FMO DATABASE

FMODB ID: YQ4L2

Calculation Name: 6A84-A-Xray63

Preferred Name:

Target Type:

Ligand Name: 2-(4-chloro-1,2-dihydro-1'h-spiro[indole-3,4'-piperidin]-1'-yl)-5,6,7,8-tetrahydroquinazolin-4(3h)-one

ligand 3-letter code: 9SU

PDB ID: 6A84

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-Ray

Registration Date: 2019-08-23

Reference:

DOI: 10.1021/acs.jmedchem.8b01888

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHL
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Manual calculation

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	212
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-2642190.874163
FMO2-HF: Nuclear repulsion	2555621.849672
FMO2-HF: Total energy	-86569.024491
FMO2-MP2: Total energy	-86817.097545

3D Structure

Snapshot

Ligand structure

9SU

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.
-116.814	-79.623	76.754	-29.442	-84.503	0.043

Interactive mode: IFIE and PIEDA for fragment #212(A:1163:9SU )

Summations of interaction energy for fragment #212(A:1163:9SU )

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.
-116.814	-79.623	76.754	-29.442	-84.503	-0.043

Interaction energy analysis for fragmet #212(A:1163:9SU )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.042 / 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].
1	A	952	GLY	1	0.818	0.886	20.551	0.234	0.234	0.000	0.000	0.000	0.000
2	A	953	THR	0	0.068	0.010	16.648	-0.024	-0.024	0.000	0.000	0.000	0.000
3	A	954	ILE	0	0.008	0.026	19.759	-0.007	-0.007	0.000	0.000	0.000	0.000
4	A	955	LEU	0	-0.005	-0.001	16.504	0.018	0.018	0.000	0.000	0.000	0.000
5	A	956	ILE	0	-0.006	-0.001	20.467	-0.027	-0.027	0.000	0.000	0.000	0.000
6	A	957	ASP	-1	-0.851	-0.934	20.957	0.552	0.552	0.000	0.000	0.000	0.000
7	A	958	LEU	0	-0.023	-0.005	19.028	-0.043	-0.043	0.000	0.000	0.000	0.000
8	A	959	SER	0	0.019	0.012	22.500	0.032	0.032	0.000	0.000	0.000	0.000
9	A	960	PRO	0	0.064	0.017	23.337	0.021	0.021	0.000	0.000	0.000	0.000
10	A	961	ASP	-1	-0.905	-0.946	24.358	0.444	0.444	0.000	0.000	0.000	0.000
11	A	962	ASP	-1	-0.931	-0.959	24.194	0.461	0.461	0.000	0.000	0.000	0.000
12	A	963	LYS	1	0.972	0.966	24.169	-0.376	-0.376	0.000	0.000	0.000	0.000
13	A	964	GLU	-1	-0.775	-0.832	20.001	0.648	0.648	0.000	0.000	0.000	0.000
14	A	965	PHE	0	-0.008	0.001	19.696	0.113	0.113	0.000	0.000	0.000	0.000
15	A	966	GLN	0	0.000	-0.014	19.202	0.108	0.108	0.000	0.000	0.000	0.000
16	A	967	SER	0	-0.009	0.007	18.705	0.032	0.032	0.000	0.000	0.000	0.000
17	A	968	VAL	0	-0.013	-0.002	14.008	0.111	0.111	0.000	0.000	0.000	0.000
18	A	969	GLU	-1	-0.894	-0.948	14.988	1.275	1.275	0.000	0.000	0.000	0.000
19	A	970	GLU	-1	-0.881	-0.957	16.104	1.110	1.110	0.000	0.000	0.000	0.000
20	A	971	GLU	-1	-0.933	-0.947	12.636	1.335	1.335	0.000	0.000	0.000	0.000
21	A	972	MET	0	-0.093	-0.035	10.322	0.492	0.492	0.000	0.000	0.000	0.000
22	A	973	GLN	0	-0.011	-0.030	12.354	0.271	0.271	0.000	0.000	0.000	0.000
23	A	974	SER	0	-0.002	0.015	14.896	0.021	0.021	0.000	0.000	0.000	0.000
24	A	975	THR	0	-0.025	0.002	10.193	0.148	0.148	0.000	0.000	0.000	0.000
25	A	976	VAL	0	-0.031	-0.011	9.981	0.431	0.431	0.000	0.000	0.000	0.000
26	A	977	ARG	1	0.841	0.932	6.469	-1.339	-1.339	0.000	0.000	0.000	0.000
27	A	978	GLU	-1	-0.858	-0.916	11.661	0.885	0.885	0.000	0.000	0.000	0.000
28	A	979	HIS	0	-0.051	-0.060	6.598	-0.304	-0.304	0.000	0.000	0.000	0.000
29	A	980	ARG	1	0.908	0.915	9.177	-0.230	-0.230	0.000	0.000	0.000	0.000
30	A	981	ASP	-1	-0.841	-0.913	10.215	1.108	1.108	0.000	0.000	0.000	0.000
31	A	982	GLY	0	0.020	0.010	12.501	0.003	0.003	0.000	0.000	0.000	0.000
32	A	983	GLY	0	0.026	0.015	12.688	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	984	HIS	0	-0.062	-0.015	12.450	0.083	0.083	0.000	0.000	0.000	0.000
34	A	985	ALA	0	-0.031	-0.026	8.638	0.049	0.049	0.000	0.000	0.000	0.000
35	A	986	GLY	0	0.030	-0.006	9.615	0.207	0.207	0.000	0.000	0.000	0.000
36	A	987	GLY	0	0.026	0.014	10.420	0.074	0.074	0.000	0.000	0.000	0.000
37	A	988	ILE	0	-0.002	0.005	13.411	0.078	0.078	0.000	0.000	0.000	0.000
38	A	989	PHE	0	-0.031	-0.016	10.147	0.028	0.028	0.000	0.000	0.000	0.000
39	A	990	ASN	0	0.062	0.033	14.968	0.069	0.069	0.000	0.000	0.000	0.000
40	A	991	ARG	1	0.903	0.952	15.773	-0.765	-0.765	0.000	0.000	0.000	0.000
41	A	992	TYR	0	-0.063	-0.067	9.839	0.148	0.148	0.000	0.000	0.000	0.000
42	A	993	ASN	0	0.016	0.013	16.251	-0.135	-0.135	0.000	0.000	0.000	0.000
43	A	994	ILE	0	0.012	0.001	14.713	0.123	0.123	0.000	0.000	0.000	0.000
44	A	995	LEU	0	-0.048	-0.017	17.253	-0.123	-0.123	0.000	0.000	0.000	0.000
45	A	996	LYS	1	0.928	0.957	17.518	-0.676	-0.676	0.000	0.000	0.000	0.000
46	A	997	ILE	0	0.028	0.036	15.621	0.174	0.174	0.000	0.000	0.000	0.000
47	A	998	GLN	0	-0.046	-0.023	16.266	-0.071	-0.071	0.000	0.000	0.000	0.000
48	A	999	LYS	1	0.907	0.949	16.268	-0.428	-0.428	0.000	0.000	0.000	0.000
49	A	1000	VAL	0	0.011	0.007	14.215	-0.119	-0.119	0.000	0.000	0.000	0.000
50	A	1001	CYS	0	-0.020	0.019	17.435	-0.024	-0.024	0.000	0.000	0.000	0.000
51	A	1002	ASN	0	0.017	-0.034	18.427	-0.075	-0.075	0.000	0.000	0.000	0.000
52	A	1003	LYS	1	0.938	0.948	20.394	0.097	0.097	0.000	0.000	0.000	0.000
53	A	1004	LYS	1	0.970	0.990	19.675	0.482	0.482	0.000	0.000	0.000	0.000
54	A	1005	LEU	0	-0.036	-0.022	15.166	-0.038	-0.038	0.000	0.000	0.000	0.000
55	A	1006	TRP	0	0.065	0.038	17.532	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	1007	GLU	-1	-0.843	-0.905	19.966	-0.155	-0.155	0.000	0.000	0.000	0.000
57	A	1008	ARG	1	0.940	0.971	15.535	0.842	0.842	0.000	0.000	0.000	0.000
58	A	1009	TYR	0	-0.041	-0.019	14.951	-0.020	-0.020	0.000	0.000	0.000	0.000
59	A	1010	THR	0	-0.070	-0.042	18.298	0.014	0.014	0.000	0.000	0.000	0.000
60	A	1011	HIS	0	-0.008	0.007	21.671	0.042	0.042	0.000	0.000	0.000	0.000
61	A	1012	ARG	1	0.890	0.947	17.432	0.562	0.562	0.000	0.000	0.000	0.000
62	A	1013	ARG	1	0.885	0.939	18.892	-0.071	-0.071	0.000	0.000	0.000	0.000
63	A	1014	LYS	1	0.882	0.933	20.372	0.184	0.184	0.000	0.000	0.000	0.000
64	A	1015	GLU	-1	-0.840	-0.917	22.539	-0.448	-0.448	0.000	0.000	0.000	0.000
65	A	1016	VAL	0	-0.007	0.001	17.705	0.010	0.010	0.000	0.000	0.000	0.000
66	A	1017	SER	0	-0.029	-0.028	20.975	0.028	0.028	0.000	0.000	0.000	0.000
67	A	1018	GLU	-1	-0.889	-0.938	22.769	-0.156	-0.156	0.000	0.000	0.000	0.000
68	A	1019	GLU	-1	-0.896	-0.905	22.372	-0.403	-0.403	0.000	0.000	0.000	0.000
69	A	1020	ASN	0	-0.087	-0.058	19.722	-0.020	-0.020	0.000	0.000	0.000	0.000
70	A	1021	HIS	1	0.872	0.933	22.428	0.105	0.105	0.000	0.000	0.000	0.000
71	A	1022	ASN	0	0.008	0.010	25.663	0.014	0.014	0.000	0.000	0.000	0.000
72	A	1023	HIS	0	0.060	0.039	19.109	0.025	0.025	0.000	0.000	0.000	0.000
73	A	1024	ALA	0	0.052	0.023	18.909	-0.033	-0.033	0.000	0.000	0.000	0.000
74	A	1025	ASN	0	-0.060	-0.023	15.280	0.062	0.062	0.000	0.000	0.000	0.000
75	A	1026	GLU	-1	-0.725	-0.844	15.042	0.270	0.270	0.000	0.000	0.000	0.000
76	A	1027	ARG	1	0.868	0.937	11.132	-0.407	-0.407	0.000	0.000	0.000	0.000
77	A	1028	MET	0	0.018	0.025	11.618	-0.160	-0.160	0.000	0.000	0.000	0.000
78	A	1029	LEU	0	-0.005	0.001	6.230	0.015	0.015	0.000	0.000	0.000	0.000
79	A	1030	PHE	0	0.026	0.018	5.209	-0.091	-0.091	0.000	0.000	0.000	0.000
80	A	1031	HIS	0	-0.026	-0.028	2.578	-6.728	-2.625	2.055	-1.974	-4.185	0.004
81	A	1032	GLY	0	0.039	0.014	1.828	-12.038	-15.818	10.841	-3.690	-3.371	0.042
82	A	1033	SER	0	0.002	-0.007	1.966	-23.606	-19.927	7.089	-4.660	-6.109	-0.058
83	A	1034	PRO	0	0.055	0.033	2.627	-0.736	-0.702	5.464	-1.261	-4.237	0.001
84	A	1035	PHE	0	-0.023	-0.018	2.745	-3.784	-0.837	2.878	-1.163	-4.661	0.011
85	A	1036	VAL	0	0.068	0.043	6.234	-0.350	-0.350	0.000	0.000	0.000	0.000
86	A	1037	ASN	0	0.046	0.012	8.058	0.138	0.138	0.000	0.000	0.000	0.000
87	A	1038	ALA	0	-0.014	-0.010	8.949	0.051	0.051	0.000	0.000	0.000	0.000
88	A	1039	ILE	0	0.027	0.025	5.191	0.150	0.150	0.000	0.000	0.000	0.000
89	A	1040	ILE	0	0.043	0.034	9.722	0.166	0.166	0.000	0.000	0.000	0.000
90	A	1041	HIS	0	-0.077	-0.001	12.894	0.133	0.133	0.000	0.000	0.000	0.000
91	A	1042	LYS	1	0.811	0.889	12.786	0.874	0.874	0.000	0.000	0.000	0.000
92	A	1043	GLY	0	0.014	0.019	12.554	0.009	0.009	0.000	0.000	0.000	0.000
93	A	1044	PHE	0	0.009	-0.006	5.827	-0.162	-0.162	0.000	0.000	0.000	0.000
94	A	1045	ASP	-1	-0.871	-0.946	8.067	-2.614	-2.614	0.000	0.000	0.000	0.000
95	A	1046	GLU	-1	-0.868	-0.930	7.161	-3.602	-3.602	0.000	0.000	0.000	0.000
96	A	1047	ARG	1	0.913	0.964	5.613	1.937	1.937	0.000	0.000	0.000	0.000
97	A	1048	HIS	0	-0.031	-0.020	3.427	-1.863	-1.239	0.013	-0.096	-0.541	0.000
98	A	1049	ALA	0	0.005	0.009	2.776	-5.902	-3.442	0.658	-1.285	-1.833	-0.014
99	A	1050	TYR	0	-0.039	-0.014	2.047	-15.563	-8.647	9.340	-4.646	-11.610	-0.022
100	A	1051	ILE	0	0.012	-0.012	2.951	1.950	1.614	0.147	1.191	-1.003	0.001
101	A	1052	GLY	0	0.002	-0.003	5.463	0.344	0.344	0.000	0.000	0.000	0.000
102	A	1053	GLY	0	-0.013	0.007	5.538	0.299	0.299	0.000	0.000	0.000	0.000
103	A	1054	MET	0	-0.006	-0.021	5.768	0.169	0.169	0.000	0.000	0.000	0.000
104	A	1055	PHE	0	0.008	0.012	5.360	0.248	0.248	0.000	0.000	0.000	0.000
105	A	1056	GLY	0	0.034	0.042	8.643	0.046	0.046	0.000	0.000	0.000	0.000
106	A	1057	ALA	0	0.013	0.007	7.032	-0.211	-0.211	0.000	0.000	0.000	0.000
107	A	1058	GLY	0	0.073	0.030	6.609	0.289	0.289	0.000	0.000	0.000	0.000
108	A	1059	ILE	0	-0.002	-0.004	4.865	-1.625	-1.625	0.000	0.000	0.000	0.000
109	A	1060	TYR	0	-0.016	-0.007	2.247	-2.318	0.475	5.387	-1.984	-6.196	0.005
110	A	1061	PHE	0	0.006	0.000	3.094	-0.468	1.732	0.183	-0.666	-1.717	-0.003
111	A	1062	ALA	0	0.008	-0.003	2.193	-4.995	-3.680	2.880	-1.177	-3.018	-0.009
112	A	1063	GLU	-1	-0.748	-0.852	3.714	1.507	1.582	0.020	0.004	-0.100	0.000
113	A	1064	ASN	0	0.015	0.006	5.826	-0.318	-0.318	0.000	0.000	0.000	0.000
114	A	1065	SER	0	0.103	0.060	5.432	1.486	1.486	0.000	0.000	0.000	0.000
115	A	1066	SER	0	0.049	0.032	6.436	1.248	1.248	0.000	0.000	0.000	0.000
116	A	1067	LYS	1	0.801	0.892	2.347	-2.452	-1.378	2.094	-0.524	-2.643	0.002
117	A	1068	SER	0	0.036	0.005	1.974	-13.930	-11.990	6.353	-3.579	-4.714	0.032
118	A	1069	ASN	0	0.010	0.030	3.448	-2.508	-2.874	0.019	0.773	-0.425	0.002
119	A	1070	GLN	0	0.017	0.019	5.023	-1.314	-1.314	0.000	0.000	0.000	0.000
120	A	1071	TYR	0	-0.003	-0.008	2.205	-14.069	-3.827	8.128	-3.375	-14.995	-0.015
121	A	1072	VAL	0	-0.009	0.004	3.568	-2.400	-0.669	0.250	-0.751	-1.229	-0.007
122	A	1073	TYR	0	-0.006	-0.009	5.821	-0.407	-0.263	-0.001	-0.004	-0.139	0.000
123	A	1074	GLY	0	0.012	-0.002	2.691	1.326	-1.144	5.145	-1.048	-1.628	0.003
124	A	1075	ILE	0	-0.011	-0.007	2.444	-0.718	-2.193	6.031	1.884	-6.439	0.005
125	A	1076	GLY	0	0.008	0.014	4.086	-0.874	-0.895	0.038	0.312	-0.329	0.001
126	A	1077	GLY	0	0.064	0.035	5.835	-0.265	-0.265	0.000	0.000	0.000	0.000
127	A	1078	GLY	0	-0.036	-0.013	6.418	-0.111	-0.111	0.000	0.000	0.000	0.000
128	A	1079	THR	0	-0.023	-0.026	7.042	-0.331	-0.331	0.000	0.000	0.000	0.000
129	A	1080	GLY	0	0.035	0.017	9.228	-0.174	-0.174	0.000	0.000	0.000	0.000
130	A	1081	CYS	0	-0.098	-0.002	10.198	-0.030	-0.030	0.000	0.000	0.000	0.000
131	A	1082	PRO	0	0.017	-0.009	10.744	-0.094	-0.094	0.000	0.000	0.000	0.000
132	A	1083	VAL	0	-0.010	-0.006	12.791	-0.080	-0.080	0.000	0.000	0.000	0.000
133	A	1084	HIS	0	0.025	-0.027	16.097	-0.067	-0.067	0.000	0.000	0.000	0.000
134	A	1085	LYS	1	0.895	0.961	12.255	-0.559	-0.559	0.000	0.000	0.000	0.000
135	A	1086	ASP	-1	-0.768	-0.891	14.538	0.877	0.877	0.000	0.000	0.000	0.000
136	A	1087	ARG	1	0.858	0.926	10.094	-1.040	-1.040	0.000	0.000	0.000	0.000
137	A	1088	SER	0	-0.004	-0.003	12.539	0.220	0.220	0.000	0.000	0.000	0.000
138	A	1089	CYS	0	-0.083	0.035	14.889	-0.084	-0.084	0.000	0.000	0.000	0.000
139	A	1090	TYR	0	0.010	-0.023	16.328	0.059	0.059	0.000	0.000	0.000	0.000
140	A	1091	ILE	0	0.001	-0.012	18.788	-0.022	-0.022	0.000	0.000	0.000	0.000
141	A	1092	CYS	0	-0.033	-0.033	15.282	-0.045	-0.045	0.000	0.000	0.000	0.000
142	A	1093	HIS	0	0.042	0.027	16.182	0.149	0.149	0.000	0.000	0.000	0.000
143	A	1094	ARG	1	0.795	0.905	10.926	-1.977	-1.977	0.000	0.000	0.000	0.000
144	A	1095	GLN	0	-0.012	-0.026	10.637	-0.252	-0.252	0.000	0.000	0.000	0.000
145	A	1096	LEU	0	-0.030	0.003	5.146	0.433	0.535	-0.001	-0.002	-0.099	0.000
146	A	1097	LEU	0	-0.029	-0.016	6.605	-1.246	-1.246	0.000	0.000	0.000	0.000
147	A	1098	PHE	0	0.043	0.026	7.152	1.514	1.514	0.000	0.000	0.000	0.000
148	A	1099	CYS	0	-0.069	-0.038	7.728	-0.884	-0.884	0.000	0.000	0.000	0.000
149	A	1100	ARG	1	0.824	0.895	10.345	-0.424	-0.424	0.000	0.000	0.000	0.000
150	A	1101	VAL	0	-0.010	-0.004	8.441	-0.237	-0.237	0.000	0.000	0.000	0.000
151	A	1102	THR	0	-0.006	-0.012	11.893	0.024	0.024	0.000	0.000	0.000	0.000
152	A	1103	LEU	0	-0.007	0.000	9.679	-0.156	-0.156	0.000	0.000	0.000	0.000
153	A	1104	GLY	0	0.052	0.044	13.490	-0.111	-0.111	0.000	0.000	0.000	0.000
154	A	1105	LYS	1	0.908	0.972	16.574	0.271	0.271	0.000	0.000	0.000	0.000
155	A	1106	SER	0	-0.006	0.007	12.024	-0.071	-0.071	0.000	0.000	0.000	0.000
156	A	1107	PHE	0	-0.023	-0.011	13.890	0.055	0.055	0.000	0.000	0.000	0.000
157	A	1108	LEU	0	-0.017	-0.001	12.854	-0.043	-0.043	0.000	0.000	0.000	0.000
158	A	1109	GLN	0	0.016	0.010	11.026	-0.029	-0.029	0.000	0.000	0.000	0.000
159	A	1110	PHE	0	0.006	-0.001	11.313	-0.018	-0.018	0.000	0.000	0.000	0.000
160	A	1111	SER	0	0.018	0.018	8.792	-0.081	-0.081	0.000	0.000	0.000	0.000
161	A	1112	ALA	0	0.033	0.027	11.087	0.058	0.058	0.000	0.000	0.000	0.000
162	A	1113	MET	0	-0.023	-0.014	7.116	0.065	0.065	0.000	0.000	0.000	0.000
163	A	1114	NME	0	0.063	0.050	8.438	0.084	0.084	0.000	0.000	0.000	0.000
164	A	1114	ACE	0	0.018	-0.018	9.892	0.101	0.101	0.000	0.000	0.000	0.000
165	A	1115	MET	0	-0.069	-0.029	8.179	-0.852	-0.852	0.000	0.000	0.000	0.000
166	A	1116	ALA	0	-0.027	0.006	10.284	0.360	0.360	0.000	0.000	0.000	0.000
167	A	1117	HIS	0	0.017	-0.002	12.723	-0.012	-0.012	0.000	0.000	0.000	0.000
168	A	1118	SER	0	-0.017	-0.005	14.242	-0.002	-0.002	0.000	0.000	0.000	0.000
169	A	1119	PRO	0	0.018	0.008	14.051	0.035	0.035	0.000	0.000	0.000	0.000
170	A	1120	PRO	0	0.075	0.024	17.293	0.026	0.026	0.000	0.000	0.000	0.000
171	A	1121	GLY	0	-0.001	0.017	20.882	0.034	0.034	0.000	0.000	0.000	0.000
172	A	1122	HIS	0	-0.091	-0.055	16.197	0.095	0.095	0.000	0.000	0.000	0.000
173	A	1123	HIS	0	0.005	-0.027	15.963	-0.038	-0.038	0.000	0.000	0.000	0.000
174	A	1124	SER	0	-0.031	-0.031	10.725	-0.052	-0.052	0.000	0.000	0.000	0.000
175	A	1125	VAL	0	0.003	0.011	9.440	0.071	0.071	0.000	0.000	0.000	0.000
176	A	1126	THR	0	-0.012	-0.027	8.749	0.036	0.036	0.000	0.000	0.000	0.000
177	A	1127	GLY	0	0.031	0.012	7.249	-0.005	-0.005	0.000	0.000	0.000	0.000
178	A	1128	ARG	1	0.983	0.970	7.636	-0.064	-0.064	0.000	0.000	0.000	0.000
179	A	1129	PRO	0	-0.036	-0.025	7.685	-0.043	-0.043	0.000	0.000	0.000	0.000
180	A	1130	SER	0	0.005	-0.001	10.312	0.077	0.077	0.000	0.000	0.000	0.000
181	A	1131	VAL	0	-0.023	0.004	12.961	0.020	0.020	0.000	0.000	0.000	0.000
182	A	1132	ASN	0	-0.015	-0.020	11.310	0.038	0.038	0.000	0.000	0.000	0.000
183	A	1133	GLY	0	0.041	0.020	12.833	0.001	0.001	0.000	0.000	0.000	0.000
184	A	1134	LEU	0	0.021	0.005	13.642	0.016	0.016	0.000	0.000	0.000	0.000
185	A	1135	ALA	0	-0.114	-0.048	8.413	0.147	0.147	0.000	0.000	0.000	0.000
186	A	1136	LEU	0	0.016	0.015	8.032	-0.149	-0.149	0.000	0.000	0.000	0.000
187	A	1137	ALA	0	-0.058	-0.023	6.890	-0.206	-0.206	0.000	0.000	0.000	0.000
188	A	1138	GLU	-1	-0.899	-0.957	2.319	-6.345	-3.378	1.744	-1.698	-3.012	-0.024
189	A	1139	TYR	0	-0.090	-0.084	4.098	-0.270	-0.110	0.000	-0.015	-0.145	0.000
190	A	1140	VAL	0	-0.018	0.003	4.754	-0.291	-0.158	-0.001	-0.008	-0.125	0.000
191	A	1141	ILE	0	0.012	0.009	7.100	0.289	0.289	0.000	0.000	0.000	0.000
192	A	1142	TYR	0	0.001	-0.030	9.573	-0.426	-0.426	0.000	0.000	0.000	0.000
193	A	1143	ARG	1	0.969	0.988	11.544	0.810	0.810	0.000	0.000	0.000	0.000
194	A	1144	GLY	0	0.061	0.036	10.634	0.049	0.049	0.000	0.000	0.000	0.000
195	A	1145	GLU	-1	-0.930	-0.986	11.627	-0.901	-0.901	0.000	0.000	0.000	0.000
196	A	1146	GLN	0	-0.051	-0.034	13.472	0.137	0.137	0.000	0.000	0.000	0.000
197	A	1147	ALA	0	0.017	0.011	10.479	0.216	0.216	0.000	0.000	0.000	0.000
198	A	1148	TYR	0	-0.037	-0.042	12.560	-0.319	-0.319	0.000	0.000	0.000	0.000
199	A	1149	PRO	0	-0.022	-0.015	10.467	0.299	0.299	0.000	0.000	0.000	0.000
200	A	1150	GLU	-1	-0.804	-0.888	11.935	0.510	0.510	0.000	0.000	0.000	0.000
201	A	1151	TYR	0	-0.034	-0.057	12.628	-0.140	-0.140	0.000	0.000	0.000	0.000
202	A	1152	LEU	0	-0.032	-0.016	11.619	0.300	0.300	0.000	0.000	0.000	0.000
203	A	1153	ILE	0	0.027	0.012	10.642	-0.181	-0.181	0.000	0.000	0.000	0.000
204	A	1154	THR	0	-0.020	-0.015	12.069	0.164	0.164	0.000	0.000	0.000	0.000
205	A	1155	TYR	0	-0.011	-0.030	9.212	0.124	0.124	0.000	0.000	0.000	0.000
206	A	1156	GLN	0	0.027	0.019	14.816	0.004	0.004	0.000	0.000	0.000	0.000
207	A	1157	ILE	0	-0.016	0.005	12.892	0.075	0.075	0.000	0.000	0.000	0.000
208	A	1158	MET	0	0.003	-0.004	15.621	-0.131	-0.131	0.000	0.000	0.000	0.000
209	A	1159	ARG	1	0.928	0.957	18.582	-0.622	-0.622	0.000	0.000	0.000	0.000
210	A	1160	PRO	0	-0.060	-0.029	19.167	-0.020	-0.020	0.000	0.000	0.000	0.000
211	A	1161	GLU	-2	-1.784	-1.869	21.735	1.200	1.200	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #212(A:1163:9SU )