FMO DATABASE

FMODB ID: GQZG1

Calculation Name: 1BVE-AB-NMR60-Model13

Preferred Name: Gag-Pol polyprotein

Target Type: SINGLE PROTEIN

Ligand Name: [4-r-(-4-alpha,5-alpha,6-beta,7-beta)]-hexahydro-5,6-bis(hydroxy)-[1,3-bis([4-hydroxymethyl-phenyl]methyl)-4,7-bis(phen ylmethyl)]-2h-1,3-diazepinone

ligand 3-letter code: DMP

PDB ID: 1BVE

Chain ID: AB

ChEMBL ID: CHEMBL3638360

UniProt ID: P04585

Base Structure: NMR

Registration Date: 2019-08-16

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	199
LigandResidueName	DMP
LigandFragmentNumber	199
LigandCharge
Software	MIZUHO/ABINIT-MP 4.0(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2298763.328919
FMO2-HF: Nuclear repulsion	2222286.217456
FMO2-HF: Total energy	-76477.111463
FMO2-MP2: Total energy	-76702.933907

3D Structure

Snapshot

Ligand structure

DMP

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.
-156.496	-208.322	258.727	-66.207	-140.698	0.041

Interactive mode: IFIE and PIEDA for fragment #199(B:100:DMP )

Summations of interaction energy for fragment #199(B:100:DMP )

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.
-156.496	-208.322	258.727	-66.207	-140.698	-0.041

Interaction energy analysis for fragmet #199(B:100:DMP )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.043 / q_NPA : -0.082

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	1	PRO	1	0.826	0.902	17.734	1.398	1.398	0.000	0.000	0.000	0.000
2	A	2	GLN	0	0.061	0.058	17.580	-0.121	-0.121	0.000	0.000	0.000	0.000
3	A	3	VAL	0	0.006	0.012	12.778	0.049	0.049	0.000	0.000	0.000	0.000
4	A	4	THR	0	0.054	0.019	13.995	-0.254	-0.254	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.012	-0.026	12.868	-0.184	-0.184	0.000	0.000	0.000	0.000
6	A	6	TRP	0	0.042	0.034	11.878	-0.022	-0.022	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.029	0.015	8.742	0.182	0.182	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.962	0.997	5.588	1.886	1.886	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.016	0.013	7.451	0.714	0.714	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.036	-0.017	6.687	-0.321	-0.321	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.009	-0.004	10.519	0.301	0.301	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.016	-0.001	12.918	-0.042	-0.042	0.000	0.000	0.000	0.000
13	A	13	ILE	0	0.009	-0.005	11.698	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.967	0.974	15.568	0.615	0.615	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.058	0.024	11.626	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.016	0.002	15.929	0.076	0.076	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.062	-0.019	17.982	0.051	0.051	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.024	0.001	16.553	0.029	0.029	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.032	-0.017	16.746	-0.080	-0.080	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.877	0.963	11.612	0.388	0.388	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.881	-0.945	9.308	-0.885	-0.885	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.022	-0.018	9.059	0.055	0.055	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.047	-0.008	3.080	-1.245	0.443	0.274	-0.480	-1.482	0.003
24	A	24	LEU	0	-0.027	-0.028	5.822	-1.729	-1.729	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.689	-0.831	1.869	-45.590	-64.833	41.036	-11.178	-10.616	-0.102
26	A	26	THR	0	-0.069	-0.068	4.462	0.161	0.411	-0.001	-0.042	-0.207	0.000
27	A	27	GLY	0	0.036	0.025	2.630	1.846	2.968	0.444	-0.656	-0.911	0.003
28	A	28	ALA	0	-0.097	-0.031	2.091	3.379	0.665	13.255	-3.793	-6.748	-0.002
29	A	29	ASP	-1	-0.821	-0.935	2.054	1.914	0.953	2.402	0.688	-2.129	0.005
30	A	30	ASP	-1	-0.901	-0.990	3.000	-0.835	0.542	0.121	-0.532	-0.966	0.005
31	A	31	THR	0	-0.049	-0.017	3.972	-3.203	-2.848	0.003	-0.108	-0.250	-0.001
32	A	32	VAL	0	-0.026	-0.004	2.719	-0.366	1.488	0.357	-0.475	-1.736	0.001
33	A	33	LEU	0	0.023	-0.001	4.509	-0.702	-0.572	0.000	-0.017	-0.113	0.000
34	A	34	GLU	-1	-0.871	-0.934	7.342	0.327	0.327	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.965	-1.016	8.431	0.676	0.676	0.000	0.000	0.000	0.000
36	A	36	MET	0	-0.018	-0.004	11.944	-0.084	-0.084	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.034	-0.015	14.746	0.077	0.077	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.029	0.005	12.477	-0.099	-0.099	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.007	0.015	15.869	0.071	0.071	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.043	0.011	17.674	-0.052	-0.052	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.912	0.946	16.747	-0.207	-0.207	0.000	0.000	0.000	0.000
42	A	42	TRP	0	0.064	0.042	12.777	0.016	0.016	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.950	0.972	11.066	-0.742	-0.742	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.003	0.010	10.435	0.109	0.109	0.000	0.000	0.000	0.000
45	A	45	LYS	1	1.003	1.001	3.147	-6.194	-5.753	0.010	-0.107	-0.344	0.001
46	A	46	MET	0	-0.055	0.012	7.728	-0.017	-0.017	0.000	0.000	0.000	0.000
47	A	47	ILE	0	-0.020	0.001	2.115	-3.953	-1.691	3.905	-1.444	-4.722	0.014
48	A	48	GLY	0	0.078	-0.023	3.819	-0.245	0.327	0.004	-0.119	-0.458	0.000
49	A	49	GLY	0	-0.024	-0.023	1.975	-5.262	-5.869	13.966	-7.134	-6.224	0.016
50	A	50	ILE	0	0.012	0.010	1.999	-2.868	-21.747	37.024	2.052	-20.197	0.036
51	A	51	GLY	0	-0.018	-0.014	4.007	-0.037	0.661	0.011	-0.175	-0.534	0.001
52	A	52	GLY	0	0.015	0.001	5.967	-2.228	-2.228	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.009	0.047	5.667	1.899	1.899	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.010	0.028	5.656	-0.646	-0.646	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.960	0.941	7.417	-2.198	-2.198	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.004	0.005	4.744	-0.215	-0.104	-0.001	-0.003	-0.107	0.000
57	A	57	ARG	1	0.867	0.947	8.168	-0.783	-0.783	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.024	-0.007	7.753	0.406	0.406	0.000	0.000	0.000	0.000
59	A	59	TYR	0	0.000	0.009	9.258	0.042	0.042	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.854	-0.943	11.577	0.274	0.274	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.060	-0.036	13.338	-0.073	-0.073	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.019	0.007	12.905	0.032	0.032	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.059	-0.030	14.819	-0.117	-0.117	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.036	0.009	11.476	0.049	0.049	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.985	-0.993	15.309	-0.769	-0.769	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.044	0.028	12.881	-0.041	-0.041	0.000	0.000	0.000	0.000
67	A	67	CYS	0	-0.042	-0.031	16.581	0.018	0.018	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.033	0.028	18.624	0.078	0.078	0.000	0.000	0.000	0.000
69	A	69	HIS	0	-0.027	-0.008	19.652	0.069	0.069	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.925	0.946	19.029	0.485	0.485	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.052	0.029	15.286	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.037	0.000	15.228	-0.026	-0.026	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.076	0.033	12.112	-0.070	-0.070	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.048	-0.018	8.800	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.040	0.077	7.959	-0.141	-0.141	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.013	-0.014	3.800	0.352	0.616	0.003	-0.034	-0.233	0.000
77	A	77	VAL	0	-0.071	-0.003	7.595	-0.197	-0.197	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.024	-0.022	9.122	0.220	0.220	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.015	0.022	8.808	-0.314	-0.314	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.035	-0.016	3.678	0.515	1.148	0.009	-0.181	-0.461	-0.001
81	A	81	PRO	0	0.023	0.016	2.056	-1.355	-1.063	2.296	-0.498	-2.090	0.000
82	A	82	VAL	0	0.036	0.006	2.640	-3.306	-0.880	1.736	-0.923	-3.240	0.006
83	A	83	ASN	0	-0.037	0.004	4.493	-0.274	-0.077	0.000	-0.015	-0.182	0.000
84	A	84	ILE	0	0.011	-0.012	1.949	-1.047	-2.951	10.724	-1.927	-6.894	0.001
85	A	85	ILE	0	0.007	0.006	5.375	0.733	0.914	-0.001	-0.005	-0.175	0.000
86	A	86	GLY	0	0.108	0.041	5.155	-1.358	-1.358	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.924	0.949	6.016	4.243	4.243	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.027	0.009	6.797	-0.121	-0.121	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.008	0.005	8.854	0.232	0.232	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.052	0.005	7.700	0.308	0.308	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.005	-0.024	11.738	0.234	0.234	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.097	-0.034	13.455	0.301	0.301	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.055	-0.015	13.966	0.118	0.118	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.015	0.013	17.214	0.041	0.041	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.013	-0.009	13.133	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.034	-0.041	14.982	0.066	0.066	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.062	-0.017	9.496	-0.038	-0.038	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.010	-0.023	13.878	0.076	0.076	0.000	0.000	0.000	0.000
99	A	99	PHE	-1	-0.820	-0.897	12.361	-1.452	-1.452	0.000	0.000	0.000	0.000
100	B	1	PRO	1	0.812	0.895	17.540	1.358	1.358	0.000	0.000	0.000	0.000
101	B	2	GLN	0	0.062	0.055	17.560	-0.147	-0.147	0.000	0.000	0.000	0.000
102	B	3	VAL	0	0.008	0.016	13.482	0.092	0.092	0.000	0.000	0.000	0.000
103	B	4	THR	0	0.089	0.014	15.266	-0.252	-0.252	0.000	0.000	0.000	0.000
104	B	5	LEU	0	-0.048	-0.012	15.213	0.130	0.130	0.000	0.000	0.000	0.000
105	B	6	TRP	0	0.023	0.003	12.269	-0.023	-0.023	0.000	0.000	0.000	0.000
106	B	7	GLN	0	-0.005	0.005	10.354	0.190	0.190	0.000	0.000	0.000	0.000
107	B	8	ARG	1	0.949	0.967	6.912	-0.028	-0.028	0.000	0.000	0.000	0.000
108	B	9	PRO	0	-0.036	0.008	8.013	0.576	0.576	0.000	0.000	0.000	0.000
109	B	10	LEU	0	0.009	0.001	7.588	-0.415	-0.415	0.000	0.000	0.000	0.000
110	B	11	VAL	0	-0.015	-0.008	10.977	0.279	0.279	0.000	0.000	0.000	0.000
111	B	12	THR	0	-0.018	-0.029	12.790	-0.029	-0.029	0.000	0.000	0.000	0.000
112	B	13	ILE	0	-0.002	0.026	11.851	0.028	0.028	0.000	0.000	0.000	0.000
113	B	14	LYS	1	0.925	0.950	14.980	0.627	0.627	0.000	0.000	0.000	0.000
114	B	15	ILE	0	0.052	0.037	11.160	-0.009	-0.009	0.000	0.000	0.000	0.000
115	B	16	GLY	0	0.005	-0.003	15.581	0.081	0.081	0.000	0.000	0.000	0.000
116	B	17	GLY	0	-0.038	-0.012	18.314	0.049	0.049	0.000	0.000	0.000	0.000
117	B	18	GLN	0	0.029	0.006	15.851	0.029	0.029	0.000	0.000	0.000	0.000
118	B	19	LEU	0	-0.022	-0.018	16.559	-0.076	-0.076	0.000	0.000	0.000	0.000
119	B	20	LYS	1	0.888	0.968	11.122	0.212	0.212	0.000	0.000	0.000	0.000
120	B	21	GLU	-1	-0.930	-0.953	8.359	-0.828	-0.828	0.000	0.000	0.000	0.000
121	B	22	ALA	0	0.062	-0.020	8.869	0.061	0.061	0.000	0.000	0.000	0.000
122	B	23	LEU	0	-0.054	0.001	3.154	-1.248	0.378	0.261	-0.395	-1.493	0.002
123	B	24	LEU	0	-0.024	-0.034	5.623	-1.528	-1.528	0.000	0.000	0.000	0.000
124	B	25	ASP	-1	-0.668	-0.818	1.557	-57.374	-77.899	48.179	-17.026	-10.628	-0.111
125	B	26	THR	0	-0.108	-0.060	4.070	0.384	0.854	0.000	-0.177	-0.294	-0.001
126	B	27	GLY	0	0.074	0.038	2.488	1.723	3.332	0.788	-1.104	-1.293	0.003
127	B	28	ALA	0	-0.039	0.003	2.021	6.954	0.548	19.766	-5.234	-8.125	-0.004
128	B	29	ASP	-1	-0.892	-0.976	2.136	-9.514	-8.038	4.679	-2.148	-4.007	0.003
129	B	30	ASP	-1	-0.952	-0.992	2.687	-3.702	-1.994	0.329	-0.720	-1.316	0.009
130	B	31	THR	0	-0.047	-0.025	3.734	-2.894	-2.371	0.008	-0.193	-0.339	-0.001
131	B	32	VAL	0	-0.037	0.001	3.015	-0.310	1.206	0.158	-0.329	-1.345	0.001
132	B	33	LEU	0	-0.012	-0.022	4.587	-0.477	-0.374	0.000	-0.013	-0.089	0.000
133	B	34	GLU	-1	-0.923	-0.970	7.258	1.109	1.109	0.000	0.000	0.000	0.000
134	B	35	GLU	-1	-0.971	-0.975	8.092	0.446	0.446	0.000	0.000	0.000	0.000
135	B	36	MET	0	-0.029	-0.015	11.329	-0.114	-0.114	0.000	0.000	0.000	0.000
136	B	37	SER	0	-0.020	-0.005	14.449	0.067	0.067	0.000	0.000	0.000	0.000
137	B	38	LEU	0	0.035	0.003	12.541	-0.070	-0.070	0.000	0.000	0.000	0.000
138	B	39	PRO	0	0.003	0.003	16.691	0.049	0.049	0.000	0.000	0.000	0.000
139	B	40	GLY	0	-0.040	-0.028	18.275	-0.002	-0.002	0.000	0.000	0.000	0.000
140	B	41	ARG	1	0.942	0.962	17.426	-0.039	-0.039	0.000	0.000	0.000	0.000
141	B	42	TRP	0	0.039	0.040	12.680	0.007	0.007	0.000	0.000	0.000	0.000
142	B	43	LYS	1	0.946	0.971	12.202	-0.094	-0.094	0.000	0.000	0.000	0.000
143	B	44	PRO	0	0.009	0.008	11.102	0.047	0.047	0.000	0.000	0.000	0.000
144	B	45	LYS	1	0.955	0.984	3.732	-1.436	-1.164	0.004	-0.047	-0.230	0.000
145	B	46	MET	0	-0.062	-0.013	7.301	0.085	0.085	0.000	0.000	0.000	0.000
146	B	47	ILE	0	-0.029	0.003	2.307	-4.546	-2.334	3.717	-1.299	-4.629	0.017
147	B	48	GLY	0	0.063	0.011	4.209	0.408	0.810	0.001	-0.070	-0.333	0.000
148	B	49	GLY	0	-0.003	0.007	2.073	-4.528	-3.093	5.907	-3.654	-3.689	0.020
149	B	50	ILE	0	-0.011	-0.007	1.953	-8.481	-18.748	30.648	-2.792	-17.589	0.034
150	B	51	GLY	0	0.012	-0.010	3.958	0.360	1.065	0.008	-0.137	-0.576	0.001
151	B	52	GLY	0	0.002	0.000	6.015	-2.224	-2.224	0.000	0.000	0.000	0.000
152	B	53	PHE	0	-0.009	-0.009	5.998	1.542	1.542	0.000	0.000	0.000	0.000
153	B	54	ILE	0	-0.006	0.031	5.585	-0.413	-0.413	0.000	0.000	0.000	0.000
154	B	55	LYS	1	0.924	0.947	7.363	-1.341	-1.341	0.000	0.000	0.000	0.000
155	B	56	VAL	0	0.041	0.036	4.999	-0.010	-0.010	0.000	0.000	0.000	0.000
156	B	57	ARG	1	0.911	0.953	8.266	-0.633	-0.633	0.000	0.000	0.000	0.000
157	B	58	GLN	0	0.042	0.007	7.053	0.113	0.113	0.000	0.000	0.000	0.000
158	B	59	TYR	0	0.025	0.013	9.023	0.022	0.022	0.000	0.000	0.000	0.000
159	B	60	ASP	-1	-0.872	-0.943	11.382	-0.127	-0.127	0.000	0.000	0.000	0.000
160	B	61	GLN	0	-0.045	-0.027	13.171	-0.025	-0.025	0.000	0.000	0.000	0.000
161	B	62	ILE	0	-0.019	-0.009	12.482	0.049	0.049	0.000	0.000	0.000	0.000
162	B	63	LEU	0	-0.053	-0.049	14.456	-0.097	-0.097	0.000	0.000	0.000	0.000
163	B	64	ILE	0	0.047	0.021	11.131	0.062	0.062	0.000	0.000	0.000	0.000
164	B	65	GLU	-1	-0.963	-0.978	14.983	-0.776	-0.776	0.000	0.000	0.000	0.000
165	B	66	ILE	0	0.071	0.028	12.700	-0.046	-0.046	0.000	0.000	0.000	0.000
166	B	67	CYS	0	-0.049	-0.023	16.529	0.024	0.024	0.000	0.000	0.000	0.000
167	B	68	GLY	0	0.045	0.026	18.497	0.041	0.041	0.000	0.000	0.000	0.000
168	B	69	HIS	0	0.002	0.000	19.780	0.071	0.071	0.000	0.000	0.000	0.000
169	B	70	LYS	1	0.876	0.929	18.979	0.535	0.535	0.000	0.000	0.000	0.000
170	B	71	ALA	0	0.059	0.036	14.847	-0.027	-0.027	0.000	0.000	0.000	0.000
171	B	72	ILE	0	-0.015	0.015	14.973	0.001	0.001	0.000	0.000	0.000	0.000
172	B	73	GLY	0	0.011	0.003	11.630	-0.101	-0.101	0.000	0.000	0.000	0.000
173	B	74	THR	0	-0.007	-0.017	8.247	0.022	0.022	0.000	0.000	0.000	0.000
174	B	75	VAL	0	0.009	0.018	7.667	-0.119	-0.119	0.000	0.000	0.000	0.000
175	B	76	LEU	0	-0.004	-0.014	3.675	0.015	0.380	0.008	-0.060	-0.313	0.000
176	B	77	VAL	0	0.009	0.014	7.166	-0.134	-0.134	0.000	0.000	0.000	0.000
177	B	78	GLY	0	0.028	-0.018	8.688	0.173	0.173	0.000	0.000	0.000	0.000
178	B	79	PRO	0	-0.034	0.014	8.484	-0.244	-0.244	0.000	0.000	0.000	0.000
179	B	80	THR	0	-0.067	-0.019	3.552	-0.192	0.737	0.026	-0.349	-0.605	-0.002
180	B	81	PRO	0	0.090	0.042	2.068	-1.164	-1.273	3.263	-0.661	-2.494	-0.001
181	B	82	VAL	0	0.044	0.002	2.616	-2.710	-0.600	1.509	-0.744	-2.875	0.005
182	B	83	ASN	0	-0.037	0.001	4.542	-0.352	-0.173	0.000	-0.010	-0.169	0.000
183	B	84	ILE	0	0.024	0.007	1.999	-0.610	-3.490	11.892	-1.932	-7.080	-0.002
184	B	85	ILE	0	0.015	0.030	5.385	0.534	0.710	-0.001	-0.007	-0.168	0.000
185	B	86	GLY	0	0.112	0.026	4.927	-1.449	-1.449	0.000	0.000	0.000	0.000
186	B	87	ARG	1	0.830	0.884	5.781	3.793	3.793	0.000	0.000	0.000	0.000
187	B	88	ASN	0	0.028	0.053	6.614	-0.190	-0.190	0.000	0.000	0.000	0.000
188	B	89	LEU	0	-0.001	-0.018	8.393	0.202	0.202	0.000	0.000	0.000	0.000
189	B	90	LEU	0	-0.056	-0.014	7.521	0.065	0.065	0.000	0.000	0.000	0.000
190	B	91	THR	0	0.008	-0.002	11.542	0.105	0.105	0.000	0.000	0.000	0.000
191	B	92	GLN	0	-0.030	0.002	11.450	0.166	0.166	0.000	0.000	0.000	0.000
192	B	93	ILE	0	-0.061	-0.011	13.595	0.110	0.110	0.000	0.000	0.000	0.000
193	B	94	GLY	0	0.031	0.019	16.661	0.043	0.043	0.000	0.000	0.000	0.000
194	B	95	ALA	0	-0.002	-0.008	12.664	0.004	0.004	0.000	0.000	0.000	0.000
195	B	96	THR	0	-0.091	-0.057	14.411	0.040	0.040	0.000	0.000	0.000	0.000
196	B	97	LEU	0	-0.025	-0.005	9.255	0.010	0.010	0.000	0.000	0.000	0.000
197	B	98	ASN	0	-0.018	-0.024	13.702	0.057	0.057	0.000	0.000	0.000	0.000
198	B	99	PHE	-1	-0.806	-0.900	12.540	-1.445	-1.445	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #199(B:100:DMP )