	0.000	0.000
132	A	156	ARG	1	0.853	0.923	21.152	0.111	0.111	0.000	0.000	0.000	0.000
133	A	157	SER	0	-0.029	-0.015	21.942	0.008	0.008	0.000	0.000	0.000	0.000
134	A	158	PHE	0	-0.002	0.003	15.961	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	159	GLY	0	0.023	0.008	21.137	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	160	ASN	0	-0.106	-0.070	24.293	0.011	0.011	0.000	0.000	0.000	0.000
137	A	161	ALA	0	0.003	0.007	23.810	0.010	0.010	0.000	0.000	0.000	0.000
138	A	162	LEU	0	0.022	0.014	19.580	0.010	0.010	0.000	0.000	0.000	0.000
139	A	163	GLY	0	0.026	0.004	24.107	0.005	0.005	0.000	0.000	0.000	0.000
140	A	164	ASN	0	-0.042	-0.013	26.671	0.013	0.013	0.000	0.000	0.000	0.000
141	A	165	CYS	0	-0.031	-0.002	28.469	0.005	0.005	0.000	0.000	0.000	0.000
142	A	166	ILE	0	-0.015	-0.002	30.612	0.007	0.007	0.000	0.000	0.000	0.000
143	A	167	LEU	0	-0.005	-0.019	31.890	0.008	0.008	0.000	0.000	0.000	0.000
144	A	168	ASP	-1	-0.839	-0.912	34.324	-0.079	-0.079	0.000	0.000	0.000	0.000
145	A	169	LYS	1	0.961	0.960	36.067	0.067	0.067	0.000	0.000	0.000	0.000
146	A	170	ASP	-1	-0.829	-0.886	38.959	-0.060	-0.060	0.000	0.000	0.000	0.000
147	A	171	TYR	0	-0.036	-0.055	33.626	0.003	0.003	0.000	0.000	0.000	0.000
148	A	172	LEU	0	-0.014	-0.018	36.689	0.004	0.004	0.000	0.000	0.000	0.000
149	A	173	ARG	1	0.816	0.902	39.346	0.059	0.059	0.000	0.000	0.000	0.000
150	A	174	SER	0	0.017	-0.011	39.650	0.004	0.004	0.000	0.000	0.000	0.000
151	A	175	LEU	0	0.025	0.019	35.977	0.003	0.003	0.000	0.000	0.000	0.000
152	A	176	ASN	0	-0.056	-0.032	40.179	0.004	0.004	0.000	0.000	0.000	0.000
153	A	177	LYS	1	0.850	0.941	43.582	0.044	0.044	0.000	0.000	0.000	0.000
154	A	178	LEU	0	0.034	0.029	39.223	0.000	0.000	0.000	0.000	0.000	0.000
155	A	179	PRO	0	0.007	0.003	43.505	0.001	0.001	0.000	0.000	0.000	0.000
156	A	180	ARG	1	0.947	0.975	39.205	0.035	0.035	0.000	0.000	0.000	0.000
157	A	181	GLN	0	-0.004	-0.009	39.878	0.002	0.002	0.000	0.000	0.000	0.000
158	A	182	LEU	0	0.021	0.013	41.692	0.000	0.000	0.000	0.000	0.000	0.000
159	A	183	PRO	0	-0.033	-0.012	38.412	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	184	LEU	0	0.005	0.013	33.143	0.001	0.001	0.000	0.000	0.000	0.000
161	A	185	GLU	-1	-0.888	-0.946	37.032	-0.012	-0.012	0.000	0.000	0.000	0.000
162	A	186	VAL	0	-0.046	-0.032	32.117	-0.001	-0.001	0.000	0.000	0.000	0.000
163	A	187	ASP	-1	-0.819	-0.883	34.113	0.008	0.008	0.000	0.000	0.000	0.000
164	A	188	LEU	0	-0.034	-0.022	32.453	0.002	0.002	0.000	0.000	0.000	0.000
165	A	189	THR	0	-0.031	-0.047	34.117	0.005	0.005	0.000	0.000	0.000	0.000
166	A	190	LYS	1	0.906	0.949	30.088	-0.019	-0.019	0.000	0.000	0.000	0.000
167	A	191	ALA	0	-0.001	0.018	29.456	0.002	0.002	0.000	0.000	0.000	0.000
168	A	192	LYS	1	0.814	0.885	23.499	-0.079	-0.079	0.000	0.000	0.000	0.000
169	A	193	ARG	1	0.935	0.961	28.335	-0.032	-0.032	0.000	0.000	0.000	0.000
170	A	194	GLN	0	-0.012	-0.004	28.469	0.004	0.004	0.000	0.000	0.000	0.000
171	A	195	ASP	-1	-0.838	-0.924	24.957	0.086	0.086	0.000	0.000	0.000	0.000
172	A	196	LEU	0	-0.019	-0.015	23.953	0.007	0.007	0.000	0.000	0.000	0.000
173	A	197	GLU	-1	-0.827	-0.889	20.862	0.076	0.076	0.000	0.000	0.000	0.000
174	A	198	PRO	0	0.016	0.010	21.588	0.017	0.017	0.000	0.000	0.000	0.000
175	A	199	SER	0	0.033	0.022	20.940	0.015	0.015	0.000	0.000	0.000	0.000
176	A	200	VAL	0	0.026	0.009	16.071	0.019	0.019	0.000	0.000	0.000	0.000
177	A	201	GLU	-1	-0.936	-0.968	17.473	0.257	0.257	0.000	0.000	0.000	0.000
178	A	202	ALA	0	-0.020	-0.011	19.348	0.020	0.020	0.000	0.000	0.000	0.000
179	A	203	ALA	0	-0.019	-0.017	15.690	0.019	0.019	0.000	0.000	0.000	0.000
180	A	204	ARG	1	0.955	0.979	14.086	-0.246	-0.246	0.000	0.000	0.000	0.000
181	A	205	TYR	0	0.028	0.045	15.480	0.053	0.053	0.000	0.000	0.000	0.000
182	A	206	ASN	0	-0.067	-0.039	17.479	0.006	0.006	0.000	0.000	0.000	0.000
183	A	207	SER	0	-0.075	-0.054	12.319	0.033	0.033	0.000	0.000	0.000	0.000
184	A	208	CYS	0	-0.033	-0.007	13.063	0.087	0.087	0.000	0.000	0.000	0.000

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