FMO DATABASE

FMODB ID: 89LQY

Calculation Name: 2O6S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O6S

Chain ID: A

ChEMBL ID:

UniProt ID: Q4G1L3

Base Structure: X-ray

Registration Date: 2023-09-24

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	204
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2338189.374648
FMO2-HF: Nuclear repulsion	2257558.264581
FMO2-HF: Total energy	-80631.110067
FMO2-MP2: Total energy	-80864.494338

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:24:CYS)

Summations of interaction energy for fragment #1(A:24: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.
-18.485	-8.445	16.61	-10.718	-15.934	0.025

Interaction energy analysis for fragmet #1(A:24:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.039

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	26	SER	0	0.054	0.029	3.798	-2.138	-1.049	-0.006	-0.485	-0.598	0.001
4	A	27	ARG	1	0.905	0.935	6.144	2.736	2.736	0.000	0.000	0.000	0.000
5	A	28	CYS	0	-0.117	-0.038	3.704	-6.169	-2.981	0.067	-1.164	-2.091	-0.003
8	A	32	GLY	0	0.023	0.018	3.787	1.414	3.409	-0.027	-0.873	-1.094	0.005
9	A	33	THR	0	-0.035	-0.029	4.754	-0.102	0.015	-0.002	-0.012	-0.103	0.000
10	A	34	THR	0	0.011	0.007	4.205	0.070	0.470	-0.001	-0.093	-0.306	0.000
11	A	35	VAL	0	-0.005	-0.018	2.306	-4.747	-2.184	8.105	-4.351	-6.318	-0.016
12	A	36	GLU	-1	-0.889	-0.947	1.898	-8.021	-9.928	7.279	-2.644	-2.729	0.041
13	A	38	TYR	0	0.027	0.030	6.400	-1.416	-1.416	0.000	0.000	0.000	0.000
14	A	39	SER	0	0.014	0.001	9.127	-0.735	-0.735	0.000	0.000	0.000	0.000
15	A	40	GLN	0	-0.048	-0.015	6.150	0.490	0.490	0.000	0.000	0.000	0.000
16	A	41	GLY	0	0.002	-0.010	11.580	-0.065	-0.065	0.000	0.000	0.000	0.000
17	A	42	ARG	1	0.819	0.916	7.609	-0.199	-0.199	0.000	0.000	0.000	0.000
18	A	43	THR	0	0.022	-0.002	14.331	0.099	0.099	0.000	0.000	0.000	0.000
19	A	44	SER	0	-0.030	-0.018	14.319	0.001	0.001	0.000	0.000	0.000	0.000
20	A	45	VAL	0	0.036	0.022	10.628	0.017	0.017	0.000	0.000	0.000	0.000
21	A	46	PRO	0	-0.035	-0.012	7.350	-0.334	-0.334	0.000	0.000	0.000	0.000
22	A	47	THR	0	0.039	0.011	8.186	0.487	0.487	0.000	0.000	0.000	0.000
23	A	48	GLY	0	0.030	-0.003	4.671	-0.339	-0.328	-0.002	-0.009	0.000	0.000
24	A	49	ILE	0	0.000	0.007	3.153	0.980	2.297	0.090	-0.513	-0.895	-0.004
25	A	50	PRO	0	0.000	0.004	2.962	-2.984	-1.859	1.109	-0.567	-1.667	0.001
26	A	51	ALA	0	0.090	0.048	5.783	-0.156	-0.156	0.000	0.000	0.000	0.000
27	A	52	GLN	0	0.000	-0.006	8.717	0.373	0.373	0.000	0.000	0.000	0.000
28	A	53	THR	0	-0.051	-0.035	6.143	0.233	0.375	-0.002	-0.007	-0.133	0.000
29	A	54	THR	0	0.014	0.022	8.186	-0.387	-0.387	0.000	0.000	0.000	0.000
30	A	55	TYR	0	0.025	0.022	6.813	-0.835	-0.835	0.000	0.000	0.000	0.000
31	A	56	LEU	0	0.027	0.009	6.877	1.896	1.896	0.000	0.000	0.000	0.000
32	A	57	ASP	-1	-0.806	-0.905	6.721	1.862	1.862	0.000	0.000	0.000	0.000
33	A	58	LEU	0	-0.027	-0.034	7.526	0.482	0.482	0.000	0.000	0.000	0.000
34	A	59	GLU	-1	-0.822	-0.915	10.186	0.945	0.945	0.000	0.000	0.000	0.000
35	A	60	THR	0	-0.052	-0.019	11.983	-0.177	-0.177	0.000	0.000	0.000	0.000
36	A	61	ASN	0	-0.057	-0.021	10.647	-0.657	-0.657	0.000	0.000	0.000	0.000
37	A	62	SER	0	-0.061	-0.042	14.881	-0.128	-0.128	0.000	0.000	0.000	0.000
38	A	63	LEU	0	0.004	0.009	13.998	-0.105	-0.105	0.000	0.000	0.000	0.000
39	A	64	LYS	1	0.943	0.969	18.136	-0.578	-0.578	0.000	0.000	0.000	0.000
40	A	65	SER	0	-0.008	-0.006	21.047	-0.017	-0.017	0.000	0.000	0.000	0.000
41	A	66	LEU	0	0.031	0.005	16.902	0.086	0.086	0.000	0.000	0.000	0.000
42	A	67	PRO	0	0.019	0.019	17.409	-0.083	-0.083	0.000	0.000	0.000	0.000
43	A	68	ASN	0	0.017	-0.014	19.448	0.082	0.082	0.000	0.000	0.000	0.000
44	A	69	GLY	0	0.058	0.026	19.130	-0.016	-0.016	0.000	0.000	0.000	0.000
45	A	70	VAL	0	-0.067	-0.018	13.913	0.093	0.093	0.000	0.000	0.000	0.000
46	A	71	PHE	0	0.031	0.001	13.087	0.224	0.224	0.000	0.000	0.000	0.000
47	A	72	ASP	-1	-0.925	-0.965	14.721	1.494	1.494	0.000	0.000	0.000	0.000
48	A	73	GLU	-1	-0.910	-0.956	12.208	1.687	1.687	0.000	0.000	0.000	0.000
49	A	74	LEU	0	-0.064	-0.022	8.992	0.172	0.172	0.000	0.000	0.000	0.000
50	A	75	THR	0	0.004	-0.016	12.525	-0.039	-0.039	0.000	0.000	0.000	0.000
51	A	76	SER	0	-0.012	0.005	12.006	-0.305	-0.305	0.000	0.000	0.000	0.000
52	A	77	LEU	0	-0.061	-0.016	10.352	0.036	0.036	0.000	0.000	0.000	0.000
53	A	78	THR	0	-0.037	-0.022	12.900	-0.382	-0.382	0.000	0.000	0.000	0.000
54	A	79	GLN	0	0.003	0.017	11.853	-0.259	-0.259	0.000	0.000	0.000	0.000
55	A	80	LEU	0	0.023	0.022	11.684	0.592	0.592	0.000	0.000	0.000	0.000
56	A	81	TYR	0	-0.032	-0.027	10.470	-0.605	-0.605	0.000	0.000	0.000	0.000
57	A	82	LEU	0	0.000	-0.017	12.108	0.266	0.266	0.000	0.000	0.000	0.000
58	A	83	GLY	0	0.050	0.046	14.794	-0.225	-0.225	0.000	0.000	0.000	0.000
59	A	84	GLY	0	0.015	0.003	15.457	0.071	0.071	0.000	0.000	0.000	0.000
60	A	85	ASN	0	-0.065	-0.033	14.252	-0.118	-0.118	0.000	0.000	0.000	0.000
61	A	86	LYS	1	0.913	0.941	18.269	-0.455	-0.455	0.000	0.000	0.000	0.000
62	A	87	LEU	0	0.000	0.007	18.391	-0.051	-0.051	0.000	0.000	0.000	0.000
63	A	88	GLN	0	0.040	0.020	22.206	-0.031	-0.031	0.000	0.000	0.000	0.000
64	A	89	SER	0	-0.038	-0.018	25.003	-0.026	-0.026	0.000	0.000	0.000	0.000
65	A	90	LEU	0	0.021	0.003	21.531	0.069	0.069	0.000	0.000	0.000	0.000
66	A	91	PRO	0	0.013	0.030	21.664	-0.067	-0.067	0.000	0.000	0.000	0.000
67	A	92	ASN	0	0.054	-0.007	24.600	0.039	0.039	0.000	0.000	0.000	0.000
68	A	93	GLY	0	-0.031	-0.027	24.761	0.017	0.017	0.000	0.000	0.000	0.000
69	A	94	VAL	0	-0.005	0.010	19.459	0.061	0.061	0.000	0.000	0.000	0.000
70	A	95	PHE	0	0.095	0.039	18.333	0.129	0.129	0.000	0.000	0.000	0.000
71	A	96	ASN	0	-0.057	-0.029	20.756	0.006	0.006	0.000	0.000	0.000	0.000
72	A	97	LYS	1	0.981	0.989	18.421	-1.158	-1.158	0.000	0.000	0.000	0.000
73	A	98	LEU	0	0.009	0.016	15.441	0.037	0.037	0.000	0.000	0.000	0.000
74	A	99	THR	0	0.012	-0.010	18.467	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	100	SER	0	0.001	0.020	17.416	-0.158	-0.158	0.000	0.000	0.000	0.000
76	A	101	LEU	0	-0.061	-0.015	15.610	0.028	0.028	0.000	0.000	0.000	0.000
77	A	102	THR	0	-0.084	-0.043	17.191	-0.174	-0.174	0.000	0.000	0.000	0.000
78	A	103	TYR	0	0.008	-0.001	15.839	-0.192	-0.192	0.000	0.000	0.000	0.000
79	A	104	LEU	0	0.027	0.021	16.310	0.236	0.236	0.000	0.000	0.000	0.000
80	A	105	ASN	0	0.066	0.057	15.781	-0.287	-0.287	0.000	0.000	0.000	0.000
81	A	106	LEU	0	0.029	-0.003	16.953	0.130	0.130	0.000	0.000	0.000	0.000
82	A	107	SER	0	-0.052	-0.024	19.144	-0.132	-0.132	0.000	0.000	0.000	0.000
83	A	108	THR	0	-0.010	-0.014	19.719	0.032	0.032	0.000	0.000	0.000	0.000
84	A	109	ASN	0	-0.042	-0.009	18.522	0.024	0.024	0.000	0.000	0.000	0.000
85	A	110	GLN	0	-0.042	-0.034	22.336	-0.078	-0.078	0.000	0.000	0.000	0.000
86	A	111	LEU	0	0.015	0.019	22.822	-0.025	-0.025	0.000	0.000	0.000	0.000
87	A	112	GLN	0	0.067	0.026	26.602	-0.038	-0.038	0.000	0.000	0.000	0.000
88	A	113	SER	0	-0.043	-0.020	29.390	-0.022	-0.022	0.000	0.000	0.000	0.000
89	A	114	LEU	0	0.015	0.002	25.961	0.048	0.048	0.000	0.000	0.000	0.000
90	A	115	PRO	0	0.012	0.015	27.009	-0.041	-0.041	0.000	0.000	0.000	0.000
91	A	116	ASN	0	0.067	0.009	29.884	0.022	0.022	0.000	0.000	0.000	0.000
92	A	117	GLY	0	0.027	0.014	30.732	0.020	0.020	0.000	0.000	0.000	0.000
93	A	118	VAL	0	-0.057	-0.015	24.603	0.042	0.042	0.000	0.000	0.000	0.000
94	A	119	PHE	0	0.049	0.010	23.054	0.080	0.080	0.000	0.000	0.000	0.000
95	A	120	ASP	-1	-0.883	-0.949	26.120	0.639	0.639	0.000	0.000	0.000	0.000
96	A	121	LYS	1	0.900	0.945	24.606	-0.866	-0.866	0.000	0.000	0.000	0.000
97	A	122	LEU	0	0.009	0.019	21.144	0.027	0.027	0.000	0.000	0.000	0.000
98	A	123	THR	0	0.022	-0.001	24.050	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	124	GLN	0	-0.019	0.001	21.485	-0.048	-0.048	0.000	0.000	0.000	0.000
100	A	125	LEU	0	-0.038	-0.008	20.278	0.022	0.022	0.000	0.000	0.000	0.000
101	A	126	LYS	1	0.911	0.949	21.252	-0.887	-0.887	0.000	0.000	0.000	0.000
102	A	127	GLU	-1	-0.943	-0.973	19.556	0.969	0.969	0.000	0.000	0.000	0.000
103	A	128	LEU	0	0.050	0.030	20.774	0.104	0.104	0.000	0.000	0.000	0.000
104	A	129	ALA	0	0.004	0.017	20.120	-0.113	-0.113	0.000	0.000	0.000	0.000
105	A	130	LEU	0	0.018	-0.013	21.607	0.065	0.065	0.000	0.000	0.000	0.000
106	A	131	ASN	0	-0.012	0.003	22.813	0.007	0.007	0.000	0.000	0.000	0.000
107	A	132	THR	0	-0.035	-0.025	23.957	0.060	0.060	0.000	0.000	0.000	0.000
108	A	133	ASN	0	-0.021	0.002	23.093	0.039	0.039	0.000	0.000	0.000	0.000
109	A	134	GLN	0	-0.026	-0.027	26.623	-0.032	-0.032	0.000	0.000	0.000	0.000
110	A	135	LEU	0	-0.003	0.010	27.393	-0.019	-0.019	0.000	0.000	0.000	0.000
111	A	136	GLN	0	0.022	0.003	30.965	-0.019	-0.019	0.000	0.000	0.000	0.000
112	A	137	SER	0	-0.079	-0.031	33.515	-0.020	-0.020	0.000	0.000	0.000	0.000
113	A	138	LEU	0	0.000	-0.006	30.554	0.032	0.032	0.000	0.000	0.000	0.000
114	A	139	PRO	0	0.002	0.007	31.349	-0.026	-0.026	0.000	0.000	0.000	0.000
115	A	140	ASP	-1	-0.830	-0.928	34.391	0.378	0.378	0.000	0.000	0.000	0.000
116	A	141	GLY	0	0.003	-0.001	35.559	0.017	0.017	0.000	0.000	0.000	0.000
117	A	142	VAL	0	-0.058	-0.019	29.357	0.030	0.030	0.000	0.000	0.000	0.000
118	A	143	PHE	0	0.028	-0.003	27.891	0.047	0.047	0.000	0.000	0.000	0.000
119	A	144	ASP	-1	-0.901	-0.946	30.961	0.456	0.456	0.000	0.000	0.000	0.000
120	A	145	LYS	1	0.853	0.928	29.707	-0.599	-0.599	0.000	0.000	0.000	0.000
121	A	146	LEU	0	-0.003	0.011	25.968	0.020	0.020	0.000	0.000	0.000	0.000
122	A	147	THR	0	0.014	0.003	28.914	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	148	GLN	0	-0.016	-0.004	26.032	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	149	LEU	0	-0.033	-0.008	24.641	0.014	0.014	0.000	0.000	0.000	0.000
125	A	150	LYS	1	0.921	0.960	24.954	-0.625	-0.625	0.000	0.000	0.000	0.000
126	A	151	ASP	-1	-0.848	-0.914	23.929	0.590	0.590	0.000	0.000	0.000	0.000
127	A	152	LEU	0	0.060	0.038	24.910	0.058	0.058	0.000	0.000	0.000	0.000
128	A	153	ARG	1	0.868	0.916	23.009	-0.706	-0.706	0.000	0.000	0.000	0.000
129	A	154	LEU	0	0.053	0.013	26.099	0.036	0.036	0.000	0.000	0.000	0.000
130	A	155	TYR	0	-0.010	0.008	24.684	-0.011	-0.011	0.000	0.000	0.000	0.000
131	A	156	GLN	0	0.028	0.016	27.891	0.051	0.051	0.000	0.000	0.000	0.000
132	A	157	ASN	0	-0.031	-0.016	27.590	0.041	0.041	0.000	0.000	0.000	0.000
133	A	158	GLN	0	-0.022	-0.023	31.040	-0.048	-0.048	0.000	0.000	0.000	0.000
134	A	159	LEU	0	0.006	0.023	32.000	-0.011	-0.011	0.000	0.000	0.000	0.000
135	A	160	LYS	1	0.977	0.989	35.622	-0.253	-0.253	0.000	0.000	0.000	0.000
136	A	161	SER	0	-0.017	-0.013	38.398	-0.012	-0.012	0.000	0.000	0.000	0.000
137	A	162	VAL	0	0.006	0.006	35.558	0.019	0.019	0.000	0.000	0.000	0.000
138	A	163	PRO	0	0.023	0.020	36.270	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	164	ASP	-1	-0.896	-0.952	39.139	0.281	0.281	0.000	0.000	0.000	0.000
140	A	165	GLY	0	0.006	-0.027	40.367	0.008	0.008	0.000	0.000	0.000	0.000
141	A	166	VAL	0	-0.048	-0.009	34.093	0.017	0.017	0.000	0.000	0.000	0.000
142	A	167	PHE	0	0.010	-0.017	32.518	0.029	0.029	0.000	0.000	0.000	0.000
143	A	168	ASP	-1	-0.862	-0.915	35.640	0.331	0.331	0.000	0.000	0.000	0.000
144	A	169	ARG	1	0.933	0.973	34.983	-0.431	-0.431	0.000	0.000	0.000	0.000
145	A	170	LEU	0	-0.015	0.004	30.533	0.017	0.017	0.000	0.000	0.000	0.000
146	A	171	THR	0	-0.016	-0.021	33.405	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	172	SER	0	-0.015	0.003	29.884	-0.026	-0.026	0.000	0.000	0.000	0.000
148	A	173	LEU	0	-0.054	-0.016	29.316	0.011	0.011	0.000	0.000	0.000	0.000
149	A	174	GLN	0	-0.056	-0.038	28.984	-0.006	-0.006	0.000	0.000	0.000	0.000
150	A	175	TYR	0	-0.059	-0.031	27.365	-0.052	-0.052	0.000	0.000	0.000	0.000
151	A	176	ILE	0	0.028	0.030	28.915	0.038	0.038	0.000	0.000	0.000	0.000
152	A	177	TRP	0	-0.021	0.006	26.280	-0.028	-0.028	0.000	0.000	0.000	0.000
153	A	178	LEU	0	0.053	0.001	30.453	0.018	0.018	0.000	0.000	0.000	0.000
154	A	179	HIS	0	-0.077	-0.043	30.133	0.002	0.002	0.000	0.000	0.000	0.000
155	A	180	ASP	-1	-0.836	-0.919	32.218	0.288	0.288	0.000	0.000	0.000	0.000
156	A	181	ASN	0	0.042	0.021	31.948	0.026	0.026	0.000	0.000	0.000	0.000
157	A	182	PRO	0	-0.014	0.011	35.406	-0.019	-0.019	0.000	0.000	0.000	0.000
158	A	183	TRP	0	-0.010	-0.018	34.866	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	184	ASP	-1	-0.860	-0.930	40.350	0.195	0.195	0.000	0.000	0.000	0.000
160	A	185	CYS	0	-0.093	-0.057	40.365	0.018	0.018	0.000	0.000	0.000	0.000
161	A	186	THR	0	0.039	0.025	45.986	-0.013	-0.013	0.000	0.000	0.000	0.000
162	A	187	CYS	0	-0.106	-0.027	48.071	0.006	0.006	0.000	0.000	0.000	0.000
163	A	188	PRO	0	0.036	-0.012	50.317	-0.005	-0.005	0.000	0.000	0.000	0.000
164	A	189	GLY	0	0.040	0.015	46.594	0.006	0.006	0.000	0.000	0.000	0.000
165	A	190	ILE	0	0.006	0.012	42.450	0.012	0.012	0.000	0.000	0.000	0.000
166	A	191	ARG	1	0.938	0.969	44.713	-0.231	-0.231	0.000	0.000	0.000	0.000
167	A	192	TYR	0	-0.034	-0.006	38.644	0.002	0.002	0.000	0.000	0.000	0.000
168	A	193	LEU	0	0.051	0.027	37.565	0.003	0.003	0.000	0.000	0.000	0.000
169	A	194	SER	0	0.002	-0.011	41.327	0.003	0.003	0.000	0.000	0.000	0.000
170	A	195	GLU	-1	-0.899	-0.962	43.863	0.213	0.213	0.000	0.000	0.000	0.000
171	A	196	TRP	0	-0.023	-0.007	34.888	-0.006	-0.006	0.000	0.000	0.000	0.000
172	A	197	ILE	0	0.012	-0.013	38.378	0.002	0.002	0.000	0.000	0.000	0.000
173	A	198	ASN	0	-0.060	-0.045	40.500	-0.009	-0.009	0.000	0.000	0.000	0.000
174	A	199	LYS	1	0.907	0.974	42.710	-0.240	-0.240	0.000	0.000	0.000	0.000
175	A	200	HIS	1	0.872	0.944	37.594	-0.303	-0.303	0.000	0.000	0.000	0.000
176	A	201	SER	0	0.043	0.024	38.128	0.014	0.014	0.000	0.000	0.000	0.000
177	A	202	GLY	0	0.014	-0.001	37.794	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	203	VAL	0	0.004	0.004	32.806	0.005	0.005	0.000	0.000	0.000	0.000
179	A	204	VAL	0	-0.004	0.004	32.925	0.024	0.024	0.000	0.000	0.000	0.000
180	A	205	ARG	1	0.902	0.958	30.024	-0.344	-0.344	0.000	0.000	0.000	0.000
181	A	206	ASN	0	0.041	0.019	32.203	0.021	0.021	0.000	0.000	0.000	0.000
182	A	207	SER	0	0.060	0.027	29.484	0.011	0.011	0.000	0.000	0.000	0.000
183	A	208	ALA	0	-0.015	-0.004	28.892	0.011	0.011	0.000	0.000	0.000	0.000
184	A	209	GLY	0	0.020	0.020	29.043	-0.002	-0.002	0.000	0.000	0.000	0.000
185	A	210	SER	0	-0.057	-0.019	29.782	-0.003	-0.003	0.000	0.000	0.000	0.000
186	A	211	VAL	0	0.015	0.003	33.283	0.015	0.015	0.000	0.000	0.000	0.000
187	A	212	ALA	0	-0.002	-0.017	35.516	-0.020	-0.020	0.000	0.000	0.000	0.000
188	A	213	PRO	0	0.026	0.023	37.190	0.011	0.011	0.000	0.000	0.000	0.000
189	A	214	ASP	-1	-0.807	-0.867	39.201	0.188	0.188	0.000	0.000	0.000	0.000
190	A	215	SER	0	-0.073	-0.049	35.692	-0.002	-0.002	0.000	0.000	0.000	0.000
191	A	216	ALA	0	0.029	0.040	37.123	0.004	0.004	0.000	0.000	0.000	0.000
192	A	217	LYS	1	0.894	0.932	38.017	-0.204	-0.204	0.000	0.000	0.000	0.000
193	A	219	SER	0	-0.026	-0.015	41.806	-0.010	-0.010	0.000	0.000	0.000	0.000
194	A	220	GLY	0	0.026	0.019	42.806	-0.004	-0.004	0.000	0.000	0.000	0.000
195	A	221	SER	0	-0.010	-0.007	46.040	-0.005	-0.005	0.000	0.000	0.000	0.000
196	A	222	GLY	0	0.070	0.047	43.573	-0.008	-0.008	0.000	0.000	0.000	0.000
197	A	223	LYS	1	0.915	0.949	44.112	-0.143	-0.143	0.000	0.000	0.000	0.000
198	A	224	PRO	0	0.039	0.021	42.750	0.010	0.010	0.000	0.000	0.000	0.000
199	A	225	VAL	0	0.094	0.046	40.409	-0.008	-0.008	0.000	0.000	0.000	0.000
200	A	226	ARG	1	0.820	0.874	42.381	-0.199	-0.199	0.000	0.000	0.000	0.000
201	A	227	SER	0	-0.078	-0.047	44.358	-0.010	-0.010	0.000	0.000	0.000	0.000
202	A	228	ILE	0	-0.031	-0.017	46.647	-0.011	-0.011	0.000	0.000	0.000	0.000
203	A	229	ILE	0	0.015	0.021	48.383	0.009	0.009	0.000	0.000	0.000	0.000
204	A	231	PRO	0	0.037	0.029	52.156	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:CYS)