FMO DATABASE

FMODB ID: NNJVQ

Calculation Name: 2VPI-A-Xray372

Preferred Name: GMP synthase [glutamine-hydrolyzing]

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2VPI

Chain ID: A

ChEMBL ID: CHEMBL5721

UniProt ID: P49915

Base Structure: X-ray

Registration Date: 2023-09-23

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	187
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1990781.030577
FMO2-HF: Nuclear repulsion	1919499.613548
FMO2-HF: Total energy	-71281.417029
FMO2-MP2: Total energy	-71488.880097

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:MET)

Summations of interaction energy for fragment #1(A:24: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.
-2.178	2.703	8.256	-6.182	-6.951	-0.024

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : 0.012

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	GLY	0	-0.099	-0.052	3.770	-0.771	0.988	-0.015	-0.883	-0.860	0.005
4	A	27	ALA	0	0.007	0.026	2.919	0.773	1.308	0.067	-0.195	-0.406	0.000
5	A	28	VAL	0	-0.039	-0.038	4.916	0.158	0.196	-0.001	-0.007	-0.031	0.000
6	A	29	VAL	0	0.024	0.028	5.858	0.132	0.132	0.000	0.000	0.000	0.000
7	A	30	ILE	0	-0.047	-0.025	7.502	0.102	0.102	0.000	0.000	0.000	0.000
8	A	31	LEU	0	-0.001	0.004	10.578	0.139	0.139	0.000	0.000	0.000	0.000
9	A	32	ASP	-1	-0.805	-0.923	13.411	-0.138	-0.138	0.000	0.000	0.000	0.000
10	A	33	ALA	0	-0.022	-0.013	16.761	0.046	0.046	0.000	0.000	0.000	0.000
11	A	34	GLY	0	-0.001	0.007	19.967	0.014	0.014	0.000	0.000	0.000	0.000
12	A	35	ALA	0	0.018	-0.008	21.385	0.014	0.014	0.000	0.000	0.000	0.000
13	A	36	GLN	0	-0.024	-0.020	20.490	0.014	0.014	0.000	0.000	0.000	0.000
14	A	37	TYR	0	-0.022	0.002	17.755	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	38	GLY	0	0.074	0.025	14.932	0.022	0.022	0.000	0.000	0.000	0.000
16	A	39	LYS	1	0.960	0.973	15.336	-0.114	-0.114	0.000	0.000	0.000	0.000
17	A	40	VAL	0	-0.022	-0.008	17.167	-0.027	-0.027	0.000	0.000	0.000	0.000
18	A	41	ILE	0	0.048	0.010	14.160	-0.022	-0.022	0.000	0.000	0.000	0.000
19	A	42	ASP	-1	-0.781	-0.869	11.343	-0.394	-0.394	0.000	0.000	0.000	0.000
20	A	43	ARG	1	0.924	0.971	13.860	0.121	0.121	0.000	0.000	0.000	0.000
21	A	44	ARG	1	0.749	0.874	16.566	0.220	0.220	0.000	0.000	0.000	0.000
22	A	45	VAL	0	0.045	0.012	10.504	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	46	ARG	1	0.960	0.977	11.023	0.197	0.197	0.000	0.000	0.000	0.000
24	A	47	GLU	-1	-0.877	-0.945	13.828	-0.276	-0.276	0.000	0.000	0.000	0.000
25	A	48	LEU	0	-0.064	-0.021	15.324	0.039	0.039	0.000	0.000	0.000	0.000
26	A	49	PHE	0	-0.018	0.004	14.032	-0.035	-0.035	0.000	0.000	0.000	0.000
27	A	50	VAL	0	0.006	0.013	9.133	-0.083	-0.083	0.000	0.000	0.000	0.000
28	A	51	GLN	0	-0.033	-0.018	3.465	-1.206	-0.915	0.004	-0.100	-0.195	0.000
29	A	52	SER	0	-0.056	-0.066	6.886	-0.482	-0.482	0.000	0.000	0.000	0.000
30	A	53	GLU	-1	-0.859	-0.919	4.261	0.641	0.785	-0.001	-0.011	-0.132	0.000
31	A	54	ILE	0	-0.050	-0.020	7.231	-0.159	-0.159	0.000	0.000	0.000	0.000
32	A	55	PHE	0	-0.021	-0.014	5.770	0.129	0.129	0.000	0.000	0.000	0.000
33	A	56	PRO	0	0.038	0.025	10.617	-0.128	-0.128	0.000	0.000	0.000	0.000
34	A	57	LEU	0	0.015	0.032	13.186	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	58	GLU	-1	-0.933	-0.976	15.444	0.269	0.269	0.000	0.000	0.000	0.000
36	A	59	THR	0	-0.061	-0.056	9.417	0.105	0.105	0.000	0.000	0.000	0.000
37	A	60	PRO	0	-0.015	-0.003	12.267	-0.108	-0.108	0.000	0.000	0.000	0.000
38	A	61	ALA	0	0.008	-0.022	11.338	0.062	0.062	0.000	0.000	0.000	0.000
39	A	62	PHE	0	-0.031	-0.023	10.902	-0.097	-0.097	0.000	0.000	0.000	0.000
40	A	63	ALA	0	0.061	0.039	9.443	0.047	0.047	0.000	0.000	0.000	0.000
41	A	64	ILE	0	0.043	0.019	6.438	0.416	0.416	0.000	0.000	0.000	0.000
42	A	65	LYS	1	0.890	0.929	6.147	-0.381	-0.381	0.000	0.000	0.000	0.000
43	A	66	GLU	-1	-0.954	-0.986	7.255	0.884	0.884	0.000	0.000	0.000	0.000
44	A	67	GLN	0	-0.002	0.003	3.030	-2.413	-1.216	0.074	-0.396	-0.874	0.001
45	A	68	GLY	0	0.011	0.019	2.080	-0.645	-1.017	7.952	-4.166	-3.413	-0.027
46	A	69	PHE	0	-0.012	0.013	3.411	-3.645	-2.473	0.177	-0.413	-0.936	-0.003
47	A	70	ARG	1	0.913	0.959	4.456	2.971	3.088	-0.001	-0.011	-0.104	0.000
48	A	71	ALA	0	-0.025	-0.021	7.647	0.561	0.561	0.000	0.000	0.000	0.000
49	A	72	ILE	0	0.010	0.013	8.256	-0.238	-0.238	0.000	0.000	0.000	0.000
50	A	73	ILE	0	-0.004	0.005	10.759	0.078	0.078	0.000	0.000	0.000	0.000
51	A	74	ILE	0	0.010	0.018	13.266	0.049	0.049	0.000	0.000	0.000	0.000
52	A	75	SER	0	0.019	0.003	15.677	0.000	0.000	0.000	0.000	0.000	0.000
53	A	76	GLY	0	0.029	0.024	18.715	0.028	0.028	0.000	0.000	0.000	0.000
54	A	86	ALA	0	-0.003	-0.004	26.406	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	87	PRO	0	-0.022	-0.020	21.554	0.014	0.014	0.000	0.000	0.000	0.000
56	A	88	TRP	0	0.006	0.006	17.869	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	89	PHE	0	0.028	0.009	17.110	0.011	0.011	0.000	0.000	0.000	0.000
58	A	90	ASP	-1	-0.729	-0.864	15.303	0.130	0.130	0.000	0.000	0.000	0.000
59	A	91	PRO	0	0.009	-0.004	16.849	-0.050	-0.050	0.000	0.000	0.000	0.000
60	A	92	ALA	0	0.023	0.008	16.457	-0.043	-0.043	0.000	0.000	0.000	0.000
61	A	93	ILE	0	-0.010	-0.011	12.771	-0.047	-0.047	0.000	0.000	0.000	0.000
62	A	94	PHE	0	-0.019	-0.006	14.280	-0.091	-0.091	0.000	0.000	0.000	0.000
63	A	95	THR	0	-0.029	-0.027	16.830	-0.019	-0.019	0.000	0.000	0.000	0.000
64	A	96	ILE	0	-0.042	-0.008	10.956	0.000	0.000	0.000	0.000	0.000	0.000
65	A	97	GLY	0	-0.007	-0.004	14.148	-0.046	-0.046	0.000	0.000	0.000	0.000
66	A	98	LYS	1	0.883	0.964	7.755	1.267	1.267	0.000	0.000	0.000	0.000
67	A	99	PRO	0	0.029	0.017	11.764	0.108	0.108	0.000	0.000	0.000	0.000
68	A	100	VAL	0	-0.001	-0.002	12.708	-0.086	-0.086	0.000	0.000	0.000	0.000
69	A	101	LEU	0	-0.010	0.006	14.832	0.057	0.057	0.000	0.000	0.000	0.000
70	A	102	GLY	0	0.009	-0.006	16.422	0.004	0.004	0.000	0.000	0.000	0.000
71	A	103	ILE	0	-0.005	-0.018	18.308	0.009	0.009	0.000	0.000	0.000	0.000
72	A	104	CYS	0	0.010	-0.004	20.875	0.029	0.029	0.000	0.000	0.000	0.000
73	A	105	TYR	0	0.006	0.005	20.674	0.003	0.003	0.000	0.000	0.000	0.000
74	A	106	GLY	0	0.025	0.010	19.694	0.012	0.012	0.000	0.000	0.000	0.000
75	A	107	MET	0	-0.033	0.009	20.506	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	108	GLN	0	-0.022	-0.019	22.847	0.003	0.003	0.000	0.000	0.000	0.000
77	A	109	MET	0	-0.046	-0.014	21.168	0.013	0.013	0.000	0.000	0.000	0.000
78	A	110	MET	0	-0.005	0.017	18.597	0.015	0.015	0.000	0.000	0.000	0.000
79	A	111	ASN	0	0.019	0.009	21.925	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	112	LYS	1	0.942	0.990	25.223	0.036	0.036	0.000	0.000	0.000	0.000
81	A	113	VAL	0	-0.051	-0.023	20.956	0.014	0.014	0.000	0.000	0.000	0.000
82	A	114	PHE	0	-0.047	-0.028	20.503	0.002	0.002	0.000	0.000	0.000	0.000
83	A	115	GLY	0	0.024	0.020	25.888	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	116	GLY	0	0.007	0.014	28.442	0.005	0.005	0.000	0.000	0.000	0.000
85	A	117	THR	0	-0.050	-0.036	30.064	0.007	0.007	0.000	0.000	0.000	0.000
86	A	118	VAL	0	-0.021	-0.024	28.721	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	119	HIS	0	0.019	0.024	32.057	0.007	0.007	0.000	0.000	0.000	0.000
88	A	120	LYS	1	0.855	0.915	30.285	0.025	0.025	0.000	0.000	0.000	0.000
89	A	121	LYS	1	0.938	0.951	34.103	0.015	0.015	0.000	0.000	0.000	0.000
90	A	122	SER	0	0.041	0.042	34.312	0.002	0.002	0.000	0.000	0.000	0.000
91	A	123	VAL	0	-0.042	-0.004	32.694	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	124	ARG	1	0.982	0.967	35.320	0.046	0.046	0.000	0.000	0.000	0.000
93	A	125	GLU	-1	-0.937	-0.962	37.033	-0.040	-0.040	0.000	0.000	0.000	0.000
94	A	126	ASP	-1	-0.841	-0.896	32.685	-0.066	-0.066	0.000	0.000	0.000	0.000
95	A	127	GLY	0	0.006	-0.003	33.666	0.005	0.005	0.000	0.000	0.000	0.000
96	A	128	VAL	0	-0.022	-0.011	32.571	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	129	PHE	0	0.001	0.004	33.754	0.007	0.007	0.000	0.000	0.000	0.000
98	A	130	ASN	0	0.026	0.015	34.040	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	131	ILE	0	-0.087	-0.035	30.343	0.007	0.007	0.000	0.000	0.000	0.000
100	A	132	SER	0	-0.004	-0.013	34.955	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	133	VAL	0	-0.004	-0.021	29.999	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	134	ASP	-1	-0.867	-0.941	30.508	-0.186	-0.186	0.000	0.000	0.000	0.000
103	A	135	ASN	0	0.026	-0.022	29.875	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	136	THR	0	-0.149	-0.056	30.252	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	137	CYS	0	-0.054	0.007	25.776	-0.016	-0.016	0.000	0.000	0.000	0.000
106	A	138	SER	0	-0.006	-0.027	22.408	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	139	LEU	0	-0.020	-0.016	20.246	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	140	PHE	0	-0.030	-0.019	23.200	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	141	ARG	1	1.034	1.028	25.184	0.355	0.355	0.000	0.000	0.000	0.000
110	A	142	GLY	0	-0.031	-0.020	26.452	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	143	LEU	0	-0.055	0.001	26.718	0.007	0.007	0.000	0.000	0.000	0.000
112	A	144	GLN	0	0.017	0.010	30.310	0.013	0.013	0.000	0.000	0.000	0.000
113	A	145	LYS	1	0.949	0.959	33.063	0.133	0.133	0.000	0.000	0.000	0.000
114	A	146	GLU	-1	-0.956	-0.971	35.450	-0.108	-0.108	0.000	0.000	0.000	0.000
115	A	147	GLU	-1	-0.776	-0.878	30.436	-0.192	-0.192	0.000	0.000	0.000	0.000
116	A	148	VAL	0	0.059	0.045	32.779	0.008	0.008	0.000	0.000	0.000	0.000
117	A	149	VAL	0	-0.019	-0.019	28.853	-0.012	-0.012	0.000	0.000	0.000	0.000
118	A	150	LEU	0	0.006	0.005	27.505	0.013	0.013	0.000	0.000	0.000	0.000
119	A	151	LEU	0	-0.023	-0.022	28.606	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	152	THR	0	0.011	0.003	28.092	0.002	0.002	0.000	0.000	0.000	0.000
121	A	153	HIS	0	-0.074	-0.056	30.551	0.003	0.003	0.000	0.000	0.000	0.000
122	A	154	GLY	0	-0.010	-0.015	31.106	0.002	0.002	0.000	0.000	0.000	0.000
123	A	155	ASP	-1	-0.854	-0.922	29.885	-0.040	-0.040	0.000	0.000	0.000	0.000
124	A	156	SER	0	-0.044	-0.025	30.366	-0.010	-0.010	0.000	0.000	0.000	0.000
125	A	157	VAL	0	0.010	-0.003	28.246	0.008	0.008	0.000	0.000	0.000	0.000
126	A	158	ASP	-1	-0.957	-0.961	31.114	-0.061	-0.061	0.000	0.000	0.000	0.000
127	A	159	LYS	1	0.952	0.970	34.185	0.050	0.050	0.000	0.000	0.000	0.000
128	A	160	VAL	0	-0.017	-0.015	29.418	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	161	ALA	0	0.018	0.011	27.458	0.004	0.004	0.000	0.000	0.000	0.000
130	A	162	ASP	-1	-0.846	-0.924	29.552	-0.109	-0.109	0.000	0.000	0.000	0.000
131	A	163	GLY	0	-0.075	-0.043	27.954	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	164	PHE	0	-0.060	-0.028	22.486	-0.023	-0.023	0.000	0.000	0.000	0.000
133	A	165	LYS	1	0.980	0.991	27.983	0.175	0.175	0.000	0.000	0.000	0.000
134	A	166	VAL	0	-0.037	-0.021	28.779	-0.009	-0.009	0.000	0.000	0.000	0.000
135	A	167	VAL	0	-0.017	-0.009	26.558	0.003	0.003	0.000	0.000	0.000	0.000
136	A	168	ALA	0	0.054	0.028	29.566	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	169	ARG	1	0.913	0.964	31.233	0.118	0.118	0.000	0.000	0.000	0.000
138	A	170	SER	0	0.086	0.053	34.012	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	171	GLY	0	0.021	0.017	36.898	0.005	0.005	0.000	0.000	0.000	0.000
140	A	172	ASN	0	-0.042	-0.038	38.583	-0.002	-0.002	0.000	0.000	0.000	0.000
141	A	173	ILE	0	0.013	0.023	33.244	0.000	0.000	0.000	0.000	0.000	0.000
142	A	174	VAL	0	0.003	0.007	30.002	-0.007	-0.007	0.000	0.000	0.000	0.000
143	A	175	ALA	0	0.026	-0.003	29.862	0.002	0.002	0.000	0.000	0.000	0.000
144	A	176	GLY	0	0.038	0.007	26.641	-0.014	-0.014	0.000	0.000	0.000	0.000
145	A	177	ILE	0	-0.053	-0.019	24.538	0.016	0.016	0.000	0.000	0.000	0.000
146	A	178	ALA	0	0.065	0.027	23.883	-0.026	-0.026	0.000	0.000	0.000	0.000
147	A	179	ASN	0	0.028	0.026	22.791	0.014	0.014	0.000	0.000	0.000	0.000
148	A	180	GLU	-1	-0.711	-0.863	22.362	-0.353	-0.353	0.000	0.000	0.000	0.000
149	A	181	SER	0	-0.055	-0.014	22.256	-0.028	-0.028	0.000	0.000	0.000	0.000
150	A	182	LYS	1	0.925	0.962	20.111	0.190	0.190	0.000	0.000	0.000	0.000
151	A	183	LYS	1	0.911	0.978	16.917	0.578	0.578	0.000	0.000	0.000	0.000
152	A	184	LEU	0	-0.009	0.008	17.246	-0.042	-0.042	0.000	0.000	0.000	0.000
153	A	185	TYR	0	-0.026	-0.040	18.867	0.026	0.026	0.000	0.000	0.000	0.000
154	A	186	GLY	0	0.018	0.007	19.952	-0.013	-0.013	0.000	0.000	0.000	0.000
155	A	187	ALA	0	0.017	0.004	22.517	0.006	0.006	0.000	0.000	0.000	0.000
156	A	188	GLN	0	0.008	0.003	23.886	-0.002	-0.002	0.000	0.000	0.000	0.000
157	A	189	PHE	0	0.015	0.002	25.638	0.009	0.009	0.000	0.000	0.000	0.000
158	A	190	HIS	1	0.837	0.900	22.888	0.128	0.128	0.000	0.000	0.000	0.000
159	A	191	PRO	0	0.016	0.044	20.668	0.012	0.012	0.000	0.000	0.000	0.000
160	A	192	GLU	-1	-0.751	-0.876	19.433	-0.224	-0.224	0.000	0.000	0.000	0.000
161	A	193	VAL	0	-0.021	-0.012	21.153	0.012	0.012	0.000	0.000	0.000	0.000
162	A	194	GLY	0	0.026	0.011	24.555	-0.005	-0.005	0.000	0.000	0.000	0.000
163	A	195	LEU	0	0.001	-0.005	26.801	0.002	0.002	0.000	0.000	0.000	0.000
164	A	196	THR	0	-0.062	-0.039	26.069	0.011	0.011	0.000	0.000	0.000	0.000
165	A	197	GLU	-1	-0.911	-0.932	27.163	-0.168	-0.168	0.000	0.000	0.000	0.000
166	A	198	ASN	0	-0.021	-0.023	27.117	-0.015	-0.015	0.000	0.000	0.000	0.000
167	A	199	GLY	0	0.016	-0.006	24.168	-0.020	-0.020	0.000	0.000	0.000	0.000
168	A	200	LYS	1	0.881	0.943	18.442	0.357	0.357	0.000	0.000	0.000	0.000
169	A	201	VAL	0	0.009	0.018	21.014	-0.045	-0.045	0.000	0.000	0.000	0.000
170	A	202	ILE	0	0.038	0.031	21.254	-0.030	-0.030	0.000	0.000	0.000	0.000
171	A	203	LEU	0	-0.009	-0.018	16.946	-0.038	-0.038	0.000	0.000	0.000	0.000
172	A	204	LYS	1	0.936	0.980	17.155	0.330	0.330	0.000	0.000	0.000	0.000
173	A	205	ASN	0	-0.008	-0.012	18.254	-0.065	-0.065	0.000	0.000	0.000	0.000
174	A	206	PHE	0	-0.001	-0.010	13.098	-0.033	-0.033	0.000	0.000	0.000	0.000
175	A	207	LEU	0	-0.005	-0.009	11.847	-0.082	-0.082	0.000	0.000	0.000	0.000
176	A	208	TYR	0	-0.060	-0.052	13.990	-0.061	-0.061	0.000	0.000	0.000	0.000
177	A	209	ASP	-1	-0.899	-0.939	16.352	-0.526	-0.526	0.000	0.000	0.000	0.000
178	A	210	ILE	0	-0.089	-0.029	16.480	-0.005	-0.005	0.000	0.000	0.000	0.000
179	A	211	ALA	0	-0.026	-0.030	12.081	-0.013	-0.013	0.000	0.000	0.000	0.000
180	A	212	GLY	0	-0.006	0.008	13.081	-0.139	-0.139	0.000	0.000	0.000	0.000
181	A	213	CYS	0	-0.102	-0.051	10.161	-0.198	-0.198	0.000	0.000	0.000	0.000
182	A	214	SER	0	0.001	-0.011	11.674	0.130	0.130	0.000	0.000	0.000	0.000
183	A	215	GLY	0	0.038	0.019	12.564	-0.085	-0.085	0.000	0.000	0.000	0.000
184	A	216	THR	0	-0.034	-0.012	13.547	0.107	0.107	0.000	0.000	0.000	0.000
185	A	217	PHE	0	0.012	0.015	12.473	-0.117	-0.117	0.000	0.000	0.000	0.000
186	A	218	THR	0	-0.018	-0.018	11.870	0.059	0.059	0.000	0.000	0.000	0.000
187	A	219	VAL	0	0.010	0.017	14.131	0.037	0.037	0.000	0.000	0.000	0.000

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