FMO DATABASE

FMODB ID: 6Y68Z

Calculation Name: 1SUL-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1SUL

Chain ID: A

ChEMBL ID:

UniProt ID: P38424

Base Structure: X-ray

Registration Date: 2023-09-21

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	OptHSide
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	186
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2104577.752801
FMO2-HF: Nuclear repulsion	2031421.371835
FMO2-HF: Total energy	-73156.380966
FMO2-MP2: Total energy	-73372.750291

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:MET)

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

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.
-19.561	-12.747	23.002	-9.413	-20.403	-0.067

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.073 / q_NPA : -0.011

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	3	VAL	0	-0.002	0.004	2.164	0.242	2.524	1.473	-1.085	-2.671	0.002
4	A	4	THR	0	-0.033	-0.018	4.505	-0.104	0.057	0.000	-0.025	-0.136	0.000
5	A	5	LYS	1	0.753	0.855	6.098	0.519	0.519	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.029	-0.008	6.233	-0.616	-0.616	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.838	-0.898	8.550	-0.380	-0.380	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.000	-0.003	11.560	-0.126	-0.126	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.040	-0.018	12.652	0.060	0.060	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.013	0.006	15.416	0.073	0.073	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.036	-0.021	17.781	-0.065	-0.065	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.023	-0.006	20.209	0.045	0.045	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.008	-0.028	21.934	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.806	0.892	24.377	0.227	0.227	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.096	0.026	22.976	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.823	-0.891	23.166	-0.219	-0.219	0.000	0.000	0.000	0.000
17	A	17	GLN	0	-0.003	-0.004	22.829	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	18	TYR	0	-0.003	0.009	18.591	-0.042	-0.042	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.011	0.009	15.086	0.039	0.039	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.884	-0.932	17.529	-0.169	-0.169	0.000	0.000	0.000	0.000
21	A	21	GLY	0	-0.022	-0.026	15.123	-0.042	-0.042	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.007	0.002	15.107	0.046	0.046	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.060	-0.013	9.137	0.020	0.020	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.027	0.012	8.254	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.709	-0.827	9.521	-0.870	-0.870	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.043	-0.009	7.548	0.022	0.022	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.047	0.040	10.395	-0.100	-0.100	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.044	-0.024	10.355	-0.058	-0.058	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.058	0.026	14.300	0.091	0.091	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.039	0.004	17.974	-0.042	-0.042	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.851	0.936	20.238	0.421	0.421	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.034	-0.029	22.202	0.024	0.024	0.000	0.000	0.000	0.000
33	A	33	ASN	0	0.109	0.049	20.373	-0.080	-0.080	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.041	0.031	19.290	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.036	-0.023	19.064	-0.039	-0.039	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.832	0.922	15.693	0.631	0.631	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.086	0.036	14.710	-0.099	-0.099	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.044	-0.016	14.181	-0.123	-0.123	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.017	0.001	10.136	-0.085	-0.085	0.000	0.000	0.000	0.000
40	A	40	ILE	0	0.057	0.032	9.506	-0.220	-0.220	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.001	-0.003	9.215	-0.297	-0.297	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.040	-0.022	10.294	-0.077	-0.077	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.026	0.017	6.174	-0.065	-0.065	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.019	0.014	4.886	-1.034	-1.034	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.046	0.006	6.625	0.164	0.164	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.953	0.979	9.519	1.053	1.053	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.929	0.943	12.079	0.564	0.564	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.009	-0.015	15.179	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.009	0.044	10.763	0.046	0.046	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.024	0.012	12.972	0.100	0.100	0.000	0.000	0.000	0.000
51	A	60	GLN	0	-0.094	-0.073	24.982	-0.028	-0.028	0.000	0.000	0.000	0.000
52	A	61	THR	0	0.016	-0.006	21.121	0.029	0.029	0.000	0.000	0.000	0.000
53	A	62	LEU	0	0.014	0.017	18.229	-0.036	-0.036	0.000	0.000	0.000	0.000
54	A	63	ASN	0	-0.013	0.017	16.598	0.073	0.073	0.000	0.000	0.000	0.000
55	A	64	PHE	0	0.026	0.022	13.728	-0.106	-0.106	0.000	0.000	0.000	0.000
56	A	65	TYR	0	-0.012	-0.015	10.290	0.089	0.089	0.000	0.000	0.000	0.000
57	A	66	ILE	0	0.061	0.066	8.191	-0.233	-0.233	0.000	0.000	0.000	0.000
58	A	67	ILE	0	-0.021	-0.038	2.851	-0.533	-0.119	0.187	-0.104	-0.497	0.000
59	A	68	ASN	0	-0.025	-0.045	2.366	-2.100	-1.379	2.173	-0.804	-2.089	-0.007
60	A	69	ASP	-1	-0.825	-0.899	4.658	0.153	0.217	-0.001	-0.006	-0.056	0.000
61	A	70	GLU	-1	-0.773	-0.884	2.539	-1.480	1.750	2.373	-2.516	-3.087	-0.035
62	A	71	LEU	0	-0.013	0.004	3.147	-0.569	-0.176	0.067	-0.083	-0.377	-0.001
63	A	72	HIS	0	0.055	0.022	7.084	-0.358	-0.358	0.000	0.000	0.000	0.000
64	A	73	PHE	0	-0.051	-0.027	5.921	-0.210	-0.210	0.000	0.000	0.000	0.000
65	A	74	VAL	0	0.017	0.001	9.647	0.156	0.156	0.000	0.000	0.000	0.000
66	A	75	ASP	-1	-0.875	-0.932	13.376	-0.777	-0.777	0.000	0.000	0.000	0.000
67	A	76	VAL	0	0.062	0.027	15.457	0.085	0.085	0.000	0.000	0.000	0.000
68	A	77	PRO	0	-0.028	-0.013	18.632	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	78	GLY	0	-0.011	-0.016	21.669	0.008	0.008	0.000	0.000	0.000	0.000
70	A	79	TYR	0	0.021	-0.015	21.120	0.015	0.015	0.000	0.000	0.000	0.000
71	A	80	GLY	0	-0.015	0.002	25.319	0.022	0.022	0.000	0.000	0.000	0.000
72	A	81	PHE	0	0.043	-0.012	27.288	0.016	0.016	0.000	0.000	0.000	0.000
73	A	82	ALA	0	-0.016	0.009	30.993	0.017	0.017	0.000	0.000	0.000	0.000
74	A	83	LYS	1	0.934	0.955	32.977	0.237	0.237	0.000	0.000	0.000	0.000
75	A	84	VAL	0	0.017	0.045	30.283	0.003	0.003	0.000	0.000	0.000	0.000
76	A	85	SER	0	0.037	0.016	33.365	0.007	0.007	0.000	0.000	0.000	0.000
77	A	86	LYS	1	0.918	0.927	34.490	0.159	0.159	0.000	0.000	0.000	0.000
78	A	87	SER	0	0.006	0.007	35.158	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	88	GLU	-1	-0.796	-0.902	30.655	-0.275	-0.275	0.000	0.000	0.000	0.000
80	A	89	ARG	1	0.884	0.959	30.510	0.213	0.213	0.000	0.000	0.000	0.000
81	A	90	GLU	-1	-0.807	-0.880	30.405	-0.192	-0.192	0.000	0.000	0.000	0.000
82	A	91	ALA	0	-0.042	-0.019	30.511	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	92	TRP	0	-0.030	-0.019	22.978	0.003	0.003	0.000	0.000	0.000	0.000
84	A	93	GLY	0	0.016	0.002	26.162	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	94	ARG	1	0.948	0.954	27.481	0.205	0.205	0.000	0.000	0.000	0.000
86	A	95	MET	0	-0.024	0.022	23.019	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	96	ILE	0	0.022	0.001	19.848	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	97	GLU	-1	-0.842	-0.908	22.783	-0.269	-0.269	0.000	0.000	0.000	0.000
89	A	98	THR	0	-0.039	-0.007	24.959	0.016	0.016	0.000	0.000	0.000	0.000
90	A	99	TYR	0	-0.087	-0.055	14.951	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	100	ILE	0	-0.030	-0.026	18.971	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	101	THR	0	-0.039	-0.032	21.241	0.015	0.015	0.000	0.000	0.000	0.000
93	A	102	THR	0	-0.080	-0.048	22.911	0.022	0.022	0.000	0.000	0.000	0.000
94	A	103	ARG	1	0.754	0.867	15.537	0.465	0.465	0.000	0.000	0.000	0.000
95	A	104	GLU	-1	-0.896	-0.936	18.509	-0.179	-0.179	0.000	0.000	0.000	0.000
96	A	105	GLU	-1	-0.841	-0.936	13.729	-0.337	-0.337	0.000	0.000	0.000	0.000
97	A	106	LEU	0	-0.057	-0.022	13.410	-0.101	-0.101	0.000	0.000	0.000	0.000
98	A	107	LYS	1	0.865	0.927	11.437	0.393	0.393	0.000	0.000	0.000	0.000
99	A	108	ALA	0	-0.008	-0.008	11.908	0.037	0.037	0.000	0.000	0.000	0.000
100	A	109	VAL	0	0.002	0.011	13.147	-0.084	-0.084	0.000	0.000	0.000	0.000
101	A	110	VAL	0	-0.016	-0.006	10.386	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	111	GLN	0	-0.002	-0.012	13.766	0.037	0.037	0.000	0.000	0.000	0.000
103	A	112	ILE	0	-0.039	-0.024	14.240	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	113	VAL	0	0.030	0.013	17.501	0.077	0.077	0.000	0.000	0.000	0.000
105	A	114	ASP	-1	-0.802	-0.863	19.656	-0.513	-0.513	0.000	0.000	0.000	0.000
106	A	115	LEU	0	0.028	0.017	19.798	0.033	0.033	0.000	0.000	0.000	0.000
107	A	116	ARG	1	0.798	0.854	22.474	0.429	0.429	0.000	0.000	0.000	0.000
108	A	117	HIS	0	-0.040	-0.014	25.759	0.019	0.019	0.000	0.000	0.000	0.000
109	A	118	ALA	0	0.037	0.017	26.519	-0.021	-0.021	0.000	0.000	0.000	0.000
110	A	119	PRO	0	-0.041	-0.009	24.352	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	120	SER	0	-0.031	-0.032	26.656	0.028	0.028	0.000	0.000	0.000	0.000
112	A	121	ASN	0	0.088	0.024	28.361	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	122	ASP	-1	-0.851	-0.933	27.838	-0.299	-0.299	0.000	0.000	0.000	0.000
114	A	123	ASP	-1	-0.776	-0.838	23.969	-0.448	-0.448	0.000	0.000	0.000	0.000
115	A	124	VAL	0	0.051	0.024	24.895	-0.020	-0.020	0.000	0.000	0.000	0.000
116	A	125	GLN	0	0.038	0.035	27.218	0.013	0.013	0.000	0.000	0.000	0.000
117	A	126	MET	0	-0.044	-0.015	20.858	0.008	0.008	0.000	0.000	0.000	0.000
118	A	127	TYR	0	-0.039	-0.042	20.341	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	128	GLU	-1	-0.900	-0.957	23.766	-0.246	-0.246	0.000	0.000	0.000	0.000
120	A	129	PHE	0	-0.059	-0.026	22.798	0.007	0.007	0.000	0.000	0.000	0.000
121	A	130	LEU	0	-0.026	-0.023	19.121	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	131	LYS	1	0.822	0.881	20.203	0.402	0.402	0.000	0.000	0.000	0.000
123	A	132	TYR	0	-0.036	0.009	24.153	0.027	0.027	0.000	0.000	0.000	0.000
124	A	133	TYR	0	-0.087	-0.066	23.372	0.022	0.022	0.000	0.000	0.000	0.000
125	A	134	GLY	0	-0.007	0.010	23.242	0.006	0.006	0.000	0.000	0.000	0.000
126	A	135	ILE	0	-0.024	-0.002	17.258	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	136	PRO	0	0.025	0.016	15.477	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	137	VAL	0	-0.008	-0.010	16.229	-0.077	-0.077	0.000	0.000	0.000	0.000
129	A	138	ILE	0	-0.019	-0.003	10.186	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	139	VAL	0	0.026	0.012	14.325	-0.051	-0.051	0.000	0.000	0.000	0.000
131	A	140	ILE	0	-0.006	-0.001	11.455	-0.021	-0.021	0.000	0.000	0.000	0.000
132	A	141	ALA	0	0.019	0.010	15.427	0.062	0.062	0.000	0.000	0.000	0.000
133	A	142	THR	0	-0.025	-0.039	15.830	0.008	0.008	0.000	0.000	0.000	0.000
134	A	143	LYS	1	0.844	0.909	18.237	0.637	0.637	0.000	0.000	0.000	0.000
135	A	144	ALA	0	0.074	0.034	17.841	0.058	0.058	0.000	0.000	0.000	0.000
136	A	145	ASP	-1	-0.845	-0.882	19.264	-0.486	-0.486	0.000	0.000	0.000	0.000
137	A	146	LYS	1	0.850	0.907	20.798	0.437	0.437	0.000	0.000	0.000	0.000
138	A	147	ILE	0	-0.012	0.017	22.943	0.031	0.031	0.000	0.000	0.000	0.000
139	A	148	PRO	0	0.041	0.019	23.893	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	149	LYS	1	1.050	1.015	20.360	0.271	0.271	0.000	0.000	0.000	0.000
141	A	150	GLY	0	0.015	0.017	24.240	-0.002	-0.002	0.000	0.000	0.000	0.000
142	A	151	LYS	1	0.902	0.941	26.590	0.191	0.191	0.000	0.000	0.000	0.000
143	A	152	TRP	0	0.054	0.027	18.716	-0.020	-0.020	0.000	0.000	0.000	0.000
144	A	153	ASP	-1	-0.778	-0.867	23.537	-0.268	-0.268	0.000	0.000	0.000	0.000
145	A	154	LYS	1	0.972	0.985	24.802	0.195	0.195	0.000	0.000	0.000	0.000
146	A	155	HIS	0	-0.038	-0.032	24.470	0.009	0.009	0.000	0.000	0.000	0.000
147	A	156	ALA	0	0.021	0.001	21.819	-0.016	-0.016	0.000	0.000	0.000	0.000
148	A	157	LYS	1	0.854	0.920	23.245	0.233	0.233	0.000	0.000	0.000	0.000
149	A	158	VAL	0	0.005	0.017	26.283	0.006	0.006	0.000	0.000	0.000	0.000
150	A	159	VAL	0	0.029	0.019	21.458	0.001	0.001	0.000	0.000	0.000	0.000
151	A	160	ARG	1	0.914	0.955	19.926	0.370	0.370	0.000	0.000	0.000	0.000
152	A	161	GLN	0	-0.025	-0.027	24.633	0.008	0.008	0.000	0.000	0.000	0.000
153	A	162	THR	0	-0.055	-0.031	27.238	0.017	0.017	0.000	0.000	0.000	0.000
154	A	163	LEU	0	-0.038	-0.022	22.090	0.003	0.003	0.000	0.000	0.000	0.000
155	A	164	ASN	0	-0.018	0.005	26.076	0.010	0.010	0.000	0.000	0.000	0.000
156	A	165	ILE	0	-0.074	-0.040	20.453	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	166	ASP	-1	-0.812	-0.902	22.339	-0.244	-0.244	0.000	0.000	0.000	0.000
158	A	167	PRO	0	-0.044	-0.042	22.029	-0.030	-0.030	0.000	0.000	0.000	0.000
159	A	168	GLU	-1	-0.848	-0.903	19.352	-0.243	-0.243	0.000	0.000	0.000	0.000
160	A	169	ASP	-1	-0.734	-0.804	17.590	-0.492	-0.492	0.000	0.000	0.000	0.000
161	A	170	GLU	-1	-0.853	-0.928	12.964	-0.691	-0.691	0.000	0.000	0.000	0.000
162	A	171	LEU	0	-0.065	-0.030	16.385	-0.026	-0.026	0.000	0.000	0.000	0.000
163	A	172	ILE	0	-0.014	-0.004	10.820	0.027	0.027	0.000	0.000	0.000	0.000
164	A	173	LEU	0	-0.049	-0.020	14.764	-0.008	-0.008	0.000	0.000	0.000	0.000
165	A	174	PHE	0	0.055	0.012	9.848	0.009	0.009	0.000	0.000	0.000	0.000
166	A	175	SER	0	-0.095	-0.072	13.997	0.129	0.129	0.000	0.000	0.000	0.000
167	A	176	SER	0	0.074	0.031	13.787	-0.092	-0.092	0.000	0.000	0.000	0.000
168	A	177	GLU	-1	-0.952	-0.964	14.874	-0.515	-0.515	0.000	0.000	0.000	0.000
169	A	178	THR	0	0.000	-0.021	15.900	-0.014	-0.014	0.000	0.000	0.000	0.000
170	A	179	LYS	1	0.858	0.930	10.452	0.895	0.895	0.000	0.000	0.000	0.000
171	A	180	LYS	1	0.950	0.985	10.854	0.530	0.530	0.000	0.000	0.000	0.000
172	A	181	GLY	0	0.059	0.021	11.060	-0.011	-0.011	0.000	0.000	0.000	0.000
173	A	182	LYS	1	0.816	0.909	5.401	2.997	2.997	0.000	0.000	0.000	0.000
174	A	183	ASP	-1	-0.885	-0.936	4.852	-3.049	-3.049	0.000	0.000	0.000	0.000
175	A	184	GLU	-1	-0.886	-0.954	5.546	-1.393	-1.393	0.000	0.000	0.000	0.000
176	A	185	ALA	0	-0.004	0.002	7.926	0.123	0.123	0.000	0.000	0.000	0.000
177	A	186	TRP	0	0.004	-0.024	2.584	-6.371	-3.422	6.379	-2.203	-7.126	-0.030
178	A	187	GLY	0	0.021	0.015	4.553	0.320	0.497	-0.001	-0.009	-0.167	0.000
179	A	188	ALA	0	-0.028	-0.021	6.364	0.437	0.437	0.000	0.000	0.000	0.000
180	A	189	ILE	0	0.021	0.009	5.035	0.176	0.176	0.000	0.000	0.000	0.000
181	A	190	LYS	1	0.786	0.859	2.437	-8.662	-12.239	10.352	-2.578	-4.197	0.004
182	A	191	LYS	1	0.843	0.920	6.669	0.976	0.976	0.000	0.000	0.000	0.000
183	A	192	MET	0	-0.024	-0.009	9.995	0.153	0.153	0.000	0.000	0.000	0.000
184	A	193	ILE	0	-0.012	-0.007	5.637	0.031	0.031	0.000	0.000	0.000	0.000
185	A	194	ASN	0	-0.111	-0.061	9.597	0.248	0.248	0.000	0.000	0.000	0.000
186	A	195	ARG	1	0.877	0.956	11.548	0.324	0.324	0.000	0.000	0.000	0.000

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