FMO DATABASE

FMODB ID: 7JRLK

Calculation Name: 2NNU-A-Xray311

Preferred Name: Bromodomain-containing protein 4

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2NNU

Chain ID: A

ChEMBL ID: CHEMBL1163125

UniProt ID: O60885

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	203
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-2233635.090461
FMO2-HF: Nuclear repulsion	2149765.856034
FMO2-HF: Total energy	-83869.234427
FMO2-MP2: Total energy	-84110.039675

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:-1:ACE )

Summations of interaction energy for fragment #1(A:-1:ACE )

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.
0.562	1.626	-0.001	-0.444	-0.619	0

Interaction energy analysis for fragmet #1(A:-1:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : -0.003

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].
3	A	1	MET	0	0.054	0.022	3.830	0.960	1.784	-0.006	-0.370	-0.448
4	A	2	GLU	-1	-0.891	-0.946	7.056	-0.434	-0.434	0.000	0.000	0.000
5	A	3	THR	0	-0.003	0.006	3.754	0.278	0.492	0.005	-0.065	-0.155
6	A	4	LEU	0	-0.035	-0.025	5.409	0.388	0.388	0.000	0.000	0.000
7	A	5	CYS	0	-0.025	-0.006	7.612	0.121	0.121	0.000	0.000	0.000
8	A	6	GLN	0	0.016	0.014	8.696	0.095	0.095	0.000	0.000	0.000
9	A	7	ARG	1	0.920	0.954	7.514	-0.466	-0.466	0.000	0.000	0.000
10	A	8	LEU	0	0.002	0.003	10.729	0.020	0.020	0.000	0.000	0.000
11	A	9	ASN	0	0.034	0.017	13.117	0.006	0.006	0.000	0.000	0.000
12	A	10	VAL	0	0.029	0.034	14.312	0.010	0.010	0.000	0.000	0.000
13	A	11	CYS	0	-0.084	-0.031	14.416	0.014	0.014	0.000	0.000	0.000
14	A	12	GLN	0	0.009	-0.011	16.383	-0.015	-0.015	0.000	0.000	0.000
15	A	13	ASP	-1	-0.872	-0.917	18.705	-0.009	-0.009	0.000	0.000	0.000
16	A	14	LYS	1	0.801	0.880	19.424	-0.087	-0.087	0.000	0.000	0.000
17	A	15	ILE	0	-0.032	-0.014	19.236	0.000	0.000	0.000	0.000	0.000
18	A	16	LEU	0	0.008	0.004	22.633	-0.003	-0.003	0.000	0.000	0.000
19	A	17	THR	0	0.019	0.005	24.307	-0.002	-0.002	0.000	0.000	0.000
20	A	18	HIS	0	-0.071	-0.054	23.730	-0.005	-0.005	0.000	0.000	0.000
21	A	19	TYR	0	-0.041	0.001	25.084	0.001	0.001	0.000	0.000	0.000
22	A	20	GLU	-1	-0.967	-0.979	28.802	0.004	0.004	0.000	0.000	0.000
23	A	21	ASN	0	-0.070	-0.036	28.774	-0.004	-0.004	0.000	0.000	0.000
24	A	22	ASP	-1	-0.967	-0.960	31.628	0.024	0.024	0.000	0.000	0.000
25	A	23	SER	0	-0.037	-0.031	31.744	-0.001	-0.001	0.000	0.000	0.000
26	A	24	THR	0	-0.020	-0.036	33.610	-0.001	-0.001	0.000	0.000	0.000
27	A	25	ASP	-1	-0.867	-0.925	32.799	0.053	0.053	0.000	0.000	0.000
28	A	26	LEU	0	0.064	0.029	31.719	0.003	0.003	0.000	0.000	0.000
29	A	27	ARG	1	0.878	0.937	27.200	-0.082	-0.082	0.000	0.000	0.000
30	A	28	ASP	-1	-0.845	-0.911	27.795	0.064	0.064	0.000	0.000	0.000
31	A	29	HIS	0	0.013	-0.001	27.011	0.007	0.007	0.000	0.000	0.000
32	A	30	ILE	0	-0.017	0.003	24.924	0.006	0.006	0.000	0.000	0.000
33	A	31	ASP	-1	-0.834	-0.886	22.421	0.117	0.117	0.000	0.000	0.000
34	A	32	TYR	0	0.030	-0.002	22.198	0.012	0.012	0.000	0.000	0.000
35	A	33	TRP	0	0.038	0.006	22.185	0.009	0.009	0.000	0.000	0.000
36	A	34	LYS	1	0.934	0.975	18.299	-0.175	-0.175	0.000	0.000	0.000
37	A	35	HIS	0	-0.076	-0.054	17.293	0.035	0.035	0.000	0.000	0.000
38	A	36	MET	0	0.051	0.040	17.522	0.005	0.005	0.000	0.000	0.000
39	A	37	ARG	1	0.907	0.954	16.787	-0.194	-0.194	0.000	0.000	0.000
40	A	38	LEU	0	-0.080	-0.042	11.168	0.036	0.036	0.000	0.000	0.000
41	A	39	GLU	-1	-0.817	-0.925	13.156	0.061	0.061	0.000	0.000	0.000
42	A	40	CYS	0	-0.037	-0.010	14.145	-0.021	-0.021	0.000	0.000	0.000
43	A	41	ALA	0	-0.007	-0.003	11.559	-0.008	-0.008	0.000	0.000	0.000
44	A	42	ILE	0	-0.031	-0.011	9.419	0.032	0.032	0.000	0.000	0.000
45	A	43	TYR	0	0.038	0.008	10.246	-0.063	-0.063	0.000	0.000	0.000
46	A	44	TYR	0	-0.064	-0.023	11.892	-0.053	-0.053	0.000	0.000	0.000
47	A	45	LYS	1	0.973	0.982	5.203	-0.524	-0.524	0.000	0.000	0.000
48	A	46	ALA	0	0.020	-0.003	8.877	-0.112	-0.112	0.000	0.000	0.000
49	A	47	ARG	1	0.885	0.945	9.897	0.017	0.017	0.000	0.000	0.000
50	A	48	GLU	-1	-0.937	-0.982	10.294	0.155	0.155	0.000	0.000	0.000
51	A	49	MET	0	-0.122	-0.040	5.670	-0.129	-0.103	0.000	-0.009	-0.016
52	A	50	GLY	0	0.004	0.016	9.687	-0.082	-0.082	0.000	0.000	0.000
53	A	51	PHE	0	-0.029	-0.011	8.720	-0.009	-0.009	0.000	0.000	0.000
54	A	52	LYS	1	0.936	0.944	13.290	0.166	0.166	0.000	0.000	0.000
55	A	53	HIS	0	-0.002	0.012	15.516	0.037	0.037	0.000	0.000	0.000
56	A	54	ILE	0	0.032	0.007	10.606	-0.058	-0.058	0.000	0.000	0.000
57	A	55	ASN	0	0.022	0.003	14.181	0.000	0.000	0.000	0.000	0.000
58	A	56	HIS	0	-0.025	-0.022	16.341	0.029	0.029	0.000	0.000	0.000
59	A	57	GLN	0	0.014	0.025	17.576	0.031	0.031	0.000	0.000	0.000
60	A	58	VAL	0	0.012	-0.004	17.662	-0.018	-0.018	0.000	0.000	0.000
61	A	59	VAL	0	0.002	0.018	13.886	0.013	0.013	0.000	0.000	0.000
62	A	60	PRO	0	0.000	0.005	16.764	-0.006	-0.006	0.000	0.000	0.000
63	A	61	THR	0	-0.003	-0.012	17.307	-0.003	-0.003	0.000	0.000	0.000
64	A	62	LEU	0	0.072	0.026	14.164	0.007	0.007	0.000	0.000	0.000
65	A	63	ALA	0	0.001	0.002	17.581	0.017	0.017	0.000	0.000	0.000
66	A	64	VAL	0	0.008	0.010	20.714	0.008	0.008	0.000	0.000	0.000
67	A	65	SER	0	0.042	0.011	16.082	0.005	0.005	0.000	0.000	0.000
68	A	66	LYS	1	0.979	0.993	17.930	-0.085	-0.085	0.000	0.000	0.000
69	A	67	ASN	0	0.002	0.001	18.738	0.013	0.013	0.000	0.000	0.000
70	A	68	LYS	1	0.997	1.003	20.195	-0.019	-0.019	0.000	0.000	0.000
71	A	69	ALA	0	0.033	0.009	17.344	0.006	0.006	0.000	0.000	0.000
72	A	70	LEU	0	-0.050	-0.032	19.287	0.009	0.009	0.000	0.000	0.000
73	A	71	GLN	0	0.048	0.026	22.049	-0.001	-0.001	0.000	0.000	0.000
74	A	72	ALA	0	0.039	0.027	20.557	-0.001	-0.001	0.000	0.000	0.000
75	A	73	ILE	0	-0.080	-0.046	18.362	0.008	0.008	0.000	0.000	0.000
76	A	74	GLU	-1	-0.839	-0.883	22.313	0.069	0.069	0.000	0.000	0.000
77	A	75	LEU	0	0.024	0.014	25.751	-0.003	-0.003	0.000	0.000	0.000
78	A	76	GLN	0	-0.038	-0.029	21.253	0.010	0.010	0.000	0.000	0.000
79	A	77	LEU	0	-0.039	-0.022	23.907	0.000	0.000	0.000	0.000	0.000
80	A	78	THR	0	0.032	0.018	26.796	-0.005	-0.005	0.000	0.000	0.000
81	A	79	LEU	0	0.005	-0.010	28.163	-0.004	-0.004	0.000	0.000	0.000
82	A	80	GLU	-1	-0.896	-0.947	24.856	0.124	0.124	0.000	0.000	0.000
83	A	81	THR	0	-0.020	0.000	29.489	-0.002	-0.002	0.000	0.000	0.000
84	A	82	ILE	0	0.019	0.012	32.446	-0.004	-0.004	0.000	0.000	0.000
85	A	83	TYR	0	-0.014	-0.001	31.675	-0.002	-0.002	0.000	0.000	0.000
86	A	84	ASN	0	-0.058	-0.032	31.346	-0.004	-0.004	0.000	0.000	0.000
87	A	85	SER	0	-0.012	-0.011	34.976	-0.004	-0.004	0.000	0.000	0.000
88	A	86	GLN	0	-0.015	-0.022	38.117	0.000	0.000	0.000	0.000	0.000
89	A	87	TYR	0	0.018	0.000	38.906	-0.002	-0.002	0.000	0.000	0.000
90	A	88	SER	0	-0.029	0.011	35.956	-0.002	-0.002	0.000	0.000	0.000
91	A	89	ASN	0	-0.020	-0.017	37.064	0.001	0.001	0.000	0.000	0.000
92	A	90	GLU	-1	-0.859	-0.901	39.632	0.034	0.034	0.000	0.000	0.000
93	A	91	LYS	1	0.949	0.976	38.819	-0.023	-0.023	0.000	0.000	0.000
94	A	92	TRP	0	-0.004	-0.013	34.722	0.000	0.000	0.000	0.000	0.000
95	A	93	THR	0	-0.010	-0.003	35.241	0.001	0.001	0.000	0.000	0.000
96	A	94	LEU	0	0.097	0.027	28.464	0.002	0.002	0.000	0.000	0.000
97	A	95	GLN	0	0.001	0.001	32.027	0.002	0.002	0.000	0.000	0.000
98	A	96	ASP	-1	-0.827	-0.908	34.532	0.033	0.033	0.000	0.000	0.000
99	A	97	VAL	0	-0.043	-0.010	29.839	0.002	0.002	0.000	0.000	0.000
100	A	98	SER	0	0.004	0.003	29.983	0.004	0.004	0.000	0.000	0.000
101	A	99	LEU	0	0.011	-0.015	26.732	0.001	0.001	0.000	0.000	0.000
102	A	100	GLU	-1	-0.941	-0.963	30.014	0.017	0.017	0.000	0.000	0.000
103	A	101	VAL	0	0.031	0.025	33.129	-0.001	-0.001	0.000	0.000	0.000
104	A	102	TYR	0	-0.079	-0.060	30.396	-0.001	-0.001	0.000	0.000	0.000
105	A	103	LEU	0	-0.030	-0.034	29.855	0.001	0.001	0.000	0.000	0.000
106	A	104	THR	0	-0.046	-0.014	34.061	-0.003	-0.003	0.000	0.000	0.000
107	A	105	ALA	0	-0.034	-0.005	37.646	0.002	0.002	0.000	0.000	0.000
108	A	106	PRO	0	0.025	0.001	40.240	-0.001	-0.001	0.000	0.000	0.000
109	A	107	THR	0	0.007	-0.002	34.577	0.002	0.002	0.000	0.000	0.000
110	A	108	GLY	0	0.026	0.015	32.996	0.001	0.001	0.000	0.000	0.000
111	A	109	CYS	0	0.012	0.030	34.057	0.002	0.002	0.000	0.000	0.000
112	A	110	ILE	0	0.014	0.006	31.549	-0.002	-0.002	0.000	0.000	0.000
113	A	111	LYS	1	0.771	0.894	35.459	-0.036	-0.036	0.000	0.000	0.000
114	A	112	LYS	1	0.856	0.936	38.312	-0.036	-0.036	0.000	0.000	0.000
115	A	113	HIS	0	-0.058	-0.034	40.786	-0.001	-0.001	0.000	0.000	0.000
116	A	114	GLY	0	0.053	0.025	42.942	0.000	0.000	0.000	0.000	0.000
117	A	115	TYR	0	-0.044	-0.023	44.048	-0.001	-0.001	0.000	0.000	0.000
118	A	116	THR	0	0.017	0.009	47.167	0.001	0.001	0.000	0.000	0.000
119	A	117	VAL	0	-0.039	-0.010	48.729	0.000	0.000	0.000	0.000	0.000
120	A	118	GLU	-1	-0.913	-0.955	50.446	0.008	0.008	0.000	0.000	0.000
121	A	119	VAL	0	-0.030	-0.023	52.582	0.000	0.000	0.000	0.000	0.000
122	A	120	GLN	0	0.030	0.026	54.527	0.000	0.000	0.000	0.000	0.000
123	A	121	PHE	0	-0.011	-0.033	52.631	0.000	0.000	0.000	0.000	0.000
124	A	122	ASP	-1	-0.957	-1.002	58.022	0.005	0.005	0.000	0.000	0.000
125	A	123	GLY	0	0.016	0.035	61.522	0.000	0.000	0.000	0.000	0.000
126	A	124	ASP	-1	-0.917	-0.949	59.669	0.003	0.003	0.000	0.000	0.000
127	A	125	ILE	0	-0.006	-0.022	58.082	0.000	0.000	0.000	0.000	0.000
128	A	126	CYS	0	-0.090	-0.036	56.324	0.000	0.000	0.000	0.000	0.000
129	A	127	ASN	0	-0.016	-0.001	54.905	0.000	0.000	0.000	0.000	0.000
130	A	128	THR	0	0.014	-0.008	53.300	0.001	0.001	0.000	0.000	0.000
131	A	129	MET	0	-0.078	-0.016	46.469	-0.001	-0.001	0.000	0.000	0.000
132	A	130	HIS	0	0.023	0.007	47.793	0.001	0.001	0.000	0.000	0.000
133	A	131	TYR	0	-0.070	-0.072	45.996	0.000	0.000	0.000	0.000	0.000
134	A	132	THR	0	-0.007	-0.008	42.407	-0.001	-0.001	0.000	0.000	0.000
135	A	133	ASN	0	0.017	0.017	44.823	0.002	0.002	0.000	0.000	0.000
136	A	134	TRP	0	0.020	-0.018	39.293	0.000	0.000	0.000	0.000	0.000
137	A	135	THR	0	0.004	-0.031	44.927	0.000	0.000	0.000	0.000	0.000
138	A	136	HIS	0	0.006	0.054	42.792	0.000	0.000	0.000	0.000	0.000
139	A	137	ILE	0	0.006	0.009	40.505	0.001	0.001	0.000	0.000	0.000
140	A	138	TYR	0	-0.041	-0.053	37.471	-0.001	-0.001	0.000	0.000	0.000
141	A	139	ILE	0	0.009	0.002	37.756	0.002	0.002	0.000	0.000	0.000
142	A	140	CYS	0	-0.040	-0.012	34.294	0.001	0.001	0.000	0.000	0.000
143	A	141	GLU	-1	-0.845	-0.912	35.750	0.046	0.046	0.000	0.000	0.000
144	A	142	GLU	-1	-0.947	-0.975	33.367	0.060	0.060	0.000	0.000	0.000
145	A	143	ALA	0	-0.041	-0.019	33.259	0.004	0.004	0.000	0.000	0.000
146	A	144	SER	0	-0.039	-0.012	34.539	-0.003	-0.003	0.000	0.000	0.000
147	A	145	VAL	0	0.018	-0.017	36.237	0.001	0.001	0.000	0.000	0.000
148	A	146	THR	0	0.001	0.010	38.771	-0.002	-0.002	0.000	0.000	0.000
149	A	147	VAL	0	-0.063	-0.010	41.576	0.000	0.000	0.000	0.000	0.000
150	A	148	VAL	0	-0.021	-0.017	43.257	-0.002	-0.002	0.000	0.000	0.000
151	A	149	GLU	-1	-0.935	-0.967	45.208	0.022	0.022	0.000	0.000	0.000
152	A	150	GLY	0	-0.020	-0.008	47.016	0.000	0.000	0.000	0.000	0.000
153	A	151	GLN	0	-0.056	-0.034	47.585	-0.002	-0.002	0.000	0.000	0.000
154	A	152	VAL	0	0.019	0.000	50.605	0.000	0.000	0.000	0.000	0.000
155	A	153	ASP	-1	-0.778	-0.880	53.078	0.016	0.016	0.000	0.000	0.000
156	A	154	TYR	0	0.006	-0.001	55.351	0.000	0.000	0.000	0.000	0.000
157	A	155	TYR	0	-0.034	-0.022	54.765	-0.001	-0.001	0.000	0.000	0.000
158	A	156	GLY	0	0.066	0.021	51.216	0.000	0.000	0.000	0.000	0.000
159	A	157	LEU	0	-0.038	0.001	46.807	0.000	0.000	0.000	0.000	0.000
160	A	158	TYR	0	-0.017	-0.019	47.804	0.001	0.001	0.000	0.000	0.000
161	A	159	TYR	0	0.078	0.046	42.296	0.000	0.000	0.000	0.000	0.000
162	A	160	VAL	0	-0.048	-0.038	47.748	0.000	0.000	0.000	0.000	0.000
163	A	161	HIS	0	0.027	0.008	42.280	-0.002	-0.002	0.000	0.000	0.000
164	A	162	GLU	-1	-0.907	-0.953	44.747	0.038	0.038	0.000	0.000	0.000
165	A	163	GLY	0	-0.051	-0.021	48.375	-0.001	-0.001	0.000	0.000	0.000
166	A	164	ILE	0	-0.014	-0.001	47.267	-0.002	-0.002	0.000	0.000	0.000
167	A	165	ARG	1	0.881	0.951	48.726	-0.019	-0.019	0.000	0.000	0.000
168	A	166	THR	0	0.006	0.005	44.076	0.000	0.000	0.000	0.000	0.000
169	A	167	TYR	0	-0.094	-0.069	47.251	0.000	0.000	0.000	0.000	0.000
170	A	168	PHE	0	-0.031	-0.023	42.911	0.001	0.001	0.000	0.000	0.000
171	A	169	VAL	0	0.002	0.010	44.239	0.000	0.000	0.000	0.000	0.000
172	A	170	GLN	0	0.025	0.007	46.902	-0.001	-0.001	0.000	0.000	0.000
173	A	171	PHE	0	0.027	0.016	50.002	0.000	0.000	0.000	0.000	0.000
174	A	172	LYS	1	0.941	0.960	52.120	-0.015	-0.015	0.000	0.000	0.000
175	A	173	ASP	-1	-0.885	-0.929	48.001	0.015	0.015	0.000	0.000	0.000
176	A	174	ASP	-1	-0.838	-0.911	48.231	0.011	0.011	0.000	0.000	0.000
177	A	175	ALA	0	-0.035	-0.012	50.907	-0.001	-0.001	0.000	0.000	0.000
178	A	176	GLU	-1	-1.000	-0.997	52.711	0.010	0.010	0.000	0.000	0.000
179	A	177	LYS	1	0.882	0.966	45.165	-0.010	-0.010	0.000	0.000	0.000
180	A	178	TYR	0	-0.029	-0.025	47.697	-0.001	-0.001	0.000	0.000	0.000
181	A	179	SER	0	0.002	0.016	54.043	-0.001	-0.001	0.000	0.000	0.000
182	A	180	LYS	1	0.930	0.966	57.588	-0.003	-0.003	0.000	0.000	0.000
183	A	181	ASN	0	0.025	0.027	60.173	0.000	0.000	0.000	0.000	0.000
184	A	182	LYS	1	0.921	0.949	57.205	-0.011	-0.011	0.000	0.000	0.000
185	A	183	VAL	0	0.007	-0.011	60.039	0.001	0.001	0.000	0.000	0.000
186	A	184	TRP	0	-0.014	-0.003	56.438	-0.001	-0.001	0.000	0.000	0.000
187	A	185	GLU	-1	-0.954	-0.968	59.031	0.008	0.008	0.000	0.000	0.000
188	A	186	VAL	0	-0.022	-0.008	54.596	0.000	0.000	0.000	0.000	0.000
189	A	187	HIS	0	0.045	0.019	55.867	0.000	0.000	0.000	0.000	0.000
190	A	188	ALA	0	0.020	0.002	53.679	0.000	0.000	0.000	0.000	0.000
191	A	189	GLY	0	0.024	0.016	54.287	0.001	0.001	0.000	0.000	0.000
192	A	190	GLY	0	-0.033	-0.013	56.055	0.000	0.000	0.000	0.000	0.000
193	A	191	GLN	0	-0.058	-0.035	59.073	-0.001	-0.001	0.000	0.000	0.000
194	A	192	VAL	0	0.030	0.022	59.197	0.000	0.000	0.000	0.000	0.000
195	A	193	ILE	0	-0.028	-0.005	57.000	0.000	0.000	0.000	0.000	0.000
196	A	194	LEU	0	0.036	0.009	60.577	0.000	0.000	0.000	0.000	0.000
197	A	195	CYS	0	-0.012	-0.011	62.482	0.001	0.001	0.000	0.000	0.000
198	A	196	PRO	0	-0.005	0.010	61.831	0.000	0.000	0.000	0.000	0.000
199	A	197	THR	0	-0.030	-0.019	63.906	0.000	0.000	0.000	0.000	0.000
200	A	198	SER	0	-0.030	-0.019	66.667	0.000	0.000	0.000	0.000	0.000
201	A	199	VAL	0	0.023	0.015	66.652	0.000	0.000	0.000	0.000	0.000
202	A	200	PHE	0	-0.037	-0.027	68.735	0.000	0.000	0.000	0.000	0.000
203	A	201	NME	0	0.029	0.028	68.997	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:ACE )