FMO DATABASE

FMODB ID: 3ZRQL

Calculation Name: 5XTB-O-Other547

Preferred Name: Mitochondrial complex I (NADH dehydrogenase)

Target Type: PROTEIN COMPLEX

Ligand Name: nadph dihydro-nicotinamide-adenine-dinucleotide phosphate | flavin mononucleotide | s-[2-({n-[(2r)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate | iron/sulfur cluster | fe2/s2 (inorganic) cluster

Ligand 3-letter code: NDP | FMN | 8Q1 | SF4 | FES

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5XTB

Chain ID: O

ChEMBL ID: CHEMBL2363065

UniProt ID: O14561

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	212
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2163064.084299
FMO2-HF: Nuclear repulsion	2080165.781703
FMO2-HF: Total energy	-82898.302596
FMO2-MP2: Total energy	-83136.608952

3D Structure Molmil

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:36:GLY)

Summations of interaction energy for fragment #1(A:36:GLY)

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.
-20.298	-18.338	0.004	-0.833	-1.132	-0.003

Interaction energy analysis for fragmet #1(A:36:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.893 / q_NPA : 0.927

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	38	LEU	0	-0.004	0.012	3.310	8.967	10.830	0.005	-0.811	-1.058	-0.003
4	A	39	PHE	0	0.017	-0.008	5.370	1.534	1.631	-0.001	-0.022	-0.074	0.000
5	A	40	VAL	0	-0.017	-0.005	7.274	3.166	3.166	0.000	0.000	0.000	0.000
6	A	41	HIS	1	0.917	0.973	9.001	25.626	25.626	0.000	0.000	0.000	0.000
7	A	42	ARG	1	0.975	0.990	10.590	21.010	21.010	0.000	0.000	0.000	0.000
8	A	43	ASP	-1	-0.919	-0.955	9.329	-27.964	-27.964	0.000	0.000	0.000	0.000
9	A	44	THR	0	-0.011	-0.018	12.211	0.032	0.032	0.000	0.000	0.000	0.000
10	A	45	PRO	0	-0.001	0.008	12.070	0.880	0.880	0.000	0.000	0.000	0.000
11	A	46	GLU	-1	-0.817	-0.925	15.111	-17.554	-17.554	0.000	0.000	0.000	0.000
12	A	47	ASN	0	-0.033	-0.019	14.544	1.090	1.090	0.000	0.000	0.000	0.000
13	A	48	ASN	0	-0.081	-0.051	13.006	-0.380	-0.380	0.000	0.000	0.000	0.000
14	A	49	PRO	0	0.025	0.035	16.298	-0.788	-0.788	0.000	0.000	0.000	0.000
15	A	50	ASP	-1	-0.902	-0.949	18.930	-13.904	-13.904	0.000	0.000	0.000	0.000
16	A	51	THR	0	-0.041	-0.031	19.615	0.693	0.693	0.000	0.000	0.000	0.000
17	A	52	PRO	0	-0.001	0.011	21.495	-0.338	-0.338	0.000	0.000	0.000	0.000
18	A	53	PHE	0	0.000	-0.011	21.270	-0.235	-0.235	0.000	0.000	0.000	0.000
19	A	54	ASP	-1	-0.807	-0.880	23.366	-10.764	-10.764	0.000	0.000	0.000	0.000
20	A	55	PHE	0	-0.044	0.000	21.525	-0.318	-0.318	0.000	0.000	0.000	0.000
21	A	56	THR	0	0.038	0.001	26.201	0.473	0.473	0.000	0.000	0.000	0.000
22	A	57	PRO	0	0.039	0.005	29.199	-0.100	-0.100	0.000	0.000	0.000	0.000
23	A	58	GLU	-1	-0.857	-0.934	30.684	-9.512	-9.512	0.000	0.000	0.000	0.000
24	A	59	ASN	0	-0.029	-0.004	26.090	-0.119	-0.119	0.000	0.000	0.000	0.000
25	A	60	TYR	0	0.014	-0.028	28.261	-0.107	-0.107	0.000	0.000	0.000	0.000
26	A	61	LYS	1	0.867	0.922	30.227	8.753	8.753	0.000	0.000	0.000	0.000
27	A	62	ARG	1	0.935	0.966	27.213	10.965	10.965	0.000	0.000	0.000	0.000
28	A	63	ILE	0	0.024	0.014	25.626	-0.053	-0.053	0.000	0.000	0.000	0.000
29	A	64	GLU	-1	-0.791	-0.867	28.467	-8.743	-8.743	0.000	0.000	0.000	0.000
30	A	65	ALA	0	-0.010	-0.007	31.715	0.172	0.172	0.000	0.000	0.000	0.000
31	A	66	ILE	0	-0.028	-0.015	25.568	0.033	0.033	0.000	0.000	0.000	0.000
32	A	67	VAL	0	-0.013	-0.013	29.429	-0.017	-0.017	0.000	0.000	0.000	0.000
33	A	68	LYS	1	0.830	0.913	31.113	8.726	8.726	0.000	0.000	0.000	0.000
34	A	69	ASN	0	-0.026	-0.003	30.070	0.488	0.488	0.000	0.000	0.000	0.000
35	A	70	TYR	0	-0.032	-0.013	27.012	-0.218	-0.218	0.000	0.000	0.000	0.000
36	A	71	PRO	0	0.016	-0.001	32.143	0.216	0.216	0.000	0.000	0.000	0.000
37	A	72	GLU	-1	-0.762	-0.863	33.288	-9.137	-9.137	0.000	0.000	0.000	0.000
38	A	73	GLY	0	-0.035	-0.012	34.326	-0.083	-0.083	0.000	0.000	0.000	0.000
39	A	74	HIS	0	-0.039	-0.022	29.895	-0.368	-0.368	0.000	0.000	0.000	0.000
40	A	75	LYS	1	0.901	0.927	28.984	9.121	9.121	0.000	0.000	0.000	0.000
41	A	76	ALA	0	0.012	0.002	24.926	-0.312	-0.312	0.000	0.000	0.000	0.000
42	A	77	ALA	0	-0.003	0.006	24.310	-0.556	-0.556	0.000	0.000	0.000	0.000
43	A	78	ALA	0	0.014	0.007	24.989	-0.284	-0.284	0.000	0.000	0.000	0.000
44	A	79	VAL	0	-0.001	-0.002	19.246	-0.306	-0.306	0.000	0.000	0.000	0.000
45	A	80	LEU	0	0.046	0.024	18.213	-0.393	-0.393	0.000	0.000	0.000	0.000
46	A	81	PRO	0	0.025	0.002	19.529	-0.517	-0.517	0.000	0.000	0.000	0.000
47	A	82	VAL	0	-0.002	0.004	21.857	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	83	LEU	0	0.009	0.008	15.719	-0.131	-0.131	0.000	0.000	0.000	0.000
49	A	84	ASP	-1	-0.831	-0.883	17.439	-16.391	-16.391	0.000	0.000	0.000	0.000
50	A	85	LEU	0	-0.047	-0.019	18.777	0.073	0.073	0.000	0.000	0.000	0.000
51	A	86	ALA	0	0.021	0.004	18.442	0.213	0.213	0.000	0.000	0.000	0.000
52	A	87	GLN	0	0.058	0.045	12.789	-0.654	-0.654	0.000	0.000	0.000	0.000
53	A	88	ARG	1	0.770	0.873	17.232	15.242	15.242	0.000	0.000	0.000	0.000
54	A	89	GLN	0	-0.050	-0.032	20.348	0.398	0.398	0.000	0.000	0.000	0.000
55	A	90	ASN	0	-0.066	-0.038	17.433	0.647	0.647	0.000	0.000	0.000	0.000
56	A	91	GLY	0	-0.011	0.006	16.145	-0.200	-0.200	0.000	0.000	0.000	0.000
57	A	92	TRP	0	-0.057	-0.057	10.446	-0.606	-0.606	0.000	0.000	0.000	0.000
58	A	93	LEU	0	-0.009	-0.003	12.235	1.533	1.533	0.000	0.000	0.000	0.000
59	A	94	PRO	0	0.019	0.023	12.469	-1.548	-1.548	0.000	0.000	0.000	0.000
60	A	95	ILE	0	0.016	-0.013	14.297	0.255	0.255	0.000	0.000	0.000	0.000
61	A	96	SER	0	-0.002	-0.006	15.535	0.311	0.311	0.000	0.000	0.000	0.000
62	A	97	ALA	0	0.011	0.010	16.953	0.807	0.807	0.000	0.000	0.000	0.000
63	A	98	MET	0	-0.070	-0.027	11.297	0.281	0.281	0.000	0.000	0.000	0.000
64	A	99	ASN	0	0.041	0.008	17.595	0.386	0.386	0.000	0.000	0.000	0.000
65	A	100	LYS	1	0.986	1.024	20.631	12.004	12.004	0.000	0.000	0.000	0.000
66	A	101	VAL	0	0.014	-0.011	20.029	0.575	0.575	0.000	0.000	0.000	0.000
67	A	102	ALA	0	-0.034	-0.016	21.363	0.356	0.356	0.000	0.000	0.000	0.000
68	A	103	GLU	-1	-0.934	-0.965	23.120	-11.278	-11.278	0.000	0.000	0.000	0.000
69	A	104	VAL	0	-0.068	-0.034	25.267	0.476	0.476	0.000	0.000	0.000	0.000
70	A	105	LEU	0	-0.043	-0.028	23.774	0.336	0.336	0.000	0.000	0.000	0.000
71	A	106	GLN	0	-0.030	-0.001	26.936	0.341	0.341	0.000	0.000	0.000	0.000
72	A	107	VAL	0	-0.023	0.007	23.176	0.141	0.141	0.000	0.000	0.000	0.000
73	A	108	PRO	0	0.018	0.002	23.766	-0.196	-0.196	0.000	0.000	0.000	0.000
74	A	109	PRO	0	0.060	0.004	20.314	-0.471	-0.471	0.000	0.000	0.000	0.000
75	A	110	MET	0	-0.009	0.011	16.358	-0.790	-0.790	0.000	0.000	0.000	0.000
76	A	111	ARG	1	0.907	0.955	17.761	13.294	13.294	0.000	0.000	0.000	0.000
77	A	112	VAL	0	0.024	0.021	16.947	-0.639	-0.639	0.000	0.000	0.000	0.000
78	A	113	TYR	0	0.015	0.000	14.277	-1.018	-1.018	0.000	0.000	0.000	0.000
79	A	114	GLU	-1	-0.849	-0.916	13.203	-18.427	-18.427	0.000	0.000	0.000	0.000
80	A	115	VAL	0	-0.012	-0.004	13.738	-1.448	-1.448	0.000	0.000	0.000	0.000
81	A	116	ALA	0	0.031	0.007	12.905	-0.979	-0.979	0.000	0.000	0.000	0.000
82	A	117	THR	0	-0.085	-0.063	8.433	-3.358	-3.358	0.000	0.000	0.000	0.000
83	A	118	PHE	0	-0.050	-0.024	9.125	-3.499	-3.499	0.000	0.000	0.000	0.000
84	A	119	TYR	0	0.005	0.002	11.207	-0.793	-0.793	0.000	0.000	0.000	0.000
85	A	120	THR	0	0.001	-0.017	7.771	0.358	0.358	0.000	0.000	0.000	0.000
86	A	121	MET	0	0.026	0.027	9.160	-2.211	-2.211	0.000	0.000	0.000	0.000
87	A	122	TYR	0	-0.031	-0.008	11.006	1.168	1.168	0.000	0.000	0.000	0.000
88	A	123	ASN	0	-0.015	-0.004	8.685	-5.123	-5.123	0.000	0.000	0.000	0.000
89	A	124	ARG	1	0.946	0.966	5.963	37.352	37.352	0.000	0.000	0.000	0.000
90	A	125	LYS	1	0.873	0.946	5.353	34.611	34.611	0.000	0.000	0.000	0.000
91	A	126	PRO	0	0.023	0.016	8.211	0.274	0.274	0.000	0.000	0.000	0.000
92	A	127	VAL	0	0.007	0.006	10.299	-1.696	-1.696	0.000	0.000	0.000	0.000
93	A	128	GLY	0	0.010	0.007	12.561	1.279	1.279	0.000	0.000	0.000	0.000
94	A	129	LYS	1	0.877	0.944	15.895	13.118	13.118	0.000	0.000	0.000	0.000
95	A	130	TYR	0	-0.023	-0.020	17.791	0.808	0.808	0.000	0.000	0.000	0.000
96	A	131	HIS	0	0.003	0.010	9.931	0.808	0.808	0.000	0.000	0.000	0.000
97	A	132	ILE	0	-0.024	-0.015	14.454	0.752	0.752	0.000	0.000	0.000	0.000
98	A	133	GLN	0	0.031	0.009	12.809	-0.685	-0.685	0.000	0.000	0.000	0.000
99	A	134	VAL	0	-0.010	0.009	13.935	1.022	1.022	0.000	0.000	0.000	0.000
100	A	135	CYS	0	-0.014	0.014	14.409	-1.045	-1.045	0.000	0.000	0.000	0.000
101	A	136	THR	0	0.102	0.041	14.101	1.237	1.237	0.000	0.000	0.000	0.000
102	A	137	THR	0	0.002	-0.015	15.610	0.712	0.712	0.000	0.000	0.000	0.000
103	A	138	THR	0	0.039	0.006	17.491	0.667	0.667	0.000	0.000	0.000	0.000
104	A	139	PRO	0	-0.009	0.000	20.828	0.489	0.489	0.000	0.000	0.000	0.000
105	A	140	CYS	0	0.010	0.000	20.082	0.442	0.442	0.000	0.000	0.000	0.000
106	A	141	MET	0	-0.006	0.008	17.878	0.568	0.568	0.000	0.000	0.000	0.000
107	A	142	LEU	0	-0.001	-0.009	21.644	0.446	0.446	0.000	0.000	0.000	0.000
108	A	143	ARG	1	0.794	0.904	24.738	11.578	11.578	0.000	0.000	0.000	0.000
109	A	144	ASN	0	0.020	0.003	23.885	-0.301	-0.301	0.000	0.000	0.000	0.000
110	A	145	SER	0	0.012	-0.029	18.677	0.205	0.205	0.000	0.000	0.000	0.000
111	A	146	ASP	-1	-0.874	-0.926	17.780	-17.877	-17.877	0.000	0.000	0.000	0.000
112	A	147	SER	0	-0.030	-0.009	19.553	-0.051	-0.051	0.000	0.000	0.000	0.000
113	A	148	ILE	0	-0.032	-0.032	19.908	0.339	0.339	0.000	0.000	0.000	0.000
114	A	149	LEU	0	0.031	0.014	13.987	-0.248	-0.248	0.000	0.000	0.000	0.000
115	A	150	GLU	-1	-0.911	-0.961	17.507	-15.026	-15.026	0.000	0.000	0.000	0.000
116	A	151	ALA	0	-0.059	-0.024	19.672	0.387	0.387	0.000	0.000	0.000	0.000
117	A	152	ILE	0	0.012	0.006	17.197	0.239	0.239	0.000	0.000	0.000	0.000
118	A	153	GLN	0	0.006	0.003	16.236	-0.255	-0.255	0.000	0.000	0.000	0.000
119	A	154	LYS	1	0.871	0.929	18.181	12.858	12.858	0.000	0.000	0.000	0.000
120	A	155	LYS	1	0.779	0.889	21.944	12.235	12.235	0.000	0.000	0.000	0.000
121	A	156	LEU	0	-0.043	-0.022	17.680	0.221	0.221	0.000	0.000	0.000	0.000
122	A	157	GLY	0	-0.007	0.005	19.592	-0.028	-0.028	0.000	0.000	0.000	0.000
123	A	158	ILE	0	-0.053	-0.017	13.455	-0.160	-0.160	0.000	0.000	0.000	0.000
124	A	159	LYS	1	0.882	0.934	12.574	18.190	18.190	0.000	0.000	0.000	0.000
125	A	160	VAL	0	0.003	-0.019	10.096	-2.477	-2.477	0.000	0.000	0.000	0.000
126	A	161	GLY	0	0.023	0.019	7.569	0.368	0.368	0.000	0.000	0.000	0.000
127	A	162	GLU	-1	-0.910	-0.940	8.331	-23.869	-23.869	0.000	0.000	0.000	0.000
128	A	163	THR	0	-0.008	-0.014	10.488	1.149	1.149	0.000	0.000	0.000	0.000
129	A	164	THR	0	0.010	0.024	12.725	0.893	0.893	0.000	0.000	0.000	0.000
130	A	165	PRO	0	0.037	0.011	16.329	-0.009	-0.009	0.000	0.000	0.000	0.000
131	A	166	ASP	-1	-0.927	-0.976	18.782	-13.605	-13.605	0.000	0.000	0.000	0.000
132	A	167	LYS	1	0.874	0.935	17.316	16.023	16.023	0.000	0.000	0.000	0.000
133	A	168	LEU	0	0.002	0.026	18.391	-0.115	-0.115	0.000	0.000	0.000	0.000
134	A	169	PHE	0	0.049	0.003	16.638	-0.373	-0.373	0.000	0.000	0.000	0.000
135	A	170	THR	0	0.001	-0.023	11.305	-0.927	-0.927	0.000	0.000	0.000	0.000
136	A	171	LEU	0	-0.013	0.016	12.529	0.297	0.297	0.000	0.000	0.000	0.000
137	A	172	ILE	0	-0.043	-0.022	6.295	-3.122	-3.122	0.000	0.000	0.000	0.000
138	A	173	GLU	-1	-0.914	-0.939	9.220	-26.912	-26.912	0.000	0.000	0.000	0.000
139	A	174	VAL	0	-0.042	-0.030	9.709	-3.349	-3.349	0.000	0.000	0.000	0.000
140	A	175	GLU	-1	-0.833	-0.906	11.423	-21.010	-21.010	0.000	0.000	0.000	0.000
141	A	176	CYS	0	-0.082	-0.037	13.681	0.939	0.939	0.000	0.000	0.000	0.000
142	A	177	LEU	0	0.040	0.020	15.228	0.210	0.210	0.000	0.000	0.000	0.000
143	A	178	GLY	0	0.018	-0.005	18.432	0.614	0.614	0.000	0.000	0.000	0.000
144	A	179	ALA	0	0.008	0.012	21.851	0.607	0.607	0.000	0.000	0.000	0.000
145	A	180	CYS	0	-0.056	-0.045	22.372	0.147	0.147	0.000	0.000	0.000	0.000
146	A	181	VAL	0	-0.008	0.002	24.767	0.164	0.164	0.000	0.000	0.000	0.000
147	A	182	ASN	0	-0.025	-0.015	27.145	0.565	0.565	0.000	0.000	0.000	0.000
148	A	183	ALA	0	0.007	0.009	25.958	0.280	0.280	0.000	0.000	0.000	0.000
149	A	184	PRO	0	0.031	0.030	21.460	-0.397	-0.397	0.000	0.000	0.000	0.000
150	A	185	MET	0	-0.010	0.002	19.822	0.660	0.660	0.000	0.000	0.000	0.000
151	A	186	VAL	0	0.013	-0.009	18.431	-1.038	-1.038	0.000	0.000	0.000	0.000
152	A	187	GLN	0	0.001	0.003	17.978	0.748	0.748	0.000	0.000	0.000	0.000
153	A	188	ILE	0	0.024	0.013	17.468	-1.201	-1.201	0.000	0.000	0.000	0.000
154	A	189	ASN	0	0.007	-0.001	17.486	0.727	0.727	0.000	0.000	0.000	0.000
155	A	190	ASP	-1	-0.838	-0.910	19.252	-15.435	-15.435	0.000	0.000	0.000	0.000
156	A	191	ASN	0	-0.097	-0.044	21.307	1.561	1.561	0.000	0.000	0.000	0.000
157	A	192	TYR	0	0.061	0.030	21.515	-0.413	-0.413	0.000	0.000	0.000	0.000
158	A	193	TYR	0	0.054	0.011	22.638	0.446	0.446	0.000	0.000	0.000	0.000
159	A	194	GLU	-1	-0.811	-0.900	23.531	-12.655	-12.655	0.000	0.000	0.000	0.000
160	A	195	ASP	-1	-0.803	-0.877	25.814	-10.006	-10.006	0.000	0.000	0.000	0.000
161	A	196	LEU	0	-0.036	0.013	23.279	0.264	0.264	0.000	0.000	0.000	0.000
162	A	197	THR	0	0.027	0.016	26.326	-0.107	-0.107	0.000	0.000	0.000	0.000
163	A	198	ALA	0	0.075	0.020	25.776	-0.205	-0.205	0.000	0.000	0.000	0.000
164	A	199	LYS	1	0.923	0.953	26.831	9.704	9.704	0.000	0.000	0.000	0.000
165	A	200	ASP	-1	-0.844	-0.928	27.644	-10.825	-10.825	0.000	0.000	0.000	0.000
166	A	201	ILE	0	-0.005	0.016	22.067	-0.158	-0.158	0.000	0.000	0.000	0.000
167	A	202	GLU	-1	-0.915	-0.950	24.970	-11.997	-11.997	0.000	0.000	0.000	0.000
168	A	203	GLU	-1	-0.911	-0.952	27.137	-9.993	-9.993	0.000	0.000	0.000	0.000
169	A	204	ILE	0	0.024	0.005	23.200	-0.038	-0.038	0.000	0.000	0.000	0.000
170	A	205	ILE	0	-0.045	-0.033	20.426	-0.275	-0.275	0.000	0.000	0.000	0.000
171	A	206	ASP	-1	-0.860	-0.917	24.257	-11.402	-11.402	0.000	0.000	0.000	0.000
172	A	207	GLU	-1	-0.834	-0.940	27.623	-10.529	-10.529	0.000	0.000	0.000	0.000
173	A	208	LEU	0	-0.056	-0.024	21.198	0.040	0.040	0.000	0.000	0.000	0.000
174	A	209	LYS	1	0.877	0.929	23.839	12.496	12.496	0.000	0.000	0.000	0.000
175	A	210	ALA	0	-0.014	0.010	27.321	0.305	0.305	0.000	0.000	0.000	0.000
176	A	211	GLY	0	-0.013	-0.014	29.375	0.415	0.415	0.000	0.000	0.000	0.000
177	A	212	LYS	1	0.879	0.945	28.519	10.020	10.020	0.000	0.000	0.000	0.000
178	A	213	ILE	0	0.017	0.035	25.171	0.272	0.272	0.000	0.000	0.000	0.000
179	A	214	PRO	0	-0.025	-0.001	28.747	-0.124	-0.124	0.000	0.000	0.000	0.000
180	A	215	LYS	1	0.851	0.901	25.431	12.014	12.014	0.000	0.000	0.000	0.000
181	A	216	PRO	0	-0.018	0.002	28.586	0.136	0.136	0.000	0.000	0.000	0.000
182	A	217	GLY	0	0.077	0.044	27.974	-0.361	-0.361	0.000	0.000	0.000	0.000
183	A	218	PRO	0	-0.069	-0.050	28.328	-0.259	-0.259	0.000	0.000	0.000	0.000
184	A	219	ARG	1	0.921	0.976	28.282	11.135	11.135	0.000	0.000	0.000	0.000
185	A	220	SER	0	-0.078	-0.074	30.808	0.365	0.365	0.000	0.000	0.000	0.000
186	A	221	GLY	0	0.022	0.020	33.245	0.266	0.266	0.000	0.000	0.000	0.000
187	A	222	ARG	1	0.800	0.897	31.726	9.982	9.982	0.000	0.000	0.000	0.000
188	A	223	PHE	0	0.040	0.013	33.263	-0.263	-0.263	0.000	0.000	0.000	0.000
189	A	224	SER	0	0.029	0.009	33.944	0.007	0.007	0.000	0.000	0.000	0.000
190	A	225	CYS	0	-0.040	-0.022	31.548	-0.077	-0.077	0.000	0.000	0.000	0.000
191	A	226	GLU	-1	-0.896	-0.934	33.069	-8.194	-8.194	0.000	0.000	0.000	0.000
192	A	227	PRO	0	-0.049	-0.040	36.149	-0.049	-0.049	0.000	0.000	0.000	0.000
193	A	228	ALA	0	0.063	0.015	37.685	0.207	0.207	0.000	0.000	0.000	0.000
194	A	229	GLY	0	-0.056	-0.024	39.681	0.189	0.189	0.000	0.000	0.000	0.000
195	A	230	GLY	0	-0.012	-0.016	41.524	0.098	0.098	0.000	0.000	0.000	0.000
196	A	231	LEU	0	-0.057	-0.002	40.518	0.124	0.124	0.000	0.000	0.000	0.000
197	A	232	THR	0	0.068	0.035	42.073	0.152	0.152	0.000	0.000	0.000	0.000
198	A	233	SER	0	-0.043	-0.025	40.335	-0.080	-0.080	0.000	0.000	0.000	0.000
199	A	234	LEU	0	-0.012	0.001	40.958	0.178	0.178	0.000	0.000	0.000	0.000
200	A	235	THR	0	0.023	0.006	44.504	0.028	0.028	0.000	0.000	0.000	0.000
201	A	236	GLU	-1	-0.935	-0.964	47.654	-6.082	-6.082	0.000	0.000	0.000	0.000
202	A	237	PRO	0	0.004	-0.006	48.082	-0.107	-0.107	0.000	0.000	0.000	0.000
203	A	238	PRO	0	-0.052	-0.012	48.791	-0.058	-0.058	0.000	0.000	0.000	0.000
204	A	239	LYS	1	0.971	0.980	46.209	6.712	6.712	0.000	0.000	0.000	0.000
205	A	240	GLY	0	0.068	0.039	49.404	-0.039	-0.039	0.000	0.000	0.000	0.000
206	A	241	PRO	0	-0.031	-0.016	51.524	-0.062	-0.062	0.000	0.000	0.000	0.000
207	A	242	GLY	0	0.023	0.010	52.481	0.114	0.114	0.000	0.000	0.000	0.000
208	A	243	PHE	0	-0.004	-0.024	52.676	-0.126	-0.126	0.000	0.000	0.000	0.000
209	A	244	GLY	0	-0.040	-0.012	52.402	0.019	0.019	0.000	0.000	0.000	0.000
210	A	245	VAL	0	0.004	-0.008	53.138	-0.034	-0.034	0.000	0.000	0.000	0.000
211	A	246	GLN	0	-0.078	-0.029	53.229	-0.046	-0.046	0.000	0.000	0.000	0.000
212	A	247	ALA	-1	-0.934	-0.949	56.174	-5.309	-5.309	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:36:GLY)