data_9F9I
# 
_entry.id   9F9I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F9I         pdb_00009f9i 10.2210/pdb9f9i/pdb 
WWPDB D_1292135922 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F9I 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              joerg.standfuss@psi.ch 
_pdbx_contact_author.name_first         Joerg 
_pdbx_contact_author.name_last          Standfuss 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8825-386X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bertrand, Q.'  1 0000-0003-3476-1775 
'Weinert, T.'   2 0000-0002-0339-3722 
'Standfuss, J.' 3 0000-0001-8825-386X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10278 
_citation.page_last                 10278 
_citation.title                     
'Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54422-8 
_citation.pdbx_database_id_PubMed   39604356 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bertrand, Q.'    1  0000-0003-3476-1775 
primary 'Nogly, P.'       2  0000-0002-8040-7753 
primary 'Nango, E.'       3  0000-0001-9851-7355 
primary 'Kekilli, D.'     4  ?                   
primary 'Khusainov, G.'   5  ?                   
primary 'Furrer, A.'      6  0000-0001-9894-6985 
primary 'James, D.'       7  ?                   
primary 'Dworkowski, F.'  8  0000-0001-5004-8684 
primary 'Skopintsev, P.'  9  ?                   
primary 'Mous, S.'        10 ?                   
primary 'Martiel, I.'     11 ?                   
primary 'Borjesson, P.'   12 0000-0002-7193-640X 
primary 'Ortolani, G.'    13 0000-0001-6373-9919 
primary 'Huang, C.Y.'     14 0000-0002-7676-0239 
primary 'Kepa, M.'        15 0000-0002-4045-3990 
primary 'Ozerov, D.'      16 0000-0002-3274-1124 
primary 'Brunle, S.'      17 ?                   
primary 'Panneels, V.'    18 0000-0001-8899-3366 
primary 'Tanaka, T.'      19 ?                   
primary 'Tanaka, R.'      20 ?                   
primary 'Tono, K.'        21 0000-0003-1218-3759 
primary 'Owada, S.'       22 ?                   
primary 'Johnson, P.J.M.' 23 0000-0002-7251-4815 
primary 'Nass, K.'        24 ?                   
primary 'Knopp, G.'       25 0000-0002-0786-3402 
primary 'Cirelli, C.'     26 0000-0003-4576-3805 
primary 'Milne, C.'       27 0000-0003-4714-9139 
primary 'Schertler, G.'   28 0000-0002-5846-6810 
primary 'Iwata, S.'       29 0000-0003-1735-2937 
primary 'Neutze, R.'      30 0000-0003-0986-6153 
primary 'Weinert, T.'     31 0000-0002-0339-3722 
primary 'Standfuss, J.'   32 0000-0001-8825-386X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Bacteriorhodopsin                                                                        25247.781 1  ? ? ? ? 
2 non-polymer syn '1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL' 639.130   12 ? ? ? ? 
3 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                                         356.540   5  ? ? ? ? 
4 non-polymer man RETINAL                                                                                  284.436   1  ? ? ? ? 
5 water       nat water                                                                                    18.015    45 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 BR,Bacterioopsin,BO 
4 BR,Bacterioopsin,BO 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GTGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM
RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GTGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM
RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL' LI1 
3 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                                         OLC 
4 RETINAL                                                                                  RET 
5 water                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   THR n 
1 3   GLY n 
1 4   ARG n 
1 5   PRO n 
1 6   GLU n 
1 7   TRP n 
1 8   ILE n 
1 9   TRP n 
1 10  LEU n 
1 11  ALA n 
1 12  LEU n 
1 13  GLY n 
1 14  THR n 
1 15  ALA n 
1 16  LEU n 
1 17  MET n 
1 18  GLY n 
1 19  LEU n 
1 20  GLY n 
1 21  THR n 
1 22  LEU n 
1 23  TYR n 
1 24  PHE n 
1 25  LEU n 
1 26  VAL n 
1 27  LYS n 
1 28  GLY n 
1 29  MET n 
1 30  GLY n 
1 31  VAL n 
1 32  SER n 
1 33  ASP n 
1 34  PRO n 
1 35  ASP n 
1 36  ALA n 
1 37  LYS n 
1 38  LYS n 
1 39  PHE n 
1 40  TYR n 
1 41  ALA n 
1 42  ILE n 
1 43  THR n 
1 44  THR n 
1 45  LEU n 
1 46  VAL n 
1 47  PRO n 
1 48  ALA n 
1 49  ILE n 
1 50  ALA n 
1 51  PHE n 
1 52  THR n 
1 53  MET n 
1 54  TYR n 
1 55  LEU n 
1 56  SER n 
1 57  MET n 
1 58  LEU n 
1 59  LEU n 
1 60  GLY n 
1 61  TYR n 
1 62  GLY n 
1 63  LEU n 
1 64  THR n 
1 65  MET n 
1 66  VAL n 
1 67  PRO n 
1 68  PHE n 
1 69  GLY n 
1 70  GLY n 
1 71  GLU n 
1 72  GLN n 
1 73  ASN n 
1 74  PRO n 
1 75  ILE n 
1 76  TYR n 
1 77  TRP n 
1 78  ALA n 
1 79  ARG n 
1 80  TYR n 
1 81  ALA n 
1 82  ASP n 
1 83  TRP n 
1 84  LEU n 
1 85  PHE n 
1 86  THR n 
1 87  THR n 
1 88  PRO n 
1 89  LEU n 
1 90  LEU n 
1 91  LEU n 
1 92  LEU n 
1 93  ASP n 
1 94  LEU n 
1 95  ALA n 
1 96  LEU n 
1 97  LEU n 
1 98  VAL n 
1 99  ASP n 
1 100 ALA n 
1 101 ASP n 
1 102 GLN n 
1 103 GLY n 
1 104 THR n 
1 105 ILE n 
1 106 LEU n 
1 107 ALA n 
1 108 LEU n 
1 109 VAL n 
1 110 GLY n 
1 111 ALA n 
1 112 ASP n 
1 113 GLY n 
1 114 ILE n 
1 115 MET n 
1 116 ILE n 
1 117 GLY n 
1 118 THR n 
1 119 GLY n 
1 120 LEU n 
1 121 VAL n 
1 122 GLY n 
1 123 ALA n 
1 124 LEU n 
1 125 THR n 
1 126 LYS n 
1 127 VAL n 
1 128 TYR n 
1 129 SER n 
1 130 TYR n 
1 131 ARG n 
1 132 PHE n 
1 133 VAL n 
1 134 TRP n 
1 135 TRP n 
1 136 ALA n 
1 137 ILE n 
1 138 SER n 
1 139 THR n 
1 140 ALA n 
1 141 ALA n 
1 142 MET n 
1 143 LEU n 
1 144 TYR n 
1 145 ILE n 
1 146 LEU n 
1 147 TYR n 
1 148 VAL n 
1 149 LEU n 
1 150 PHE n 
1 151 PHE n 
1 152 GLY n 
1 153 PHE n 
1 154 THR n 
1 155 SER n 
1 156 LYS n 
1 157 ALA n 
1 158 GLU n 
1 159 SER n 
1 160 MET n 
1 161 ARG n 
1 162 PRO n 
1 163 GLU n 
1 164 VAL n 
1 165 ALA n 
1 166 SER n 
1 167 THR n 
1 168 PHE n 
1 169 LYS n 
1 170 VAL n 
1 171 LEU n 
1 172 ARG n 
1 173 ASN n 
1 174 VAL n 
1 175 THR n 
1 176 VAL n 
1 177 VAL n 
1 178 LEU n 
1 179 TRP n 
1 180 SER n 
1 181 ALA n 
1 182 TYR n 
1 183 PRO n 
1 184 VAL n 
1 185 VAL n 
1 186 TRP n 
1 187 LEU n 
1 188 ILE n 
1 189 GLY n 
1 190 SER n 
1 191 GLU n 
1 192 GLY n 
1 193 ALA n 
1 194 GLY n 
1 195 ILE n 
1 196 VAL n 
1 197 PRO n 
1 198 LEU n 
1 199 ASN n 
1 200 ILE n 
1 201 GLU n 
1 202 THR n 
1 203 LEU n 
1 204 LEU n 
1 205 PHE n 
1 206 MET n 
1 207 VAL n 
1 208 LEU n 
1 209 ASP n 
1 210 VAL n 
1 211 SER n 
1 212 ALA n 
1 213 LYS n 
1 214 VAL n 
1 215 GLY n 
1 216 PHE n 
1 217 GLY n 
1 218 LEU n 
1 219 ILE n 
1 220 LEU n 
1 221 LEU n 
1 222 ARG n 
1 223 SER n 
1 224 ARG n 
1 225 ALA n 
1 226 ILE n 
1 227 PHE n 
1 228 GLY n 
1 229 GLU n 
1 230 ALA n 
1 231 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 231 ? ? 'bop, VNG_1467G' ? ? ? ? ? ? 'Halobacterium salinarum' 2242 ? ? 700922 ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 231 ? ? 'bop, VNG_1467G' ? ? ? ? ? ? 'Halobacterium salinarum' 2242 ? ? 700922 ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                  ? 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                                 ? 
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                               ? 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                          ? 'C4 H7 N O4' 
133.103 
GLN 'L-peptide linking' y GLUTAMINE                                                                                ? 
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                          ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                                  ? 'C2 H5 N O2' 
75.067  
HOH non-polymer         . WATER                                                                                    ? 'H2 O' 18.015 
ILE 'L-peptide linking' y ISOLEUCINE                                                                               ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                  ? 'C6 H13 N O2' 
131.173 
LI1 non-polymer         . '1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL' 
'LIPID FRAGMENT'    'C42 H86 O3'     639.130 
LYS 'L-peptide linking' y LYSINE                                                                                   ? 
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                               ? 
'C5 H11 N O2 S'  149.211 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                                         
1-Oleoyl-R-glycerol 'C21 H40 O4'     356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                                                            ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                                  ? 'C5 H9 N O2' 
115.130 
RET non-polymer         . RETINAL                                                                                  ? 'C20 H28 O' 
284.436 
SER 'L-peptide linking' y SERINE                                                                                   ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                                ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                               ? 
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                 ? 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE                                                                                   ? 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   4   4   GLY GLY A . n 
A 1 2   THR 2   5   5   THR THR A . n 
A 1 3   GLY 3   6   6   GLY GLY A . n 
A 1 4   ARG 4   7   7   ARG ARG A . n 
A 1 5   PRO 5   8   8   PRO PRO A . n 
A 1 6   GLU 6   9   9   GLU GLU A . n 
A 1 7   TRP 7   10  10  TRP TRP A . n 
A 1 8   ILE 8   11  11  ILE ILE A . n 
A 1 9   TRP 9   12  12  TRP TRP A . n 
A 1 10  LEU 10  13  13  LEU LEU A . n 
A 1 11  ALA 11  14  14  ALA ALA A . n 
A 1 12  LEU 12  15  15  LEU LEU A . n 
A 1 13  GLY 13  16  16  GLY GLY A . n 
A 1 14  THR 14  17  17  THR THR A . n 
A 1 15  ALA 15  18  18  ALA ALA A . n 
A 1 16  LEU 16  19  19  LEU LEU A . n 
A 1 17  MET 17  20  20  MET MET A . n 
A 1 18  GLY 18  21  21  GLY GLY A . n 
A 1 19  LEU 19  22  22  LEU LEU A . n 
A 1 20  GLY 20  23  23  GLY GLY A . n 
A 1 21  THR 21  24  24  THR THR A . n 
A 1 22  LEU 22  25  25  LEU LEU A . n 
A 1 23  TYR 23  26  26  TYR TYR A . n 
A 1 24  PHE 24  27  27  PHE PHE A . n 
A 1 25  LEU 25  28  28  LEU LEU A . n 
A 1 26  VAL 26  29  29  VAL VAL A . n 
A 1 27  LYS 27  30  30  LYS LYS A . n 
A 1 28  GLY 28  31  31  GLY GLY A . n 
A 1 29  MET 29  32  32  MET MET A . n 
A 1 30  GLY 30  33  33  GLY GLY A . n 
A 1 31  VAL 31  34  34  VAL VAL A . n 
A 1 32  SER 32  35  35  SER SER A . n 
A 1 33  ASP 33  36  36  ASP ASP A . n 
A 1 34  PRO 34  37  37  PRO PRO A . n 
A 1 35  ASP 35  38  38  ASP ASP A . n 
A 1 36  ALA 36  39  39  ALA ALA A . n 
A 1 37  LYS 37  40  40  LYS LYS A . n 
A 1 38  LYS 38  41  41  LYS LYS A . n 
A 1 39  PHE 39  42  42  PHE PHE A . n 
A 1 40  TYR 40  43  43  TYR TYR A . n 
A 1 41  ALA 41  44  44  ALA ALA A . n 
A 1 42  ILE 42  45  45  ILE ILE A . n 
A 1 43  THR 43  46  46  THR THR A . n 
A 1 44  THR 44  47  47  THR THR A . n 
A 1 45  LEU 45  48  48  LEU LEU A . n 
A 1 46  VAL 46  49  49  VAL VAL A . n 
A 1 47  PRO 47  50  50  PRO PRO A . n 
A 1 48  ALA 48  51  51  ALA ALA A . n 
A 1 49  ILE 49  52  52  ILE ILE A . n 
A 1 50  ALA 50  53  53  ALA ALA A . n 
A 1 51  PHE 51  54  54  PHE PHE A . n 
A 1 52  THR 52  55  55  THR THR A . n 
A 1 53  MET 53  56  56  MET MET A . n 
A 1 54  TYR 54  57  57  TYR TYR A . n 
A 1 55  LEU 55  58  58  LEU LEU A . n 
A 1 56  SER 56  59  59  SER SER A . n 
A 1 57  MET 57  60  60  MET MET A . n 
A 1 58  LEU 58  61  61  LEU LEU A . n 
A 1 59  LEU 59  62  62  LEU LEU A . n 
A 1 60  GLY 60  63  63  GLY GLY A . n 
A 1 61  TYR 61  64  64  TYR TYR A . n 
A 1 62  GLY 62  65  65  GLY GLY A . n 
A 1 63  LEU 63  66  66  LEU LEU A . n 
A 1 64  THR 64  67  67  THR THR A . n 
A 1 65  MET 65  68  68  MET MET A . n 
A 1 66  VAL 66  69  69  VAL VAL A . n 
A 1 67  PRO 67  70  70  PRO PRO A . n 
A 1 68  PHE 68  71  71  PHE PHE A . n 
A 1 69  GLY 69  72  72  GLY GLY A . n 
A 1 70  GLY 70  73  73  GLY GLY A . n 
A 1 71  GLU 71  74  74  GLU GLU A . n 
A 1 72  GLN 72  75  75  GLN GLN A . n 
A 1 73  ASN 73  76  76  ASN ASN A . n 
A 1 74  PRO 74  77  77  PRO PRO A . n 
A 1 75  ILE 75  78  78  ILE ILE A . n 
A 1 76  TYR 76  79  79  TYR TYR A . n 
A 1 77  TRP 77  80  80  TRP TRP A . n 
A 1 78  ALA 78  81  81  ALA ALA A . n 
A 1 79  ARG 79  82  82  ARG ARG A . n 
A 1 80  TYR 80  83  83  TYR TYR A . n 
A 1 81  ALA 81  84  84  ALA ALA A . n 
A 1 82  ASP 82  85  85  ASP ASP A . n 
A 1 83  TRP 83  86  86  TRP TRP A . n 
A 1 84  LEU 84  87  87  LEU LEU A . n 
A 1 85  PHE 85  88  88  PHE PHE A . n 
A 1 86  THR 86  89  89  THR THR A . n 
A 1 87  THR 87  90  90  THR THR A . n 
A 1 88  PRO 88  91  91  PRO PRO A . n 
A 1 89  LEU 89  92  92  LEU LEU A . n 
A 1 90  LEU 90  93  93  LEU LEU A . n 
A 1 91  LEU 91  94  94  LEU LEU A . n 
A 1 92  LEU 92  95  95  LEU LEU A . n 
A 1 93  ASP 93  96  96  ASP ASP A . n 
A 1 94  LEU 94  97  97  LEU LEU A . n 
A 1 95  ALA 95  98  98  ALA ALA A . n 
A 1 96  LEU 96  99  99  LEU LEU A . n 
A 1 97  LEU 97  100 100 LEU LEU A . n 
A 1 98  VAL 98  101 101 VAL VAL A . n 
A 1 99  ASP 99  102 102 ASP ASP A . n 
A 1 100 ALA 100 103 103 ALA ALA A . n 
A 1 101 ASP 101 104 104 ASP ASP A . n 
A 1 102 GLN 102 105 105 GLN GLN A . n 
A 1 103 GLY 103 106 106 GLY GLY A . n 
A 1 104 THR 104 107 107 THR THR A . n 
A 1 105 ILE 105 108 108 ILE ILE A . n 
A 1 106 LEU 106 109 109 LEU LEU A . n 
A 1 107 ALA 107 110 110 ALA ALA A . n 
A 1 108 LEU 108 111 111 LEU LEU A . n 
A 1 109 VAL 109 112 112 VAL VAL A . n 
A 1 110 GLY 110 113 113 GLY GLY A . n 
A 1 111 ALA 111 114 114 ALA ALA A . n 
A 1 112 ASP 112 115 115 ASP ASP A . n 
A 1 113 GLY 113 116 116 GLY GLY A . n 
A 1 114 ILE 114 117 117 ILE ILE A . n 
A 1 115 MET 115 118 118 MET MET A . n 
A 1 116 ILE 116 119 119 ILE ILE A . n 
A 1 117 GLY 117 120 120 GLY GLY A . n 
A 1 118 THR 118 121 121 THR THR A . n 
A 1 119 GLY 119 122 122 GLY GLY A . n 
A 1 120 LEU 120 123 123 LEU LEU A . n 
A 1 121 VAL 121 124 124 VAL VAL A . n 
A 1 122 GLY 122 125 125 GLY GLY A . n 
A 1 123 ALA 123 126 126 ALA ALA A . n 
A 1 124 LEU 124 127 127 LEU LEU A . n 
A 1 125 THR 125 128 128 THR THR A . n 
A 1 126 LYS 126 129 129 LYS LYS A . n 
A 1 127 VAL 127 130 130 VAL VAL A . n 
A 1 128 TYR 128 131 131 TYR TYR A . n 
A 1 129 SER 129 132 132 SER SER A . n 
A 1 130 TYR 130 133 133 TYR TYR A . n 
A 1 131 ARG 131 134 134 ARG ARG A . n 
A 1 132 PHE 132 135 135 PHE PHE A . n 
A 1 133 VAL 133 136 136 VAL VAL A . n 
A 1 134 TRP 134 137 137 TRP TRP A . n 
A 1 135 TRP 135 138 138 TRP TRP A . n 
A 1 136 ALA 136 139 139 ALA ALA A . n 
A 1 137 ILE 137 140 140 ILE ILE A . n 
A 1 138 SER 138 141 141 SER SER A . n 
A 1 139 THR 139 142 142 THR THR A . n 
A 1 140 ALA 140 143 143 ALA ALA A . n 
A 1 141 ALA 141 144 144 ALA ALA A . n 
A 1 142 MET 142 145 145 MET MET A . n 
A 1 143 LEU 143 146 146 LEU LEU A . n 
A 1 144 TYR 144 147 147 TYR TYR A . n 
A 1 145 ILE 145 148 148 ILE ILE A . n 
A 1 146 LEU 146 149 149 LEU LEU A . n 
A 1 147 TYR 147 150 150 TYR TYR A . n 
A 1 148 VAL 148 151 151 VAL VAL A . n 
A 1 149 LEU 149 152 152 LEU LEU A . n 
A 1 150 PHE 150 153 153 PHE PHE A . n 
A 1 151 PHE 151 154 154 PHE PHE A . n 
A 1 152 GLY 152 155 155 GLY GLY A . n 
A 1 153 PHE 153 156 156 PHE PHE A . n 
A 1 154 THR 154 157 157 THR THR A . n 
A 1 155 SER 155 158 158 SER SER A . n 
A 1 156 LYS 156 159 159 LYS LYS A . n 
A 1 157 ALA 157 160 160 ALA ALA A . n 
A 1 158 GLU 158 161 161 GLU GLU A . n 
A 1 159 SER 159 162 162 SER SER A . n 
A 1 160 MET 160 163 163 MET MET A . n 
A 1 161 ARG 161 164 164 ARG ARG A . n 
A 1 162 PRO 162 165 165 PRO PRO A . n 
A 1 163 GLU 163 166 166 GLU GLU A . n 
A 1 164 VAL 164 167 167 VAL VAL A . n 
A 1 165 ALA 165 168 168 ALA ALA A . n 
A 1 166 SER 166 169 169 SER SER A . n 
A 1 167 THR 167 170 170 THR THR A . n 
A 1 168 PHE 168 171 171 PHE PHE A . n 
A 1 169 LYS 169 172 172 LYS LYS A . n 
A 1 170 VAL 170 173 173 VAL VAL A . n 
A 1 171 LEU 171 174 174 LEU LEU A . n 
A 1 172 ARG 172 175 175 ARG ARG A . n 
A 1 173 ASN 173 176 176 ASN ASN A . n 
A 1 174 VAL 174 177 177 VAL VAL A . n 
A 1 175 THR 175 178 178 THR THR A . n 
A 1 176 VAL 176 179 179 VAL VAL A . n 
A 1 177 VAL 177 180 180 VAL VAL A . n 
A 1 178 LEU 178 181 181 LEU LEU A . n 
A 1 179 TRP 179 182 182 TRP TRP A . n 
A 1 180 SER 180 183 183 SER SER A . n 
A 1 181 ALA 181 184 184 ALA ALA A . n 
A 1 182 TYR 182 185 185 TYR TYR A . n 
A 1 183 PRO 183 186 186 PRO PRO A . n 
A 1 184 VAL 184 187 187 VAL VAL A . n 
A 1 185 VAL 185 188 188 VAL VAL A . n 
A 1 186 TRP 186 189 189 TRP TRP A . n 
A 1 187 LEU 187 190 190 LEU LEU A . n 
A 1 188 ILE 188 191 191 ILE ILE A . n 
A 1 189 GLY 189 192 192 GLY GLY A . n 
A 1 190 SER 190 193 193 SER SER A . n 
A 1 191 GLU 191 194 194 GLU GLU A . n 
A 1 192 GLY 192 195 195 GLY GLY A . n 
A 1 193 ALA 193 196 196 ALA ALA A . n 
A 1 194 GLY 194 197 197 GLY GLY A . n 
A 1 195 ILE 195 198 198 ILE ILE A . n 
A 1 196 VAL 196 199 199 VAL VAL A . n 
A 1 197 PRO 197 200 200 PRO PRO A . n 
A 1 198 LEU 198 201 201 LEU LEU A . n 
A 1 199 ASN 199 202 202 ASN ASN A . n 
A 1 200 ILE 200 203 203 ILE ILE A . n 
A 1 201 GLU 201 204 204 GLU GLU A . n 
A 1 202 THR 202 205 205 THR THR A . n 
A 1 203 LEU 203 206 206 LEU LEU A . n 
A 1 204 LEU 204 207 207 LEU LEU A . n 
A 1 205 PHE 205 208 208 PHE PHE A . n 
A 1 206 MET 206 209 209 MET MET A . n 
A 1 207 VAL 207 210 210 VAL VAL A . n 
A 1 208 LEU 208 211 211 LEU LEU A . n 
A 1 209 ASP 209 212 212 ASP ASP A . n 
A 1 210 VAL 210 213 213 VAL VAL A . n 
A 1 211 SER 211 214 214 SER SER A . n 
A 1 212 ALA 212 215 215 ALA ALA A . n 
A 1 213 LYS 213 216 216 LYS LYR A . n 
A 1 214 VAL 214 217 217 VAL VAL A . n 
A 1 215 GLY 215 218 218 GLY GLY A . n 
A 1 216 PHE 216 219 219 PHE PHE A . n 
A 1 217 GLY 217 220 220 GLY GLY A . n 
A 1 218 LEU 218 221 221 LEU LEU A . n 
A 1 219 ILE 219 222 222 ILE ILE A . n 
A 1 220 LEU 220 223 223 LEU LEU A . n 
A 1 221 LEU 221 224 224 LEU LEU A . n 
A 1 222 ARG 222 225 225 ARG ARG A . n 
A 1 223 SER 223 226 226 SER SER A . n 
A 1 224 ARG 224 227 227 ARG ARG A . n 
A 1 225 ALA 225 228 228 ALA ALA A . n 
A 1 226 ILE 226 229 229 ILE ILE A . n 
A 1 227 PHE 227 230 230 PHE PHE A . n 
A 1 228 GLY 228 231 231 GLY GLY A . n 
A 1 229 GLU 229 232 232 GLU GLU A . n 
A 1 230 ALA 230 233 233 ALA ALA A . n 
A 1 231 GLU 231 234 234 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RET 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RET 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 LI1 1  301 303 LI1 LI1 A . 
C 2 LI1 1  302 305 LI1 LI1 A . 
D 2 LI1 1  303 306 LI1 LI1 A . 
E 2 LI1 1  304 307 LI1 LI1 A . 
F 2 LI1 1  305 308 LI1 LI1 A . 
G 3 OLC 1  306 309 OLC OLC A . 
H 3 OLC 1  307 310 OLC OLC A . 
I 3 OLC 1  308 312 OLC OLC A . 
J 3 OLC 1  309 313 OLC OLC A . 
K 3 OLC 1  310 314 OLC OLC A . 
L 2 LI1 1  311 316 LI1 LI1 A . 
M 2 LI1 1  312 317 LI1 LI1 A . 
N 2 LI1 1  313 318 LI1 LI1 A . 
O 2 LI1 1  314 319 LI1 LI1 A . 
P 2 LI1 1  315 320 LI1 LI1 A . 
Q 2 LI1 1  316 321 LI1 LI1 A . 
R 2 LI1 1  317 322 LI1 LI1 A . 
S 4 RET 1  318 216 RET LYR A . 
T 5 HOH 1  401 432 HOH HOH A . 
T 5 HOH 2  402 482 HOH HOH A . 
T 5 HOH 3  403 441 HOH HOH A . 
T 5 HOH 4  404 504 HOH HOH A . 
T 5 HOH 5  405 500 HOH HOH A . 
T 5 HOH 6  406 402 HOH HOH A . 
T 5 HOH 7  407 480 HOH HOH A . 
T 5 HOH 8  408 434 HOH HOH A . 
T 5 HOH 9  409 400 HOH HOH A . 
T 5 HOH 10 410 404 HOH HOH A . 
T 5 HOH 11 411 403 HOH HOH A . 
T 5 HOH 12 412 485 HOH HOH A . 
T 5 HOH 13 413 423 HOH HOH A . 
T 5 HOH 14 414 456 HOH HOH A . 
T 5 HOH 15 415 477 HOH HOH A . 
T 5 HOH 16 416 401 HOH HOH A . 
T 5 HOH 17 417 489 HOH HOH A . 
T 5 HOH 18 418 407 HOH HOH A . 
T 5 HOH 19 419 414 HOH HOH A . 
T 5 HOH 20 420 412 HOH HOH A . 
T 5 HOH 21 421 479 HOH HOH A . 
T 5 HOH 22 422 421 HOH HOH A . 
T 5 HOH 23 423 505 HOH HOH A . 
T 5 HOH 24 424 501 HOH HOH A . 
T 5 HOH 25 425 417 HOH HOH A . 
T 5 HOH 26 426 502 HOH HOH A . 
T 5 HOH 27 427 411 HOH HOH A . 
T 5 HOH 28 428 409 HOH HOH A . 
T 5 HOH 29 429 426 HOH HOH A . 
T 5 HOH 30 430 416 HOH HOH A . 
T 5 HOH 31 431 415 HOH HOH A . 
T 5 HOH 32 432 418 HOH HOH A . 
T 5 HOH 33 433 419 HOH HOH A . 
T 5 HOH 34 434 499 HOH HOH A . 
T 5 HOH 35 435 420 HOH HOH A . 
T 5 HOH 36 436 413 HOH HOH A . 
T 5 HOH 37 437 422 HOH HOH A . 
T 5 HOH 38 438 475 HOH HOH A . 
T 5 HOH 39 439 478 HOH HOH A . 
T 5 HOH 40 440 490 HOH HOH A . 
T 5 HOH 41 441 496 HOH HOH A . 
T 5 HOH 42 442 498 HOH HOH A . 
T 5 HOH 43 443 506 HOH HOH A . 
T 5 HOH 44 444 484 HOH HOH A . 
T 5 HOH 45 445 476 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 74  ? CG  ? A GLU 71  CG  
2   1 Y 1 A GLU 74  ? CD  ? A GLU 71  CD  
3   1 Y 1 A GLU 74  ? OE1 ? A GLU 71  OE1 
4   1 Y 1 A GLU 74  ? OE2 ? A GLU 71  OE2 
5   1 Y 1 A SER 158 ? OG  ? A SER 155 OG  
6   1 Y 1 A LYS 172 ? CG  ? A LYS 169 CG  
7   1 Y 1 A LYS 172 ? CD  ? A LYS 169 CD  
8   1 Y 1 A LYS 172 ? CE  ? A LYS 169 CE  
9   1 Y 1 A LYS 172 ? NZ  ? A LYS 169 NZ  
10  1 N 1 A LI1 301 ? C1  ? B LI1 1   C1  
11  1 N 1 A LI1 301 ? C2  ? B LI1 1   C2  
12  1 N 1 A LI1 301 ? C3  ? B LI1 1   C3  
13  1 N 1 A LI1 301 ? O1  ? B LI1 1   O1  
14  1 N 1 A LI1 301 ? O2  ? B LI1 1   O2  
15  1 N 1 A LI1 301 ? O3  ? B LI1 1   O3  
16  1 N 1 A LI1 301 ? C41 ? B LI1 1   C41 
17  1 N 1 A LI1 301 ? C42 ? B LI1 1   C42 
18  1 N 1 A LI1 301 ? C43 ? B LI1 1   C43 
19  1 N 1 A LI1 301 ? C44 ? B LI1 1   C44 
20  1 N 1 A LI1 301 ? C45 ? B LI1 1   C45 
21  1 N 1 A LI1 301 ? C11 ? B LI1 1   C11 
22  1 N 1 A LI1 301 ? C12 ? B LI1 1   C12 
23  1 N 1 A LI1 301 ? C13 ? B LI1 1   C13 
24  1 N 1 A LI1 301 ? C14 ? B LI1 1   C14 
25  1 N 1 A LI1 301 ? C15 ? B LI1 1   C15 
26  1 N 1 A LI1 301 ? C16 ? B LI1 1   C16 
27  1 N 1 A LI1 301 ? C17 ? B LI1 1   C17 
28  1 N 1 A LI1 301 ? C18 ? B LI1 1   C18 
29  1 N 1 A LI1 301 ? C19 ? B LI1 1   C19 
30  1 N 1 A LI1 301 ? C20 ? B LI1 1   C20 
31  1 N 1 A LI1 301 ? C21 ? B LI1 1   C21 
32  1 N 1 A LI1 301 ? C22 ? B LI1 1   C22 
33  1 N 1 A LI1 301 ? C23 ? B LI1 1   C23 
34  1 N 1 A LI1 301 ? C24 ? B LI1 1   C24 
35  1 N 1 A LI1 301 ? C25 ? B LI1 1   C25 
36  1 N 1 A LI1 301 ? C26 ? B LI1 1   C26 
37  1 N 1 A LI1 301 ? C27 ? B LI1 1   C27 
38  1 N 1 A LI1 301 ? C28 ? B LI1 1   C28 
39  1 N 1 A LI1 301 ? C29 ? B LI1 1   C29 
40  1 N 1 A LI1 301 ? C30 ? B LI1 1   C30 
41  1 N 1 A LI1 302 ? C1  ? C LI1 1   C1  
42  1 N 1 A LI1 302 ? C2  ? C LI1 1   C2  
43  1 N 1 A LI1 302 ? C3  ? C LI1 1   C3  
44  1 N 1 A LI1 302 ? O1  ? C LI1 1   O1  
45  1 N 1 A LI1 302 ? O2  ? C LI1 1   O2  
46  1 N 1 A LI1 302 ? O3  ? C LI1 1   O3  
47  1 N 1 A LI1 302 ? C41 ? C LI1 1   C41 
48  1 N 1 A LI1 302 ? C42 ? C LI1 1   C42 
49  1 N 1 A LI1 302 ? C43 ? C LI1 1   C43 
50  1 N 1 A LI1 302 ? C44 ? C LI1 1   C44 
51  1 N 1 A LI1 302 ? C45 ? C LI1 1   C45 
52  1 N 1 A LI1 302 ? C46 ? C LI1 1   C46 
53  1 N 1 A LI1 302 ? C47 ? C LI1 1   C47 
54  1 N 1 A LI1 302 ? C48 ? C LI1 1   C48 
55  1 N 1 A LI1 302 ? C49 ? C LI1 1   C49 
56  1 N 1 A LI1 302 ? C59 ? C LI1 1   C59 
57  1 N 1 A LI1 302 ? C60 ? C LI1 1   C60 
58  1 N 1 A LI1 302 ? C11 ? C LI1 1   C11 
59  1 N 1 A LI1 302 ? C12 ? C LI1 1   C12 
60  1 N 1 A LI1 302 ? C13 ? C LI1 1   C13 
61  1 N 1 A LI1 302 ? C14 ? C LI1 1   C14 
62  1 N 1 A LI1 302 ? C15 ? C LI1 1   C15 
63  1 N 1 A LI1 302 ? C16 ? C LI1 1   C16 
64  1 N 1 A LI1 302 ? C17 ? C LI1 1   C17 
65  1 N 1 A LI1 302 ? C18 ? C LI1 1   C18 
66  1 N 1 A LI1 302 ? C19 ? C LI1 1   C19 
67  1 N 1 A LI1 302 ? C20 ? C LI1 1   C20 
68  1 N 1 A LI1 302 ? C21 ? C LI1 1   C21 
69  1 N 1 A LI1 302 ? C22 ? C LI1 1   C22 
70  1 N 1 A LI1 302 ? C23 ? C LI1 1   C23 
71  1 N 1 A LI1 302 ? C24 ? C LI1 1   C24 
72  1 N 1 A LI1 302 ? C25 ? C LI1 1   C25 
73  1 N 1 A LI1 302 ? C26 ? C LI1 1   C26 
74  1 N 1 A LI1 302 ? C27 ? C LI1 1   C27 
75  1 N 1 A LI1 302 ? C28 ? C LI1 1   C28 
76  1 N 1 A LI1 302 ? C29 ? C LI1 1   C29 
77  1 N 1 A LI1 302 ? C30 ? C LI1 1   C30 
78  1 N 1 A LI1 303 ? C1  ? D LI1 1   C1  
79  1 N 1 A LI1 303 ? C2  ? D LI1 1   C2  
80  1 N 1 A LI1 303 ? C3  ? D LI1 1   C3  
81  1 N 1 A LI1 303 ? O1  ? D LI1 1   O1  
82  1 N 1 A LI1 303 ? O2  ? D LI1 1   O2  
83  1 N 1 A LI1 303 ? O3  ? D LI1 1   O3  
84  1 N 1 A LI1 303 ? C41 ? D LI1 1   C41 
85  1 N 1 A LI1 303 ? C42 ? D LI1 1   C42 
86  1 N 1 A LI1 303 ? C43 ? D LI1 1   C43 
87  1 N 1 A LI1 303 ? C44 ? D LI1 1   C44 
88  1 N 1 A LI1 303 ? C49 ? D LI1 1   C49 
89  1 N 1 A LI1 303 ? C59 ? D LI1 1   C59 
90  1 N 1 A LI1 303 ? C60 ? D LI1 1   C60 
91  1 N 1 A LI1 303 ? C11 ? D LI1 1   C11 
92  1 N 1 A LI1 303 ? C12 ? D LI1 1   C12 
93  1 N 1 A LI1 303 ? C13 ? D LI1 1   C13 
94  1 N 1 A LI1 303 ? C14 ? D LI1 1   C14 
95  1 N 1 A LI1 303 ? C15 ? D LI1 1   C15 
96  1 N 1 A LI1 303 ? C16 ? D LI1 1   C16 
97  1 N 1 A LI1 303 ? C17 ? D LI1 1   C17 
98  1 N 1 A LI1 303 ? C18 ? D LI1 1   C18 
99  1 N 1 A LI1 303 ? C19 ? D LI1 1   C19 
100 1 N 1 A LI1 303 ? C20 ? D LI1 1   C20 
101 1 N 1 A LI1 303 ? C21 ? D LI1 1   C21 
102 1 N 1 A LI1 303 ? C22 ? D LI1 1   C22 
103 1 N 1 A LI1 303 ? C23 ? D LI1 1   C23 
104 1 N 1 A LI1 303 ? C24 ? D LI1 1   C24 
105 1 N 1 A LI1 303 ? C25 ? D LI1 1   C25 
106 1 N 1 A LI1 303 ? C26 ? D LI1 1   C26 
107 1 N 1 A LI1 303 ? C27 ? D LI1 1   C27 
108 1 N 1 A LI1 303 ? C28 ? D LI1 1   C28 
109 1 N 1 A LI1 303 ? C29 ? D LI1 1   C29 
110 1 N 1 A LI1 303 ? C30 ? D LI1 1   C30 
111 1 N 1 A LI1 304 ? C1  ? E LI1 1   C1  
112 1 N 1 A LI1 304 ? C2  ? E LI1 1   C2  
113 1 N 1 A LI1 304 ? C3  ? E LI1 1   C3  
114 1 N 1 A LI1 304 ? O1  ? E LI1 1   O1  
115 1 N 1 A LI1 304 ? O2  ? E LI1 1   O2  
116 1 N 1 A LI1 304 ? O3  ? E LI1 1   O3  
117 1 N 1 A LI1 304 ? C41 ? E LI1 1   C41 
118 1 N 1 A LI1 304 ? C42 ? E LI1 1   C42 
119 1 N 1 A LI1 304 ? C43 ? E LI1 1   C43 
120 1 N 1 A LI1 304 ? C44 ? E LI1 1   C44 
121 1 N 1 A LI1 304 ? C49 ? E LI1 1   C49 
122 1 N 1 A LI1 304 ? C60 ? E LI1 1   C60 
123 1 N 1 A LI1 304 ? C11 ? E LI1 1   C11 
124 1 N 1 A LI1 304 ? C12 ? E LI1 1   C12 
125 1 N 1 A LI1 304 ? C13 ? E LI1 1   C13 
126 1 N 1 A LI1 304 ? C14 ? E LI1 1   C14 
127 1 N 1 A LI1 304 ? C15 ? E LI1 1   C15 
128 1 N 1 A LI1 304 ? C16 ? E LI1 1   C16 
129 1 N 1 A LI1 304 ? C17 ? E LI1 1   C17 
130 1 N 1 A LI1 304 ? C18 ? E LI1 1   C18 
131 1 N 1 A LI1 304 ? C19 ? E LI1 1   C19 
132 1 N 1 A LI1 304 ? C20 ? E LI1 1   C20 
133 1 N 1 A LI1 304 ? C21 ? E LI1 1   C21 
134 1 N 1 A LI1 304 ? C22 ? E LI1 1   C22 
135 1 N 1 A LI1 304 ? C23 ? E LI1 1   C23 
136 1 N 1 A LI1 304 ? C24 ? E LI1 1   C24 
137 1 N 1 A LI1 304 ? C25 ? E LI1 1   C25 
138 1 N 1 A LI1 304 ? C26 ? E LI1 1   C26 
139 1 N 1 A LI1 304 ? C27 ? E LI1 1   C27 
140 1 N 1 A LI1 304 ? C28 ? E LI1 1   C28 
141 1 N 1 A LI1 304 ? C29 ? E LI1 1   C29 
142 1 N 1 A LI1 304 ? C30 ? E LI1 1   C30 
143 1 N 1 A LI1 305 ? C1  ? F LI1 1   C1  
144 1 N 1 A LI1 305 ? C2  ? F LI1 1   C2  
145 1 N 1 A LI1 305 ? C3  ? F LI1 1   C3  
146 1 N 1 A LI1 305 ? O1  ? F LI1 1   O1  
147 1 N 1 A LI1 305 ? O2  ? F LI1 1   O2  
148 1 N 1 A LI1 305 ? O3  ? F LI1 1   O3  
149 1 N 1 A LI1 305 ? C41 ? F LI1 1   C41 
150 1 N 1 A LI1 305 ? C42 ? F LI1 1   C42 
151 1 N 1 A LI1 305 ? C43 ? F LI1 1   C43 
152 1 N 1 A LI1 305 ? C44 ? F LI1 1   C44 
153 1 N 1 A LI1 305 ? C45 ? F LI1 1   C45 
154 1 N 1 A LI1 305 ? C49 ? F LI1 1   C49 
155 1 N 1 A LI1 305 ? C11 ? F LI1 1   C11 
156 1 N 1 A LI1 305 ? C12 ? F LI1 1   C12 
157 1 N 1 A LI1 305 ? C13 ? F LI1 1   C13 
158 1 N 1 A LI1 305 ? C14 ? F LI1 1   C14 
159 1 N 1 A LI1 305 ? C15 ? F LI1 1   C15 
160 1 N 1 A LI1 305 ? C16 ? F LI1 1   C16 
161 1 N 1 A LI1 305 ? C17 ? F LI1 1   C17 
162 1 N 1 A LI1 305 ? C18 ? F LI1 1   C18 
163 1 N 1 A LI1 305 ? C19 ? F LI1 1   C19 
164 1 N 1 A LI1 305 ? C20 ? F LI1 1   C20 
165 1 N 1 A LI1 305 ? C21 ? F LI1 1   C21 
166 1 N 1 A LI1 305 ? C22 ? F LI1 1   C22 
167 1 N 1 A LI1 305 ? C23 ? F LI1 1   C23 
168 1 N 1 A LI1 305 ? C24 ? F LI1 1   C24 
169 1 N 1 A LI1 305 ? C25 ? F LI1 1   C25 
170 1 N 1 A LI1 305 ? C26 ? F LI1 1   C26 
171 1 N 1 A LI1 305 ? C27 ? F LI1 1   C27 
172 1 N 1 A LI1 305 ? C28 ? F LI1 1   C28 
173 1 N 1 A LI1 305 ? C29 ? F LI1 1   C29 
174 1 N 1 A LI1 305 ? C30 ? F LI1 1   C30 
175 1 N 1 A LI1 311 ? C1  ? L LI1 1   C1  
176 1 N 1 A LI1 311 ? C2  ? L LI1 1   C2  
177 1 N 1 A LI1 311 ? C3  ? L LI1 1   C3  
178 1 N 1 A LI1 311 ? O1  ? L LI1 1   O1  
179 1 N 1 A LI1 311 ? O2  ? L LI1 1   O2  
180 1 N 1 A LI1 311 ? O3  ? L LI1 1   O3  
181 1 N 1 A LI1 311 ? C41 ? L LI1 1   C41 
182 1 N 1 A LI1 311 ? C42 ? L LI1 1   C42 
183 1 N 1 A LI1 311 ? C43 ? L LI1 1   C43 
184 1 N 1 A LI1 311 ? C44 ? L LI1 1   C44 
185 1 N 1 A LI1 311 ? C49 ? L LI1 1   C49 
186 1 N 1 A LI1 311 ? C57 ? L LI1 1   C57 
187 1 N 1 A LI1 311 ? C58 ? L LI1 1   C58 
188 1 N 1 A LI1 311 ? C59 ? L LI1 1   C59 
189 1 N 1 A LI1 311 ? C60 ? L LI1 1   C60 
190 1 N 1 A LI1 311 ? C11 ? L LI1 1   C11 
191 1 N 1 A LI1 311 ? C12 ? L LI1 1   C12 
192 1 N 1 A LI1 311 ? C13 ? L LI1 1   C13 
193 1 N 1 A LI1 311 ? C14 ? L LI1 1   C14 
194 1 N 1 A LI1 311 ? C15 ? L LI1 1   C15 
195 1 N 1 A LI1 311 ? C16 ? L LI1 1   C16 
196 1 N 1 A LI1 311 ? C17 ? L LI1 1   C17 
197 1 N 1 A LI1 311 ? C18 ? L LI1 1   C18 
198 1 N 1 A LI1 311 ? C19 ? L LI1 1   C19 
199 1 N 1 A LI1 311 ? C20 ? L LI1 1   C20 
200 1 N 1 A LI1 311 ? C21 ? L LI1 1   C21 
201 1 N 1 A LI1 311 ? C22 ? L LI1 1   C22 
202 1 N 1 A LI1 311 ? C23 ? L LI1 1   C23 
203 1 N 1 A LI1 311 ? C24 ? L LI1 1   C24 
204 1 N 1 A LI1 311 ? C25 ? L LI1 1   C25 
205 1 N 1 A LI1 311 ? C26 ? L LI1 1   C26 
206 1 N 1 A LI1 311 ? C27 ? L LI1 1   C27 
207 1 N 1 A LI1 311 ? C28 ? L LI1 1   C28 
208 1 N 1 A LI1 311 ? C29 ? L LI1 1   C29 
209 1 N 1 A LI1 311 ? C30 ? L LI1 1   C30 
210 1 N 1 A LI1 312 ? C1  ? M LI1 1   C1  
211 1 N 1 A LI1 312 ? C2  ? M LI1 1   C2  
212 1 N 1 A LI1 312 ? C3  ? M LI1 1   C3  
213 1 N 1 A LI1 312 ? O1  ? M LI1 1   O1  
214 1 N 1 A LI1 312 ? O2  ? M LI1 1   O2  
215 1 N 1 A LI1 312 ? O3  ? M LI1 1   O3  
216 1 N 1 A LI1 312 ? C41 ? M LI1 1   C41 
217 1 N 1 A LI1 312 ? C42 ? M LI1 1   C42 
218 1 N 1 A LI1 312 ? C43 ? M LI1 1   C43 
219 1 N 1 A LI1 312 ? C44 ? M LI1 1   C44 
220 1 N 1 A LI1 312 ? C49 ? M LI1 1   C49 
221 1 N 1 A LI1 312 ? C60 ? M LI1 1   C60 
222 1 N 1 A LI1 312 ? C11 ? M LI1 1   C11 
223 1 N 1 A LI1 312 ? C12 ? M LI1 1   C12 
224 1 N 1 A LI1 312 ? C13 ? M LI1 1   C13 
225 1 N 1 A LI1 312 ? C14 ? M LI1 1   C14 
226 1 N 1 A LI1 312 ? C15 ? M LI1 1   C15 
227 1 N 1 A LI1 312 ? C16 ? M LI1 1   C16 
228 1 N 1 A LI1 312 ? C17 ? M LI1 1   C17 
229 1 N 1 A LI1 312 ? C18 ? M LI1 1   C18 
230 1 N 1 A LI1 312 ? C19 ? M LI1 1   C19 
231 1 N 1 A LI1 312 ? C20 ? M LI1 1   C20 
232 1 N 1 A LI1 312 ? C21 ? M LI1 1   C21 
233 1 N 1 A LI1 312 ? C22 ? M LI1 1   C22 
234 1 N 1 A LI1 312 ? C23 ? M LI1 1   C23 
235 1 N 1 A LI1 312 ? C24 ? M LI1 1   C24 
236 1 N 1 A LI1 312 ? C25 ? M LI1 1   C25 
237 1 N 1 A LI1 312 ? C26 ? M LI1 1   C26 
238 1 N 1 A LI1 312 ? C27 ? M LI1 1   C27 
239 1 N 1 A LI1 312 ? C28 ? M LI1 1   C28 
240 1 N 1 A LI1 312 ? C29 ? M LI1 1   C29 
241 1 N 1 A LI1 312 ? C30 ? M LI1 1   C30 
242 1 N 1 A LI1 313 ? C1  ? N LI1 1   C1  
243 1 N 1 A LI1 313 ? C2  ? N LI1 1   C2  
244 1 N 1 A LI1 313 ? C3  ? N LI1 1   C3  
245 1 N 1 A LI1 313 ? O1  ? N LI1 1   O1  
246 1 N 1 A LI1 313 ? O2  ? N LI1 1   O2  
247 1 N 1 A LI1 313 ? O3  ? N LI1 1   O3  
248 1 N 1 A LI1 313 ? C41 ? N LI1 1   C41 
249 1 N 1 A LI1 313 ? C42 ? N LI1 1   C42 
250 1 N 1 A LI1 313 ? C43 ? N LI1 1   C43 
251 1 N 1 A LI1 313 ? C44 ? N LI1 1   C44 
252 1 N 1 A LI1 313 ? C45 ? N LI1 1   C45 
253 1 N 1 A LI1 313 ? C46 ? N LI1 1   C46 
254 1 N 1 A LI1 313 ? C47 ? N LI1 1   C47 
255 1 N 1 A LI1 313 ? C48 ? N LI1 1   C48 
256 1 N 1 A LI1 313 ? C49 ? N LI1 1   C49 
257 1 N 1 A LI1 313 ? C59 ? N LI1 1   C59 
258 1 N 1 A LI1 313 ? C60 ? N LI1 1   C60 
259 1 N 1 A LI1 313 ? C11 ? N LI1 1   C11 
260 1 N 1 A LI1 313 ? C12 ? N LI1 1   C12 
261 1 N 1 A LI1 313 ? C13 ? N LI1 1   C13 
262 1 N 1 A LI1 313 ? C14 ? N LI1 1   C14 
263 1 N 1 A LI1 313 ? C15 ? N LI1 1   C15 
264 1 N 1 A LI1 313 ? C16 ? N LI1 1   C16 
265 1 N 1 A LI1 313 ? C17 ? N LI1 1   C17 
266 1 N 1 A LI1 313 ? C18 ? N LI1 1   C18 
267 1 N 1 A LI1 313 ? C19 ? N LI1 1   C19 
268 1 N 1 A LI1 313 ? C20 ? N LI1 1   C20 
269 1 N 1 A LI1 313 ? C21 ? N LI1 1   C21 
270 1 N 1 A LI1 313 ? C22 ? N LI1 1   C22 
271 1 N 1 A LI1 313 ? C23 ? N LI1 1   C23 
272 1 N 1 A LI1 313 ? C24 ? N LI1 1   C24 
273 1 N 1 A LI1 313 ? C25 ? N LI1 1   C25 
274 1 N 1 A LI1 313 ? C26 ? N LI1 1   C26 
275 1 N 1 A LI1 313 ? C27 ? N LI1 1   C27 
276 1 N 1 A LI1 313 ? C28 ? N LI1 1   C28 
277 1 N 1 A LI1 313 ? C29 ? N LI1 1   C29 
278 1 N 1 A LI1 313 ? C30 ? N LI1 1   C30 
279 1 N 1 A LI1 314 ? C1  ? O LI1 1   C1  
280 1 N 1 A LI1 314 ? C2  ? O LI1 1   C2  
281 1 N 1 A LI1 314 ? C3  ? O LI1 1   C3  
282 1 N 1 A LI1 314 ? O1  ? O LI1 1   O1  
283 1 N 1 A LI1 314 ? O2  ? O LI1 1   O2  
284 1 N 1 A LI1 314 ? O3  ? O LI1 1   O3  
285 1 N 1 A LI1 314 ? C41 ? O LI1 1   C41 
286 1 N 1 A LI1 314 ? C42 ? O LI1 1   C42 
287 1 N 1 A LI1 314 ? C43 ? O LI1 1   C43 
288 1 N 1 A LI1 314 ? C44 ? O LI1 1   C44 
289 1 N 1 A LI1 314 ? C45 ? O LI1 1   C45 
290 1 N 1 A LI1 314 ? C49 ? O LI1 1   C49 
291 1 N 1 A LI1 314 ? C11 ? O LI1 1   C11 
292 1 N 1 A LI1 314 ? C12 ? O LI1 1   C12 
293 1 N 1 A LI1 314 ? C13 ? O LI1 1   C13 
294 1 N 1 A LI1 314 ? C14 ? O LI1 1   C14 
295 1 N 1 A LI1 314 ? C15 ? O LI1 1   C15 
296 1 N 1 A LI1 314 ? C16 ? O LI1 1   C16 
297 1 N 1 A LI1 314 ? C17 ? O LI1 1   C17 
298 1 N 1 A LI1 314 ? C18 ? O LI1 1   C18 
299 1 N 1 A LI1 314 ? C19 ? O LI1 1   C19 
300 1 N 1 A LI1 314 ? C20 ? O LI1 1   C20 
301 1 N 1 A LI1 314 ? C21 ? O LI1 1   C21 
302 1 N 1 A LI1 314 ? C22 ? O LI1 1   C22 
303 1 N 1 A LI1 314 ? C23 ? O LI1 1   C23 
304 1 N 1 A LI1 314 ? C24 ? O LI1 1   C24 
305 1 N 1 A LI1 314 ? C25 ? O LI1 1   C25 
306 1 N 1 A LI1 314 ? C26 ? O LI1 1   C26 
307 1 N 1 A LI1 314 ? C27 ? O LI1 1   C27 
308 1 N 1 A LI1 314 ? C28 ? O LI1 1   C28 
309 1 N 1 A LI1 314 ? C29 ? O LI1 1   C29 
310 1 N 1 A LI1 314 ? C30 ? O LI1 1   C30 
311 1 N 1 A LI1 315 ? C1  ? P LI1 1   C1  
312 1 N 1 A LI1 315 ? C2  ? P LI1 1   C2  
313 1 N 1 A LI1 315 ? C3  ? P LI1 1   C3  
314 1 N 1 A LI1 315 ? O1  ? P LI1 1   O1  
315 1 N 1 A LI1 315 ? O2  ? P LI1 1   O2  
316 1 N 1 A LI1 315 ? O3  ? P LI1 1   O3  
317 1 N 1 A LI1 315 ? C41 ? P LI1 1   C41 
318 1 N 1 A LI1 315 ? C42 ? P LI1 1   C42 
319 1 N 1 A LI1 315 ? C43 ? P LI1 1   C43 
320 1 N 1 A LI1 315 ? C44 ? P LI1 1   C44 
321 1 N 1 A LI1 315 ? C49 ? P LI1 1   C49 
322 1 N 1 A LI1 315 ? C60 ? P LI1 1   C60 
323 1 N 1 A LI1 315 ? C11 ? P LI1 1   C11 
324 1 N 1 A LI1 315 ? C12 ? P LI1 1   C12 
325 1 N 1 A LI1 315 ? C13 ? P LI1 1   C13 
326 1 N 1 A LI1 315 ? C14 ? P LI1 1   C14 
327 1 N 1 A LI1 315 ? C15 ? P LI1 1   C15 
328 1 N 1 A LI1 315 ? C16 ? P LI1 1   C16 
329 1 N 1 A LI1 315 ? C17 ? P LI1 1   C17 
330 1 N 1 A LI1 315 ? C18 ? P LI1 1   C18 
331 1 N 1 A LI1 315 ? C19 ? P LI1 1   C19 
332 1 N 1 A LI1 315 ? C20 ? P LI1 1   C20 
333 1 N 1 A LI1 315 ? C21 ? P LI1 1   C21 
334 1 N 1 A LI1 315 ? C22 ? P LI1 1   C22 
335 1 N 1 A LI1 315 ? C23 ? P LI1 1   C23 
336 1 N 1 A LI1 315 ? C24 ? P LI1 1   C24 
337 1 N 1 A LI1 315 ? C25 ? P LI1 1   C25 
338 1 N 1 A LI1 315 ? C26 ? P LI1 1   C26 
339 1 N 1 A LI1 315 ? C27 ? P LI1 1   C27 
340 1 N 1 A LI1 315 ? C28 ? P LI1 1   C28 
341 1 N 1 A LI1 315 ? C29 ? P LI1 1   C29 
342 1 N 1 A LI1 315 ? C30 ? P LI1 1   C30 
343 1 N 1 A LI1 316 ? C1  ? Q LI1 1   C1  
344 1 N 1 A LI1 316 ? C2  ? Q LI1 1   C2  
345 1 N 1 A LI1 316 ? C3  ? Q LI1 1   C3  
346 1 N 1 A LI1 316 ? O1  ? Q LI1 1   O1  
347 1 N 1 A LI1 316 ? O2  ? Q LI1 1   O2  
348 1 N 1 A LI1 316 ? O3  ? Q LI1 1   O3  
349 1 N 1 A LI1 316 ? C41 ? Q LI1 1   C41 
350 1 N 1 A LI1 316 ? C42 ? Q LI1 1   C42 
351 1 N 1 A LI1 316 ? C43 ? Q LI1 1   C43 
352 1 N 1 A LI1 316 ? C44 ? Q LI1 1   C44 
353 1 N 1 A LI1 316 ? C45 ? Q LI1 1   C45 
354 1 N 1 A LI1 316 ? C46 ? Q LI1 1   C46 
355 1 N 1 A LI1 316 ? C47 ? Q LI1 1   C47 
356 1 N 1 A LI1 316 ? C48 ? Q LI1 1   C48 
357 1 N 1 A LI1 316 ? C49 ? Q LI1 1   C49 
358 1 N 1 A LI1 316 ? C50 ? Q LI1 1   C50 
359 1 N 1 A LI1 316 ? C51 ? Q LI1 1   C51 
360 1 N 1 A LI1 316 ? C59 ? Q LI1 1   C59 
361 1 N 1 A LI1 316 ? C60 ? Q LI1 1   C60 
362 1 N 1 A LI1 316 ? C11 ? Q LI1 1   C11 
363 1 N 1 A LI1 316 ? C12 ? Q LI1 1   C12 
364 1 N 1 A LI1 316 ? C13 ? Q LI1 1   C13 
365 1 N 1 A LI1 316 ? C14 ? Q LI1 1   C14 
366 1 N 1 A LI1 316 ? C15 ? Q LI1 1   C15 
367 1 N 1 A LI1 316 ? C16 ? Q LI1 1   C16 
368 1 N 1 A LI1 316 ? C17 ? Q LI1 1   C17 
369 1 N 1 A LI1 316 ? C18 ? Q LI1 1   C18 
370 1 N 1 A LI1 316 ? C19 ? Q LI1 1   C19 
371 1 N 1 A LI1 316 ? C20 ? Q LI1 1   C20 
372 1 N 1 A LI1 316 ? C21 ? Q LI1 1   C21 
373 1 N 1 A LI1 316 ? C22 ? Q LI1 1   C22 
374 1 N 1 A LI1 316 ? C23 ? Q LI1 1   C23 
375 1 N 1 A LI1 316 ? C24 ? Q LI1 1   C24 
376 1 N 1 A LI1 316 ? C25 ? Q LI1 1   C25 
377 1 N 1 A LI1 316 ? C26 ? Q LI1 1   C26 
378 1 N 1 A LI1 316 ? C27 ? Q LI1 1   C27 
379 1 N 1 A LI1 316 ? C28 ? Q LI1 1   C28 
380 1 N 1 A LI1 316 ? C29 ? Q LI1 1   C29 
381 1 N 1 A LI1 316 ? C30 ? Q LI1 1   C30 
382 1 N 1 A LI1 317 ? C1  ? R LI1 1   C1  
383 1 N 1 A LI1 317 ? C2  ? R LI1 1   C2  
384 1 N 1 A LI1 317 ? C3  ? R LI1 1   C3  
385 1 N 1 A LI1 317 ? O1  ? R LI1 1   O1  
386 1 N 1 A LI1 317 ? O2  ? R LI1 1   O2  
387 1 N 1 A LI1 317 ? O3  ? R LI1 1   O3  
388 1 N 1 A LI1 317 ? C41 ? R LI1 1   C41 
389 1 N 1 A LI1 317 ? C42 ? R LI1 1   C42 
390 1 N 1 A LI1 317 ? C43 ? R LI1 1   C43 
391 1 N 1 A LI1 317 ? C44 ? R LI1 1   C44 
392 1 N 1 A LI1 317 ? C45 ? R LI1 1   C45 
393 1 N 1 A LI1 317 ? C11 ? R LI1 1   C11 
394 1 N 1 A LI1 317 ? C12 ? R LI1 1   C12 
395 1 N 1 A LI1 317 ? C13 ? R LI1 1   C13 
396 1 N 1 A LI1 317 ? C14 ? R LI1 1   C14 
397 1 N 1 A LI1 317 ? C15 ? R LI1 1   C15 
398 1 N 1 A LI1 317 ? C16 ? R LI1 1   C16 
399 1 N 1 A LI1 317 ? C17 ? R LI1 1   C17 
400 1 N 1 A LI1 317 ? C18 ? R LI1 1   C18 
401 1 N 1 A LI1 317 ? C19 ? R LI1 1   C19 
402 1 N 1 A LI1 317 ? C20 ? R LI1 1   C20 
403 1 N 1 A LI1 317 ? C21 ? R LI1 1   C21 
404 1 N 1 A LI1 317 ? C22 ? R LI1 1   C22 
405 1 N 1 A LI1 317 ? C23 ? R LI1 1   C23 
406 1 N 1 A LI1 317 ? C24 ? R LI1 1   C24 
407 1 N 1 A LI1 317 ? C25 ? R LI1 1   C25 
408 1 N 1 A LI1 317 ? C26 ? R LI1 1   C26 
409 1 N 1 A LI1 317 ? C27 ? R LI1 1   C27 
410 1 N 1 A LI1 317 ? C28 ? R LI1 1   C28 
411 1 N 1 A LI1 317 ? C29 ? R LI1 1   C29 
412 1 N 1 A LI1 317 ? C30 ? R LI1 1   C30 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.1              2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.1              3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F9I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.450 
_cell.length_a_esd                 ? 
_cell.length_b                     62.450 
_cell.length_b_esd                 ? 
_cell.length_c                     111.170 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F9I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F9I 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.85 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Na/K Phosphate buffer pH 5.6 30 % PEG 2000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MPCCD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.227 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.227 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL3 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F9I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               31.23 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     32843 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1944 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   0.0423 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.59 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.19 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3272 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  0.614 
_reflns_shell.pdbx_R_split                                  0.8581 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F9I 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             31.23 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     32349 
_refine.ls_number_reflns_R_free                  1994 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 6.16 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1518 
_refine.ls_R_factor_R_free                       0.1785 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1501 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.50 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        31.23 
_refine_hist.number_atoms_solvent             45 
_refine_hist.number_atoms_total               2101 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1794 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         262 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  ? 2147 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.182  ? 2853 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.746 ? 455  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.075  ? 312  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 335  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.64  . . 143 2166 100.00 . . . . 0.2698 . . . . . . . . . . . 0.2949 
'X-RAY DIFFRACTION' 1.64 1.68  . . 138 2165 100.00 . . . . 0.2469 . . . . . . . . . . . 0.2838 
'X-RAY DIFFRACTION' 1.68 1.73  . . 142 2151 100.00 . . . . 0.2175 . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 1.73 1.79  . . 143 2166 100.00 . . . . 0.1946 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 1.79 1.85  . . 137 2145 100.00 . . . . 0.1694 . . . . . . . . . . . 0.2345 
'X-RAY DIFFRACTION' 1.85 1.93  . . 139 2180 100.00 . . . . 0.1553 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 1.93 2.02  . . 142 2177 100.00 . . . . 0.1391 . . . . . . . . . . . 0.1741 
'X-RAY DIFFRACTION' 2.02 2.12  . . 143 2152 100.00 . . . . 0.1435 . . . . . . . . . . . 0.1531 
'X-RAY DIFFRACTION' 2.12 2.26  . . 139 2173 100.00 . . . . 0.1284 . . . . . . . . . . . 0.1570 
'X-RAY DIFFRACTION' 2.26 2.43  . . 142 2166 100.00 . . . . 0.1269 . . . . . . . . . . . 0.1675 
'X-RAY DIFFRACTION' 2.43 2.67  . . 149 2157 100.00 . . . . 0.1379 . . . . . . . . . . . 0.1655 
'X-RAY DIFFRACTION' 2.67 3.06  . . 141 2180 100.00 . . . . 0.1482 . . . . . . . . . . . 0.1433 
'X-RAY DIFFRACTION' 3.06 3.85  . . 144 2190 100.00 . . . . 0.1362 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 3.86 31.23 . . 152 2187 100.00 . . . . 0.1531 . . . . . . . . . . . 0.1824 
# 
_struct.entry_id                     9F9I 
_struct.title                        'Laser excitation effects on BR: Dark dataset recorded at SACLA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9F9I 
_struct_keywords.text            
'Bacteriorhodospin, Proton transport, Membrane, RETINAL, TIME-RESOLVED CRYSTALLOGRAPHY, SERIAL CRYSTALLOGRAPHY, Laser excitation' 
_struct_keywords.pdbx_keywords   'PROTON TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 4 ? 
T N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BACR_HALSA 
_struct_ref.pdbx_db_accession          P02945 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYA
DWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMR
PEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_struct_ref.pdbx_align_begin           18 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F9I 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 231 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02945 
_struct_ref_seq.db_align_beg                  18 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       5 
_struct_ref_seq.pdbx_auth_seq_align_end       234 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9F9I 
_struct_ref_seq_dif.mon_id                       GLY 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P02945 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            4 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3660  ? 
1 MORE         -54   ? 
1 'SSA (A^2)'  12780 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 6   ? GLY A 28  ? GLU A 9   GLY A 31  1 ? 23 
HELX_P HELX_P2 AA2 ASP A 33  ? LEU A 59  ? ASP A 36  LEU A 62  1 ? 27 
HELX_P HELX_P3 AA3 TRP A 77  ? VAL A 98  ? TRP A 80  VAL A 101 1 ? 22 
HELX_P HELX_P4 AA4 ASP A 101 ? THR A 125 ? ASP A 104 THR A 128 1 ? 25 
HELX_P HELX_P5 AA5 VAL A 127 ? GLY A 152 ? VAL A 130 GLY A 155 1 ? 26 
HELX_P HELX_P6 AA6 GLY A 152 ? GLU A 158 ? GLY A 155 GLU A 161 1 ? 7  
HELX_P HELX_P7 AA7 ARG A 161 ? GLY A 189 ? ARG A 164 GLY A 192 1 ? 29 
HELX_P HELX_P8 AA8 PRO A 197 ? ARG A 222 ? PRO A 200 ARG A 225 1 ? 26 
HELX_P HELX_P9 AA9 SER A 223 ? PHE A 227 ? SER A 226 PHE A 230 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            213 
_struct_conn.ptnr1_label_atom_id           NZ 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           S 
_struct_conn.ptnr2_label_comp_id           RET 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             216 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            RET 
_struct_conn.ptnr2_auth_seq_id             318 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.340 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      RET 
_pdbx_modification_feature.label_asym_id                      S 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     LYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      213 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       RET 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        318 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      LYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       216 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C15 
_pdbx_modification_feature.modified_residue_id_linking_atom   NZ 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        RET 
_pdbx_modification_feature.type                               Retinoylation 
_pdbx_modification_feature.category                           Lipid/lipid-like 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 64 ? PHE A 68 ? THR A 67 PHE A 71 
AA1 2 GLU A 71 ? ILE A 75 ? GLU A 74 ILE A 78 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   THR 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    64 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    THR 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     67 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    75 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     78 
# 
_pdbx_entry_details.entry_id                   9F9I 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A MET 32  ? ? O A HOH 401 ? ? 2.01 
2 1 OD2 A ASP 104 ? ? O A HOH 402 ? ? 2.11 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 23.6324 27.1637 29.8210 0.1365 ? 0.0317  ? -0.0037 ? 0.1870 ? -0.0265 ? 0.3009 ? 3.3649 ? 1.6116  
? -2.6252 ? 7.6121 ? -5.6777 ? 5.5236 ? -0.1306 ? 0.2160  ? -0.1499 ? -0.2990 ? -0.0159 ? -0.4376 ? 0.4068  ? 0.2210  ? 0.1825  ? 
2 'X-RAY DIFFRACTION' ? refined 15.2023 27.7280 41.1771 0.2603 ? 0.0165  ? -0.0281 ? 0.1918 ? 0.0422  ? 0.2479 ? 2.1506 ? -0.1371 
? -0.4883 ? 1.9459 ? 1.3648  ? 1.6420 ? -0.0448 ? -0.3433 ? -0.1319 ? 0.4420  ? 0.0475  ? -0.0390 ? 0.4377  ? -0.0979 ? 0.0231  ? 
3 'X-RAY DIFFRACTION' ? refined 12.6421 38.6794 28.6410 0.1870 ? 0.0064  ? -0.0126 ? 0.1998 ? 0.0115  ? 0.2102 ? 1.7658 ? -0.3199 
? -0.4327 ? 2.5235 ? 0.8175  ? 1.2457 ? 0.0315  ? 0.2269  ? 0.0066  ? -0.2937 ? 0.0089  ? -0.0338 ? -0.0568 ? -0.1485 ? -0.0411 ? 
4 'X-RAY DIFFRACTION' ? refined 7.5492  45.9376 37.1993 0.1827 ? 0.0189  ? -0.0300 ? 0.1706 ? 0.0003  ? 0.2293 ? 1.8349 ? 0.0335  
? -0.8751 ? 1.9448 ? -2.1844 ? 9.4067 ? 0.1292  ? -0.1443 ? 0.0203  ? 0.0793  ? 0.1904  ? 0.0487  ? 0.1003  ? -0.2312 ? -0.3491 ? 
5 'X-RAY DIFFRACTION' ? refined 13.1132 53.1879 32.8403 0.2045 ? -0.0218 ? -0.0031 ? 0.1755 ? -0.0087 ? 0.2579 ? 3.3206 ? 0.1092  
? 0.2860  ? 2.9818 ? -2.1129 ? 5.5728 ? 0.0900  ? -0.0250 ? 0.2335  ? 0.2464  ? -0.0845 ? -0.1232 ? -0.5131 ? 0.3949  ? 0.0463  ? 
6 'X-RAY DIFFRACTION' ? refined 17.7046 46.5209 57.7572 1.0671 ? 0.0340  ? -0.0482 ? 0.9261 ? -0.0708 ? 0.6843 ? 5.5475 ? -4.5446 
? 5.6198  ? 3.7842 ? -4.6330 ? 5.7085 ? -0.9621 ? -2.0321 ? 1.0497  ? 1.2310  ? 0.5732  ? -0.2086 ? -2.3035 ? -0.3161 ? 0.3793  ? 
7 'X-RAY DIFFRACTION' ? refined 22.9133 41.9897 35.2981 0.1930 ? -0.0315 ? -0.0441 ? 0.2375 ? -0.0073 ? 0.2877 ? 1.0925 ? -0.1151 
? -0.3664 ? 1.2176 ? -0.6359 ? 3.1333 ? -0.0150 ? -0.1189 ? 0.0581  ? 0.1894  ? 0.0404  ? -0.2686 ? -0.2669 ? 0.1377  ? -0.0292 ? 
8 'X-RAY DIFFRACTION' ? refined 23.7118 31.4564 55.2073 0.4537 ? 0.0195  ? -0.1802 ? 0.6644 ? 0.1561  ? 0.4891 ? 2.0002 ? 1.9389  
? -4.7916 ? 3.0935 ? -0.1200 ? 2.4753 ? -0.1115 ? -0.0355 ? -0.6387 ? 0.9720  ? -0.3657 ? -1.5042 ? 0.9438  ? 1.7200  ? 0.0005  ? 
9 'X-RAY DIFFRACTION' ? refined 19.0731 30.0620 64.7397 0.8047 ? -0.0769 ? -0.1386 ? 0.5389 ? 0.0678  ? 0.2152 ? 3.6886 ? -1.3440 
? 1.6924  ? 0.6396 ? -0.1636 ? 2.1366 ? 0.4566  ? -0.5697 ? -0.4377 ? 0.4034  ? -0.0154 ? 0.0059  ? 0.4772  ? -0.1632 ? -0.3105 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 4 through 30 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 31 through 62 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 63 through 100 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 101 through 130 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 131 through 154 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 155 through 164 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 165 through 224 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 225 through 229 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 230 through 234 )
;
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HOH O    O N N 123 
HOH H1   H N N 124 
HOH H2   H N N 125 
ILE N    N N N 126 
ILE CA   C N S 127 
ILE C    C N N 128 
ILE O    O N N 129 
ILE CB   C N S 130 
ILE CG1  C N N 131 
ILE CG2  C N N 132 
ILE CD1  C N N 133 
ILE OXT  O N N 134 
ILE H    H N N 135 
ILE H2   H N N 136 
ILE HA   H N N 137 
ILE HB   H N N 138 
ILE HG12 H N N 139 
ILE HG13 H N N 140 
ILE HG21 H N N 141 
ILE HG22 H N N 142 
ILE HG23 H N N 143 
ILE HD11 H N N 144 
ILE HD12 H N N 145 
ILE HD13 H N N 146 
ILE HXT  H N N 147 
LEU N    N N N 148 
LEU CA   C N S 149 
LEU C    C N N 150 
LEU O    O N N 151 
LEU CB   C N N 152 
LEU CG   C N N 153 
LEU CD1  C N N 154 
LEU CD2  C N N 155 
LEU OXT  O N N 156 
LEU H    H N N 157 
LEU H2   H N N 158 
LEU HA   H N N 159 
LEU HB2  H N N 160 
LEU HB3  H N N 161 
LEU HG   H N N 162 
LEU HD11 H N N 163 
LEU HD12 H N N 164 
LEU HD13 H N N 165 
LEU HD21 H N N 166 
LEU HD22 H N N 167 
LEU HD23 H N N 168 
LEU HXT  H N N 169 
LI1 C1   C N N 170 
LI1 C2   C N R 171 
LI1 C3   C N N 172 
LI1 O1   O N N 173 
LI1 O2   O N N 174 
LI1 O3   O N N 175 
LI1 C41  C N N 176 
LI1 C42  C N N 177 
LI1 C43  C N R 178 
LI1 C44  C N N 179 
LI1 C45  C N N 180 
LI1 C46  C N N 181 
LI1 C47  C N N 182 
LI1 C48  C N R 183 
LI1 C49  C N N 184 
LI1 C50  C N N 185 
LI1 C51  C N N 186 
LI1 C52  C N N 187 
LI1 C53  C N N 188 
LI1 C55  C N N 189 
LI1 C56  C N N 190 
LI1 C57  C N N 191 
LI1 C58  C N N 192 
LI1 C59  C N N 193 
LI1 C60  C N N 194 
LI1 C11  C N N 195 
LI1 C12  C N N 196 
LI1 C13  C N S 197 
LI1 C14  C N N 198 
LI1 C15  C N N 199 
LI1 C16  C N N 200 
LI1 C17  C N N 201 
LI1 C18  C N R 202 
LI1 C19  C N N 203 
LI1 C20  C N N 204 
LI1 C21  C N N 205 
LI1 C22  C N N 206 
LI1 C23  C N S 207 
LI1 C24  C N N 208 
LI1 C25  C N N 209 
LI1 C26  C N N 210 
LI1 C27  C N N 211 
LI1 C28  C N N 212 
LI1 C29  C N N 213 
LI1 C30  C N N 214 
LI1 H11  H N N 215 
LI1 H12  H N N 216 
LI1 H2   H N N 217 
LI1 H31  H N N 218 
LI1 H32  H N N 219 
LI1 HO3  H N N 220 
LI1 H411 H N N 221 
LI1 H412 H N N 222 
LI1 H421 H N N 223 
LI1 H422 H N N 224 
LI1 H43  H N N 225 
LI1 H441 H N N 226 
LI1 H442 H N N 227 
LI1 H443 H N N 228 
LI1 H451 H N N 229 
LI1 H452 H N N 230 
LI1 H461 H N N 231 
LI1 H462 H N N 232 
LI1 H471 H N N 233 
LI1 H472 H N N 234 
LI1 H48  H N N 235 
LI1 H491 H N N 236 
LI1 H492 H N N 237 
LI1 H493 H N N 238 
LI1 H501 H N N 239 
LI1 H502 H N N 240 
LI1 H511 H N N 241 
LI1 H512 H N N 242 
LI1 H521 H N N 243 
LI1 H522 H N N 244 
LI1 H531 H N N 245 
LI1 H532 H N N 246 
LI1 H551 H N N 247 
LI1 H552 H N N 248 
LI1 H561 H N N 249 
LI1 H562 H N N 250 
LI1 H571 H N N 251 
LI1 H572 H N N 252 
LI1 H58  H N N 253 
LI1 H591 H N N 254 
LI1 H592 H N N 255 
LI1 H593 H N N 256 
LI1 H601 H N N 257 
LI1 H602 H N N 258 
LI1 H603 H N N 259 
LI1 H111 H N N 260 
LI1 H112 H N N 261 
LI1 H121 H N N 262 
LI1 H122 H N N 263 
LI1 H13  H N N 264 
LI1 H141 H N N 265 
LI1 H142 H N N 266 
LI1 H143 H N N 267 
LI1 H151 H N N 268 
LI1 H152 H N N 269 
LI1 H161 H N N 270 
LI1 H162 H N N 271 
LI1 H171 H N N 272 
LI1 H172 H N N 273 
LI1 H18  H N N 274 
LI1 H191 H N N 275 
LI1 H192 H N N 276 
LI1 H193 H N N 277 
LI1 H201 H N N 278 
LI1 H202 H N N 279 
LI1 H211 H N N 280 
LI1 H212 H N N 281 
LI1 H221 H N N 282 
LI1 H222 H N N 283 
LI1 H23  H N N 284 
LI1 H241 H N N 285 
LI1 H242 H N N 286 
LI1 H243 H N N 287 
LI1 H251 H N N 288 
LI1 H252 H N N 289 
LI1 H261 H N N 290 
LI1 H262 H N N 291 
LI1 H271 H N N 292 
LI1 H272 H N N 293 
LI1 H28  H N N 294 
LI1 H291 H N N 295 
LI1 H292 H N N 296 
LI1 H293 H N N 297 
LI1 H301 H N N 298 
LI1 H302 H N N 299 
LI1 H303 H N N 300 
LYS N    N N N 301 
LYS CA   C N S 302 
LYS C    C N N 303 
LYS O    O N N 304 
LYS CB   C N N 305 
LYS CG   C N N 306 
LYS CD   C N N 307 
LYS CE   C N N 308 
LYS NZ   N N N 309 
LYS OXT  O N N 310 
LYS H    H N N 311 
LYS H2   H N N 312 
LYS HA   H N N 313 
LYS HB2  H N N 314 
LYS HB3  H N N 315 
LYS HG2  H N N 316 
LYS HG3  H N N 317 
LYS HD2  H N N 318 
LYS HD3  H N N 319 
LYS HE2  H N N 320 
LYS HE3  H N N 321 
LYS HZ1  H N N 322 
LYS HZ2  H N N 323 
LYS HZ3  H N N 324 
LYS HXT  H N N 325 
MET N    N N N 326 
MET CA   C N S 327 
MET C    C N N 328 
MET O    O N N 329 
MET CB   C N N 330 
MET CG   C N N 331 
MET SD   S N N 332 
MET CE   C N N 333 
MET OXT  O N N 334 
MET H    H N N 335 
MET H2   H N N 336 
MET HA   H N N 337 
MET HB2  H N N 338 
MET HB3  H N N 339 
MET HG2  H N N 340 
MET HG3  H N N 341 
MET HE1  H N N 342 
MET HE2  H N N 343 
MET HE3  H N N 344 
MET HXT  H N N 345 
OLC C18  C N N 346 
OLC C10  C N N 347 
OLC C9   C N N 348 
OLC C17  C N N 349 
OLC C11  C N N 350 
OLC C8   C N N 351 
OLC C24  C N N 352 
OLC C16  C N N 353 
OLC C12  C N N 354 
OLC C7   C N N 355 
OLC C15  C N N 356 
OLC C13  C N N 357 
OLC C6   C N N 358 
OLC C14  C N N 359 
OLC C5   C N N 360 
OLC C4   C N N 361 
OLC C3   C N N 362 
OLC C2   C N N 363 
OLC C21  C N N 364 
OLC C1   C N N 365 
OLC C22  C N R 366 
OLC O19  O N N 367 
OLC O25  O N N 368 
OLC O23  O N N 369 
OLC O20  O N N 370 
OLC H18  H N N 371 
OLC H18A H N N 372 
OLC H18B H N N 373 
OLC H10  H N N 374 
OLC H9   H N N 375 
OLC H17  H N N 376 
OLC H17A H N N 377 
OLC H11  H N N 378 
OLC H11A H N N 379 
OLC H8   H N N 380 
OLC H8A  H N N 381 
OLC H24  H N N 382 
OLC H24A H N N 383 
OLC H16  H N N 384 
OLC H16A H N N 385 
OLC H12  H N N 386 
OLC H12A H N N 387 
OLC H7   H N N 388 
OLC H7A  H N N 389 
OLC H15  H N N 390 
OLC H15A H N N 391 
OLC H13  H N N 392 
OLC H13A H N N 393 
OLC H6   H N N 394 
OLC H6A  H N N 395 
OLC H14  H N N 396 
OLC H14A H N N 397 
OLC H5   H N N 398 
OLC H5A  H N N 399 
OLC H4   H N N 400 
OLC H4A  H N N 401 
OLC H3   H N N 402 
OLC H3A  H N N 403 
OLC H2   H N N 404 
OLC H2A  H N N 405 
OLC H21  H N N 406 
OLC H21A H N N 407 
OLC H22  H N N 408 
OLC HO25 H N N 409 
OLC HO23 H N N 410 
PHE N    N N N 411 
PHE CA   C N S 412 
PHE C    C N N 413 
PHE O    O N N 414 
PHE CB   C N N 415 
PHE CG   C Y N 416 
PHE CD1  C Y N 417 
PHE CD2  C Y N 418 
PHE CE1  C Y N 419 
PHE CE2  C Y N 420 
PHE CZ   C Y N 421 
PHE OXT  O N N 422 
PHE H    H N N 423 
PHE H2   H N N 424 
PHE HA   H N N 425 
PHE HB2  H N N 426 
PHE HB3  H N N 427 
PHE HD1  H N N 428 
PHE HD2  H N N 429 
PHE HE1  H N N 430 
PHE HE2  H N N 431 
PHE HZ   H N N 432 
PHE HXT  H N N 433 
PRO N    N N N 434 
PRO CA   C N S 435 
PRO C    C N N 436 
PRO O    O N N 437 
PRO CB   C N N 438 
PRO CG   C N N 439 
PRO CD   C N N 440 
PRO OXT  O N N 441 
PRO H    H N N 442 
PRO HA   H N N 443 
PRO HB2  H N N 444 
PRO HB3  H N N 445 
PRO HG2  H N N 446 
PRO HG3  H N N 447 
PRO HD2  H N N 448 
PRO HD3  H N N 449 
PRO HXT  H N N 450 
RET C1   C N N 451 
RET C2   C N N 452 
RET C3   C N N 453 
RET C4   C N N 454 
RET C5   C N N 455 
RET C6   C N N 456 
RET C7   C N N 457 
RET C8   C N N 458 
RET C9   C N N 459 
RET C10  C N N 460 
RET C11  C N N 461 
RET C12  C N N 462 
RET C13  C N N 463 
RET C14  C N N 464 
RET C15  C N N 465 
RET O1   O N N 466 
RET C16  C N N 467 
RET C17  C N N 468 
RET C18  C N N 469 
RET C19  C N N 470 
RET C20  C N N 471 
RET H21  H N N 472 
RET H22  H N N 473 
RET H31  H N N 474 
RET H32  H N N 475 
RET H41  H N N 476 
RET H42  H N N 477 
RET H7   H N N 478 
RET H8   H N N 479 
RET H10  H N N 480 
RET H11  H N N 481 
RET H12  H N N 482 
RET H14  H N N 483 
RET H15  H N N 484 
RET H161 H N N 485 
RET H162 H N N 486 
RET H163 H N N 487 
RET H171 H N N 488 
RET H172 H N N 489 
RET H173 H N N 490 
RET H181 H N N 491 
RET H182 H N N 492 
RET H183 H N N 493 
RET H191 H N N 494 
RET H192 H N N 495 
RET H193 H N N 496 
RET H201 H N N 497 
RET H202 H N N 498 
RET H203 H N N 499 
SER N    N N N 500 
SER CA   C N S 501 
SER C    C N N 502 
SER O    O N N 503 
SER CB   C N N 504 
SER OG   O N N 505 
SER OXT  O N N 506 
SER H    H N N 507 
SER H2   H N N 508 
SER HA   H N N 509 
SER HB2  H N N 510 
SER HB3  H N N 511 
SER HG   H N N 512 
SER HXT  H N N 513 
THR N    N N N 514 
THR CA   C N S 515 
THR C    C N N 516 
THR O    O N N 517 
THR CB   C N R 518 
THR OG1  O N N 519 
THR CG2  C N N 520 
THR OXT  O N N 521 
THR H    H N N 522 
THR H2   H N N 523 
THR HA   H N N 524 
THR HB   H N N 525 
THR HG1  H N N 526 
THR HG21 H N N 527 
THR HG22 H N N 528 
THR HG23 H N N 529 
THR HXT  H N N 530 
TRP N    N N N 531 
TRP CA   C N S 532 
TRP C    C N N 533 
TRP O    O N N 534 
TRP CB   C N N 535 
TRP CG   C Y N 536 
TRP CD1  C Y N 537 
TRP CD2  C Y N 538 
TRP NE1  N Y N 539 
TRP CE2  C Y N 540 
TRP CE3  C Y N 541 
TRP CZ2  C Y N 542 
TRP CZ3  C Y N 543 
TRP CH2  C Y N 544 
TRP OXT  O N N 545 
TRP H    H N N 546 
TRP H2   H N N 547 
TRP HA   H N N 548 
TRP HB2  H N N 549 
TRP HB3  H N N 550 
TRP HD1  H N N 551 
TRP HE1  H N N 552 
TRP HE3  H N N 553 
TRP HZ2  H N N 554 
TRP HZ3  H N N 555 
TRP HH2  H N N 556 
TRP HXT  H N N 557 
TYR N    N N N 558 
TYR CA   C N S 559 
TYR C    C N N 560 
TYR O    O N N 561 
TYR CB   C N N 562 
TYR CG   C Y N 563 
TYR CD1  C Y N 564 
TYR CD2  C Y N 565 
TYR CE1  C Y N 566 
TYR CE2  C Y N 567 
TYR CZ   C Y N 568 
TYR OH   O N N 569 
TYR OXT  O N N 570 
TYR H    H N N 571 
TYR H2   H N N 572 
TYR HA   H N N 573 
TYR HB2  H N N 574 
TYR HB3  H N N 575 
TYR HD1  H N N 576 
TYR HD2  H N N 577 
TYR HE1  H N N 578 
TYR HE2  H N N 579 
TYR HH   H N N 580 
TYR HXT  H N N 581 
VAL N    N N N 582 
VAL CA   C N S 583 
VAL C    C N N 584 
VAL O    O N N 585 
VAL CB   C N N 586 
VAL CG1  C N N 587 
VAL CG2  C N N 588 
VAL OXT  O N N 589 
VAL H    H N N 590 
VAL H2   H N N 591 
VAL HA   H N N 592 
VAL HB   H N N 593 
VAL HG11 H N N 594 
VAL HG12 H N N 595 
VAL HG13 H N N 596 
VAL HG21 H N N 597 
VAL HG22 H N N 598 
VAL HG23 H N N 599 
VAL HXT  H N N 600 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HOH O   H1   sing N N 116 
HOH O   H2   sing N N 117 
ILE N   CA   sing N N 118 
ILE N   H    sing N N 119 
ILE N   H2   sing N N 120 
ILE CA  C    sing N N 121 
ILE CA  CB   sing N N 122 
ILE CA  HA   sing N N 123 
ILE C   O    doub N N 124 
ILE C   OXT  sing N N 125 
ILE CB  CG1  sing N N 126 
ILE CB  CG2  sing N N 127 
ILE CB  HB   sing N N 128 
ILE CG1 CD1  sing N N 129 
ILE CG1 HG12 sing N N 130 
ILE CG1 HG13 sing N N 131 
ILE CG2 HG21 sing N N 132 
ILE CG2 HG22 sing N N 133 
ILE CG2 HG23 sing N N 134 
ILE CD1 HD11 sing N N 135 
ILE CD1 HD12 sing N N 136 
ILE CD1 HD13 sing N N 137 
ILE OXT HXT  sing N N 138 
LEU N   CA   sing N N 139 
LEU N   H    sing N N 140 
LEU N   H2   sing N N 141 
LEU CA  C    sing N N 142 
LEU CA  CB   sing N N 143 
LEU CA  HA   sing N N 144 
LEU C   O    doub N N 145 
LEU C   OXT  sing N N 146 
LEU CB  CG   sing N N 147 
LEU CB  HB2  sing N N 148 
LEU CB  HB3  sing N N 149 
LEU CG  CD1  sing N N 150 
LEU CG  CD2  sing N N 151 
LEU CG  HG   sing N N 152 
LEU CD1 HD11 sing N N 153 
LEU CD1 HD12 sing N N 154 
LEU CD1 HD13 sing N N 155 
LEU CD2 HD21 sing N N 156 
LEU CD2 HD22 sing N N 157 
LEU CD2 HD23 sing N N 158 
LEU OXT HXT  sing N N 159 
LI1 C1  C2   sing N N 160 
LI1 C1  O1   sing N N 161 
LI1 C1  H11  sing N N 162 
LI1 C1  H12  sing N N 163 
LI1 C2  C3   sing N N 164 
LI1 C2  O2   sing N N 165 
LI1 C2  H2   sing N N 166 
LI1 C3  O3   sing N N 167 
LI1 C3  H31  sing N N 168 
LI1 C3  H32  sing N N 169 
LI1 O1  C11  sing N N 170 
LI1 O2  C41  sing N N 171 
LI1 O3  HO3  sing N N 172 
LI1 C41 C42  sing N N 173 
LI1 C41 H411 sing N N 174 
LI1 C41 H412 sing N N 175 
LI1 C42 C43  sing N N 176 
LI1 C42 H421 sing N N 177 
LI1 C42 H422 sing N N 178 
LI1 C43 C44  sing N N 179 
LI1 C43 C45  sing N N 180 
LI1 C43 H43  sing N N 181 
LI1 C44 H441 sing N N 182 
LI1 C44 H442 sing N N 183 
LI1 C44 H443 sing N N 184 
LI1 C45 C46  sing N N 185 
LI1 C45 H451 sing N N 186 
LI1 C45 H452 sing N N 187 
LI1 C46 C47  sing N N 188 
LI1 C46 H461 sing N N 189 
LI1 C46 H462 sing N N 190 
LI1 C47 C48  sing N N 191 
LI1 C47 H471 sing N N 192 
LI1 C47 H472 sing N N 193 
LI1 C48 C49  sing N N 194 
LI1 C48 C50  sing N N 195 
LI1 C48 H48  sing N N 196 
LI1 C49 H491 sing N N 197 
LI1 C49 H492 sing N N 198 
LI1 C49 H493 sing N N 199 
LI1 C50 C51  sing N N 200 
LI1 C50 H501 sing N N 201 
LI1 C50 H502 sing N N 202 
LI1 C51 C52  sing N N 203 
LI1 C51 H511 sing N N 204 
LI1 C51 H512 sing N N 205 
LI1 C52 C53  sing N N 206 
LI1 C52 H521 sing N N 207 
LI1 C52 H522 sing N N 208 
LI1 C53 C55  sing N N 209 
LI1 C53 H531 sing N N 210 
LI1 C53 H532 sing N N 211 
LI1 C55 C56  sing N N 212 
LI1 C55 H551 sing N N 213 
LI1 C55 H552 sing N N 214 
LI1 C56 C57  sing N N 215 
LI1 C56 H561 sing N N 216 
LI1 C56 H562 sing N N 217 
LI1 C57 C58  sing N N 218 
LI1 C57 H571 sing N N 219 
LI1 C57 H572 sing N N 220 
LI1 C58 C59  sing N N 221 
LI1 C58 C60  sing N N 222 
LI1 C58 H58  sing N N 223 
LI1 C59 H591 sing N N 224 
LI1 C59 H592 sing N N 225 
LI1 C59 H593 sing N N 226 
LI1 C60 H601 sing N N 227 
LI1 C60 H602 sing N N 228 
LI1 C60 H603 sing N N 229 
LI1 C11 C12  sing N N 230 
LI1 C11 H111 sing N N 231 
LI1 C11 H112 sing N N 232 
LI1 C12 C13  sing N N 233 
LI1 C12 H121 sing N N 234 
LI1 C12 H122 sing N N 235 
LI1 C13 C14  sing N N 236 
LI1 C13 C15  sing N N 237 
LI1 C13 H13  sing N N 238 
LI1 C14 H141 sing N N 239 
LI1 C14 H142 sing N N 240 
LI1 C14 H143 sing N N 241 
LI1 C15 C16  sing N N 242 
LI1 C15 H151 sing N N 243 
LI1 C15 H152 sing N N 244 
LI1 C16 C17  sing N N 245 
LI1 C16 H161 sing N N 246 
LI1 C16 H162 sing N N 247 
LI1 C17 C18  sing N N 248 
LI1 C17 H171 sing N N 249 
LI1 C17 H172 sing N N 250 
LI1 C18 C19  sing N N 251 
LI1 C18 C20  sing N N 252 
LI1 C18 H18  sing N N 253 
LI1 C19 H191 sing N N 254 
LI1 C19 H192 sing N N 255 
LI1 C19 H193 sing N N 256 
LI1 C20 C21  sing N N 257 
LI1 C20 H201 sing N N 258 
LI1 C20 H202 sing N N 259 
LI1 C21 C22  sing N N 260 
LI1 C21 H211 sing N N 261 
LI1 C21 H212 sing N N 262 
LI1 C22 C23  sing N N 263 
LI1 C22 H221 sing N N 264 
LI1 C22 H222 sing N N 265 
LI1 C23 C24  sing N N 266 
LI1 C23 C25  sing N N 267 
LI1 C23 H23  sing N N 268 
LI1 C24 H241 sing N N 269 
LI1 C24 H242 sing N N 270 
LI1 C24 H243 sing N N 271 
LI1 C25 C26  sing N N 272 
LI1 C25 H251 sing N N 273 
LI1 C25 H252 sing N N 274 
LI1 C26 C27  sing N N 275 
LI1 C26 H261 sing N N 276 
LI1 C26 H262 sing N N 277 
LI1 C27 C28  sing N N 278 
LI1 C27 H271 sing N N 279 
LI1 C27 H272 sing N N 280 
LI1 C28 C29  sing N N 281 
LI1 C28 C30  sing N N 282 
LI1 C28 H28  sing N N 283 
LI1 C29 H291 sing N N 284 
LI1 C29 H292 sing N N 285 
LI1 C29 H293 sing N N 286 
LI1 C30 H301 sing N N 287 
LI1 C30 H302 sing N N 288 
LI1 C30 H303 sing N N 289 
LYS N   CA   sing N N 290 
LYS N   H    sing N N 291 
LYS N   H2   sing N N 292 
LYS CA  C    sing N N 293 
LYS CA  CB   sing N N 294 
LYS CA  HA   sing N N 295 
LYS C   O    doub N N 296 
LYS C   OXT  sing N N 297 
LYS CB  CG   sing N N 298 
LYS CB  HB2  sing N N 299 
LYS CB  HB3  sing N N 300 
LYS CG  CD   sing N N 301 
LYS CG  HG2  sing N N 302 
LYS CG  HG3  sing N N 303 
LYS CD  CE   sing N N 304 
LYS CD  HD2  sing N N 305 
LYS CD  HD3  sing N N 306 
LYS CE  NZ   sing N N 307 
LYS CE  HE2  sing N N 308 
LYS CE  HE3  sing N N 309 
LYS NZ  HZ1  sing N N 310 
LYS NZ  HZ2  sing N N 311 
LYS NZ  HZ3  sing N N 312 
LYS OXT HXT  sing N N 313 
MET N   CA   sing N N 314 
MET N   H    sing N N 315 
MET N   H2   sing N N 316 
MET CA  C    sing N N 317 
MET CA  CB   sing N N 318 
MET CA  HA   sing N N 319 
MET C   O    doub N N 320 
MET C   OXT  sing N N 321 
MET CB  CG   sing N N 322 
MET CB  HB2  sing N N 323 
MET CB  HB3  sing N N 324 
MET CG  SD   sing N N 325 
MET CG  HG2  sing N N 326 
MET CG  HG3  sing N N 327 
MET SD  CE   sing N N 328 
MET CE  HE1  sing N N 329 
MET CE  HE2  sing N N 330 
MET CE  HE3  sing N N 331 
MET OXT HXT  sing N N 332 
OLC C18 C17  sing N N 333 
OLC C10 C9   doub N N 334 
OLC C10 C11  sing N N 335 
OLC C9  C8   sing N N 336 
OLC C17 C16  sing N Z 337 
OLC C11 C12  sing N N 338 
OLC C8  C7   sing N N 339 
OLC C24 C22  sing N N 340 
OLC C24 O25  sing N N 341 
OLC C16 C15  sing N N 342 
OLC C12 C13  sing N N 343 
OLC C7  C6   sing N N 344 
OLC C15 C14  sing N N 345 
OLC C13 C14  sing N N 346 
OLC C6  C5   sing N N 347 
OLC C5  C4   sing N N 348 
OLC C4  C3   sing N N 349 
OLC C3  C2   sing N N 350 
OLC C2  C1   sing N N 351 
OLC C21 C22  sing N N 352 
OLC C21 O20  sing N N 353 
OLC C1  O19  doub N N 354 
OLC C1  O20  sing N N 355 
OLC C22 O23  sing N N 356 
OLC C18 H18  sing N N 357 
OLC C18 H18A sing N N 358 
OLC C18 H18B sing N N 359 
OLC C10 H10  sing N N 360 
OLC C9  H9   sing N N 361 
OLC C17 H17  sing N N 362 
OLC C17 H17A sing N N 363 
OLC C11 H11  sing N N 364 
OLC C11 H11A sing N N 365 
OLC C8  H8   sing N N 366 
OLC C8  H8A  sing N N 367 
OLC C24 H24  sing N N 368 
OLC C24 H24A sing N N 369 
OLC C16 H16  sing N N 370 
OLC C16 H16A sing N N 371 
OLC C12 H12  sing N N 372 
OLC C12 H12A sing N N 373 
OLC C7  H7   sing N N 374 
OLC C7  H7A  sing N N 375 
OLC C15 H15  sing N N 376 
OLC C15 H15A sing N N 377 
OLC C13 H13  sing N N 378 
OLC C13 H13A sing N N 379 
OLC C6  H6   sing N N 380 
OLC C6  H6A  sing N N 381 
OLC C14 H14  sing N N 382 
OLC C14 H14A sing N N 383 
OLC C5  H5   sing N N 384 
OLC C5  H5A  sing N N 385 
OLC C4  H4   sing N N 386 
OLC C4  H4A  sing N N 387 
OLC C3  H3   sing N N 388 
OLC C3  H3A  sing N N 389 
OLC C2  H2   sing N N 390 
OLC C2  H2A  sing N N 391 
OLC C21 H21  sing N N 392 
OLC C21 H21A sing N N 393 
OLC C22 H22  sing N N 394 
OLC O25 HO25 sing N N 395 
OLC O23 HO23 sing N N 396 
PHE N   CA   sing N N 397 
PHE N   H    sing N N 398 
PHE N   H2   sing N N 399 
PHE CA  C    sing N N 400 
PHE CA  CB   sing N N 401 
PHE CA  HA   sing N N 402 
PHE C   O    doub N N 403 
PHE C   OXT  sing N N 404 
PHE CB  CG   sing N N 405 
PHE CB  HB2  sing N N 406 
PHE CB  HB3  sing N N 407 
PHE CG  CD1  doub Y N 408 
PHE CG  CD2  sing Y N 409 
PHE CD1 CE1  sing Y N 410 
PHE CD1 HD1  sing N N 411 
PHE CD2 CE2  doub Y N 412 
PHE CD2 HD2  sing N N 413 
PHE CE1 CZ   doub Y N 414 
PHE CE1 HE1  sing N N 415 
PHE CE2 CZ   sing Y N 416 
PHE CE2 HE2  sing N N 417 
PHE CZ  HZ   sing N N 418 
PHE OXT HXT  sing N N 419 
PRO N   CA   sing N N 420 
PRO N   CD   sing N N 421 
PRO N   H    sing N N 422 
PRO CA  C    sing N N 423 
PRO CA  CB   sing N N 424 
PRO CA  HA   sing N N 425 
PRO C   O    doub N N 426 
PRO C   OXT  sing N N 427 
PRO CB  CG   sing N N 428 
PRO CB  HB2  sing N N 429 
PRO CB  HB3  sing N N 430 
PRO CG  CD   sing N N 431 
PRO CG  HG2  sing N N 432 
PRO CG  HG3  sing N N 433 
PRO CD  HD2  sing N N 434 
PRO CD  HD3  sing N N 435 
PRO OXT HXT  sing N N 436 
RET C1  C2   sing N N 437 
RET C1  C6   sing N N 438 
RET C1  C16  sing N N 439 
RET C1  C17  sing N N 440 
RET C2  C3   sing N N 441 
RET C2  H21  sing N N 442 
RET C2  H22  sing N N 443 
RET C3  C4   sing N N 444 
RET C3  H31  sing N N 445 
RET C3  H32  sing N N 446 
RET C4  C5   sing N N 447 
RET C4  H41  sing N N 448 
RET C4  H42  sing N N 449 
RET C5  C6   doub N N 450 
RET C5  C18  sing N N 451 
RET C6  C7   sing N N 452 
RET C7  C8   doub N E 453 
RET C7  H7   sing N N 454 
RET C8  C9   sing N N 455 
RET C8  H8   sing N N 456 
RET C9  C10  doub N E 457 
RET C9  C19  sing N N 458 
RET C10 C11  sing N N 459 
RET C10 H10  sing N N 460 
RET C11 C12  doub N E 461 
RET C11 H11  sing N N 462 
RET C12 C13  sing N N 463 
RET C12 H12  sing N N 464 
RET C13 C14  doub N E 465 
RET C13 C20  sing N N 466 
RET C14 C15  sing N N 467 
RET C14 H14  sing N N 468 
RET C15 O1   doub N N 469 
RET C15 H15  sing N N 470 
RET C16 H161 sing N N 471 
RET C16 H162 sing N N 472 
RET C16 H163 sing N N 473 
RET C17 H171 sing N N 474 
RET C17 H172 sing N N 475 
RET C17 H173 sing N N 476 
RET C18 H181 sing N N 477 
RET C18 H182 sing N N 478 
RET C18 H183 sing N N 479 
RET C19 H191 sing N N 480 
RET C19 H192 sing N N 481 
RET C19 H193 sing N N 482 
RET C20 H201 sing N N 483 
RET C20 H202 sing N N 484 
RET C20 H203 sing N N 485 
SER N   CA   sing N N 486 
SER N   H    sing N N 487 
SER N   H2   sing N N 488 
SER CA  C    sing N N 489 
SER CA  CB   sing N N 490 
SER CA  HA   sing N N 491 
SER C   O    doub N N 492 
SER C   OXT  sing N N 493 
SER CB  OG   sing N N 494 
SER CB  HB2  sing N N 495 
SER CB  HB3  sing N N 496 
SER OG  HG   sing N N 497 
SER OXT HXT  sing N N 498 
THR N   CA   sing N N 499 
THR N   H    sing N N 500 
THR N   H2   sing N N 501 
THR CA  C    sing N N 502 
THR CA  CB   sing N N 503 
THR CA  HA   sing N N 504 
THR C   O    doub N N 505 
THR C   OXT  sing N N 506 
THR CB  OG1  sing N N 507 
THR CB  CG2  sing N N 508 
THR CB  HB   sing N N 509 
THR OG1 HG1  sing N N 510 
THR CG2 HG21 sing N N 511 
THR CG2 HG22 sing N N 512 
THR CG2 HG23 sing N N 513 
THR OXT HXT  sing N N 514 
TRP N   CA   sing N N 515 
TRP N   H    sing N N 516 
TRP N   H2   sing N N 517 
TRP CA  C    sing N N 518 
TRP CA  CB   sing N N 519 
TRP CA  HA   sing N N 520 
TRP C   O    doub N N 521 
TRP C   OXT  sing N N 522 
TRP CB  CG   sing N N 523 
TRP CB  HB2  sing N N 524 
TRP CB  HB3  sing N N 525 
TRP CG  CD1  doub Y N 526 
TRP CG  CD2  sing Y N 527 
TRP CD1 NE1  sing Y N 528 
TRP CD1 HD1  sing N N 529 
TRP CD2 CE2  doub Y N 530 
TRP CD2 CE3  sing Y N 531 
TRP NE1 CE2  sing Y N 532 
TRP NE1 HE1  sing N N 533 
TRP CE2 CZ2  sing Y N 534 
TRP CE3 CZ3  doub Y N 535 
TRP CE3 HE3  sing N N 536 
TRP CZ2 CH2  doub Y N 537 
TRP CZ2 HZ2  sing N N 538 
TRP CZ3 CH2  sing Y N 539 
TRP CZ3 HZ3  sing N N 540 
TRP CH2 HH2  sing N N 541 
TRP OXT HXT  sing N N 542 
TYR N   CA   sing N N 543 
TYR N   H    sing N N 544 
TYR N   H2   sing N N 545 
TYR CA  C    sing N N 546 
TYR CA  CB   sing N N 547 
TYR CA  HA   sing N N 548 
TYR C   O    doub N N 549 
TYR C   OXT  sing N N 550 
TYR CB  CG   sing N N 551 
TYR CB  HB2  sing N N 552 
TYR CB  HB3  sing N N 553 
TYR CG  CD1  doub Y N 554 
TYR CG  CD2  sing Y N 555 
TYR CD1 CE1  sing Y N 556 
TYR CD1 HD1  sing N N 557 
TYR CD2 CE2  doub Y N 558 
TYR CD2 HD2  sing N N 559 
TYR CE1 CZ   doub Y N 560 
TYR CE1 HE1  sing N N 561 
TYR CE2 CZ   sing Y N 562 
TYR CE2 HE2  sing N N 563 
TYR CZ  OH   sing N N 564 
TYR OH  HH   sing N N 565 
TYR OXT HXT  sing N N 566 
VAL N   CA   sing N N 567 
VAL N   H    sing N N 568 
VAL N   H2   sing N N 569 
VAL CA  C    sing N N 570 
VAL CA  CB   sing N N 571 
VAL CA  HA   sing N N 572 
VAL C   O    doub N N 573 
VAL C   OXT  sing N N 574 
VAL CB  CG1  sing N N 575 
VAL CB  CG2  sing N N 576 
VAL CB  HB   sing N N 577 
VAL CG1 HG11 sing N N 578 
VAL CG1 HG12 sing N N 579 
VAL CG1 HG13 sing N N 580 
VAL CG2 HG21 sing N N 581 
VAL CG2 HG22 sing N N 582 
VAL CG2 HG23 sing N N 583 
VAL OXT HXT  sing N N 584 
# 
_pdbx_audit_support.funding_organization   Innosuisse 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           '42711.1 IP-LS' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6g7h 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F9I 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016013 
_atom_sites.fract_transf_matrix[1][2]   0.009245 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018490 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008995 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . GLY A 1 1   ? 20.078 25.600 13.983 1.00 92.87  ? 4   GLY A N    1 
ATOM   2    C CA   . GLY A 1 1   ? 20.595 26.028 15.269 1.00 89.22  ? 4   GLY A CA   1 
ATOM   3    C C    . GLY A 1 1   ? 21.945 26.712 15.164 1.00 85.55  ? 4   GLY A C    1 
ATOM   4    O O    . GLY A 1 1   ? 22.101 27.872 15.557 1.00 68.87  ? 4   GLY A O    1 
ATOM   5    N N    . THR A 1 2   ? 22.929 25.991 14.623 1.00 73.60  ? 5   THR A N    1 
ATOM   6    C CA   . THR A 1 2   ? 24.267 26.546 14.478 1.00 53.42  ? 5   THR A CA   1 
ATOM   7    C C    . THR A 1 2   ? 24.352 27.595 13.379 1.00 55.88  ? 5   THR A C    1 
ATOM   8    O O    . THR A 1 2   ? 25.403 28.231 13.233 1.00 69.63  ? 5   THR A O    1 
ATOM   9    C CB   . THR A 1 2   ? 25.272 25.422 14.202 1.00 77.40  ? 5   THR A CB   1 
ATOM   10   O OG1  . THR A 1 2   ? 24.853 24.678 13.054 1.00 76.18  ? 5   THR A OG1  1 
ATOM   11   C CG2  . THR A 1 2   ? 25.371 24.487 15.410 1.00 69.34  ? 5   THR A CG2  1 
ATOM   12   H HA   . THR A 1 2   ? 24.519 26.972 15.313 0.00 64.11  ? 5   THR A HA   1 
ATOM   13   H HB   . THR A 1 2   ? 26.149 25.802 14.036 0.00 92.90  ? 5   THR A HB   1 
ATOM   14   H HG1  . THR A 1 2   ? 24.107 24.321 13.200 0.00 91.43  ? 5   THR A HG1  1 
ATOM   15   H HG21 . THR A 1 2   ? 24.505 24.090 15.594 0.00 83.22  ? 5   THR A HG21 1 
ATOM   16   H HG22 . THR A 1 2   ? 26.010 23.780 15.230 0.00 83.22  ? 5   THR A HG22 1 
ATOM   17   H HG23 . THR A 1 2   ? 25.662 24.983 16.191 0.00 83.22  ? 5   THR A HG23 1 
ATOM   18   N N    . GLY A 1 3   ? 23.285 27.789 12.599 1.00 64.80  ? 6   GLY A N    1 
ATOM   19   C CA   . GLY A 1 3   ? 23.290 28.826 11.583 1.00 59.88  ? 6   GLY A CA   1 
ATOM   20   C C    . GLY A 1 3   ? 23.337 30.233 12.143 1.00 56.79  ? 6   GLY A C    1 
ATOM   21   O O    . GLY A 1 3   ? 23.634 31.174 11.400 1.00 63.32  ? 6   GLY A O    1 
ATOM   22   H H    . GLY A 1 3   ? 22.556 27.336 12.643 0.00 77.77  ? 6   GLY A H    1 
ATOM   23   H HA2  . GLY A 1 3   ? 24.066 28.704 11.014 0.00 71.87  ? 6   GLY A HA2  1 
ATOM   24   H HA3  . GLY A 1 3   ? 22.488 28.743 11.045 0.00 71.87  ? 6   GLY A HA3  1 
ATOM   25   N N    . ARG A 1 4   ? 23.038 30.397 13.430 1.00 50.53  ? 7   ARG A N    1 
ATOM   26   C CA   . ARG A 1 4   ? 23.061 31.706 14.080 1.00 42.61  ? 7   ARG A CA   1 
ATOM   27   C C    . ARG A 1 4   ? 24.351 31.856 14.876 1.00 35.89  ? 7   ARG A C    1 
ATOM   28   O O    . ARG A 1 4   ? 24.611 31.033 15.763 1.00 40.80  ? 7   ARG A O    1 
ATOM   29   C CB   . ARG A 1 4   ? 21.855 31.855 15.011 1.00 36.86  ? 7   ARG A CB   1 
ATOM   30   C CG   . ARG A 1 4   ? 20.507 31.971 14.295 1.00 38.95  ? 7   ARG A CG   1 
ATOM   31   C CD   . ARG A 1 4   ? 19.405 31.794 15.339 1.00 48.14  ? 7   ARG A CD   1 
ATOM   32   N NE   . ARG A 1 4   ? 19.221 30.392 15.686 1.00 58.44  ? 7   ARG A NE   1 
ATOM   33   C CZ   . ARG A 1 4   ? 18.692 29.949 16.821 1.00 55.30  ? 7   ARG A CZ   1 
ATOM   34   N NH1  . ARG A 1 4   ? 18.455 30.761 17.851 1.00 34.87  ? 7   ARG A NH1  1 
ATOM   35   N NH2  . ARG A 1 4   ? 18.424 28.651 16.943 1.00 54.85  ? 7   ARG A NH2  1 
ATOM   36   H H    . ARG A 1 4   ? 22.815 29.756 13.958 0.00 60.65  ? 7   ARG A H    1 
ATOM   37   H HA   . ARG A 1 4   ? 23.028 32.403 13.407 0.00 51.14  ? 7   ARG A HA   1 
ATOM   38   H HB2  . ARG A 1 4   ? 21.814 31.077 15.589 0.00 44.24  ? 7   ARG A HB2  1 
ATOM   39   H HB3  . ARG A 1 4   ? 21.974 32.658 15.543 0.00 44.24  ? 7   ARG A HB3  1 
ATOM   40   H HG2  . ARG A 1 4   ? 20.420 32.845 13.883 0.00 46.68  ? 7   ARG A HG2  1 
ATOM   41   H HG3  . ARG A 1 4   ? 20.424 31.278 13.622 0.00 46.68  ? 7   ARG A HG3  1 
ATOM   42   H HD2  . ARG A 1 4   ? 19.645 32.280 16.144 0.00 57.78  ? 7   ARG A HD2  1 
ATOM   43   H HD3  . ARG A 1 4   ? 18.569 32.133 14.983 0.00 57.78  ? 7   ARG A HD3  1 
ATOM   44   H HE   . ARG A 1 4   ? 19.475 29.804 15.112 0.00 70.15  ? 7   ARG A HE   1 
ATOM   45   H HH11 . ARG A 1 4   ? 18.646 31.598 17.792 0.00 41.85  ? 7   ARG A HH11 1 
ATOM   46   H HH12 . ARG A 1 4   ? 18.112 30.449 18.575 0.00 41.85  ? 7   ARG A HH12 1 
ATOM   47   H HH21 . ARG A 1 4   ? 18.594 28.114 16.292 0.00 65.84  ? 7   ARG A HH21 1 
ATOM   48   H HH22 . ARG A 1 4   ? 18.082 28.349 17.671 0.00 65.84  ? 7   ARG A HH22 1 
ATOM   49   N N    . PRO A 1 5   ? 25.153 32.893 14.647 1.00 35.34  ? 8   PRO A N    1 
ATOM   50   C CA   . PRO A 1 5   ? 26.452 32.960 15.340 1.00 38.29  ? 8   PRO A CA   1 
ATOM   51   C C    . PRO A 1 5   ? 26.337 33.052 16.835 1.00 40.48  ? 8   PRO A C    1 
ATOM   52   O O    . PRO A 1 5   ? 27.251 32.618 17.549 1.00 37.34  ? 8   PRO A O    1 
ATOM   53   C CB   . PRO A 1 5   ? 27.115 34.223 14.747 1.00 39.54  ? 8   PRO A CB   1 
ATOM   54   C CG   . PRO A 1 5   ? 26.022 34.993 14.089 1.00 56.14  ? 8   PRO A CG   1 
ATOM   55   C CD   . PRO A 1 5   ? 24.938 34.029 13.717 1.00 36.51  ? 8   PRO A CD   1 
ATOM   56   H HA   . PRO A 1 5   ? 26.981 32.181 15.108 0.00 45.95  ? 8   PRO A HA   1 
ATOM   57   H HB2  . PRO A 1 5   ? 27.521 34.743 15.458 0.00 47.46  ? 8   PRO A HB2  1 
ATOM   58   H HB3  . PRO A 1 5   ? 27.789 33.963 14.100 0.00 47.46  ? 8   PRO A HB3  1 
ATOM   59   H HG2  . PRO A 1 5   ? 25.682 35.657 14.709 0.00 67.38  ? 8   PRO A HG2  1 
ATOM   60   H HG3  . PRO A 1 5   ? 26.372 35.428 13.296 0.00 67.38  ? 8   PRO A HG3  1 
ATOM   61   H HD2  . PRO A 1 5   ? 24.063 34.425 13.852 0.00 43.75  ? 8   PRO A HD2  1 
ATOM   62   H HD3  . PRO A 1 5   ? 25.034 33.742 12.795 0.00 43.75  ? 8   PRO A HD3  1 
ATOM   63   N N    . GLU A 1 6   ? 25.222 33.583 17.356 1.00 32.92  ? 9   GLU A N    1 
ATOM   64   C CA   . GLU A 1 6   ? 25.061 33.706 18.793 1.00 30.86  ? 9   GLU A CA   1 
ATOM   65   C C    . GLU A 1 6   ? 24.726 32.384 19.473 1.00 29.81  ? 9   GLU A C    1 
ATOM   66   O O    . GLU A 1 6   ? 24.578 32.350 20.674 1.00 27.48  ? 9   GLU A O    1 
ATOM   67   C CB   . GLU A 1 6   ? 23.952 34.726 19.110 1.00 30.90  ? 9   GLU A CB   1 
ATOM   68   C CG   . GLU A 1 6   ? 22.519 34.302 18.712 1.00 29.07  ? 9   GLU A CG   1 
ATOM   69   C CD   . GLU A 1 6   ? 22.150 34.688 17.298 1.00 31.43  ? 9   GLU A CD   1 
ATOM   70   O OE1  . GLU A 1 6   ? 23.072 34.958 16.480 1.00 33.67  ? 9   GLU A OE1  1 
ATOM   71   O OE2  . GLU A 1 6   ? 20.938 34.716 16.983 1.00 30.72  ? 9   GLU A OE2  1 
ATOM   72   H H    . GLU A 1 6   ? 24.557 33.874 16.895 0.00 39.52  ? 9   GLU A H    1 
ATOM   73   H HA   . GLU A 1 6   ? 25.895 34.031 19.165 0.00 37.05  ? 9   GLU A HA   1 
ATOM   74   H HB2  . GLU A 1 6   ? 23.950 34.887 20.066 0.00 37.09  ? 9   GLU A HB2  1 
ATOM   75   H HB3  . GLU A 1 6   ? 24.151 35.549 18.636 0.00 37.09  ? 9   GLU A HB3  1 
ATOM   76   H HG2  . GLU A 1 6   ? 22.445 33.338 18.787 0.00 34.89  ? 9   GLU A HG2  1 
ATOM   77   H HG3  . GLU A 1 6   ? 21.888 34.731 19.312 0.00 34.89  ? 9   GLU A HG3  1 
ATOM   78   N N    . TRP A 1 7   ? 24.609 31.281 18.698 1.00 27.65  ? 10  TRP A N    1 
ATOM   79   C CA   . TRP A 1 7   ? 24.162 30.044 19.310 1.00 27.57  ? 10  TRP A CA   1 
ATOM   80   C C    . TRP A 1 7   ? 25.085 29.595 20.433 1.00 28.84  ? 10  TRP A C    1 
ATOM   81   O O    . TRP A 1 7   ? 24.622 29.010 21.418 1.00 28.38  ? 10  TRP A O    1 
ATOM   82   C CB   . TRP A 1 7   ? 24.053 28.954 18.211 1.00 31.26  ? 10  TRP A CB   1 
ATOM   83   C CG   . TRP A 1 7   ? 25.347 28.309 17.850 1.00 40.40  ? 10  TRP A CG   1 
ATOM   84   C CD1  . TRP A 1 7   ? 26.186 28.663 16.830 1.00 50.05  ? 10  TRP A CD1  1 
ATOM   85   C CD2  . TRP A 1 7   ? 25.944 27.167 18.487 1.00 36.36  ? 10  TRP A CD2  1 
ATOM   86   N NE1  . TRP A 1 7   ? 27.276 27.820 16.793 1.00 49.46  ? 10  TRP A NE1  1 
ATOM   87   C CE2  . TRP A 1 7   ? 27.155 26.899 17.800 1.00 42.36  ? 10  TRP A CE2  1 
ATOM   88   C CE3  . TRP A 1 7   ? 25.584 26.357 19.560 1.00 41.89  ? 10  TRP A CE3  1 
ATOM   89   C CZ2  . TRP A 1 7   ? 27.994 25.853 18.165 1.00 53.06  ? 10  TRP A CZ2  1 
ATOM   90   C CZ3  . TRP A 1 7   ? 26.421 25.321 19.922 1.00 55.44  ? 10  TRP A CZ3  1 
ATOM   91   C CH2  . TRP A 1 7   ? 27.611 25.084 19.229 1.00 47.25  ? 10  TRP A CH2  1 
ATOM   92   H H    . TRP A 1 7   ? 24.777 31.241 17.855 0.00 33.12  ? 10  TRP A H    1 
ATOM   93   H HA   . TRP A 1 7   ? 23.286 30.175 19.704 0.00 33.02  ? 10  TRP A HA   1 
ATOM   94   H HB2  . TRP A 1 7   ? 23.456 28.257 18.525 0.00 37.45  ? 10  TRP A HB2  1 
ATOM   95   H HB3  . TRP A 1 7   ? 23.694 29.361 17.407 0.00 37.45  ? 10  TRP A HB3  1 
ATOM   96   H HD1  . TRP A 1 7   ? 26.042 29.372 16.245 0.00 60.07  ? 10  TRP A HD1  1 
ATOM   97   H HE1  . TRP A 1 7   ? 27.926 27.866 16.231 0.00 59.36  ? 10  TRP A HE1  1 
ATOM   98   H HE3  . TRP A 1 7   ? 24.794 26.511 20.025 0.00 50.29  ? 10  TRP A HE3  1 
ATOM   99   H HZ2  . TRP A 1 7   ? 28.784 25.684 17.705 0.00 63.68  ? 10  TRP A HZ2  1 
ATOM   100  H HZ3  . TRP A 1 7   ? 26.189 24.773 20.637 0.00 66.54  ? 10  TRP A HZ3  1 
ATOM   101  H HH2  . TRP A 1 7   ? 28.158 24.382 19.500 0.00 56.72  ? 10  TRP A HH2  1 
ATOM   102  N N    . ILE A 1 8   ? 26.389 29.854 20.309 1.00 30.61  ? 11  ILE A N    1 
ATOM   103  C CA   . ILE A 1 8   ? 27.323 29.324 21.315 1.00 27.22  ? 11  ILE A CA   1 
ATOM   104  C C    . ILE A 1 8   ? 27.020 29.933 22.678 1.00 26.71  ? 11  ILE A C    1 
ATOM   105  O O    . ILE A 1 8   ? 27.130 29.262 23.707 1.00 29.41  ? 11  ILE A O    1 
ATOM   106  C CB   . ILE A 1 8   ? 28.781 29.572 20.876 1.00 34.82  ? 11  ILE A CB   1 
ATOM   107  C CG1  . ILE A 1 8   ? 29.748 29.222 22.005 1.00 43.83  ? 11  ILE A CG1  1 
ATOM   108  C CG2  . ILE A 1 8   ? 28.987 31.035 20.494 1.00 38.27  ? 11  ILE A CG2  1 
ATOM   109  C CD1  . ILE A 1 8   ? 29.828 27.740 22.297 1.00 52.08  ? 11  ILE A CD1  1 
ATOM   110  H H    . ILE A 1 8   ? 26.748 30.316 19.679 0.00 36.75  ? 11  ILE A H    1 
ATOM   111  H HA   . ILE A 1 8   ? 27.201 28.364 21.385 0.00 32.68  ? 11  ILE A HA   1 
ATOM   112  H HB   . ILE A 1 8   ? 28.955 29.005 20.108 0.00 41.80  ? 11  ILE A HB   1 
ATOM   113  H HG12 . ILE A 1 8   ? 30.637 29.524 21.760 0.00 52.61  ? 11  ILE A HG12 1 
ATOM   114  H HG13 . ILE A 1 8   ? 29.457 29.669 22.815 0.00 52.61  ? 11  ILE A HG13 1 
ATOM   115  H HG21 . ILE A 1 8   ? 29.924 31.179 20.289 0.00 45.93  ? 11  ILE A HG21 1 
ATOM   116  H HG22 . ILE A 1 8   ? 28.443 31.238 19.717 0.00 45.93  ? 11  ILE A HG22 1 
ATOM   117  H HG23 . ILE A 1 8   ? 28.721 31.596 21.239 0.00 45.93  ? 11  ILE A HG23 1 
ATOM   118  H HD11 . ILE A 1 8   ? 30.432 27.597 23.042 0.00 62.51  ? 11  ILE A HD11 1 
ATOM   119  H HD12 . ILE A 1 8   ? 28.942 27.415 22.523 0.00 62.51  ? 11  ILE A HD12 1 
ATOM   120  H HD13 . ILE A 1 8   ? 30.158 27.280 21.510 0.00 62.51  ? 11  ILE A HD13 1 
ATOM   121  N N    . TRP A 1 9   ? 26.645 31.212 22.711 1.00 27.75  ? 12  TRP A N    1 
ATOM   122  C CA   . TRP A 1 9   ? 26.352 31.830 23.993 1.00 24.44  ? 12  TRP A CA   1 
ATOM   123  C C    . TRP A 1 9   ? 25.018 31.372 24.550 1.00 25.77  ? 12  TRP A C    1 
ATOM   124  O O    . TRP A 1 9   ? 24.858 31.257 25.761 1.00 26.50  ? 12  TRP A O    1 
ATOM   125  C CB   . TRP A 1 9   ? 26.407 33.361 23.849 1.00 26.06  ? 12  TRP A CB   1 
ATOM   126  C CG   . TRP A 1 9   ? 27.625 33.825 23.122 1.00 25.86  ? 12  TRP A CG   1 
ATOM   127  C CD1  . TRP A 1 9   ? 27.650 34.573 21.964 1.00 31.04  ? 12  TRP A CD1  1 
ATOM   128  C CD2  . TRP A 1 9   ? 28.983 33.564 23.458 1.00 29.41  ? 12  TRP A CD2  1 
ATOM   129  N NE1  . TRP A 1 9   ? 28.951 34.789 21.578 1.00 32.56  ? 12  TRP A NE1  1 
ATOM   130  C CE2  . TRP A 1 9   ? 29.794 34.171 22.461 1.00 32.21  ? 12  TRP A CE2  1 
ATOM   131  C CE3  . TRP A 1 9   ? 29.605 32.866 24.497 1.00 34.88  ? 12  TRP A CE3  1 
ATOM   132  C CZ2  . TRP A 1 9   ? 31.191 34.117 22.502 1.00 35.38  ? 12  TRP A CZ2  1 
ATOM   133  C CZ3  . TRP A 1 9   ? 30.989 32.814 24.519 1.00 33.08  ? 12  TRP A CZ3  1 
ATOM   134  C CH2  . TRP A 1 9   ? 31.761 33.431 23.525 1.00 38.73  ? 12  TRP A CH2  1 
ATOM   135  H H    . TRP A 1 9   ? 26.556 31.723 22.025 0.00 33.31  ? 12  TRP A H    1 
ATOM   136  H HA   . TRP A 1 9   ? 27.028 31.577 24.640 0.00 29.34  ? 12  TRP A HA   1 
ATOM   137  H HB2  . TRP A 1 9   ? 25.629 33.661 23.355 0.00 31.28  ? 12  TRP A HB2  1 
ATOM   138  H HB3  . TRP A 1 9   ? 26.414 33.762 24.733 0.00 31.28  ? 12  TRP A HB3  1 
ATOM   139  H HD1  . TRP A 1 9   ? 26.899 34.884 21.512 0.00 37.26  ? 12  TRP A HD1  1 
ATOM   140  H HE1  . TRP A 1 9   ? 29.196 35.243 20.890 0.00 39.09  ? 12  TRP A HE1  1 
ATOM   141  H HE3  . TRP A 1 9   ? 29.101 32.446 25.157 0.00 41.87  ? 12  TRP A HE3  1 
ATOM   142  H HZ2  . TRP A 1 9   ? 31.710 34.535 21.853 0.00 42.47  ? 12  TRP A HZ2  1 
ATOM   143  H HZ3  . TRP A 1 9   ? 31.415 32.359 25.210 0.00 39.71  ? 12  TRP A HZ3  1 
ATOM   144  H HH2  . TRP A 1 9   ? 32.688 33.369 23.568 0.00 46.49  ? 12  TRP A HH2  1 
ATOM   145  N N    . LEU A 1 10  ? 24.031 31.102 23.669 1.00 22.55  ? 13  LEU A N    1 
ATOM   146  C CA   . LEU A 1 10  ? 22.790 30.534 24.159 1.00 20.72  ? 13  LEU A CA   1 
ATOM   147  C C    . LEU A 1 10  ? 23.008 29.144 24.718 1.00 22.93  ? 13  LEU A C    1 
ATOM   148  O O    . LEU A 1 10  ? 22.364 28.773 25.712 1.00 24.34  ? 13  LEU A O    1 
ATOM   149  C CB   . LEU A 1 10  ? 21.736 30.489 23.014 1.00 21.83  ? 13  LEU A CB   1 
ATOM   150  C CG   . LEU A 1 10  ? 21.380 31.893 22.469 1.00 24.17  ? 13  LEU A CG   1 
ATOM   151  C CD1  . LEU A 1 10  ? 20.563 31.749 21.209 1.00 23.20  ? 13  LEU A CD1  1 
ATOM   152  C CD2  . LEU A 1 10  ? 20.593 32.687 23.536 1.00 28.87  ? 13  LEU A CD2  1 
ATOM   153  H H    . LEU A 1 10  ? 24.067 31.237 22.821 0.00 27.08  ? 13  LEU A H    1 
ATOM   154  H HA   . LEU A 1 10  ? 22.448 31.101 24.868 0.00 24.88  ? 13  LEU A HA   1 
ATOM   155  H HB2  . LEU A 1 10  ? 22.091 29.962 22.280 0.00 26.20  ? 13  LEU A HB2  1 
ATOM   156  H HB3  . LEU A 1 10  ? 20.923 30.082 23.351 0.00 26.20  ? 13  LEU A HB3  1 
ATOM   157  H HG   . LEU A 1 10  ? 22.189 32.385 22.260 0.00 29.02  ? 13  LEU A HG   1 
ATOM   158  H HD11 . LEU A 1 10  ? 20.351 32.632 20.867 0.00 27.78  ? 13  LEU A HD11 1 
ATOM   159  H HD12 . LEU A 1 10  ? 21.079 31.255 20.553 0.00 27.78  ? 13  LEU A HD12 1 
ATOM   160  H HD13 . LEU A 1 10  ? 19.745 31.269 21.416 0.00 27.78  ? 13  LEU A HD13 1 
ATOM   161  H HD21 . LEU A 1 10  ? 20.251 33.501 23.134 0.00 34.66  ? 13  LEU A HD21 1 
ATOM   162  H HD22 . LEU A 1 10  ? 19.859 32.142 23.857 0.00 34.66  ? 13  LEU A HD22 1 
ATOM   163  H HD23 . LEU A 1 10  ? 21.189 32.905 24.269 0.00 34.66  ? 13  LEU A HD23 1 
ATOM   164  N N    . ALA A 1 11  ? 23.879 28.349 24.090 1.00 23.58  ? 14  ALA A N    1 
ATOM   165  C CA   . ALA A 1 11  ? 24.144 26.999 24.582 1.00 23.64  ? 14  ALA A CA   1 
ATOM   166  C C    . ALA A 1 11  ? 24.859 27.046 25.926 1.00 25.60  ? 14  ALA A C    1 
ATOM   167  O O    . ALA A 1 11  ? 24.521 26.281 26.843 1.00 24.56  ? 14  ALA A O    1 
ATOM   168  C CB   . ALA A 1 11  ? 24.979 26.232 23.534 1.00 28.98  ? 14  ALA A CB   1 
ATOM   169  H H    . ALA A 1 11  ? 24.322 28.566 23.385 0.00 28.31  ? 14  ALA A H    1 
ATOM   170  H HA   . ALA A 1 11  ? 23.309 26.523 24.709 0.00 28.38  ? 14  ALA A HA   1 
ATOM   171  H HB1  . ALA A 1 11  ? 25.151 25.335 23.861 0.00 34.79  ? 14  ALA A HB1  1 
ATOM   172  H HB2  . ALA A 1 11  ? 24.482 26.191 22.702 0.00 34.79  ? 14  ALA A HB2  1 
ATOM   173  H HB3  . ALA A 1 11  ? 25.818 26.699 23.395 0.00 34.79  ? 14  ALA A HB3  1 
ATOM   174  N N    A LEU A 1 12  ? 25.871 27.917 26.059 0.60 25.91  ? 15  LEU A N    1 
ATOM   175  N N    B LEU A 1 12  ? 25.875 27.911 26.060 0.40 26.03  ? 15  LEU A N    1 
ATOM   176  C CA   A LEU A 1 12  ? 26.573 28.037 27.328 0.60 28.38  ? 15  LEU A CA   1 
ATOM   177  C CA   B LEU A 1 12  ? 26.563 28.026 27.339 0.40 28.39  ? 15  LEU A CA   1 
ATOM   178  C C    A LEU A 1 12  ? 25.640 28.542 28.420 0.60 26.45  ? 15  LEU A C    1 
ATOM   179  C C    B LEU A 1 12  ? 25.618 28.525 28.421 0.40 26.55  ? 15  LEU A C    1 
ATOM   180  O O    A LEU A 1 12  ? 25.656 28.031 29.542 0.60 26.25  ? 15  LEU A O    1 
ATOM   181  O O    B LEU A 1 12  ? 25.615 28.005 29.541 0.40 26.20  ? 15  LEU A O    1 
ATOM   182  C CB   A LEU A 1 12  ? 27.791 28.962 27.151 0.60 30.00  ? 15  LEU A CB   1 
ATOM   183  C CB   B LEU A 1 12  ? 27.777 28.955 27.207 0.40 30.10  ? 15  LEU A CB   1 
ATOM   184  C CG   A LEU A 1 12  ? 28.745 29.126 28.326 0.60 34.96  ? 15  LEU A CG   1 
ATOM   185  C CG   B LEU A 1 12  ? 28.941 28.388 26.408 0.40 32.99  ? 15  LEU A CG   1 
ATOM   186  C CD1  A LEU A 1 12  ? 29.179 27.787 28.890 0.60 31.65  ? 15  LEU A CD1  1 
ATOM   187  C CD1  B LEU A 1 12  ? 29.904 29.508 26.013 0.40 39.82  ? 15  LEU A CD1  1 
ATOM   188  C CD2  A LEU A 1 12  ? 29.953 29.939 27.886 0.60 32.58  ? 15  LEU A CD2  1 
ATOM   189  C CD2  B LEU A 1 12  ? 29.675 27.307 27.188 0.40 42.15  ? 15  LEU A CD2  1 
ATOM   190  H H    A LEU A 1 12  ? 26.160 28.436 25.437 0.60 31.10  ? 15  LEU A H    1 
ATOM   191  H H    B LEU A 1 12  ? 26.173 28.426 25.440 0.40 31.25  ? 15  LEU A H    1 
ATOM   192  H HA   A LEU A 1 12  ? 26.899 27.167 27.607 0.60 34.07  ? 15  LEU A HA   1 
ATOM   193  H HA   B LEU A 1 12  ? 26.889 27.150 27.601 0.40 34.08  ? 15  LEU A HA   1 
ATOM   194  H HB2  A LEU A 1 12  ? 28.316 28.618 26.412 0.60 36.01  ? 15  LEU A HB2  1 
ATOM   195  H HB2  B LEU A 1 12  ? 27.491 29.770 26.765 0.40 36.14  ? 15  LEU A HB2  1 
ATOM   196  H HB3  A LEU A 1 12  ? 27.458 29.848 26.938 0.60 36.01  ? 15  LEU A HB3  1 
ATOM   197  H HB3  B LEU A 1 12  ? 28.106 29.157 28.096 0.40 36.14  ? 15  LEU A HB3  1 
ATOM   198  H HG   A LEU A 1 12  ? 28.287 29.594 29.041 0.60 41.97  ? 15  LEU A HG   1 
ATOM   199  H HG   B LEU A 1 12  ? 28.591 27.978 25.601 0.40 39.60  ? 15  LEU A HG   1 
ATOM   200  H HD11 A LEU A 1 12  ? 29.861 27.934 29.564 0.60 37.99  ? 15  LEU A HD11 1 
ATOM   201  H HD11 B LEU A 1 12  ? 30.603 29.140 25.450 0.40 47.80  ? 15  LEU A HD11 1 
ATOM   202  H HD12 A LEU A 1 12  ? 28.411 27.347 29.287 0.60 37.99  ? 15  LEU A HD12 1 
ATOM   203  H HD12 B LEU A 1 12  ? 29.413 30.190 25.528 0.40 47.80  ? 15  LEU A HD12 1 
ATOM   204  H HD13 A LEU A 1 12  ? 29.537 27.242 28.171 0.60 37.99  ? 15  LEU A HD13 1 
ATOM   205  H HD13 B LEU A 1 12  ? 30.292 29.889 26.816 0.40 47.80  ? 15  LEU A HD13 1 
ATOM   206  H HD21 A LEU A 1 12  ? 30.405 30.283 28.672 0.60 39.11  ? 15  LEU A HD21 1 
ATOM   207  H HD21 B LEU A 1 12  ? 30.412 26.976 26.650 0.40 50.60  ? 15  LEU A HD21 1 
ATOM   208  H HD22 A LEU A 1 12  ? 30.553 29.367 27.383 0.60 39.11  ? 15  LEU A HD22 1 
ATOM   209  H HD22 B LEU A 1 12  ? 30.013 27.688 28.013 0.40 50.60  ? 15  LEU A HD22 1 
ATOM   210  H HD23 A LEU A 1 12  ? 29.653 30.674 27.329 0.60 39.11  ? 15  LEU A HD23 1 
ATOM   211  H HD23 B LEU A 1 12  ? 29.058 26.585 27.384 0.40 50.60  ? 15  LEU A HD23 1 
ATOM   212  N N    . GLY A 1 13  ? 24.775 29.513 28.096 1.00 21.78  ? 16  GLY A N    1 
ATOM   213  C CA   . GLY A 1 13  ? 23.834 29.999 29.082 1.00 21.11  ? 16  GLY A CA   1 
ATOM   214  C C    . GLY A 1 13  ? 22.874 28.901 29.524 1.00 25.97  ? 16  GLY A C    1 
ATOM   215  O O    . GLY A 1 13  ? 22.524 28.787 30.697 1.00 24.53  ? 16  GLY A O    1 
ATOM   216  H H    . GLY A 1 13  ? 24.725 29.890 27.325 0.00 26.15  ? 16  GLY A H    1 
ATOM   217  H HA2  . GLY A 1 13  ? 24.315 30.321 29.860 0.00 25.34  ? 16  GLY A HA2  1 
ATOM   218  H HA3  . GLY A 1 13  ? 23.317 30.729 28.706 0.00 25.34  ? 16  GLY A HA3  1 
ATOM   219  N N    . THR A 1 14  ? 22.405 28.085 28.574 1.00 21.43  ? 17  THR A N    1 
ATOM   220  C CA   . THR A 1 14  ? 21.534 26.979 28.926 1.00 22.00  ? 17  THR A CA   1 
ATOM   221  C C    . THR A 1 14  ? 22.226 26.049 29.896 1.00 25.97  ? 17  THR A C    1 
ATOM   222  O O    . THR A 1 14  ? 21.617 25.606 30.892 1.00 24.56  ? 17  THR A O    1 
ATOM   223  C CB   . THR A 1 14  ? 21.106 26.226 27.672 1.00 21.94  ? 17  THR A CB   1 
ATOM   224  O OG1  . THR A 1 14  ? 20.403 27.100 26.779 1.00 22.15  ? 17  THR A OG1  1 
ATOM   225  C CG2  . THR A 1 14  ? 20.146 25.064 28.026 1.00 26.26  ? 17  THR A CG2  1 
ATOM   226  H H    . THR A 1 14  ? 22.577 28.155 27.735 0.00 25.73  ? 17  THR A H    1 
ATOM   227  H HA   . THR A 1 14  ? 20.733 27.328 29.350 0.00 26.41  ? 17  THR A HA   1 
ATOM   228  H HB   . THR A 1 14  ? 21.903 25.875 27.245 0.00 26.35  ? 17  THR A HB   1 
ATOM   229  H HG1  . THR A 1 14  ? 20.900 27.738 26.551 0.00 26.60  ? 17  THR A HG1  1 
ATOM   230  H HG21 . THR A 1 14  ? 19.767 24.688 27.217 0.00 31.52  ? 17  THR A HG21 1 
ATOM   231  H HG22 . THR A 1 14  ? 20.627 24.369 28.502 0.00 31.52  ? 17  THR A HG22 1 
ATOM   232  H HG23 . THR A 1 14  ? 19.426 25.389 28.589 0.00 31.52  ? 17  THR A HG23 1 
ATOM   233  N N    . ALA A 1 15  ? 23.487 25.700 29.593 1.00 23.99  ? 18  ALA A N    1 
ATOM   234  C CA   . ALA A 1 15  ? 24.208 24.748 30.426 1.00 26.60  ? 18  ALA A CA   1 
ATOM   235  C C    . ALA A 1 15  ? 24.441 25.318 31.822 1.00 26.52  ? 18  ALA A C    1 
ATOM   236  O O    . ALA A 1 15  ? 24.257 24.613 32.828 1.00 28.59  ? 18  ALA A O    1 
ATOM   237  C CB   . ALA A 1 15  ? 25.541 24.392 29.765 1.00 29.61  ? 18  ALA A CB   1 
ATOM   238  H H    . ALA A 1 15  ? 23.934 25.999 28.922 0.00 28.80  ? 18  ALA A H    1 
ATOM   239  H HA   . ALA A 1 15  ? 23.685 23.936 30.511 0.00 31.93  ? 18  ALA A HA   1 
ATOM   240  H HB1  . ALA A 1 15  ? 26.011 23.755 30.326 0.00 35.54  ? 18  ALA A HB1  1 
ATOM   241  H HB2  . ALA A 1 15  ? 25.367 24.000 28.895 0.00 35.54  ? 18  ALA A HB2  1 
ATOM   242  H HB3  . ALA A 1 15  ? 26.070 25.199 29.665 0.00 35.54  ? 18  ALA A HB3  1 
ATOM   243  N N    . LEU A 1 16  ? 24.806 26.598 31.904 1.00 23.36  ? 19  LEU A N    1 
ATOM   244  C CA   . LEU A 1 16  ? 25.147 27.159 33.214 1.00 25.28  ? 19  LEU A CA   1 
ATOM   245  C C    . LEU A 1 16  ? 23.877 27.307 34.066 1.00 24.87  ? 19  LEU A C    1 
ATOM   246  O O    . LEU A 1 16  ? 23.917 27.098 35.277 1.00 26.76  ? 19  LEU A O    1 
ATOM   247  C CB   . LEU A 1 16  ? 25.877 28.478 33.051 1.00 26.14  ? 19  LEU A CB   1 
ATOM   248  C CG   . LEU A 1 16  ? 27.272 28.343 32.428 1.00 28.17  ? 19  LEU A CG   1 
ATOM   249  C CD1  . LEU A 1 16  ? 27.855 29.712 32.137 1.00 34.97  ? 19  LEU A CD1  1 
ATOM   250  C CD2  . LEU A 1 16  ? 28.178 27.533 33.355 1.00 36.67  ? 19  LEU A CD2  1 
ATOM   251  H H    . LEU A 1 16  ? 24.864 27.144 31.242 0.00 28.05  ? 19  LEU A H    1 
ATOM   252  H HA   . LEU A 1 16  ? 25.756 26.565 33.680 0.00 30.35  ? 19  LEU A HA   1 
ATOM   253  H HB2  . LEU A 1 16  ? 25.350 29.056 32.477 0.00 31.38  ? 19  LEU A HB2  1 
ATOM   254  H HB3  . LEU A 1 16  ? 25.981 28.885 33.926 0.00 31.38  ? 19  LEU A HB3  1 
ATOM   255  H HG   . LEU A 1 16  ? 27.211 27.871 31.583 0.00 33.82  ? 19  LEU A HG   1 
ATOM   256  H HD11 . LEU A 1 16  ? 28.742 29.604 31.760 0.00 41.98  ? 19  LEU A HD11 1 
ATOM   257  H HD12 . LEU A 1 16  ? 27.281 30.173 31.505 0.00 41.98  ? 19  LEU A HD12 1 
ATOM   258  H HD13 . LEU A 1 16  ? 27.907 30.216 32.965 0.00 41.98  ? 19  LEU A HD13 1 
ATOM   259  H HD21 . LEU A 1 16  ? 29.095 27.615 33.051 0.00 44.02  ? 19  LEU A HD21 1 
ATOM   260  H HD22 . LEU A 1 16  ? 28.097 27.879 34.257 0.00 44.02  ? 19  LEU A HD22 1 
ATOM   261  H HD23 . LEU A 1 16  ? 27.903 26.603 33.331 0.00 44.02  ? 19  LEU A HD23 1 
ATOM   262  N N    . MET A 1 17  ? 22.752 27.684 33.454 1.00 21.51  ? 20  MET A N    1 
ATOM   263  C CA   . MET A 1 17  ? 21.521 27.775 34.253 1.00 21.30  ? 20  MET A CA   1 
ATOM   264  C C    . MET A 1 17  ? 21.080 26.386 34.701 1.00 22.62  ? 20  MET A C    1 
ATOM   265  O O    . MET A 1 17  ? 20.541 26.233 35.805 1.00 25.20  ? 20  MET A O    1 
ATOM   266  C CB   . MET A 1 17  ? 20.368 28.424 33.442 1.00 23.21  ? 20  MET A CB   1 
ATOM   267  C CG   . MET A 1 17  ? 20.681 29.861 33.069 1.00 22.11  ? 20  MET A CG   1 
ATOM   268  S SD   . MET A 1 17  ? 20.851 30.926 34.523 1.00 24.05  ? 20  MET A SD   1 
ATOM   269  C CE   . MET A 1 17  ? 21.073 32.502 33.692 1.00 23.09  ? 20  MET A CE   1 
ATOM   270  H H    . MET A 1 17  ? 22.675 27.883 32.621 0.00 25.82  ? 20  MET A H    1 
ATOM   271  H HA   . MET A 1 17  ? 21.706 28.344 35.016 0.00 25.57  ? 20  MET A HA   1 
ATOM   272  H HB2  . MET A 1 17  ? 20.229 27.920 32.625 0.00 27.86  ? 20  MET A HB2  1 
ATOM   273  H HB3  . MET A 1 17  ? 19.558 28.418 33.977 0.00 27.86  ? 20  MET A HB3  1 
ATOM   274  H HG2  . MET A 1 17  ? 21.516 29.887 32.576 0.00 26.55  ? 20  MET A HG2  1 
ATOM   275  H HG3  . MET A 1 17  ? 19.961 30.211 32.520 0.00 26.55  ? 20  MET A HG3  1 
ATOM   276  H HE1  . MET A 1 17  ? 21.168 33.200 34.359 0.00 27.72  ? 20  MET A HE1  1 
ATOM   277  H HE2  . MET A 1 17  ? 21.871 32.459 33.142 0.00 27.72  ? 20  MET A HE2  1 
ATOM   278  H HE3  . MET A 1 17  ? 20.298 32.678 33.136 0.00 27.72  ? 20  MET A HE3  1 
ATOM   279  N N    . GLY A 1 18  ? 21.260 25.397 33.841 1.00 25.24  ? 21  GLY A N    1 
ATOM   280  C CA   . GLY A 1 18  ? 20.869 24.034 34.210 1.00 26.82  ? 21  GLY A CA   1 
ATOM   281  C C    . GLY A 1 18  ? 21.713 23.512 35.350 1.00 28.37  ? 21  GLY A C    1 
ATOM   282  O O    . GLY A 1 18  ? 21.187 22.924 36.291 1.00 27.93  ? 21  GLY A O    1 
ATOM   283  H H    . GLY A 1 18  ? 21.597 25.478 33.054 0.00 30.30  ? 21  GLY A H    1 
ATOM   284  H HA2  . GLY A 1 18  ? 19.939 24.025 34.484 0.00 32.19  ? 21  GLY A HA2  1 
ATOM   285  H HA3  . GLY A 1 18  ? 20.980 23.446 33.447 0.00 32.19  ? 21  GLY A HA3  1 
ATOM   286  N N    . LEU A 1 19  ? 23.026 23.708 35.261 1.00 27.08  ? 22  LEU A N    1 
ATOM   287  C CA   . LEU A 1 19  ? 23.925 23.265 36.329 1.00 27.48  ? 22  LEU A CA   1 
ATOM   288  C C    . LEU A 1 19  ? 23.644 24.027 37.616 1.00 31.90  ? 22  LEU A C    1 
ATOM   289  O O    . LEU A 1 19  ? 23.672 23.446 38.707 1.00 31.80  ? 22  LEU A O    1 
ATOM   290  C CB   . LEU A 1 19  ? 25.375 23.450 35.902 1.00 30.60  ? 22  LEU A CB   1 
ATOM   291  C CG   . LEU A 1 19  ? 25.861 22.534 34.782 1.00 42.74  ? 22  LEU A CG   1 
ATOM   292  C CD1  . LEU A 1 19  ? 27.269 22.921 34.365 1.00 54.79  ? 22  LEU A CD1  1 
ATOM   293  C CD2  . LEU A 1 19  ? 25.807 21.063 35.205 1.00 52.04  ? 22  LEU A CD2  1 
ATOM   294  H H    . LEU A 1 19  ? 23.421 24.092 34.600 1.00 32.51  ? 22  LEU A H    1 
ATOM   295  H HA   . LEU A 1 19  ? 23.783 22.320 36.494 1.00 32.99  ? 22  LEU A HA   1 
ATOM   296  H HB2  . LEU A 1 19  ? 25.487 24.364 35.596 1.00 36.73  ? 22  LEU A HB2  1 
ATOM   297  H HB3  . LEU A 1 19  ? 25.941 23.288 36.673 1.00 36.73  ? 22  LEU A HB3  1 
ATOM   298  H HG   . LEU A 1 19  ? 25.273 22.637 34.017 1.00 51.30  ? 22  LEU A HG   1 
ATOM   299  H HD11 . LEU A 1 19  ? 27.550 22.351 33.632 1.00 65.76  ? 22  LEU A HD11 1 
ATOM   300  H HD12 . LEU A 1 19  ? 27.271 23.849 34.082 1.00 65.76  ? 22  LEU A HD12 1 
ATOM   301  H HD13 . LEU A 1 19  ? 27.866 22.805 35.121 1.00 65.76  ? 22  LEU A HD13 1 
ATOM   302  H HD21 . LEU A 1 19  ? 26.211 20.519 34.510 1.00 62.46  ? 22  LEU A HD21 1 
ATOM   303  H HD22 . LEU A 1 19  ? 26.296 20.954 36.035 1.00 62.46  ? 22  LEU A HD22 1 
ATOM   304  H HD23 . LEU A 1 19  ? 24.881 20.804 35.330 1.00 62.46  ? 22  LEU A HD23 1 
ATOM   305  N N    . GLY A 1 20  ? 23.390 25.333 37.518 1.00 24.40  ? 23  GLY A N    1 
ATOM   306  C CA   . GLY A 1 20  ? 23.031 26.103 38.703 1.00 25.23  ? 23  GLY A CA   1 
ATOM   307  C C    . GLY A 1 20  ? 21.764 25.592 39.351 1.00 28.57  ? 23  GLY A C    1 
ATOM   308  O O    . GLY A 1 20  ? 21.682 25.466 40.581 1.00 27.36  ? 23  GLY A O    1 
ATOM   309  H H    . GLY A 1 20  ? 23.420 25.789 36.789 0.00 29.29  ? 23  GLY A H    1 
ATOM   310  H HA2  . GLY A 1 20  ? 23.750 26.049 39.352 0.00 30.29  ? 23  GLY A HA2  1 
ATOM   311  H HA3  . GLY A 1 20  ? 22.896 27.031 38.456 0.00 30.29  ? 23  GLY A HA3  1 
ATOM   312  N N    . THR A 1 21  ? 20.762 25.256 38.537 1.00 25.11  ? 24  THR A N    1 
ATOM   313  C CA   . THR A 1 21  ? 19.519 24.720 39.091 1.00 26.38  ? 24  THR A CA   1 
ATOM   314  C C    . THR A 1 21  ? 19.773 23.435 39.868 1.00 26.64  ? 24  THR A C    1 
ATOM   315  O O    . THR A 1 21  ? 19.277 23.285 40.987 1.00 27.41  ? 24  THR A O    1 
ATOM   316  C CB   . THR A 1 21  ? 18.517 24.450 37.958 1.00 26.83  ? 24  THR A CB   1 
ATOM   317  O OG1  . THR A 1 21  ? 18.247 25.666 37.267 1.00 24.07  ? 24  THR A OG1  1 
ATOM   318  C CG2  . THR A 1 21  ? 17.190 23.914 38.520 1.00 31.61  ? 24  THR A CG2  1 
ATOM   319  H H    . THR A 1 21  ? 20.777 25.327 37.680 0.00 30.14  ? 24  THR A H    1 
ATOM   320  H HA   . THR A 1 21  ? 19.141 25.380 39.694 0.00 31.66  ? 24  THR A HA   1 
ATOM   321  H HB   . THR A 1 21  ? 18.892 23.791 37.353 0.00 32.20  ? 24  THR A HB   1 
ATOM   322  H HG1  . THR A 1 21  ? 18.955 25.970 36.933 0.00 28.90  ? 24  THR A HG1  1 
ATOM   323  H HG21 . THR A 1 21  ? 16.504 23.942 37.836 0.00 37.95  ? 24  THR A HG21 1 
ATOM   324  H HG22 . THR A 1 21  ? 17.301 22.997 38.816 0.00 37.95  ? 24  THR A HG22 1 
ATOM   325  H HG23 . THR A 1 21  ? 16.906 24.455 39.273 0.00 37.95  ? 24  THR A HG23 1 
ATOM   326  N N    . LEU A 1 22  ? 20.504 22.496 39.265 1.00 25.83  ? 25  LEU A N    1 
ATOM   327  C CA   . LEU A 1 22  ? 20.758 21.203 39.897 1.00 25.76  ? 25  LEU A CA   1 
ATOM   328  C C    . LEU A 1 22  ? 21.546 21.377 41.182 1.00 28.02  ? 25  LEU A C    1 
ATOM   329  O O    . LEU A 1 22  ? 21.279 20.670 42.178 1.00 30.71  ? 25  LEU A O    1 
ATOM   330  C CB   . LEU A 1 22  ? 21.510 20.289 38.945 1.00 32.52  ? 25  LEU A CB   1 
ATOM   331  C CG   . LEU A 1 22  ? 20.688 19.764 37.770 1.00 45.86  ? 25  LEU A CG   1 
ATOM   332  C CD1  . LEU A 1 22  ? 21.635 19.239 36.697 1.00 43.78  ? 25  LEU A CD1  1 
ATOM   333  C CD2  . LEU A 1 22  ? 19.718 18.685 38.215 1.00 54.98  ? 25  LEU A CD2  1 
ATOM   334  H H    . LEU A 1 22  ? 20.865 22.582 38.489 1.00 31.00  ? 25  LEU A H    1 
ATOM   335  H HA   . LEU A 1 22  ? 19.907 20.786 40.106 1.00 30.93  ? 25  LEU A HA   1 
ATOM   336  H HB2  . LEU A 1 22  ? 22.262 20.781 38.578 1.00 39.03  ? 25  LEU A HB2  1 
ATOM   337  H HB3  . LEU A 1 22  ? 21.829 19.521 39.445 1.00 39.03  ? 25  LEU A HB3  1 
ATOM   338  H HG   . LEU A 1 22  ? 20.154 20.482 37.398 1.00 55.04  ? 25  LEU A HG   1 
ATOM   339  H HD11 . LEU A 1 22  ? 21.113 18.870 35.968 1.00 52.55  ? 25  LEU A HD11 1 
ATOM   340  H HD12 . LEU A 1 22  ? 22.183 19.971 36.374 1.00 52.55  ? 25  LEU A HD12 1 
ATOM   341  H HD13 . LEU A 1 22  ? 22.199 18.550 37.082 1.00 52.55  ? 25  LEU A HD13 1 
ATOM   342  H HD21 . LEU A 1 22  ? 19.210 18.381 37.447 1.00 65.99  ? 25  LEU A HD21 1 
ATOM   343  H HD22 . LEU A 1 22  ? 20.219 17.946 38.595 1.00 65.99  ? 25  LEU A HD22 1 
ATOM   344  H HD23 . LEU A 1 22  ? 19.119 19.055 38.882 1.00 65.99  ? 25  LEU A HD23 1 
ATOM   345  N N    . TYR A 1 23  ? 22.528 22.277 41.182 1.00 25.57  ? 26  TYR A N    1 
ATOM   346  C CA   . TYR A 1 23  ? 23.312 22.493 42.404 1.00 30.21  ? 26  TYR A CA   1 
ATOM   347  C C    . TYR A 1 23  ? 22.426 23.002 43.539 1.00 27.92  ? 26  TYR A C    1 
ATOM   348  O O    . TYR A 1 23  ? 22.462 22.461 44.651 1.00 29.61  ? 26  TYR A O    1 
ATOM   349  C CB   . TYR A 1 23  ? 24.467 23.457 42.144 1.00 27.69  ? 26  TYR A CB   1 
ATOM   350  C CG   . TYR A 1 23  ? 25.318 23.735 43.352 1.00 28.07  ? 26  TYR A CG   1 
ATOM   351  C CD1  . TYR A 1 23  ? 26.164 22.762 43.866 1.00 42.67  ? 26  TYR A CD1  1 
ATOM   352  C CD2  . TYR A 1 23  ? 25.272 24.960 43.989 1.00 31.34  ? 26  TYR A CD2  1 
ATOM   353  C CE1  . TYR A 1 23  ? 26.946 23.011 44.982 1.00 44.51  ? 26  TYR A CE1  1 
ATOM   354  C CE2  . TYR A 1 23  ? 26.043 25.226 45.107 1.00 38.26  ? 26  TYR A CE2  1 
ATOM   355  C CZ   . TYR A 1 23  ? 26.882 24.250 45.592 1.00 45.18  ? 26  TYR A CZ   1 
ATOM   356  O OH   . TYR A 1 23  ? 27.655 24.499 46.698 1.00 51.72  ? 26  TYR A OH   1 
ATOM   357  H H    . TYR A 1 23  ? 22.757 22.763 40.510 0.00 30.69  ? 26  TYR A H    1 
ATOM   358  H HA   . TYR A 1 23  ? 23.697 21.645 42.675 0.00 36.26  ? 26  TYR A HA   1 
ATOM   359  H HB2  . TYR A 1 23  ? 25.041 23.077 41.460 0.00 33.24  ? 26  TYR A HB2  1 
ATOM   360  H HB3  . TYR A 1 23  ? 24.103 24.303 41.839 0.00 33.24  ? 26  TYR A HB3  1 
ATOM   361  H HD1  . TYR A 1 23  ? 26.207 21.930 43.455 0.00 51.21  ? 26  TYR A HD1  1 
ATOM   362  H HD2  . TYR A 1 23  ? 24.708 25.622 43.658 0.00 37.62  ? 26  TYR A HD2  1 
ATOM   363  H HE1  . TYR A 1 23  ? 27.508 22.351 45.318 0.00 53.42  ? 26  TYR A HE1  1 
ATOM   364  H HE2  . TYR A 1 23  ? 25.996 26.056 45.525 0.00 45.93  ? 26  TYR A HE2  1 
ATOM   365  H HH   . TYR A 1 23  ? 27.889 25.306 46.709 0.00 62.08  ? 26  TYR A HH   1 
ATOM   366  N N    . PHE A 1 24  ? 21.615 24.034 43.263 1.00 27.10  ? 27  PHE A N    1 
ATOM   367  C CA   . PHE A 1 24  ? 20.765 24.583 44.326 1.00 27.26  ? 27  PHE A CA   1 
ATOM   368  C C    . PHE A 1 24  ? 19.754 23.539 44.784 1.00 30.19  ? 27  PHE A C    1 
ATOM   369  O O    . PHE A 1 24  ? 19.386 23.502 45.953 1.00 32.48  ? 27  PHE A O    1 
ATOM   370  C CB   . PHE A 1 24  ? 20.034 25.847 43.837 1.00 25.07  ? 27  PHE A CB   1 
ATOM   371  C CG   . PHE A 1 24  ? 20.938 27.010 43.543 1.00 26.35  ? 27  PHE A CG   1 
ATOM   372  C CD1  . PHE A 1 24  ? 22.185 27.130 44.152 1.00 29.54  ? 27  PHE A CD1  1 
ATOM   373  C CD2  . PHE A 1 24  ? 20.530 28.005 42.685 1.00 26.01  ? 27  PHE A CD2  1 
ATOM   374  C CE1  . PHE A 1 24  ? 23.007 28.217 43.881 1.00 36.24  ? 27  PHE A CE1  1 
ATOM   375  C CE2  . PHE A 1 24  ? 21.351 29.112 42.412 1.00 32.41  ? 27  PHE A CE2  1 
ATOM   376  C CZ   . PHE A 1 24  ? 22.597 29.201 43.014 1.00 34.55  ? 27  PHE A CZ   1 
ATOM   377  H H    . PHE A 1 24  ? 21.542 24.419 42.497 0.00 32.54  ? 27  PHE A H    1 
ATOM   378  H HA   . PHE A 1 24  ? 21.324 24.838 45.076 0.00 32.73  ? 27  PHE A HA   1 
ATOM   379  H HB2  . PHE A 1 24  ? 19.557 25.633 43.021 0.00 30.10  ? 27  PHE A HB2  1 
ATOM   380  H HB3  . PHE A 1 24  ? 19.409 26.128 44.523 0.00 30.10  ? 27  PHE A HB3  1 
ATOM   381  H HD1  . PHE A 1 24  ? 22.471 26.475 44.747 0.00 35.46  ? 27  PHE A HD1  1 
ATOM   382  H HD2  . PHE A 1 24  ? 19.695 27.944 42.279 0.00 31.23  ? 27  PHE A HD2  1 
ATOM   383  H HE1  . PHE A 1 24  ? 23.840 28.279 44.289 0.00 43.50  ? 27  PHE A HE1  1 
ATOM   384  H HE2  . PHE A 1 24  ? 21.062 29.779 41.833 0.00 38.90  ? 27  PHE A HE2  1 
ATOM   385  H HZ   . PHE A 1 24  ? 23.153 29.923 42.832 0.00 41.48  ? 27  PHE A HZ   1 
ATOM   386  N N    . LEU A 1 25  ? 19.269 22.706 43.846 1.00 26.23  ? 28  LEU A N    1 
ATOM   387  C CA   . LEU A 1 25  ? 18.280 21.699 44.217 1.00 30.77  ? 28  LEU A CA   1 
ATOM   388  C C    . LEU A 1 25  ? 18.883 20.673 45.170 1.00 33.25  ? 28  LEU A C    1 
ATOM   389  O O    . LEU A 1 25  ? 18.263 20.305 46.178 1.00 37.89  ? 28  LEU A O    1 
ATOM   390  C CB   . LEU A 1 25  ? 17.751 21.009 42.958 1.00 43.33  ? 28  LEU A CB   1 
ATOM   391  C CG   . LEU A 1 25  ? 16.532 20.113 43.164 1.00 51.87  ? 28  LEU A CG   1 
ATOM   392  C CD1  . LEU A 1 25  ? 15.305 20.935 43.515 1.00 46.51  ? 28  LEU A CD1  1 
ATOM   393  C CD2  . LEU A 1 25  ? 16.275 19.268 41.922 1.00 63.02  ? 28  LEU A CD2  1 
ATOM   394  H H    . LEU A 1 25  ? 19.494 22.709 43.016 0.00 31.48  ? 28  LEU A H    1 
ATOM   395  H HA   . LEU A 1 25  ? 17.536 22.133 44.665 0.00 36.94  ? 28  LEU A HA   1 
ATOM   396  H HB2  . LEU A 1 25  ? 17.502 21.694 42.318 0.00 52.01  ? 28  LEU A HB2  1 
ATOM   397  H HB3  . LEU A 1 25  ? 18.460 20.456 42.594 0.00 52.01  ? 28  LEU A HB3  1 
ATOM   398  H HG   . LEU A 1 25  ? 16.709 19.515 43.907 0.00 62.26  ? 28  LEU A HG   1 
ATOM   399  H HD11 . LEU A 1 25  ? 14.548 20.339 43.626 0.00 55.82  ? 28  LEU A HD11 1 
ATOM   400  H HD12 . LEU A 1 25  ? 15.472 21.414 44.341 0.00 55.82  ? 28  LEU A HD12 1 
ATOM   401  H HD13 . LEU A 1 25  ? 15.130 21.563 42.797 0.00 55.82  ? 28  LEU A HD13 1 
ATOM   402  H HD21 . LEU A 1 25  ? 15.502 18.703 42.079 0.00 75.63  ? 28  LEU A HD21 1 
ATOM   403  H HD22 . LEU A 1 25  ? 16.106 19.857 41.169 0.00 75.63  ? 28  LEU A HD22 1 
ATOM   404  H HD23 . LEU A 1 25  ? 17.055 18.721 41.745 0.00 75.63  ? 28  LEU A HD23 1 
ATOM   405  N N    . VAL A 1 26  ? 20.091 20.196 44.873 1.00 32.74  ? 29  VAL A N    1 
ATOM   406  C CA   . VAL A 1 26  ? 20.721 19.210 45.749 1.00 33.56  ? 29  VAL A CA   1 
ATOM   407  C C    . VAL A 1 26  ? 21.105 19.846 47.072 1.00 37.80  ? 29  VAL A C    1 
ATOM   408  O O    . VAL A 1 26  ? 20.929 19.232 48.144 1.00 37.30  ? 29  VAL A O    1 
ATOM   409  C CB   . VAL A 1 26  ? 21.951 18.584 45.051 1.00 38.47  ? 29  VAL A CB   1 
ATOM   410  C CG1  . VAL A 1 26  ? 22.676 17.648 45.991 1.00 45.54  ? 29  VAL A CG1  1 
ATOM   411  C CG2  . VAL A 1 26  ? 21.520 17.863 43.784 1.00 49.85  ? 29  VAL A CG2  1 
ATOM   412  H H    . VAL A 1 26  ? 20.556 20.422 44.186 0.00 39.30  ? 29  VAL A H    1 
ATOM   413  H HA   . VAL A 1 26  ? 20.081 18.504 45.927 0.00 40.28  ? 29  VAL A HA   1 
ATOM   414  H HB   . VAL A 1 26  ? 22.571 19.287 44.802 0.00 46.18  ? 29  VAL A HB   1 
ATOM   415  H HG11 . VAL A 1 26  ? 23.291 17.100 45.479 0.00 54.66  ? 29  VAL A HG11 1 
ATOM   416  H HG12 . VAL A 1 26  ? 23.166 18.173 46.644 0.00 54.66  ? 29  VAL A HG12 1 
ATOM   417  H HG13 . VAL A 1 26  ? 22.026 17.085 46.440 0.00 54.66  ? 29  VAL A HG13 1 
ATOM   418  H HG21 . VAL A 1 26  ? 22.307 17.518 43.334 0.00 59.83  ? 29  VAL A HG21 1 
ATOM   419  H HG22 . VAL A 1 26  ? 20.929 17.131 44.022 0.00 59.83  ? 29  VAL A HG22 1 
ATOM   420  H HG23 . VAL A 1 26  ? 21.056 18.489 43.207 0.00 59.83  ? 29  VAL A HG23 1 
ATOM   421  N N    . LYS A 1 27  ? 21.659 21.064 47.026 1.00 31.26  ? 30  LYS A N    1 
ATOM   422  C CA   . LYS A 1 27  ? 22.048 21.750 48.258 1.00 34.19  ? 30  LYS A CA   1 
ATOM   423  C C    . LYS A 1 27  ? 20.854 21.922 49.187 1.00 36.47  ? 30  LYS A C    1 
ATOM   424  O O    . LYS A 1 27  ? 20.985 21.798 50.409 1.00 44.01  ? 30  LYS A O    1 
ATOM   425  C CB   . LYS A 1 27  ? 22.682 23.101 47.919 1.00 36.81  ? 30  LYS A CB   1 
ATOM   426  C CG   . LYS A 1 27  ? 23.620 23.646 48.966 1.00 48.72  ? 30  LYS A CG   1 
ATOM   427  C CD   . LYS A 1 27  ? 24.007 25.095 48.672 1.00 53.47  ? 30  LYS A CD   1 
ATOM   428  C CE   . LYS A 1 27  ? 25.271 25.498 49.417 1.00 70.11  ? 30  LYS A CE   1 
ATOM   429  N NZ   . LYS A 1 27  ? 26.403 25.751 48.476 1.00 85.99  ? 30  LYS A NZ   1 
ATOM   430  H H    . LYS A 1 27  ? 21.818 21.506 46.305 0.00 37.53  ? 30  LYS A H    1 
ATOM   431  H HA   . LYS A 1 27  ? 22.712 21.220 48.726 0.00 41.05  ? 30  LYS A HA   1 
ATOM   432  H HB2  . LYS A 1 27  ? 23.188 23.005 47.097 0.00 44.19  ? 30  LYS A HB2  1 
ATOM   433  H HB3  . LYS A 1 27  ? 21.973 23.752 47.798 0.00 44.19  ? 30  LYS A HB3  1 
ATOM   434  H HG2  . LYS A 1 27  ? 23.186 23.616 49.833 0.00 58.48  ? 30  LYS A HG2  1 
ATOM   435  H HG3  . LYS A 1 27  ? 24.430 23.112 48.981 0.00 58.48  ? 30  LYS A HG3  1 
ATOM   436  H HD2  . LYS A 1 27  ? 24.168 25.198 47.721 0.00 64.18  ? 30  LYS A HD2  1 
ATOM   437  H HD3  . LYS A 1 27  ? 23.287 25.682 48.953 0.00 64.18  ? 30  LYS A HD3  1 
ATOM   438  H HE2  . LYS A 1 27  ? 25.102 26.312 49.918 0.00 84.15  ? 30  LYS A HE2  1 
ATOM   439  H HE3  . LYS A 1 27  ? 25.529 24.785 50.021 0.00 84.15  ? 30  LYS A HE3  1 
ATOM   440  H HZ1  . LYS A 1 27  ? 27.122 26.015 48.929 0.00 103.21 ? 30  LYS A HZ1  1 
ATOM   441  H HZ2  . LYS A 1 27  ? 26.599 25.007 48.029 0.00 103.21 ? 30  LYS A HZ2  1 
ATOM   442  H HZ3  . LYS A 1 27  ? 26.179 26.387 47.894 0.00 103.21 ? 30  LYS A HZ3  1 
ATOM   443  N N    . GLY A 1 28  ? 19.670 22.206 48.619 1.00 36.62  ? 31  GLY A N    1 
ATOM   444  C CA   . GLY A 1 28  ? 18.492 22.411 49.440 1.00 40.50  ? 31  GLY A CA   1 
ATOM   445  C C    . GLY A 1 28  ? 17.825 21.146 49.925 1.00 49.70  ? 31  GLY A C    1 
ATOM   446  O O    . GLY A 1 28  ? 16.881 21.232 50.722 1.00 44.72  ? 31  GLY A O    1 
ATOM   447  H H    . GLY A 1 28  ? 19.536 22.281 47.773 0.00 43.96  ? 31  GLY A H    1 
ATOM   448  H HA2  . GLY A 1 28  ? 18.744 22.929 50.220 0.00 48.61  ? 31  GLY A HA2  1 
ATOM   449  H HA3  . GLY A 1 28  ? 17.839 22.911 48.926 0.00 48.61  ? 31  GLY A HA3  1 
ATOM   450  N N    . MET A 1 29  ? 18.296 19.985 49.471 1.00 46.00  ? 32  MET A N    1 
ATOM   451  C CA   . MET A 1 29  ? 17.742 18.711 49.915 1.00 57.72  ? 32  MET A CA   1 
ATOM   452  C C    . MET A 1 29  ? 18.075 18.498 51.380 1.00 53.88  ? 32  MET A C    1 
ATOM   453  O O    . MET A 1 29  ? 19.251 18.461 51.760 1.00 73.48  ? 32  MET A O    1 
ATOM   454  C CB   . MET A 1 29  ? 18.298 17.565 49.074 1.00 65.01  ? 32  MET A CB   1 
ATOM   455  C CG   . MET A 1 29  ? 17.432 17.188 47.886 1.00 76.14  ? 32  MET A CG   1 
ATOM   456  S SD   . MET A 1 29  ? 18.175 15.879 46.885 1.00 95.16  ? 32  MET A SD   1 
ATOM   457  C CE   . MET A 1 29  ? 17.812 14.437 47.881 1.00 80.81  ? 32  MET A CE   1 
ATOM   458  H H    . MET A 1 29  ? 18.939 19.910 48.905 0.00 55.21  ? 32  MET A H    1 
ATOM   459  H HA   . MET A 1 29  ? 16.779 18.727 49.796 0.00 69.27  ? 32  MET A HA   1 
ATOM   460  H HB2  . MET A 1 29  ? 19.168 17.824 48.733 0.00 78.02  ? 32  MET A HB2  1 
ATOM   461  H HB3  . MET A 1 29  ? 18.383 16.780 49.637 0.00 78.02  ? 32  MET A HB3  1 
ATOM   462  H HG2  . MET A 1 29  ? 16.573 16.872 48.207 0.00 91.38  ? 32  MET A HG2  1 
ATOM   463  H HG3  . MET A 1 29  ? 17.309 17.968 47.322 0.00 91.38  ? 32  MET A HG3  1 
ATOM   464  H HE1  . MET A 1 29  ? 18.166 13.650 47.438 0.00 96.99  ? 32  MET A HE1  1 
ATOM   465  H HE2  . MET A 1 29  ? 18.228 14.542 48.751 0.00 96.99  ? 32  MET A HE2  1 
ATOM   466  H HE3  . MET A 1 29  ? 16.851 14.357 47.982 0.00 96.99  ? 32  MET A HE3  1 
ATOM   467  N N    . GLY A 1 30  ? 17.050 18.357 52.204 1.00 58.75  ? 33  GLY A N    1 
ATOM   468  C CA   . GLY A 1 30  ? 17.229 18.105 53.614 1.00 64.13  ? 33  GLY A CA   1 
ATOM   469  C C    . GLY A 1 30  ? 17.130 19.326 54.499 1.00 70.22  ? 33  GLY A C    1 
ATOM   470  O O    . GLY A 1 30  ? 17.002 19.172 55.722 1.00 75.73  ? 33  GLY A O    1 
ATOM   471  H H    . GLY A 1 30  ? 16.226 18.405 51.961 0.00 70.51  ? 33  GLY A H    1 
ATOM   472  H HA2  . GLY A 1 30  ? 16.551 17.474 53.905 0.00 76.97  ? 33  GLY A HA2  1 
ATOM   473  H HA3  . GLY A 1 30  ? 18.105 17.712 53.751 0.00 76.97  ? 33  GLY A HA3  1 
ATOM   474  N N    . VAL A 1 31  ? 17.196 20.531 53.929 1.00 53.23  ? 34  VAL A N    1 
ATOM   475  C CA   . VAL A 1 31  ? 16.974 21.727 54.731 1.00 54.06  ? 34  VAL A CA   1 
ATOM   476  C C    . VAL A 1 31  ? 15.569 21.664 55.314 1.00 53.11  ? 34  VAL A C    1 
ATOM   477  O O    . VAL A 1 31  ? 14.586 21.463 54.586 1.00 56.69  ? 34  VAL A O    1 
ATOM   478  C CB   . VAL A 1 31  ? 17.183 22.989 53.883 1.00 62.03  ? 34  VAL A CB   1 
ATOM   479  C CG1  . VAL A 1 31  ? 16.779 24.231 54.673 1.00 55.92  ? 34  VAL A CG1  1 
ATOM   480  C CG2  . VAL A 1 31  ? 18.631 23.085 53.421 1.00 55.92  ? 34  VAL A CG2  1 
ATOM   481  H H    . VAL A 1 31  ? 17.364 20.678 53.099 0.00 63.88  ? 34  VAL A H    1 
ATOM   482  H HA   . VAL A 1 31  ? 17.614 21.753 55.459 0.00 64.89  ? 34  VAL A HA   1 
ATOM   483  H HB   . VAL A 1 31  ? 16.620 22.940 53.095 0.00 74.45  ? 34  VAL A HB   1 
ATOM   484  H HG11 . VAL A 1 31  ? 17.092 25.019 54.203 0.00 67.11  ? 34  VAL A HG11 1 
ATOM   485  H HG12 . VAL A 1 31  ? 15.813 24.254 54.753 0.00 67.11  ? 34  VAL A HG12 1 
ATOM   486  H HG13 . VAL A 1 31  ? 17.183 24.189 55.554 0.00 67.11  ? 34  VAL A HG13 1 
ATOM   487  H HG21 . VAL A 1 31  ? 18.747 23.902 52.912 0.00 67.11  ? 34  VAL A HG21 1 
ATOM   488  H HG22 . VAL A 1 31  ? 19.211 23.094 54.198 0.00 67.11  ? 34  VAL A HG22 1 
ATOM   489  H HG23 . VAL A 1 31  ? 18.836 22.317 52.864 0.00 67.11  ? 34  VAL A HG23 1 
ATOM   490  N N    . SER A 1 32  ? 15.464 21.840 56.627 1.00 53.37  ? 35  SER A N    1 
ATOM   491  C CA   . SER A 1 32  ? 14.187 21.737 57.322 1.00 53.67  ? 35  SER A CA   1 
ATOM   492  C C    . SER A 1 32  ? 13.725 23.040 57.949 1.00 65.88  ? 35  SER A C    1 
ATOM   493  O O    . SER A 1 32  ? 12.539 23.157 58.279 1.00 61.63  ? 35  SER A O    1 
ATOM   494  C CB   . SER A 1 32  ? 14.256 20.660 58.417 1.00 66.79  ? 35  SER A CB   1 
ATOM   495  O OG   . SER A 1 32  ? 15.424 20.802 59.209 1.00 74.69  ? 35  SER A OG   1 
ATOM   496  H H    . SER A 1 32  ? 16.126 22.022 57.144 0.00 64.05  ? 35  SER A H    1 
ATOM   497  H HA   . SER A 1 32  ? 13.512 21.464 56.681 0.00 64.42  ? 35  SER A HA   1 
ATOM   498  H HB2  . SER A 1 32  ? 13.477 20.743 58.988 0.00 80.16  ? 35  SER A HB2  1 
ATOM   499  H HB3  . SER A 1 32  ? 14.267 19.785 57.996 0.00 80.16  ? 35  SER A HB3  1 
ATOM   500  H HG   . SER A 1 32  ? 15.405 21.535 59.619 0.00 89.64  ? 35  SER A HG   1 
ATOM   501  N N    . ASP A 1 33  ? 14.616 24.009 58.125 1.00 54.22  ? 36  ASP A N    1 
ATOM   502  C CA   . ASP A 1 33  ? 14.230 25.288 58.709 1.00 56.46  ? 36  ASP A CA   1 
ATOM   503  C C    . ASP A 1 33  ? 13.227 25.976 57.776 1.00 41.06  ? 36  ASP A C    1 
ATOM   504  O O    . ASP A 1 33  ? 13.541 26.202 56.624 1.00 38.76  ? 36  ASP A O    1 
ATOM   505  C CB   . ASP A 1 33  ? 15.457 26.174 58.908 1.00 51.03  ? 36  ASP A CB   1 
ATOM   506  C CG   . ASP A 1 33  ? 15.106 27.523 59.516 1.00 45.62  ? 36  ASP A CG   1 
ATOM   507  O OD1  . ASP A 1 33  ? 14.809 27.568 60.722 1.00 57.10  ? 36  ASP A OD1  1 
ATOM   508  O OD2  . ASP A 1 33  ? 15.119 28.534 58.792 1.00 45.83  ? 36  ASP A OD2  1 
ATOM   509  H H    . ASP A 1 33  ? 15.448 23.951 57.916 0.00 65.08  ? 36  ASP A H    1 
ATOM   510  H HA   . ASP A 1 33  ? 13.822 25.147 59.578 0.00 67.76  ? 36  ASP A HA   1 
ATOM   511  H HB2  . ASP A 1 33  ? 16.078 25.727 59.504 0.00 61.25  ? 36  ASP A HB2  1 
ATOM   512  H HB3  . ASP A 1 33  ? 15.877 26.332 58.048 0.00 61.25  ? 36  ASP A HB3  1 
ATOM   513  N N    . PRO A 1 34  ? 12.033 26.336 58.256 1.00 43.57  ? 37  PRO A N    1 
ATOM   514  C CA   . PRO A 1 34  ? 11.031 26.906 57.338 1.00 47.76  ? 37  PRO A CA   1 
ATOM   515  C C    . PRO A 1 34  ? 11.472 28.199 56.691 1.00 43.11  ? 37  PRO A C    1 
ATOM   516  O O    . PRO A 1 34  ? 11.113 28.457 55.536 1.00 42.23  ? 37  PRO A O    1 
ATOM   517  C CB   . PRO A 1 34  ? 9.793  27.119 58.235 1.00 53.56  ? 37  PRO A CB   1 
ATOM   518  C CG   . PRO A 1 34  ? 10.234 26.913 59.621 1.00 56.17  ? 37  PRO A CG   1 
ATOM   519  C CD   . PRO A 1 34  ? 11.543 26.206 59.645 1.00 50.75  ? 37  PRO A CD   1 
ATOM   520  H HA   . PRO A 1 34  ? 10.817 26.256 56.650 0.00 57.32  ? 37  PRO A HA   1 
ATOM   521  H HB2  . PRO A 1 34  ? 9.459  28.021 58.115 0.00 64.29  ? 37  PRO A HB2  1 
ATOM   522  H HB3  . PRO A 1 34  ? 9.107  26.476 57.997 0.00 64.29  ? 37  PRO A HB3  1 
ATOM   523  H HG2  . PRO A 1 34  ? 10.322 27.779 60.049 0.00 67.42  ? 37  PRO A HG2  1 
ATOM   524  H HG3  . PRO A 1 34  ? 9.567  26.382 60.082 0.00 67.42  ? 37  PRO A HG3  1 
ATOM   525  H HD2  . PRO A 1 34  ? 12.153 26.632 60.267 0.00 60.91  ? 37  PRO A HD2  1 
ATOM   526  H HD3  . PRO A 1 34  ? 11.426 25.273 59.883 0.00 60.91  ? 37  PRO A HD3  1 
ATOM   527  N N    . ASP A 1 35  ? 12.246 29.031 57.397 1.00 45.26  ? 38  ASP A N    1 
ATOM   528  C CA   . ASP A 1 35  ? 12.740 30.260 56.793 1.00 40.60  ? 38  ASP A CA   1 
ATOM   529  C C    . ASP A 1 35  ? 13.715 29.953 55.664 1.00 36.01  ? 38  ASP A C    1 
ATOM   530  O O    . ASP A 1 35  ? 13.612 30.510 54.551 1.00 34.16  ? 38  ASP A O    1 
ATOM   531  C CB   . ASP A 1 35  ? 13.418 31.129 57.847 1.00 42.29  ? 38  ASP A CB   1 
ATOM   532  C CG   . ASP A 1 35  ? 12.468 32.115 58.490 1.00 68.14  ? 38  ASP A CG   1 
ATOM   533  O OD1  . ASP A 1 35  ? 12.948 33.024 59.201 1.00 98.32  ? 38  ASP A OD1  1 
ATOM   534  O OD2  . ASP A 1 35  ? 11.243 31.981 58.287 1.00 72.99  ? 38  ASP A OD2  1 
ATOM   535  H H    . ASP A 1 35  ? 12.492 28.906 58.211 0.00 54.33  ? 38  ASP A H    1 
ATOM   536  H HA   . ASP A 1 35  ? 11.988 30.753 56.430 0.00 48.73  ? 38  ASP A HA   1 
ATOM   537  H HB2  . ASP A 1 35  ? 13.775 30.558 58.545 0.00 50.76  ? 38  ASP A HB2  1 
ATOM   538  H HB3  . ASP A 1 35  ? 14.135 31.631 57.430 0.00 50.76  ? 38  ASP A HB3  1 
ATOM   539  N N    . ALA A 1 36  ? 14.660 29.043 55.908 1.00 35.09  ? 39  ALA A N    1 
ATOM   540  C CA   . ALA A 1 36  ? 15.618 28.696 54.867 1.00 33.71  ? 39  ALA A CA   1 
ATOM   541  C C    . ALA A 1 36  ? 14.923 28.058 53.667 1.00 32.28  ? 39  ALA A C    1 
ATOM   542  O O    . ALA A 1 36  ? 15.345 28.270 52.533 1.00 30.44  ? 39  ALA A O    1 
ATOM   543  C CB   . ALA A 1 36  ? 16.689 27.755 55.414 1.00 35.47  ? 39  ALA A CB   1 
ATOM   544  H H    . ALA A 1 36  ? 14.764 28.623 56.651 0.00 42.05  ? 39  ALA A H    1 
ATOM   545  H HA   . ALA A 1 36  ? 16.061 29.507 54.572 0.00 40.39  ? 39  ALA A HA   1 
ATOM   546  H HB1  . ALA A 1 36  ? 17.317 27.544 54.705 0.00 42.51  ? 39  ALA A HB1  1 
ATOM   547  H HB2  . ALA A 1 36  ? 17.152 28.194 56.145 0.00 42.51  ? 39  ALA A HB2  1 
ATOM   548  H HB3  . ALA A 1 36  ? 16.264 26.943 55.732 0.00 42.51  ? 39  ALA A HB3  1 
ATOM   549  N N    . LYS A 1 37  ? 13.857 27.286 53.914 1.00 35.84  ? 40  LYS A N    1 
ATOM   550  C CA   . LYS A 1 37  ? 13.118 26.681 52.794 1.00 32.38  ? 40  LYS A CA   1 
ATOM   551  C C    . LYS A 1 37  ? 12.550 27.728 51.862 1.00 31.14  ? 40  LYS A C    1 
ATOM   552  O O    . LYS A 1 37  ? 12.503 27.506 50.638 1.00 35.59  ? 40  LYS A O    1 
ATOM   553  C CB   . LYS A 1 37  ? 11.984 25.801 53.355 1.00 37.61  ? 40  LYS A CB   1 
ATOM   554  C CG   . LYS A 1 37  ? 12.462 24.522 54.001 1.00 47.28  ? 40  LYS A CG   1 
ATOM   555  C CD   . LYS A 1 37  ? 11.356 23.866 54.827 1.00 55.96  ? 40  LYS A CD   1 
ATOM   556  C CE   . LYS A 1 37  ? 10.544 22.877 54.005 1.00 66.16  ? 40  LYS A CE   1 
ATOM   557  N NZ   . LYS A 1 37  ? 9.426  22.299 54.813 1.00 68.09  ? 40  LYS A NZ   1 
ATOM   558  H H    . LYS A 1 37  ? 13.549 27.102 54.695 0.00 43.01  ? 40  LYS A H    1 
ATOM   559  H HA   . LYS A 1 37  ? 13.726 26.129 52.278 0.00 38.87  ? 40  LYS A HA   1 
ATOM   560  H HB2  . LYS A 1 37  ? 11.501 26.307 54.026 0.00 45.15  ? 40  LYS A HB2  1 
ATOM   561  H HB3  . LYS A 1 37  ? 11.389 25.559 52.628 0.00 45.15  ? 40  LYS A HB3  1 
ATOM   562  H HG2  . LYS A 1 37  ? 12.739 23.898 53.312 0.00 56.74  ? 40  LYS A HG2  1 
ATOM   563  H HG3  . LYS A 1 37  ? 13.207 24.718 54.590 0.00 56.74  ? 40  LYS A HG3  1 
ATOM   564  H HD2  . LYS A 1 37  ? 11.754 23.387 55.570 0.00 67.17  ? 40  LYS A HD2  1 
ATOM   565  H HD3  . LYS A 1 37  ? 10.754 24.551 55.157 0.00 67.17  ? 40  LYS A HD3  1 
ATOM   566  H HE2  . LYS A 1 37  ? 10.165 23.331 53.236 0.00 79.41  ? 40  LYS A HE2  1 
ATOM   567  H HE3  . LYS A 1 37  ? 11.119 22.152 53.712 0.00 79.41  ? 40  LYS A HE3  1 
ATOM   568  H HZ1  . LYS A 1 37  ? 8.954  21.731 54.316 0.00 81.72  ? 40  LYS A HZ1  1 
ATOM   569  H HZ2  . LYS A 1 37  ? 9.752  21.865 55.518 0.00 81.72  ? 40  LYS A HZ2  1 
ATOM   570  H HZ3  . LYS A 1 37  ? 8.889  22.949 55.098 0.00 81.72  ? 40  LYS A HZ3  1 
ATOM   571  N N    . LYS A 1 38  ? 12.060 28.854 52.407 1.00 30.01  ? 41  LYS A N    1 
ATOM   572  C CA   . LYS A 1 38  ? 11.579 29.938 51.536 1.00 28.17  ? 41  LYS A CA   1 
ATOM   573  C C    . LYS A 1 38  ? 12.663 30.395 50.574 1.00 27.55  ? 41  LYS A C    1 
ATOM   574  O O    . LYS A 1 38  ? 12.445 30.527 49.375 1.00 26.14  ? 41  LYS A O    1 
ATOM   575  C CB   . LYS A 1 38  ? 11.159 31.150 52.386 1.00 32.61  ? 41  LYS A CB   1 
ATOM   576  C CG   . LYS A 1 38  ? 9.762  31.145 52.934 1.00 56.62  ? 41  LYS A CG   1 
ATOM   577  C CD   . LYS A 1 38  ? 9.788  31.754 54.325 1.00 62.46  ? 41  LYS A CD   1 
ATOM   578  C CE   . LYS A 1 38  ? 8.415  32.179 54.804 1.00 80.97  ? 41  LYS A CE   1 
ATOM   579  N NZ   . LYS A 1 38  ? 7.964  31.342 55.947 1.00 90.00  ? 41  LYS A NZ   1 
ATOM   580  H H    . LYS A 1 38  ? 11.997 29.010 53.250 0.00 35.95  ? 41  LYS A H    1 
ATOM   581  H HA   . LYS A 1 38  ? 10.818 29.602 51.038 0.00 33.74  ? 41  LYS A HA   1 
ATOM   582  H HB2  . LYS A 1 38  ? 11.760 31.205 53.146 0.00 39.14  ? 41  LYS A HB2  1 
ATOM   583  H HB3  . LYS A 1 38  ? 11.244 31.945 51.837 0.00 39.14  ? 41  LYS A HB3  1 
ATOM   584  H HG2  . LYS A 1 38  ? 9.181  31.675 52.367 0.00 67.96  ? 41  LYS A HG2  1 
ATOM   585  H HG3  . LYS A 1 38  ? 9.431  30.236 52.992 0.00 67.96  ? 41  LYS A HG3  1 
ATOM   586  H HD2  . LYS A 1 38  ? 10.134 31.099 54.951 0.00 74.97  ? 41  LYS A HD2  1 
ATOM   587  H HD3  . LYS A 1 38  ? 10.358 32.539 54.317 0.00 74.97  ? 41  LYS A HD3  1 
ATOM   588  H HE2  . LYS A 1 38  ? 8.447  33.104 55.096 0.00 97.17  ? 41  LYS A HE2  1 
ATOM   589  H HE3  . LYS A 1 38  ? 7.776  32.081 54.081 0.00 97.17  ? 41  LYS A HE3  1 
ATOM   590  H HZ1  . LYS A 1 38  ? 7.161  31.609 56.222 0.00 108.01 ? 41  LYS A HZ1  1 
ATOM   591  H HZ2  . LYS A 1 38  ? 7.916  30.489 55.699 0.00 108.01 ? 41  LYS A HZ2  1 
ATOM   592  H HZ3  . LYS A 1 38  ? 8.539  31.414 56.623 0.00 108.01 ? 41  LYS A HZ3  1 
ATOM   593  N N    . PHE A 1 39  ? 13.857 30.694 51.118 1.00 26.92  ? 42  PHE A N    1 
ATOM   594  C CA   . PHE A 1 39  ? 14.911 31.221 50.270 1.00 25.54  ? 42  PHE A CA   1 
ATOM   595  C C    . PHE A 1 39  ? 15.409 30.190 49.261 1.00 24.86  ? 42  PHE A C    1 
ATOM   596  O O    . PHE A 1 39  ? 15.690 30.546 48.115 1.00 25.18  ? 42  PHE A O    1 
ATOM   597  C CB   . PHE A 1 39  ? 16.080 31.698 51.150 1.00 28.28  ? 42  PHE A CB   1 
ATOM   598  C CG   . PHE A 1 39  ? 15.737 32.937 51.953 1.00 26.91  ? 42  PHE A CG   1 
ATOM   599  C CD1  . PHE A 1 39  ? 15.638 34.168 51.305 1.00 28.21  ? 42  PHE A CD1  1 
ATOM   600  C CD2  . PHE A 1 39  ? 15.519 32.869 53.303 1.00 32.15  ? 42  PHE A CD2  1 
ATOM   601  C CE1  . PHE A 1 39  ? 15.326 35.325 52.051 1.00 33.00  ? 42  PHE A CE1  1 
ATOM   602  C CE2  . PHE A 1 39  ? 15.224 34.011 54.043 1.00 33.56  ? 42  PHE A CE2  1 
ATOM   603  C CZ   . PHE A 1 39  ? 15.124 35.237 53.410 1.00 38.44  ? 42  PHE A CZ   1 
ATOM   604  H H    . PHE A 1 39  ? 14.064 30.600 51.947 0.00 32.24  ? 42  PHE A H    1 
ATOM   605  H HA   . PHE A 1 39  ? 14.555 31.972 49.769 0.00 30.59  ? 42  PHE A HA   1 
ATOM   606  H HB2  . PHE A 1 39  ? 16.316 30.993 51.772 0.00 33.95  ? 42  PHE A HB2  1 
ATOM   607  H HB3  . PHE A 1 39  ? 16.838 31.908 50.583 0.00 33.95  ? 42  PHE A HB3  1 
ATOM   608  H HD1  . PHE A 1 39  ? 15.776 34.227 50.387 0.00 33.87  ? 42  PHE A HD1  1 
ATOM   609  H HD2  . PHE A 1 39  ? 15.569 32.046 53.733 0.00 38.60  ? 42  PHE A HD2  1 
ATOM   610  H HE1  . PHE A 1 39  ? 15.257 36.148 51.623 0.00 39.61  ? 42  PHE A HE1  1 
ATOM   611  H HE2  . PHE A 1 39  ? 15.094 33.950 54.962 0.00 40.29  ? 42  PHE A HE2  1 
ATOM   612  H HZ   . PHE A 1 39  ? 14.921 36.001 53.901 0.00 46.14  ? 42  PHE A HZ   1 
ATOM   613  N N    . TYR A 1 40  ? 15.497 28.913 49.662 1.00 26.20  ? 43  TYR A N    1 
ATOM   614  C CA   . TYR A 1 40  ? 15.913 27.893 48.686 1.00 25.59  ? 43  TYR A CA   1 
ATOM   615  C C    . TYR A 1 40  ? 14.883 27.742 47.571 1.00 27.18  ? 43  TYR A C    1 
ATOM   616  O O    . TYR A 1 40  ? 15.241 27.581 46.391 1.00 25.66  ? 43  TYR A O    1 
ATOM   617  C CB   . TYR A 1 40  ? 16.111 26.555 49.383 1.00 27.45  ? 43  TYR A CB   1 
ATOM   618  C CG   . TYR A 1 40  ? 17.536 26.337 49.819 1.00 28.81  ? 43  TYR A CG   1 
ATOM   619  C CD1  . TYR A 1 40  ? 18.487 25.890 48.908 1.00 32.26  ? 43  TYR A CD1  1 
ATOM   620  C CD2  . TYR A 1 40  ? 17.912 26.590 51.114 1.00 32.08  ? 43  TYR A CD2  1 
ATOM   621  C CE1  . TYR A 1 40  ? 19.812 25.680 49.332 1.00 35.34  ? 43  TYR A CE1  1 
ATOM   622  C CE2  . TYR A 1 40  ? 19.222 26.385 51.548 1.00 36.07  ? 43  TYR A CE2  1 
ATOM   623  C CZ   . TYR A 1 40  ? 20.157 25.947 50.616 1.00 35.97  ? 43  TYR A CZ   1 
ATOM   624  O OH   . TYR A 1 40  ? 21.464 25.752 51.069 1.00 41.26  ? 43  TYR A OH   1 
ATOM   625  H H    . TYR A 1 40  ? 15.329 28.624 50.454 0.00 31.45  ? 43  TYR A H    1 
ATOM   626  H HA   . TYR A 1 40  ? 16.757 28.167 48.294 0.00 30.65  ? 43  TYR A HA   1 
ATOM   627  H HB2  . TYR A 1 40  ? 15.546 26.522 50.171 0.00 32.88  ? 43  TYR A HB2  1 
ATOM   628  H HB3  . TYR A 1 40  ? 15.870 25.840 48.773 0.00 32.88  ? 43  TYR A HB3  1 
ATOM   629  H HD1  . TYR A 1 40  ? 18.249 25.731 48.023 0.00 38.73  ? 43  TYR A HD1  1 
ATOM   630  H HD2  . TYR A 1 40  ? 17.278 26.906 51.717 0.00 38.51  ? 43  TYR A HD2  1 
ATOM   631  H HE1  . TYR A 1 40  ? 20.449 25.359 48.735 0.00 42.42  ? 43  TYR A HE1  1 
ATOM   632  H HE2  . TYR A 1 40  ? 19.463 26.537 52.434 0.00 43.30  ? 43  TYR A HE2  1 
ATOM   633  H HH   . TYR A 1 40  ? 21.531 25.999 51.869 0.00 49.52  ? 43  TYR A HH   1 
ATOM   634  N N    . ALA A 1 41  ? 13.601 27.798 47.920 1.00 26.16  ? 44  ALA A N    1 
ATOM   635  C CA   . ALA A 1 41  ? 12.566 27.656 46.871 1.00 26.36  ? 44  ALA A CA   1 
ATOM   636  C C    . ALA A 1 41  ? 12.630 28.802 45.887 1.00 25.35  ? 44  ALA A C    1 
ATOM   637  O O    . ALA A 1 41  ? 12.669 28.581 44.659 1.00 25.25  ? 44  ALA A O    1 
ATOM   638  C CB   . ALA A 1 41  ? 11.179 27.555 47.530 1.00 27.53  ? 44  ALA A CB   1 
ATOM   639  H H    . ALA A 1 41  ? 13.305 27.911 48.719 0.00 31.41  ? 44  ALA A H    1 
ATOM   640  H HA   . ALA A 1 41  ? 12.720 26.838 46.373 0.00 31.65  ? 44  ALA A HA   1 
ATOM   641  H HB1  . ALA A 1 41  ? 10.507 27.462 46.838 0.00 33.05  ? 44  ALA A HB1  1 
ATOM   642  H HB2  . ALA A 1 41  ? 11.163 26.781 48.114 0.00 33.05  ? 44  ALA A HB2  1 
ATOM   643  H HB3  . ALA A 1 41  ? 11.015 28.361 48.045 0.00 33.05  ? 44  ALA A HB3  1 
ATOM   644  N N    . ILE A 1 42  ? 12.642 30.037 46.380 1.00 23.53  ? 45  ILE A N    1 
ATOM   645  C CA   . ILE A 1 42  ? 12.697 31.202 45.491 1.00 22.98  ? 45  ILE A CA   1 
ATOM   646  C C    . ILE A 1 42  ? 13.941 31.144 44.632 1.00 23.96  ? 45  ILE A C    1 
ATOM   647  O O    . ILE A 1 42  ? 13.903 31.350 43.419 1.00 25.32  ? 45  ILE A O    1 
ATOM   648  C CB   . ILE A 1 42  ? 12.658 32.508 46.342 1.00 25.56  ? 45  ILE A CB   1 
ATOM   649  C CG1  . ILE A 1 42  ? 11.322 32.651 47.059 1.00 28.66  ? 45  ILE A CG1  1 
ATOM   650  C CG2  . ILE A 1 42  ? 12.948 33.706 45.424 1.00 28.19  ? 45  ILE A CG2  1 
ATOM   651  C CD1  . ILE A 1 42  ? 11.331 33.684 48.165 1.00 33.34  ? 45  ILE A CD1  1 
ATOM   652  H H    . ILE A 1 42  ? 12.620 30.230 47.218 0.00 28.24  ? 45  ILE A H    1 
ATOM   653  H HA   . ILE A 1 42  ? 11.926 31.190 44.902 0.00 27.59  ? 45  ILE A HA   1 
ATOM   654  H HB   . ILE A 1 42  ? 13.340 32.468 47.032 0.00 30.68  ? 45  ILE A HB   1 
ATOM   655  H HG12 . ILE A 1 42  ? 10.648 32.915 46.413 0.00 34.41  ? 45  ILE A HG12 1 
ATOM   656  H HG13 . ILE A 1 42  ? 11.086 31.797 47.454 0.00 34.41  ? 45  ILE A HG13 1 
ATOM   657  H HG21 . ILE A 1 42  ? 12.678 34.521 45.874 0.00 33.84  ? 45  ILE A HG21 1 
ATOM   658  H HG22 . ILE A 1 42  ? 13.899 33.733 45.232 0.00 33.84  ? 45  ILE A HG22 1 
ATOM   659  H HG23 . ILE A 1 42  ? 12.447 33.601 44.600 0.00 33.84  ? 45  ILE A HG23 1 
ATOM   660  H HD11 . ILE A 1 42  ? 10.488 33.644 48.642 0.00 40.02  ? 45  ILE A HD11 1 
ATOM   661  H HD12 . ILE A 1 42  ? 12.063 33.491 48.771 0.00 40.02  ? 45  ILE A HD12 1 
ATOM   662  H HD13 . ILE A 1 42  ? 11.448 34.564 47.774 0.00 40.02  ? 45  ILE A HD13 1 
ATOM   663  N N    . THR A 1 43  ? 15.085 30.865 45.247 1.00 22.89  ? 46  THR A N    1 
ATOM   664  C CA   . THR A 1 43  ? 16.357 31.013 44.555 1.00 22.35  ? 46  THR A CA   1 
ATOM   665  C C    . THR A 1 43  ? 16.608 29.881 43.568 1.00 28.24  ? 46  THR A C    1 
ATOM   666  O O    . THR A 1 43  ? 17.338 30.082 42.585 1.00 27.28  ? 46  THR A O    1 
ATOM   667  C CB   . THR A 1 43  ? 17.467 31.069 45.605 1.00 23.07  ? 46  THR A CB   1 
ATOM   668  O OG1  . THR A 1 43  ? 17.162 32.137 46.521 1.00 24.61  ? 46  THR A OG1  1 
ATOM   669  C CG2  . THR A 1 43  ? 18.830 31.341 44.935 1.00 29.85  ? 46  THR A CG2  1 
ATOM   670  H H    . THR A 1 43  ? 15.151 30.591 46.059 0.00 27.48  ? 46  THR A H    1 
ATOM   671  H HA   . THR A 1 43  ? 16.365 31.837 44.044 0.00 26.84  ? 46  THR A HA   1 
ATOM   672  H HB   . THR A 1 43  ? 17.530 30.225 46.079 0.00 27.69  ? 46  THR A HB   1 
ATOM   673  H HG1  . THR A 1 43  ? 16.454 31.964 46.939 0.00 29.54  ? 46  THR A HG1  1 
ATOM   674  H HG21 . THR A 1 43  ? 19.508 31.497 45.612 0.00 35.83  ? 46  THR A HG21 1 
ATOM   675  H HG22 . THR A 1 43  ? 19.093 30.578 44.397 0.00 35.83  ? 46  THR A HG22 1 
ATOM   676  H HG23 . THR A 1 43  ? 18.769 32.123 44.364 0.00 35.83  ? 46  THR A HG23 1 
ATOM   677  N N    . THR A 1 44  ? 16.036 28.697 43.811 1.00 21.55  ? 47  THR A N    1 
ATOM   678  C CA   . THR A 1 44  ? 16.206 27.581 42.877 1.00 20.44  ? 47  THR A CA   1 
ATOM   679  C C    . THR A 1 44  ? 15.286 27.767 41.662 1.00 24.94  ? 47  THR A C    1 
ATOM   680  O O    . THR A 1 44  ? 15.660 27.397 40.534 1.00 23.06  ? 47  THR A O    1 
ATOM   681  C CB   . THR A 1 44  ? 15.875 26.269 43.560 1.00 21.22  ? 47  THR A CB   1 
ATOM   682  O OG1  . THR A 1 44  ? 16.729 26.071 44.733 1.00 26.20  ? 47  THR A OG1  1 
ATOM   683  C CG2  . THR A 1 44  ? 16.110 25.057 42.603 1.00 26.67  ? 47  THR A CG2  1 
ATOM   684  H H    . THR A 1 44  ? 15.552 28.517 44.498 0.00 25.87  ? 47  THR A H    1 
ATOM   685  H HA   . THR A 1 44  ? 17.131 27.537 42.587 0.00 24.55  ? 47  THR A HA   1 
ATOM   686  H HB   . THR A 1 44  ? 14.942 26.301 43.822 0.00 25.43  ? 47  THR A HB   1 
ATOM   687  H HG1  . THR A 1 44  ? 16.632 26.710 45.270 0.00 31.45  ? 47  THR A HG1  1 
ATOM   688  H HG21 . THR A 1 44  ? 15.986 24.225 43.085 0.00 32.02  ? 47  THR A HG21 1 
ATOM   689  H HG22 . THR A 1 44  ? 15.481 25.090 41.865 0.00 32.02  ? 47  THR A HG22 1 
ATOM   690  H HG23 . THR A 1 44  ? 17.012 25.084 42.248 0.00 32.02  ? 47  THR A HG23 1 
ATOM   691  N N    . LEU A 1 45  ? 14.105 28.327 41.877 1.00 22.42  ? 48  LEU A N    1 
ATOM   692  C CA   . LEU A 1 45  ? 13.185 28.560 40.763 1.00 21.51  ? 48  LEU A CA   1 
ATOM   693  C C    . LEU A 1 45  ? 13.774 29.519 39.733 1.00 22.05  ? 48  LEU A C    1 
ATOM   694  O O    . LEU A 1 45  ? 13.489 29.410 38.557 1.00 23.08  ? 48  LEU A O    1 
ATOM   695  C CB   . LEU A 1 45  ? 11.851 29.090 41.279 1.00 22.85  ? 48  LEU A CB   1 
ATOM   696  C CG   . LEU A 1 45  ? 10.858 28.127 41.811 1.00 28.98  ? 48  LEU A CG   1 
ATOM   697  C CD1  . LEU A 1 45  ? 9.711  28.877 42.486 1.00 33.80  ? 48  LEU A CD1  1 
ATOM   698  C CD2  . LEU A 1 45  ? 10.308 27.231 40.681 1.00 30.21  ? 48  LEU A CD2  1 
ATOM   699  H H    . LEU A 1 45  ? 13.812 28.580 42.645 1.00 26.92  ? 48  LEU A H    1 
ATOM   700  H HA   . LEU A 1 45  ? 13.018 27.713 40.321 1.00 25.82  ? 48  LEU A HA   1 
ATOM   701  H HB2  . LEU A 1 45  ? 12.043 29.712 41.998 1.00 27.43  ? 48  LEU A HB2  1 
ATOM   702  H HB3  . LEU A 1 45  ? 11.418 29.554 40.546 1.00 27.43  ? 48  LEU A HB3  1 
ATOM   703  H HG   . LEU A 1 45  ? 11.291 27.558 42.467 1.00 34.79  ? 48  LEU A HG   1 
ATOM   704  H HD11 . LEU A 1 45  ? 9.121  28.236 42.911 1.00 40.57  ? 48  LEU A HD11 1 
ATOM   705  H HD12 . LEU A 1 45  ? 10.076 29.482 43.150 1.00 40.57  ? 48  LEU A HD12 1 
ATOM   706  H HD13 . LEU A 1 45  ? 9.223  29.380 41.814 1.00 40.57  ? 48  LEU A HD13 1 
ATOM   707  H HD21 . LEU A 1 45  ? 9.623  26.650 41.045 1.00 36.26  ? 48  LEU A HD21 1 
ATOM   708  H HD22 . LEU A 1 45  ? 9.930  27.794 39.988 1.00 36.26  ? 48  LEU A HD22 1 
ATOM   709  H HD23 . LEU A 1 45  ? 11.034 26.701 40.317 1.00 36.26  ? 48  LEU A HD23 1 
ATOM   710  N N    . VAL A 1 46  ? 14.581 30.498 40.158 1.00 19.29  ? 49  VAL A N    1 
ATOM   711  C CA   . VAL A 1 46  ? 15.073 31.532 39.270 1.00 19.67  ? 49  VAL A CA   1 
ATOM   712  C C    . VAL A 1 46  ? 15.921 30.929 38.140 1.00 23.86  ? 49  VAL A C    1 
ATOM   713  O O    . VAL A 1 46  ? 15.603 31.166 36.953 1.00 21.02  ? 49  VAL A O    1 
ATOM   714  C CB   . VAL A 1 46  ? 15.843 32.588 40.070 1.00 19.91  ? 49  VAL A CB   1 
ATOM   715  C CG1  . VAL A 1 46  ? 16.683 33.482 39.117 1.00 23.44  ? 49  VAL A CG1  1 
ATOM   716  C CG2  . VAL A 1 46  ? 14.845 33.482 40.862 1.00 22.44  ? 49  VAL A CG2  1 
ATOM   717  H H    . VAL A 1 46  ? 14.857 30.577 40.969 0.00 23.16  ? 49  VAL A H    1 
ATOM   718  H HA   . VAL A 1 46  ? 14.317 31.953 38.832 0.00 23.61  ? 49  VAL A HA   1 
ATOM   719  H HB   . VAL A 1 46  ? 16.439 32.140 40.691 0.00 23.90  ? 49  VAL A HB   1 
ATOM   720  H HG11 . VAL A 1 46  ? 16.949 34.286 39.590 0.00 28.14  ? 49  VAL A HG11 1 
ATOM   721  H HG12 . VAL A 1 46  ? 17.469 32.990 38.833 0.00 28.14  ? 49  VAL A HG12 1 
ATOM   722  H HG13 . VAL A 1 46  ? 16.142 33.716 38.346 0.00 28.14  ? 49  VAL A HG13 1 
ATOM   723  H HG21 . VAL A 1 46  ? 15.345 34.130 41.382 0.00 26.95  ? 49  VAL A HG21 1 
ATOM   724  H HG22 . VAL A 1 46  ? 14.264 33.940 40.233 0.00 26.95  ? 49  VAL A HG22 1 
ATOM   725  H HG23 . VAL A 1 46  ? 14.317 32.921 41.451 0.00 26.95  ? 49  VAL A HG23 1 
ATOM   726  N N    . PRO A 1 47  ? 16.953 30.164 38.394 1.00 20.83  ? 50  PRO A N    1 
ATOM   727  C CA   . PRO A 1 47  ? 17.693 29.556 37.257 1.00 19.00  ? 50  PRO A CA   1 
ATOM   728  C C    . PRO A 1 47  ? 16.906 28.498 36.535 1.00 22.16  ? 50  PRO A C    1 
ATOM   729  O O    . PRO A 1 47  ? 17.197 28.240 35.365 1.00 21.87  ? 50  PRO A O    1 
ATOM   730  C CB   . PRO A 1 47  ? 18.972 29.005 37.905 1.00 22.18  ? 50  PRO A CB   1 
ATOM   731  C CG   . PRO A 1 47  ? 18.577 28.756 39.374 1.00 25.44  ? 50  PRO A CG   1 
ATOM   732  C CD   . PRO A 1 47  ? 17.649 29.885 39.710 1.00 21.80  ? 50  PRO A CD   1 
ATOM   733  H HA   . PRO A 1 47  ? 17.955 30.239 36.619 0.00 22.81  ? 50  PRO A HA   1 
ATOM   734  H HB2  . PRO A 1 47  ? 19.237 28.180 37.470 0.00 26.63  ? 50  PRO A HB2  1 
ATOM   735  H HB3  . PRO A 1 47  ? 19.686 29.659 37.841 0.00 26.63  ? 50  PRO A HB3  1 
ATOM   736  H HG2  . PRO A 1 47  ? 18.129 27.900 39.458 0.00 30.54  ? 50  PRO A HG2  1 
ATOM   737  H HG3  . PRO A 1 47  ? 19.366 28.774 39.938 0.00 30.54  ? 50  PRO A HG3  1 
ATOM   738  H HD2  . PRO A 1 47  ? 17.010 29.617 40.389 0.00 26.17  ? 50  PRO A HD2  1 
ATOM   739  H HD3  . PRO A 1 47  ? 18.146 30.663 40.010 0.00 26.17  ? 50  PRO A HD3  1 
ATOM   740  N N    . ALA A 1 48  ? 15.938 27.856 37.193 1.00 20.15  ? 51  ALA A N    1 
ATOM   741  C CA   . ALA A 1 48  ? 15.144 26.837 36.498 1.00 20.10  ? 51  ALA A CA   1 
ATOM   742  C C    . ALA A 1 48  ? 14.314 27.493 35.401 1.00 20.20  ? 51  ALA A C    1 
ATOM   743  O O    . ALA A 1 48  ? 14.197 26.931 34.300 1.00 20.69  ? 51  ALA A O    1 
ATOM   744  C CB   . ALA A 1 48  ? 14.236 26.121 37.481 1.00 19.18  ? 51  ALA A CB   1 
ATOM   745  H H    . ALA A 1 48  ? 15.726 27.986 38.016 0.00 24.19  ? 51  ALA A H    1 
ATOM   746  H HA   . ALA A 1 48  ? 15.736 26.176 36.105 0.00 24.13  ? 51  ALA A HA   1 
ATOM   747  H HB1  . ALA A 1 48  ? 13.725 25.447 37.006 0.00 23.03  ? 51  ALA A HB1  1 
ATOM   748  H HB2  . ALA A 1 48  ? 14.780 25.701 38.166 0.00 23.03  ? 51  ALA A HB2  1 
ATOM   749  H HB3  . ALA A 1 48  ? 13.636 26.767 37.885 0.00 23.03  ? 51  ALA A HB3  1 
ATOM   750  N N    . ILE A 1 49  ? 13.674 28.625 35.703 1.00 18.87  ? 52  ILE A N    1 
ATOM   751  C CA   . ILE A 1 49  ? 12.910 29.334 34.678 1.00 17.84  ? 52  ILE A CA   1 
ATOM   752  C C    . ILE A 1 49  ? 13.870 29.814 33.585 1.00 19.74  ? 52  ILE A C    1 
ATOM   753  O O    . ILE A 1 49  ? 13.577 29.697 32.373 1.00 21.97  ? 52  ILE A O    1 
ATOM   754  C CB   . ILE A 1 49  ? 12.153 30.520 35.315 1.00 18.51  ? 52  ILE A CB   1 
ATOM   755  C CG1  . ILE A 1 49  ? 11.067 29.984 36.224 1.00 19.04  ? 52  ILE A CG1  1 
ATOM   756  C CG2  . ILE A 1 49  ? 11.512 31.437 34.256 1.00 22.61  ? 52  ILE A CG2  1 
ATOM   757  C CD1  . ILE A 1 49  ? 10.521 31.037 37.214 1.00 24.19  ? 52  ILE A CD1  1 
ATOM   758  H H    . ILE A 1 49  ? 13.667 28.995 36.479 0.00 22.65  ? 52  ILE A H    1 
ATOM   759  H HA   . ILE A 1 49  ? 12.258 28.734 34.284 0.00 21.42  ? 52  ILE A HA   1 
ATOM   760  H HB   . ILE A 1 49  ? 12.799 31.044 35.814 0.00 22.23  ? 52  ILE A HB   1 
ATOM   761  H HG12 . ILE A 1 49  ? 10.326 29.675 35.679 0.00 22.86  ? 52  ILE A HG12 1 
ATOM   762  H HG13 . ILE A 1 49  ? 11.427 29.247 36.742 0.00 22.86  ? 52  ILE A HG13 1 
ATOM   763  H HG21 . ILE A 1 49  ? 10.897 32.045 34.696 0.00 27.14  ? 52  ILE A HG21 1 
ATOM   764  H HG22 . ILE A 1 49  ? 12.211 31.940 33.809 0.00 27.14  ? 52  ILE A HG22 1 
ATOM   765  H HG23 . ILE A 1 49  ? 11.035 30.891 33.613 0.00 27.14  ? 52  ILE A HG23 1 
ATOM   766  H HD11 . ILE A 1 49  ? 9.903  30.606 37.825 0.00 29.04  ? 52  ILE A HD11 1 
ATOM   767  H HD12 . ILE A 1 49  ? 11.262 31.420 37.708 0.00 29.04  ? 52  ILE A HD12 1 
ATOM   768  H HD13 . ILE A 1 49  ? 10.062 31.731 36.715 0.00 29.04  ? 52  ILE A HD13 1 
ATOM   769  N N    . ALA A 1 50  ? 15.000 30.397 33.994 1.00 18.33  ? 53  ALA A N    1 
ATOM   770  C CA   . ALA A 1 50  ? 15.934 30.897 32.960 1.00 20.87  ? 53  ALA A CA   1 
ATOM   771  C C    . ALA A 1 50  ? 16.458 29.763 32.085 1.00 20.04  ? 53  ALA A C    1 
ATOM   772  O O    . ALA A 1 50  ? 16.651 29.982 30.881 1.00 22.39  ? 53  ALA A O    1 
ATOM   773  C CB   . ALA A 1 50  ? 17.117 31.641 33.640 1.00 22.36  ? 53  ALA A CB   1 
ATOM   774  H H    . ALA A 1 50  ? 15.243 30.512 34.811 0.00 22.01  ? 53  ALA A H    1 
ATOM   775  H HA   . ALA A 1 50  ? 15.462 31.522 32.388 0.00 25.06  ? 53  ALA A HA   1 
ATOM   776  H HB1  . ALA A 1 50  ? 17.717 31.974 32.954 0.00 26.85  ? 53  ALA A HB1  1 
ATOM   777  H HB2  . ALA A 1 50  ? 16.767 32.380 34.161 0.00 26.85  ? 53  ALA A HB2  1 
ATOM   778  H HB3  . ALA A 1 50  ? 17.588 31.021 34.219 0.00 26.85  ? 53  ALA A HB3  1 
ATOM   779  N N    . PHE A 1 51  ? 16.717 28.570 32.650 1.00 17.96  ? 54  PHE A N    1 
ATOM   780  C CA   . PHE A 1 51  ? 17.095 27.414 31.850 1.00 18.56  ? 54  PHE A CA   1 
ATOM   781  C C    . PHE A 1 51  ? 16.077 27.169 30.737 1.00 20.99  ? 54  PHE A C    1 
ATOM   782  O O    . PHE A 1 51  ? 16.478 26.961 29.578 1.00 20.97  ? 54  PHE A O    1 
ATOM   783  C CB   . PHE A 1 51  ? 17.195 26.156 32.752 1.00 20.37  ? 54  PHE A CB   1 
ATOM   784  C CG   . PHE A 1 51  ? 17.245 24.876 31.982 1.00 22.61  ? 54  PHE A CG   1 
ATOM   785  C CD1  . PHE A 1 51  ? 18.411 24.497 31.347 1.00 24.59  ? 54  PHE A CD1  1 
ATOM   786  C CD2  . PHE A 1 51  ? 16.116 24.075 31.873 1.00 24.42  ? 54  PHE A CD2  1 
ATOM   787  C CE1  . PHE A 1 51  ? 18.466 23.303 30.636 1.00 25.55  ? 54  PHE A CE1  1 
ATOM   788  C CE2  . PHE A 1 51  ? 16.165 22.900 31.126 1.00 27.62  ? 54  PHE A CE2  1 
ATOM   789  C CZ   . PHE A 1 51  ? 17.336 22.519 30.528 1.00 28.44  ? 54  PHE A CZ   1 
ATOM   790  H H    . PHE A 1 51  ? 16.678 28.413 33.495 0.00 21.56  ? 54  PHE A H    1 
ATOM   791  H HA   . PHE A 1 51  ? 17.964 27.582 31.453 0.00 22.28  ? 54  PHE A HA   1 
ATOM   792  H HB2  . PHE A 1 51  ? 18.004 26.215 33.284 0.00 24.45  ? 54  PHE A HB2  1 
ATOM   793  H HB3  . PHE A 1 51  ? 16.418 26.124 33.332 0.00 24.45  ? 54  PHE A HB3  1 
ATOM   794  H HD1  . PHE A 1 51  ? 19.163 25.043 31.396 0.00 29.52  ? 54  PHE A HD1  1 
ATOM   795  H HD2  . PHE A 1 51  ? 15.328 24.323 32.300 0.00 29.32  ? 54  PHE A HD2  1 
ATOM   796  H HE1  . PHE A 1 51  ? 19.262 23.034 30.236 0.00 30.67  ? 54  PHE A HE1  1 
ATOM   797  H HE2  . PHE A 1 51  ? 15.402 22.375 31.033 0.00 33.16  ? 54  PHE A HE2  1 
ATOM   798  H HZ   . PHE A 1 51  ? 17.371 21.725 30.044 0.00 34.14  ? 54  PHE A HZ   1 
ATOM   799  N N    . THR A 1 52  ? 14.794 27.143 31.074 1.00 20.84  ? 55  THR A N    1 
ATOM   800  C CA   . THR A 1 52  ? 13.788 26.806 30.042 1.00 18.57  ? 55  THR A CA   1 
ATOM   801  C C    . THR A 1 52  ? 13.764 27.866 28.958 1.00 22.04  ? 55  THR A C    1 
ATOM   802  O O    . THR A 1 52  ? 13.546 27.545 27.780 1.00 19.92  ? 55  THR A O    1 
ATOM   803  C CB   . THR A 1 52  ? 12.378 26.634 30.628 1.00 21.05  ? 55  THR A CB   1 
ATOM   804  O OG1  . THR A 1 52  ? 11.875 27.870 31.118 1.00 27.75  ? 55  THR A OG1  1 
ATOM   805  C CG2  . THR A 1 52  ? 12.421 25.629 31.790 1.00 25.50  ? 55  THR A CG2  1 
ATOM   806  H H    . THR A 1 52  ? 14.479 27.307 31.857 0.00 25.03  ? 55  THR A H    1 
ATOM   807  H HA   . THR A 1 52  ? 14.034 25.947 29.663 0.00 22.29  ? 55  THR A HA   1 
ATOM   808  H HB   . THR A 1 52  ? 11.786 26.312 29.931 0.00 25.28  ? 55  THR A HB   1 
ATOM   809  H HG1  . THR A 1 52  ? 11.100 27.763 31.425 0.00 33.31  ? 55  THR A HG1  1 
ATOM   810  H HG21 . THR A 1 52  ? 11.519 25.394 32.058 0.00 30.62  ? 55  THR A HG21 1 
ATOM   811  H HG22 . THR A 1 52  ? 12.888 24.825 31.516 0.00 30.62  ? 55  THR A HG22 1 
ATOM   812  H HG23 . THR A 1 52  ? 12.883 26.018 32.549 0.00 30.62  ? 55  THR A HG23 1 
ATOM   813  N N    . MET A 1 53  ? 13.998 29.138 29.312 1.00 18.59  ? 56  MET A N    1 
ATOM   814  C CA   . MET A 1 53  ? 13.885 30.154 28.312 1.00 18.02  ? 56  MET A CA   1 
ATOM   815  C C    . MET A 1 53  ? 15.157 30.280 27.487 1.00 21.11  ? 56  MET A C    1 
ATOM   816  O O    . MET A 1 53  ? 15.058 30.543 26.285 1.00 20.94  ? 56  MET A O    1 
ATOM   817  C CB   . MET A 1 53  ? 13.525 31.506 28.968 1.00 21.07  ? 56  MET A CB   1 
ATOM   818  C CG   . MET A 1 53  ? 12.121 31.503 29.571 1.00 22.28  ? 56  MET A CG   1 
ATOM   819  S SD   . MET A 1 53  ? 10.858 31.406 28.285 1.00 28.24  ? 56  MET A SD   1 
ATOM   820  C CE   . MET A 1 53  ? 10.581 29.648 28.057 1.00 35.04  ? 56  MET A CE   1 
ATOM   821  H H    . MET A 1 53  ? 14.215 29.408 30.099 0.00 22.32  ? 56  MET A H    1 
ATOM   822  H HA   . MET A 1 53  ? 13.157 29.924 27.714 0.00 21.64  ? 56  MET A HA   1 
ATOM   823  H HB2  . MET A 1 53  ? 14.158 31.693 29.678 0.00 25.30  ? 56  MET A HB2  1 
ATOM   824  H HB3  . MET A 1 53  ? 13.564 32.205 28.296 0.00 25.30  ? 56  MET A HB3  1 
ATOM   825  H HG2  . MET A 1 53  ? 12.023 30.735 30.155 0.00 26.75  ? 56  MET A HG2  1 
ATOM   826  H HG3  . MET A 1 53  ? 11.984 32.321 30.074 0.00 26.75  ? 56  MET A HG3  1 
ATOM   827  H HE1  . MET A 1 53  ? 9.897  29.521 27.381 0.00 42.06  ? 56  MET A HE1  1 
ATOM   828  H HE2  . MET A 1 53  ? 11.409 29.232 27.771 0.00 42.06  ? 56  MET A HE2  1 
ATOM   829  H HE3  . MET A 1 53  ? 10.290 29.263 28.898 0.00 42.06  ? 56  MET A HE3  1 
ATOM   830  N N    . TYR A 1 54  ? 16.344 30.062 28.089 1.00 19.74  ? 57  TYR A N    1 
ATOM   831  C CA   . TYR A 1 54  ? 17.554 29.918 27.266 1.00 20.33  ? 57  TYR A CA   1 
ATOM   832  C C    . TYR A 1 54  ? 17.405 28.763 26.297 1.00 21.66  ? 57  TYR A C    1 
ATOM   833  O O    . TYR A 1 54  ? 17.799 28.879 25.135 1.00 20.64  ? 57  TYR A O    1 
ATOM   834  C CB   . TYR A 1 54  ? 18.798 29.713 28.173 1.00 18.29  ? 57  TYR A CB   1 
ATOM   835  C CG   . TYR A 1 54  ? 19.490 31.025 28.442 1.00 18.39  ? 57  TYR A CG   1 
ATOM   836  C CD1  . TYR A 1 54  ? 19.091 31.870 29.475 1.00 20.00  ? 57  TYR A CD1  1 
ATOM   837  C CD2  . TYR A 1 54  ? 20.527 31.469 27.608 1.00 21.00  ? 57  TYR A CD2  1 
ATOM   838  C CE1  . TYR A 1 54  ? 19.696 33.112 29.689 1.00 19.56  ? 57  TYR A CE1  1 
ATOM   839  C CE2  . TYR A 1 54  ? 21.135 32.694 27.804 1.00 25.06  ? 57  TYR A CE2  1 
ATOM   840  C CZ   . TYR A 1 54  ? 20.748 33.507 28.830 1.00 22.17  ? 57  TYR A CZ   1 
ATOM   841  O OH   . TYR A 1 54  ? 21.337 34.752 29.010 1.00 21.01  ? 57  TYR A OH   1 
ATOM   842  H H    . TYR A 1 54  ? 16.467 29.996 28.938 0.00 23.70  ? 57  TYR A H    1 
ATOM   843  H HA   . TYR A 1 54  ? 17.691 30.731 26.756 0.00 24.41  ? 57  TYR A HA   1 
ATOM   844  H HB2  . TYR A 1 54  ? 18.520 29.333 29.021 0.00 21.96  ? 57  TYR A HB2  1 
ATOM   845  H HB3  . TYR A 1 54  ? 19.425 29.119 27.732 0.00 21.96  ? 57  TYR A HB3  1 
ATOM   846  H HD1  . TYR A 1 54  ? 18.403 31.599 30.039 0.00 24.02  ? 57  TYR A HD1  1 
ATOM   847  H HD2  . TYR A 1 54  ? 20.812 30.926 26.908 0.00 25.21  ? 57  TYR A HD2  1 
ATOM   848  H HE1  . TYR A 1 54  ? 19.414 33.666 30.381 0.00 23.49  ? 57  TYR A HE1  1 
ATOM   849  H HE2  . TYR A 1 54  ? 21.814 32.968 27.230 0.00 30.08  ? 57  TYR A HE2  1 
ATOM   850  H HH   . TYR A 1 54  ? 20.962 35.158 29.643 0.00 25.22  ? 57  TYR A HH   1 
ATOM   851  N N    . LEU A 1 55  ? 16.866 27.613 26.748 1.00 18.23  ? 58  LEU A N    1 
ATOM   852  C CA   . LEU A 1 55  ? 16.703 26.504 25.822 1.00 18.96  ? 58  LEU A CA   1 
ATOM   853  C C    . LEU A 1 55  ? 15.759 26.895 24.689 1.00 21.10  ? 58  LEU A C    1 
ATOM   854  O O    . LEU A 1 55  ? 15.993 26.513 23.536 1.00 21.92  ? 58  LEU A O    1 
ATOM   855  C CB   . LEU A 1 55  ? 16.155 25.279 26.566 1.00 19.86  ? 58  LEU A CB   1 
ATOM   856  C CG   . LEU A 1 55  ? 15.988 24.019 25.714 1.00 20.75  ? 58  LEU A CG   1 
ATOM   857  C CD1  . LEU A 1 55  ? 17.322 23.551 25.124 1.00 25.56  ? 58  LEU A CD1  1 
ATOM   858  C CD2  . LEU A 1 55  ? 15.360 22.919 26.588 1.00 24.12  ? 58  LEU A CD2  1 
ATOM   859  H H    . LEU A 1 55  ? 16.601 27.466 27.553 0.00 21.89  ? 58  LEU A H    1 
ATOM   860  H HA   . LEU A 1 55  ? 17.566 26.270 25.446 0.00 22.77  ? 58  LEU A HA   1 
ATOM   861  H HB2  . LEU A 1 55  ? 16.765 25.062 27.289 0.00 23.85  ? 58  LEU A HB2  1 
ATOM   862  H HB3  . LEU A 1 55  ? 15.282 25.504 26.925 0.00 23.85  ? 58  LEU A HB3  1 
ATOM   863  H HG   . LEU A 1 55  ? 15.408 24.210 24.960 0.00 24.91  ? 58  LEU A HG   1 
ATOM   864  H HD11 . LEU A 1 55  ? 17.182 22.719 24.646 0.00 30.69  ? 58  LEU A HD11 1 
ATOM   865  H HD12 . LEU A 1 55  ? 17.654 24.230 24.515 0.00 30.69  ? 58  LEU A HD12 1 
ATOM   866  H HD13 . LEU A 1 55  ? 17.956 23.415 25.845 0.00 30.69  ? 58  LEU A HD13 1 
ATOM   867  H HD21 . LEU A 1 55  ? 15.255 22.114 26.056 0.00 28.95  ? 58  LEU A HD21 1 
ATOM   868  H HD22 . LEU A 1 55  ? 15.944 22.743 27.342 0.00 28.95  ? 58  LEU A HD22 1 
ATOM   869  H HD23 . LEU A 1 55  ? 14.494 23.222 26.904 0.00 28.95  ? 58  LEU A HD23 1 
ATOM   870  N N    . SER A 1 56  ? 14.700 27.641 24.998 1.00 17.57  ? 59  SER A N    1 
ATOM   871  C CA   . SER A 1 56  ? 13.760 28.019 23.938 1.00 18.57  ? 59  SER A CA   1 
ATOM   872  C C    . SER A 1 56  ? 14.421 28.954 22.924 1.00 21.73  ? 59  SER A C    1 
ATOM   873  O O    . SER A 1 56  ? 14.073 28.905 21.758 1.00 23.83  ? 59  SER A O    1 
ATOM   874  C CB   . SER A 1 56  ? 12.518 28.705 24.517 1.00 21.45  ? 59  SER A CB   1 
ATOM   875  O OG   . SER A 1 56  ? 12.753 30.087 24.782 1.00 27.34  ? 59  SER A OG   1 
ATOM   876  H H    . SER A 1 56  ? 14.506 27.932 25.784 0.00 21.10  ? 59  SER A H    1 
ATOM   877  H HA   . SER A 1 56  ? 13.470 27.208 23.492 0.00 22.30  ? 59  SER A HA   1 
ATOM   878  H HB2  . SER A 1 56  ? 11.793 28.628 23.877 0.00 25.75  ? 59  SER A HB2  1 
ATOM   879  H HB3  . SER A 1 56  ? 12.277 28.265 25.347 0.00 25.75  ? 59  SER A HB3  1 
ATOM   880  H HG   . SER A 1 56  ? 13.359 30.171 25.357 0.00 32.82  ? 59  SER A HG   1 
ATOM   881  N N    . MET A 1 57  ? 15.388 29.776 23.366 1.00 19.66  ? 60  MET A N    1 
ATOM   882  C CA   . MET A 1 57  ? 16.108 30.610 22.393 1.00 20.01  ? 60  MET A CA   1 
ATOM   883  C C    . MET A 1 57  ? 17.084 29.780 21.582 1.00 22.09  ? 60  MET A C    1 
ATOM   884  O O    . MET A 1 57  ? 17.212 29.988 20.369 1.00 22.38  ? 60  MET A O    1 
ATOM   885  C CB   . MET A 1 57  ? 16.841 31.763 23.143 1.00 19.61  ? 60  MET A CB   1 
ATOM   886  C CG   . MET A 1 57  ? 15.874 32.609 23.899 1.00 22.19  ? 60  MET A CG   1 
ATOM   887  S SD   . MET A 1 57  ? 16.664 34.237 24.465 1.00 25.56  ? 60  MET A SD   1 
ATOM   888  C CE   . MET A 1 57  ? 17.325 33.561 26.075 1.00 26.84  ? 60  MET A CE   1 
ATOM   889  H H    . MET A 1 57  ? 15.634 29.864 24.185 0.00 23.61  ? 60  MET A H    1 
ATOM   890  H HA   . MET A 1 57  ? 15.470 31.012 21.782 0.00 24.02  ? 60  MET A HA   1 
ATOM   891  H HB2  . MET A 1 57  ? 17.477 31.386 23.771 0.00 23.55  ? 60  MET A HB2  1 
ATOM   892  H HB3  . MET A 1 57  ? 17.303 32.324 22.500 0.00 23.55  ? 60  MET A HB3  1 
ATOM   893  H HG2  . MET A 1 57  ? 15.118 32.819 23.329 0.00 26.64  ? 60  MET A HG2  1 
ATOM   894  H HG3  . MET A 1 57  ? 15.573 32.126 24.685 0.00 26.64  ? 60  MET A HG3  1 
ATOM   895  H HE1  . MET A 1 57  ? 17.773 34.274 26.557 0.00 32.22  ? 60  MET A HE1  1 
ATOM   896  H HE2  . MET A 1 57  ? 16.586 33.219 26.602 0.00 32.22  ? 60  MET A HE2  1 
ATOM   897  H HE3  . MET A 1 57  ? 17.953 32.846 25.884 0.00 32.22  ? 60  MET A HE3  1 
ATOM   898  N N    . LEU A 1 58  ? 17.768 28.837 22.228 1.00 19.56  ? 61  LEU A N    1 
ATOM   899  C CA   . LEU A 1 58  ? 18.708 27.975 21.491 1.00 18.35  ? 61  LEU A CA   1 
ATOM   900  C C    . LEU A 1 58  ? 17.992 27.207 20.390 1.00 24.48  ? 61  LEU A C    1 
ATOM   901  O O    . LEU A 1 58  ? 18.520 27.087 19.277 1.00 26.87  ? 61  LEU A O    1 
ATOM   902  C CB   . LEU A 1 58  ? 19.363 26.990 22.500 1.00 21.76  ? 61  LEU A CB   1 
ATOM   903  C CG   . LEU A 1 58  ? 20.340 25.993 21.890 1.00 27.28  ? 61  LEU A CG   1 
ATOM   904  C CD1  . LEU A 1 58  ? 21.550 26.714 21.310 1.00 28.38  ? 61  LEU A CD1  1 
ATOM   905  C CD2  . LEU A 1 58  ? 20.781 24.991 22.965 1.00 31.26  ? 61  LEU A CD2  1 
ATOM   906  H H    . LEU A 1 58  ? 17.713 28.674 23.070 0.00 23.48  ? 61  LEU A H    1 
ATOM   907  H HA   . LEU A 1 58  ? 19.399 28.514 21.075 0.00 22.04  ? 61  LEU A HA   1 
ATOM   908  H HB2  . LEU A 1 58  ? 19.851 27.508 23.160 0.00 26.12  ? 61  LEU A HB2  1 
ATOM   909  H HB3  . LEU A 1 58  ? 18.659 26.481 22.931 0.00 26.12  ? 61  LEU A HB3  1 
ATOM   910  H HG   . LEU A 1 58  ? 19.907 25.512 21.167 0.00 32.74  ? 61  LEU A HG   1 
ATOM   911  H HD11 . LEU A 1 58  ? 22.188 26.056 20.994 0.00 34.07  ? 61  LEU A HD11 1 
ATOM   912  H HD12 . LEU A 1 58  ? 21.260 27.274 20.572 0.00 34.07  ? 61  LEU A HD12 1 
ATOM   913  H HD13 . LEU A 1 58  ? 21.954 27.261 22.002 0.00 34.07  ? 61  LEU A HD13 1 
ATOM   914  H HD21 . LEU A 1 58  ? 21.381 24.342 22.565 0.00 37.52  ? 61  LEU A HD21 1 
ATOM   915  H HD22 . LEU A 1 58  ? 21.238 25.470 23.674 0.00 37.52  ? 61  LEU A HD22 1 
ATOM   916  H HD23 . LEU A 1 58  ? 19.998 24.544 23.320 0.00 37.52  ? 61  LEU A HD23 1 
ATOM   917  N N    . LEU A 1 59  ? 16.785 26.675 20.667 1.00 22.39  ? 62  LEU A N    1 
ATOM   918  C CA   . LEU A 1 59  ? 16.100 25.845 19.675 1.00 21.95  ? 62  LEU A CA   1 
ATOM   919  C C    . LEU A 1 59  ? 15.365 26.689 18.650 1.00 25.06  ? 62  LEU A C    1 
ATOM   920  O O    . LEU A 1 59  ? 14.804 26.119 17.713 1.00 28.48  ? 62  LEU A O    1 
ATOM   921  C CB   . LEU A 1 59  ? 15.106 24.902 20.391 1.00 25.28  ? 62  LEU A CB   1 
ATOM   922  C CG   . LEU A 1 59  ? 15.747 23.913 21.364 1.00 24.91  ? 62  LEU A CG   1 
ATOM   923  C CD1  . LEU A 1 59  ? 14.687 22.980 21.970 1.00 27.47  ? 62  LEU A CD1  1 
ATOM   924  C CD2  . LEU A 1 59  ? 16.831 23.086 20.675 1.00 29.84  ? 62  LEU A CD2  1 
ATOM   925  H H    . LEU A 1 59  ? 16.358 26.782 21.407 0.00 26.88  ? 62  LEU A H    1 
ATOM   926  H HA   . LEU A 1 59  ? 16.743 25.290 19.206 0.00 26.35  ? 62  LEU A HA   1 
ATOM   927  H HB2  . LEU A 1 59  ? 14.479 25.443 20.896 0.00 30.35  ? 62  LEU A HB2  1 
ATOM   928  H HB3  . LEU A 1 59  ? 14.633 24.387 19.719 0.00 30.35  ? 62  LEU A HB3  1 
ATOM   929  H HG   . LEU A 1 59  ? 16.161 24.419 22.080 0.00 29.90  ? 62  LEU A HG   1 
ATOM   930  H HD11 . LEU A 1 59  ? 15.119 22.367 22.584 0.00 32.98  ? 62  LEU A HD11 1 
ATOM   931  H HD12 . LEU A 1 59  ? 14.030 23.514 22.443 0.00 32.98  ? 62  LEU A HD12 1 
ATOM   932  H HD13 . LEU A 1 59  ? 14.257 22.484 21.255 0.00 32.98  ? 62  LEU A HD13 1 
ATOM   933  H HD21 . LEU A 1 59  ? 17.083 22.350 21.255 0.00 35.82  ? 62  LEU A HD21 1 
ATOM   934  H HD22 . LEU A 1 59  ? 16.482 22.742 19.838 0.00 35.82  ? 62  LEU A HD22 1 
ATOM   935  H HD23 . LEU A 1 59  ? 17.600 23.652 20.505 0.00 35.82  ? 62  LEU A HD23 1 
ATOM   936  N N    . GLY A 1 60  ? 15.309 28.008 18.848 1.00 26.37  ? 63  GLY A N    1 
ATOM   937  C CA   . GLY A 1 60  ? 14.708 28.905 17.873 1.00 28.67  ? 63  GLY A CA   1 
ATOM   938  C C    . GLY A 1 60  ? 13.282 29.287 18.180 1.00 28.94  ? 63  GLY A C    1 
ATOM   939  O O    . GLY A 1 60  ? 12.701 30.092 17.421 1.00 30.91  ? 63  GLY A O    1 
ATOM   940  H H    . GLY A 1 60  ? 15.616 28.405 19.546 0.00 31.66  ? 63  GLY A H    1 
ATOM   941  H HA2  . GLY A 1 60  ? 15.233 29.720 17.833 0.00 34.42  ? 63  GLY A HA2  1 
ATOM   942  H HA3  . GLY A 1 60  ? 14.722 28.477 17.003 0.00 34.42  ? 63  GLY A HA3  1 
ATOM   943  N N    . TYR A 1 61  ? 12.677 28.722 19.233 1.00 23.84  ? 64  TYR A N    1 
ATOM   944  C CA   . TYR A 1 61  ? 11.274 29.026 19.509 1.00 25.91  ? 64  TYR A CA   1 
ATOM   945  C C    . TYR A 1 61  ? 11.111 30.448 20.036 1.00 27.31  ? 64  TYR A C    1 
ATOM   946  O O    . TYR A 1 61  ? 10.110 31.114 19.725 1.00 29.17  ? 64  TYR A O    1 
ATOM   947  C CB   . TYR A 1 61  ? 10.726 28.004 20.528 1.00 26.19  ? 64  TYR A CB   1 
ATOM   948  C CG   . TYR A 1 61  ? 9.237  28.183 20.803 1.00 26.27  ? 64  TYR A CG   1 
ATOM   949  C CD1  . TYR A 1 61  ? 8.302  27.576 20.005 1.00 29.57  ? 64  TYR A CD1  1 
ATOM   950  C CD2  . TYR A 1 61  ? 8.814  28.956 21.862 1.00 31.36  ? 64  TYR A CD2  1 
ATOM   951  C CE1  . TYR A 1 61  ? 6.940  27.741 20.243 1.00 40.24  ? 64  TYR A CE1  1 
ATOM   952  C CE2  . TYR A 1 61  ? 7.451  29.132 22.110 1.00 32.17  ? 64  TYR A CE2  1 
ATOM   953  C CZ   . TYR A 1 61  ? 6.542  28.529 21.302 1.00 32.81  ? 64  TYR A CZ   1 
ATOM   954  O OH   . TYR A 1 61  ? 5.184  28.684 21.546 1.00 39.86  ? 64  TYR A OH   1 
ATOM   955  H H    . TYR A 1 61  ? 13.047 28.177 19.785 0.00 28.54  ? 64  TYR A H    1 
ATOM   956  H HA   . TYR A 1 61  ? 10.760 28.954 18.689 0.00 31.10  ? 64  TYR A HA   1 
ATOM   957  H HB2  . TYR A 1 61  ? 10.862 27.109 20.181 0.00 31.44  ? 64  TYR A HB2  1 
ATOM   958  H HB3  . TYR A 1 61  ? 11.200 28.110 21.368 0.00 31.44  ? 64  TYR A HB3  1 
ATOM   959  H HD1  . TYR A 1 61  ? 8.581  27.046 19.294 0.00 35.49  ? 64  TYR A HD1  1 
ATOM   960  H HD2  . TYR A 1 61  ? 9.441  29.363 22.416 0.00 37.65  ? 64  TYR A HD2  1 
ATOM   961  H HE1  . TYR A 1 61  ? 6.310  27.328 19.697 0.00 48.30  ? 64  TYR A HE1  1 
ATOM   962  H HE2  . TYR A 1 61  ? 7.168  29.659 22.822 0.00 38.61  ? 64  TYR A HE2  1 
ATOM   963  H HH   . TYR A 1 61  ? 5.066  29.215 22.186 0.00 47.84  ? 64  TYR A HH   1 
ATOM   964  N N    . GLY A 1 62  ? 12.067 30.926 20.790 1.00 22.78  ? 65  GLY A N    1 
ATOM   965  C CA   . GLY A 1 62  ? 11.901 32.183 21.507 1.00 25.37  ? 65  GLY A CA   1 
ATOM   966  C C    . GLY A 1 62  ? 12.406 33.389 20.707 1.00 27.33  ? 65  GLY A C    1 
ATOM   967  O O    . GLY A 1 62  ? 12.816 34.388 21.313 1.00 24.67  ? 65  GLY A O    1 
ATOM   968  H H    . GLY A 1 62  ? 12.829 30.547 20.910 0.00 27.35  ? 65  GLY A H    1 
ATOM   969  H HA2  . GLY A 1 62  ? 10.960 32.319 21.701 0.00 30.45  ? 65  GLY A HA2  1 
ATOM   970  H HA3  . GLY A 1 62  ? 12.393 32.143 22.341 0.00 30.45  ? 65  GLY A HA3  1 
ATOM   971  N N    . LEU A 1 63  ? 12.399 33.262 19.386 1.00 27.71  ? 66  LEU A N    1 
ATOM   972  C CA   . LEU A 1 63  ? 12.886 34.307 18.468 1.00 25.20  ? 66  LEU A CA   1 
ATOM   973  C C    . LEU A 1 63  ? 11.772 34.707 17.537 1.00 29.85  ? 66  LEU A C    1 
ATOM   974  O O    . LEU A 1 63  ? 11.052 33.848 16.996 1.00 33.09  ? 66  LEU A O    1 
ATOM   975  C CB   . LEU A 1 63  ? 14.098 33.768 17.678 1.00 28.77  ? 66  LEU A CB   1 
ATOM   976  C CG   . LEU A 1 63  ? 14.707 34.628 16.585 1.00 30.79  ? 66  LEU A CG   1 
ATOM   977  C CD1  . LEU A 1 63  ? 15.321 35.885 17.115 1.00 32.73  ? 66  LEU A CD1  1 
ATOM   978  C CD2  . LEU A 1 63  ? 15.739 33.810 15.832 1.00 35.80  ? 66  LEU A CD2  1 
ATOM   979  H H    . LEU A 1 63  ? 12.110 32.562 18.978 0.00 33.26  ? 66  LEU A H    1 
ATOM   980  H HA   . LEU A 1 63  ? 13.159 35.104 18.950 0.00 30.26  ? 66  LEU A HA   1 
ATOM   981  H HB2  . LEU A 1 63  ? 14.806 33.594 18.317 0.00 34.54  ? 66  LEU A HB2  1 
ATOM   982  H HB3  . LEU A 1 63  ? 13.823 32.940 17.254 0.00 34.54  ? 66  LEU A HB3  1 
ATOM   983  H HG   . LEU A 1 63  ? 14.001 34.908 15.982 0.00 36.96  ? 66  LEU A HG   1 
ATOM   984  H HD11 . LEU A 1 63  ? 15.709 36.382 16.378 0.00 39.29  ? 66  LEU A HD11 1 
ATOM   985  H HD12 . LEU A 1 63  ? 14.633 36.415 17.546 0.00 39.29  ? 66  LEU A HD12 1 
ATOM   986  H HD13 . LEU A 1 63  ? 16.011 35.653 17.756 0.00 39.29  ? 66  LEU A HD13 1 
ATOM   987  H HD21 . LEU A 1 63  ? 16.130 34.359 15.134 0.00 42.97  ? 66  LEU A HD21 1 
ATOM   988  H HD22 . LEU A 1 63  ? 16.427 33.522 16.451 0.00 42.97  ? 66  LEU A HD22 1 
ATOM   989  H HD23 . LEU A 1 63  ? 15.303 33.037 15.439 0.00 42.97  ? 66  LEU A HD23 1 
ATOM   990  N N    . THR A 1 64  ? 11.617 36.028 17.305 1.00 25.76  ? 67  THR A N    1 
ATOM   991  C CA   . THR A 1 64  ? 10.720 36.510 16.259 1.00 30.64  ? 67  THR A CA   1 
ATOM   992  C C    . THR A 1 64  ? 11.421 37.607 15.479 1.00 28.91  ? 67  THR A C    1 
ATOM   993  O O    . THR A 1 64  ? 12.439 38.144 15.909 1.00 31.35  ? 67  THR A O    1 
ATOM   994  C CB   . THR A 1 64  ? 9.390  37.013 16.869 1.00 32.59  ? 67  THR A CB   1 
ATOM   995  O OG1  . THR A 1 64  ? 8.429  37.197 15.835 1.00 36.15  ? 67  THR A OG1  1 
ATOM   996  C CG2  . THR A 1 64  ? 9.593  38.322 17.650 1.00 34.51  ? 67  THR A CG2  1 
ATOM   997  H H    . THR A 1 64  ? 12.021 36.650 17.742 0.00 30.92  ? 67  THR A H    1 
ATOM   998  H HA   . THR A 1 64  ? 10.513 35.798 15.633 0.00 36.78  ? 67  THR A HA   1 
ATOM   999  H HB   . THR A 1 64  ? 9.055  36.354 17.497 0.00 39.12  ? 67  THR A HB   1 
ATOM   1000 H HG1  . THR A 1 64  ? 7.697  37.446 16.163 0.00 43.39  ? 67  THR A HG1  1 
ATOM   1001 H HG21 . THR A 1 64  ? 8.790  38.537 18.151 0.00 41.42  ? 67  THR A HG21 1 
ATOM   1002 H HG22 . THR A 1 64  ? 10.334 38.228 18.269 0.00 41.42  ? 67  THR A HG22 1 
ATOM   1003 H HG23 . THR A 1 64  ? 9.785  39.049 17.037 0.00 41.42  ? 67  THR A HG23 1 
ATOM   1004 N N    . MET A 1 65  ? 10.864 37.916 14.309 1.00 31.34  ? 68  MET A N    1 
ATOM   1005 C CA   . MET A 1 65  ? 11.381 38.996 13.460 1.00 34.91  ? 68  MET A CA   1 
ATOM   1006 C C    . MET A 1 65  ? 10.462 40.205 13.575 1.00 48.01  ? 68  MET A C    1 
ATOM   1007 O O    . MET A 1 65  ? 9.246  40.079 13.404 1.00 44.57  ? 68  MET A O    1 
ATOM   1008 C CB   . MET A 1 65  ? 11.477 38.558 12.002 1.00 41.20  ? 68  MET A CB   1 
ATOM   1009 C CG   . MET A 1 65  ? 12.353 37.337 11.759 1.00 56.51  ? 68  MET A CG   1 
ATOM   1010 S SD   . MET A 1 65  ? 14.049 37.552 12.354 1.00 53.97  ? 68  MET A SD   1 
ATOM   1011 C CE   . MET A 1 65  ? 14.756 38.549 11.071 1.00 56.91  ? 68  MET A CE   1 
ATOM   1012 H H    . MET A 1 65  ? 10.180 37.511 13.979 0.00 37.62  ? 68  MET A H    1 
ATOM   1013 H HA   . MET A 1 65  ? 12.273 39.232 13.759 0.00 41.91  ? 68  MET A HA   1 
ATOM   1014 H HB2  . MET A 1 65  ? 10.585 38.345 11.686 0.00 49.45  ? 68  MET A HB2  1 
ATOM   1015 H HB3  . MET A 1 65  ? 11.847 39.291 11.485 0.00 49.45  ? 68  MET A HB3  1 
ATOM   1016 H HG2  . MET A 1 65  ? 11.969 36.576 12.221 0.00 67.83  ? 68  MET A HG2  1 
ATOM   1017 H HG3  . MET A 1 65  ? 12.391 37.162 10.806 0.00 67.83  ? 68  MET A HG3  1 
ATOM   1018 H HE1  . MET A 1 65  ? 15.685 38.726 11.286 0.00 68.30  ? 68  MET A HE1  1 
ATOM   1019 H HE2  . MET A 1 65  ? 14.696 38.070 10.230 0.00 68.30  ? 68  MET A HE2  1 
ATOM   1020 H HE3  . MET A 1 65  ? 14.265 39.383 11.013 0.00 68.30  ? 68  MET A HE3  1 
ATOM   1021 N N    . VAL A 1 66  ? 11.046 41.365 13.859 1.00 37.52  ? 69  VAL A N    1 
ATOM   1022 C CA   . VAL A 1 66  ? 10.299 42.615 14.003 1.00 36.38  ? 69  VAL A CA   1 
ATOM   1023 C C    . VAL A 1 66  ? 10.811 43.564 12.931 1.00 40.04  ? 69  VAL A C    1 
ATOM   1024 O O    . VAL A 1 66  ? 12.015 43.823 12.854 1.00 40.29  ? 69  VAL A O    1 
ATOM   1025 C CB   . VAL A 1 66  ? 10.466 43.233 15.401 1.00 33.64  ? 69  VAL A CB   1 
ATOM   1026 C CG1  . VAL A 1 66  ? 9.700  44.559 15.476 1.00 41.02  ? 69  VAL A CG1  1 
ATOM   1027 C CG2  . VAL A 1 66  ? 9.983  42.279 16.490 1.00 32.74  ? 69  VAL A CG2  1 
ATOM   1028 H H    . VAL A 1 66  ? 11.893 41.457 13.976 0.00 45.04  ? 69  VAL A H    1 
ATOM   1029 H HA   . VAL A 1 66  ? 9.354  42.454 13.857 0.00 43.67  ? 69  VAL A HA   1 
ATOM   1030 H HB   . VAL A 1 66  ? 11.408 43.401 15.557 0.00 40.38  ? 69  VAL A HB   1 
ATOM   1031 H HG11 . VAL A 1 66  ? 9.674  44.857 16.399 0.00 49.24  ? 69  VAL A HG11 1 
ATOM   1032 H HG12 . VAL A 1 66  ? 10.155 45.218 14.928 0.00 49.24  ? 69  VAL A HG12 1 
ATOM   1033 H HG13 . VAL A 1 66  ? 8.798  44.421 15.147 0.00 49.24  ? 69  VAL A HG13 1 
ATOM   1034 H HG21 . VAL A 1 66  ? 10.072 42.714 17.353 0.00 39.30  ? 69  VAL A HG21 1 
ATOM   1035 H HG22 . VAL A 1 66  ? 9.053  42.057 16.326 0.00 39.30  ? 69  VAL A HG22 1 
ATOM   1036 H HG23 . VAL A 1 66  ? 10.525 41.475 16.468 0.00 39.30  ? 69  VAL A HG23 1 
ATOM   1037 N N    . PRO A 1 67  ? 9.948  44.114 12.077 1.00 37.24  ? 70  PRO A N    1 
ATOM   1038 C CA   . PRO A 1 67  ? 10.417 45.082 11.085 1.00 39.98  ? 70  PRO A CA   1 
ATOM   1039 C C    . PRO A 1 67  ? 10.510 46.476 11.692 1.00 54.72  ? 70  PRO A C    1 
ATOM   1040 O O    . PRO A 1 67  ? 9.560  46.968 12.298 1.00 53.66  ? 70  PRO A O    1 
ATOM   1041 C CB   . PRO A 1 67  ? 9.347  45.020 9.996  1.00 46.35  ? 70  PRO A CB   1 
ATOM   1042 C CG   . PRO A 1 67  ? 8.105  44.649 10.739 1.00 45.03  ? 70  PRO A CG   1 
ATOM   1043 C CD   . PRO A 1 67  ? 8.521  43.780 11.889 1.00 43.14  ? 70  PRO A CD   1 
ATOM   1044 H HA   . PRO A 1 67  ? 11.278 44.822 10.721 0.00 47.99  ? 70  PRO A HA   1 
ATOM   1045 H HB2  . PRO A 1 67  ? 9.255  45.885 9.567  0.00 55.63  ? 70  PRO A HB2  1 
ATOM   1046 H HB3  . PRO A 1 67  ? 9.578  44.346 9.338  0.00 55.63  ? 70  PRO A HB3  1 
ATOM   1047 H HG2  . PRO A 1 67  ? 7.671  45.454 11.062 0.00 54.05  ? 70  PRO A HG2  1 
ATOM   1048 H HG3  . PRO A 1 67  ? 7.508  44.165 10.147 0.00 54.05  ? 70  PRO A HG3  1 
ATOM   1049 H HD2  . PRO A 1 67  ? 8.010  43.994 12.685 0.00 51.79  ? 70  PRO A HD2  1 
ATOM   1050 H HD3  . PRO A 1 67  ? 8.414  42.842 11.668 0.00 51.79  ? 70  PRO A HD3  1 
ATOM   1051 N N    . PHE A 1 68  ? 11.679 47.087 11.554 1.00 49.66  ? 71  PHE A N    1 
ATOM   1052 C CA   . PHE A 1 68  ? 11.852 48.504 11.843 1.00 50.07  ? 71  PHE A CA   1 
ATOM   1053 C C    . PHE A 1 68  ? 13.169 48.941 11.214 1.00 51.66  ? 71  PHE A C    1 
ATOM   1054 O O    . PHE A 1 68  ? 14.108 48.146 11.084 1.00 52.12  ? 71  PHE A O    1 
ATOM   1055 C CB   . PHE A 1 68  ? 11.794 48.824 13.339 1.00 51.44  ? 71  PHE A CB   1 
ATOM   1056 C CG   . PHE A 1 68  ? 12.838 48.118 14.188 1.00 39.45  ? 71  PHE A CG   1 
ATOM   1057 C CD1  . PHE A 1 68  ? 14.139 48.603 14.241 1.00 49.98  ? 71  PHE A CD1  1 
ATOM   1058 C CD2  . PHE A 1 68  ? 12.508 47.010 14.919 1.00 35.02  ? 71  PHE A CD2  1 
ATOM   1059 C CE1  . PHE A 1 68  ? 15.093 47.979 15.029 1.00 44.04  ? 71  PHE A CE1  1 
ATOM   1060 C CE2  . PHE A 1 68  ? 13.456 46.361 15.715 1.00 40.64  ? 71  PHE A CE2  1 
ATOM   1061 C CZ   . PHE A 1 68  ? 14.761 46.856 15.765 1.00 37.51  ? 71  PHE A CZ   1 
ATOM   1062 H H    . PHE A 1 68  ? 12.399 46.697 11.291 0.00 59.60  ? 71  PHE A H    1 
ATOM   1063 H HA   . PHE A 1 68  ? 11.131 49.013 11.440 0.00 60.10  ? 71  PHE A HA   1 
ATOM   1064 H HB2  . PHE A 1 68  ? 11.923 49.779 13.453 0.00 61.74  ? 71  PHE A HB2  1 
ATOM   1065 H HB3  . PHE A 1 68  ? 10.922 48.564 13.675 0.00 61.74  ? 71  PHE A HB3  1 
ATOM   1066 H HD1  . PHE A 1 68  ? 14.372 49.353 13.743 0.00 59.99  ? 71  PHE A HD1  1 
ATOM   1067 H HD2  . PHE A 1 68  ? 11.638 46.683 14.887 0.00 42.04  ? 71  PHE A HD2  1 
ATOM   1068 H HE1  . PHE A 1 68  ? 15.959 48.316 15.062 0.00 52.86  ? 71  PHE A HE1  1 
ATOM   1069 H HE2  . PHE A 1 68  ? 13.221 45.607 16.206 0.00 48.78  ? 71  PHE A HE2  1 
ATOM   1070 H HZ   . PHE A 1 68  ? 15.403 46.434 16.290 0.00 45.03  ? 71  PHE A HZ   1 
ATOM   1071 N N    . GLY A 1 69  ? 13.221 50.206 10.809 1.00 57.93  ? 72  GLY A N    1 
ATOM   1072 C CA   . GLY A 1 69  ? 14.374 50.689 10.075 1.00 59.80  ? 72  GLY A CA   1 
ATOM   1073 C C    . GLY A 1 69  ? 14.563 50.005 8.741  1.00 68.02  ? 72  GLY A C    1 
ATOM   1074 O O    . GLY A 1 69  ? 15.701 49.857 8.278  1.00 70.69  ? 72  GLY A O    1 
ATOM   1075 H H    . GLY A 1 69  ? 12.608 50.794 10.947 0.00 69.53  ? 72  GLY A H    1 
ATOM   1076 H HA2  . GLY A 1 69  ? 14.273 51.640 9.915  0.00 71.78  ? 72  GLY A HA2  1 
ATOM   1077 H HA3  . GLY A 1 69  ? 15.172 50.541 10.606 0.00 71.78  ? 72  GLY A HA3  1 
ATOM   1078 N N    . GLY A 1 70  ? 13.473 49.568 8.109  1.00 56.28  ? 73  GLY A N    1 
ATOM   1079 C CA   . GLY A 1 70  ? 13.557 48.946 6.813  1.00 58.77  ? 73  GLY A CA   1 
ATOM   1080 C C    . GLY A 1 70  ? 14.195 47.584 6.776  1.00 67.27  ? 73  GLY A C    1 
ATOM   1081 O O    . GLY A 1 70  ? 14.513 47.096 5.689  1.00 63.90  ? 73  GLY A O    1 
ATOM   1082 H H    . GLY A 1 70  ? 12.674 49.625 8.421  0.00 67.55  ? 73  GLY A H    1 
ATOM   1083 H HA2  . GLY A 1 70  ? 12.659 48.856 6.458  0.00 70.53  ? 73  GLY A HA2  1 
ATOM   1084 H HA3  . GLY A 1 70  ? 14.071 49.525 6.228  0.00 70.53  ? 73  GLY A HA3  1 
ATOM   1085 N N    . GLU A 1 71  ? 14.401 46.957 7.929  1.00 55.42  ? 74  GLU A N    1 
ATOM   1086 C CA   . GLU A 1 71  ? 14.979 45.629 8.005  1.00 56.23  ? 74  GLU A CA   1 
ATOM   1087 C C    . GLU A 1 71  ? 14.074 44.757 8.858  1.00 43.77  ? 74  GLU A C    1 
ATOM   1088 O O    . GLU A 1 71  ? 13.255 45.253 9.631  1.00 50.95  ? 74  GLU A O    1 
ATOM   1089 C CB   . GLU A 1 71  ? 16.392 45.664 8.603  1.00 61.64  ? 74  GLU A CB   1 
ATOM   1090 H H    . GLU A 1 71  ? 14.207 47.292 8.697  0.00 66.52  ? 74  GLU A H    1 
ATOM   1091 H HA   . GLU A 1 71  ? 15.042 45.242 7.118  0.00 67.49  ? 74  GLU A HA   1 
ATOM   1092 N N    . GLN A 1 72  ? 14.229 43.441 8.697  1.00 51.68  ? 75  GLN A N    1 
ATOM   1093 C CA   . GLN A 1 72  ? 13.629 42.476 9.624  1.00 52.14  ? 75  GLN A CA   1 
ATOM   1094 C C    . GLN A 1 72  ? 14.663 42.148 10.691 1.00 49.63  ? 75  GLN A C    1 
ATOM   1095 O O    . GLN A 1 72  ? 15.700 41.540 10.404 1.00 52.03  ? 75  GLN A O    1 
ATOM   1096 C CB   . GLN A 1 72  ? 13.162 41.221 8.895  1.00 55.34  ? 75  GLN A CB   1 
ATOM   1097 C CG   . GLN A 1 72  ? 12.390 41.483 7.608  1.00 81.04  ? 75  GLN A CG   1 
ATOM   1098 C CD   . GLN A 1 72  ? 10.891 41.549 7.838  1.00 90.07  ? 75  GLN A CD   1 
ATOM   1099 O OE1  . GLN A 1 72  ? 10.300 40.643 8.429  1.00 91.98  ? 75  GLN A OE1  1 
ATOM   1100 N NE2  . GLN A 1 72  ? 10.268 42.627 7.370  1.00 81.06  ? 75  GLN A NE2  1 
ATOM   1101 H H    . GLN A 1 72  ? 14.677 43.081 8.057  0.00 62.03  ? 75  GLN A H    1 
ATOM   1102 H HA   . GLN A 1 72  ? 12.851 42.872 10.047 0.00 62.58  ? 75  GLN A HA   1 
ATOM   1103 H HB2  . GLN A 1 72  ? 13.941 40.690 8.665  0.00 66.42  ? 75  GLN A HB2  1 
ATOM   1104 H HB3  . GLN A 1 72  ? 12.581 40.718 9.487  0.00 66.42  ? 75  GLN A HB3  1 
ATOM   1105 H HG2  . GLN A 1 72  ? 12.675 42.331 7.233  0.00 97.26  ? 75  GLN A HG2  1 
ATOM   1106 H HG3  . GLN A 1 72  ? 12.568 40.766 6.979  0.00 97.26  ? 75  GLN A HG3  1 
ATOM   1107 H HE21 . GLN A 1 72  ? 10.714 43.239 6.962  0.00 97.28  ? 75  GLN A HE21 1 
ATOM   1108 H HE22 . GLN A 1 72  ? 9.418  42.712 7.475  0.00 97.28  ? 75  GLN A HE22 1 
ATOM   1109 N N    . ASN A 1 73  ? 14.394 42.555 11.901 1.00 35.66  ? 76  ASN A N    1 
ATOM   1110 C CA   . ASN A 1 73  ? 15.372 42.436 12.975 1.00 32.67  ? 76  ASN A CA   1 
ATOM   1111 C C    . ASN A 1 73  ? 15.042 41.254 13.867 1.00 36.56  ? 76  ASN A C    1 
ATOM   1112 O O    . ASN A 1 73  ? 13.908 41.120 14.314 1.00 32.92  ? 76  ASN A O    1 
ATOM   1113 C CB   . ASN A 1 73  ? 15.380 43.723 13.810 1.00 31.99  ? 76  ASN A CB   1 
ATOM   1114 C CG   . ASN A 1 73  ? 15.665 44.960 12.949 1.00 38.88  ? 76  ASN A CG   1 
ATOM   1115 O OD1  . ASN A 1 73  ? 16.816 45.289 12.688 1.00 50.83  ? 76  ASN A OD1  1 
ATOM   1116 N ND2  . ASN A 1 73  ? 14.607 45.624 12.485 1.00 41.76  ? 76  ASN A ND2  1 
ATOM   1117 H H    . ASN A 1 73  ? 13.648 42.910 12.140 0.00 42.81  ? 76  ASN A H    1 
ATOM   1118 H HA   . ASN A 1 73  ? 16.254 42.292 12.597 0.00 39.15  ? 76  ASN A HA   1 
ATOM   1119 H HB2  . ASN A 1 73  ? 14.513 43.837 14.229 0.00 38.32  ? 76  ASN A HB2  1 
ATOM   1120 H HB3  . ASN A 1 73  ? 16.071 43.659 14.488 0.00 38.32  ? 76  ASN A HB3  1 
ATOM   1121 H HD21 . ASN A 1 73  ? 14.718 46.324 11.998 0.00 50.13  ? 76  ASN A HD21 1 
ATOM   1122 H HD22 . ASN A 1 73  ? 13.813 45.353 12.673 0.00 50.13  ? 76  ASN A HD22 1 
ATOM   1123 N N    . PRO A 1 74  ? 16.002 40.375 14.162 1.00 34.36  ? 77  PRO A N    1 
ATOM   1124 C CA   . PRO A 1 74  ? 15.734 39.271 15.096 1.00 31.63  ? 77  PRO A CA   1 
ATOM   1125 C C    . PRO A 1 74  ? 15.612 39.765 16.526 1.00 33.91  ? 77  PRO A C    1 
ATOM   1126 O O    . PRO A 1 74  ? 16.523 40.389 17.076 1.00 34.91  ? 77  PRO A O    1 
ATOM   1127 C CB   . PRO A 1 74  ? 16.950 38.342 14.919 1.00 40.79  ? 77  PRO A CB   1 
ATOM   1128 C CG   . PRO A 1 74  ? 18.005 39.158 14.266 1.00 42.54  ? 77  PRO A CG   1 
ATOM   1129 C CD   . PRO A 1 74  ? 17.358 40.320 13.561 1.00 38.14  ? 77  PRO A CD   1 
ATOM   1130 H HA   . PRO A 1 74  ? 14.920 38.808 14.842 0.00 37.96  ? 77  PRO A HA   1 
ATOM   1131 H HB2  . PRO A 1 74  ? 17.248 38.028 15.787 0.00 48.96  ? 77  PRO A HB2  1 
ATOM   1132 H HB3  . PRO A 1 74  ? 16.705 37.588 14.360 0.00 48.96  ? 77  PRO A HB3  1 
ATOM   1133 H HG2  . PRO A 1 74  ? 18.618 39.481 14.944 0.00 51.06  ? 77  PRO A HG2  1 
ATOM   1134 H HG3  . PRO A 1 74  ? 18.480 38.605 13.626 0.00 51.06  ? 77  PRO A HG3  1 
ATOM   1135 H HD2  . PRO A 1 74  ? 17.844 41.142 13.732 0.00 45.79  ? 77  PRO A HD2  1 
ATOM   1136 H HD3  . PRO A 1 74  ? 17.305 40.159 12.606 0.00 45.79  ? 77  PRO A HD3  1 
ATOM   1137 N N    . ILE A 1 75  ? 14.468 39.482 17.154 1.00 25.70  ? 78  ILE A N    1 
ATOM   1138 C CA   . ILE A 1 75  ? 14.201 39.887 18.521 1.00 24.26  ? 78  ILE A CA   1 
ATOM   1139 C C    . ILE A 1 75  ? 13.916 38.629 19.329 1.00 26.22  ? 78  ILE A C    1 
ATOM   1140 O O    . ILE A 1 75  ? 12.953 37.897 19.040 1.00 25.48  ? 78  ILE A O    1 
ATOM   1141 C CB   . ILE A 1 75  ? 13.009 40.874 18.604 1.00 30.28  ? 78  ILE A CB   1 
ATOM   1142 C CG1  . ILE A 1 75  ? 13.322 42.170 17.858 1.00 30.10  ? 78  ILE A CG1  1 
ATOM   1143 C CG2  . ILE A 1 75  ? 12.631 41.131 20.069 1.00 30.45  ? 78  ILE A CG2  1 
ATOM   1144 C CD1  . ILE A 1 75  ? 14.481 42.993 18.463 1.00 35.83  ? 78  ILE A CD1  1 
ATOM   1145 H H    . ILE A 1 75  ? 13.820 39.047 16.794 0.00 30.78  ? 78  ILE A H    1 
ATOM   1146 H HA   . ILE A 1 75  ? 14.987 40.320 18.890 0.00 29.12  ? 78  ILE A HA   1 
ATOM   1147 H HB   . ILE A 1 75  ? 12.243 40.471 18.166 0.00 36.35  ? 78  ILE A HB   1 
ATOM   1148 H HG12 . ILE A 1 75  ? 13.565 41.950 16.945 0.00 36.13  ? 78  ILE A HG12 1 
ATOM   1149 H HG13 . ILE A 1 75  ? 12.530 42.730 17.865 0.00 36.13  ? 78  ILE A HG13 1 
ATOM   1150 H HG21 . ILE A 1 75  ? 12.058 41.913 20.114 0.00 36.55  ? 78  ILE A HG21 1 
ATOM   1151 H HG22 . ILE A 1 75  ? 12.162 40.356 20.414 0.00 36.55  ? 78  ILE A HG22 1 
ATOM   1152 H HG23 . ILE A 1 75  ? 13.440 41.284 20.581 0.00 36.55  ? 78  ILE A HG23 1 
ATOM   1153 H HD11 . ILE A 1 75  ? 14.607 43.796 17.934 0.00 43.01  ? 78  ILE A HD11 1 
ATOM   1154 H HD12 . ILE A 1 75  ? 14.256 43.229 19.376 0.00 43.01  ? 78  ILE A HD12 1 
ATOM   1155 H HD13 . ILE A 1 75  ? 15.289 42.457 18.449 0.00 43.01  ? 78  ILE A HD13 1 
ATOM   1156 N N    . TYR A 1 76  ? 14.786 38.347 20.287 1.00 22.59  ? 79  TYR A N    1 
ATOM   1157 C CA   . TYR A 1 76  ? 14.567 37.231 21.220 1.00 21.48  ? 79  TYR A CA   1 
ATOM   1158 C C    . TYR A 1 76  ? 13.549 37.660 22.274 1.00 22.81  ? 79  TYR A C    1 
ATOM   1159 O O    . TYR A 1 76  ? 13.889 38.245 23.315 1.00 25.12  ? 79  TYR A O    1 
ATOM   1160 C CB   . TYR A 1 76  ? 15.901 36.832 21.853 1.00 22.24  ? 79  TYR A CB   1 
ATOM   1161 C CG   . TYR A 1 76  ? 16.757 35.980 20.918 1.00 21.44  ? 79  TYR A CG   1 
ATOM   1162 C CD1  . TYR A 1 76  ? 16.470 34.636 20.715 1.00 22.69  ? 79  TYR A CD1  1 
ATOM   1163 C CD2  . TYR A 1 76  ? 17.831 36.536 20.257 1.00 29.07  ? 79  TYR A CD2  1 
ATOM   1164 C CE1  . TYR A 1 76  ? 17.275 33.843 19.897 1.00 22.08  ? 79  TYR A CE1  1 
ATOM   1165 C CE2  . TYR A 1 76  ? 18.632 35.761 19.413 1.00 24.50  ? 79  TYR A CE2  1 
ATOM   1166 C CZ   . TYR A 1 76  ? 18.325 34.397 19.237 1.00 25.99  ? 79  TYR A CZ   1 
ATOM   1167 O OH   . TYR A 1 76  ? 19.099 33.628 18.383 1.00 28.67  ? 79  TYR A OH   1 
ATOM   1168 H H    . TYR A 1 76  ? 15.514 38.784 20.424 0.00 27.12  ? 79  TYR A H    1 
ATOM   1169 H HA   . TYR A 1 76  ? 14.195 36.472 20.745 0.00 25.79  ? 79  TYR A HA   1 
ATOM   1170 H HB2  . TYR A 1 76  ? 16.401 37.634 22.073 0.00 26.70  ? 79  TYR A HB2  1 
ATOM   1171 H HB3  . TYR A 1 76  ? 15.729 36.317 22.657 0.00 26.70  ? 79  TYR A HB3  1 
ATOM   1172 H HD1  . TYR A 1 76  ? 15.729 34.258 21.130 0.00 27.24  ? 79  TYR A HD1  1 
ATOM   1173 H HD2  . TYR A 1 76  ? 18.026 37.438 20.374 0.00 34.89  ? 79  TYR A HD2  1 
ATOM   1174 H HE1  . TYR A 1 76  ? 17.093 32.935 19.804 0.00 26.50  ? 79  TYR A HE1  1 
ATOM   1175 H HE2  . TYR A 1 76  ? 19.358 36.141 18.973 0.00 29.42  ? 79  TYR A HE2  1 
ATOM   1176 H HH   . TYR A 1 76  ? 19.691 34.103 18.025 0.00 34.41  ? 79  TYR A HH   1 
ATOM   1177 N N    . TRP A 1 77  ? 12.273 37.345 22.028 1.00 22.53  ? 80  TRP A N    1 
ATOM   1178 C CA   . TRP A 1 77  ? 11.247 37.751 22.973 1.00 21.38  ? 80  TRP A CA   1 
ATOM   1179 C C    . TRP A 1 77  ? 11.266 36.892 24.216 1.00 20.97  ? 80  TRP A C    1 
ATOM   1180 O O    . TRP A 1 77  ? 10.749 37.305 25.251 1.00 20.96  ? 80  TRP A O    1 
ATOM   1181 C CB   . TRP A 1 77  ? 9.838  37.692 22.328 1.00 21.62  ? 80  TRP A CB   1 
ATOM   1182 C CG   . TRP A 1 77  ? 9.455  36.321 21.820 1.00 22.92  ? 80  TRP A CG   1 
ATOM   1183 C CD1  . TRP A 1 77  ? 9.587  35.848 20.547 1.00 26.69  ? 80  TRP A CD1  1 
ATOM   1184 C CD2  . TRP A 1 77  ? 8.911  35.239 22.600 1.00 24.87  ? 80  TRP A CD2  1 
ATOM   1185 N NE1  . TRP A 1 77  ? 9.136  34.538 20.472 1.00 33.85  ? 80  TRP A NE1  1 
ATOM   1186 C CE2  . TRP A 1 77  ? 8.728  34.146 21.719 1.00 27.28  ? 80  TRP A CE2  1 
ATOM   1187 C CE3  . TRP A 1 77  ? 8.558  35.091 23.946 1.00 28.54  ? 80  TRP A CE3  1 
ATOM   1188 C CZ2  . TRP A 1 77  ? 8.212  32.929 22.150 1.00 31.50  ? 80  TRP A CZ2  1 
ATOM   1189 C CZ3  . TRP A 1 77  ? 8.049  33.871 24.374 1.00 30.32  ? 80  TRP A CZ3  1 
ATOM   1190 C CH2  . TRP A 1 77  ? 7.868  32.803 23.457 1.00 30.32  ? 80  TRP A CH2  1 
ATOM   1191 H H    . TRP A 1 77  ? 11.991 36.910 21.342 0.00 27.05  ? 80  TRP A H    1 
ATOM   1192 H HA   . TRP A 1 77  ? 11.411 38.674 23.221 0.00 25.67  ? 80  TRP A HA   1 
ATOM   1193 H HB2  . TRP A 1 77  ? 9.181  37.955 22.992 0.00 25.95  ? 80  TRP A HB2  1 
ATOM   1194 H HB3  . TRP A 1 77  ? 9.813  38.303 21.576 0.00 25.95  ? 80  TRP A HB3  1 
ATOM   1195 H HD1  . TRP A 1 77  ? 9.931  36.334 19.832 0.00 32.04  ? 80  TRP A HD1  1 
ATOM   1196 H HE1  . TRP A 1 77  ? 9.116  34.054 19.762 0.00 40.63  ? 80  TRP A HE1  1 
ATOM   1197 H HE3  . TRP A 1 77  ? 8.661  35.796 24.543 0.00 34.26  ? 80  TRP A HE3  1 
ATOM   1198 H HZ2  . TRP A 1 77  ? 8.106  32.219 21.558 0.00 37.81  ? 80  TRP A HZ2  1 
ATOM   1199 H HZ3  . TRP A 1 77  ? 7.826  33.753 25.269 0.00 36.40  ? 80  TRP A HZ3  1 
ATOM   1200 H HH2  . TRP A 1 77  ? 7.505  32.002 23.757 0.00 36.39  ? 80  TRP A HH2  1 
ATOM   1201 N N    . ALA A 1 78  ? 11.879 35.689 24.152 1.00 19.98  ? 81  ALA A N    1 
ATOM   1202 C CA   . ALA A 1 78  ? 11.855 34.818 25.322 1.00 19.77  ? 81  ALA A CA   1 
ATOM   1203 C C    . ALA A 1 78  ? 12.551 35.442 26.532 1.00 19.23  ? 81  ALA A C    1 
ATOM   1204 O O    . ALA A 1 78  ? 12.271 35.046 27.666 1.00 21.32  ? 81  ALA A O    1 
ATOM   1205 C CB   . ALA A 1 78  ? 12.482 33.476 25.001 1.00 25.46  ? 81  ALA A CB   1 
ATOM   1206 H H    . ALA A 1 78  ? 12.296 35.377 23.468 0.00 23.99  ? 81  ALA A H    1 
ATOM   1207 H HA   . ALA A 1 78  ? 10.928 34.662 25.561 0.00 23.73  ? 81  ALA A HA   1 
ATOM   1208 H HB1  . ALA A 1 78  ? 12.496 32.934 25.805 0.00 30.57  ? 81  ALA A HB1  1 
ATOM   1209 H HB2  . ALA A 1 78  ? 11.955 33.038 24.315 0.00 30.57  ? 81  ALA A HB2  1 
ATOM   1210 H HB3  . ALA A 1 78  ? 13.387 33.619 24.682 0.00 30.57  ? 81  ALA A HB3  1 
ATOM   1211 N N    . ARG A 1 79  ? 13.477 36.401 26.312 1.00 19.85  ? 82  ARG A N    1 
ATOM   1212 C CA   . ARG A 1 79  ? 14.106 37.056 27.446 1.00 19.71  ? 82  ARG A CA   1 
ATOM   1213 C C    . ARG A 1 79  ? 13.089 37.693 28.360 1.00 20.65  ? 82  ARG A C    1 
ATOM   1214 O O    . ARG A 1 79  ? 13.246 37.639 29.576 1.00 20.25  ? 82  ARG A O    1 
ATOM   1215 C CB   . ARG A 1 79  ? 15.067 38.179 26.942 1.00 24.67  ? 82  ARG A CB   1 
ATOM   1216 C CG   . ARG A 1 79  ? 16.197 37.655 26.168 1.00 24.21  ? 82  ARG A CG   1 
ATOM   1217 C CD   . ARG A 1 79  ? 17.276 38.767 26.009 1.00 26.86  ? 82  ARG A CD   1 
ATOM   1218 N NE   . ARG A 1 79  ? 18.295 38.360 25.041 1.00 24.97  ? 82  ARG A NE   1 
ATOM   1219 C CZ   . ARG A 1 79  ? 19.219 37.437 25.292 1.00 25.03  ? 82  ARG A CZ   1 
ATOM   1220 N NH1  . ARG A 1 79  ? 19.311 36.848 26.468 1.00 29.10  ? 82  ARG A NH1  1 
ATOM   1221 N NH2  . ARG A 1 79  ? 20.091 37.137 24.341 1.00 31.57  ? 82  ARG A NH2  1 
ATOM   1222 H H    . ARG A 1 79  ? 13.739 36.672 25.539 0.00 23.84  ? 82  ARG A H    1 
ATOM   1223 H HA   . ARG A 1 79  ? 14.603 36.383 27.937 0.00 23.66  ? 82  ARG A HA   1 
ATOM   1224 H HB2  . ARG A 1 79  ? 14.570 38.787 26.372 0.00 29.61  ? 82  ARG A HB2  1 
ATOM   1225 H HB3  . ARG A 1 79  ? 15.423 38.657 27.707 0.00 29.61  ? 82  ARG A HB3  1 
ATOM   1226 H HG2  . ARG A 1 79  ? 16.591 36.899 26.631 0.00 29.06  ? 82  ARG A HG2  1 
ATOM   1227 H HG3  . ARG A 1 79  ? 15.895 37.383 25.287 0.00 29.06  ? 82  ARG A HG3  1 
ATOM   1228 H HD2  . ARG A 1 79  ? 16.857 39.583 25.693 0.00 32.24  ? 82  ARG A HD2  1 
ATOM   1229 H HD3  . ARG A 1 79  ? 17.707 38.925 26.864 0.00 32.24  ? 82  ARG A HD3  1 
ATOM   1230 H HE   . ARG A 1 79  ? 18.296 38.739 24.268 0.00 29.98  ? 82  ARG A HE   1 
ATOM   1231 H HH11 . ARG A 1 79  ? 18.764 37.058 27.098 0.00 34.93  ? 82  ARG A HH11 1 
ATOM   1232 H HH12 . ARG A 1 79  ? 19.917 36.254 26.606 0.00 34.93  ? 82  ARG A HH12 1 
ATOM   1233 H HH21 . ARG A 1 79  ? 20.052 37.537 23.580 0.00 37.89  ? 82  ARG A HH21 1 
ATOM   1234 H HH22 . ARG A 1 79  ? 20.696 36.543 24.484 0.00 37.89  ? 82  ARG A HH22 1 
ATOM   1235 N N    . TYR A 1 80  ? 12.063 38.336 27.788 1.00 20.77  ? 83  TYR A N    1 
ATOM   1236 C CA   . TYR A 1 80  ? 11.100 39.055 28.629 1.00 16.73  ? 83  TYR A CA   1 
ATOM   1237 C C    . TYR A 1 80  ? 10.196 38.116 29.366 1.00 19.93  ? 83  TYR A C    1 
ATOM   1238 O O    . TYR A 1 80  ? 9.746  38.438 30.477 1.00 21.59  ? 83  TYR A O    1 
ATOM   1239 C CB   . TYR A 1 80  ? 10.262 40.026 27.744 1.00 18.23  ? 83  TYR A CB   1 
ATOM   1240 C CG   . TYR A 1 80  ? 11.221 40.922 26.991 1.00 20.82  ? 83  TYR A CG   1 
ATOM   1241 C CD1  . TYR A 1 80  ? 11.696 42.114 27.561 1.00 22.76  ? 83  TYR A CD1  1 
ATOM   1242 C CD2  . TYR A 1 80  ? 11.701 40.551 25.757 1.00 23.17  ? 83  TYR A CD2  1 
ATOM   1243 C CE1  . TYR A 1 80  ? 12.601 42.892 26.862 1.00 24.59  ? 83  TYR A CE1  1 
ATOM   1244 C CE2  . TYR A 1 80  ? 12.608 41.331 25.053 1.00 21.67  ? 83  TYR A CE2  1 
ATOM   1245 C CZ   . TYR A 1 80  ? 13.061 42.493 25.638 1.00 24.99  ? 83  TYR A CZ   1 
ATOM   1246 O OH   . TYR A 1 80  ? 13.971 43.248 24.967 1.00 25.21  ? 83  TYR A OH   1 
ATOM   1247 H H    . TYR A 1 80  ? 11.906 38.370 26.943 0.00 24.94  ? 83  TYR A H    1 
ATOM   1248 H HA   . TYR A 1 80  ? 11.584 39.578 29.288 0.00 20.09  ? 83  TYR A HA   1 
ATOM   1249 H HB2  . TYR A 1 80  ? 9.728  39.522 27.110 0.00 21.89  ? 83  TYR A HB2  1 
ATOM   1250 H HB3  . TYR A 1 80  ? 9.685  40.572 28.302 0.00 21.89  ? 83  TYR A HB3  1 
ATOM   1251 H HD1  . TYR A 1 80  ? 11.405 42.378 28.404 0.00 27.33  ? 83  TYR A HD1  1 
ATOM   1252 H HD2  . TYR A 1 80  ? 11.408 39.751 25.382 0.00 27.82  ? 83  TYR A HD2  1 
ATOM   1253 H HE1  . TYR A 1 80  ? 12.898 43.694 27.228 0.00 29.52  ? 83  TYR A HE1  1 
ATOM   1254 H HE2  . TYR A 1 80  ? 12.903 41.076 24.208 0.00 26.01  ? 83  TYR A HE2  1 
ATOM   1255 H HH   . TYR A 1 80  ? 14.138 42.901 24.221 0.00 30.27  ? 83  TYR A HH   1 
ATOM   1256 N N    . ALA A 1 81  ? 9.891  36.935 28.775 1.00 18.03  ? 84  ALA A N    1 
ATOM   1257 C CA   . ALA A 1 81  ? 9.123  35.951 29.536 1.00 18.25  ? 84  ALA A CA   1 
ATOM   1258 C C    . ALA A 1 81  ? 9.912  35.435 30.738 1.00 23.65  ? 84  ALA A C    1 
ATOM   1259 O O    . ALA A 1 81  ? 9.332  35.206 31.807 1.00 24.10  ? 84  ALA A O    1 
ATOM   1260 C CB   . ALA A 1 81  ? 8.730  34.786 28.589 1.00 19.82  ? 84  ALA A CB   1 
ATOM   1261 H H    . ALA A 1 81  ? 10.111 36.702 27.977 0.00 21.65  ? 84  ALA A H    1 
ATOM   1262 H HA   . ALA A 1 81  ? 8.313  36.361 29.879 0.00 21.91  ? 84  ALA A HA   1 
ATOM   1263 H HB1  . ALA A 1 81  ? 8.213  34.134 29.088 0.00 23.80  ? 84  ALA A HB1  1 
ATOM   1264 H HB2  . ALA A 1 81  ? 8.199  35.139 27.858 0.00 23.80  ? 84  ALA A HB2  1 
ATOM   1265 H HB3  . ALA A 1 81  ? 9.537  34.374 28.243 0.00 23.80  ? 84  ALA A HB3  1 
ATOM   1266 N N    . ASP A 1 82  ? 11.217 35.191 30.570 1.00 18.56  ? 85  ASP A N    1 
ATOM   1267 C CA   . ASP A 1 82  ? 12.085 34.855 31.696 1.00 18.59  ? 85  ASP A CA   1 
ATOM   1268 C C    . ASP A 1 82  ? 12.033 35.964 32.736 1.00 18.68  ? 85  ASP A C    1 
ATOM   1269 O O    . ASP A 1 82  ? 11.638 35.736 33.911 1.00 20.16  ? 85  ASP A O    1 
ATOM   1270 C CB   . ASP A 1 82  ? 13.478 34.680 31.099 1.00 18.08  ? 85  ASP A CB   1 
ATOM   1271 C CG   . ASP A 1 82  ? 14.626 34.532 32.141 1.00 19.64  ? 85  ASP A CG   1 
ATOM   1272 O OD1  . ASP A 1 82  ? 14.489 34.890 33.311 1.00 21.55  ? 85  ASP A OD1  1 
ATOM   1273 O OD2  . ASP A 1 82  ? 15.675 34.109 31.685 1.00 20.72  ? 85  ASP A OD2  1 
ATOM   1274 H H    . ASP A 1 82  ? 11.622 35.214 29.812 0.00 22.28  ? 85  ASP A H    1 
ATOM   1275 H HA   . ASP A 1 82  ? 11.822 34.040 32.152 0.00 22.32  ? 85  ASP A HA   1 
ATOM   1276 H HB2  . ASP A 1 82  ? 13.479 33.880 30.550 0.00 21.71  ? 85  ASP A HB2  1 
ATOM   1277 H HB3  . ASP A 1 82  ? 13.679 35.457 30.554 0.00 21.71  ? 85  ASP A HB3  1 
ATOM   1278 N N    . TRP A 1 83  ? 12.380 37.179 32.320 1.00 17.55  ? 86  TRP A N    1 
ATOM   1279 C CA   . TRP A 1 83  ? 12.556 38.262 33.317 1.00 18.63  ? 86  TRP A CA   1 
ATOM   1280 C C    . TRP A 1 83  ? 11.252 38.613 34.009 1.00 20.30  ? 86  TRP A C    1 
ATOM   1281 O O    . TRP A 1 83  ? 11.260 39.065 35.151 1.00 20.57  ? 86  TRP A O    1 
ATOM   1282 C CB   . TRP A 1 83  ? 13.109 39.495 32.593 1.00 17.68  ? 86  TRP A CB   1 
ATOM   1283 C CG   . TRP A 1 83  ? 14.479 39.276 31.972 1.00 17.28  ? 86  TRP A CG   1 
ATOM   1284 C CD1  . TRP A 1 83  ? 15.333 38.264 32.209 1.00 19.46  ? 86  TRP A CD1  1 
ATOM   1285 C CD2  . TRP A 1 83  ? 15.104 40.133 30.988 1.00 17.62  ? 86  TRP A CD2  1 
ATOM   1286 N NE1  . TRP A 1 83  ? 16.498 38.413 31.433 1.00 19.48  ? 86  TRP A NE1  1 
ATOM   1287 C CE2  . TRP A 1 83  ? 16.336 39.542 30.664 1.00 18.70  ? 86  TRP A CE2  1 
ATOM   1288 C CE3  . TRP A 1 83  ? 14.686 41.278 30.300 1.00 21.81  ? 86  TRP A CE3  1 
ATOM   1289 C CZ2  . TRP A 1 83  ? 17.230 40.115 29.741 1.00 21.28  ? 86  TRP A CZ2  1 
ATOM   1290 C CZ3  . TRP A 1 83  ? 15.571 41.853 29.373 1.00 22.30  ? 86  TRP A CZ3  1 
ATOM   1291 C CH2  . TRP A 1 83  ? 16.830 41.252 29.109 1.00 21.85  ? 86  TRP A CH2  1 
ATOM   1292 H H    . TRP A 1 83  ? 12.517 37.405 31.502 0.00 21.07  ? 86  TRP A H    1 
ATOM   1293 H HA   . TRP A 1 83  ? 13.181 37.975 34.001 0.00 22.37  ? 86  TRP A HA   1 
ATOM   1294 H HB2  . TRP A 1 83  ? 12.497 39.740 31.882 0.00 21.23  ? 86  TRP A HB2  1 
ATOM   1295 H HB3  . TRP A 1 83  ? 13.185 40.223 33.230 0.00 21.23  ? 86  TRP A HB3  1 
ATOM   1296 H HD1  . TRP A 1 83  ? 15.175 37.564 32.801 0.00 23.36  ? 86  TRP A HD1  1 
ATOM   1297 H HE1  . TRP A 1 83  ? 17.185 37.895 31.438 0.00 23.39  ? 86  TRP A HE1  1 
ATOM   1298 H HE3  . TRP A 1 83  ? 13.847 41.649 30.453 0.00 26.19  ? 86  TRP A HE3  1 
ATOM   1299 H HZ2  . TRP A 1 83  ? 18.060 39.733 29.570 0.00 25.55  ? 86  TRP A HZ2  1 
ATOM   1300 H HZ3  . TRP A 1 83  ? 15.330 42.633 28.928 0.00 26.77  ? 86  TRP A HZ3  1 
ATOM   1301 H HH2  . TRP A 1 83  ? 17.397 41.646 28.486 0.00 26.23  ? 86  TRP A HH2  1 
ATOM   1302 N N    . LEU A 1 84  ? 10.091 38.455 33.316 1.00 19.03  ? 87  LEU A N    1 
ATOM   1303 C CA   . LEU A 1 84  ? 8.825  38.753 33.957 1.00 18.75  ? 87  LEU A CA   1 
ATOM   1304 C C    . LEU A 1 84  ? 8.638  37.968 35.241 1.00 19.88  ? 87  LEU A C    1 
ATOM   1305 O O    . LEU A 1 84  ? 8.039  38.486 36.217 1.00 23.27  ? 87  LEU A O    1 
ATOM   1306 C CB   . LEU A 1 84  ? 7.682  38.412 32.983 1.00 20.73  ? 87  LEU A CB   1 
ATOM   1307 C CG   . LEU A 1 84  ? 6.271  38.610 33.530 1.00 33.68  ? 87  LEU A CG   1 
ATOM   1308 C CD1  . LEU A 1 84  ? 6.021  40.086 33.796 1.00 36.64  ? 87  LEU A CD1  1 
ATOM   1309 C CD2  . LEU A 1 84  ? 5.241  38.036 32.539 1.00 41.55  ? 87  LEU A CD2  1 
ATOM   1310 H H    . LEU A 1 84  ? 10.033 38.184 32.502 0.00 22.85  ? 87  LEU A H    1 
ATOM   1311 H HA   . LEU A 1 84  ? 8.805  39.697 34.178 0.00 22.51  ? 87  LEU A HA   1 
ATOM   1312 H HB2  . LEU A 1 84  ? 7.771  38.977 32.200 0.00 24.89  ? 87  LEU A HB2  1 
ATOM   1313 H HB3  . LEU A 1 84  ? 7.766  37.479 32.730 0.00 24.89  ? 87  LEU A HB3  1 
ATOM   1314 H HG   . LEU A 1 84  ? 6.169  38.138 34.371 0.00 40.43  ? 87  LEU A HG   1 
ATOM   1315 H HD11 . LEU A 1 84  ? 5.089  40.211 34.032 0.00 43.98  ? 87  LEU A HD11 1 
ATOM   1316 H HD12 . LEU A 1 84  ? 6.589  40.376 34.526 0.00 43.98  ? 87  LEU A HD12 1 
ATOM   1317 H HD13 . LEU A 1 84  ? 6.230  40.590 32.994 0.00 43.98  ? 87  LEU A HD13 1 
ATOM   1318 H HD21 . LEU A 1 84  ? 4.349  38.190 32.886 0.00 49.87  ? 87  LEU A HD21 1 
ATOM   1319 H HD22 . LEU A 1 84  ? 5.345  38.481 31.683 0.00 49.87  ? 87  LEU A HD22 1 
ATOM   1320 H HD23 . LEU A 1 84  ? 5.397  37.084 32.437 0.00 49.87  ? 87  LEU A HD23 1 
ATOM   1321 N N    . PHE A 1 85  ? 9.129  36.730 35.287 1.00 20.56  ? 88  PHE A N    1 
ATOM   1322 C CA   . PHE A 1 85  ? 8.972  35.920 36.493 1.00 20.95  ? 88  PHE A CA   1 
ATOM   1323 C C    . PHE A 1 85  ? 10.217 35.912 37.360 1.00 22.36  ? 88  PHE A C    1 
ATOM   1324 O O    . PHE A 1 85  ? 10.104 35.861 38.580 1.00 24.35  ? 88  PHE A O    1 
ATOM   1325 C CB   . PHE A 1 85  ? 8.620  34.480 36.125 1.00 23.76  ? 88  PHE A CB   1 
ATOM   1326 C CG   . PHE A 1 85  ? 7.280  34.370 35.441 1.00 24.57  ? 88  PHE A CG   1 
ATOM   1327 C CD1  . PHE A 1 85  ? 6.120  34.479 36.198 1.00 31.47  ? 88  PHE A CD1  1 
ATOM   1328 C CD2  . PHE A 1 85  ? 7.207  34.207 34.100 1.00 27.02  ? 88  PHE A CD2  1 
ATOM   1329 C CE1  . PHE A 1 85  ? 4.879  34.396 35.578 1.00 40.00  ? 88  PHE A CE1  1 
ATOM   1330 C CE2  . PHE A 1 85  ? 5.958  34.130 33.464 1.00 33.85  ? 88  PHE A CE2  1 
ATOM   1331 C CZ   . PHE A 1 85  ? 4.808  34.224 34.218 1.00 34.71  ? 88  PHE A CZ   1 
ATOM   1332 H H    . PHE A 1 85  ? 9.550  36.345 34.643 0.00 24.69  ? 88  PHE A H    1 
ATOM   1333 H HA   . PHE A 1 85  ? 8.237  36.278 37.016 0.00 25.15  ? 88  PHE A HA   1 
ATOM   1334 H HB2  . PHE A 1 85  ? 9.296  34.133 35.522 0.00 28.53  ? 88  PHE A HB2  1 
ATOM   1335 H HB3  . PHE A 1 85  ? 8.591  33.945 36.934 0.00 28.53  ? 88  PHE A HB3  1 
ATOM   1336 H HD1  . PHE A 1 85  ? 6.174  34.608 37.118 0.00 37.78  ? 88  PHE A HD1  1 
ATOM   1337 H HD2  . PHE A 1 85  ? 7.987  34.145 33.598 0.00 32.44  ? 88  PHE A HD2  1 
ATOM   1338 H HE1  . PHE A 1 85  ? 4.100  34.456 36.082 0.00 48.01  ? 88  PHE A HE1  1 
ATOM   1339 H HE2  . PHE A 1 85  ? 5.907  34.017 32.543 0.00 40.63  ? 88  PHE A HE2  1 
ATOM   1340 H HZ   . PHE A 1 85  ? 3.977  34.171 33.802 0.00 41.67  ? 88  PHE A HZ   1 
ATOM   1341 N N    . THR A 1 86  ? 11.416 35.974 36.766 1.00 18.77  ? 89  THR A N    1 
ATOM   1342 C CA   . THR A 1 86  ? 12.601 35.826 37.619 1.00 17.95  ? 89  THR A CA   1 
ATOM   1343 C C    . THR A 1 86  ? 12.983 37.139 38.315 1.00 22.03  ? 89  THR A C    1 
ATOM   1344 O O    . THR A 1 86  ? 13.551 37.081 39.427 1.00 21.89  ? 89  THR A O    1 
ATOM   1345 C CB   . THR A 1 86  ? 13.807 35.294 36.821 1.00 19.02  ? 89  THR A CB   1 
ATOM   1346 O OG1  . THR A 1 86  ? 14.131 36.176 35.728 1.00 19.00  ? 89  THR A OG1  1 
ATOM   1347 C CG2  . THR A 1 86  ? 13.544 33.887 36.289 1.00 19.46  ? 89  THR A CG2  1 
ATOM   1348 H H    . THR A 1 86  ? 11.561 36.093 35.926 0.00 22.54  ? 89  THR A H    1 
ATOM   1349 H HA   . THR A 1 86  ? 12.391 35.167 38.299 0.00 21.56  ? 89  THR A HA   1 
ATOM   1350 H HB   . THR A 1 86  ? 14.569 35.249 37.418 0.00 22.84  ? 89  THR A HB   1 
ATOM   1351 H HG1  . THR A 1 86  ? 14.788 35.874 35.299 0.00 22.81  ? 89  THR A HG1  1 
ATOM   1352 H HG21 . THR A 1 86  ? 14.315 33.571 35.791 0.00 23.37  ? 89  THR A HG21 1 
ATOM   1353 H HG22 . THR A 1 86  ? 13.375 33.280 37.026 0.00 23.37  ? 89  THR A HG22 1 
ATOM   1354 H HG23 . THR A 1 86  ? 12.771 33.893 35.702 0.00 23.37  ? 89  THR A HG23 1 
ATOM   1355 N N    . THR A 1 87  ? 12.710 38.293 37.723 1.00 20.67  ? 90  THR A N    1 
ATOM   1356 C CA   . THR A 1 87  ? 13.155 39.521 38.401 1.00 19.34  ? 90  THR A CA   1 
ATOM   1357 C C    . THR A 1 87  ? 12.274 39.816 39.637 1.00 21.37  ? 90  THR A C    1 
ATOM   1358 O O    . THR A 1 87  ? 12.859 40.220 40.673 1.00 20.72  ? 90  THR A O    1 
ATOM   1359 C CB   . THR A 1 87  ? 13.234 40.751 37.487 1.00 19.15  ? 90  THR A CB   1 
ATOM   1360 O OG1  . THR A 1 87  ? 11.987 40.962 36.749 1.00 21.01  ? 90  THR A OG1  1 
ATOM   1361 C CG2  . THR A 1 87  ? 14.352 40.542 36.456 1.00 20.72  ? 90  THR A CG2  1 
ATOM   1362 H H    . THR A 1 87  ? 12.296 38.393 36.976 0.00 24.81  ? 90  THR A H    1 
ATOM   1363 H HA   . THR A 1 87  ? 14.064 39.353 38.696 0.00 23.21  ? 90  THR A HA   1 
ATOM   1364 H HB   . THR A 1 87  ? 13.404 41.531 38.038 0.00 22.99  ? 90  THR A HB   1 
ATOM   1365 H HG1  . THR A 1 87  ? 11.416 41.322 37.248 0.00 25.22  ? 90  THR A HG1  1 
ATOM   1366 H HG21 . THR A 1 87  ? 14.449 41.336 35.906 0.00 24.88  ? 90  THR A HG21 1 
ATOM   1367 H HG22 . THR A 1 87  ? 15.192 40.368 36.909 0.00 24.88  ? 90  THR A HG22 1 
ATOM   1368 H HG23 . THR A 1 87  ? 14.140 39.787 35.885 0.00 24.88  ? 90  THR A HG23 1 
ATOM   1369 N N    . PRO A 1 88  ? 10.983 39.541 39.670 1.00 20.28  ? 91  PRO A N    1 
ATOM   1370 C CA   . PRO A 1 88  ? 10.260 39.724 40.946 1.00 22.63  ? 91  PRO A CA   1 
ATOM   1371 C C    . PRO A 1 88  ? 10.664 38.696 41.988 1.00 23.18  ? 91  PRO A C    1 
ATOM   1372 O O    . PRO A 1 88  ? 10.673 39.005 43.187 1.00 25.89  ? 91  PRO A O    1 
ATOM   1373 C CB   . PRO A 1 88  ? 8.776  39.609 40.567 1.00 28.90  ? 91  PRO A CB   1 
ATOM   1374 C CG   . PRO A 1 88  ? 8.738  39.002 39.208 1.00 34.07  ? 91  PRO A CG   1 
ATOM   1375 C CD   . PRO A 1 88  ? 10.040 39.271 38.534 1.00 22.68  ? 91  PRO A CD   1 
ATOM   1376 H HA   . PRO A 1 88  ? 10.410 40.619 41.288 0.00 27.17  ? 91  PRO A HA   1 
ATOM   1377 H HB2  . PRO A 1 88  ? 8.320  39.042 41.208 0.00 34.69  ? 91  PRO A HB2  1 
ATOM   1378 H HB3  . PRO A 1 88  ? 8.374  40.492 40.559 0.00 34.69  ? 91  PRO A HB3  1 
ATOM   1379 H HG2  . PRO A 1 88  ? 8.596  38.046 39.292 0.00 40.89  ? 91  PRO A HG2  1 
ATOM   1380 H HG3  . PRO A 1 88  ? 8.012  39.401 38.703 0.00 40.89  ? 91  PRO A HG3  1 
ATOM   1381 H HD2  . PRO A 1 88  ? 10.330 38.497 38.025 0.00 27.22  ? 91  PRO A HD2  1 
ATOM   1382 H HD3  . PRO A 1 88  ? 9.973  40.044 37.953 0.00 27.22  ? 91  PRO A HD3  1 
ATOM   1383 N N    . LEU A 1 89  ? 11.035 37.472 41.566 1.00 22.55  ? 92  LEU A N    1 
ATOM   1384 C CA   . LEU A 1 89  ? 11.524 36.495 42.531 1.00 20.00  ? 92  LEU A CA   1 
ATOM   1385 C C    . LEU A 1 89  ? 12.820 36.952 43.164 1.00 23.31  ? 92  LEU A C    1 
ATOM   1386 O O    . LEU A 1 89  ? 13.046 36.774 44.375 1.00 25.89  ? 92  LEU A O    1 
ATOM   1387 C CB   . LEU A 1 89  ? 11.737 35.141 41.817 1.00 22.49  ? 92  LEU A CB   1 
ATOM   1388 C CG   . LEU A 1 89  ? 10.426 34.381 41.534 1.00 23.84  ? 92  LEU A CG   1 
ATOM   1389 C CD1  . LEU A 1 89  ? 10.733 33.108 40.752 1.00 24.44  ? 92  LEU A CD1  1 
ATOM   1390 C CD2  . LEU A 1 89  ? 9.702  34.015 42.836 1.00 27.67  ? 92  LEU A CD2  1 
ATOM   1391 H H    . LEU A 1 89  ? 11.012 37.200 40.751 0.00 27.08  ? 92  LEU A H    1 
ATOM   1392 H HA   . LEU A 1 89  ? 10.865 36.383 43.235 0.00 24.01  ? 92  LEU A HA   1 
ATOM   1393 H HB2  . LEU A 1 89  ? 12.176 35.302 40.968 0.00 27.00  ? 92  LEU A HB2  1 
ATOM   1394 H HB3  . LEU A 1 89  ? 12.293 34.577 42.377 0.00 27.00  ? 92  LEU A HB3  1 
ATOM   1395 H HG   . LEU A 1 89  ? 9.840  34.953 41.015 0.00 28.62  ? 92  LEU A HG   1 
ATOM   1396 H HD11 . LEU A 1 89  ? 9.900  32.662 40.533 0.00 29.33  ? 92  LEU A HD11 1 
ATOM   1397 H HD12 . LEU A 1 89  ? 11.206 33.343 39.938 0.00 29.33  ? 92  LEU A HD12 1 
ATOM   1398 H HD13 . LEU A 1 89  ? 11.285 32.526 41.299 0.00 29.33  ? 92  LEU A HD13 1 
ATOM   1399 H HD21 . LEU A 1 89  ? 8.999  33.376 42.638 0.00 33.21  ? 92  LEU A HD21 1 
ATOM   1400 H HD22 . LEU A 1 89  ? 10.340 33.623 43.453 0.00 33.21  ? 92  LEU A HD22 1 
ATOM   1401 H HD23 . LEU A 1 89  ? 9.320  34.818 43.222 0.00 33.21  ? 92  LEU A HD23 1 
ATOM   1402 N N    . LEU A 1 90  ? 13.717 37.563 42.370 1.00 21.28  ? 93  LEU A N    1 
ATOM   1403 C CA   . LEU A 1 90  ? 14.973 38.041 42.991 1.00 18.79  ? 93  LEU A CA   1 
ATOM   1404 C C    . LEU A 1 90  ? 14.692 39.187 43.962 1.00 19.66  ? 93  LEU A C    1 
ATOM   1405 O O    . LEU A 1 90  ? 15.350 39.283 45.014 1.00 24.05  ? 93  LEU A O    1 
ATOM   1406 C CB   . LEU A 1 90  ? 15.934 38.508 41.894 1.00 20.81  ? 93  LEU A CB   1 
ATOM   1407 C CG   . LEU A 1 90  ? 16.513 37.343 41.077 1.00 23.66  ? 93  LEU A CG   1 
ATOM   1408 C CD1  . LEU A 1 90  ? 17.122 37.885 39.768 1.00 23.29  ? 93  LEU A CD1  1 
ATOM   1409 C CD2  . LEU A 1 90  ? 17.566 36.597 41.891 1.00 23.64  ? 93  LEU A CD2  1 
ATOM   1410 H H    . LEU A 1 90  ? 13.633 37.705 41.526 0.00 25.55  ? 93  LEU A H    1 
ATOM   1411 H HA   . LEU A 1 90  ? 15.388 37.315 43.482 0.00 22.56  ? 93  LEU A HA   1 
ATOM   1412 H HB2  . LEU A 1 90  ? 15.458 39.095 41.286 0.00 24.98  ? 93  LEU A HB2  1 
ATOM   1413 H HB3  . LEU A 1 90  ? 16.673 38.985 42.304 0.00 24.98  ? 93  LEU A HB3  1 
ATOM   1414 H HG   . LEU A 1 90  ? 15.808 36.714 40.856 0.00 28.40  ? 93  LEU A HG   1 
ATOM   1415 H HD11 . LEU A 1 90  ? 17.479 37.144 39.254 0.00 27.96  ? 93  LEU A HD11 1 
ATOM   1416 H HD12 . LEU A 1 90  ? 16.429 38.335 39.260 0.00 27.96  ? 93  LEU A HD12 1 
ATOM   1417 H HD13 . LEU A 1 90  ? 17.831 38.510 39.984 0.00 27.96  ? 93  LEU A HD13 1 
ATOM   1418 H HD21 . LEU A 1 90  ? 17.989 35.932 41.325 0.00 28.38  ? 93  LEU A HD21 1 
ATOM   1419 H HD22 . LEU A 1 90  ? 18.228 37.232 42.207 0.00 28.38  ? 93  LEU A HD22 1 
ATOM   1420 H HD23 . LEU A 1 90  ? 17.135 36.165 42.645 0.00 28.38  ? 93  LEU A HD23 1 
ATOM   1421 N N    . LEU A 1 91  ? 13.749 40.075 43.621 1.00 22.00  ? 94  LEU A N    1 
ATOM   1422 C CA   . LEU A 1 91  ? 13.395 41.148 44.548 1.00 21.27  ? 94  LEU A CA   1 
ATOM   1423 C C    . LEU A 1 91  ? 12.730 40.582 45.821 1.00 22.73  ? 94  LEU A C    1 
ATOM   1424 O O    . LEU A 1 91  ? 12.935 41.105 46.904 1.00 25.20  ? 94  LEU A O    1 
ATOM   1425 C CB   . LEU A 1 91  ? 12.427 42.149 43.871 1.00 20.87  ? 94  LEU A CB   1 
ATOM   1426 C CG   . LEU A 1 91  ? 13.092 42.968 42.772 1.00 24.55  ? 94  LEU A CG   1 
ATOM   1427 C CD1  . LEU A 1 91  ? 12.032 43.896 42.100 1.00 27.90  ? 94  LEU A CD1  1 
ATOM   1428 C CD2  . LEU A 1 91  ? 14.213 43.823 43.312 1.00 26.70  ? 94  LEU A CD2  1 
ATOM   1429 H H    . LEU A 1 91  ? 13.314 40.076 42.879 0.00 26.41  ? 94  LEU A H    1 
ATOM   1430 H HA   . LEU A 1 91  ? 14.206 41.620 44.793 0.00 25.53  ? 94  LEU A HA   1 
ATOM   1431 H HB2  . LEU A 1 91  ? 11.692 41.655 43.475 0.00 25.05  ? 94  LEU A HB2  1 
ATOM   1432 H HB3  . LEU A 1 91  ? 12.090 42.763 44.542 0.00 25.05  ? 94  LEU A HB3  1 
ATOM   1433 H HG   . LEU A 1 91  ? 13.467 42.355 42.121 0.00 29.48  ? 94  LEU A HG   1 
ATOM   1434 H HD11 . LEU A 1 91  ? 12.457 44.396 41.386 0.00 33.49  ? 94  LEU A HD11 1 
ATOM   1435 H HD12 . LEU A 1 91  ? 11.316 43.349 41.740 0.00 33.49  ? 94  LEU A HD12 1 
ATOM   1436 H HD13 . LEU A 1 91  ? 11.679 44.507 42.766 0.00 33.49  ? 94  LEU A HD13 1 
ATOM   1437 H HD21 . LEU A 1 91  ? 14.472 44.468 42.635 0.00 32.05  ? 94  LEU A HD21 1 
ATOM   1438 H HD22 . LEU A 1 91  ? 13.904 44.284 44.107 0.00 32.05  ? 94  LEU A HD22 1 
ATOM   1439 H HD23 . LEU A 1 91  ? 14.967 43.254 43.532 0.00 32.05  ? 94  LEU A HD23 1 
ATOM   1440 N N    A LEU A 1 92  ? 11.978 39.496 45.696 0.61 23.02  ? 95  LEU A N    1 
ATOM   1441 N N    B LEU A 1 92  ? 11.953 39.507 45.700 0.39 23.14  ? 95  LEU A N    1 
ATOM   1442 C CA   A LEU A 1 92  ? 11.375 38.869 46.866 0.61 26.17  ? 95  LEU A CA   1 
ATOM   1443 C CA   B LEU A 1 92  ? 11.385 38.890 46.894 0.39 26.27  ? 95  LEU A CA   1 
ATOM   1444 C C    A LEU A 1 92  ? 12.438 38.303 47.796 0.61 27.00  ? 95  LEU A C    1 
ATOM   1445 C C    B LEU A 1 92  ? 12.480 38.366 47.808 0.39 27.13  ? 95  LEU A C    1 
ATOM   1446 O O    A LEU A 1 92  ? 12.303 38.383 49.027 0.61 28.04  ? 95  LEU A O    1 
ATOM   1447 O O    B LEU A 1 92  ? 12.408 38.532 49.033 0.39 28.46  ? 95  LEU A O    1 
ATOM   1448 C CB   A LEU A 1 92  ? 10.396 37.793 46.415 0.61 24.14  ? 95  LEU A CB   1 
ATOM   1449 C CB   B LEU A 1 92  ? 10.432 37.760 46.526 0.39 24.46  ? 95  LEU A CB   1 
ATOM   1450 C CG   A LEU A 1 92  ? 9.505  37.177 47.474 0.61 23.31  ? 95  LEU A CG   1 
ATOM   1451 C CG   B LEU A 1 92  ? 9.046  38.123 46.010 0.39 31.67  ? 95  LEU A CG   1 
ATOM   1452 C CD1  A LEU A 1 92  ? 8.579  38.226 48.095 0.61 34.40  ? 95  LEU A CD1  1 
ATOM   1453 C CD1  B LEU A 1 92  ? 8.301  36.824 45.747 0.39 40.64  ? 95  LEU A CD1  1 
ATOM   1454 C CD2  A LEU A 1 92  ? 8.722  36.036 46.882 0.61 25.73  ? 95  LEU A CD2  1 
ATOM   1455 C CD2  B LEU A 1 92  ? 8.269  38.992 46.984 0.39 33.56  ? 95  LEU A CD2  1 
ATOM   1456 H H    A LEU A 1 92  ? 11.802 39.103 44.952 0.61 27.64  ? 95  LEU A H    1 
ATOM   1457 H H    B LEU A 1 92  ? 11.745 39.125 44.957 0.39 27.78  ? 95  LEU A H    1 
ATOM   1458 H HA   A LEU A 1 92  ? 10.876 39.531 47.370 0.61 31.41  ? 95  LEU A HA   1 
ATOM   1459 H HA   B LEU A 1 92  ? 10.873 39.565 47.367 0.39 31.54  ? 95  LEU A HA   1 
ATOM   1460 H HB2  A LEU A 1 92  ? 9.811  38.184 45.747 0.61 28.99  ? 95  LEU A HB2  1 
ATOM   1461 H HB2  B LEU A 1 92  ? 10.857 37.232 45.832 0.39 29.36  ? 95  LEU A HB2  1 
ATOM   1462 H HB3  A LEU A 1 92  ? 10.909 37.069 46.023 0.61 28.99  ? 95  LEU A HB3  1 
ATOM   1463 H HB3  B LEU A 1 92  ? 10.299 37.218 47.320 0.39 29.36  ? 95  LEU A HB3  1 
ATOM   1464 H HG   A LEU A 1 92  ? 10.055 36.828 48.192 0.61 27.99  ? 95  LEU A HG   1 
ATOM   1465 H HG   B LEU A 1 92  ? 9.127  38.646 45.197 0.39 38.02  ? 95  LEU A HG   1 
ATOM   1466 H HD11 A LEU A 1 92  ? 7.957  37.783 48.693 0.61 41.29  ? 95  LEU A HD11 1 
ATOM   1467 H HD11 B LEU A 1 92  ? 7.347  37.002 45.745 0.39 48.78  ? 95  LEU A HD11 1 
ATOM   1468 H HD12 A LEU A 1 92  ? 9.114  38.867 48.588 0.61 41.29  ? 95  LEU A HD12 1 
ATOM   1469 H HD12 B LEU A 1 92  ? 8.573  36.473 44.884 0.39 48.78  ? 95  LEU A HD12 1 
ATOM   1470 H HD13 A LEU A 1 92  ? 8.092  38.677 47.387 0.61 41.29  ? 95  LEU A HD13 1 
ATOM   1471 H HD13 B LEU A 1 92  ? 8.518  36.188 46.446 0.39 48.78  ? 95  LEU A HD13 1 
ATOM   1472 H HD21 A LEU A 1 92  ? 8.202  35.613 47.583 0.61 30.89  ? 95  LEU A HD21 1 
ATOM   1473 H HD21 B LEU A 1 92  ? 7.397  39.186 46.607 0.39 40.28  ? 95  LEU A HD21 1 
ATOM   1474 H HD22 A LEU A 1 92  ? 8.131  36.381 46.195 0.61 30.89  ? 95  LEU A HD22 1 
ATOM   1475 H HD22 B LEU A 1 92  ? 8.170  38.515 47.822 0.39 40.28  ? 95  LEU A HD22 1 
ATOM   1476 H HD23 A LEU A 1 92  ? 9.340  35.396 46.496 0.61 30.89  ? 95  LEU A HD23 1 
ATOM   1477 H HD23 B LEU A 1 92  ? 8.758  39.818 47.129 0.39 40.28  ? 95  LEU A HD23 1 
ATOM   1478 N N    . ASP A 1 93  ? 13.501 37.724 47.233 1.00 22.79  ? 96  ASP A N    1 
ATOM   1479 C CA   . ASP A 1 93  ? 14.615 37.251 48.058 1.00 24.61  ? 96  ASP A CA   1 
ATOM   1480 C C    . ASP A 1 93  ? 15.156 38.405 48.912 1.00 28.39  ? 96  ASP A C    1 
ATOM   1481 O O    . ASP A 1 93  ? 15.427 38.242 50.104 1.00 30.20  ? 96  ASP A O    1 
ATOM   1482 C CB   . ASP A 1 93  ? 15.752 36.725 47.178 1.00 28.83  ? 96  ASP A CB   1 
ATOM   1483 C CG   . ASP A 1 93  ? 15.789 35.223 47.073 1.00 24.76  ? 96  ASP A CG   1 
ATOM   1484 O OD1  . ASP A 1 93  ? 15.200 34.506 47.906 1.00 24.99  ? 96  ASP A OD1  1 
ATOM   1485 O OD2  . ASP A 1 93  ? 16.491 34.733 46.167 1.00 28.09  ? 96  ASP A OD2  1 
ATOM   1486 H H    . ASP A 1 93  ? 13.598 37.596 46.388 0.00 27.36  ? 96  ASP A H    1 
ATOM   1487 H HA   . ASP A 1 93  ? 14.297 36.528 48.621 0.00 29.54  ? 96  ASP A HA   1 
ATOM   1488 H HB2  . ASP A 1 93  ? 15.645 37.082 46.283 0.00 34.61  ? 96  ASP A HB2  1 
ATOM   1489 H HB3  . ASP A 1 93  ? 16.598 37.017 47.553 0.00 34.61  ? 96  ASP A HB3  1 
ATOM   1490 N N    . LEU A 1 94  ? 15.374 39.571 48.288 1.00 25.02  ? 97  LEU A N    1 
ATOM   1491 C CA   . LEU A 1 94  ? 15.884 40.711 49.052 1.00 25.40  ? 97  LEU A CA   1 
ATOM   1492 C C    . LEU A 1 94  ? 14.871 41.217 50.065 1.00 28.36  ? 97  LEU A C    1 
ATOM   1493 O O    . LEU A 1 94  ? 15.238 41.560 51.205 1.00 29.99  ? 97  LEU A O    1 
ATOM   1494 C CB   . LEU A 1 94  ? 16.277 41.870 48.113 1.00 25.14  ? 97  LEU A CB   1 
ATOM   1495 C CG   . LEU A 1 94  ? 17.416 41.544 47.140 1.00 29.17  ? 97  LEU A CG   1 
ATOM   1496 C CD1  . LEU A 1 94  ? 17.512 42.639 46.068 1.00 33.37  ? 97  LEU A CD1  1 
ATOM   1497 C CD2  . LEU A 1 94  ? 18.736 41.395 47.898 1.00 36.59  ? 97  LEU A CD2  1 
ATOM   1498 H H    . LEU A 1 94  ? 15.240 39.721 47.452 0.00 30.04  ? 97  LEU A H    1 
ATOM   1499 H HA   . LEU A 1 94  ? 16.676 40.408 49.525 0.00 30.49  ? 97  LEU A HA   1 
ATOM   1500 H HB2  . LEU A 1 94  ? 15.501 42.114 47.584 0.00 30.18  ? 97  LEU A HB2  1 
ATOM   1501 H HB3  . LEU A 1 94  ? 16.560 42.623 48.655 0.00 30.18  ? 97  LEU A HB3  1 
ATOM   1502 H HG   . LEU A 1 94  ? 17.239 40.700 46.695 0.00 35.02  ? 97  LEU A HG   1 
ATOM   1503 H HD11 . LEU A 1 94  ? 18.221 42.412 45.447 0.00 40.06  ? 97  LEU A HD11 1 
ATOM   1504 H HD12 . LEU A 1 94  ? 16.666 42.695 45.598 0.00 40.06  ? 97  LEU A HD12 1 
ATOM   1505 H HD13 . LEU A 1 94  ? 17.708 43.486 46.499 0.00 40.06  ? 97  LEU A HD13 1 
ATOM   1506 H HD21 . LEU A 1 94  ? 19.463 41.339 47.258 0.00 43.92  ? 97  LEU A HD21 1 
ATOM   1507 H HD22 . LEU A 1 94  ? 18.859 42.167 48.472 0.00 43.92  ? 97  LEU A HD22 1 
ATOM   1508 H HD23 . LEU A 1 94  ? 18.703 40.587 48.433 0.00 43.92  ? 97  LEU A HD23 1 
ATOM   1509 N N    . ALA A 1 95  ? 13.606 41.296 49.669 1.00 27.06  ? 98  ALA A N    1 
ATOM   1510 C CA   . ALA A 1 95  ? 12.587 41.836 50.573 1.00 28.91  ? 98  ALA A CA   1 
ATOM   1511 C C    . ALA A 1 95  ? 12.376 40.932 51.789 1.00 31.41  ? 98  ALA A C    1 
ATOM   1512 O O    . ALA A 1 95  ? 12.183 41.418 52.906 1.00 32.16  ? 98  ALA A O    1 
ATOM   1513 C CB   . ALA A 1 95  ? 11.274 42.018 49.806 1.00 27.30  ? 98  ALA A CB   1 
ATOM   1514 H H    . ALA A 1 95  ? 13.313 41.050 48.899 0.00 32.49  ? 98  ALA A H    1 
ATOM   1515 H HA   . ALA A 1 95  ? 12.879 42.702 50.899 0.00 34.71  ? 98  ALA A HA   1 
ATOM   1516 H HB1  . ALA A 1 95  ? 10.603 42.376 50.409 0.00 32.78  ? 98  ALA A HB1  1 
ATOM   1517 H HB2  . ALA A 1 95  ? 11.420 42.633 49.071 0.00 32.78  ? 98  ALA A HB2  1 
ATOM   1518 H HB3  . ALA A 1 95  ? 10.985 41.157 49.465 0.00 32.78  ? 98  ALA A HB3  1 
ATOM   1519 N N    . LEU A 1 96  ? 12.398 39.612 51.587 1.00 27.41  ? 99  LEU A N    1 
ATOM   1520 C CA   . LEU A 1 96  ? 12.214 38.712 52.722 1.00 32.71  ? 99  LEU A CA   1 
ATOM   1521 C C    . LEU A 1 96  ? 13.409 38.769 53.658 1.00 34.70  ? 99  LEU A C    1 
ATOM   1522 O O    . LEU A 1 96  ? 13.270 38.593 54.874 1.00 36.10  ? 99  LEU A O    1 
ATOM   1523 C CB   . LEU A 1 96  ? 11.996 37.285 52.209 1.00 36.63  ? 99  LEU A CB   1 
ATOM   1524 C CG   . LEU A 1 96  ? 10.657 37.051 51.481 1.00 43.94  ? 99  LEU A CG   1 
ATOM   1525 C CD1  . LEU A 1 96  ? 10.540 35.573 51.104 1.00 42.64  ? 99  LEU A CD1  1 
ATOM   1526 C CD2  . LEU A 1 96  ? 9.447  37.478 52.308 1.00 53.26  ? 99  LEU A CD2  1 
ATOM   1527 H H    . LEU A 1 96  ? 12.513 39.226 50.827 0.00 32.91  ? 99  LEU A H    1 
ATOM   1528 H HA   . LEU A 1 96  ? 11.426 38.972 53.225 0.00 39.26  ? 99  LEU A HA   1 
ATOM   1529 H HB2  . LEU A 1 96  ? 12.708 37.072 51.585 0.00 43.96  ? 99  LEU A HB2  1 
ATOM   1530 H HB3  . LEU A 1 96  ? 12.026 36.679 52.966 0.00 43.96  ? 99  LEU A HB3  1 
ATOM   1531 H HG   . LEU A 1 96  ? 10.649 37.603 50.683 0.00 52.74  ? 99  LEU A HG   1 
ATOM   1532 H HD11 . LEU A 1 96  ? 9.691  35.427 50.659 0.00 51.18  ? 99  LEU A HD11 1 
ATOM   1533 H HD12 . LEU A 1 96  ? 11.270 35.340 50.510 0.00 51.18  ? 99  LEU A HD12 1 
ATOM   1534 H HD13 . LEU A 1 96  ? 10.587 35.037 51.911 0.00 51.18  ? 99  LEU A HD13 1 
ATOM   1535 H HD21 . LEU A 1 96  ? 8.638  37.220 51.839 0.00 63.92  ? 99  LEU A HD21 1 
ATOM   1536 H HD22 . LEU A 1 96  ? 9.483  37.038 53.171 0.00 63.92  ? 99  LEU A HD22 1 
ATOM   1537 H HD23 . LEU A 1 96  ? 9.468  38.441 52.426 0.00 63.92  ? 99  LEU A HD23 1 
ATOM   1538 N N    . LEU A 1 97  ? 14.594 39.029 53.112 1.00 30.45  ? 100 LEU A N    1 
ATOM   1539 C CA   . LEU A 1 97  ? 15.794 39.095 53.938 1.00 33.93  ? 100 LEU A CA   1 
ATOM   1540 C C    . LEU A 1 97  ? 15.680 40.206 54.973 1.00 36.76  ? 100 LEU A C    1 
ATOM   1541 O O    . LEU A 1 97  ? 16.110 40.041 56.126 1.00 40.87  ? 100 LEU A O    1 
ATOM   1542 C CB   . LEU A 1 97  ? 17.007 39.313 53.039 1.00 35.77  ? 100 LEU A CB   1 
ATOM   1543 C CG   . LEU A 1 97  ? 18.399 39.036 53.570 1.00 47.27  ? 100 LEU A CG   1 
ATOM   1544 C CD1  . LEU A 1 97  ? 18.535 37.586 53.996 1.00 43.06  ? 100 LEU A CD1  1 
ATOM   1545 C CD2  . LEU A 1 97  ? 19.416 39.384 52.496 1.00 41.08  ? 100 LEU A CD2  1 
ATOM   1546 H H    . LEU A 1 97  ? 14.729 39.171 52.275 0.00 36.55  ? 100 LEU A H    1 
ATOM   1547 H HA   . LEU A 1 97  ? 15.911 38.257 54.413 0.00 40.73  ? 100 LEU A HA   1 
ATOM   1548 H HB2  . LEU A 1 97  ? 16.896 38.743 52.262 0.00 42.94  ? 100 LEU A HB2  1 
ATOM   1549 H HB3  . LEU A 1 97  ? 17.001 40.245 52.770 0.00 42.94  ? 100 LEU A HB3  1 
ATOM   1550 H HG   . LEU A 1 97  ? 18.568 39.581 54.354 0.00 56.73  ? 100 LEU A HG   1 
ATOM   1551 H HD11 . LEU A 1 97  ? 19.469 37.396 54.176 0.00 51.68  ? 100 LEU A HD11 1 
ATOM   1552 H HD12 . LEU A 1 97  ? 18.008 37.441 54.797 0.00 51.68  ? 100 LEU A HD12 1 
ATOM   1553 H HD13 . LEU A 1 97  ? 18.213 37.015 53.281 0.00 51.68  ? 100 LEU A HD13 1 
ATOM   1554 H HD21 . LEU A 1 97  ? 20.309 39.242 52.849 0.00 49.31  ? 100 LEU A HD21 1 
ATOM   1555 H HD22 . LEU A 1 97  ? 19.270 38.813 51.726 0.00 49.31  ? 100 LEU A HD22 1 
ATOM   1556 H HD23 . LEU A 1 97  ? 19.304 40.314 52.245 0.00 49.31  ? 100 LEU A HD23 1 
ATOM   1557 N N    . VAL A 1 98  ? 15.104 41.339 54.588 1.00 37.46  ? 101 VAL A N    1 
ATOM   1558 C CA   . VAL A 1 98  ? 14.987 42.498 55.485 1.00 35.91  ? 101 VAL A CA   1 
ATOM   1559 C C    . VAL A 1 98  ? 13.613 42.594 56.138 1.00 38.80  ? 101 VAL A C    1 
ATOM   1560 O O    . VAL A 1 98  ? 13.325 43.584 56.820 1.00 42.32  ? 101 VAL A O    1 
ATOM   1561 C CB   . VAL A 1 98  ? 15.307 43.812 54.726 1.00 39.59  ? 101 VAL A CB   1 
ATOM   1562 C CG1  . VAL A 1 98  ? 16.672 43.717 54.058 1.00 50.17  ? 101 VAL A CG1  1 
ATOM   1563 C CG2  . VAL A 1 98  ? 14.241 44.122 53.701 1.00 38.36  ? 101 VAL A CG2  1 
ATOM   1564 H H    . VAL A 1 98  ? 14.768 41.469 53.807 0.00 44.97  ? 101 VAL A H    1 
ATOM   1565 H HA   . VAL A 1 98  ? 15.635 42.381 56.197 0.00 43.11  ? 101 VAL A HA   1 
ATOM   1566 H HB   . VAL A 1 98  ? 15.323 44.540 55.366 0.00 47.53  ? 101 VAL A HB   1 
ATOM   1567 H HG11 . VAL A 1 98  ? 16.871 44.563 53.626 0.00 60.21  ? 101 VAL A HG11 1 
ATOM   1568 H HG12 . VAL A 1 98  ? 17.341 43.525 54.733 0.00 60.21  ? 101 VAL A HG12 1 
ATOM   1569 H HG13 . VAL A 1 98  ? 16.652 43.006 53.399 0.00 60.21  ? 101 VAL A HG13 1 
ATOM   1570 H HG21 . VAL A 1 98  ? 14.534 44.871 53.158 0.00 46.05  ? 101 VAL A HG21 1 
ATOM   1571 H HG22 . VAL A 1 98  ? 14.105 43.341 53.141 0.00 46.05  ? 101 VAL A HG22 1 
ATOM   1572 H HG23 . VAL A 1 98  ? 13.417 44.348 54.160 0.00 46.05  ? 101 VAL A HG23 1 
ATOM   1573 N N    . ASP A 1 99  ? 12.751 41.600 55.948 1.00 34.90  ? 102 ASP A N    1 
ATOM   1574 C CA   . ASP A 1 99  ? 11.411 41.611 56.537 1.00 36.56  ? 102 ASP A CA   1 
ATOM   1575 C C    . ASP A 1 99  ? 10.634 42.854 56.097 1.00 42.07  ? 102 ASP A C    1 
ATOM   1576 O O    . ASP A 1 99  ? 10.010 43.550 56.915 1.00 38.59  ? 102 ASP A O    1 
ATOM   1577 C CB   . ASP A 1 99  ? 11.479 41.528 58.058 1.00 45.37  ? 102 ASP A CB   1 
ATOM   1578 C CG   . ASP A 1 99  ? 10.171 41.079 58.676 1.00 61.82  ? 102 ASP A CG   1 
ATOM   1579 O OD1  . ASP A 1 99  ? 9.410  40.362 57.993 1.00 61.52  ? 102 ASP A OD1  1 
ATOM   1580 O OD2  . ASP A 1 99  ? 9.903  41.444 59.839 1.00 69.93  ? 102 ASP A OD2  1 
ATOM   1581 H H    . ASP A 1 99  ? 12.919 40.899 55.479 0.00 41.89  ? 102 ASP A H    1 
ATOM   1582 H HA   . ASP A 1 99  ? 10.930 40.832 56.215 0.00 43.88  ? 102 ASP A HA   1 
ATOM   1583 H HB2  . ASP A 1 99  ? 12.165 40.890 58.310 0.00 54.46  ? 102 ASP A HB2  1 
ATOM   1584 H HB3  . ASP A 1 99  ? 11.695 42.404 58.414 0.00 54.46  ? 102 ASP A HB3  1 
ATOM   1585 N N    . ALA A 1 100 ? 10.672 43.128 54.805 1.00 33.40  ? 103 ALA A N    1 
ATOM   1586 C CA   . ALA A 1 100 ? 9.978  44.290 54.248 1.00 31.78  ? 103 ALA A CA   1 
ATOM   1587 C C    . ALA A 1 100 ? 8.479  44.193 54.493 1.00 36.30  ? 103 ALA A C    1 
ATOM   1588 O O    . ALA A 1 100 ? 7.879  43.110 54.509 1.00 34.95  ? 103 ALA A O    1 
ATOM   1589 C CB   . ALA A 1 100 ? 10.260 44.399 52.741 1.00 33.59  ? 103 ALA A CB   1 
ATOM   1590 H H    . ALA A 1 100 ? 11.093 42.658 54.220 0.00 40.09  ? 103 ALA A H    1 
ATOM   1591 H HA   . ALA A 1 100 ? 10.300 45.097 54.681 0.00 38.15  ? 103 ALA A HA   1 
ATOM   1592 H HB1  . ALA A 1 100 ? 9.795  45.174 52.387 0.00 40.32  ? 103 ALA A HB1  1 
ATOM   1593 H HB2  . ALA A 1 100 ? 11.215 44.495 52.604 0.00 40.32  ? 103 ALA A HB2  1 
ATOM   1594 H HB3  . ALA A 1 100 ? 9.943  43.594 52.301 0.00 40.32  ? 103 ALA A HB3  1 
ATOM   1595 N N    . ASP A 1 101 ? 7.857  45.352 54.693 1.00 37.14  ? 104 ASP A N    1 
ATOM   1596 C CA   . ASP A 1 101 ? 6.419  45.405 54.859 1.00 40.20  ? 104 ASP A CA   1 
ATOM   1597 C C    . ASP A 1 101 ? 5.708  45.078 53.544 1.00 36.24  ? 104 ASP A C    1 
ATOM   1598 O O    . ASP A 1 101 ? 6.251  45.234 52.442 1.00 31.17  ? 104 ASP A O    1 
ATOM   1599 C CB   . ASP A 1 101 ? 6.001  46.796 55.344 1.00 44.79  ? 104 ASP A CB   1 
ATOM   1600 C CG   . ASP A 1 101 ? 6.352  47.882 54.349 1.00 41.92  ? 104 ASP A CG   1 
ATOM   1601 O OD1  . ASP A 1 101 ? 5.466  48.274 53.553 1.00 51.88  ? 104 ASP A OD1  1 
ATOM   1602 O OD2  . ASP A 1 101 ? 7.513  48.347 54.358 1.00 58.95  ? 104 ASP A OD2  1 
ATOM   1603 H H    . ASP A 1 101 ? 8.249  46.116 54.736 0.00 44.58  ? 104 ASP A H    1 
ATOM   1604 H HA   . ASP A 1 101 ? 6.144  44.751 55.520 0.00 48.25  ? 104 ASP A HA   1 
ATOM   1605 H HB2  . ASP A 1 101 ? 5.040  46.810 55.479 1.00 53.76  ? 104 ASP A HB2  1 
ATOM   1606 H HB3  . ASP A 1 101 ? 6.456  46.992 56.178 1.00 53.76  ? 104 ASP A HB3  1 
ATOM   1607 N N    . GLN A 1 102 ? 4.452  44.651 53.669 1.00 35.38  ? 105 GLN A N    1 
ATOM   1608 C CA   . GLN A 1 102 ? 3.720  44.144 52.523 1.00 35.44  ? 105 GLN A CA   1 
ATOM   1609 C C    . GLN A 1 102 ? 3.503  45.224 51.471 1.00 35.06  ? 105 GLN A C    1 
ATOM   1610 O O    . GLN A 1 102 ? 3.526  44.930 50.271 1.00 31.68  ? 105 GLN A O    1 
ATOM   1611 C CB   . GLN A 1 102 ? 2.369  43.582 52.978 1.00 50.85  ? 105 GLN A CB   1 
ATOM   1612 C CG   . GLN A 1 102 ? 2.418  42.110 53.338 1.00 52.98  ? 105 GLN A CG   1 
ATOM   1613 C CD   . GLN A 1 102 ? 1.232  41.687 54.180 1.00 76.88  ? 105 GLN A CD   1 
ATOM   1614 O OE1  . GLN A 1 102 ? 0.131  42.217 54.029 1.00 75.54  ? 105 GLN A OE1  1 
ATOM   1615 N NE2  . GLN A 1 102 ? 1.452  40.728 55.073 1.00 85.47  ? 105 GLN A NE2  1 
ATOM   1616 H H    . GLN A 1 102 ? 4.006  44.647 54.405 0.00 42.46  ? 105 GLN A H    1 
ATOM   1617 H HA   . GLN A 1 102 ? 4.239  43.430 52.121 0.00 42.54  ? 105 GLN A HA   1 
ATOM   1618 H HB2  . GLN A 1 102 ? 2.075  44.071 53.763 0.00 61.03  ? 105 GLN A HB2  1 
ATOM   1619 H HB3  . GLN A 1 102 ? 1.727  43.691 52.259 0.00 61.03  ? 105 GLN A HB3  1 
ATOM   1620 H HG2  . GLN A 1 102 ? 2.414  41.583 52.524 0.00 63.59  ? 105 GLN A HG2  1 
ATOM   1621 H HG3  . GLN A 1 102 ? 3.226  41.932 53.845 0.00 63.59  ? 105 GLN A HG3  1 
ATOM   1622 H HE21 . GLN A 1 102 ? 2.236  40.383 55.148 0.00 102.57 ? 105 GLN A HE21 1 
ATOM   1623 H HE22 . GLN A 1 102 ? 0.811  40.453 55.575 0.00 102.57 ? 105 GLN A HE22 1 
ATOM   1624 N N    . GLY A 1 103 ? 3.235  46.465 51.896 1.00 30.23  ? 106 GLY A N    1 
ATOM   1625 C CA   . GLY A 1 103 ? 3.025  47.534 50.920 1.00 31.78  ? 106 GLY A CA   1 
ATOM   1626 C C    . GLY A 1 103 ? 4.258  47.808 50.075 1.00 33.95  ? 106 GLY A C    1 
ATOM   1627 O O    . GLY A 1 103 ? 4.163  48.073 48.871 1.00 31.17  ? 106 GLY A O    1 
ATOM   1628 H H    . GLY A 1 103 ? 3.171  46.705 52.719 0.00 36.28  ? 106 GLY A H    1 
ATOM   1629 H HA2  . GLY A 1 103 ? 2.298  47.287 50.326 0.00 38.14  ? 106 GLY A HA2  1 
ATOM   1630 H HA3  . GLY A 1 103 ? 2.788  48.350 51.386 0.00 38.14  ? 106 GLY A HA3  1 
ATOM   1631 N N    . THR A 1 104 ? 5.436  47.720 50.687 1.00 29.14  ? 107 THR A N    1 
ATOM   1632 C CA   . THR A 1 104 ? 6.663  47.963 49.947 1.00 30.70  ? 107 THR A CA   1 
ATOM   1633 C C    . THR A 1 104 ? 6.922  46.834 48.967 1.00 30.35  ? 107 THR A C    1 
ATOM   1634 O O    . THR A 1 104 ? 7.417  47.066 47.847 1.00 29.90  ? 107 THR A O    1 
ATOM   1635 C CB   . THR A 1 104 ? 7.827  48.111 50.926 1.00 32.48  ? 107 THR A CB   1 
ATOM   1636 O OG1  . THR A 1 104 ? 7.576  49.236 51.790 1.00 36.43  ? 107 THR A OG1  1 
ATOM   1637 C CG2  . THR A 1 104 ? 9.140  48.334 50.171 1.00 38.60  ? 107 THR A CG2  1 
ATOM   1638 H H    . THR A 1 104 ? 5.549  47.524 51.517 0.00 34.98  ? 107 THR A H    1 
ATOM   1639 H HA   . THR A 1 104 ? 6.586  48.789 49.445 0.00 36.85  ? 107 THR A HA   1 
ATOM   1640 H HB   . THR A 1 104 ? 7.917  47.303 51.455 0.00 38.99  ? 107 THR A HB   1 
ATOM   1641 H HG1  . THR A 1 104 ? 8.205  49.323 52.340 0.00 43.73  ? 107 THR A HG1  1 
ATOM   1642 H HG21 . THR A 1 104 ? 9.829  48.630 50.785 0.00 46.34  ? 107 THR A HG21 1 
ATOM   1643 H HG22 . THR A 1 104 ? 9.425  47.507 49.752 0.00 46.34  ? 107 THR A HG22 1 
ATOM   1644 H HG23 . THR A 1 104 ? 9.018  49.009 49.485 0.00 46.34  ? 107 THR A HG23 1 
ATOM   1645 N N    . ILE A 1 105 ? 6.615  45.608 49.370 1.00 26.68  ? 108 ILE A N    1 
ATOM   1646 C CA   . ILE A 1 105 ? 6.800  44.469 48.443 1.00 25.33  ? 108 ILE A CA   1 
ATOM   1647 C C    . ILE A 1 105 ? 5.911  44.640 47.218 1.00 31.21  ? 108 ILE A C    1 
ATOM   1648 O O    . ILE A 1 105 ? 6.338  44.415 46.079 1.00 28.45  ? 108 ILE A O    1 
ATOM   1649 C CB   . ILE A 1 105 ? 6.521  43.140 49.158 1.00 27.06  ? 108 ILE A CB   1 
ATOM   1650 C CG1  . ILE A 1 105 ? 7.572  42.890 50.221 1.00 30.18  ? 108 ILE A CG1  1 
ATOM   1651 C CG2  . ILE A 1 105 ? 6.499  42.003 48.135 1.00 38.40  ? 108 ILE A CG2  1 
ATOM   1652 C CD1  . ILE A 1 105 ? 7.301  41.622 51.048 1.00 33.19  ? 108 ILE A CD1  1 
ATOM   1653 H H    . ILE A 1 105 ? 6.308  45.403 50.147 0.00 32.02  ? 108 ILE A H    1 
ATOM   1654 H HA   . ILE A 1 105 ? 7.724  44.459 48.148 0.00 30.41  ? 108 ILE A HA   1 
ATOM   1655 H HB   . ILE A 1 105 ? 5.655  43.185 49.593 0.00 32.49  ? 108 ILE A HB   1 
ATOM   1656 H HG12 . ILE A 1 105 ? 8.436  42.788 49.791 0.00 36.23  ? 108 ILE A HG12 1 
ATOM   1657 H HG13 . ILE A 1 105 ? 7.591  43.645 50.829 0.00 36.23  ? 108 ILE A HG13 1 
ATOM   1658 H HG21 . ILE A 1 105 ? 6.478  41.155 48.606 0.00 46.10  ? 108 ILE A HG21 1 
ATOM   1659 H HG22 . ILE A 1 105 ? 5.708  42.093 47.580 0.00 46.10  ? 108 ILE A HG22 1 
ATOM   1660 H HG23 . ILE A 1 105 ? 7.296  42.057 47.586 0.00 46.10  ? 108 ILE A HG23 1 
ATOM   1661 H HD11 . ILE A 1 105 ? 7.820  41.662 51.867 0.00 39.84  ? 108 ILE A HD11 1 
ATOM   1662 H HD12 . ILE A 1 105 ? 6.355  41.577 51.258 0.00 39.84  ? 108 ILE A HD12 1 
ATOM   1663 H HD13 . ILE A 1 105 ? 7.562  40.844 50.529 0.00 39.84  ? 108 ILE A HD13 1 
ATOM   1664 N N    . LEU A 1 106 ? 4.647  45.004 47.426 1.00 27.82  ? 109 LEU A N    1 
ATOM   1665 C CA   A LEU A 1 106 ? 3.752  45.205 46.295 0.57 25.01  ? 109 LEU A CA   1 
ATOM   1666 C CA   B LEU A 1 106 ? 3.726  45.239 46.317 0.43 25.08  ? 109 LEU A CA   1 
ATOM   1667 C C    . LEU A 1 106 ? 4.256  46.305 45.377 1.00 29.84  ? 109 LEU A C    1 
ATOM   1668 O O    . LEU A 1 106 ? 4.227  46.147 44.141 1.00 28.50  ? 109 LEU A O    1 
ATOM   1669 C CB   A LEU A 1 106 ? 2.334  45.515 46.780 0.57 31.20  ? 109 LEU A CB   1 
ATOM   1670 C CB   B LEU A 1 106 ? 2.355  45.661 46.855 0.43 31.09  ? 109 LEU A CB   1 
ATOM   1671 C CG   A LEU A 1 106 ? 1.343  45.718 45.633 0.57 31.97  ? 109 LEU A CG   1 
ATOM   1672 C CG   B LEU A 1 106 ? 1.447  44.610 47.477 0.43 30.03  ? 109 LEU A CG   1 
ATOM   1673 C CD1  A LEU A 1 106 ? 1.248  44.475 44.767 0.57 41.39  ? 109 LEU A CD1  1 
ATOM   1674 C CD1  B LEU A 1 106 ? 0.510  45.269 48.482 0.43 38.47  ? 109 LEU A CD1  1 
ATOM   1675 C CD2  A LEU A 1 106 ? -0.020 46.106 46.150 0.57 35.00  ? 109 LEU A CD2  1 
ATOM   1676 C CD2  B LEU A 1 106 ? 0.657  43.891 46.409 0.43 42.28  ? 109 LEU A CD2  1 
ATOM   1677 H H    A LEU A 1 106 ? 4.292  45.139 48.197 0.57 33.39  ? 109 LEU A H    1 
ATOM   1678 H H    B LEU A 1 106 ? 4.297  45.123 48.202 0.43 33.39  ? 109 LEU A H    1 
ATOM   1679 H HA   A LEU A 1 106 ? 3.716  44.381 45.785 0.57 30.02  ? 109 LEU A HA   1 
ATOM   1680 H HA   B LEU A 1 106 ? 3.627  44.410 45.822 0.43 30.11  ? 109 LEU A HA   1 
ATOM   1681 H HB2  A LEU A 1 106 ? 2.018  44.775 47.322 0.57 37.45  ? 109 LEU A HB2  1 
ATOM   1682 H HB2  B LEU A 1 106 ? 2.507  46.331 47.540 0.43 37.32  ? 109 LEU A HB2  1 
ATOM   1683 H HB3  A LEU A 1 106 ? 2.353  46.328 47.308 0.57 37.45  ? 109 LEU A HB3  1 
ATOM   1684 H HB3  B LEU A 1 106 ? 1.860  46.048 46.116 0.43 37.32  ? 109 LEU A HB3  1 
ATOM   1685 H HG   A LEU A 1 106 ? 1.669  46.445 45.079 0.57 38.38  ? 109 LEU A HG   1 
ATOM   1686 H HG   B LEU A 1 106 ? 1.986  43.951 47.941 0.43 36.05  ? 109 LEU A HG   1 
ATOM   1687 H HD11 A LEU A 1 106 ? 0.366  44.438 44.364 0.57 49.69  ? 109 LEU A HD11 1 
ATOM   1688 H HD11 B LEU A 1 106 ? -0.070 44.592 48.864 0.43 46.18  ? 109 LEU A HD11 1 
ATOM   1689 H HD12 A LEU A 1 106 ? 1.926  44.520 44.075 0.57 49.69  ? 109 LEU A HD12 1 
ATOM   1690 H HD12 B LEU A 1 106 ? 1.039  45.685 49.181 0.43 46.18  ? 109 LEU A HD12 1 
ATOM   1691 H HD13 A LEU A 1 106 ? 1.392  43.692 45.321 0.57 49.69  ? 109 LEU A HD13 1 
ATOM   1692 H HD13 B LEU A 1 106 ? -0.021 45.941 48.025 0.43 46.18  ? 109 LEU A HD13 1 
ATOM   1693 H HD21 A LEU A 1 106 ? -0.586 46.346 45.399 0.57 42.01  ? 109 LEU A HD21 1 
ATOM   1694 H HD21 B LEU A 1 106 ? 0.078  43.236 46.831 0.43 50.75  ? 109 LEU A HD21 1 
ATOM   1695 H HD22 A LEU A 1 106 ? -0.403 45.353 46.626 0.57 42.01  ? 109 LEU A HD22 1 
ATOM   1696 H HD22 B LEU A 1 106 ? 0.124  44.538 45.921 0.43 50.75  ? 109 LEU A HD22 1 
ATOM   1697 H HD23 A LEU A 1 106 ? 0.073  46.863 46.749 0.57 42.01  ? 109 LEU A HD23 1 
ATOM   1698 H HD23 B LEU A 1 106 ? 1.273  43.447 45.805 0.43 50.75  ? 109 LEU A HD23 1 
ATOM   1699 N N    . ALA A 1 107 ? 4.719  47.419 45.936 1.00 27.69  ? 110 ALA A N    1 
ATOM   1700 C CA   . ALA A 1 107 ? 5.254  48.504 45.121 1.00 28.81  ? 110 ALA A CA   1 
ATOM   1701 C C    . ALA A 1 107 ? 6.412  48.016 44.256 1.00 26.46  ? 110 ALA A C    1 
ATOM   1702 O O    . ALA A 1 107 ? 6.506  48.381 43.089 1.00 26.86  ? 110 ALA A O    1 
ATOM   1703 C CB   . ALA A 1 107 ? 5.725  49.650 46.029 1.00 33.77  ? 110 ALA A CB   1 
ATOM   1704 H H    . ALA A 1 107 ? 4.735  47.572 46.782 0.00 33.24  ? 110 ALA A H    1 
ATOM   1705 H HA   . ALA A 1 107 ? 4.553  48.837 44.539 0.00 34.59  ? 110 ALA A HA   1 
ATOM   1706 H HB1  . ALA A 1 107 ? 6.207  50.300 45.494 0.00 40.54  ? 110 ALA A HB1  1 
ATOM   1707 H HB2  . ALA A 1 107 ? 4.951  50.068 46.438 0.00 40.54  ? 110 ALA A HB2  1 
ATOM   1708 H HB3  . ALA A 1 107 ? 6.308  49.290 46.716 0.00 40.54  ? 110 ALA A HB3  1 
ATOM   1709 N N    . LEU A 1 108 ? 7.328  47.232 44.840 1.00 22.27  ? 111 LEU A N    1 
ATOM   1710 C CA   . LEU A 1 108 ? 8.498  46.745 44.120 1.00 24.08  ? 111 LEU A CA   1 
ATOM   1711 C C    . LEU A 1 108 ? 8.102  45.796 42.998 1.00 26.88  ? 111 LEU A C    1 
ATOM   1712 O O    . LEU A 1 108 ? 8.586  45.917 41.856 1.00 26.06  ? 111 LEU A O    1 
ATOM   1713 C CB   . LEU A 1 108 ? 9.448  46.013 45.086 1.00 24.65  ? 111 LEU A CB   1 
ATOM   1714 C CG   . LEU A 1 108 ? 10.461 46.808 45.898 1.00 33.69  ? 111 LEU A CG   1 
ATOM   1715 C CD1  . LEU A 1 108 ? 11.329 45.848 46.710 1.00 40.01  ? 111 LEU A CD1  1 
ATOM   1716 C CD2  . LEU A 1 108 ? 11.339 47.685 45.010 1.00 40.47  ? 111 LEU A CD2  1 
ATOM   1717 H H    . LEU A 1 108 ? 7.291  46.969 45.657 0.00 26.74  ? 111 LEU A H    1 
ATOM   1718 H HA   . LEU A 1 108 ? 8.958  47.510 43.740 0.00 28.91  ? 111 LEU A HA   1 
ATOM   1719 H HB2  . LEU A 1 108 ? 8.896  45.542 45.729 0.00 29.59  ? 111 LEU A HB2  1 
ATOM   1720 H HB3  . LEU A 1 108 ? 9.960  45.379 44.560 0.00 29.59  ? 111 LEU A HB3  1 
ATOM   1721 H HG   . LEU A 1 108 ? 9.982  47.400 46.498 0.00 40.44  ? 111 LEU A HG   1 
ATOM   1722 H HD11 . LEU A 1 108 ? 11.995 46.359 47.197 0.00 48.03  ? 111 LEU A HD11 1 
ATOM   1723 H HD12 . LEU A 1 108 ? 10.765 45.363 47.332 0.00 48.03  ? 111 LEU A HD12 1 
ATOM   1724 H HD13 . LEU A 1 108 ? 11.764 45.228 46.105 0.00 48.03  ? 111 LEU A HD13 1 
ATOM   1725 H HD21 . LEU A 1 108 ? 12.033 48.090 45.554 0.00 48.58  ? 111 LEU A HD21 1 
ATOM   1726 H HD22 . LEU A 1 108 ? 11.739 47.134 44.319 0.00 48.58  ? 111 LEU A HD22 1 
ATOM   1727 H HD23 . LEU A 1 108 ? 10.790 48.375 44.606 0.00 48.58  ? 111 LEU A HD23 1 
ATOM   1728 N N    . VAL A 1 109 ? 7.250  44.820 43.302 1.00 22.82  ? 112 VAL A N    1 
ATOM   1729 C CA   . VAL A 1 109 ? 6.836  43.842 42.292 1.00 23.09  ? 112 VAL A CA   1 
ATOM   1730 C C    . VAL A 1 109 ? 6.043  44.527 41.190 1.00 27.33  ? 112 VAL A C    1 
ATOM   1731 O O    . VAL A 1 109 ? 6.218  44.213 40.007 1.00 23.70  ? 112 VAL A O    1 
ATOM   1732 C CB   . VAL A 1 109 ? 6.049  42.704 42.961 1.00 25.90  ? 112 VAL A CB   1 
ATOM   1733 C CG1  . VAL A 1 109 ? 5.371  41.825 41.916 1.00 29.13  ? 112 VAL A CG1  1 
ATOM   1734 C CG2  . VAL A 1 109 ? 7.006  41.871 43.827 1.00 32.61  ? 112 VAL A CG2  1 
ATOM   1735 H H    . VAL A 1 109 ? 6.898  44.699 44.078 0.00 27.39  ? 112 VAL A H    1 
ATOM   1736 H HA   . VAL A 1 109 ? 7.624  43.454 41.881 0.00 27.72  ? 112 VAL A HA   1 
ATOM   1737 H HB   . VAL A 1 109 ? 5.352  43.078 43.523 0.00 31.10  ? 112 VAL A HB   1 
ATOM   1738 H HG11 . VAL A 1 109 ? 5.088  40.996 42.334 0.00 34.97  ? 112 VAL A HG11 1 
ATOM   1739 H HG12 . VAL A 1 109 ? 4.600  42.294 41.559 0.00 34.97  ? 112 VAL A HG12 1 
ATOM   1740 H HG13 . VAL A 1 109 ? 6.002  41.637 41.203 0.00 34.97  ? 112 VAL A HG13 1 
ATOM   1741 H HG21 . VAL A 1 109 ? 6.499  41.184 44.287 0.00 39.14  ? 112 VAL A HG21 1 
ATOM   1742 H HG22 . VAL A 1 109 ? 7.674  41.461 43.255 0.00 39.14  ? 112 VAL A HG22 1 
ATOM   1743 H HG23 . VAL A 1 109 ? 7.436  42.453 44.472 0.00 39.14  ? 112 VAL A HG23 1 
ATOM   1744 N N    . GLY A 1 110 ? 5.163  45.480 41.541 1.00 22.86  ? 113 GLY A N    1 
ATOM   1745 C CA   . GLY A 1 110 ? 4.415  46.201 40.534 1.00 22.08  ? 113 GLY A CA   1 
ATOM   1746 C C    . GLY A 1 110 ? 5.294  47.033 39.626 1.00 25.15  ? 113 GLY A C    1 
ATOM   1747 O O    . GLY A 1 110 ? 5.130  47.039 38.402 1.00 23.63  ? 113 GLY A O    1 
ATOM   1748 H H    . GLY A 1 110 ? 4.991  45.716 42.349 0.00 27.44  ? 113 GLY A H    1 
ATOM   1749 H HA2  . GLY A 1 110 ? 3.927  45.567 39.986 0.00 26.51  ? 113 GLY A HA2  1 
ATOM   1750 H HA3  . GLY A 1 110 ? 3.783  46.793 40.971 0.00 26.51  ? 113 GLY A HA3  1 
ATOM   1751 N N    . ALA A 1 111 ? 6.230  47.787 40.221 1.00 20.43  ? 114 ALA A N    1 
ATOM   1752 C CA   . ALA A 1 111 ? 7.161  48.553 39.391 1.00 21.66  ? 114 ALA A CA   1 
ATOM   1753 C C    . ALA A 1 111 ? 7.977  47.641 38.486 1.00 19.45  ? 114 ALA A C    1 
ATOM   1754 O O    . ALA A 1 111 ? 8.325  48.005 37.345 1.00 22.67  ? 114 ALA A O    1 
ATOM   1755 C CB   . ALA A 1 111 ? 8.098  49.376 40.308 1.00 23.85  ? 114 ALA A CB   1 
ATOM   1756 H H    . ALA A 1 111 ? 6.340  47.868 41.070 0.00 24.53  ? 114 ALA A H    1 
ATOM   1757 H HA   . ALA A 1 111 ? 6.660  49.161 38.826 0.00 26.01  ? 114 ALA A HA   1 
ATOM   1758 H HB1  . ALA A 1 111 ? 8.709  49.890 39.756 0.00 28.63  ? 114 ALA A HB1  1 
ATOM   1759 H HB2  . ALA A 1 111 ? 7.562  49.974 40.853 0.00 28.63  ? 114 ALA A HB2  1 
ATOM   1760 H HB3  . ALA A 1 111 ? 8.597  48.769 40.877 0.00 28.63  ? 114 ALA A HB3  1 
ATOM   1761 N N    . ASP A 1 112 ? 8.346  46.461 38.995 1.00 19.23  ? 115 ASP A N    1 
ATOM   1762 C CA   . ASP A 1 112 ? 9.139  45.515 38.200 1.00 18.68  ? 115 ASP A CA   1 
ATOM   1763 C C    . ASP A 1 112 ? 8.324  45.005 37.036 1.00 20.29  ? 115 ASP A C    1 
ATOM   1764 O O    . ASP A 1 112 ? 8.861  44.847 35.921 1.00 19.71  ? 115 ASP A O    1 
ATOM   1765 C CB   . ASP A 1 112 ? 9.594  44.356 39.137 1.00 20.10  ? 115 ASP A CB   1 
ATOM   1766 C CG   . ASP A 1 112 ? 10.592 43.448 38.464 1.00 25.29  ? 115 ASP A CG   1 
ATOM   1767 O OD1  . ASP A 1 112 ? 10.187 42.611 37.626 1.00 26.60  ? 115 ASP A OD1  1 
ATOM   1768 O OD2  . ASP A 1 112 ? 11.785 43.604 38.720 1.00 34.13  ? 115 ASP A OD2  1 
ATOM   1769 H H    . ASP A 1 112 ? 8.154  46.186 39.786 0.00 23.09  ? 115 ASP A H    1 
ATOM   1770 H HA   . ASP A 1 112 ? 9.932  45.939 37.836 0.00 22.42  ? 115 ASP A HA   1 
ATOM   1771 H HB2  . ASP A 1 112 ? 10.011 44.730 39.929 0.00 24.13  ? 115 ASP A HB2  1 
ATOM   1772 H HB3  . ASP A 1 112 ? 8.822  43.826 39.388 0.00 24.13  ? 115 ASP A HB3  1 
ATOM   1773 N N    . GLY A 1 113 ? 7.056  44.692 37.254 1.00 20.71  ? 116 GLY A N    1 
ATOM   1774 C CA   . GLY A 1 113 ? 6.187  44.272 36.151 1.00 20.00  ? 116 GLY A CA   1 
ATOM   1775 C C    . GLY A 1 113 ? 6.072  45.334 35.077 1.00 20.84  ? 116 GLY A C    1 
ATOM   1776 O O    . GLY A 1 113 ? 6.049  45.035 33.878 1.00 22.62  ? 116 GLY A O    1 
ATOM   1777 H H    . GLY A 1 113 ? 6.670  44.711 38.022 0.00 24.86  ? 116 GLY A H    1 
ATOM   1778 H HA2  . GLY A 1 113 ? 6.547  43.466 35.747 0.00 24.02  ? 116 GLY A HA2  1 
ATOM   1779 H HA3  . GLY A 1 113 ? 5.300  44.085 36.494 0.00 24.02  ? 116 GLY A HA3  1 
ATOM   1780 N N    . ILE A 1 114 ? 5.927  46.607 35.505 1.00 18.40  ? 117 ILE A N    1 
ATOM   1781 C CA   . ILE A 1 114 ? 5.884  47.701 34.554 1.00 18.48  ? 117 ILE A CA   1 
ATOM   1782 C C    . ILE A 1 114 ? 7.205  47.787 33.794 1.00 21.21  ? 117 ILE A C    1 
ATOM   1783 O O    . ILE A 1 114 ? 7.223  47.983 32.579 1.00 21.05  ? 117 ILE A O    1 
ATOM   1784 C CB   . ILE A 1 114 ? 5.574  49.017 35.277 1.00 20.49  ? 117 ILE A CB   1 
ATOM   1785 C CG1  . ILE A 1 114 ? 4.102  48.977 35.688 1.00 24.37  ? 117 ILE A CG1  1 
ATOM   1786 C CG2  . ILE A 1 114 ? 5.824  50.186 34.345 1.00 24.88  ? 117 ILE A CG2  1 
ATOM   1787 C CD1  . ILE A 1 114 ? 3.688  50.194 36.547 1.00 30.02  ? 117 ILE A CD1  1 
ATOM   1788 H H    . ILE A 1 114 ? 5.854  46.845 36.329 0.00 22.09  ? 117 ILE A H    1 
ATOM   1789 H HA   . ILE A 1 114 ? 5.174  47.530 33.916 0.00 22.19  ? 117 ILE A HA   1 
ATOM   1790 H HB   . ILE A 1 114 ? 6.142  49.122 36.056 0.00 24.60  ? 117 ILE A HB   1 
ATOM   1791 H HG12 . ILE A 1 114 ? 3.551  48.971 34.890 0.00 29.26  ? 117 ILE A HG12 1 
ATOM   1792 H HG13 . ILE A 1 114 ? 3.941  48.174 36.208 0.00 29.26  ? 117 ILE A HG13 1 
ATOM   1793 H HG21 . ILE A 1 114 ? 5.435  50.986 34.730 0.00 29.87  ? 117 ILE A HG21 1 
ATOM   1794 H HG22 . ILE A 1 114 ? 6.781  50.303 34.235 0.00 29.87  ? 117 ILE A HG22 1 
ATOM   1795 H HG23 . ILE A 1 114 ? 5.413  49.999 33.486 0.00 29.87  ? 117 ILE A HG23 1 
ATOM   1796 H HD11 . ILE A 1 114 ? 2.808  50.032 36.921 0.00 36.03  ? 117 ILE A HD11 1 
ATOM   1797 H HD12 . ILE A 1 114 ? 4.334  50.311 37.261 0.00 36.03  ? 117 ILE A HD12 1 
ATOM   1798 H HD13 . ILE A 1 114 ? 3.669  50.985 35.985 0.00 36.03  ? 117 ILE A HD13 1 
ATOM   1799 N N    . MET A 1 115 ? 8.335  47.600 34.495 1.00 18.31  ? 118 MET A N    1 
ATOM   1800 C CA   . MET A 1 115 ? 9.633  47.698 33.811 1.00 18.62  ? 118 MET A CA   1 
ATOM   1801 C C    . MET A 1 115 ? 9.776  46.627 32.731 1.00 20.59  ? 118 MET A C    1 
ATOM   1802 O O    . MET A 1 115 ? 10.174 46.910 31.601 1.00 20.63  ? 118 MET A O    1 
ATOM   1803 C CB   . MET A 1 115 ? 10.764 47.577 34.876 1.00 20.09  ? 118 MET A CB   1 
ATOM   1804 C CG   . MET A 1 115 ? 12.151 47.372 34.315 1.00 21.04  ? 118 MET A CG   1 
ATOM   1805 S SD   . MET A 1 115 ? 13.397 47.197 35.646 1.00 23.53  ? 118 MET A SD   1 
ATOM   1806 C CE   . MET A 1 115 ? 13.228 45.423 35.908 1.00 25.96  ? 118 MET A CE   1 
ATOM   1807 H H    . MET A 1 115 ? 8.375  47.423 35.336 0.00 21.98  ? 118 MET A H    1 
ATOM   1808 H HA   . MET A 1 115 ? 9.706  48.562 33.378 0.00 22.36  ? 118 MET A HA   1 
ATOM   1809 H HB2  . MET A 1 115 ? 10.780 48.394 35.399 0.00 24.12  ? 118 MET A HB2  1 
ATOM   1810 H HB3  . MET A 1 115 ? 10.567 46.820 35.448 0.00 24.12  ? 118 MET A HB3  1 
ATOM   1811 H HG2  . MET A 1 115 ? 12.164 46.565 33.778 0.00 25.26  ? 118 MET A HG2  1 
ATOM   1812 H HG3  . MET A 1 115 ? 12.393 48.137 33.770 0.00 25.26  ? 118 MET A HG3  1 
ATOM   1813 H HE1  . MET A 1 115 ? 13.838 45.148 36.611 0.00 31.16  ? 118 MET A HE1  1 
ATOM   1814 H HE2  . MET A 1 115 ? 12.314 45.227 36.167 0.00 31.16  ? 118 MET A HE2  1 
ATOM   1815 H HE3  . MET A 1 115 ? 13.445 44.960 35.083 0.00 31.16  ? 118 MET A HE3  1 
ATOM   1816 N N    . ILE A 1 116 ? 9.468  45.349 33.063 1.00 18.58  ? 119 ILE A N    1 
ATOM   1817 C CA   . ILE A 1 116 ? 9.612  44.311 32.044 1.00 18.72  ? 119 ILE A CA   1 
ATOM   1818 C C    . ILE A 1 116 ? 8.552  44.445 30.963 1.00 20.95  ? 119 ILE A C    1 
ATOM   1819 O O    . ILE A 1 116 ? 8.843  44.234 29.778 1.00 22.03  ? 119 ILE A O    1 
ATOM   1820 C CB   . ILE A 1 116 ? 9.567  42.931 32.697 1.00 20.24  ? 119 ILE A CB   1 
ATOM   1821 C CG1  . ILE A 1 116 ? 10.678 42.826 33.736 1.00 22.15  ? 119 ILE A CG1  1 
ATOM   1822 C CG2  . ILE A 1 116 ? 9.726  41.837 31.619 1.00 25.82  ? 119 ILE A CG2  1 
ATOM   1823 C CD1  . ILE A 1 116 ? 12.074 43.121 33.198 1.00 23.35  ? 119 ILE A CD1  1 
ATOM   1824 H H    . ILE A 1 116 ? 9.189  45.083 33.832 0.00 22.31  ? 119 ILE A H    1 
ATOM   1825 H HA   . ILE A 1 116 ? 10.476 44.427 31.619 0.00 22.47  ? 119 ILE A HA   1 
ATOM   1826 H HB   . ILE A 1 116 ? 8.711  42.809 33.138 0.00 24.30  ? 119 ILE A HB   1 
ATOM   1827 H HG12 . ILE A 1 116 ? 10.498 43.461 34.447 0.00 26.59  ? 119 ILE A HG12 1 
ATOM   1828 H HG13 . ILE A 1 116 ? 10.685 41.923 34.091 0.00 26.59  ? 119 ILE A HG13 1 
ATOM   1829 H HG21 . ILE A 1 116 ? 9.954  40.999 32.051 0.00 31.00  ? 119 ILE A HG21 1 
ATOM   1830 H HG22 . ILE A 1 116 ? 8.889  41.744 31.137 0.00 31.00  ? 119 ILE A HG22 1 
ATOM   1831 H HG23 . ILE A 1 116 ? 10.432 42.097 31.007 0.00 31.00  ? 119 ILE A HG23 1 
ATOM   1832 H HD11 . ILE A 1 116 ? 12.731 42.820 33.844 0.00 28.03  ? 119 ILE A HD11 1 
ATOM   1833 H HD12 . ILE A 1 116 ? 12.194 42.649 32.358 0.00 28.03  ? 119 ILE A HD12 1 
ATOM   1834 H HD13 . ILE A 1 116 ? 12.162 44.076 33.056 0.00 28.03  ? 119 ILE A HD13 1 
ATOM   1835 N N    . GLY A 1 117 ? 7.296  44.773 31.340 1.00 18.23  ? 120 GLY A N    1 
ATOM   1836 C CA   . GLY A 1 117 ? 6.234  44.824 30.343 1.00 18.84  ? 120 GLY A CA   1 
ATOM   1837 C C    . GLY A 1 117 ? 6.489  45.927 29.317 1.00 20.75  ? 120 GLY A C    1 
ATOM   1838 O O    . GLY A 1 117 ? 6.253  45.729 28.107 1.00 22.11  ? 120 GLY A O    1 
ATOM   1839 H H    . GLY A 1 117 ? 7.052  44.963 32.143 0.00 21.88  ? 120 GLY A H    1 
ATOM   1840 H HA2  . GLY A 1 117 ? 6.183  43.974 29.878 0.00 22.62  ? 120 GLY A HA2  1 
ATOM   1841 H HA3  . GLY A 1 117 ? 5.385  44.996 30.780 0.00 22.62  ? 120 GLY A HA3  1 
ATOM   1842 N N    . THR A 1 118 ? 6.930  47.096 29.773 1.00 19.01  ? 121 THR A N    1 
ATOM   1843 C CA   . THR A 1 118 ? 7.205  48.161 28.816 1.00 18.83  ? 121 THR A CA   1 
ATOM   1844 C C    . THR A 1 118 ? 8.476  47.861 28.016 1.00 21.26  ? 121 THR A C    1 
ATOM   1845 O O    . THR A 1 118 ? 8.578  48.284 26.857 1.00 20.80  ? 121 THR A O    1 
ATOM   1846 C CB   . THR A 1 118 ? 7.300  49.564 29.489 1.00 20.99  ? 121 THR A CB   1 
ATOM   1847 O OG1  . THR A 1 118 ? 8.300  49.557 30.518 1.00 21.95  ? 121 THR A OG1  1 
ATOM   1848 C CG2  . THR A 1 118 ? 5.966  49.977 30.046 1.00 27.00  ? 121 THR A CG2  1 
ATOM   1849 H H    . THR A 1 118 ? 7.073  47.290 30.598 0.00 22.82  ? 121 THR A H    1 
ATOM   1850 H HA   . THR A 1 118 ? 6.449  48.212 28.210 0.00 22.61  ? 121 THR A HA   1 
ATOM   1851 H HB   . THR A 1 118 ? 7.556  50.222 28.824 0.00 25.20  ? 121 THR A HB   1 
ATOM   1852 H HG1  . THR A 1 118 ? 8.101  48.994 31.109 0.00 26.35  ? 121 THR A HG1  1 
ATOM   1853 H HG21 . THR A 1 118 ? 6.038  50.848 30.466 0.00 32.41  ? 121 THR A HG21 1 
ATOM   1854 H HG22 . THR A 1 118 ? 5.309  50.024 29.334 0.00 32.41  ? 121 THR A HG22 1 
ATOM   1855 H HG23 . THR A 1 118 ? 5.669  49.333 30.707 0.00 32.41  ? 121 THR A HG23 1 
ATOM   1856 N N    . GLY A 1 119 ? 9.459  47.164 28.608 1.00 18.65  ? 122 GLY A N    1 
ATOM   1857 C CA   . GLY A 1 119 ? 10.597 46.700 27.817 1.00 19.91  ? 122 GLY A CA   1 
ATOM   1858 C C    . GLY A 1 119 ? 10.170 45.793 26.673 1.00 24.56  ? 122 GLY A C    1 
ATOM   1859 O O    . GLY A 1 119 ? 10.724 45.881 25.571 1.00 22.42  ? 122 GLY A O    1 
ATOM   1860 H H    . GLY A 1 119 ? 9.486  46.955 29.441 0.00 22.39  ? 122 GLY A H    1 
ATOM   1861 H HA2  . GLY A 1 119 ? 11.063 47.465 27.444 0.00 23.90  ? 122 GLY A HA2  1 
ATOM   1862 H HA3  . GLY A 1 119 ? 11.207 46.207 28.388 0.00 23.90  ? 122 GLY A HA3  1 
ATOM   1863 N N    . LEU A 1 120 ? 9.210  44.894 26.920 1.00 19.49  ? 123 LEU A N    1 
ATOM   1864 C CA   . LEU A 1 120 ? 8.712  44.014 25.884 1.00 19.14  ? 123 LEU A CA   1 
ATOM   1865 C C    . LEU A 1 120 ? 7.965  44.799 24.799 1.00 20.90  ? 123 LEU A C    1 
ATOM   1866 O O    . LEU A 1 120 ? 8.162  44.535 23.615 1.00 21.26  ? 123 LEU A O    1 
ATOM   1867 C CB   . LEU A 1 120 ? 7.771  42.977 26.523 1.00 19.87  ? 123 LEU A CB   1 
ATOM   1868 C CG   . LEU A 1 120 ? 7.011  42.054 25.607 1.00 22.41  ? 123 LEU A CG   1 
ATOM   1869 C CD1  . LEU A 1 120 ? 7.916  41.170 24.718 1.00 26.15  ? 123 LEU A CD1  1 
ATOM   1870 C CD2  . LEU A 1 120 ? 6.086  41.168 26.467 1.00 33.65  ? 123 LEU A CD2  1 
ATOM   1871 H H    . LEU A 1 120 ? 8.836  44.779 27.686 0.00 23.40  ? 123 LEU A H    1 
ATOM   1872 H HA   . LEU A 1 120 ? 9.457  43.558 25.464 0.00 22.98  ? 123 LEU A HA   1 
ATOM   1873 H HB2  . LEU A 1 120 ? 8.305  42.414 27.105 0.00 23.86  ? 123 LEU A HB2  1 
ATOM   1874 H HB3  . LEU A 1 120 ? 7.110  43.459 27.044 0.00 23.86  ? 123 LEU A HB3  1 
ATOM   1875 H HG   . LEU A 1 120 ? 6.499  42.600 24.990 0.00 26.91  ? 123 LEU A HG   1 
ATOM   1876 H HD11 . LEU A 1 120 ? 7.357  40.599 24.168 0.00 31.40  ? 123 LEU A HD11 1 
ATOM   1877 H HD12 . LEU A 1 120 ? 8.460  41.742 24.154 0.00 31.40  ? 123 LEU A HD12 1 
ATOM   1878 H HD13 . LEU A 1 120 ? 8.485  40.629 25.287 0.00 31.40  ? 123 LEU A HD13 1 
ATOM   1879 H HD21 . LEU A 1 120 ? 5.611  40.552 25.887 0.00 40.39  ? 123 LEU A HD21 1 
ATOM   1880 H HD22 . LEU A 1 120 ? 6.625  40.673 27.104 0.00 40.39  ? 123 LEU A HD22 1 
ATOM   1881 H HD23 . LEU A 1 120 ? 5.454  41.734 26.937 0.00 40.39  ? 123 LEU A HD23 1 
ATOM   1882 N N    . VAL A 1 121 ? 7.111  45.757 25.195 1.00 18.90  ? 124 VAL A N    1 
ATOM   1883 C CA   . VAL A 1 121 ? 6.431  46.558 24.198 1.00 18.61  ? 124 VAL A CA   1 
ATOM   1884 C C    . VAL A 1 121 ? 7.468  47.306 23.351 1.00 21.74  ? 124 VAL A C    1 
ATOM   1885 O O    . VAL A 1 121 ? 7.372  47.368 22.139 1.00 22.24  ? 124 VAL A O    1 
ATOM   1886 C CB   . VAL A 1 121 ? 5.491  47.550 24.888 1.00 20.36  ? 124 VAL A CB   1 
ATOM   1887 C CG1  . VAL A 1 121 ? 4.900  48.535 23.872 1.00 23.07  ? 124 VAL A CG1  1 
ATOM   1888 C CG2  . VAL A 1 121 ? 4.341  46.770 25.578 1.00 26.30  ? 124 VAL A CG2  1 
ATOM   1889 H H    . VAL A 1 121 ? 6.923  45.949 26.012 0.00 22.70  ? 124 VAL A H    1 
ATOM   1890 H HA   . VAL A 1 121 ? 5.908  45.976 23.624 0.00 22.34  ? 124 VAL A HA   1 
ATOM   1891 H HB   . VAL A 1 121 ? 5.992  48.054 25.549 0.00 24.45  ? 124 VAL A HB   1 
ATOM   1892 H HG11 . VAL A 1 121 ? 4.140  48.985 24.273 0.00 27.69  ? 124 VAL A HG11 1 
ATOM   1893 H HG12 . VAL A 1 121 ? 5.579  49.185 23.629 0.00 27.69  ? 124 VAL A HG12 1 
ATOM   1894 H HG13 . VAL A 1 121 ? 4.616  48.045 23.085 0.00 27.69  ? 124 VAL A HG13 1 
ATOM   1895 H HG21 . VAL A 1 121 ? 3.764  47.400 26.038 0.00 31.57  ? 124 VAL A HG21 1 
ATOM   1896 H HG22 . VAL A 1 121 ? 3.836  46.290 24.904 0.00 31.57  ? 124 VAL A HG22 1 
ATOM   1897 H HG23 . VAL A 1 121 ? 4.721  46.144 26.215 0.00 31.57  ? 124 VAL A HG23 1 
ATOM   1898 N N    . GLY A 1 122 ? 8.474  47.876 24.003 1.00 19.94  ? 125 GLY A N    1 
ATOM   1899 C CA   . GLY A 1 122 ? 9.519  48.546 23.222 1.00 22.71  ? 125 GLY A CA   1 
ATOM   1900 C C    . GLY A 1 122 ? 10.225 47.622 22.266 1.00 23.49  ? 125 GLY A C    1 
ATOM   1901 O O    . GLY A 1 122 ? 10.549 48.001 21.136 1.00 23.19  ? 125 GLY A O    1 
ATOM   1902 H H    . GLY A 1 122 ? 8.576  47.893 24.857 0.00 23.95  ? 125 GLY A H    1 
ATOM   1903 H HA2  . GLY A 1 122 ? 9.121  49.266 22.709 0.00 27.26  ? 125 GLY A HA2  1 
ATOM   1904 H HA3  . GLY A 1 122 ? 10.180 48.917 23.828 0.00 27.26  ? 125 GLY A HA3  1 
ATOM   1905 N N    . ALA A 1 123 ? 10.515 46.383 22.703 1.00 20.73  ? 126 ALA A N    1 
ATOM   1906 C CA   . ALA A 1 123 ? 11.222 45.452 21.837 1.00 20.81  ? 126 ALA A CA   1 
ATOM   1907 C C    . ALA A 1 123 ? 10.426 45.062 20.596 1.00 24.76  ? 126 ALA A C    1 
ATOM   1908 O O    . ALA A 1 123 ? 11.019 44.713 19.554 1.00 23.48  ? 126 ALA A O    1 
ATOM   1909 C CB   . ALA A 1 123 ? 11.577 44.182 22.622 1.00 25.07  ? 126 ALA A CB   1 
ATOM   1910 H H    . ALA A 1 123 ? 10.313 46.072 23.480 0.00 24.88  ? 126 ALA A H    1 
ATOM   1911 H HA   . ALA A 1 123 ? 12.034 45.892 21.540 0.00 24.98  ? 126 ALA A HA   1 
ATOM   1912 H HB1  . ALA A 1 123 ? 12.050 43.570 22.036 0.00 30.09  ? 126 ALA A HB1  1 
ATOM   1913 H HB2  . ALA A 1 123 ? 12.140 44.422 23.374 0.00 30.09  ? 126 ALA A HB2  1 
ATOM   1914 H HB3  . ALA A 1 123 ? 10.759 43.768 22.940 0.00 30.09  ? 126 ALA A HB3  1 
ATOM   1915 N N    . LEU A 1 124 ? 9.092  45.094 20.661 1.00 21.05  ? 127 LEU A N    1 
ATOM   1916 C CA   . LEU A 1 124 ? 8.247  44.658 19.570 1.00 21.85  ? 127 LEU A CA   1 
ATOM   1917 C C    . LEU A 1 124 ? 7.639  45.815 18.766 1.00 22.59  ? 127 LEU A C    1 
ATOM   1918 O O    . LEU A 1 124 ? 6.872  45.569 17.843 1.00 24.72  ? 127 LEU A O    1 
ATOM   1919 C CB   . LEU A 1 124 ? 7.101  43.779 20.155 1.00 24.18  ? 127 LEU A CB   1 
ATOM   1920 C CG   . LEU A 1 124 ? 7.560  42.507 20.854 1.00 25.60  ? 127 LEU A CG   1 
ATOM   1921 C CD1  . LEU A 1 124 ? 6.320  41.777 21.420 1.00 32.20  ? 127 LEU A CD1  1 
ATOM   1922 C CD2  . LEU A 1 124 ? 8.288  41.605 19.878 1.00 27.11  ? 127 LEU A CD2  1 
ATOM   1923 H H    . LEU A 1 124 ? 8.652  45.372 21.346 0.00 25.27  ? 127 LEU A H    1 
ATOM   1924 H HA   . LEU A 1 124 ? 8.776  44.130 18.951 0.00 26.17  ? 127 LEU A HA   1 
ATOM   1925 H HB2  . LEU A 1 124 ? 6.610  44.307 20.804 0.00 29.03  ? 127 LEU A HB2  1 
ATOM   1926 H HB3  . LEU A 1 124 ? 6.514  43.517 19.429 0.00 29.03  ? 127 LEU A HB3  1 
ATOM   1927 H HG   . LEU A 1 124 ? 8.170  42.726 21.576 0.00 30.73  ? 127 LEU A HG   1 
ATOM   1928 H HD11 . LEU A 1 124 ? 6.610  40.978 21.887 0.00 38.66  ? 127 LEU A HD11 1 
ATOM   1929 H HD12 . LEU A 1 124 ? 5.857  42.369 22.033 0.00 38.66  ? 127 LEU A HD12 1 
ATOM   1930 H HD13 . LEU A 1 124 ? 5.733  41.536 20.686 0.00 38.66  ? 127 LEU A HD13 1 
ATOM   1931 H HD21 . LEU A 1 124 ? 8.424  40.738 20.292 0.00 32.54  ? 127 LEU A HD21 1 
ATOM   1932 H HD22 . LEU A 1 124 ? 7.751  41.509 19.076 0.00 32.54  ? 127 LEU A HD22 1 
ATOM   1933 H HD23 . LEU A 1 124 ? 9.144  42.004 19.658 0.00 32.54  ? 127 LEU A HD23 1 
ATOM   1934 N N    . THR A 1 125 ? 7.972  47.050 19.102 1.00 22.97  ? 128 THR A N    1 
ATOM   1935 C CA   . THR A 1 125 ? 7.379  48.223 18.445 1.00 21.64  ? 128 THR A CA   1 
ATOM   1936 C C    . THR A 1 125 ? 8.015  48.473 17.075 1.00 24.85  ? 128 THR A C    1 
ATOM   1937 O O    . THR A 1 125 ? 9.225  48.438 16.922 1.00 26.50  ? 128 THR A O    1 
ATOM   1938 C CB   . THR A 1 125 ? 7.553  49.423 19.391 1.00 24.14  ? 128 THR A CB   1 
ATOM   1939 O OG1  . THR A 1 125 ? 6.562  49.340 20.413 1.00 28.02  ? 128 THR A OG1  1 
ATOM   1940 C CG2  . THR A 1 125 ? 7.370  50.756 18.614 1.00 28.52  ? 128 THR A CG2  1 
ATOM   1941 H H    . THR A 1 125 ? 8.545  47.247 19.713 0.00 27.57  ? 128 THR A H    1 
ATOM   1942 H HA   . THR A 1 125 ? 6.435  48.085 18.268 0.00 25.98  ? 128 THR A HA   1 
ATOM   1943 H HB   . THR A 1 125 ? 8.441  49.416 19.781 0.00 28.97  ? 128 THR A HB   1 
ATOM   1944 H HG1  . THR A 1 125 ? 6.637  49.990 20.939 0.00 33.64  ? 128 THR A HG1  1 
ATOM   1945 H HG21 . THR A 1 125 ? 7.237  51.488 19.237 0.00 34.23  ? 128 THR A HG21 1 
ATOM   1946 H HG22 . THR A 1 125 ? 8.157  50.938 18.078 0.00 34.23  ? 128 THR A HG22 1 
ATOM   1947 H HG23 . THR A 1 125 ? 6.598  50.696 18.029 0.00 34.23  ? 128 THR A HG23 1 
ATOM   1948 N N    . LYS A 1 126 ? 7.163  48.700 16.055 1.00 23.92  ? 129 LYS A N    1 
ATOM   1949 C CA   . LYS A 1 126 ? 7.643  48.788 14.689 1.00 28.28  ? 129 LYS A CA   1 
ATOM   1950 C C    . LYS A 1 126 ? 8.063  50.195 14.289 1.00 31.50  ? 129 LYS A C    1 
ATOM   1951 O O    . LYS A 1 126 ? 8.761  50.351 13.274 1.00 34.73  ? 129 LYS A O    1 
ATOM   1952 C CB   . LYS A 1 126 ? 6.532  48.338 13.711 1.00 30.57  ? 129 LYS A CB   1 
ATOM   1953 C CG   . LYS A 1 126 ? 6.159  46.873 13.874 1.00 37.40  ? 129 LYS A CG   1 
ATOM   1954 C CD   . LYS A 1 126 ? 4.842  46.583 13.128 1.00 48.69  ? 129 LYS A CD   1 
ATOM   1955 C CE   . LYS A 1 126 ? 4.816  45.187 12.528 1.00 84.03  ? 129 LYS A CE   1 
ATOM   1956 N NZ   . LYS A 1 126 ? 4.188  44.200 13.450 1.00 95.15  ? 129 LYS A NZ   1 
ATOM   1957 H H    . LYS A 1 126 ? 6.314  48.804 16.142 0.00 28.71  ? 129 LYS A H    1 
ATOM   1958 H HA   . LYS A 1 126 ? 8.407  48.198 14.600 0.00 33.95  ? 129 LYS A HA   1 
ATOM   1959 H HB2  . LYS A 1 126 ? 5.737  48.870 13.871 0.00 36.70  ? 129 LYS A HB2  1 
ATOM   1960 H HB3  . LYS A 1 126 ? 6.841  48.470 12.801 0.00 36.70  ? 129 LYS A HB3  1 
ATOM   1961 H HG2  . LYS A 1 126 ? 6.858  46.314 13.501 0.00 44.89  ? 129 LYS A HG2  1 
ATOM   1962 H HG3  . LYS A 1 126 ? 6.037  46.669 14.814 0.00 44.89  ? 129 LYS A HG3  1 
ATOM   1963 H HD2  . LYS A 1 126 ? 4.101  46.658 13.750 0.00 58.44  ? 129 LYS A HD2  1 
ATOM   1964 H HD3  . LYS A 1 126 ? 4.736  47.224 12.408 0.00 58.44  ? 129 LYS A HD3  1 
ATOM   1965 H HE2  . LYS A 1 126 ? 4.303  45.203 11.704 0.00 100.84 ? 129 LYS A HE2  1 
ATOM   1966 H HE3  . LYS A 1 126 ? 5.725  44.900 12.348 0.00 100.84 ? 129 LYS A HE3  1 
ATOM   1967 H HZ1  . LYS A 1 126 ? 4.181  43.394 13.074 0.00 114.19 ? 129 LYS A HZ1  1 
ATOM   1968 H HZ2  . LYS A 1 126 ? 4.647  44.160 14.211 0.00 114.19 ? 129 LYS A HZ2  1 
ATOM   1969 H HZ3  . LYS A 1 126 ? 3.351  44.442 13.630 0.00 114.19 ? 129 LYS A HZ3  1 
ATOM   1970 N N    . VAL A 1 127 ? 7.649  51.212 15.031 1.00 26.97  ? 130 VAL A N    1 
ATOM   1971 C CA   . VAL A 1 127 ? 8.047  52.597 14.752 1.00 25.74  ? 130 VAL A CA   1 
ATOM   1972 C C    . VAL A 1 127 ? 9.324  52.870 15.554 1.00 29.80  ? 130 VAL A C    1 
ATOM   1973 O O    . VAL A 1 127 ? 9.301  52.881 16.783 1.00 27.95  ? 130 VAL A O    1 
ATOM   1974 C CB   . VAL A 1 127 ? 6.958  53.581 15.125 1.00 28.16  ? 130 VAL A CB   1 
ATOM   1975 C CG1  . VAL A 1 127 ? 7.438  55.012 14.908 1.00 29.78  ? 130 VAL A CG1  1 
ATOM   1976 C CG2  . VAL A 1 127 ? 5.692  53.316 14.283 1.00 34.71  ? 130 VAL A CG2  1 
ATOM   1977 H H    . VAL A 1 127 ? 7.130  51.131 15.712 0.00 32.37  ? 130 VAL A H    1 
ATOM   1978 H HA   . VAL A 1 127 ? 8.233  52.694 13.805 0.00 30.90  ? 130 VAL A HA   1 
ATOM   1979 H HB   . VAL A 1 127 ? 6.738  53.469 16.064 0.00 33.80  ? 130 VAL A HB   1 
ATOM   1980 H HG11 . VAL A 1 127 ? 6.676  55.611 14.944 0.00 35.75  ? 130 VAL A HG11 1 
ATOM   1981 H HG12 . VAL A 1 127 ? 8.072  55.242 15.605 0.00 35.75  ? 130 VAL A HG12 1 
ATOM   1982 H HG13 . VAL A 1 127 ? 7.866  55.073 14.039 0.00 35.75  ? 130 VAL A HG13 1 
ATOM   1983 H HG21 . VAL A 1 127 ? 5.019  53.977 14.508 0.00 41.66  ? 130 VAL A HG21 1 
ATOM   1984 H HG22 . VAL A 1 127 ? 5.919  53.381 13.342 0.00 41.66  ? 130 VAL A HG22 1 
ATOM   1985 H HG23 . VAL A 1 127 ? 5.361  52.426 14.482 0.00 41.66  ? 130 VAL A HG23 1 
ATOM   1986 N N    . TYR A 1 128 ? 10.431 53.099 14.834 1.00 28.23  ? 131 TYR A N    1 
ATOM   1987 C CA   . TYR A 1 128 ? 11.745 53.091 15.477 1.00 27.05  ? 131 TYR A CA   1 
ATOM   1988 C C    . TYR A 1 128 ? 11.828 54.079 16.634 1.00 26.61  ? 131 TYR A C    1 
ATOM   1989 O O    . TYR A 1 128 ? 12.311 53.753 17.714 1.00 26.83  ? 131 TYR A O    1 
ATOM   1990 C CB   . TYR A 1 128 ? 12.796 53.424 14.421 1.00 29.26  ? 131 TYR A CB   1 
ATOM   1991 C CG   . TYR A 1 128 ? 14.225 53.323 14.916 1.00 33.05  ? 131 TYR A CG   1 
ATOM   1992 C CD1  . TYR A 1 128 ? 14.733 52.123 15.367 1.00 35.70  ? 131 TYR A CD1  1 
ATOM   1993 C CD2  . TYR A 1 128 ? 15.059 54.440 14.901 1.00 35.97  ? 131 TYR A CD2  1 
ATOM   1994 C CE1  . TYR A 1 128 ? 16.050 52.027 15.814 1.00 37.90  ? 131 TYR A CE1  1 
ATOM   1995 C CE2  . TYR A 1 128 ? 16.381 54.352 15.350 1.00 36.53  ? 131 TYR A CE2  1 
ATOM   1996 C CZ   . TYR A 1 128 ? 16.860 53.143 15.797 1.00 46.79  ? 131 TYR A CZ   1 
ATOM   1997 O OH   . TYR A 1 128 ? 18.166 53.050 16.222 1.00 45.18  ? 131 TYR A OH   1 
ATOM   1998 H H    . TYR A 1 128 ? 10.445 53.259 13.989 0.00 33.89  ? 131 TYR A H    1 
ATOM   1999 H HA   . TYR A 1 128 ? 11.911 52.209 15.845 0.00 32.40  ? 131 TYR A HA   1 
ATOM   2000 H HB2  . TYR A 1 128 ? 12.697 52.808 13.679 0.00 35.12  ? 131 TYR A HB2  1 
ATOM   2001 H HB3  . TYR A 1 128 ? 12.653 54.335 14.118 0.00 35.12  ? 131 TYR A HB3  1 
ATOM   2002 H HD1  . TYR A 1 128 ? 14.190 51.368 15.373 0.00 42.85  ? 131 TYR A HD1  1 
ATOM   2003 H HD2  . TYR A 1 128 ? 14.732 55.253 14.590 0.00 43.18  ? 131 TYR A HD2  1 
ATOM   2004 H HE1  . TYR A 1 128 ? 16.380 51.214 16.122 0.00 45.49  ? 131 TYR A HE1  1 
ATOM   2005 H HE2  . TYR A 1 128 ? 16.930 55.103 15.346 0.00 43.85  ? 131 TYR A HE2  1 
ATOM   2006 H HH   . TYR A 1 128 ? 18.300 53.584 16.857 0.00 54.23  ? 131 TYR A HH   1 
ATOM   2007 N N    A SER A 1 129 ? 11.394 55.333 16.404 0.48 28.94  ? 132 SER A N    1 
ATOM   2008 N N    B SER A 1 129 ? 11.390 55.333 16.401 0.52 28.93  ? 132 SER A N    1 
ATOM   2009 C CA   A SER A 1 129 ? 11.571 56.329 17.452 0.48 26.96  ? 132 SER A CA   1 
ATOM   2010 C CA   B SER A 1 129 ? 11.541 56.340 17.445 0.52 27.00  ? 132 SER A CA   1 
ATOM   2011 C C    A SER A 1 129 ? 10.745 56.018 18.693 0.48 27.06  ? 132 SER A C    1 
ATOM   2012 C C    B SER A 1 129 ? 10.763 55.978 18.699 0.52 27.15  ? 132 SER A C    1 
ATOM   2013 O O    A SER A 1 129 ? 11.147 56.373 19.810 0.48 27.85  ? 132 SER A O    1 
ATOM   2014 O O    B SER A 1 129 ? 11.210 56.252 19.823 0.52 27.73  ? 132 SER A O    1 
ATOM   2015 C CB   A SER A 1 129 ? 11.208 57.713 16.906 0.48 32.64  ? 132 SER A CB   1 
ATOM   2016 C CB   B SER A 1 129 ? 11.082 57.701 16.914 0.52 32.48  ? 132 SER A CB   1 
ATOM   2017 O OG   A SER A 1 129 ? 9.822  57.818 16.715 0.48 33.94  ? 132 SER A OG   1 
ATOM   2018 O OG   B SER A 1 129 ? 11.951 58.140 15.895 0.52 35.93  ? 132 SER A OG   1 
ATOM   2019 H H    A SER A 1 129 ? 11.015 55.609 15.683 0.48 34.74  ? 132 SER A H    1 
ATOM   2020 H H    B SER A 1 129 ? 11.020 55.606 15.675 0.52 34.73  ? 132 SER A H    1 
ATOM   2021 H HA   A SER A 1 129 ? 12.503 56.335 17.721 0.48 32.37  ? 132 SER A HA   1 
ATOM   2022 H HA   B SER A 1 129 ? 12.479 56.396 17.686 0.52 32.42  ? 132 SER A HA   1 
ATOM   2023 H HB2  A SER A 1 129 ? 11.493 58.390 17.540 0.48 39.17  ? 132 SER A HB2  1 
ATOM   2024 H HB2  B SER A 1 129 ? 10.185 57.617 16.554 0.52 38.99  ? 132 SER A HB2  1 
ATOM   2025 H HB3  A SER A 1 129 ? 11.656 57.846 16.056 0.48 39.17  ? 132 SER A HB3  1 
ATOM   2026 H HB3  B SER A 1 129 ? 11.089 58.345 17.639 0.52 38.99  ? 132 SER A HB3  1 
ATOM   2027 H HG   A SER A 1 129 ? 9.637  58.549 16.347 0.48 40.74  ? 132 SER A HG   1 
ATOM   2028 H HG   B SER A 1 129 ? 11.664 58.855 15.560 0.52 43.12  ? 132 SER A HG   1 
ATOM   2029 N N    . TYR A 1 130 ? 9.609  55.343 18.537 1.00 25.84  ? 133 TYR A N    1 
ATOM   2030 C CA   . TYR A 1 130 ? 8.812  54.994 19.700 1.00 23.93  ? 133 TYR A CA   1 
ATOM   2031 C C    . TYR A 1 130 ? 9.469  53.929 20.573 1.00 24.74  ? 133 TYR A C    1 
ATOM   2032 O O    . TYR A 1 130 ? 9.140  53.820 21.752 1.00 24.13  ? 133 TYR A O    1 
ATOM   2033 C CB   . TYR A 1 130 ? 7.418  54.485 19.306 1.00 24.38  ? 133 TYR A CB   1 
ATOM   2034 C CG   . TYR A 1 130 ? 6.513  55.480 18.609 1.00 30.58  ? 133 TYR A CG   1 
ATOM   2035 C CD1  . TYR A 1 130 ? 6.803  56.825 18.618 1.00 31.27  ? 133 TYR A CD1  1 
ATOM   2036 C CD2  . TYR A 1 130 ? 5.381  55.047 17.970 1.00 31.40  ? 133 TYR A CD2  1 
ATOM   2037 C CE1  . TYR A 1 130 ? 5.981  57.732 17.969 1.00 36.70  ? 133 TYR A CE1  1 
ATOM   2038 C CE2  . TYR A 1 130 ? 4.536  55.936 17.330 1.00 32.40  ? 133 TYR A CE2  1 
ATOM   2039 C CZ   . TYR A 1 130 ? 4.854  57.278 17.332 1.00 38.43  ? 133 TYR A CZ   1 
ATOM   2040 O OH   . TYR A 1 130 ? 4.010  58.168 16.685 1.00 45.69  ? 133 TYR A OH   1 
ATOM   2041 H H    . TYR A 1 130 ? 9.275  55.110 17.779 0.00 31.02  ? 133 TYR A H    1 
ATOM   2042 H HA   . TYR A 1 130 ? 8.706  55.811 20.213 0.00 28.73  ? 133 TYR A HA   1 
ATOM   2043 H HB2  . TYR A 1 130 ? 7.530  53.732 18.706 0.00 29.27  ? 133 TYR A HB2  1 
ATOM   2044 H HB3  . TYR A 1 130 ? 6.961  54.201 20.114 0.00 29.27  ? 133 TYR A HB3  1 
ATOM   2045 H HD1  . TYR A 1 130 ? 7.560  57.128 19.065 0.00 37.54  ? 133 TYR A HD1  1 
ATOM   2046 H HD2  . TYR A 1 130 ? 5.178  54.139 17.966 0.00 37.69  ? 133 TYR A HD2  1 
ATOM   2047 H HE1  . TYR A 1 130 ? 6.191  58.638 17.965 0.00 44.05  ? 133 TYR A HE1  1 
ATOM   2048 H HE2  . TYR A 1 130 ? 3.767  55.633 16.904 0.00 38.89  ? 133 TYR A HE2  1 
ATOM   2049 H HH   . TYR A 1 130 ? 3.389  57.749 16.304 0.00 54.84  ? 133 TYR A HH   1 
ATOM   2050 N N    . ARG A 1 131 ? 10.373 53.108 20.009 1.00 21.80  ? 134 ARG A N    1 
ATOM   2051 C CA   . ARG A 1 131 ? 11.042 52.114 20.835 1.00 20.05  ? 134 ARG A CA   1 
ATOM   2052 C C    . ARG A 1 131 ? 11.740 52.769 22.025 1.00 26.51  ? 134 ARG A C    1 
ATOM   2053 O O    . ARG A 1 131 ? 11.796 52.194 23.125 1.00 22.77  ? 134 ARG A O    1 
ATOM   2054 C CB   . ARG A 1 131 ? 12.052 51.327 19.999 1.00 24.32  ? 134 ARG A CB   1 
ATOM   2055 C CG   . ARG A 1 131 ? 11.377 50.571 18.830 1.00 25.45  ? 134 ARG A CG   1 
ATOM   2056 C CD   . ARG A 1 131 ? 12.426 49.923 17.908 1.00 26.48  ? 134 ARG A CD   1 
ATOM   2057 N NE   . ARG A 1 131 ? 13.129 48.810 18.572 1.00 25.49  ? 134 ARG A NE   1 
ATOM   2058 C CZ   . ARG A 1 131 ? 12.651 47.574 18.653 1.00 28.21  ? 134 ARG A CZ   1 
ATOM   2059 N NH1  . ARG A 1 131 ? 11.458 47.252 18.148 1.00 24.70  ? 134 ARG A NH1  1 
ATOM   2060 N NH2  . ARG A 1 131 ? 13.391 46.628 19.238 1.00 29.17  ? 134 ARG A NH2  1 
ATOM   2061 H H    . ARG A 1 131 ? 10.602 53.113 19.181 0.00 26.17  ? 134 ARG A H    1 
ATOM   2062 H HA   . ARG A 1 131 ? 10.383 51.487 21.171 0.00 24.00  ? 134 ARG A HA   1 
ATOM   2063 H HB2  . ARG A 1 131 ? 12.704 51.942 19.626 0.00 29.20  ? 134 ARG A HB2  1 
ATOM   2064 H HB3  . ARG A 1 131 ? 12.496 50.677 20.565 0.00 29.20  ? 134 ARG A HB3  1 
ATOM   2065 H HG2  . ARG A 1 131 ? 10.807 49.872 19.185 0.00 30.56  ? 134 ARG A HG2  1 
ATOM   2066 H HG3  . ARG A 1 131 ? 10.851 51.194 18.304 0.00 30.56  ? 134 ARG A HG3  1 
ATOM   2067 H HD2  . ARG A 1 131 ? 11.985 49.574 17.118 0.00 31.79  ? 134 ARG A HD2  1 
ATOM   2068 H HD3  . ARG A 1 131 ? 13.084 50.589 17.655 0.00 31.79  ? 134 ARG A HD3  1 
ATOM   2069 H HE   . ARG A 1 131 ? 13.895 48.971 18.928 0.00 30.60  ? 134 ARG A HE   1 
ATOM   2070 H HH11 . ARG A 1 131 ? 10.979 47.851 17.759 0.00 29.58  ? 134 ARG A HH11 1 
ATOM   2071 H HH12 . ARG A 1 131 ? 11.168 46.445 18.211 0.00 29.58  ? 134 ARG A HH12 1 
ATOM   2072 H HH21 . ARG A 1 131 ? 14.166 46.823 19.556 0.00 35.02  ? 134 ARG A HH21 1 
ATOM   2073 H HH22 . ARG A 1 131 ? 13.092 45.824 19.296 0.00 35.02  ? 134 ARG A HH22 1 
ATOM   2074 N N    . PHE A 1 132 ? 12.273 53.979 21.823 1.00 22.14  ? 135 PHE A N    1 
ATOM   2075 C CA   . PHE A 1 132 ? 13.026 54.630 22.879 1.00 22.33  ? 135 PHE A CA   1 
ATOM   2076 C C    . PHE A 1 132 ? 12.126 55.323 23.894 1.00 25.57  ? 135 PHE A C    1 
ATOM   2077 O O    . PHE A 1 132 ? 12.564 55.548 25.023 1.00 22.41  ? 135 PHE A O    1 
ATOM   2078 C CB   . PHE A 1 132 ? 13.996 55.632 22.234 1.00 24.18  ? 135 PHE A CB   1 
ATOM   2079 C CG   . PHE A 1 132 ? 14.961 54.947 21.293 1.00 23.25  ? 135 PHE A CG   1 
ATOM   2080 C CD1  . PHE A 1 132 ? 16.027 54.222 21.810 1.00 28.64  ? 135 PHE A CD1  1 
ATOM   2081 C CD2  . PHE A 1 132 ? 14.762 55.006 19.933 1.00 28.83  ? 135 PHE A CD2  1 
ATOM   2082 C CE1  . PHE A 1 132 ? 16.915 53.579 20.944 1.00 32.47  ? 135 PHE A CE1  1 
ATOM   2083 C CE2  . PHE A 1 132 ? 15.642 54.367 19.065 1.00 32.91  ? 135 PHE A CE2  1 
ATOM   2084 C CZ   . PHE A 1 132 ? 16.723 53.647 19.590 1.00 31.31  ? 135 PHE A CZ   1 
ATOM   2085 H H    . PHE A 1 132 ? 12.209 54.430 21.094 0.00 26.58  ? 135 PHE A H    1 
ATOM   2086 H HA   . PHE A 1 132 ? 13.547 53.977 23.372 0.00 26.81  ? 135 PHE A HA   1 
ATOM   2087 H HB2  . PHE A 1 132 ? 13.491 56.288 21.729 0.00 29.03  ? 135 PHE A HB2  1 
ATOM   2088 H HB3  . PHE A 1 132 ? 14.510 56.073 22.929 0.00 29.03  ? 135 PHE A HB3  1 
ATOM   2089 H HD1  . PHE A 1 132 ? 16.150 54.165 22.730 0.00 34.38  ? 135 PHE A HD1  1 
ATOM   2090 H HD2  . PHE A 1 132 ? 14.036 55.475 19.592 0.00 34.60  ? 135 PHE A HD2  1 
ATOM   2091 H HE1  . PHE A 1 132 ? 17.637 53.104 21.287 0.00 38.98  ? 135 PHE A HE1  1 
ATOM   2092 H HE2  . PHE A 1 132 ? 15.514 54.417 18.146 0.00 39.50  ? 135 PHE A HE2  1 
ATOM   2093 H HZ   . PHE A 1 132 ? 17.313 53.214 19.017 0.00 37.59  ? 135 PHE A HZ   1 
ATOM   2094 N N    . VAL A 1 133 ? 10.896 55.627 23.535 1.00 21.54  ? 136 VAL A N    1 
ATOM   2095 C CA   . VAL A 1 133 ? 9.915  56.111 24.507 1.00 21.45  ? 136 VAL A CA   1 
ATOM   2096 C C    . VAL A 1 133 ? 9.651  55.033 25.529 1.00 22.56  ? 136 VAL A C    1 
ATOM   2097 O O    . VAL A 1 133 ? 9.657  55.260 26.730 1.00 22.12  ? 136 VAL A O    1 
ATOM   2098 C CB   . VAL A 1 133 ? 8.613  56.542 23.812 1.00 25.55  ? 136 VAL A CB   1 
ATOM   2099 C CG1  . VAL A 1 133 ? 7.546  56.936 24.841 1.00 28.38  ? 136 VAL A CG1  1 
ATOM   2100 C CG2  . VAL A 1 133 ? 8.904  57.722 22.864 1.00 29.69  ? 136 VAL A CG2  1 
ATOM   2101 H H    . VAL A 1 133 ? 10.593 55.565 22.732 0.00 25.85  ? 136 VAL A H    1 
ATOM   2102 H HA   . VAL A 1 133 ? 10.280 56.892 24.952 0.00 25.75  ? 136 VAL A HA   1 
ATOM   2103 H HB   . VAL A 1 133 ? 8.266  55.796 23.299 0.00 30.67  ? 136 VAL A HB   1 
ATOM   2104 H HG11 . VAL A 1 133 ? 6.820  57.390 24.385 0.00 34.07  ? 136 VAL A HG11 1 
ATOM   2105 H HG12 . VAL A 1 133 ? 7.214  56.134 25.274 0.00 34.07  ? 136 VAL A HG12 1 
ATOM   2106 H HG13 . VAL A 1 133 ? 7.945  57.527 25.499 0.00 34.07  ? 136 VAL A HG13 1 
ATOM   2107 H HG21 . VAL A 1 133 ? 8.075  58.002 22.445 0.00 35.64  ? 136 VAL A HG21 1 
ATOM   2108 H HG22 . VAL A 1 133 ? 9.279  58.455 23.378 0.00 35.64  ? 136 VAL A HG22 1 
ATOM   2109 H HG23 . VAL A 1 133 ? 9.536  57.435 22.187 0.00 35.64  ? 136 VAL A HG23 1 
ATOM   2110 N N    . TRP A 1 134 ? 9.454  53.787 25.048 1.00 20.15  ? 137 TRP A N    1 
ATOM   2111 C CA   . TRP A 1 134 ? 9.202  52.698 25.983 1.00 18.79  ? 137 TRP A CA   1 
ATOM   2112 C C    . TRP A 1 134 ? 10.445 52.413 26.815 1.00 20.81  ? 137 TRP A C    1 
ATOM   2113 O O    . TRP A 1 134 ? 10.336 52.082 27.995 1.00 21.83  ? 137 TRP A O    1 
ATOM   2114 C CB   . TRP A 1 134 ? 8.774  51.442 25.213 1.00 17.35  ? 137 TRP A CB   1 
ATOM   2115 C CG   . TRP A 1 134 ? 7.443  51.659 24.572 1.00 17.72  ? 137 TRP A CG   1 
ATOM   2116 C CD1  . TRP A 1 134 ? 7.154  51.793 23.239 1.00 22.08  ? 137 TRP A CD1  1 
ATOM   2117 C CD2  . TRP A 1 134 ? 6.189  51.789 25.270 1.00 21.29  ? 137 TRP A CD2  1 
ATOM   2118 N NE1  . TRP A 1 134 ? 5.821  52.023 23.052 1.00 21.49  ? 137 TRP A NE1  1 
ATOM   2119 C CE2  . TRP A 1 134 ? 5.181  51.990 24.292 1.00 20.02  ? 137 TRP A CE2  1 
ATOM   2120 C CE3  . TRP A 1 134 ? 5.814  51.741 26.620 1.00 24.16  ? 137 TRP A CE3  1 
ATOM   2121 C CZ2  . TRP A 1 134 ? 3.850  52.170 24.614 1.00 25.17  ? 137 TRP A CZ2  1 
ATOM   2122 C CZ3  . TRP A 1 134 ? 4.475  51.898 26.929 1.00 25.78  ? 137 TRP A CZ3  1 
ATOM   2123 C CH2  . TRP A 1 134 ? 3.506  52.118 25.938 1.00 26.45  ? 137 TRP A CH2  1 
ATOM   2124 H H    . TRP A 1 134 ? 9.464  53.565 24.217 0.00 24.20  ? 137 TRP A H    1 
ATOM   2125 H HA   . TRP A 1 134 ? 8.480  52.946 26.581 0.00 22.56  ? 137 TRP A HA   1 
ATOM   2126 H HB2  . TRP A 1 134 ? 9.425  51.247 24.521 0.00 20.83  ? 137 TRP A HB2  1 
ATOM   2127 H HB3  . TRP A 1 134 ? 8.706  50.693 25.825 0.00 20.83  ? 137 TRP A HB3  1 
ATOM   2128 H HD1  . TRP A 1 134 ? 7.781  51.734 22.555 0.00 26.51  ? 137 TRP A HD1  1 
ATOM   2129 H HE1  . TRP A 1 134 ? 5.439  52.166 22.295 0.00 25.80  ? 137 TRP A HE1  1 
ATOM   2130 H HE3  . TRP A 1 134 ? 6.447  51.608 27.288 0.00 29.00  ? 137 TRP A HE3  1 
ATOM   2131 H HZ2  . TRP A 1 134 ? 3.211  52.321 23.955 0.00 30.22  ? 137 TRP A HZ2  1 
ATOM   2132 H HZ3  . TRP A 1 134 ? 4.209  51.856 27.819 0.00 30.95  ? 137 TRP A HZ3  1 
ATOM   2133 H HH2  . TRP A 1 134 ? 2.617  52.230 26.185 0.00 31.76  ? 137 TRP A HH2  1 
ATOM   2134 N N    . TRP A 1 135 ? 11.633 52.485 26.202 1.00 18.81  ? 138 TRP A N    1 
ATOM   2135 C CA   . TRP A 1 135 ? 12.855 52.304 26.984 1.00 16.67  ? 138 TRP A CA   1 
ATOM   2136 C C    . TRP A 1 135 ? 12.944 53.316 28.114 1.00 22.26  ? 138 TRP A C    1 
ATOM   2137 O O    . TRP A 1 135 ? 13.390 52.976 29.227 1.00 21.59  ? 138 TRP A O    1 
ATOM   2138 C CB   . TRP A 1 135 ? 14.067 52.429 26.023 1.00 20.95  ? 138 TRP A CB   1 
ATOM   2139 C CG   . TRP A 1 135 ? 15.418 52.355 26.719 1.00 20.90  ? 138 TRP A CG   1 
ATOM   2140 C CD1  . TRP A 1 135 ? 16.179 51.217 26.919 1.00 20.66  ? 138 TRP A CD1  1 
ATOM   2141 C CD2  . TRP A 1 135 ? 16.143 53.431 27.297 1.00 21.50  ? 138 TRP A CD2  1 
ATOM   2142 N NE1  . TRP A 1 135 ? 17.341 51.547 27.571 1.00 24.48  ? 138 TRP A NE1  1 
ATOM   2143 C CE2  . TRP A 1 135 ? 17.337 52.896 27.833 1.00 24.32  ? 138 TRP A CE2  1 
ATOM   2144 C CE3  . TRP A 1 135 ? 15.913 54.810 27.404 1.00 25.29  ? 138 TRP A CE3  1 
ATOM   2145 C CZ2  . TRP A 1 135 ? 18.300 53.690 28.452 1.00 30.12  ? 138 TRP A CZ2  1 
ATOM   2146 C CZ3  . TRP A 1 135 ? 16.860 55.589 28.045 1.00 28.23  ? 138 TRP A CZ3  1 
ATOM   2147 C CH2  . TRP A 1 135 ? 18.037 55.034 28.551 1.00 29.58  ? 138 TRP A CH2  1 
ATOM   2148 H H    . TRP A 1 135 ? 11.753 52.633 25.364 0.00 22.59  ? 138 TRP A H    1 
ATOM   2149 H HA   . TRP A 1 135 ? 12.864 51.424 27.391 0.00 20.02  ? 138 TRP A HA   1 
ATOM   2150 H HB2  . TRP A 1 135 ? 14.028 51.707 25.377 0.00 25.15  ? 138 TRP A HB2  1 
ATOM   2151 H HB3  . TRP A 1 135 ? 14.016 53.284 25.568 0.00 25.15  ? 138 TRP A HB3  1 
ATOM   2152 H HD1  . TRP A 1 135 ? 15.939 50.359 26.652 0.00 24.80  ? 138 TRP A HD1  1 
ATOM   2153 H HE1  . TRP A 1 135 ? 17.969 50.999 27.781 0.00 29.39  ? 138 TRP A HE1  1 
ATOM   2154 H HE3  . TRP A 1 135 ? 15.142 55.192 27.052 0.00 30.36  ? 138 TRP A HE3  1 
ATOM   2155 H HZ2  . TRP A 1 135 ? 19.088 53.324 28.785 0.00 36.15  ? 138 TRP A HZ2  1 
ATOM   2156 H HZ3  . TRP A 1 135 ? 16.709 56.502 28.140 0.00 33.89  ? 138 TRP A HZ3  1 
ATOM   2157 H HH2  . TRP A 1 135 ? 18.658 55.588 28.966 0.00 35.50  ? 138 TRP A HH2  1 
ATOM   2158 N N    . ALA A 1 136 ? 12.511 54.552 27.874 1.00 22.14  ? 139 ALA A N    1 
ATOM   2159 C CA   . ALA A 1 136 ? 12.636 55.576 28.935 1.00 23.40  ? 139 ALA A CA   1 
ATOM   2160 C C    . ALA A 1 136 ? 11.658 55.322 30.072 1.00 24.21  ? 139 ALA A C    1 
ATOM   2161 O O    . ALA A 1 136 ? 12.007 55.483 31.239 1.00 23.74  ? 139 ALA A O    1 
ATOM   2162 C CB   . ALA A 1 136 ? 12.407 56.967 28.342 1.00 23.19  ? 139 ALA A CB   1 
ATOM   2163 H H    . ALA A 1 136 ? 12.155 54.823 27.140 0.00 26.58  ? 139 ALA A H    1 
ATOM   2164 H HA   . ALA A 1 136 ? 13.535 55.539 29.298 0.00 28.10  ? 139 ALA A HA   1 
ATOM   2165 H HB1  . ALA A 1 136 ? 12.492 57.628 29.045 0.00 27.83  ? 139 ALA A HB1  1 
ATOM   2166 H HB2  . ALA A 1 136 ? 13.070 57.129 27.652 0.00 27.83  ? 139 ALA A HB2  1 
ATOM   2167 H HB3  . ALA A 1 136 ? 11.516 57.004 27.959 0.00 27.83  ? 139 ALA A HB3  1 
ATOM   2168 N N    . ILE A 1 137 ? 10.419 54.890 29.756 1.00 19.00  ? 140 ILE A N    1 
ATOM   2169 C CA   . ILE A 1 137 ? 9.460  54.577 30.820 1.00 20.76  ? 140 ILE A CA   1 
ATOM   2170 C C    . ILE A 1 137 ? 9.959  53.390 31.636 1.00 23.68  ? 140 ILE A C    1 
ATOM   2171 O O    . ILE A 1 137 ? 9.847  53.360 32.864 1.00 24.04  ? 140 ILE A O    1 
ATOM   2172 C CB   . ILE A 1 137 ? 8.073  54.324 30.191 1.00 23.99  ? 140 ILE A CB   1 
ATOM   2173 C CG1  . ILE A 1 137 ? 7.509  55.602 29.637 1.00 25.47  ? 140 ILE A CG1  1 
ATOM   2174 C CG2  . ILE A 1 137 ? 7.135  53.673 31.242 1.00 26.90  ? 140 ILE A CG2  1 
ATOM   2175 C CD1  . ILE A 1 137 ? 6.356  55.373 28.653 1.00 30.92  ? 140 ILE A CD1  1 
ATOM   2176 H H    . ILE A 1 137 ? 10.124 54.775 28.956 0.00 22.81  ? 140 ILE A H    1 
ATOM   2177 H HA   . ILE A 1 137 ? 9.379  55.328 31.428 0.00 24.92  ? 140 ILE A HA   1 
ATOM   2178 H HB   . ILE A 1 137 ? 8.160  53.708 29.447 0.00 28.80  ? 140 ILE A HB   1 
ATOM   2179 H HG12 . ILE A 1 137 ? 7.174  56.142 30.370 0.00 30.58  ? 140 ILE A HG12 1 
ATOM   2180 H HG13 . ILE A 1 137 ? 8.212  56.079 29.169 0.00 30.58  ? 140 ILE A HG13 1 
ATOM   2181 H HG21 . ILE A 1 137 ? 6.216  53.769 30.947 0.00 32.29  ? 140 ILE A HG21 1 
ATOM   2182 H HG22 . ILE A 1 137 ? 7.359  52.732 31.324 0.00 32.29  ? 140 ILE A HG22 1 
ATOM   2183 H HG23 . ILE A 1 137 ? 7.258  54.118 32.094 0.00 32.29  ? 140 ILE A HG23 1 
ATOM   2184 H HD11 . ILE A 1 137 ? 6.087  56.226 28.277 0.00 37.11  ? 140 ILE A HD11 1 
ATOM   2185 H HD12 . ILE A 1 137 ? 6.657  54.781 27.946 0.00 37.11  ? 140 ILE A HD12 1 
ATOM   2186 H HD13 . ILE A 1 137 ? 5.611  54.971 29.127 0.00 37.11  ? 140 ILE A HD13 1 
ATOM   2187 N N    . SER A 1 138 ? 10.502 52.349 30.967 1.00 19.33  ? 141 SER A N    1 
ATOM   2188 C CA   . SER A 1 138 ? 10.982 51.185 31.688 1.00 20.54  ? 141 SER A CA   1 
ATOM   2189 C C    . SER A 1 138 ? 12.154 51.559 32.577 1.00 23.00  ? 141 SER A C    1 
ATOM   2190 O O    . SER A 1 138 ? 12.275 51.064 33.716 1.00 21.27  ? 141 SER A O    1 
ATOM   2191 C CB   . SER A 1 138 ? 11.395 50.124 30.653 1.00 20.48  ? 141 SER A CB   1 
ATOM   2192 O OG   . SER A 1 138 ? 11.970 48.974 31.241 1.00 20.54  ? 141 SER A OG   1 
ATOM   2193 H H    . SER A 1 138 ? 10.595 52.306 30.113 0.00 23.21  ? 141 SER A H    1 
ATOM   2194 H HA   . SER A 1 138 ? 10.286 50.820 32.256 0.00 24.66  ? 141 SER A HA   1 
ATOM   2195 H HB2  . SER A 1 138 ? 10.605 49.854 30.158 0.00 24.59  ? 141 SER A HB2  1 
ATOM   2196 H HB3  . SER A 1 138 ? 12.044 50.519 30.050 0.00 24.59  ? 141 SER A HB3  1 
ATOM   2197 H HG   . SER A 1 138 ? 11.421 48.615 31.765 0.00 24.66  ? 141 SER A HG   1 
ATOM   2198 N N    . THR A 1 139 ? 13.037 52.390 32.075 1.00 18.22  ? 142 THR A N    1 
ATOM   2199 C CA   . THR A 1 139 ? 14.208 52.831 32.867 1.00 20.34  ? 142 THR A CA   1 
ATOM   2200 C C    . THR A 1 139 ? 13.742 53.640 34.083 1.00 25.25  ? 142 THR A C    1 
ATOM   2201 O O    . THR A 1 139 ? 14.326 53.517 35.171 1.00 24.31  ? 142 THR A O    1 
ATOM   2202 C CB   . THR A 1 139 ? 15.161 53.631 31.978 1.00 23.01  ? 142 THR A CB   1 
ATOM   2203 O OG1  . THR A 1 139 ? 15.703 52.765 30.971 1.00 23.72  ? 142 THR A OG1  1 
ATOM   2204 C CG2  . THR A 1 139 ? 16.336 54.171 32.814 1.00 28.17  ? 142 THR A CG2  1 
ATOM   2205 H H    . THR A 1 139 ? 13.001 52.724 31.283 0.00 21.87  ? 142 THR A H    1 
ATOM   2206 H HA   . THR A 1 139 ? 14.705 52.064 33.193 0.00 24.42  ? 142 THR A HA   1 
ATOM   2207 H HB   . THR A 1 139 ? 14.682 54.371 31.573 0.00 27.63  ? 142 THR A HB   1 
ATOM   2208 H HG1  . THR A 1 139 ? 15.083 52.441 30.507 0.00 28.47  ? 142 THR A HG1  1 
ATOM   2209 H HG21 . THR A 1 139 ? 17.030 54.513 32.229 0.00 33.82  ? 142 THR A HG21 1 
ATOM   2210 H HG22 . THR A 1 139 ? 16.030 54.888 33.392 0.00 33.82  ? 142 THR A HG22 1 
ATOM   2211 H HG23 . THR A 1 139 ? 16.707 53.462 33.362 0.00 33.82  ? 142 THR A HG23 1 
ATOM   2212 N N    . ALA A 1 140 ? 12.709 54.465 33.931 1.00 24.01  ? 143 ALA A N    1 
ATOM   2213 C CA   . ALA A 1 140 ? 12.182 55.178 35.091 1.00 24.01  ? 143 ALA A CA   1 
ATOM   2214 C C    . ALA A 1 140 ? 11.644 54.210 36.150 1.00 25.50  ? 143 ALA A C    1 
ATOM   2215 O O    . ALA A 1 140 ? 11.827 54.453 37.356 1.00 27.49  ? 143 ALA A O    1 
ATOM   2216 C CB   . ALA A 1 140 ? 11.074 56.168 34.652 1.00 26.49  ? 143 ALA A CB   1 
ATOM   2217 H H    . ALA A 1 140 ? 12.306 54.625 33.189 0.00 28.83  ? 143 ALA A H    1 
ATOM   2218 H HA   . ALA A 1 140 ? 12.903 55.689 35.491 0.00 28.83  ? 143 ALA A HA   1 
ATOM   2219 H HB1  . ALA A 1 140 ? 10.770 56.665 35.427 0.00 31.80  ? 143 ALA A HB1  1 
ATOM   2220 H HB2  . ALA A 1 140 ? 11.439 56.777 33.990 0.00 31.80  ? 143 ALA A HB2  1 
ATOM   2221 H HB3  . ALA A 1 140 ? 10.337 55.667 34.269 0.00 31.80  ? 143 ALA A HB3  1 
ATOM   2222 N N    . ALA A 1 141 ? 10.984 53.136 35.734 1.00 20.61  ? 144 ALA A N    1 
ATOM   2223 C CA   . ALA A 1 141 ? 10.521 52.131 36.696 1.00 20.97  ? 144 ALA A CA   1 
ATOM   2224 C C    . ALA A 1 141 ? 11.711 51.469 37.395 1.00 23.57  ? 144 ALA A C    1 
ATOM   2225 O O    . ALA A 1 141 ? 11.665 51.215 38.613 1.00 23.87  ? 144 ALA A O    1 
ATOM   2226 C CB   . ALA A 1 141 ? 9.670  51.051 35.987 1.00 19.12  ? 144 ALA A CB   1 
ATOM   2227 H H    . ALA A 1 141 ? 10.791 52.964 34.914 0.00 24.74  ? 144 ALA A H    1 
ATOM   2228 H HA   . ALA A 1 141 ? 9.962  52.568 37.357 0.00 25.17  ? 144 ALA A HA   1 
ATOM   2229 H HB1  . ALA A 1 141 ? 9.376  50.400 36.642 0.00 22.96  ? 144 ALA A HB1  1 
ATOM   2230 H HB2  . ALA A 1 141 ? 8.901  51.476 35.574 0.00 22.96  ? 144 ALA A HB2  1 
ATOM   2231 H HB3  . ALA A 1 141 ? 10.211 50.618 35.309 0.00 22.96  ? 144 ALA A HB3  1 
ATOM   2232 N N    . MET A 1 142 ? 12.789 51.181 36.642 1.00 23.05  ? 145 MET A N    1 
ATOM   2233 C CA   . MET A 1 142 ? 13.969 50.602 37.279 1.00 22.16  ? 145 MET A CA   1 
ATOM   2234 C C    . MET A 1 142 ? 14.562 51.565 38.312 1.00 23.56  ? 145 MET A C    1 
ATOM   2235 O O    . MET A 1 142 ? 15.000 51.124 39.361 1.00 26.72  ? 145 MET A O    1 
ATOM   2236 C CB   . MET A 1 142 ? 15.068 50.308 36.223 1.00 23.64  ? 145 MET A CB   1 
ATOM   2237 C CG   . MET A 1 142 ? 16.258 49.558 36.848 1.00 26.09  ? 145 MET A CG   1 
ATOM   2238 S SD   . MET A 1 142 ? 17.640 49.352 35.709 1.00 30.10  ? 145 MET A SD   1 
ATOM   2239 C CE   . MET A 1 142 ? 18.491 50.868 35.918 1.00 37.65  ? 145 MET A CE   1 
ATOM   2240 H H    . MET A 1 142 ? 12.854 51.308 35.794 0.00 27.67  ? 145 MET A H    1 
ATOM   2241 H HA   . MET A 1 142 ? 13.695 49.772 37.698 0.00 26.60  ? 145 MET A HA   1 
ATOM   2242 H HB2  . MET A 1 142 ? 14.695 49.757 35.517 0.00 28.38  ? 145 MET A HB2  1 
ATOM   2243 H HB3  . MET A 1 142 ? 15.392 51.145 35.855 0.00 28.38  ? 145 MET A HB3  1 
ATOM   2244 H HG2  . MET A 1 142 ? 16.577 50.057 37.616 0.00 31.32  ? 145 MET A HG2  1 
ATOM   2245 H HG3  . MET A 1 142 ? 15.965 48.676 37.123 0.00 31.32  ? 145 MET A HG3  1 
ATOM   2246 H HE1  . MET A 1 142 ? 19.234 50.901 35.296 0.00 45.20  ? 145 MET A HE1  1 
ATOM   2247 H HE2  . MET A 1 142 ? 17.879 51.600 35.743 0.00 45.20  ? 145 MET A HE2  1 
ATOM   2248 H HE3  . MET A 1 142 ? 18.820 50.923 36.829 0.00 45.20  ? 145 MET A HE3  1 
ATOM   2249 N N    . LEU A 1 143 ? 14.614 52.861 37.999 1.00 22.14  ? 146 LEU A N    1 
ATOM   2250 C CA   . LEU A 1 143 ? 15.188 53.808 38.965 1.00 27.33  ? 146 LEU A CA   1 
ATOM   2251 C C    . LEU A 1 143 ? 14.357 53.873 40.243 1.00 28.95  ? 146 LEU A C    1 
ATOM   2252 O O    . LEU A 1 143 ? 14.909 54.067 41.335 1.00 29.08  ? 146 LEU A O    1 
ATOM   2253 C CB   . LEU A 1 143 ? 15.329 55.193 38.336 1.00 27.58  ? 146 LEU A CB   1 
ATOM   2254 C CG   . LEU A 1 143 ? 16.350 55.244 37.193 1.00 36.48  ? 146 LEU A CG   1 
ATOM   2255 C CD1  . LEU A 1 143 ? 16.297 56.599 36.486 1.00 36.67  ? 146 LEU A CD1  1 
ATOM   2256 C CD2  . LEU A 1 143 ? 17.768 54.986 37.715 1.00 36.34  ? 146 LEU A CD2  1 
ATOM   2257 H H    . LEU A 1 143 ? 14.335 53.208 37.263 0.00 26.58  ? 146 LEU A H    1 
ATOM   2258 H HA   . LEU A 1 143 ? 16.079 53.508 39.204 0.00 32.80  ? 146 LEU A HA   1 
ATOM   2259 H HB2  . LEU A 1 143 ? 14.468 55.463 37.980 0.00 33.11  ? 146 LEU A HB2  1 
ATOM   2260 H HB3  . LEU A 1 143 ? 15.616 55.819 39.020 0.00 33.11  ? 146 LEU A HB3  1 
ATOM   2261 H HG   . LEU A 1 143 ? 16.128 54.550 36.553 0.00 43.79  ? 146 LEU A HG   1 
ATOM   2262 H HD11 . LEU A 1 143 ? 16.965 56.614 35.782 0.00 44.02  ? 146 LEU A HD11 1 
ATOM   2263 H HD12 . LEU A 1 143 ? 15.413 56.723 36.107 0.00 44.02  ? 146 LEU A HD12 1 
ATOM   2264 H HD13 . LEU A 1 143 ? 16.482 57.299 37.132 0.00 44.02  ? 146 LEU A HD13 1 
ATOM   2265 H HD21 . LEU A 1 143 ? 18.406 55.209 37.019 0.00 43.63  ? 146 LEU A HD21 1 
ATOM   2266 H HD22 . LEU A 1 143 ? 17.923 55.541 38.495 0.00 43.63  ? 146 LEU A HD22 1 
ATOM   2267 H HD23 . LEU A 1 143 ? 17.851 54.049 37.953 0.00 43.63  ? 146 LEU A HD23 1 
ATOM   2268 N N    . TYR A 1 144 ? 13.036 53.718 40.131 1.00 24.55  ? 147 TYR A N    1 
ATOM   2269 C CA   . TYR A 1 144 ? 12.227 53.617 41.339 1.00 25.43  ? 147 TYR A CA   1 
ATOM   2270 C C    . TYR A 1 144 ? 12.628 52.407 42.170 1.00 25.88  ? 147 TYR A C    1 
ATOM   2271 O O    . TYR A 1 144 ? 12.777 52.489 43.383 1.00 27.80  ? 147 TYR A O    1 
ATOM   2272 C CB   . TYR A 1 144 ? 10.729 53.552 40.968 1.00 26.15  ? 147 TYR A CB   1 
ATOM   2273 C CG   . TYR A 1 144 ? 9.856  53.367 42.173 1.00 29.10  ? 147 TYR A CG   1 
ATOM   2274 C CD1  . TYR A 1 144 ? 9.508  54.459 42.964 1.00 33.60  ? 147 TYR A CD1  1 
ATOM   2275 C CD2  . TYR A 1 144 ? 9.428  52.113 42.560 1.00 33.34  ? 147 TYR A CD2  1 
ATOM   2276 C CE1  . TYR A 1 144 ? 8.718  54.292 44.083 1.00 34.78  ? 147 TYR A CE1  1 
ATOM   2277 C CE2  . TYR A 1 144 ? 8.642  51.936 43.685 1.00 35.85  ? 147 TYR A CE2  1 
ATOM   2278 C CZ   . TYR A 1 144 ? 8.293  53.038 44.440 1.00 36.15  ? 147 TYR A CZ   1 
ATOM   2279 O OH   . TYR A 1 144 ? 7.514  52.882 45.570 1.00 47.88  ? 147 TYR A OH   1 
ATOM   2280 H H    . TYR A 1 144 ? 12.601 53.671 39.391 0.00 29.47  ? 147 TYR A H    1 
ATOM   2281 H HA   . TYR A 1 144 ? 12.370 54.411 41.878 0.00 30.52  ? 147 TYR A HA   1 
ATOM   2282 H HB2  . TYR A 1 144 ? 10.473 54.381 40.533 0.00 31.39  ? 147 TYR A HB2  1 
ATOM   2283 H HB3  . TYR A 1 144 ? 10.582 52.804 40.369 0.00 31.39  ? 147 TYR A HB3  1 
ATOM   2284 H HD1  . TYR A 1 144 ? 9.810  55.309 42.736 0.00 40.34  ? 147 TYR A HD1  1 
ATOM   2285 H HD2  . TYR A 1 144 ? 9.673  51.372 42.054 0.00 40.02  ? 147 TYR A HD2  1 
ATOM   2286 H HE1  . TYR A 1 144 ? 8.475  55.029 44.596 0.00 41.75  ? 147 TYR A HE1  1 
ATOM   2287 H HE2  . TYR A 1 144 ? 8.353  51.087 43.930 0.00 43.03  ? 147 TYR A HE2  1 
ATOM   2288 H HH   . TYR A 1 144 ? 7.375  52.066 45.712 0.00 57.47  ? 147 TYR A HH   1 
ATOM   2289 N N    . ILE A 1 145 ? 12.814 51.244 41.506 1.00 22.94  ? 148 ILE A N    1 
ATOM   2290 C CA   . ILE A 1 145 ? 13.204 50.049 42.252 1.00 22.58  ? 148 ILE A CA   1 
ATOM   2291 C C    . ILE A 1 145 ? 14.547 50.276 42.953 1.00 25.28  ? 148 ILE A C    1 
ATOM   2292 O O    . ILE A 1 145 ? 14.709 49.956 44.136 1.00 27.83  ? 148 ILE A O    1 
ATOM   2293 C CB   . ILE A 1 145 ? 13.277 48.838 41.291 1.00 24.41  ? 148 ILE A CB   1 
ATOM   2294 C CG1  . ILE A 1 145 ? 11.853 48.461 40.898 1.00 24.43  ? 148 ILE A CG1  1 
ATOM   2295 C CG2  . ILE A 1 145 ? 13.978 47.656 41.948 1.00 27.87  ? 148 ILE A CG2  1 
ATOM   2296 C CD1  . ILE A 1 145 ? 11.785 47.580 39.617 1.00 29.35  ? 148 ILE A CD1  1 
ATOM   2297 H H    . ILE A 1 145 ? 12.722 51.135 40.658 0.00 27.55  ? 148 ILE A H    1 
ATOM   2298 H HA   . ILE A 1 145 ? 12.537 49.871 42.933 0.00 27.10  ? 148 ILE A HA   1 
ATOM   2299 H HB   . ILE A 1 145 ? 13.792 49.079 40.506 0.00 29.30  ? 148 ILE A HB   1 
ATOM   2300 H HG12 . ILE A 1 145 ? 11.448 47.963 41.625 0.00 29.32  ? 148 ILE A HG12 1 
ATOM   2301 H HG13 . ILE A 1 145 ? 11.348 49.272 40.730 0.00 29.32  ? 148 ILE A HG13 1 
ATOM   2302 H HG21 . ILE A 1 145 ? 13.757 46.847 41.460 0.00 33.46  ? 148 ILE A HG21 1 
ATOM   2303 H HG22 . ILE A 1 145 ? 14.936 47.805 41.926 0.00 33.46  ? 148 ILE A HG22 1 
ATOM   2304 H HG23 . ILE A 1 145 ? 13.676 47.581 42.867 0.00 33.46  ? 148 ILE A HG23 1 
ATOM   2305 H HD11 . ILE A 1 145 ? 10.856 47.465 39.362 0.00 35.23  ? 148 ILE A HD11 1 
ATOM   2306 H HD12 . ILE A 1 145 ? 12.272 48.022 38.904 0.00 35.23  ? 148 ILE A HD12 1 
ATOM   2307 H HD13 . ILE A 1 145 ? 12.185 46.717 39.806 0.00 35.23  ? 148 ILE A HD13 1 
ATOM   2308 N N    . LEU A 1 146 ? 15.532 50.810 42.227 1.00 27.68  ? 149 LEU A N    1 
ATOM   2309 C CA   . LEU A 1 146 ? 16.854 50.992 42.831 1.00 27.35  ? 149 LEU A CA   1 
ATOM   2310 C C    . LEU A 1 146 ? 16.791 51.972 44.001 1.00 38.20  ? 149 LEU A C    1 
ATOM   2311 O O    . LEU A 1 146 ? 17.502 51.802 45.003 1.00 32.79  ? 149 LEU A O    1 
ATOM   2312 C CB   . LEU A 1 146 ? 17.861 51.472 41.784 1.00 30.00  ? 149 LEU A CB   1 
ATOM   2313 C CG   . LEU A 1 146 ? 18.040 50.542 40.575 1.00 33.50  ? 149 LEU A CG   1 
ATOM   2314 C CD1  . LEU A 1 146 ? 19.222 51.040 39.727 1.00 44.71  ? 149 LEU A CD1  1 
ATOM   2315 C CD2  . LEU A 1 146 ? 18.244 49.096 40.984 1.00 45.98  ? 149 LEU A CD2  1 
ATOM   2316 H H    . LEU A 1 146 ? 15.463 51.066 41.409 0.00 33.23  ? 149 LEU A H    1 
ATOM   2317 H HA   . LEU A 1 146 ? 17.162 50.136 43.166 0.00 32.83  ? 149 LEU A HA   1 
ATOM   2318 H HB2  . LEU A 1 146 ? 17.565 52.332 41.448 0.00 36.01  ? 149 LEU A HB2  1 
ATOM   2319 H HB3  . LEU A 1 146 ? 18.727 51.562 42.212 0.00 36.01  ? 149 LEU A HB3  1 
ATOM   2320 H HG   . LEU A 1 146 ? 17.229 50.560 40.043 0.00 40.21  ? 149 LEU A HG   1 
ATOM   2321 H HD11 . LEU A 1 146 ? 19.353 50.435 38.980 0.00 53.66  ? 149 LEU A HD11 1 
ATOM   2322 H HD12 . LEU A 1 146 ? 19.023 51.931 39.400 0.00 53.66  ? 149 LEU A HD12 1 
ATOM   2323 H HD13 . LEU A 1 146 ? 20.020 51.061 40.279 0.00 53.66  ? 149 LEU A HD13 1 
ATOM   2324 H HD21 . LEU A 1 146 ? 18.505 48.581 40.205 0.00 55.19  ? 149 LEU A HD21 1 
ATOM   2325 H HD22 . LEU A 1 146 ? 18.941 49.054 41.658 0.00 55.19  ? 149 LEU A HD22 1 
ATOM   2326 H HD23 . LEU A 1 146 ? 17.413 48.750 41.346 0.00 55.19  ? 149 LEU A HD23 1 
ATOM   2327 N N    . TYR A 1 147 ? 15.962 53.024 43.881 1.00 27.30  ? 150 TYR A N    1 
ATOM   2328 C CA   . TYR A 1 147 ? 15.788 53.961 44.988 1.00 33.92  ? 150 TYR A CA   1 
ATOM   2329 C C    . TYR A 1 147 ? 15.284 53.251 46.234 1.00 32.49  ? 150 TYR A C    1 
ATOM   2330 O O    . TYR A 1 147 ? 15.798 53.444 47.331 1.00 37.11  ? 150 TYR A O    1 
ATOM   2331 C CB   . TYR A 1 147 ? 14.812 55.065 44.558 1.00 33.14  ? 150 TYR A CB   1 
ATOM   2332 C CG   . TYR A 1 147 ? 14.341 55.920 45.726 1.00 42.98  ? 150 TYR A CG   1 
ATOM   2333 C CD1  . TYR A 1 147 ? 13.111 55.680 46.323 1.00 53.47  ? 150 TYR A CD1  1 
ATOM   2334 C CD2  . TYR A 1 147 ? 15.118 56.955 46.208 1.00 65.63  ? 150 TYR A CD2  1 
ATOM   2335 C CE1  . TYR A 1 147 ? 12.668 56.452 47.382 1.00 59.32  ? 150 TYR A CE1  1 
ATOM   2336 C CE2  . TYR A 1 147 ? 14.688 57.735 47.268 1.00 63.71  ? 150 TYR A CE2  1 
ATOM   2337 C CZ   . TYR A 1 147 ? 13.461 57.477 47.849 1.00 71.78  ? 150 TYR A CZ   1 
ATOM   2338 O OH   . TYR A 1 147 ? 13.022 58.249 48.901 1.00 83.39  ? 150 TYR A OH   1 
ATOM   2339 H H    . TYR A 1 147 ? 15.499 53.209 43.180 0.00 32.71  ? 150 TYR A H    1 
ATOM   2340 H HA   . TYR A 1 147 ? 16.642 54.367 45.206 0.00 40.71  ? 150 TYR A HA   1 
ATOM   2341 H HB2  . TYR A 1 147 ? 15.254 55.646 43.919 0.00 39.78  ? 150 TYR A HB2  1 
ATOM   2342 H HB3  . TYR A 1 147 ? 14.033 54.656 44.151 0.00 39.78  ? 150 TYR A HB3  1 
ATOM   2343 H HD1  . TYR A 1 147 ? 12.575 54.989 46.005 0.00 64.17  ? 150 TYR A HD1  1 
ATOM   2344 H HD2  . TYR A 1 147 ? 15.942 57.131 45.814 0.00 78.76  ? 150 TYR A HD2  1 
ATOM   2345 H HE1  . TYR A 1 147 ? 11.843 56.281 47.775 0.00 71.19  ? 150 TYR A HE1  1 
ATOM   2346 H HE2  . TYR A 1 147 ? 15.220 58.428 47.587 0.00 76.47  ? 150 TYR A HE2  1 
ATOM   2347 H HH   . TYR A 1 147 ? 13.598 58.831 49.090 0.00 100.08 ? 150 TYR A HH   1 
ATOM   2348 N N    . VAL A 1 148 ? 14.250 52.415 46.079 1.00 29.31  ? 151 VAL A N    1 
ATOM   2349 C CA   . VAL A 1 148 ? 13.690 51.728 47.245 1.00 30.04  ? 151 VAL A CA   1 
ATOM   2350 C C    . VAL A 1 148 ? 14.737 50.814 47.872 1.00 30.37  ? 151 VAL A C    1 
ATOM   2351 O O    . VAL A 1 148 ? 14.847 50.712 49.085 1.00 35.14  ? 151 VAL A O    1 
ATOM   2352 C CB   . VAL A 1 148 ? 12.429 50.945 46.831 1.00 30.83  ? 151 VAL A CB   1 
ATOM   2353 C CG1  . VAL A 1 148 ? 11.996 49.978 47.954 1.00 32.34  ? 151 VAL A CG1  1 
ATOM   2354 C CG2  . VAL A 1 148 ? 11.310 51.897 46.453 1.00 34.82  ? 151 VAL A CG2  1 
ATOM   2355 H H    . VAL A 1 148 ? 13.867 52.234 45.331 0.00 35.18  ? 151 VAL A H    1 
ATOM   2356 H HA   . VAL A 1 148 ? 13.435 52.387 47.909 0.00 36.06  ? 151 VAL A HA   1 
ATOM   2357 H HB   . VAL A 1 148 ? 12.632 50.409 46.048 0.00 37.01  ? 151 VAL A HB   1 
ATOM   2358 H HG11 . VAL A 1 148 ? 11.083 49.693 47.791 0.00 38.82  ? 151 VAL A HG11 1 
ATOM   2359 H HG12 . VAL A 1 148 ? 12.588 49.209 47.954 0.00 38.82  ? 151 VAL A HG12 1 
ATOM   2360 H HG13 . VAL A 1 148 ? 12.051 50.438 48.806 0.00 38.82  ? 151 VAL A HG13 1 
ATOM   2361 H HG21 . VAL A 1 148 ? 10.524 51.382 46.216 0.00 41.80  ? 151 VAL A HG21 1 
ATOM   2362 H HG22 . VAL A 1 148 ? 11.114 52.471 47.210 0.00 41.80  ? 151 VAL A HG22 1 
ATOM   2363 H HG23 . VAL A 1 148 ? 11.594 52.433 45.696 0.00 41.80  ? 151 VAL A HG23 1 
ATOM   2364 N N    . LEU A 1 149 ? 15.499 50.100 47.018 1.00 31.68  ? 152 LEU A N    1 
ATOM   2365 C CA   . LEU A 1 149 ? 16.502 49.181 47.570 1.00 32.89  ? 152 LEU A CA   1 
ATOM   2366 C C    . LEU A 1 149 ? 17.556 49.920 48.378 1.00 40.12  ? 152 LEU A C    1 
ATOM   2367 O O    . LEU A 1 149 ? 18.126 49.345 49.310 1.00 38.51  ? 152 LEU A O    1 
ATOM   2368 C CB   . LEU A 1 149 ? 17.165 48.389 46.428 1.00 32.16  ? 152 LEU A CB   1 
ATOM   2369 C CG   . LEU A 1 149 ? 16.291 47.387 45.694 1.00 35.55  ? 152 LEU A CG   1 
ATOM   2370 C CD1  . LEU A 1 149 ? 17.129 46.651 44.645 1.00 40.15  ? 152 LEU A CD1  1 
ATOM   2371 C CD2  . LEU A 1 149 ? 15.653 46.385 46.643 1.00 38.24  ? 152 LEU A CD2  1 
ATOM   2372 H H    . LEU A 1 149 ? 15.454 50.131 46.160 0.00 38.03  ? 152 LEU A H    1 
ATOM   2373 H HA   . LEU A 1 149 ? 16.060 48.553 48.162 0.00 39.48  ? 152 LEU A HA   1 
ATOM   2374 H HB2  . LEU A 1 149 ? 17.483 49.025 45.768 0.00 38.60  ? 152 LEU A HB2  1 
ATOM   2375 H HB3  . LEU A 1 149 ? 17.912 47.895 46.801 0.00 38.60  ? 152 LEU A HB3  1 
ATOM   2376 H HG   . LEU A 1 149 ? 15.570 47.868 45.259 0.00 42.67  ? 152 LEU A HG   1 
ATOM   2377 H HD11 . LEU A 1 149 ? 16.557 46.040 44.155 0.00 48.19  ? 152 LEU A HD11 1 
ATOM   2378 H HD12 . LEU A 1 149 ? 17.516 47.300 44.037 0.00 48.19  ? 152 LEU A HD12 1 
ATOM   2379 H HD13 . LEU A 1 149 ? 17.833 46.156 45.093 0.00 48.19  ? 152 LEU A HD13 1 
ATOM   2380 H HD21 . LEU A 1 149 ? 15.209 45.697 46.123 0.00 45.90  ? 152 LEU A HD21 1 
ATOM   2381 H HD22 . LEU A 1 149 ? 16.346 45.988 47.194 0.00 45.90  ? 152 LEU A HD22 1 
ATOM   2382 H HD23 . LEU A 1 149 ? 15.009 46.846 47.202 0.00 45.90  ? 152 LEU A HD23 1 
ATOM   2383 N N    . PHE A 1 150 ? 17.827 51.197 48.063 1.00 40.82  ? 153 PHE A N    1 
ATOM   2384 C CA   . PHE A 1 150 ? 18.839 51.963 48.812 1.00 39.46  ? 153 PHE A CA   1 
ATOM   2385 C C    . PHE A 1 150 ? 18.250 52.769 49.959 1.00 61.88  ? 153 PHE A C    1 
ATOM   2386 O O    . PHE A 1 150 ? 18.753 52.708 51.085 1.00 71.44  ? 153 PHE A O    1 
ATOM   2387 C CB   . PHE A 1 150 ? 19.584 52.909 47.869 1.00 53.76  ? 153 PHE A CB   1 
ATOM   2388 C CG   . PHE A 1 150 ? 20.805 52.309 47.255 1.00 59.60  ? 153 PHE A CG   1 
ATOM   2389 C CD1  . PHE A 1 150 ? 20.831 51.991 45.905 1.00 57.55  ? 153 PHE A CD1  1 
ATOM   2390 C CD2  . PHE A 1 150 ? 21.924 52.055 48.024 1.00 55.42  ? 153 PHE A CD2  1 
ATOM   2391 C CE1  . PHE A 1 150 ? 21.966 51.436 45.340 1.00 72.36  ? 153 PHE A CE1  1 
ATOM   2392 C CE2  . PHE A 1 150 ? 23.054 51.497 47.469 1.00 75.48  ? 153 PHE A CE2  1 
ATOM   2393 C CZ   . PHE A 1 150 ? 23.078 51.184 46.131 1.00 62.65  ? 153 PHE A CZ   1 
ATOM   2394 H H    . PHE A 1 150 ? 17.444 51.636 47.430 0.00 48.99  ? 153 PHE A H    1 
ATOM   2395 H HA   . PHE A 1 150 ? 19.467 51.325 49.187 0.00 47.36  ? 153 PHE A HA   1 
ATOM   2396 H HB2  . PHE A 1 150 ? 18.987 53.166 47.149 0.00 64.52  ? 153 PHE A HB2  1 
ATOM   2397 H HB3  . PHE A 1 150 ? 19.859 53.694 48.368 0.00 64.52  ? 153 PHE A HB3  1 
ATOM   2398 H HD1  . PHE A 1 150 ? 20.082 52.151 45.378 0.00 69.08  ? 153 PHE A HD1  1 
ATOM   2399 H HD2  . PHE A 1 150 ? 21.914 52.264 48.931 0.00 66.52  ? 153 PHE A HD2  1 
ATOM   2400 H HE1  . PHE A 1 150 ? 21.983 51.233 44.433 0.00 86.84  ? 153 PHE A HE1  1 
ATOM   2401 H HE2  . PHE A 1 150 ? 23.800 51.332 47.999 0.00 90.59  ? 153 PHE A HE2  1 
ATOM   2402 H HZ   . PHE A 1 150 ? 23.839 50.804 45.755 0.00 75.19  ? 153 PHE A HZ   1 
ATOM   2403 N N    . PHE A 1 151 ? 17.209 53.550 49.696 1.00 59.14  ? 154 PHE A N    1 
ATOM   2404 C CA   . PHE A 1 151 ? 16.671 54.469 50.687 1.00 71.66  ? 154 PHE A CA   1 
ATOM   2405 C C    . PHE A 1 151 ? 15.420 53.928 51.363 1.00 73.68  ? 154 PHE A C    1 
ATOM   2406 O O    . PHE A 1 151 ? 14.705 54.689 52.026 1.00 87.76  ? 154 PHE A O    1 
ATOM   2407 C CB   . PHE A 1 151 ? 16.393 55.826 50.037 1.00 61.89  ? 154 PHE A CB   1 
ATOM   2408 C CG   . PHE A 1 151 ? 17.592 56.417 49.351 1.00 65.55  ? 154 PHE A CG   1 
ATOM   2409 C CD1  . PHE A 1 151 ? 17.960 56.003 48.088 1.00 55.97  ? 154 PHE A CD1  1 
ATOM   2410 C CD2  . PHE A 1 151 ? 18.375 57.371 49.993 1.00 65.65  ? 154 PHE A CD2  1 
ATOM   2411 C CE1  . PHE A 1 151 ? 19.066 56.531 47.454 1.00 67.10  ? 154 PHE A CE1  1 
ATOM   2412 C CE2  . PHE A 1 151 ? 19.486 57.904 49.365 1.00 76.98  ? 154 PHE A CE2  1 
ATOM   2413 C CZ   . PHE A 1 151 ? 19.834 57.483 48.096 1.00 76.22  ? 154 PHE A CZ   1 
ATOM   2414 H H    . PHE A 1 151 ? 16.794 53.564 48.942 0.00 70.98  ? 154 PHE A H    1 
ATOM   2415 H HA   . PHE A 1 151 ? 17.333 54.609 51.382 0.00 86.01  ? 154 PHE A HA   1 
ATOM   2416 H HB2  . PHE A 1 151 ? 15.694 55.718 49.373 0.00 74.28  ? 154 PHE A HB2  1 
ATOM   2417 H HB3  . PHE A 1 151 ? 16.106 56.449 50.722 0.00 74.28  ? 154 PHE A HB3  1 
ATOM   2418 H HD1  . PHE A 1 151 ? 17.452 55.355 47.654 0.00 67.18  ? 154 PHE A HD1  1 
ATOM   2419 H HD2  . PHE A 1 151 ? 18.150 57.652 50.851 0.00 78.79  ? 154 PHE A HD2  1 
ATOM   2420 H HE1  . PHE A 1 151 ? 19.294 56.246 46.598 0.00 80.54  ? 154 PHE A HE1  1 
ATOM   2421 H HE2  . PHE A 1 151 ? 19.999 58.547 49.797 0.00 92.38  ? 154 PHE A HE2  1 
ATOM   2422 H HZ   . PHE A 1 151 ? 20.583 57.839 47.675 0.00 91.47  ? 154 PHE A HZ   1 
ATOM   2423 N N    . GLY A 1 152 ? 15.144 52.635 51.215 1.00 71.40  ? 155 GLY A N    1 
ATOM   2424 C CA   . GLY A 1 152 ? 14.088 51.987 51.964 1.00 73.30  ? 155 GLY A CA   1 
ATOM   2425 C C    . GLY A 1 152 ? 14.586 50.739 52.667 1.00 68.81  ? 155 GLY A C    1 
ATOM   2426 O O    . GLY A 1 152 ? 14.420 50.586 53.880 1.00 71.84  ? 155 GLY A O    1 
ATOM   2427 H H    . GLY A 1 152 ? 15.563 52.110 50.679 0.00 85.62  ? 155 GLY A H    1 
ATOM   2428 H HA2  . GLY A 1 152 ? 13.742 52.600 52.631 0.00 87.98  ? 155 GLY A HA2  1 
ATOM   2429 H HA3  . GLY A 1 152 ? 13.370 51.737 51.362 0.00 87.98  ? 155 GLY A HA3  1 
ATOM   2430 N N    . PHE A 1 153 ? 15.219 49.844 51.913 1.00 65.99  ? 156 PHE A N    1 
ATOM   2431 C CA   . PHE A 1 153 ? 15.634 48.561 52.479 1.00 61.83  ? 156 PHE A CA   1 
ATOM   2432 C C    . PHE A 1 153 ? 16.886 48.705 53.342 1.00 79.89  ? 156 PHE A C    1 
ATOM   2433 O O    . PHE A 1 153 ? 16.959 48.134 54.436 1.00 65.95  ? 156 PHE A O    1 
ATOM   2434 C CB   . PHE A 1 153 ? 15.885 47.548 51.362 1.00 56.38  ? 156 PHE A CB   1 
ATOM   2435 C CG   . PHE A 1 153 ? 14.641 46.894 50.834 1.00 53.29  ? 156 PHE A CG   1 
ATOM   2436 C CD1  . PHE A 1 153 ? 13.390 47.413 51.099 1.00 55.18  ? 156 PHE A CD1  1 
ATOM   2437 C CD2  . PHE A 1 153 ? 14.738 45.733 50.087 1.00 54.79  ? 156 PHE A CD2  1 
ATOM   2438 C CE1  . PHE A 1 153 ? 12.260 46.800 50.612 1.00 52.76  ? 156 PHE A CE1  1 
ATOM   2439 C CE2  . PHE A 1 153 ? 13.613 45.107 49.603 1.00 52.12  ? 156 PHE A CE2  1 
ATOM   2440 C CZ   . PHE A 1 153 ? 12.368 45.643 49.863 1.00 56.07  ? 156 PHE A CZ   1 
ATOM   2441 H H    . PHE A 1 153 ? 15.418 49.951 51.084 0.00 79.20  ? 156 PHE A H    1 
ATOM   2442 H HA   . PHE A 1 153 ? 14.915 48.229 53.039 0.00 74.13  ? 156 PHE A HA   1 
ATOM   2443 H HB2  . PHE A 1 153 ? 16.315 48.004 50.622 0.00 67.59  ? 156 PHE A HB2  1 
ATOM   2444 H HB3  . PHE A 1 153 ? 16.464 46.848 51.703 0.00 67.59  ? 156 PHE A HB3  1 
ATOM   2445 H HD1  . PHE A 1 153 ? 13.311 48.186 51.610 0.00 66.15  ? 156 PHE A HD1  1 
ATOM   2446 H HD2  . PHE A 1 153 ? 15.576 45.370 49.910 0.00 65.75  ? 156 PHE A HD2  1 
ATOM   2447 H HE1  . PHE A 1 153 ? 11.422 47.163 50.788 0.00 63.26  ? 156 PHE A HE1  1 
ATOM   2448 H HE2  . PHE A 1 153 ? 13.691 44.327 49.103 0.00 62.56  ? 156 PHE A HE2  1 
ATOM   2449 H HZ   . PHE A 1 153 ? 11.604 45.226 49.535 0.00 67.29  ? 156 PHE A HZ   1 
ATOM   2450 N N    . THR A 1 154 ? 17.890 49.447 52.854 1.00 74.24  ? 157 THR A N    1 
ATOM   2451 C CA   . THR A 1 154 ? 19.122 49.616 53.619 1.00 79.10  ? 157 THR A CA   1 
ATOM   2452 C C    . THR A 1 154 ? 18.830 50.152 55.015 1.00 77.14  ? 157 THR A C    1 
ATOM   2453 O O    . THR A 1 154 ? 19.496 49.774 55.983 1.00 76.71  ? 157 THR A O    1 
ATOM   2454 C CB   . THR A 1 154 ? 20.084 50.554 52.884 1.00 72.52  ? 157 THR A CB   1 
ATOM   2455 O OG1  . THR A 1 154 ? 20.443 49.988 51.617 1.00 67.57  ? 157 THR A OG1  1 
ATOM   2456 C CG2  . THR A 1 154 ? 21.350 50.793 53.708 1.00 82.07  ? 157 THR A CG2  1 
ATOM   2457 H H    . THR A 1 154 ? 17.880 49.853 52.096 0.00 89.10  ? 157 THR A H    1 
ATOM   2458 H HA   . THR A 1 154 ? 19.555 48.752 53.705 0.00 94.94  ? 157 THR A HA   1 
ATOM   2459 H HB   . THR A 1 154 ? 19.647 51.408 52.743 0.00 87.04  ? 157 THR A HB   1 
ATOM   2460 H HG1  . THR A 1 154 ? 19.755 49.870 51.149 0.00 81.03  ? 157 THR A HG1  1 
ATOM   2461 H HG21 . THR A 1 154 ? 22.014 51.253 53.171 0.00 98.50  ? 157 THR A HG21 1 
ATOM   2462 H HG22 . THR A 1 154 ? 21.142 51.337 54.484 0.00 98.50  ? 157 THR A HG22 1 
ATOM   2463 H HG23 . THR A 1 154 ? 21.717 49.946 54.006 0.00 98.50  ? 157 THR A HG23 1 
ATOM   2464 N N    . SER A 1 155 ? 17.830 51.028 55.134 1.00 95.01  ? 158 SER A N    1 
ATOM   2465 C CA   . SER A 1 155 ? 17.522 51.624 56.430 1.00 108.65 ? 158 SER A CA   1 
ATOM   2466 C C    . SER A 1 155 ? 16.987 50.583 57.407 1.00 107.90 ? 158 SER A C    1 
ATOM   2467 O O    . SER A 1 155 ? 17.295 50.632 58.604 1.00 102.47 ? 158 SER A O    1 
ATOM   2468 C CB   . SER A 1 155 ? 16.515 52.763 56.255 1.00 100.31 ? 158 SER A CB   1 
ATOM   2469 H H    . SER A 1 155 ? 17.323 51.288 54.490 0.00 114.02 ? 158 SER A H    1 
ATOM   2470 H HA   . SER A 1 155 ? 18.336 51.995 56.804 0.00 130.39 ? 158 SER A HA   1 
ATOM   2471 N N    . LYS A 1 156 ? 16.185 49.633 56.920 1.00 93.46  ? 159 LYS A N    1 
ATOM   2472 C CA   . LYS A 1 156 ? 15.621 48.630 57.816 1.00 99.28  ? 159 LYS A CA   1 
ATOM   2473 C C    . LYS A 1 156 ? 16.625 47.527 58.123 1.00 92.94  ? 159 LYS A C    1 
ATOM   2474 O O    . LYS A 1 156 ? 16.682 47.037 59.256 1.00 91.36  ? 159 LYS A O    1 
ATOM   2475 C CB   . LYS A 1 156 ? 14.348 48.038 57.212 1.00 88.51  ? 159 LYS A CB   1 
ATOM   2476 C CG   . LYS A 1 156 ? 13.327 47.617 58.263 1.00 98.21  ? 159 LYS A CG   1 
ATOM   2477 C CD   . LYS A 1 156 ? 12.014 47.172 57.630 1.00 83.79  ? 159 LYS A CD   1 
ATOM   2478 C CE   . LYS A 1 156 ? 11.322 46.057 58.416 1.00 80.09  ? 159 LYS A CE   1 
ATOM   2479 N NZ   . LYS A 1 156 ? 12.239 45.008 58.944 1.00 73.54  ? 159 LYS A NZ   1 
ATOM   2480 H H    . LYS A 1 156 ? 15.959 49.551 56.095 0.00 112.17 ? 159 LYS A H    1 
ATOM   2481 H HA   . LYS A 1 156 ? 15.382 49.061 58.652 0.00 119.15 ? 159 LYS A HA   1 
ATOM   2482 H HB2  . LYS A 1 156 ? 13.932 48.703 56.641 0.00 106.22 ? 159 LYS A HB2  1 
ATOM   2483 H HB3  . LYS A 1 156 ? 14.583 47.253 56.692 0.00 106.22 ? 159 LYS A HB3  1 
ATOM   2484 H HG2  . LYS A 1 156 ? 13.684 46.874 58.776 0.00 117.87 ? 159 LYS A HG2  1 
ATOM   2485 H HG3  . LYS A 1 156 ? 13.143 48.367 58.849 0.00 117.87 ? 159 LYS A HG3  1 
ATOM   2486 H HD2  . LYS A 1 156 ? 11.410 47.930 57.591 0.00 100.56 ? 159 LYS A HD2  1 
ATOM   2487 H HD3  . LYS A 1 156 ? 12.191 46.841 56.735 0.00 100.56 ? 159 LYS A HD3  1 
ATOM   2488 H HE2  . LYS A 1 156 ? 10.864 46.453 59.175 0.00 96.12  ? 159 LYS A HE2  1 
ATOM   2489 H HE3  . LYS A 1 156 ? 10.682 45.620 57.833 0.00 96.12  ? 159 LYS A HE3  1 
ATOM   2490 H HZ1  . LYS A 1 156 ? 11.769 44.305 59.222 0.00 88.19  ? 159 LYS A HZ1  1 
ATOM   2491 H HZ2  . LYS A 1 156 ? 12.800 44.745 58.305 0.00 88.19  ? 159 LYS A HZ2  1 
ATOM   2492 H HZ3  . LYS A 1 156 ? 12.709 45.330 59.627 0.00 88.19  ? 159 LYS A HZ3  1 
ATOM   2493 N N    . ALA A 1 157 ? 17.425 47.129 57.131 1.00 86.97  ? 160 ALA A N    1 
ATOM   2494 C CA   . ALA A 1 157 ? 18.408 46.071 57.348 1.00 72.01  ? 160 ALA A CA   1 
ATOM   2495 C C    . ALA A 1 157 ? 19.358 46.420 58.484 1.00 87.37  ? 160 ALA A C    1 
ATOM   2496 O O    . ALA A 1 157 ? 19.731 45.551 59.279 1.00 71.88  ? 160 ALA A O    1 
ATOM   2497 C CB   . ALA A 1 157 ? 19.192 45.818 56.061 1.00 65.73  ? 160 ALA A CB   1 
ATOM   2498 H H    . ALA A 1 157 ? 17.419 47.453 56.334 0.00 104.37 ? 160 ALA A H    1 
ATOM   2499 H HA   . ALA A 1 157 ? 17.939 45.257 57.587 0.00 86.42  ? 160 ALA A HA   1 
ATOM   2500 H HB1  . ALA A 1 157 ? 19.837 45.111 56.219 0.00 78.89  ? 160 ALA A HB1  1 
ATOM   2501 H HB2  . ALA A 1 157 ? 18.574 45.551 55.362 0.00 78.89  ? 160 ALA A HB2  1 
ATOM   2502 H HB3  . ALA A 1 157 ? 19.650 46.633 55.804 0.00 78.89  ? 160 ALA A HB3  1 
ATOM   2503 N N    . GLU A 1 158 ? 19.760 47.691 58.578 1.00 78.36  ? 161 GLU A N    1 
ATOM   2504 C CA   . GLU A 1 158 ? 20.719 48.115 59.590 1.00 90.86  ? 161 GLU A CA   1 
ATOM   2505 C C    . GLU A 1 158 ? 20.176 48.002 61.008 1.00 92.07  ? 161 GLU A C    1 
ATOM   2506 O O    . GLU A 1 158 ? 20.943 48.186 61.959 1.00 89.93  ? 161 GLU A O    1 
ATOM   2507 C CB   . GLU A 1 158 ? 21.157 49.555 59.314 1.00 99.90  ? 161 GLU A CB   1 
ATOM   2508 C CG   . GLU A 1 158 ? 21.986 49.710 58.045 1.00 106.50 ? 161 GLU A CG   1 
ATOM   2509 C CD   . GLU A 1 158 ? 22.728 51.032 57.980 1.00 119.05 ? 161 GLU A CD   1 
ATOM   2510 O OE1  . GLU A 1 158 ? 22.586 51.846 58.918 1.00 132.90 ? 161 GLU A OE1  1 
ATOM   2511 O OE2  . GLU A 1 158 ? 23.449 51.259 56.985 1.00 109.85 ? 161 GLU A OE2  1 
ATOM   2512 H H    . GLU A 1 158 ? 19.490 48.326 58.064 0.00 94.05  ? 161 GLU A H    1 
ATOM   2513 H HA   . GLU A 1 158 ? 21.503 47.545 59.534 0.00 109.04 ? 161 GLU A HA   1 
ATOM   2514 H HB2  . GLU A 1 158 ? 20.366 50.108 59.221 0.00 119.89 ? 161 GLU A HB2  1 
ATOM   2515 H HB3  . GLU A 1 158 ? 21.694 49.866 60.059 0.00 119.89 ? 161 GLU A HB3  1 
ATOM   2516 H HG2  . GLU A 1 158 ? 22.643 48.996 58.009 0.00 127.82 ? 161 GLU A HG2  1 
ATOM   2517 H HG3  . GLU A 1 158 ? 21.398 49.658 57.276 0.00 127.82 ? 161 GLU A HG3  1 
ATOM   2518 N N    . SER A 1 159 ? 18.886 47.708 61.175 1.00 85.40  ? 162 SER A N    1 
ATOM   2519 C CA   . SER A 1 159 ? 18.288 47.509 62.489 1.00 91.31  ? 162 SER A CA   1 
ATOM   2520 C C    . SER A 1 159 ? 17.991 46.043 62.778 1.00 88.01  ? 162 SER A C    1 
ATOM   2521 O O    . SER A 1 159 ? 17.246 45.745 63.718 1.00 93.05  ? 162 SER A O    1 
ATOM   2522 C CB   . SER A 1 159 ? 17.005 48.334 62.612 1.00 97.64  ? 162 SER A CB   1 
ATOM   2523 O OG   . SER A 1 159 ? 16.039 47.920 61.659 1.00 91.39  ? 162 SER A OG   1 
ATOM   2524 H H    . SER A 1 159 ? 18.328 47.616 60.527 0.00 102.42 ? 162 SER A H    1 
ATOM   2525 H HA   . SER A 1 159 ? 18.913 47.823 63.161 0.00 109.59 ? 162 SER A HA   1 
ATOM   2526 H HB2  . SER A 1 159 ? 16.639 48.217 63.503 0.00 117.18 ? 162 SER A HB2  1 
ATOM   2527 H HB3  . SER A 1 159 ? 17.215 49.269 62.461 0.00 117.18 ? 162 SER A HB3  1 
ATOM   2528 H HG   . SER A 1 159 ? 16.329 48.049 60.881 0.00 109.68 ? 162 SER A HG   1 
ATOM   2529 N N    . MET A 1 160 ? 18.556 45.123 61.998 1.00 83.17  ? 163 MET A N    1 
ATOM   2530 C CA   . MET A 1 160 ? 18.307 43.699 62.129 1.00 79.67  ? 163 MET A CA   1 
ATOM   2531 C C    . MET A 1 160 ? 19.583 42.979 62.559 1.00 74.33  ? 163 MET A C    1 
ATOM   2532 O O    . MET A 1 160 ? 20.597 43.606 62.880 1.00 76.87  ? 163 MET A O    1 
ATOM   2533 C CB   . MET A 1 160 ? 17.774 43.148 60.806 1.00 74.14  ? 163 MET A CB   1 
ATOM   2534 C CG   . MET A 1 160 ? 16.643 43.966 60.224 1.00 93.45  ? 163 MET A CG   1 
ATOM   2535 S SD   . MET A 1 160 ? 15.824 43.141 58.856 1.00 78.33  ? 163 MET A SD   1 
ATOM   2536 C CE   . MET A 1 160 ? 14.997 41.790 59.690 1.00 65.54  ? 163 MET A CE   1 
ATOM   2537 H H    . MET A 1 160 ? 19.106 45.312 61.364 0.00 99.81  ? 163 MET A H    1 
ATOM   2538 H HA   . MET A 1 160 ? 17.631 43.571 62.813 0.00 95.61  ? 163 MET A HA   1 
ATOM   2539 H HB2  . MET A 1 160 ? 18.496 43.137 60.158 0.00 88.98  ? 163 MET A HB2  1 
ATOM   2540 H HB3  . MET A 1 160 ? 17.446 42.247 60.952 0.00 88.98  ? 163 MET A HB3  1 
ATOM   2541 H HG2  . MET A 1 160 ? 15.982 44.129 60.916 0.00 112.15 ? 163 MET A HG2  1 
ATOM   2542 H HG3  . MET A 1 160 ? 16.996 44.809 59.898 0.00 112.15 ? 163 MET A HG3  1 
ATOM   2543 H HE1  . MET A 1 160 ? 14.463 41.299 59.045 0.00 78.58  ? 163 MET A HE1  1 
ATOM   2544 H HE2  . MET A 1 160 ? 15.664 41.204 60.081 0.00 78.58  ? 163 MET A HE2  1 
ATOM   2545 H HE3  . MET A 1 160 ? 14.425 42.151 60.386 0.00 78.58  ? 163 MET A HE3  1 
ATOM   2546 N N    . ARG A 1 161 ? 19.526 41.652 62.557 1.00 70.62  ? 164 ARG A N    1 
ATOM   2547 C CA   . ARG A 1 161 ? 20.692 40.857 62.918 1.00 69.58  ? 164 ARG A CA   1 
ATOM   2548 C C    . ARG A 1 161 ? 21.890 41.279 62.068 1.00 67.13  ? 164 ARG A C    1 
ATOM   2549 O O    . ARG A 1 161 ? 21.728 41.591 60.885 1.00 64.69  ? 164 ARG A O    1 
ATOM   2550 C CB   . ARG A 1 161 ? 20.408 39.362 62.721 1.00 65.86  ? 164 ARG A CB   1 
ATOM   2551 C CG   . ARG A 1 161 ? 19.182 38.839 63.472 1.00 66.87  ? 164 ARG A CG   1 
ATOM   2552 C CD   . ARG A 1 161 ? 18.464 37.759 62.668 1.00 79.52  ? 164 ARG A CD   1 
ATOM   2553 N NE   . ARG A 1 161 ? 19.354 36.660 62.310 1.00 71.25  ? 164 ARG A NE   1 
ATOM   2554 C CZ   . ARG A 1 161 ? 18.991 35.601 61.600 1.00 69.74  ? 164 ARG A CZ   1 
ATOM   2555 N NH1  . ARG A 1 161 ? 17.752 35.453 61.164 1.00 62.68  ? 164 ARG A NH1  1 
ATOM   2556 N NH2  . ARG A 1 161 ? 19.895 34.667 61.321 1.00 64.46  ? 164 ARG A NH2  1 
ATOM   2557 H H    . ARG A 1 161 ? 18.830 41.191 62.351 0.00 84.69  ? 164 ARG A H    1 
ATOM   2558 H HA   . ARG A 1 161 ? 20.905 41.002 63.853 0.00 83.51  ? 164 ARG A HA   1 
ATOM   2559 H HB2  . ARG A 1 161 ? 20.263 39.198 61.776 0.00 79.05  ? 164 ARG A HB2  1 
ATOM   2560 H HB3  . ARG A 1 161 ? 21.176 38.859 63.032 0.00 79.05  ? 164 ARG A HB3  1 
ATOM   2561 H HG2  . ARG A 1 161 ? 19.460 38.456 64.318 0.00 80.19  ? 164 ARG A HG2  1 
ATOM   2562 H HG3  . ARG A 1 161 ? 18.562 39.569 63.626 0.00 80.19  ? 164 ARG A HG3  1 
ATOM   2563 H HD2  . ARG A 1 161 ? 17.736 37.398 63.197 0.00 95.44  ? 164 ARG A HD2  1 
ATOM   2564 H HD3  . ARG A 1 161 ? 18.119 38.147 61.849 0.00 95.44  ? 164 ARG A HD3  1 
ATOM   2565 H HE   . ARG A 1 161 ? 20.170 36.702 62.578 0.00 85.52  ? 164 ARG A HE   1 
ATOM   2566 H HH11 . ARG A 1 161 ? 17.160 36.053 61.339 0.00 75.23  ? 164 ARG A HH11 1 
ATOM   2567 H HH12 . ARG A 1 161 ? 17.537 34.758 60.705 0.00 75.23  ? 164 ARG A HH12 1 
ATOM   2568 H HH21 . ARG A 1 161 ? 20.704 34.755 61.601 0.00 77.37  ? 164 ARG A HH21 1 
ATOM   2569 H HH22 . ARG A 1 161 ? 19.671 33.975 60.862 0.00 77.37  ? 164 ARG A HH22 1 
ATOM   2570 N N    . PRO A 1 162 ? 23.098 41.318 62.637 1.00 42.76  ? 165 PRO A N    1 
ATOM   2571 C CA   . PRO A 1 162 ? 24.256 41.745 61.832 1.00 41.67  ? 165 PRO A CA   1 
ATOM   2572 C C    . PRO A 1 162 ? 24.490 40.896 60.600 1.00 47.53  ? 165 PRO A C    1 
ATOM   2573 O O    . PRO A 1 162 ? 24.921 41.430 59.562 1.00 41.36  ? 165 PRO A O    1 
ATOM   2574 C CB   . PRO A 1 162 ? 25.428 41.635 62.817 1.00 43.02  ? 165 PRO A CB   1 
ATOM   2575 C CG   . PRO A 1 162 ? 24.829 41.677 64.163 1.00 51.93  ? 165 PRO A CG   1 
ATOM   2576 C CD   . PRO A 1 162 ? 23.451 41.118 64.061 1.00 46.26  ? 165 PRO A CD   1 
ATOM   2577 H HA   . PRO A 1 162 ? 24.135 42.670 61.567 0.00 50.02  ? 165 PRO A HA   1 
ATOM   2578 H HB2  . PRO A 1 162 ? 25.897 40.798 62.674 0.00 51.63  ? 165 PRO A HB2  1 
ATOM   2579 H HB3  . PRO A 1 162 ? 26.035 42.381 62.687 0.00 51.63  ? 165 PRO A HB3  1 
ATOM   2580 H HG2  . PRO A 1 162 ? 25.366 41.142 64.769 0.00 62.33  ? 165 PRO A HG2  1 
ATOM   2581 H HG3  . PRO A 1 162 ? 24.798 42.596 64.471 0.00 62.33  ? 165 PRO A HG3  1 
ATOM   2582 H HD2  . PRO A 1 162 ? 23.445 40.175 64.288 0.00 55.53  ? 165 PRO A HD2  1 
ATOM   2583 H HD3  . PRO A 1 162 ? 22.840 41.602 64.638 0.00 55.53  ? 165 PRO A HD3  1 
ATOM   2584 N N    . GLU A 1 163 ? 24.243 39.581 60.676 1.00 41.13  ? 166 GLU A N    1 
ATOM   2585 C CA   . GLU A 1 163 ? 24.452 38.750 59.483 1.00 44.75  ? 166 GLU A CA   1 
ATOM   2586 C C    . GLU A 1 163 ? 23.407 39.030 58.405 1.00 39.44  ? 166 GLU A C    1 
ATOM   2587 O O    . GLU A 1 163 ? 23.695 38.862 57.221 1.00 42.37  ? 166 GLU A O    1 
ATOM   2588 C CB   . GLU A 1 163 ? 24.454 37.263 59.858 1.00 49.83  ? 166 GLU A CB   1 
ATOM   2589 C CG   . GLU A 1 163 ? 23.117 36.675 60.262 1.00 55.62  ? 166 GLU A CG   1 
ATOM   2590 C CD   . GLU A 1 163 ? 22.829 36.869 61.735 1.00 69.44  ? 166 GLU A CD   1 
ATOM   2591 O OE1  . GLU A 1 163 ? 23.373 37.826 62.330 1.00 58.50  ? 166 GLU A OE1  1 
ATOM   2592 O OE2  . GLU A 1 163 ? 22.069 36.058 62.309 1.00 77.94  ? 166 GLU A OE2  1 
ATOM   2593 H H    . GLU A 1 163 ? 23.967 39.164 61.375 0.00 49.37  ? 166 GLU A H    1 
ATOM   2594 H HA   . GLU A 1 163 ? 25.324 38.961 59.114 0.00 53.72  ? 166 GLU A HA   1 
ATOM   2595 H HB2  . GLU A 1 163 ? 24.768 36.759 59.091 0.00 59.81  ? 166 GLU A HB2  1 
ATOM   2596 H HB3  . GLU A 1 163 ? 25.058 37.141 60.606 0.00 59.81  ? 166 GLU A HB3  1 
ATOM   2597 H HG2  . GLU A 1 163 ? 22.412 37.109 59.756 0.00 66.75  ? 166 GLU A HG2  1 
ATOM   2598 H HG3  . GLU A 1 163 ? 23.120 35.723 60.077 0.00 66.75  ? 166 GLU A HG3  1 
ATOM   2599 N N    . VAL A 1 164 ? 22.199 39.462 58.794 1.00 41.02  ? 167 VAL A N    1 
ATOM   2600 C CA   . VAL A 1 164 ? 21.221 39.888 57.802 1.00 38.16  ? 167 VAL A CA   1 
ATOM   2601 C C    . VAL A 1 164 ? 21.668 41.187 57.150 1.00 32.97  ? 167 VAL A C    1 
ATOM   2602 O O    . VAL A 1 164 ? 21.609 41.333 55.917 1.00 34.61  ? 167 VAL A O    1 
ATOM   2603 C CB   . VAL A 1 164 ? 19.835 40.039 58.460 1.00 40.73  ? 167 VAL A CB   1 
ATOM   2604 C CG1  . VAL A 1 164 ? 18.855 40.683 57.488 1.00 43.98  ? 167 VAL A CG1  1 
ATOM   2605 C CG2  . VAL A 1 164 ? 19.316 38.676 58.914 1.00 43.96  ? 167 VAL A CG2  1 
ATOM   2606 H H    . VAL A 1 164 ? 21.933 39.514 59.610 0.00 49.23  ? 167 VAL A H    1 
ATOM   2607 H HA   . VAL A 1 164 ? 21.158 39.209 57.113 0.00 45.81  ? 167 VAL A HA   1 
ATOM   2608 H HB   . VAL A 1 164 ? 19.912 40.612 59.238 0.00 48.89  ? 167 VAL A HB   1 
ATOM   2609 H HG11 . VAL A 1 164 ? 17.956 40.594 57.840 0.00 52.78  ? 167 VAL A HG11 1 
ATOM   2610 H HG12 . VAL A 1 164 ? 19.080 41.622 57.389 0.00 52.78  ? 167 VAL A HG12 1 
ATOM   2611 H HG13 . VAL A 1 164 ? 18.921 40.235 56.630 0.00 52.78  ? 167 VAL A HG13 1 
ATOM   2612 H HG21 . VAL A 1 164 ? 18.439 38.789 59.312 0.00 52.76  ? 167 VAL A HG21 1 
ATOM   2613 H HG22 . VAL A 1 164 ? 19.258 38.088 58.145 0.00 52.76  ? 167 VAL A HG22 1 
ATOM   2614 H HG23 . VAL A 1 164 ? 19.931 38.307 59.568 0.00 52.76  ? 167 VAL A HG23 1 
ATOM   2615 N N    . ALA A 1 165 ? 22.149 42.143 57.961 1.00 41.37  ? 168 ALA A N    1 
ATOM   2616 C CA   . ALA A 1 165 ? 22.559 43.436 57.421 1.00 40.80  ? 168 ALA A CA   1 
ATOM   2617 C C    . ALA A 1 165 ? 23.702 43.282 56.426 1.00 39.17  ? 168 ALA A C    1 
ATOM   2618 O O    . ALA A 1 165 ? 23.684 43.881 55.344 1.00 39.56  ? 168 ALA A O    1 
ATOM   2619 C CB   . ALA A 1 165 ? 22.961 44.371 58.569 1.00 40.12  ? 168 ALA A CB   1 
ATOM   2620 H H    . ALA A 1 165 ? 22.244 42.065 58.812 0.00 49.65  ? 168 ALA A H    1 
ATOM   2621 H HA   . ALA A 1 165 ? 21.808 43.832 56.952 0.00 48.97  ? 168 ALA A HA   1 
ATOM   2622 H HB1  . ALA A 1 165 ? 23.238 45.224 58.199 0.00 48.16  ? 168 ALA A HB1  1 
ATOM   2623 H HB2  . ALA A 1 165 ? 22.198 44.497 59.155 0.00 48.16  ? 168 ALA A HB2  1 
ATOM   2624 H HB3  . ALA A 1 165 ? 23.694 43.970 59.061 0.00 48.16  ? 168 ALA A HB3  1 
ATOM   2625 N N    . SER A 1 166 ? 24.720 42.490 56.780 1.00 37.71  ? 169 SER A N    1 
ATOM   2626 C CA   . SER A 1 166 ? 25.901 42.388 55.924 1.00 39.72  ? 169 SER A CA   1 
ATOM   2627 C C    . SER A 1 166 ? 25.592 41.626 54.644 1.00 40.68  ? 169 SER A C    1 
ATOM   2628 O O    . SER A 1 166 ? 26.048 42.013 53.555 1.00 39.31  ? 169 SER A O    1 
ATOM   2629 C CB   . SER A 1 166 ? 27.051 41.731 56.688 1.00 52.19  ? 169 SER A CB   1 
ATOM   2630 O OG   . SER A 1 166 ? 26.796 40.360 56.927 1.00 58.34  ? 169 SER A OG   1 
ATOM   2631 H H    . SER A 1 166 ? 24.750 42.013 57.495 0.00 45.26  ? 169 SER A H    1 
ATOM   2632 H HA   . SER A 1 166 ? 26.184 43.281 55.675 0.00 47.68  ? 169 SER A HA   1 
ATOM   2633 H HB2  . SER A 1 166 ? 27.863 41.813 56.164 0.00 62.64  ? 169 SER A HB2  1 
ATOM   2634 H HB3  . SER A 1 166 ? 27.160 42.183 57.540 0.00 62.64  ? 169 SER A HB3  1 
ATOM   2635 H HG   . SER A 1 166 ? 27.450 40.011 57.322 0.00 70.02  ? 169 SER A HG   1 
ATOM   2636 N N    . THR A 1 167 ? 24.804 40.547 54.735 1.00 37.36  ? 170 THR A N    1 
ATOM   2637 C CA   . THR A 1 167 ? 24.430 39.822 53.526 1.00 33.96  ? 170 THR A CA   1 
ATOM   2638 C C    . THR A 1 167 ? 23.558 40.680 52.613 1.00 36.25  ? 170 THR A C    1 
ATOM   2639 O O    . THR A 1 167 ? 23.738 40.677 51.382 1.00 34.24  ? 170 THR A O    1 
ATOM   2640 C CB   . THR A 1 167 ? 23.718 38.526 53.896 1.00 33.08  ? 170 THR A CB   1 
ATOM   2641 O OG1  . THR A 1 167 ? 24.614 37.697 54.643 1.00 38.16  ? 170 THR A OG1  1 
ATOM   2642 C CG2  . THR A 1 167 ? 23.238 37.781 52.636 1.00 36.44  ? 170 THR A CG2  1 
ATOM   2643 H H    . THR A 1 167 ? 24.484 40.226 55.466 0.00 44.84  ? 170 THR A H    1 
ATOM   2644 H HA   . THR A 1 167 ? 25.234 39.590 53.036 0.00 40.76  ? 170 THR A HA   1 
ATOM   2645 H HB   . THR A 1 167 ? 22.934 38.723 54.434 0.00 39.70  ? 170 THR A HB   1 
ATOM   2646 H HG1  . THR A 1 167 ? 24.181 37.119 55.072 0.00 45.80  ? 170 THR A HG1  1 
ATOM   2647 H HG21 . THR A 1 167 ? 22.903 36.903 52.877 0.00 43.74  ? 170 THR A HG21 1 
ATOM   2648 H HG22 . THR A 1 167 ? 22.528 38.281 52.205 0.00 43.74  ? 170 THR A HG22 1 
ATOM   2649 H HG23 . THR A 1 167 ? 23.973 37.677 52.012 0.00 43.74  ? 170 THR A HG23 1 
ATOM   2650 N N    . PHE A 1 168 ? 22.601 41.399 53.184 1.00 31.82  ? 171 PHE A N    1 
ATOM   2651 C CA   . PHE A 1 168 ? 21.781 42.287 52.362 1.00 32.26  ? 171 PHE A CA   1 
ATOM   2652 C C    . PHE A 1 168 ? 22.637 43.319 51.642 1.00 32.01  ? 171 PHE A C    1 
ATOM   2653 O O    . PHE A 1 168 ? 22.478 43.540 50.434 1.00 33.87  ? 171 PHE A O    1 
ATOM   2654 C CB   . PHE A 1 168 ? 20.739 43.009 53.226 1.00 32.99  ? 171 PHE A CB   1 
ATOM   2655 C CG   . PHE A 1 168 ? 19.980 44.053 52.444 1.00 36.96  ? 171 PHE A CG   1 
ATOM   2656 C CD1  . PHE A 1 168 ? 19.048 43.675 51.507 1.00 36.55  ? 171 PHE A CD1  1 
ATOM   2657 C CD2  . PHE A 1 168 ? 20.252 45.392 52.626 1.00 39.18  ? 171 PHE A CD2  1 
ATOM   2658 C CE1  . PHE A 1 168 ? 18.375 44.633 50.766 1.00 37.74  ? 171 PHE A CE1  1 
ATOM   2659 C CE2  . PHE A 1 168 ? 19.581 46.344 51.902 1.00 40.12  ? 171 PHE A CE2  1 
ATOM   2660 C CZ   . PHE A 1 168 ? 18.658 45.959 50.964 1.00 37.00  ? 171 PHE A CZ   1 
ATOM   2661 H H    . PHE A 1 168 ? 22.408 41.394 54.022 0.00 38.20  ? 171 PHE A H    1 
ATOM   2662 H HA   . PHE A 1 168 ? 21.320 41.742 51.705 0.00 38.72  ? 171 PHE A HA   1 
ATOM   2663 H HB2  . PHE A 1 168 ? 20.102 42.361 53.565 0.00 39.60  ? 171 PHE A HB2  1 
ATOM   2664 H HB3  . PHE A 1 168 ? 21.188 43.451 53.964 0.00 39.60  ? 171 PHE A HB3  1 
ATOM   2665 H HD1  . PHE A 1 168 ? 18.869 42.773 51.370 0.00 43.87  ? 171 PHE A HD1  1 
ATOM   2666 H HD2  . PHE A 1 168 ? 20.896 45.651 53.245 0.00 47.02  ? 171 PHE A HD2  1 
ATOM   2667 H HE1  . PHE A 1 168 ? 17.736 44.378 50.140 0.00 45.30  ? 171 PHE A HE1  1 
ATOM   2668 H HE2  . PHE A 1 168 ? 19.752 47.247 52.047 0.00 48.16  ? 171 PHE A HE2  1 
ATOM   2669 H HZ   . PHE A 1 168 ? 18.220 46.604 50.458 0.00 44.42  ? 171 PHE A HZ   1 
ATOM   2670 N N    . LYS A 1 169 ? 23.543 43.984 52.376 1.00 35.31  ? 172 LYS A N    1 
ATOM   2671 C CA   . LYS A 1 169 ? 24.357 45.026 51.760 1.00 35.52  ? 172 LYS A CA   1 
ATOM   2672 C C    . LYS A 1 169 ? 25.092 44.494 50.535 1.00 38.75  ? 172 LYS A C    1 
ATOM   2673 O O    . LYS A 1 169 ? 25.135 45.154 49.482 1.00 36.75  ? 172 LYS A O    1 
ATOM   2674 C CB   . LYS A 1 169 ? 25.345 45.584 52.801 1.00 33.07  ? 172 LYS A CB   1 
ATOM   2675 H H    . LYS A 1 169 ? 23.697 43.850 53.211 0.00 42.39  ? 172 LYS A H    1 
ATOM   2676 H HA   . LYS A 1 169 ? 23.788 45.755 51.467 0.00 42.63  ? 172 LYS A HA   1 
ATOM   2677 N N    . VAL A 1 170 ? 25.657 43.293 50.638 1.00 33.30  ? 173 VAL A N    1 
ATOM   2678 C CA   . VAL A 1 170 ? 26.402 42.730 49.504 1.00 31.54  ? 173 VAL A CA   1 
ATOM   2679 C C    . VAL A 1 170 ? 25.466 42.429 48.343 1.00 30.98  ? 173 VAL A C    1 
ATOM   2680 O O    . VAL A 1 170 ? 25.771 42.727 47.180 1.00 30.18  ? 173 VAL A O    1 
ATOM   2681 C CB   . VAL A 1 170 ? 27.151 41.464 49.942 1.00 35.18  ? 173 VAL A CB   1 
ATOM   2682 C CG1  . VAL A 1 170 ? 27.756 40.754 48.742 1.00 37.47  ? 173 VAL A CG1  1 
ATOM   2683 C CG2  . VAL A 1 170 ? 28.238 41.842 50.968 1.00 40.58  ? 173 VAL A CG2  1 
ATOM   2684 H H    . VAL A 1 170 ? 25.627 42.792 51.337 0.00 39.98  ? 173 VAL A H    1 
ATOM   2685 H HA   . VAL A 1 170 ? 27.048 43.390 49.207 0.00 37.85  ? 173 VAL A HA   1 
ATOM   2686 H HB   . VAL A 1 170 ? 26.529 40.847 50.360 0.00 42.23  ? 173 VAL A HB   1 
ATOM   2687 H HG11 . VAL A 1 170 ? 28.434 40.133 49.052 0.00 44.98  ? 173 VAL A HG11 1 
ATOM   2688 H HG12 . VAL A 1 170 ? 27.056 40.273 48.274 0.00 44.98  ? 173 VAL A HG12 1 
ATOM   2689 H HG13 . VAL A 1 170 ? 28.156 41.414 48.154 0.00 44.98  ? 173 VAL A HG13 1 
ATOM   2690 H HG21 . VAL A 1 170 ? 28.709 41.038 51.240 0.00 48.71  ? 173 VAL A HG21 1 
ATOM   2691 H HG22 . VAL A 1 170 ? 28.858 42.465 50.557 0.00 48.71  ? 173 VAL A HG22 1 
ATOM   2692 H HG23 . VAL A 1 170 ? 27.817 42.254 51.738 0.00 48.71  ? 173 VAL A HG23 1 
ATOM   2693 N N    . LEU A 1 171 ? 24.320 41.801 48.634 1.00 27.71  ? 174 LEU A N    1 
ATOM   2694 C CA   . LEU A 1 171 ? 23.385 41.447 47.552 1.00 29.99  ? 174 LEU A CA   1 
ATOM   2695 C C    . LEU A 1 171 ? 22.756 42.688 46.935 1.00 30.68  ? 174 LEU A C    1 
ATOM   2696 O O    . LEU A 1 171 ? 22.483 42.708 45.734 1.00 29.84  ? 174 LEU A O    1 
ATOM   2697 C CB   . LEU A 1 171 ? 22.288 40.520 48.091 1.00 28.86  ? 174 LEU A CB   1 
ATOM   2698 C CG   . LEU A 1 171 ? 22.775 39.128 48.498 1.00 30.67  ? 174 LEU A CG   1 
ATOM   2699 C CD1  . LEU A 1 171 ? 21.639 38.355 49.144 1.00 37.25  ? 174 LEU A CD1  1 
ATOM   2700 C CD2  . LEU A 1 171 ? 23.291 38.364 47.266 1.00 31.88  ? 174 LEU A CD2  1 
ATOM   2701 H H    . LEU A 1 171 ? 24.065 41.575 49.424 0.00 33.26  ? 174 LEU A H    1 
ATOM   2702 H HA   . LEU A 1 171 ? 23.873 40.974 46.859 0.00 36.00  ? 174 LEU A HA   1 
ATOM   2703 H HB2  . LEU A 1 171 ? 21.893 40.934 48.875 0.00 34.64  ? 174 LEU A HB2  1 
ATOM   2704 H HB3  . LEU A 1 171 ? 21.615 40.406 47.402 0.00 34.64  ? 174 LEU A HB3  1 
ATOM   2705 H HG   . LEU A 1 171 ? 23.501 39.214 49.135 0.00 36.81  ? 174 LEU A HG   1 
ATOM   2706 H HD11 . LEU A 1 171 ? 21.965 37.485 49.419 0.00 44.71  ? 174 LEU A HD11 1 
ATOM   2707 H HD12 . LEU A 1 171 ? 21.320 38.849 49.916 0.00 44.71  ? 174 LEU A HD12 1 
ATOM   2708 H HD13 . LEU A 1 171 ? 20.922 38.251 48.499 0.00 44.71  ? 174 LEU A HD13 1 
ATOM   2709 H HD21 . LEU A 1 171 ? 23.459 37.442 47.514 0.00 38.26  ? 174 LEU A HD21 1 
ATOM   2710 H HD22 . LEU A 1 171 ? 22.620 38.402 46.567 0.00 38.26  ? 174 LEU A HD22 1 
ATOM   2711 H HD23 . LEU A 1 171 ? 24.113 38.779 46.959 0.00 38.26  ? 174 LEU A HD23 1 
ATOM   2712 N N    A ARG A 1 172 ? 22.495 43.717 47.754 0.75 27.92  ? 175 ARG A N    1 
ATOM   2713 N N    B ARG A 1 172 ? 22.527 43.732 47.738 0.25 28.24  ? 175 ARG A N    1 
ATOM   2714 C CA   A ARG A 1 172 ? 22.009 44.989 47.226 0.75 30.13  ? 175 ARG A CA   1 
ATOM   2715 C CA   B ARG A 1 172 ? 21.994 44.975 47.190 0.25 30.30  ? 175 ARG A CA   1 
ATOM   2716 C C    A ARG A 1 172 ? 23.003 45.568 46.224 0.75 30.94  ? 175 ARG A C    1 
ATOM   2717 C C    B ARG A 1 172 ? 22.995 45.634 46.247 0.25 31.24  ? 175 ARG A C    1 
ATOM   2718 O O    A ARG A 1 172 ? 22.624 46.009 45.126 0.75 30.39  ? 175 ARG A O    1 
ATOM   2719 O O    B ARG A 1 172 ? 22.609 46.178 45.202 0.25 30.05  ? 175 ARG A O    1 
ATOM   2720 C CB   A ARG A 1 172 ? 21.775 45.969 48.391 0.75 37.13  ? 175 ARG A CB   1 
ATOM   2721 C CB   B ARG A 1 172 ? 21.618 45.923 48.330 0.25 36.59  ? 175 ARG A CB   1 
ATOM   2722 C CG   A ARG A 1 172 ? 21.559 47.439 47.989 0.75 36.26  ? 175 ARG A CG   1 
ATOM   2723 C CG   B ARG A 1 172 ? 20.941 47.205 47.876 0.25 35.96  ? 175 ARG A CG   1 
ATOM   2724 C CD   A ARG A 1 172 ? 21.929 48.406 49.118 0.75 37.52  ? 175 ARG A CD   1 
ATOM   2725 C CD   B ARG A 1 172 ? 21.849 48.404 48.090 0.25 41.62  ? 175 ARG A CD   1 
ATOM   2726 N NE   A ARG A 1 172 ? 23.369 48.568 49.279 0.75 43.88  ? 175 ARG A NE   1 
ATOM   2727 N NE   B ARG A 1 172 ? 21.955 48.754 49.503 0.25 37.42  ? 175 ARG A NE   1 
ATOM   2728 C CZ   A ARG A 1 172 ? 23.929 49.280 50.250 0.75 40.78  ? 175 ARG A CZ   1 
ATOM   2729 C CZ   B ARG A 1 172 ? 23.086 48.774 50.200 0.25 45.62  ? 175 ARG A CZ   1 
ATOM   2730 N NH1  A ARG A 1 172 ? 23.198 49.912 51.150 0.75 45.79  ? 175 ARG A NH1  1 
ATOM   2731 N NH1  B ARG A 1 172 ? 24.248 48.456 49.650 0.25 39.60  ? 175 ARG A NH1  1 
ATOM   2732 N NH2  A ARG A 1 172 ? 25.257 49.367 50.307 0.75 49.38  ? 175 ARG A NH2  1 
ATOM   2733 N NH2  B ARG A 1 172 ? 23.048 49.121 51.482 0.25 42.43  ? 175 ARG A NH2  1 
ATOM   2734 H H    A ARG A 1 172 ? 22.590 43.700 48.609 0.75 33.51  ? 175 ARG A H    1 
ATOM   2735 H H    B ARG A 1 172 ? 22.670 43.744 48.586 0.25 33.89  ? 175 ARG A H    1 
ATOM   2736 H HA   A ARG A 1 172 ? 21.165 44.852 46.768 0.75 36.17  ? 175 ARG A HA   1 
ATOM   2737 H HA   B ARG A 1 172 ? 21.191 44.780 46.683 0.25 36.37  ? 175 ARG A HA   1 
ATOM   2738 H HB2  A ARG A 1 172 ? 20.985 45.683 48.875 0.75 44.56  ? 175 ARG A HB2  1 
ATOM   2739 H HB2  B ARG A 1 172 ? 21.007 45.463 48.927 0.25 43.92  ? 175 ARG A HB2  1 
ATOM   2740 H HB3  A ARG A 1 172 ? 22.550 45.939 48.974 0.75 44.56  ? 175 ARG A HB3  1 
ATOM   2741 H HB3  B ARG A 1 172 ? 22.426 46.170 48.807 0.25 43.92  ? 175 ARG A HB3  1 
ATOM   2742 H HG2  A ARG A 1 172 ? 22.115 47.645 47.222 0.75 43.53  ? 175 ARG A HG2  1 
ATOM   2743 H HG2  B ARG A 1 172 ? 20.731 47.144 46.931 0.25 43.16  ? 175 ARG A HG2  1 
ATOM   2744 H HG3  A ARG A 1 172 ? 20.625 47.576 47.768 0.75 43.53  ? 175 ARG A HG3  1 
ATOM   2745 H HG3  B ARG A 1 172 ? 20.128 47.341 48.388 0.25 43.16  ? 175 ARG A HG3  1 
ATOM   2746 H HD2  A ARG A 1 172 ? 21.550 49.278 48.924 0.75 45.03  ? 175 ARG A HD2  1 
ATOM   2747 H HD2  B ARG A 1 172 ? 22.737 48.196 47.760 0.25 49.95  ? 175 ARG A HD2  1 
ATOM   2748 H HD3  A ARG A 1 172 ? 21.571 48.068 49.954 0.75 45.03  ? 175 ARG A HD3  1 
ATOM   2749 H HD3  B ARG A 1 172 ? 21.489 49.168 47.614 0.25 49.95  ? 175 ARG A HD3  1 
ATOM   2750 H HE   A ARG A 1 172 ? 23.886 48.179 48.712 0.75 52.67  ? 175 ARG A HE   1 
ATOM   2751 H HE   B ARG A 1 172 ? 21.231 48.963 49.916 0.25 44.92  ? 175 ARG A HE   1 
ATOM   2752 H HH11 A ARG A 1 172 ? 22.340 49.867 51.116 0.75 54.96  ? 175 ARG A HH11 1 
ATOM   2753 H HH11 B ARG A 1 172 ? 24.284 48.229 48.822 0.25 47.53  ? 175 ARG A HH11 1 
ATOM   2754 H HH12 A ARG A 1 172 ? 23.580 50.368 51.771 0.75 54.96  ? 175 ARG A HH12 1 
ATOM   2755 H HH12 B ARG A 1 172 ? 24.967 48.477 50.122 0.25 47.53  ? 175 ARG A HH12 1 
ATOM   2756 H HH21 A ARG A 1 172 ? 25.740 48.965 49.720 0.75 59.27  ? 175 ARG A HH21 1 
ATOM   2757 H HH21 B ARG A 1 172 ? 23.773 49.138 51.944 0.25 50.93  ? 175 ARG A HH21 1 
ATOM   2758 H HH22 A ARG A 1 172 ? 25.631 49.825 50.931 0.75 59.27  ? 175 ARG A HH22 1 
ATOM   2759 H HH22 B ARG A 1 172 ? 22.298 49.327 51.849 0.25 50.93  ? 175 ARG A HH22 1 
ATOM   2760 N N    . ASN A 1 173 ? 24.283 45.624 46.610 1.00 31.67  ? 176 ASN A N    1 
ATOM   2761 C CA   . ASN A 1 173 ? 25.295 46.206 45.731 1.00 34.30  ? 176 ASN A CA   1 
ATOM   2762 C C    . ASN A 1 173 ? 25.468 45.405 44.452 1.00 32.61  ? 176 ASN A C    1 
ATOM   2763 O O    . ASN A 1 173 ? 25.637 45.994 43.362 1.00 31.96  ? 176 ASN A O    1 
ATOM   2764 C CB   . ASN A 1 173 ? 26.630 46.288 46.493 1.00 36.06  ? 176 ASN A CB   1 
ATOM   2765 C CG   . ASN A 1 173 ? 26.602 47.340 47.568 1.00 43.37  ? 176 ASN A CG   1 
ATOM   2766 O OD1  . ASN A 1 173 ? 25.654 48.118 47.652 1.00 40.26  ? 176 ASN A OD1  1 
ATOM   2767 N ND2  . ASN A 1 173 ? 27.631 47.361 48.415 1.00 45.95  ? 176 ASN A ND2  1 
ATOM   2768 H H    . ASN A 1 173 ? 24.581 45.336 47.363 0.00 38.02  ? 176 ASN A H    1 
ATOM   2769 H HA   . ASN A 1 173 ? 25.016 47.099 45.478 0.00 41.17  ? 176 ASN A HA   1 
ATOM   2770 H HB2  . ASN A 1 173 ? 26.811 45.432 46.911 0.00 43.28  ? 176 ASN A HB2  1 
ATOM   2771 H HB3  . ASN A 1 173 ? 27.340 46.510 45.870 0.00 43.28  ? 176 ASN A HB3  1 
ATOM   2772 H HD21 . ASN A 1 173 ? 27.657 47.945 49.045 0.00 55.15  ? 176 ASN A HD21 1 
ATOM   2773 H HD22 . ASN A 1 173 ? 28.268 46.790 48.331 0.00 55.15  ? 176 ASN A HD22 1 
ATOM   2774 N N    . VAL A 1 174 ? 25.427 44.070 44.538 1.00 28.74  ? 177 VAL A N    1 
ATOM   2775 C CA   . VAL A 1 174 ? 25.509 43.247 43.348 1.00 25.67  ? 177 VAL A CA   1 
ATOM   2776 C C    . VAL A 1 174 ? 24.331 43.547 42.418 1.00 28.12  ? 177 VAL A C    1 
ATOM   2777 O O    . VAL A 1 174 ? 24.501 43.718 41.196 1.00 29.00  ? 177 VAL A O    1 
ATOM   2778 C CB   . VAL A 1 174 ? 25.539 41.755 43.723 1.00 29.03  ? 177 VAL A CB   1 
ATOM   2779 C CG1  . VAL A 1 174 ? 25.296 40.889 42.513 1.00 34.46  ? 177 VAL A CG1  1 
ATOM   2780 C CG2  . VAL A 1 174 ? 26.879 41.410 44.372 1.00 30.82  ? 177 VAL A CG2  1 
ATOM   2781 H H    . VAL A 1 174 ? 25.353 43.627 45.272 0.00 34.50  ? 177 VAL A H    1 
ATOM   2782 H HA   . VAL A 1 174 ? 26.334 43.464 42.886 0.00 30.82  ? 177 VAL A HA   1 
ATOM   2783 H HB   . VAL A 1 174 ? 24.828 41.575 44.358 0.00 34.85  ? 177 VAL A HB   1 
ATOM   2784 H HG11 . VAL A 1 174 ? 25.597 39.987 42.705 0.00 41.36  ? 177 VAL A HG11 1 
ATOM   2785 H HG12 . VAL A 1 174 ? 24.347 40.886 42.312 0.00 41.36  ? 177 VAL A HG12 1 
ATOM   2786 H HG13 . VAL A 1 174 ? 25.791 41.251 41.761 0.00 41.36  ? 177 VAL A HG13 1 
ATOM   2787 H HG21 . VAL A 1 174 ? 26.878 40.473 44.622 0.00 36.99  ? 177 VAL A HG21 1 
ATOM   2788 H HG22 . VAL A 1 174 ? 27.592 41.582 43.736 0.00 36.99  ? 177 VAL A HG22 1 
ATOM   2789 H HG23 . VAL A 1 174 ? 27.000 41.962 45.161 0.00 36.99  ? 177 VAL A HG23 1 
ATOM   2790 N N    . THR A 1 175 ? 23.120 43.595 42.988 1.00 27.32  ? 178 THR A N    1 
ATOM   2791 C CA   . THR A 1 175 ? 21.913 43.821 42.194 1.00 27.70  ? 178 THR A CA   1 
ATOM   2792 C C    . THR A 1 175 ? 21.958 45.171 41.496 1.00 27.99  ? 178 THR A C    1 
ATOM   2793 O O    . THR A 1 175 ? 21.649 45.276 40.304 1.00 28.59  ? 178 THR A O    1 
ATOM   2794 C CB   . THR A 1 175 ? 20.693 43.724 43.114 1.00 29.73  ? 178 THR A CB   1 
ATOM   2795 O OG1  . THR A 1 175 ? 20.623 42.402 43.667 1.00 29.87  ? 178 THR A OG1  1 
ATOM   2796 C CG2  . THR A 1 175 ? 19.410 44.022 42.354 1.00 29.74  ? 178 THR A CG2  1 
ATOM   2797 H H    . THR A 1 175 ? 22.972 43.499 43.830 0.00 32.79  ? 178 THR A H    1 
ATOM   2798 H HA   . THR A 1 175 ? 21.843 43.141 41.506 0.00 33.26  ? 178 THR A HA   1 
ATOM   2799 H HB   . THR A 1 175 ? 20.774 44.376 43.828 0.00 35.69  ? 178 THR A HB   1 
ATOM   2800 H HG1  . THR A 1 175 ? 21.324 42.233 44.097 0.00 35.85  ? 178 THR A HG1  1 
ATOM   2801 H HG21 . THR A 1 175 ? 18.642 43.750 42.879 0.00 35.70  ? 178 THR A HG21 1 
ATOM   2802 H HG22 . THR A 1 175 ? 19.346 44.973 42.172 0.00 35.70  ? 178 THR A HG22 1 
ATOM   2803 H HG23 . THR A 1 175 ? 19.403 43.540 41.512 0.00 35.70  ? 178 THR A HG23 1 
ATOM   2804 N N    . VAL A 1 176 ? 22.322 46.233 42.223 1.00 25.15  ? 179 VAL A N    1 
ATOM   2805 C CA   . VAL A 1 176 ? 22.264 47.565 41.613 1.00 25.36  ? 179 VAL A CA   1 
ATOM   2806 C C    . VAL A 1 176 ? 23.215 47.657 40.434 1.00 27.92  ? 179 VAL A C    1 
ATOM   2807 O O    . VAL A 1 176 ? 22.889 48.257 39.386 1.00 31.73  ? 179 VAL A O    1 
ATOM   2808 C CB   . VAL A 1 176 ? 22.533 48.649 42.672 1.00 33.66  ? 179 VAL A CB   1 
ATOM   2809 C CG1  . VAL A 1 176 ? 22.808 49.986 42.004 1.00 39.96  ? 179 VAL A CG1  1 
ATOM   2810 C CG2  . VAL A 1 176 ? 21.358 48.739 43.612 1.00 38.42  ? 179 VAL A CG2  1 
ATOM   2811 H H    . VAL A 1 176 ? 22.595 46.210 43.038 0.00 30.19  ? 179 VAL A H    1 
ATOM   2812 H HA   . VAL A 1 176 ? 21.368 47.709 41.270 0.00 30.45  ? 179 VAL A HA   1 
ATOM   2813 H HB   . VAL A 1 176 ? 23.320 48.415 43.189 0.00 40.40  ? 179 VAL A HB   1 
ATOM   2814 H HG11 . VAL A 1 176 ? 22.730 50.691 42.665 0.00 47.97  ? 179 VAL A HG11 1 
ATOM   2815 H HG12 . VAL A 1 176 ? 23.705 49.976 41.635 0.00 47.97  ? 179 VAL A HG12 1 
ATOM   2816 H HG13 . VAL A 1 176 ? 22.160 50.123 41.295 0.00 47.97  ? 179 VAL A HG13 1 
ATOM   2817 H HG21 . VAL A 1 176 ? 21.686 48.823 44.521 0.00 46.11  ? 179 VAL A HG21 1 
ATOM   2818 H HG22 . VAL A 1 176 ? 20.827 49.517 43.379 0.00 46.11  ? 179 VAL A HG22 1 
ATOM   2819 H HG23 . VAL A 1 176 ? 20.823 47.935 43.526 0.00 46.11  ? 179 VAL A HG23 1 
ATOM   2820 N N    . VAL A 1 177 ? 24.429 47.098 40.580 1.00 26.84  ? 180 VAL A N    1 
ATOM   2821 C CA   . VAL A 1 177 ? 25.411 47.181 39.508 1.00 25.77  ? 180 VAL A CA   1 
ATOM   2822 C C    . VAL A 1 177 ? 24.982 46.346 38.312 1.00 27.66  ? 180 VAL A C    1 
ATOM   2823 O O    . VAL A 1 177 ? 25.035 46.801 37.150 1.00 29.96  ? 180 VAL A O    1 
ATOM   2824 C CB   . VAL A 1 177 ? 26.789 46.724 40.033 1.00 33.42  ? 180 VAL A CB   1 
ATOM   2825 C CG1  . VAL A 1 177 ? 27.786 46.634 38.870 1.00 37.45  ? 180 VAL A CG1  1 
ATOM   2826 C CG2  . VAL A 1 177 ? 27.284 47.678 41.104 1.00 37.61  ? 180 VAL A CG2  1 
ATOM   2827 H H    . VAL A 1 177 ? 24.696 46.675 41.280 0.00 32.21  ? 180 VAL A H    1 
ATOM   2828 H HA   . VAL A 1 177 ? 25.471 48.104 39.217 0.00 30.94  ? 180 VAL A HA   1 
ATOM   2829 H HB   . VAL A 1 177 ? 26.709 45.844 40.432 0.00 40.12  ? 180 VAL A HB   1 
ATOM   2830 H HG11 . VAL A 1 177 ? 28.687 46.598 39.229 0.00 44.95  ? 180 VAL A HG11 1 
ATOM   2831 H HG12 . VAL A 1 177 ? 27.602 45.832 38.357 0.00 44.95  ? 180 VAL A HG12 1 
ATOM   2832 H HG13 . VAL A 1 177 ? 27.686 47.417 38.306 0.00 44.95  ? 180 VAL A HG13 1 
ATOM   2833 H HG21 . VAL A 1 177 ? 28.150 47.375 41.421 0.00 45.14  ? 180 VAL A HG21 1 
ATOM   2834 H HG22 . VAL A 1 177 ? 27.364 48.567 40.724 0.00 45.14  ? 180 VAL A HG22 1 
ATOM   2835 H HG23 . VAL A 1 177 ? 26.649 47.688 41.837 0.00 45.14  ? 180 VAL A HG23 1 
ATOM   2836 N N    . LEU A 1 178 ? 24.554 45.100 38.546 1.00 23.47  ? 181 LEU A N    1 
ATOM   2837 C CA   . LEU A 1 178 ? 24.246 44.232 37.413 1.00 24.86  ? 181 LEU A CA   1 
ATOM   2838 C C    . LEU A 1 178 ? 22.967 44.671 36.708 1.00 24.58  ? 181 LEU A C    1 
ATOM   2839 O O    . LEU A 1 178 ? 22.905 44.693 35.467 1.00 24.63  ? 181 LEU A O    1 
ATOM   2840 C CB   . LEU A 1 178 ? 24.089 42.774 37.880 1.00 23.96  ? 181 LEU A CB   1 
ATOM   2841 C CG   . LEU A 1 178 ? 25.368 42.128 38.410 1.00 30.64  ? 181 LEU A CG   1 
ATOM   2842 C CD1  . LEU A 1 178 ? 25.043 40.719 38.932 1.00 29.90  ? 181 LEU A CD1  1 
ATOM   2843 C CD2  . LEU A 1 178 ? 26.435 42.069 37.324 1.00 34.15  ? 181 LEU A CD2  1 
ATOM   2844 H H    . LEU A 1 178 ? 24.439 44.749 39.322 0.00 28.18  ? 181 LEU A H    1 
ATOM   2845 H HA   . LEU A 1 178 ? 24.986 44.284 36.788 0.00 29.85  ? 181 LEU A HA   1 
ATOM   2846 H HB2  . LEU A 1 178 ? 23.432 42.749 38.593 0.00 28.76  ? 181 LEU A HB2  1 
ATOM   2847 H HB3  . LEU A 1 178 ? 23.783 42.243 37.128 0.00 28.76  ? 181 LEU A HB3  1 
ATOM   2848 H HG   . LEU A 1 178 ? 25.727 42.659 39.138 0.00 36.79  ? 181 LEU A HG   1 
ATOM   2849 H HD11 . LEU A 1 178 ? 25.858 40.309 39.261 0.00 35.90  ? 181 LEU A HD11 1 
ATOM   2850 H HD12 . LEU A 1 178 ? 24.396 40.791 39.651 0.00 35.90  ? 181 LEU A HD12 1 
ATOM   2851 H HD13 . LEU A 1 178 ? 24.676 40.191 38.207 0.00 35.90  ? 181 LEU A HD13 1 
ATOM   2852 H HD21 . LEU A 1 178 ? 27.166 41.509 37.629 0.00 40.99  ? 181 LEU A HD21 1 
ATOM   2853 H HD22 . LEU A 1 178 ? 26.045 41.695 36.518 0.00 40.99  ? 181 LEU A HD22 1 
ATOM   2854 H HD23 . LEU A 1 178 ? 26.757 42.967 37.149 0.00 40.99  ? 181 LEU A HD23 1 
ATOM   2855 N N    . TRP A 1 179 ? 21.925 45.036 37.478 1.00 21.03  ? 182 TRP A N    1 
ATOM   2856 C CA   . TRP A 1 179 ? 20.654 45.383 36.815 1.00 22.69  ? 182 TRP A CA   1 
ATOM   2857 C C    . TRP A 1 179 ? 20.805 46.646 35.972 1.00 22.45  ? 182 TRP A C    1 
ATOM   2858 O O    . TRP A 1 179 ? 20.182 46.770 34.893 1.00 23.85  ? 182 TRP A O    1 
ATOM   2859 C CB   . TRP A 1 179 ? 19.540 45.566 37.830 1.00 21.90  ? 182 TRP A CB   1 
ATOM   2860 C CG   . TRP A 1 179 ? 19.029 44.282 38.433 1.00 21.11  ? 182 TRP A CG   1 
ATOM   2861 C CD1  . TRP A 1 179 ? 19.773 43.173 38.753 1.00 23.46  ? 182 TRP A CD1  1 
ATOM   2862 C CD2  . TRP A 1 179 ? 17.652 43.990 38.805 1.00 21.16  ? 182 TRP A CD2  1 
ATOM   2863 N NE1  . TRP A 1 179 ? 18.939 42.203 39.344 1.00 24.27  ? 182 TRP A NE1  1 
ATOM   2864 C CE2  . TRP A 1 179 ? 17.656 42.684 39.381 1.00 22.49  ? 182 TRP A CE2  1 
ATOM   2865 C CE3  . TRP A 1 179 ? 16.479 44.711 38.743 1.00 26.23  ? 182 TRP A CE3  1 
ATOM   2866 C CZ2  . TRP A 1 179 ? 16.483 42.089 39.854 1.00 26.11  ? 182 TRP A CZ2  1 
ATOM   2867 C CZ3  . TRP A 1 179 ? 15.292 44.097 39.212 1.00 26.97  ? 182 TRP A CZ3  1 
ATOM   2868 C CH2  . TRP A 1 179 ? 15.333 42.812 39.757 1.00 23.61  ? 182 TRP A CH2  1 
ATOM   2869 H H    . TRP A 1 179 ? 21.927 45.087 38.336 0.00 25.25  ? 182 TRP A H    1 
ATOM   2870 H HA   . TRP A 1 179 ? 20.405 44.645 36.236 0.00 27.24  ? 182 TRP A HA   1 
ATOM   2871 H HB2  . TRP A 1 179 ? 19.870 46.119 38.554 0.00 26.30  ? 182 TRP A HB2  1 
ATOM   2872 H HB3  . TRP A 1 179 ? 18.792 46.002 37.393 0.00 26.30  ? 182 TRP A HB3  1 
ATOM   2873 H HD1  . TRP A 1 179 ? 20.685 43.077 38.603 0.00 28.16  ? 182 TRP A HD1  1 
ATOM   2874 H HE1  . TRP A 1 179 ? 19.194 41.435 39.635 0.00 29.14  ? 182 TRP A HE1  1 
ATOM   2875 H HE3  . TRP A 1 179 ? 16.467 45.576 38.402 0.00 31.49  ? 182 TRP A HE3  1 
ATOM   2876 H HZ2  . TRP A 1 179 ? 16.487 41.234 40.221 0.00 31.34  ? 182 TRP A HZ2  1 
ATOM   2877 H HZ3  . TRP A 1 179 ? 14.482 44.551 39.157 0.00 32.37  ? 182 TRP A HZ3  1 
ATOM   2878 H HH2  . TRP A 1 179 ? 14.542 42.434 40.067 0.00 28.34  ? 182 TRP A HH2  1 
ATOM   2879 N N    . SER A 1 180 ? 21.613 47.611 36.445 1.00 23.23  ? 183 SER A N    1 
ATOM   2880 C CA   . SER A 1 180 ? 21.789 48.863 35.713 1.00 24.03  ? 183 SER A CA   1 
ATOM   2881 C C    . SER A 1 180 ? 22.419 48.650 34.350 1.00 24.91  ? 183 SER A C    1 
ATOM   2882 O O    . SER A 1 180 ? 22.257 49.497 33.472 1.00 25.35  ? 183 SER A O    1 
ATOM   2883 C CB   . SER A 1 180 ? 22.659 49.825 36.531 1.00 26.76  ? 183 SER A CB   1 
ATOM   2884 O OG   . SER A 1 180 ? 21.978 50.209 37.688 1.00 33.14  ? 183 SER A OG   1 
ATOM   2885 H H    . SER A 1 180 ? 22.061 47.561 37.178 0.00 27.89  ? 183 SER A H    1 
ATOM   2886 H HA   . SER A 1 180 ? 20.919 49.270 35.582 0.00 28.85  ? 183 SER A HA   1 
ATOM   2887 H HB2  . SER A 1 180 ? 23.484 49.379 36.778 0.00 32.12  ? 183 SER A HB2  1 
ATOM   2888 H HB3  . SER A 1 180 ? 22.854 50.612 35.999 0.00 32.12  ? 183 SER A HB3  1 
ATOM   2889 H HG   . SER A 1 180 ? 22.459 50.720 38.149 0.00 39.78  ? 183 SER A HG   1 
ATOM   2890 N N    . ALA A 1 181 ? 23.133 47.554 34.156 1.00 23.53  ? 184 ALA A N    1 
ATOM   2891 C CA   . ALA A 1 181 ? 23.762 47.316 32.848 1.00 23.06  ? 184 ALA A CA   1 
ATOM   2892 C C    . ALA A 1 181 ? 22.758 46.891 31.779 1.00 22.88  ? 184 ALA A C    1 
ATOM   2893 O O    . ALA A 1 181 ? 22.999 47.150 30.604 1.00 25.37  ? 184 ALA A O    1 
ATOM   2894 C CB   . ALA A 1 181 ? 24.846 46.230 32.972 1.00 24.35  ? 184 ALA A CB   1 
ATOM   2895 H H    . ALA A 1 181 ? 23.272 46.941 34.743 0.00 28.25  ? 184 ALA A H    1 
ATOM   2896 H HA   . ALA A 1 181 ? 24.172 48.149 32.566 0.00 27.68  ? 184 ALA A HA   1 
ATOM   2897 H HB1  . ALA A 1 181 ? 25.249 46.085 32.101 0.00 29.23  ? 184 ALA A HB1  1 
ATOM   2898 H HB2  . ALA A 1 181 ? 25.520 46.526 33.603 0.00 29.23  ? 184 ALA A HB2  1 
ATOM   2899 H HB3  . ALA A 1 181 ? 24.436 45.409 33.287 0.00 29.23  ? 184 ALA A HB3  1 
ATOM   2900 N N    . TYR A 1 182 ? 21.628 46.280 32.172 1.00 21.00  ? 185 TYR A N    1 
ATOM   2901 C CA   . TYR A 1 182 ? 20.692 45.762 31.162 1.00 21.35  ? 185 TYR A CA   1 
ATOM   2902 C C    . TYR A 1 182 ? 20.133 46.863 30.260 1.00 21.24  ? 185 TYR A C    1 
ATOM   2903 O O    . TYR A 1 182 ? 20.106 46.660 29.039 1.00 23.07  ? 185 TYR A O    1 
ATOM   2904 C CB   . TYR A 1 182 ? 19.545 44.998 31.854 1.00 20.10  ? 185 TYR A CB   1 
ATOM   2905 C CG   . TYR A 1 182 ? 19.919 43.619 32.359 1.00 20.02  ? 185 TYR A CG   1 
ATOM   2906 C CD1  . TYR A 1 182 ? 20.634 43.440 33.542 1.00 22.87  ? 185 TYR A CD1  1 
ATOM   2907 C CD2  . TYR A 1 182 ? 19.527 42.465 31.657 1.00 20.32  ? 185 TYR A CD2  1 
ATOM   2908 C CE1  . TYR A 1 182 ? 20.960 42.170 34.005 1.00 23.59  ? 185 TYR A CE1  1 
ATOM   2909 C CE2  . TYR A 1 182 ? 19.838 41.225 32.112 1.00 20.59  ? 185 TYR A CE2  1 
ATOM   2910 C CZ   . TYR A 1 182 ? 20.541 41.062 33.263 1.00 19.59  ? 185 TYR A CZ   1 
ATOM   2911 O OH   . TYR A 1 182 ? 20.841 39.776 33.713 1.00 21.61  ? 185 TYR A OH   1 
ATOM   2912 H H    . TYR A 1 182 ? 21.387 46.157 32.989 0.00 25.22  ? 185 TYR A H    1 
ATOM   2913 H HA   . TYR A 1 182 ? 21.188 45.139 30.608 0.00 25.63  ? 185 TYR A HA   1 
ATOM   2914 H HB2  . TYR A 1 182 ? 19.244 45.517 32.616 0.00 24.13  ? 185 TYR A HB2  1 
ATOM   2915 H HB3  . TYR A 1 182 ? 18.819 44.890 31.219 0.00 24.13  ? 185 TYR A HB3  1 
ATOM   2916 H HD1  . TYR A 1 182 ? 20.897 44.185 34.032 0.00 27.45  ? 185 TYR A HD1  1 
ATOM   2917 H HD2  . TYR A 1 182 ? 19.045 42.553 30.867 0.00 24.40  ? 185 TYR A HD2  1 
ATOM   2918 H HE1  . TYR A 1 182 ? 21.446 42.061 34.790 0.00 28.32  ? 185 TYR A HE1  1 
ATOM   2919 H HE2  . TYR A 1 182 ? 19.567 40.477 31.630 0.00 24.72  ? 185 TYR A HE2  1 
ATOM   2920 H HH   . TYR A 1 182 ? 20.557 39.207 33.165 0.00 25.94  ? 185 TYR A HH   1 
ATOM   2921 N N    . PRO A 1 183 ? 19.673 47.998 30.766 1.00 22.68  ? 186 PRO A N    1 
ATOM   2922 C CA   . PRO A 1 183 ? 19.167 49.041 29.847 1.00 20.47  ? 186 PRO A CA   1 
ATOM   2923 C C    . PRO A 1 183 ? 20.228 49.578 28.938 1.00 21.28  ? 186 PRO A C    1 
ATOM   2924 O O    . PRO A 1 183 ? 19.926 50.027 27.838 1.00 24.07  ? 186 PRO A O    1 
ATOM   2925 C CB   . PRO A 1 183 ? 18.624 50.131 30.793 1.00 23.82  ? 186 PRO A CB   1 
ATOM   2926 C CG   . PRO A 1 183 ? 19.189 49.794 32.183 1.00 25.84  ? 186 PRO A CG   1 
ATOM   2927 C CD   . PRO A 1 183 ? 19.365 48.305 32.187 1.00 22.72  ? 186 PRO A CD   1 
ATOM   2928 H HA   . PRO A 1 183 ? 18.431 48.690 29.321 0.00 24.50  ? 186 PRO A HA   1 
ATOM   2929 H HB2  . PRO A 1 183 ? 18.931 51.002 30.499 0.00 28.60  ? 186 PRO A HB2  1 
ATOM   2930 H HB3  . PRO A 1 183 ? 17.655 50.105 30.800 0.00 28.60  ? 186 PRO A HB3  1 
ATOM   2931 H HG2  . PRO A 1 183 ? 20.040 50.242 32.311 0.00 31.02  ? 186 PRO A HG2  1 
ATOM   2932 H HG3  . PRO A 1 183 ? 18.562 50.069 32.869 0.00 31.02  ? 186 PRO A HG3  1 
ATOM   2933 H HD2  . PRO A 1 183 ? 20.099 48.045 32.764 0.00 27.27  ? 186 PRO A HD2  1 
ATOM   2934 H HD3  . PRO A 1 183 ? 18.549 47.861 32.467 0.00 27.27  ? 186 PRO A HD3  1 
ATOM   2935 N N    . VAL A 1 184 ? 21.506 49.577 29.377 1.00 23.07  ? 187 VAL A N    1 
ATOM   2936 C CA   . VAL A 1 184 ? 22.577 50.043 28.498 1.00 23.58  ? 187 VAL A CA   1 
ATOM   2937 C C    . VAL A 1 184 ? 22.791 49.061 27.344 1.00 23.45  ? 187 VAL A C    1 
ATOM   2938 O O    . VAL A 1 184 ? 22.945 49.473 26.178 1.00 25.08  ? 187 VAL A O    1 
ATOM   2939 C CB   . VAL A 1 184 ? 23.859 50.233 29.310 1.00 25.96  ? 187 VAL A CB   1 
ATOM   2940 C CG1  . VAL A 1 184 ? 25.014 50.712 28.389 1.00 29.04  ? 187 VAL A CG1  1 
ATOM   2941 C CG2  . VAL A 1 184 ? 23.657 51.250 30.421 1.00 28.27  ? 187 VAL A CG2  1 
ATOM   2942 H H    . VAL A 1 184 ? 21.761 49.317 30.156 0.00 27.70  ? 187 VAL A H    1 
ATOM   2943 H HA   . VAL A 1 184 ? 22.321 50.897 28.115 0.00 28.31  ? 187 VAL A HA   1 
ATOM   2944 H HB   . VAL A 1 184 ? 24.092 49.379 29.707 0.00 31.16  ? 187 VAL A HB   1 
ATOM   2945 H HG11 . VAL A 1 184 ? 25.745 51.032 28.940 0.00 34.86  ? 187 VAL A HG11 1 
ATOM   2946 H HG12 . VAL A 1 184 ? 25.312 49.968 27.843 0.00 34.86  ? 187 VAL A HG12 1 
ATOM   2947 H HG13 . VAL A 1 184 ? 24.689 51.429 27.822 0.00 34.86  ? 187 VAL A HG13 1 
ATOM   2948 H HG21 . VAL A 1 184 ? 24.498 51.381 30.887 0.00 33.94  ? 187 VAL A HG21 1 
ATOM   2949 H HG22 . VAL A 1 184 ? 23.360 52.088 30.033 0.00 33.94  ? 187 VAL A HG22 1 
ATOM   2950 H HG23 . VAL A 1 184 ? 22.986 50.915 31.038 0.00 33.94  ? 187 VAL A HG23 1 
ATOM   2951 N N    . VAL A 1 185 ? 22.836 47.765 27.655 1.00 20.95  ? 188 VAL A N    1 
ATOM   2952 C CA   . VAL A 1 185 ? 23.030 46.751 26.597 1.00 20.80  ? 188 VAL A CA   1 
ATOM   2953 C C    . VAL A 1 185 ? 21.884 46.818 25.586 1.00 24.84  ? 188 VAL A C    1 
ATOM   2954 O O    . VAL A 1 185 ? 22.094 46.721 24.374 1.00 26.17  ? 188 VAL A O    1 
ATOM   2955 C CB   . VAL A 1 185 ? 23.129 45.350 27.226 1.00 24.22  ? 188 VAL A CB   1 
ATOM   2956 C CG1  . VAL A 1 185 ? 23.178 44.280 26.112 1.00 26.87  ? 188 VAL A CG1  1 
ATOM   2957 C CG2  . VAL A 1 185 ? 24.384 45.289 28.106 1.00 27.77  ? 188 VAL A CG2  1 
ATOM   2958 H H    . VAL A 1 185 ? 22.759 47.446 28.450 0.00 25.16  ? 188 VAL A H    1 
ATOM   2959 H HA   . VAL A 1 185 ? 23.860 46.942 26.132 0.00 24.97  ? 188 VAL A HA   1 
ATOM   2960 H HB   . VAL A 1 185 ? 22.352 45.169 27.777 0.00 29.08  ? 188 VAL A HB   1 
ATOM   2961 H HG11 . VAL A 1 185 ? 23.457 43.435 26.498 0.00 32.25  ? 188 VAL A HG11 1 
ATOM   2962 H HG12 . VAL A 1 185 ? 22.295 44.190 25.721 0.00 32.25  ? 188 VAL A HG12 1 
ATOM   2963 H HG13 . VAL A 1 185 ? 23.813 44.559 25.434 0.00 32.25  ? 188 VAL A HG13 1 
ATOM   2964 H HG21 . VAL A 1 185 ? 24.453 44.403 28.496 0.00 33.33  ? 188 VAL A HG21 1 
ATOM   2965 H HG22 . VAL A 1 185 ? 25.164 45.470 27.558 0.00 33.33  ? 188 VAL A HG22 1 
ATOM   2966 H HG23 . VAL A 1 185 ? 24.311 45.955 28.807 0.00 33.33  ? 188 VAL A HG23 1 
ATOM   2967 N N    . TRP A 1 186 ? 20.654 46.979 26.081 1.00 22.69  ? 189 TRP A N    1 
ATOM   2968 C CA   . TRP A 1 186 ? 19.499 47.048 25.181 1.00 21.60  ? 189 TRP A CA   1 
ATOM   2969 C C    . TRP A 1 186 ? 19.615 48.261 24.270 1.00 23.36  ? 189 TRP A C    1 
ATOM   2970 O O    . TRP A 1 186 ? 19.355 48.173 23.046 1.00 24.40  ? 189 TRP A O    1 
ATOM   2971 C CB   . TRP A 1 186 ? 18.246 47.137 26.070 1.00 21.16  ? 189 TRP A CB   1 
ATOM   2972 C CG   . TRP A 1 186 ? 16.881 46.919 25.425 1.00 22.11  ? 189 TRP A CG   1 
ATOM   2973 C CD1  . TRP A 1 186 ? 16.122 45.797 25.551 1.00 25.53  ? 189 TRP A CD1  1 
ATOM   2974 C CD2  . TRP A 1 186 ? 16.092 47.870 24.673 1.00 20.42  ? 189 TRP A CD2  1 
ATOM   2975 N NE1  . TRP A 1 186 ? 14.926 45.971 24.889 1.00 23.19  ? 189 TRP A NE1  1 
ATOM   2976 C CE2  . TRP A 1 186 ? 14.870 47.219 24.360 1.00 24.37  ? 189 TRP A CE2  1 
ATOM   2977 C CE3  . TRP A 1 186 ? 16.290 49.171 24.216 1.00 22.66  ? 189 TRP A CE3  1 
ATOM   2978 C CZ2  . TRP A 1 186 ? 13.855 47.840 23.626 1.00 24.41  ? 189 TRP A CZ2  1 
ATOM   2979 C CZ3  . TRP A 1 186 ? 15.305 49.795 23.480 1.00 28.18  ? 189 TRP A CZ3  1 
ATOM   2980 C CH2  . TRP A 1 186 ? 14.094 49.140 23.184 1.00 27.26  ? 189 TRP A CH2  1 
ATOM   2981 H H    . TRP A 1 186 ? 20.464 47.050 26.917 0.00 27.25  ? 189 TRP A H    1 
ATOM   2982 H HA   . TRP A 1 186 ? 19.437 46.265 24.612 0.00 25.94  ? 189 TRP A HA   1 
ATOM   2983 H HB2  . TRP A 1 186 ? 18.332 46.466 26.766 0.00 25.41  ? 189 TRP A HB2  1 
ATOM   2984 H HB3  . TRP A 1 186 ? 18.227 48.023 26.463 0.00 25.41  ? 189 TRP A HB3  1 
ATOM   2985 H HD1  . TRP A 1 186 ? 16.372 45.029 26.013 0.00 30.64  ? 189 TRP A HD1  1 
ATOM   2986 H HE1  . TRP A 1 186 ? 14.308 45.378 24.822 0.00 27.84  ? 189 TRP A HE1  1 
ATOM   2987 H HE3  . TRP A 1 186 ? 17.084 49.616 24.406 0.00 27.21  ? 189 TRP A HE3  1 
ATOM   2988 H HZ2  . TRP A 1 186 ? 13.055 47.404 23.441 0.00 29.30  ? 189 TRP A HZ2  1 
ATOM   2989 H HZ3  . TRP A 1 186 ? 15.443 50.662 23.174 0.00 33.83  ? 189 TRP A HZ3  1 
ATOM   2990 H HH2  . TRP A 1 186 ? 13.444 49.581 22.686 0.00 32.72  ? 189 TRP A HH2  1 
ATOM   2991 N N    . LEU A 1 187 ? 20.013 49.404 24.835 1.00 24.18  ? 190 LEU A N    1 
ATOM   2992 C CA   . LEU A 1 187 ? 20.037 50.647 24.079 1.00 23.30  ? 190 LEU A CA   1 
ATOM   2993 C C    . LEU A 1 187 ? 21.082 50.593 22.978 1.00 31.11  ? 190 LEU A C    1 
ATOM   2994 O O    . LEU A 1 187 ? 20.845 51.069 21.863 1.00 27.92  ? 190 LEU A O    1 
ATOM   2995 C CB   . LEU A 1 187 ? 20.309 51.798 25.047 1.00 27.56  ? 190 LEU A CB   1 
ATOM   2996 C CG   . LEU A 1 187 ? 20.267 53.204 24.470 1.00 29.27  ? 190 LEU A CG   1 
ATOM   2997 C CD1  . LEU A 1 187 ? 18.849 53.557 24.045 1.00 33.01  ? 190 LEU A CD1  1 
ATOM   2998 C CD2  . LEU A 1 187 ? 20.769 54.204 25.518 1.00 34.87  ? 190 LEU A CD2  1 
ATOM   2999 H H    . LEU A 1 187 ? 20.273 49.482 25.651 0.00 29.03  ? 190 LEU A H    1 
ATOM   3000 H HA   . LEU A 1 187 ? 19.179 50.798 23.652 0.00 27.97  ? 190 LEU A HA   1 
ATOM   3001 H HB2  . LEU A 1 187 ? 19.643 51.760 25.751 0.00 33.08  ? 190 LEU A HB2  1 
ATOM   3002 H HB3  . LEU A 1 187 ? 21.195 51.671 25.421 0.00 33.08  ? 190 LEU A HB3  1 
ATOM   3003 H HG   . LEU A 1 187 ? 20.840 53.253 23.689 0.00 35.14  ? 190 LEU A HG   1 
ATOM   3004 H HD11 . LEU A 1 187 ? 18.830 54.478 23.742 0.00 39.63  ? 190 LEU A HD11 1 
ATOM   3005 H HD12 . LEU A 1 187 ? 18.579 52.966 23.324 0.00 39.63  ? 190 LEU A HD12 1 
ATOM   3006 H HD13 . LEU A 1 187 ? 18.254 53.446 24.804 0.00 39.63  ? 190 LEU A HD13 1 
ATOM   3007 H HD21 . LEU A 1 187 ? 20.717 55.100 25.150 0.00 41.86  ? 190 LEU A HD21 1 
ATOM   3008 H HD22 . LEU A 1 187 ? 20.211 54.140 26.309 0.00 41.86  ? 190 LEU A HD22 1 
ATOM   3009 H HD23 . LEU A 1 187 ? 21.688 53.991 25.743 0.00 41.86  ? 190 LEU A HD23 1 
ATOM   3010 N N    . ILE A 1 188 ? 22.246 49.990 23.255 1.00 26.36  ? 191 ILE A N    1 
ATOM   3011 C CA   . ILE A 1 188 ? 23.314 49.968 22.222 1.00 25.47  ? 191 ILE A CA   1 
ATOM   3012 C C    . ILE A 1 188 ? 23.254 48.741 21.345 1.00 27.03  ? 191 ILE A C    1 
ATOM   3013 O O    . ILE A 1 188 ? 23.965 48.688 20.332 1.00 30.68  ? 191 ILE A O    1 
ATOM   3014 C CB   . ILE A 1 188 ? 24.711 50.072 22.888 1.00 27.04  ? 191 ILE A CB   1 
ATOM   3015 C CG1  . ILE A 1 188 ? 25.049 48.786 23.622 1.00 34.63  ? 191 ILE A CG1  1 
ATOM   3016 C CG2  . ILE A 1 188 ? 24.753 51.296 23.795 1.00 39.29  ? 191 ILE A CG2  1 
ATOM   3017 C CD1  . ILE A 1 188 ? 26.278 48.901 24.506 1.00 51.27  ? 191 ILE A CD1  1 
ATOM   3018 H H    . ILE A 1 188 ? 22.441 49.602 23.997 0.00 31.65  ? 191 ILE A H    1 
ATOM   3019 H HA   . ILE A 1 188 ? 23.192 50.736 21.643 0.00 30.58  ? 191 ILE A HA   1 
ATOM   3020 H HB   . ILE A 1 188 ? 25.390 50.187 22.205 0.00 32.46  ? 191 ILE A HB   1 
ATOM   3021 H HG12 . ILE A 1 188 ? 24.299 48.541 24.186 0.00 41.57  ? 191 ILE A HG12 1 
ATOM   3022 H HG13 . ILE A 1 188 ? 25.216 48.088 22.970 0.00 41.57  ? 191 ILE A HG13 1 
ATOM   3023 H HG21 . ILE A 1 188 ? 25.678 51.500 24.007 0.00 47.16  ? 191 ILE A HG21 1 
ATOM   3024 H HG22 . ILE A 1 188 ? 24.347 52.046 23.332 0.00 47.16  ? 191 ILE A HG22 1 
ATOM   3025 H HG23 . ILE A 1 188 ? 24.262 51.104 24.608 0.00 47.16  ? 191 ILE A HG23 1 
ATOM   3026 H HD11 . ILE A 1 188 ? 26.549 48.013 24.787 0.00 61.54  ? 191 ILE A HD11 1 
ATOM   3027 H HD12 . ILE A 1 188 ? 26.992 49.320 24.001 0.00 61.54  ? 191 ILE A HD12 1 
ATOM   3028 H HD13 . ILE A 1 188 ? 26.060 49.442 25.281 0.00 61.54  ? 191 ILE A HD13 1 
ATOM   3029 N N    . GLY A 1 189 ? 22.407 47.755 21.663 1.00 28.17  ? 192 GLY A N    1 
ATOM   3030 C CA   . GLY A 1 189 ? 22.324 46.509 20.944 1.00 25.28  ? 192 GLY A CA   1 
ATOM   3031 C C    . GLY A 1 189 ? 21.275 46.495 19.852 1.00 25.42  ? 192 GLY A C    1 
ATOM   3032 O O    . GLY A 1 189 ? 20.801 47.539 19.391 1.00 30.04  ? 192 GLY A O    1 
ATOM   3033 H H    . GLY A 1 189 ? 21.854 47.799 22.319 0.00 33.81  ? 192 GLY A H    1 
ATOM   3034 H HA2  . GLY A 1 189 ? 23.183 46.324 20.534 0.00 30.35  ? 192 GLY A HA2  1 
ATOM   3035 H HA3  . GLY A 1 189 ? 22.113 45.798 21.569 0.00 30.35  ? 192 GLY A HA3  1 
ATOM   3036 N N    A SER A 1 190 ? 20.914 45.289 19.436 0.67 28.63  ? 193 SER A N    1 
ATOM   3037 N N    B SER A 1 190 ? 20.908 45.286 19.439 0.33 28.75  ? 193 SER A N    1 
ATOM   3038 C CA   A SER A 1 190 ? 20.045 45.124 18.275 0.67 31.16  ? 193 SER A CA   1 
ATOM   3039 C CA   B SER A 1 190 ? 20.043 45.113 18.278 0.33 31.24  ? 193 SER A CA   1 
ATOM   3040 C C    A SER A 1 190 ? 18.640 45.656 18.518 0.67 33.98  ? 193 SER A C    1 
ATOM   3041 C C    B SER A 1 190 ? 18.619 45.592 18.518 0.33 33.92  ? 193 SER A C    1 
ATOM   3042 O O    A SER A 1 190 ? 17.952 46.036 17.553 0.67 37.52  ? 193 SER A O    1 
ATOM   3043 O O    B SER A 1 190 ? 17.897 45.855 17.546 0.33 37.15  ? 193 SER A O    1 
ATOM   3044 C CB   A SER A 1 190 ? 19.994 43.650 17.879 0.67 32.87  ? 193 SER A CB   1 
ATOM   3045 C CB   B SER A 1 190 ? 20.033 43.642 17.861 0.33 32.88  ? 193 SER A CB   1 
ATOM   3046 O OG   A SER A 1 190 ? 19.360 42.883 18.879 0.67 34.71  ? 193 SER A OG   1 
ATOM   3047 O OG   B SER A 1 190 ? 21.211 43.315 17.154 0.33 34.07  ? 193 SER A OG   1 
ATOM   3048 H H    A SER A 1 190 ? 21.156 44.550 19.804 0.67 34.37  ? 193 SER A H    1 
ATOM   3049 H H    B SER A 1 190 ? 21.146 44.550 19.814 0.33 34.51  ? 193 SER A H    1 
ATOM   3050 H HA   A SER A 1 190 ? 20.419 45.630 17.537 0.67 37.40  ? 193 SER A HA   1 
ATOM   3051 H HA   B SER A 1 190 ? 20.403 45.639 17.546 0.33 37.50  ? 193 SER A HA   1 
ATOM   3052 H HB2  A SER A 1 190 ? 19.496 43.562 17.051 0.67 39.46  ? 193 SER A HB2  1 
ATOM   3053 H HB2  B SER A 1 190 ? 19.976 43.089 18.655 0.33 39.47  ? 193 SER A HB2  1 
ATOM   3054 H HB3  A SER A 1 190 ? 20.899 43.324 17.758 0.67 39.46  ? 193 SER A HB3  1 
ATOM   3055 H HB3  B SER A 1 190 ? 19.266 43.481 17.288 0.33 39.47  ? 193 SER A HB3  1 
ATOM   3056 H HG   A SER A 1 190 ? 19.793 42.933 19.597 0.67 41.67  ? 193 SER A HG   1 
ATOM   3057 H HG   B SER A 1 190 ? 21.303 43.828 16.495 0.33 40.90  ? 193 SER A HG   1 
ATOM   3058 N N    . GLU A 1 191 ? 18.182 45.684 19.772 1.00 26.70  ? 194 GLU A N    1 
ATOM   3059 C CA   . GLU A 1 191 ? 16.863 46.233 20.078 1.00 28.78  ? 194 GLU A CA   1 
ATOM   3060 C C    . GLU A 1 191 ? 16.811 47.741 19.979 1.00 30.41  ? 194 GLU A C    1 
ATOM   3061 O O    . GLU A 1 191 ? 15.715 48.299 19.832 1.00 28.64  ? 194 GLU A O    1 
ATOM   3062 C CB   . GLU A 1 191 ? 16.437 45.847 21.492 1.00 27.64  ? 194 GLU A CB   1 
ATOM   3063 C CG   . GLU A 1 191 ? 16.124 44.396 21.672 1.00 29.96  ? 194 GLU A CG   1 
ATOM   3064 C CD   . GLU A 1 191 ? 17.358 43.594 22.027 1.00 39.87  ? 194 GLU A CD   1 
ATOM   3065 O OE1  . GLU A 1 191 ? 18.448 44.207 22.083 1.00 35.94  ? 194 GLU A OE1  1 
ATOM   3066 O OE2  . GLU A 1 191 ? 17.230 42.387 22.258 1.00 43.61  ? 194 GLU A OE2  1 
ATOM   3067 H H    . GLU A 1 191 ? 18.613 45.394 20.457 0.00 32.05  ? 194 GLU A H    1 
ATOM   3068 H HA   . GLU A 1 191 ? 16.237 45.854 19.442 0.00 34.54  ? 194 GLU A HA   1 
ATOM   3069 H HB2  . GLU A 1 191 ? 17.157 46.069 22.103 0.00 33.19  ? 194 GLU A HB2  1 
ATOM   3070 H HB3  . GLU A 1 191 ? 15.640 46.350 21.723 0.00 33.19  ? 194 GLU A HB3  1 
ATOM   3071 H HG2  . GLU A 1 191 ? 15.479 44.295 22.389 0.00 35.96  ? 194 GLU A HG2  1 
ATOM   3072 H HG3  . GLU A 1 191 ? 15.759 44.043 20.846 0.00 35.96  ? 194 GLU A HG3  1 
ATOM   3073 N N    . GLY A 1 192 ? 17.960 48.418 20.092 1.00 28.08  ? 195 GLY A N    1 
ATOM   3074 C CA   . GLY A 1 192 ? 17.995 49.863 20.145 1.00 28.11  ? 195 GLY A CA   1 
ATOM   3075 C C    . GLY A 1 192 ? 18.729 50.480 18.985 1.00 31.58  ? 195 GLY A C    1 
ATOM   3076 O O    . GLY A 1 192 ? 18.272 50.396 17.851 1.00 30.55  ? 195 GLY A O    1 
ATOM   3077 H H    . GLY A 1 192 ? 18.735 48.050 20.140 0.00 33.71  ? 195 GLY A H    1 
ATOM   3078 H HA2  . GLY A 1 192 ? 17.087 50.204 20.144 0.00 33.74  ? 195 GLY A HA2  1 
ATOM   3079 H HA3  . GLY A 1 192 ? 18.436 50.140 20.963 0.00 33.74  ? 195 GLY A HA3  1 
ATOM   3080 N N    . ALA A 1 193 ? 19.886 51.107 19.264 1.00 27.25  ? 196 ALA A N    1 
ATOM   3081 C CA   . ALA A 1 193 ? 20.632 51.840 18.252 1.00 32.15  ? 196 ALA A CA   1 
ATOM   3082 C C    . ALA A 1 193 ? 21.421 50.929 17.320 1.00 34.88  ? 196 ALA A C    1 
ATOM   3083 O O    . ALA A 1 193 ? 21.889 51.399 16.273 1.00 36.68  ? 196 ALA A O    1 
ATOM   3084 C CB   . ALA A 1 193 ? 21.584 52.821 18.935 1.00 37.74  ? 196 ALA A CB   1 
ATOM   3085 H H    . ALA A 1 193 ? 20.255 51.117 20.041 0.00 32.71  ? 196 ALA A H    1 
ATOM   3086 H HA   . ALA A 1 193 ? 20.009 52.344 17.705 0.00 38.59  ? 196 ALA A HA   1 
ATOM   3087 H HB1  . ALA A 1 193 ? 22.078 53.307 18.255 0.00 45.30  ? 196 ALA A HB1  1 
ATOM   3088 H HB2  . ALA A 1 193 ? 21.067 53.439 19.474 0.00 45.30  ? 196 ALA A HB2  1 
ATOM   3089 H HB3  . ALA A 1 193 ? 22.199 52.325 19.498 0.00 45.30  ? 196 ALA A HB3  1 
ATOM   3090 N N    . GLY A 1 194 ? 21.609 49.660 17.683 1.00 31.39  ? 197 GLY A N    1 
ATOM   3091 C CA   . GLY A 1 194 ? 22.246 48.723 16.765 1.00 33.53  ? 197 GLY A CA   1 
ATOM   3092 C C    . GLY A 1 194 ? 23.732 48.920 16.602 1.00 37.10  ? 197 GLY A C    1 
ATOM   3093 O O    . GLY A 1 194 ? 24.279 48.605 15.534 1.00 37.21  ? 197 GLY A O    1 
ATOM   3094 H H    . GLY A 1 194 ? 21.381 49.324 18.441 0.00 37.68  ? 197 GLY A H    1 
ATOM   3095 H HA2  . GLY A 1 194 ? 22.100 47.820 17.088 0.00 40.25  ? 197 GLY A HA2  1 
ATOM   3096 H HA3  . GLY A 1 194 ? 21.837 48.815 15.890 0.00 40.25  ? 197 GLY A HA3  1 
ATOM   3097 N N    . ILE A 1 195 ? 24.413 49.430 17.629 1.00 27.40  ? 198 ILE A N    1 
ATOM   3098 C CA   . ILE A 1 195 ? 25.857 49.653 17.518 1.00 30.17  ? 198 ILE A CA   1 
ATOM   3099 C C    . ILE A 1 195 ? 26.626 48.366 17.795 1.00 41.51  ? 198 ILE A C    1 
ATOM   3100 O O    . ILE A 1 195 ? 27.680 48.120 17.199 1.00 40.65  ? 198 ILE A O    1 
ATOM   3101 C CB   . ILE A 1 195 ? 26.288 50.779 18.479 1.00 37.54  ? 198 ILE A CB   1 
ATOM   3102 C CG1  . ILE A 1 195 ? 25.386 52.007 18.305 1.00 48.83  ? 198 ILE A CG1  1 
ATOM   3103 C CG2  . ILE A 1 195 ? 27.752 51.128 18.254 1.00 55.42  ? 198 ILE A CG2  1 
ATOM   3104 C CD1  . ILE A 1 195 ? 25.422 52.595 16.920 1.00 48.52  ? 198 ILE A CD1  1 
ATOM   3105 H H    . ILE A 1 195 ? 24.071 49.652 18.386 0.00 32.89  ? 198 ILE A H    1 
ATOM   3106 H HA   . ILE A 1 195 ? 26.058 49.931 16.610 0.00 36.21  ? 198 ILE A HA   1 
ATOM   3107 H HB   . ILE A 1 195 ? 26.189 50.468 19.392 0.00 45.06  ? 198 ILE A HB   1 
ATOM   3108 H HG12 . ILE A 1 195 ? 24.470 51.750 18.494 0.00 58.61  ? 198 ILE A HG12 1 
ATOM   3109 H HG13 . ILE A 1 195 ? 25.672 52.695 18.926 0.00 58.61  ? 198 ILE A HG13 1 
ATOM   3110 H HG21 . ILE A 1 195 ? 27.962 51.941 18.739 0.00 66.51  ? 198 ILE A HG21 1 
ATOM   3111 H HG22 . ILE A 1 195 ? 28.304 50.398 18.577 0.00 66.51  ? 198 ILE A HG22 1 
ATOM   3112 H HG23 . ILE A 1 195 ? 27.903 51.261 17.305 0.00 66.51  ? 198 ILE A HG23 1 
ATOM   3113 H HD11 . ILE A 1 195 ? 24.981 53.459 16.932 0.00 58.24  ? 198 ILE A HD11 1 
ATOM   3114 H HD12 . ILE A 1 195 ? 26.346 52.699 16.645 0.00 58.24  ? 198 ILE A HD12 1 
ATOM   3115 H HD13 . ILE A 1 195 ? 24.961 51.996 16.311 0.00 58.24  ? 198 ILE A HD13 1 
ATOM   3116 N N    . VAL A 1 196 ? 26.142 47.555 18.724 1.00 33.24  ? 199 VAL A N    1 
ATOM   3117 C CA   . VAL A 1 196 ? 26.773 46.278 19.078 1.00 31.06  ? 199 VAL A CA   1 
ATOM   3118 C C    . VAL A 1 196 ? 26.019 45.171 18.350 1.00 32.58  ? 199 VAL A C    1 
ATOM   3119 O O    . VAL A 1 196 ? 24.782 45.155 18.392 1.00 33.42  ? 199 VAL A O    1 
ATOM   3120 C CB   . VAL A 1 196 ? 26.719 46.054 20.608 1.00 38.10  ? 199 VAL A CB   1 
ATOM   3121 C CG1  . VAL A 1 196 ? 27.184 44.656 20.978 1.00 40.38  ? 199 VAL A CG1  1 
ATOM   3122 C CG2  . VAL A 1 196 ? 27.608 47.109 21.292 1.00 40.13  ? 199 VAL A CG2  1 
ATOM   3123 H H    . VAL A 1 196 ? 25.430 47.721 19.178 0.00 39.90  ? 199 VAL A H    1 
ATOM   3124 H HA   . VAL A 1 196 ? 27.699 46.267 18.788 0.00 37.29  ? 199 VAL A HA   1 
ATOM   3125 H HB   . VAL A 1 196 ? 25.803 46.142 20.914 0.00 45.73  ? 199 VAL A HB   1 
ATOM   3126 H HG11 . VAL A 1 196 ? 27.249 44.591 21.944 0.00 48.47  ? 199 VAL A HG11 1 
ATOM   3127 H HG12 . VAL A 1 196 ? 26.542 44.011 20.645 0.00 48.47  ? 199 VAL A HG12 1 
ATOM   3128 H HG13 . VAL A 1 196 ? 28.053 44.496 20.577 0.00 48.47  ? 199 VAL A HG13 1 
ATOM   3129 H HG21 . VAL A 1 196 ? 27.639 46.926 22.244 0.00 48.17  ? 199 VAL A HG21 1 
ATOM   3130 H HG22 . VAL A 1 196 ? 28.501 47.060 20.917 0.00 48.17  ? 199 VAL A HG22 1 
ATOM   3131 H HG23 . VAL A 1 196 ? 27.231 47.989 21.136 0.00 48.17  ? 199 VAL A HG23 1 
ATOM   3132 N N    . PRO A 1 197 ? 26.714 44.243 17.678 1.00 27.36  ? 200 PRO A N    1 
ATOM   3133 C CA   . PRO A 1 197 ? 26.014 43.186 16.946 1.00 30.27  ? 200 PRO A CA   1 
ATOM   3134 C C    . PRO A 1 197 ? 25.347 42.187 17.901 1.00 31.98  ? 200 PRO A C    1 
ATOM   3135 O O    . PRO A 1 197 ? 25.737 42.032 19.050 1.00 30.41  ? 200 PRO A O    1 
ATOM   3136 C CB   . PRO A 1 197 ? 27.123 42.511 16.131 1.00 37.06  ? 200 PRO A CB   1 
ATOM   3137 C CG   . PRO A 1 197 ? 28.400 42.990 16.680 1.00 43.54  ? 200 PRO A CG   1 
ATOM   3138 C CD   . PRO A 1 197 ? 28.163 44.265 17.412 1.00 35.17  ? 200 PRO A CD   1 
ATOM   3139 H HA   . PRO A 1 197 ? 25.352 43.565 16.347 0.00 36.34  ? 200 PRO A HA   1 
ATOM   3140 H HB2  . PRO A 1 197 ? 27.051 41.548 16.223 0.00 44.48  ? 200 PRO A HB2  1 
ATOM   3141 H HB3  . PRO A 1 197 ? 27.037 42.762 15.198 0.00 44.48  ? 200 PRO A HB3  1 
ATOM   3142 H HG2  . PRO A 1 197 ? 28.753 42.320 17.286 0.00 52.26  ? 200 PRO A HG2  1 
ATOM   3143 H HG3  . PRO A 1 197 ? 29.021 43.137 15.949 0.00 52.26  ? 200 PRO A HG3  1 
ATOM   3144 H HD2  . PRO A 1 197 ? 28.665 44.284 18.241 0.00 42.22  ? 200 PRO A HD2  1 
ATOM   3145 H HD3  . PRO A 1 197 ? 28.401 45.027 16.862 0.00 42.22  ? 200 PRO A HD3  1 
ATOM   3146 N N    . LEU A 1 198 ? 24.363 41.482 17.352 1.00 29.88  ? 201 LEU A N    1 
ATOM   3147 C CA   . LEU A 1 198 ? 23.551 40.568 18.175 1.00 25.16  ? 201 LEU A CA   1 
ATOM   3148 C C    . LEU A 1 198 ? 24.399 39.507 18.852 1.00 29.39  ? 201 LEU A C    1 
ATOM   3149 O O    . LEU A 1 198 ? 24.094 39.094 19.984 1.00 28.86  ? 201 LEU A O    1 
ATOM   3150 C CB   . LEU A 1 198 ? 22.471 39.920 17.296 1.00 27.57  ? 201 LEU A CB   1 
ATOM   3151 C CG   . LEU A 1 198 ? 21.514 38.927 17.940 1.00 31.11  ? 201 LEU A CG   1 
ATOM   3152 C CD1  . LEU A 1 198 ? 20.787 39.538 19.146 1.00 33.13  ? 201 LEU A CD1  1 
ATOM   3153 C CD2  . LEU A 1 198 ? 20.503 38.454 16.901 1.00 36.84  ? 201 LEU A CD2  1 
ATOM   3154 H H    . LEU A 1 198 ? 24.143 41.508 16.522 0.00 35.87  ? 201 LEU A H    1 
ATOM   3155 H HA   . LEU A 1 198 ? 23.119 41.078 18.878 0.00 30.20  ? 201 LEU A HA   1 
ATOM   3156 H HB2  . LEU A 1 198 ? 21.925 40.633 16.930 0.00 33.10  ? 201 LEU A HB2  1 
ATOM   3157 H HB3  . LEU A 1 198 ? 22.921 39.445 16.580 0.00 33.10  ? 201 LEU A HB3  1 
ATOM   3158 H HG   . LEU A 1 198 ? 22.023 38.170 18.268 0.00 37.34  ? 201 LEU A HG   1 
ATOM   3159 H HD11 . LEU A 1 198 ? 20.173 38.881 19.510 0.00 39.76  ? 201 LEU A HD11 1 
ATOM   3160 H HD12 . LEU A 1 198 ? 21.442 39.787 19.817 0.00 39.76  ? 201 LEU A HD12 1 
ATOM   3161 H HD13 . LEU A 1 198 ? 20.297 40.323 18.855 0.00 39.76  ? 201 LEU A HD13 1 
ATOM   3162 H HD21 . LEU A 1 198 ? 20.025 37.687 17.252 0.00 44.22  ? 201 LEU A HD21 1 
ATOM   3163 H HD22 . LEU A 1 198 ? 19.881 39.175 16.715 0.00 44.22  ? 201 LEU A HD22 1 
ATOM   3164 H HD23 . LEU A 1 198 ? 20.975 38.207 16.090 0.00 44.22  ? 201 LEU A HD23 1 
ATOM   3165 N N    A ASN A 1 199 ? 25.454 39.016 18.199 0.79 28.46  ? 202 ASN A N    1 
ATOM   3166 N N    B ASN A 1 199 ? 25.434 39.012 18.174 0.21 28.78  ? 202 ASN A N    1 
ATOM   3167 C CA   A ASN A 1 199 ? 26.230 37.953 18.826 0.79 29.93  ? 202 ASN A CA   1 
ATOM   3168 C CA   B ASN A 1 199 ? 26.288 37.986 18.761 0.21 30.10  ? 202 ASN A CA   1 
ATOM   3169 C C    A ASN A 1 199 ? 26.961 38.451 20.069 0.79 33.65  ? 202 ASN A C    1 
ATOM   3170 C C    B ASN A 1 199 ? 26.917 38.475 20.058 0.21 33.55  ? 202 ASN A C    1 
ATOM   3171 O O    A ASN A 1 199 ? 27.016 37.743 21.086 0.79 30.57  ? 202 ASN A O    1 
ATOM   3172 O O    B ASN A 1 199 ? 26.870 37.788 21.087 0.21 30.28  ? 202 ASN A O    1 
ATOM   3173 C CB   A ASN A 1 199 ? 27.205 37.334 17.817 0.79 35.39  ? 202 ASN A CB   1 
ATOM   3174 C CB   B ASN A 1 199 ? 27.369 37.579 17.757 0.21 35.62  ? 202 ASN A CB   1 
ATOM   3175 C CG   A ASN A 1 199 ? 28.318 38.269 17.449 0.79 36.10  ? 202 ASN A CG   1 
ATOM   3176 C CG   B ASN A 1 199 ? 28.119 36.337 18.178 0.21 32.58  ? 202 ASN A CG   1 
ATOM   3177 O OD1  A ASN A 1 199 ? 28.076 39.377 17.002 0.79 37.92  ? 202 ASN A OD1  1 
ATOM   3178 O OD1  B ASN A 1 199 ? 27.782 35.698 19.173 0.21 33.49  ? 202 ASN A OD1  1 
ATOM   3179 N ND2  A ASN A 1 199 ? 29.559 37.811 17.626 0.79 46.42  ? 202 ASN A ND2  1 
ATOM   3180 N ND2  B ASN A 1 199 ? 29.145 35.982 17.414 0.21 46.60  ? 202 ASN A ND2  1 
ATOM   3181 H H    A ASN A 1 199 ? 25.729 39.272 17.425 0.79 34.16  ? 202 ASN A H    1 
ATOM   3182 H H    B ASN A 1 199 ? 25.660 39.252 17.380 0.21 34.55  ? 202 ASN A H    1 
ATOM   3183 H HA   A ASN A 1 199 ? 25.622 37.252 19.107 0.79 35.93  ? 202 ASN A HA   1 
ATOM   3184 H HA   B ASN A 1 199 ? 25.751 37.204 18.964 0.21 36.13  ? 202 ASN A HA   1 
ATOM   3185 H HB2  A ASN A 1 199 ? 27.597 36.535 18.204 0.79 42.48  ? 202 ASN A HB2  1 
ATOM   3186 H HB2  B ASN A 1 199 ? 26.952 37.402 16.899 0.21 42.76  ? 202 ASN A HB2  1 
ATOM   3187 H HB3  A ASN A 1 199 ? 26.721 37.107 17.007 0.79 42.48  ? 202 ASN A HB3  1 
ATOM   3188 H HB3  B ASN A 1 199 ? 28.009 38.303 17.672 0.21 42.76  ? 202 ASN A HB3  1 
ATOM   3189 H HD21 A ASN A 1 199 ? 29.685 37.018 17.935 0.79 55.71  ? 202 ASN A HD21 1 
ATOM   3190 H HD21 B ASN A 1 199 ? 29.350 36.451 16.723 0.21 55.93  ? 202 ASN A HD21 1 
ATOM   3191 H HD22 A ASN A 1 199 ? 30.232 38.308 17.430 0.79 55.71  ? 202 ASN A HD22 1 
ATOM   3192 H HD22 B ASN A 1 199 ? 29.605 35.282 17.610 0.21 55.93  ? 202 ASN A HD22 1 
ATOM   3193 N N    . ILE A 1 200 ? 27.503 39.676 20.029 1.00 30.45  ? 203 ILE A N    1 
ATOM   3194 C CA   . ILE A 1 200 ? 28.132 40.226 21.228 1.00 25.61  ? 203 ILE A CA   1 
ATOM   3195 C C    . ILE A 1 200 ? 27.072 40.597 22.257 1.00 29.05  ? 203 ILE A C    1 
ATOM   3196 O O    . ILE A 1 200 ? 27.267 40.411 23.460 1.00 28.62  ? 203 ILE A O    1 
ATOM   3197 C CB   . ILE A 1 200 ? 29.001 41.440 20.839 1.00 30.39  ? 203 ILE A CB   1 
ATOM   3198 C CG1  . ILE A 1 200 ? 30.110 40.997 19.881 1.00 35.72  ? 203 ILE A CG1  1 
ATOM   3199 C CG2  . ILE A 1 200 ? 29.578 42.107 22.089 1.00 36.09  ? 203 ILE A CG2  1 
ATOM   3200 C CD1  . ILE A 1 200 ? 30.967 39.877 20.407 1.00 40.24  ? 203 ILE A CD1  1 
ATOM   3201 H H    . ILE A 1 200 ? 27.516 40.188 19.338 0.00 36.55  ? 203 ILE A H    1 
ATOM   3202 H HA   . ILE A 1 200 ? 28.706 39.553 21.627 0.00 30.74  ? 203 ILE A HA   1 
ATOM   3203 H HB   . ILE A 1 200 ? 28.447 42.094 20.384 0.00 36.48  ? 203 ILE A HB   1 
ATOM   3204 H HG12 . ILE A 1 200 ? 29.704 40.693 19.054 0.00 42.87  ? 203 ILE A HG12 1 
ATOM   3205 H HG13 . ILE A 1 200 ? 30.691 41.755 19.706 0.00 42.87  ? 203 ILE A HG13 1 
ATOM   3206 H HG21 . ILE A 1 200 ? 30.271 42.732 21.823 0.00 43.33  ? 203 ILE A HG21 1 
ATOM   3207 H HG22 . ILE A 1 200 ? 28.868 42.579 22.552 0.00 43.33  ? 203 ILE A HG22 1 
ATOM   3208 H HG23 . ILE A 1 200 ? 29.953 41.424 22.667 0.00 43.33  ? 203 ILE A HG23 1 
ATOM   3209 H HD11 . ILE A 1 200 ? 31.755 39.792 19.848 0.00 48.30  ? 203 ILE A HD11 1 
ATOM   3210 H HD12 . ILE A 1 200 ? 31.229 40.081 21.319 0.00 48.30  ? 203 ILE A HD12 1 
ATOM   3211 H HD13 . ILE A 1 200 ? 30.457 39.052 20.387 0.00 48.30  ? 203 ILE A HD13 1 
ATOM   3212 N N    . GLU A 1 201 ? 25.946 41.138 21.813 1.00 24.57  ? 204 GLU A N    1 
ATOM   3213 C CA   . GLU A 1 201 ? 24.855 41.446 22.749 1.00 26.08  ? 204 GLU A CA   1 
ATOM   3214 C C    . GLU A 1 201 ? 24.435 40.198 23.510 1.00 30.78  ? 204 GLU A C    1 
ATOM   3215 O O    . GLU A 1 201 ? 24.163 40.252 24.725 1.00 26.27  ? 204 GLU A O    1 
ATOM   3216 C CB   . GLU A 1 201 ? 23.672 42.028 21.972 1.00 28.26  ? 204 GLU A CB   1 
ATOM   3217 C CG   . GLU A 1 201 ? 22.448 42.277 22.866 1.00 31.41  ? 204 GLU A CG   1 
ATOM   3218 C CD   . GLU A 1 201 ? 21.220 42.696 22.090 1.00 36.09  ? 204 GLU A CD   1 
ATOM   3219 O OE1  . GLU A 1 201 ? 21.335 43.041 20.907 1.00 33.12  ? 204 GLU A OE1  1 
ATOM   3220 O OE2  . GLU A 1 201 ? 20.114 42.619 22.664 1.00 43.52  ? 204 GLU A OE2  1 
ATOM   3221 H H    . GLU A 1 201 ? 25.783 41.336 20.992 0.00 29.50  ? 204 GLU A H    1 
ATOM   3222 H HA   . GLU A 1 201 ? 25.153 42.107 23.394 0.00 31.30  ? 204 GLU A HA   1 
ATOM   3223 H HB2  . GLU A 1 201 ? 23.937 42.874 21.580 0.00 33.93  ? 204 GLU A HB2  1 
ATOM   3224 H HB3  . GLU A 1 201 ? 23.415 41.405 21.275 0.00 33.93  ? 204 GLU A HB3  1 
ATOM   3225 H HG2  . GLU A 1 201 ? 22.235 41.460 23.343 0.00 37.70  ? 204 GLU A HG2  1 
ATOM   3226 H HG3  . GLU A 1 201 ? 22.657 42.984 23.496 0.00 37.70  ? 204 GLU A HG3  1 
ATOM   3227 N N    . THR A 1 202 ? 24.362 39.066 22.816 1.00 24.45  ? 205 THR A N    1 
ATOM   3228 C CA   . THR A 1 202 ? 23.912 37.820 23.464 1.00 22.51  ? 205 THR A CA   1 
ATOM   3229 C C    . THR A 1 202 ? 24.918 37.365 24.499 1.00 25.02  ? 205 THR A C    1 
ATOM   3230 O O    . THR A 1 202 ? 24.536 36.846 25.564 1.00 24.32  ? 205 THR A O    1 
ATOM   3231 C CB   . THR A 1 202 ? 23.696 36.752 22.390 1.00 25.25  ? 205 THR A CB   1 
ATOM   3232 O OG1  . THR A 1 202 ? 22.697 37.211 21.426 1.00 25.98  ? 205 THR A OG1  1 
ATOM   3233 C CG2  . THR A 1 202 ? 23.169 35.459 23.010 1.00 24.19  ? 205 THR A CG2  1 
ATOM   3234 H H    . THR A 1 202 ? 24.562 38.985 21.983 0.00 29.35  ? 205 THR A H    1 
ATOM   3235 H HA   . THR A 1 202 ? 23.068 37.964 23.920 0.00 27.02  ? 205 THR A HA   1 
ATOM   3236 H HB   . THR A 1 202 ? 24.544 36.583 21.951 0.00 30.31  ? 205 THR A HB   1 
ATOM   3237 H HG1  . THR A 1 202 ? 22.960 37.916 21.052 0.00 31.19  ? 205 THR A HG1  1 
ATOM   3238 H HG21 . THR A 1 202 ? 22.976 34.812 22.313 0.00 29.04  ? 205 THR A HG21 1 
ATOM   3239 H HG22 . THR A 1 202 ? 23.832 35.086 23.612 0.00 29.04  ? 205 THR A HG22 1 
ATOM   3240 H HG23 . THR A 1 202 ? 22.356 35.637 23.508 0.00 29.04  ? 205 THR A HG23 1 
ATOM   3241 N N    . LEU A 1 203 ? 26.209 37.474 24.171 1.00 23.87  ? 206 LEU A N    1 
ATOM   3242 C CA   . LEU A 1 203 ? 27.271 37.206 25.150 1.00 25.03  ? 206 LEU A CA   1 
ATOM   3243 C C    . LEU A 1 203 ? 27.095 38.079 26.394 1.00 24.18  ? 206 LEU A C    1 
ATOM   3244 O O    . LEU A 1 203 ? 27.164 37.582 27.526 1.00 25.73  ? 206 LEU A O    1 
ATOM   3245 C CB   . LEU A 1 203 ? 28.631 37.453 24.484 1.00 23.64  ? 206 LEU A CB   1 
ATOM   3246 C CG   . LEU A 1 203 ? 29.857 37.487 25.389 1.00 27.41  ? 206 LEU A CG   1 
ATOM   3247 C CD1  . LEU A 1 203 ? 30.040 36.164 26.118 1.00 30.05  ? 206 LEU A CD1  1 
ATOM   3248 C CD2  . LEU A 1 203 ? 31.088 37.799 24.551 1.00 34.63  ? 206 LEU A CD2  1 
ATOM   3249 H H    . LEU A 1 203 ? 26.497 37.700 23.393 0.00 28.66  ? 206 LEU A H    1 
ATOM   3250 H HA   . LEU A 1 203 ? 27.233 36.280 25.437 0.00 30.05  ? 206 LEU A HA   1 
ATOM   3251 H HB2  . LEU A 1 203 ? 28.777 36.745 23.837 0.00 28.38  ? 206 LEU A HB2  1 
ATOM   3252 H HB3  . LEU A 1 203 ? 28.589 38.311 24.033 0.00 28.38  ? 206 LEU A HB3  1 
ATOM   3253 H HG   . LEU A 1 203 ? 29.740 38.175 26.063 0.00 32.91  ? 206 LEU A HG   1 
ATOM   3254 H HD11 . LEU A 1 203 ? 30.849 36.207 26.652 0.00 36.07  ? 206 LEU A HD11 1 
ATOM   3255 H HD12 . LEU A 1 203 ? 29.273 36.009 26.690 0.00 36.07  ? 206 LEU A HD12 1 
ATOM   3256 H HD13 . LEU A 1 203 ? 30.114 35.451 25.464 0.00 36.07  ? 206 LEU A HD13 1 
ATOM   3257 H HD21 . LEU A 1 203 ? 31.864 37.836 25.132 0.00 41.57  ? 206 LEU A HD21 1 
ATOM   3258 H HD22 . LEU A 1 203 ? 31.204 37.100 23.888 0.00 41.57  ? 206 LEU A HD22 1 
ATOM   3259 H HD23 . LEU A 1 203 ? 30.962 38.654 24.111 0.00 41.57  ? 206 LEU A HD23 1 
ATOM   3260 N N    . LEU A 1 204 ? 26.852 39.387 26.203 1.00 25.72  ? 207 LEU A N    1 
ATOM   3261 C CA   . LEU A 1 204 ? 26.768 40.289 27.356 1.00 25.83  ? 207 LEU A CA   1 
ATOM   3262 C C    . LEU A 1 204 ? 25.567 39.929 28.236 1.00 21.30  ? 207 LEU A C    1 
ATOM   3263 O O    . LEU A 1 204 ? 25.687 39.878 29.472 1.00 25.88  ? 207 LEU A O    1 
ATOM   3264 C CB   . LEU A 1 204 ? 26.663 41.738 26.897 1.00 23.19  ? 207 LEU A CB   1 
ATOM   3265 C CG   . LEU A 1 204 ? 27.873 42.287 26.159 1.00 27.19  ? 207 LEU A CG   1 
ATOM   3266 C CD1  . LEU A 1 204 ? 27.572 43.667 25.635 1.00 29.73  ? 207 LEU A CD1  1 
ATOM   3267 C CD2  . LEU A 1 204 ? 29.069 42.344 27.102 1.00 37.87  ? 207 LEU A CD2  1 
ATOM   3268 H H    . LEU A 1 204 ? 26.735 39.762 25.438 0.00 30.88  ? 207 LEU A H    1 
ATOM   3269 H HA   . LEU A 1 204 ? 27.582 40.202 27.877 0.00 31.00  ? 207 LEU A HA   1 
ATOM   3270 H HB2  . LEU A 1 204 ? 25.902 41.812 26.300 0.00 27.85  ? 207 LEU A HB2  1 
ATOM   3271 H HB3  . LEU A 1 204 ? 26.525 42.294 27.680 0.00 27.85  ? 207 LEU A HB3  1 
ATOM   3272 H HG   . LEU A 1 204 ? 28.089 41.708 25.411 0.00 32.64  ? 207 LEU A HG   1 
ATOM   3273 H HD11 . LEU A 1 204 ? 28.354 44.006 25.171 0.00 35.69  ? 207 LEU A HD11 1 
ATOM   3274 H HD12 . LEU A 1 204 ? 26.821 43.615 25.022 0.00 35.69  ? 207 LEU A HD12 1 
ATOM   3275 H HD13 . LEU A 1 204 ? 27.352 44.247 26.380 0.00 35.69  ? 207 LEU A HD13 1 
ATOM   3276 H HD21 . LEU A 1 204 ? 29.807 42.782 26.650 0.00 45.46  ? 207 LEU A HD21 1 
ATOM   3277 H HD22 . LEU A 1 204 ? 28.823 42.846 27.895 0.00 45.46  ? 207 LEU A HD22 1 
ATOM   3278 H HD23 . LEU A 1 204 ? 29.321 41.440 27.348 0.00 45.46  ? 207 LEU A HD23 1 
ATOM   3279 N N    . PHE A 1 205 ? 24.412 39.659 27.641 1.00 21.49  ? 208 PHE A N    1 
ATOM   3280 C CA   . PHE A 1 205 ? 23.259 39.287 28.471 1.00 20.95  ? 208 PHE A CA   1 
ATOM   3281 C C    . PHE A 1 205 ? 23.502 37.974 29.171 1.00 21.85  ? 208 PHE A C    1 
ATOM   3282 O O    . PHE A 1 205 ? 22.999 37.757 30.275 1.00 22.28  ? 208 PHE A O    1 
ATOM   3283 C CB   . PHE A 1 205 ? 21.980 39.169 27.614 1.00 21.74  ? 208 PHE A CB   1 
ATOM   3284 C CG   . PHE A 1 205 ? 21.287 40.494 27.348 1.00 21.77  ? 208 PHE A CG   1 
ATOM   3285 C CD1  . PHE A 1 205 ? 21.092 41.409 28.356 1.00 21.97  ? 208 PHE A CD1  1 
ATOM   3286 C CD2  . PHE A 1 205 ? 20.770 40.760 26.086 1.00 23.85  ? 208 PHE A CD2  1 
ATOM   3287 C CE1  . PHE A 1 205 ? 20.418 42.611 28.102 1.00 24.12  ? 208 PHE A CE1  1 
ATOM   3288 C CE2  . PHE A 1 205 ? 20.076 41.942 25.833 1.00 24.67  ? 208 PHE A CE2  1 
ATOM   3289 C CZ   . PHE A 1 205 ? 19.927 42.869 26.835 1.00 26.43  ? 208 PHE A CZ   1 
ATOM   3290 H H    . PHE A 1 205 ? 24.268 39.682 26.794 0.00 25.80  ? 208 PHE A H    1 
ATOM   3291 H HA   . PHE A 1 205 ? 23.119 39.986 29.128 0.00 25.16  ? 208 PHE A HA   1 
ATOM   3292 H HB2  . PHE A 1 205 ? 22.216 38.782 26.756 0.00 26.10  ? 208 PHE A HB2  1 
ATOM   3293 H HB3  . PHE A 1 205 ? 21.350 38.594 28.075 0.00 26.10  ? 208 PHE A HB3  1 
ATOM   3294 H HD1  . PHE A 1 205 ? 21.410 41.229 29.211 0.00 26.38  ? 208 PHE A HD1  1 
ATOM   3295 H HD2  . PHE A 1 205 ? 20.889 40.141 25.402 0.00 28.63  ? 208 PHE A HD2  1 
ATOM   3296 H HE1  . PHE A 1 205 ? 20.301 43.233 28.783 0.00 28.96  ? 208 PHE A HE1  1 
ATOM   3297 H HE2  . PHE A 1 205 ? 19.716 42.101 24.991 0.00 29.61  ? 208 PHE A HE2  1 
ATOM   3298 H HZ   . PHE A 1 205 ? 19.495 43.674 26.660 0.00 31.72  ? 208 PHE A HZ   1 
ATOM   3299 N N    . MET A 1 206 ? 24.250 37.042 28.554 1.00 22.63  ? 209 MET A N    1 
ATOM   3300 C CA   . MET A 1 206 ? 24.458 35.771 29.224 1.00 24.20  ? 209 MET A CA   1 
ATOM   3301 C C    . MET A 1 206 ? 25.355 35.935 30.445 1.00 21.96  ? 209 MET A C    1 
ATOM   3302 O O    . MET A 1 206 ? 25.086 35.306 31.492 1.00 24.51  ? 209 MET A O    1 
ATOM   3303 C CB   . MET A 1 206 ? 25.065 34.766 28.255 1.00 28.60  ? 209 MET A CB   1 
ATOM   3304 C CG   . MET A 1 206 ? 25.208 33.403 28.881 1.00 28.50  ? 209 MET A CG   1 
ATOM   3305 S SD   . MET A 1 206 ? 26.845 33.058 29.402 1.00 41.66  ? 209 MET A SD   1 
ATOM   3306 C CE   . MET A 1 206 ? 27.313 32.440 27.823 1.00 26.36  ? 209 MET A CE   1 
ATOM   3307 H H    . MET A 1 206 ? 24.625 37.126 27.785 0.00 27.17  ? 209 MET A H    1 
ATOM   3308 H HA   . MET A 1 206 ? 23.596 35.429 29.511 0.00 29.05  ? 209 MET A HA   1 
ATOM   3309 H HB2  . MET A 1 206 ? 24.492 34.686 27.477 0.00 34.34  ? 209 MET A HB2  1 
ATOM   3310 H HB3  . MET A 1 206 ? 25.946 35.073 27.987 0.00 34.34  ? 209 MET A HB3  1 
ATOM   3311 H HG2  . MET A 1 206 ? 24.630 33.351 29.659 0.00 34.21  ? 209 MET A HG2  1 
ATOM   3312 H HG3  . MET A 1 206 ? 24.953 32.729 28.232 0.00 34.21  ? 209 MET A HG3  1 
ATOM   3313 H HE1  . MET A 1 206 ? 28.243 32.166 27.854 0.00 31.65  ? 209 MET A HE1  1 
ATOM   3314 H HE2  . MET A 1 206 ? 26.751 31.681 27.601 0.00 31.65  ? 209 MET A HE2  1 
ATOM   3315 H HE3  . MET A 1 206 ? 27.197 33.141 27.162 0.00 31.65  ? 209 MET A HE3  1 
ATOM   3316 N N    . VAL A 1 207 ? 26.402 36.745 30.332 1.00 21.67  ? 210 VAL A N    1 
ATOM   3317 C CA   . VAL A 1 207 ? 27.257 37.011 31.497 1.00 23.72  ? 210 VAL A CA   1 
ATOM   3318 C C    . VAL A 1 207 ? 26.436 37.707 32.594 1.00 23.12  ? 210 VAL A C    1 
ATOM   3319 O O    . VAL A 1 207 ? 26.533 37.362 33.787 1.00 23.60  ? 210 VAL A O    1 
ATOM   3320 C CB   . VAL A 1 207 ? 28.479 37.863 31.100 1.00 25.67  ? 210 VAL A CB   1 
ATOM   3321 C CG1  . VAL A 1 207 ? 29.290 38.258 32.315 1.00 30.27  ? 210 VAL A CG1  1 
ATOM   3322 C CG2  . VAL A 1 207 ? 29.368 37.053 30.135 1.00 30.37  ? 210 VAL A CG2  1 
ATOM   3323 H H    . VAL A 1 207 ? 26.638 37.149 29.610 0.00 26.02  ? 210 VAL A H    1 
ATOM   3324 H HA   . VAL A 1 207 ? 27.586 36.163 31.835 0.00 28.47  ? 210 VAL A HA   1 
ATOM   3325 H HB   . VAL A 1 207 ? 28.168 38.675 30.669 0.00 30.82  ? 210 VAL A HB   1 
ATOM   3326 H HG11 . VAL A 1 207 ? 30.163 38.565 32.026 0.00 36.33  ? 210 VAL A HG11 1 
ATOM   3327 H HG12 . VAL A 1 207 ? 28.828 38.969 32.785 0.00 36.33  ? 210 VAL A HG12 1 
ATOM   3328 H HG13 . VAL A 1 207 ? 29.386 37.486 32.895 0.00 36.33  ? 210 VAL A HG13 1 
ATOM   3329 H HG21 . VAL A 1 207 ? 30.138 37.590 29.889 0.00 36.45  ? 210 VAL A HG21 1 
ATOM   3330 H HG22 . VAL A 1 207 ? 29.658 36.241 30.579 0.00 36.45  ? 210 VAL A HG22 1 
ATOM   3331 H HG23 . VAL A 1 207 ? 28.854 36.832 29.343 0.00 36.45  ? 210 VAL A HG23 1 
ATOM   3332 N N    . LEU A 1 208 ? 25.633 38.691 32.214 1.00 21.82  ? 211 LEU A N    1 
ATOM   3333 C CA   . LEU A 1 208 ? 24.809 39.376 33.227 1.00 19.90  ? 211 LEU A CA   1 
ATOM   3334 C C    . LEU A 1 208 ? 23.834 38.428 33.873 1.00 22.72  ? 211 LEU A C    1 
ATOM   3335 O O    . LEU A 1 208 ? 23.684 38.425 35.104 1.00 24.10  ? 211 LEU A O    1 
ATOM   3336 C CB   . LEU A 1 208 ? 24.054 40.553 32.570 1.00 21.47  ? 211 LEU A CB   1 
ATOM   3337 C CG   . LEU A 1 208 ? 24.921 41.740 32.132 1.00 23.54  ? 211 LEU A CG   1 
ATOM   3338 C CD1  . LEU A 1 208 ? 24.021 42.702 31.352 1.00 25.97  ? 211 LEU A CD1  1 
ATOM   3339 C CD2  . LEU A 1 208 ? 25.526 42.432 33.333 1.00 30.05  ? 211 LEU A CD2  1 
ATOM   3340 H H    . LEU A 1 208 ? 25.543 38.978 31.408 0.00 26.20  ? 211 LEU A H    1 
ATOM   3341 H HA   . LEU A 1 208 ? 25.392 39.726 33.918 0.00 23.89  ? 211 LEU A HA   1 
ATOM   3342 H HB2  . LEU A 1 208 ? 23.602 40.219 31.779 0.00 25.78  ? 211 LEU A HB2  1 
ATOM   3343 H HB3  . LEU A 1 208 ? 23.404 40.890 33.206 0.00 25.78  ? 211 LEU A HB3  1 
ATOM   3344 H HG   . LEU A 1 208 ? 25.659 41.446 31.575 0.00 28.26  ? 211 LEU A HG   1 
ATOM   3345 H HD11 . LEU A 1 208 ? 24.549 43.459 31.054 0.00 31.17  ? 211 LEU A HD11 1 
ATOM   3346 H HD12 . LEU A 1 208 ? 23.650 42.237 30.586 0.00 31.17  ? 211 LEU A HD12 1 
ATOM   3347 H HD13 . LEU A 1 208 ? 23.305 43.006 31.932 0.00 31.17  ? 211 LEU A HD13 1 
ATOM   3348 H HD21 . LEU A 1 208 ? 26.013 43.215 33.034 0.00 36.07  ? 211 LEU A HD21 1 
ATOM   3349 H HD22 . LEU A 1 208 ? 24.814 42.695 33.937 0.00 36.07  ? 211 LEU A HD22 1 
ATOM   3350 H HD23 . LEU A 1 208 ? 26.129 41.818 33.780 0.00 36.07  ? 211 LEU A HD23 1 
ATOM   3351 N N    . ASP A 1 209 ? 23.118 37.614 33.056 1.00 20.42  ? 212 ASP A N    1 
ATOM   3352 C CA   . ASP A 1 209 ? 22.094 36.723 33.594 1.00 19.49  ? 212 ASP A CA   1 
ATOM   3353 C C    . ASP A 1 209 ? 22.703 35.709 34.550 1.00 23.43  ? 212 ASP A C    1 
ATOM   3354 O O    . ASP A 1 209 ? 22.146 35.421 35.631 1.00 22.24  ? 212 ASP A O    1 
ATOM   3355 C CB   . ASP A 1 209 ? 21.374 35.940 32.455 1.00 20.42  ? 212 ASP A CB   1 
ATOM   3356 C CG   . ASP A 1 209 ? 20.394 36.780 31.680 1.00 24.87  ? 212 ASP A CG   1 
ATOM   3357 O OD1  . ASP A 1 209 ? 19.958 37.853 32.162 1.00 23.86  ? 212 ASP A OD1  1 
ATOM   3358 O OD2  . ASP A 1 209 ? 19.985 36.319 30.581 1.00 22.17  ? 212 ASP A OD2  1 
ATOM   3359 H H    . ASP A 1 209 ? 23.214 37.568 32.202 0.00 24.51  ? 212 ASP A H    1 
ATOM   3360 H HA   . ASP A 1 209 ? 21.446 37.277 34.057 0.00 23.40  ? 212 ASP A HA   1 
ATOM   3361 H HB2  . ASP A 1 209 ? 22.040 35.609 31.833 0.00 24.52  ? 212 ASP A HB2  1 
ATOM   3362 H HB3  . ASP A 1 209 ? 20.886 35.198 32.845 0.00 24.52  ? 212 ASP A HB3  1 
ATOM   3363 N N    . VAL A 1 210 ? 23.810 35.085 34.151 1.00 22.45  ? 213 VAL A N    1 
ATOM   3364 C CA   . VAL A 1 210 ? 24.382 34.053 35.027 1.00 21.91  ? 213 VAL A CA   1 
ATOM   3365 C C    . VAL A 1 210 ? 24.855 34.690 36.325 1.00 24.15  ? 213 VAL A C    1 
ATOM   3366 O O    . VAL A 1 210 ? 24.658 34.116 37.420 1.00 23.95  ? 213 VAL A O    1 
ATOM   3367 C CB   . VAL A 1 210 ? 25.545 33.358 34.276 1.00 23.74  ? 213 VAL A CB   1 
ATOM   3368 C CG1  . VAL A 1 210 ? 26.304 32.401 35.238 1.00 29.67  ? 213 VAL A CG1  1 
ATOM   3369 C CG2  . VAL A 1 210 ? 25.014 32.566 33.103 1.00 26.16  ? 213 VAL A CG2  1 
ATOM   3370 H H    . VAL A 1 210 ? 24.231 35.229 33.416 0.00 26.95  ? 213 VAL A H    1 
ATOM   3371 H HA   . VAL A 1 210 ? 23.709 33.390 35.248 0.00 26.30  ? 213 VAL A HA   1 
ATOM   3372 H HB   . VAL A 1 210 ? 26.155 34.037 33.949 0.00 28.50  ? 213 VAL A HB   1 
ATOM   3373 H HG11 . VAL A 1 210 ? 26.872 31.813 34.716 0.00 35.62  ? 213 VAL A HG11 1 
ATOM   3374 H HG12 . VAL A 1 210 ? 26.845 32.929 35.846 0.00 35.62  ? 213 VAL A HG12 1 
ATOM   3375 H HG13 . VAL A 1 210 ? 25.658 31.878 35.738 0.00 35.62  ? 213 VAL A HG13 1 
ATOM   3376 H HG21 . VAL A 1 210 ? 25.760 32.163 32.632 0.00 31.41  ? 213 VAL A HG21 1 
ATOM   3377 H HG22 . VAL A 1 210 ? 24.418 31.876 33.432 0.00 31.41  ? 213 VAL A HG22 1 
ATOM   3378 H HG23 . VAL A 1 210 ? 24.533 33.164 32.510 0.00 31.41  ? 213 VAL A HG23 1 
ATOM   3379 N N    . SER A 1 211 ? 25.448 35.881 36.237 1.00 24.25  ? 214 SER A N    1 
ATOM   3380 C CA   . SER A 1 211 ? 25.937 36.566 37.441 1.00 22.45  ? 214 SER A CA   1 
ATOM   3381 C C    . SER A 1 211 ? 24.786 36.978 38.349 1.00 23.82  ? 214 SER A C    1 
ATOM   3382 O O    . SER A 1 211 ? 24.869 36.847 39.571 1.00 24.68  ? 214 SER A O    1 
ATOM   3383 C CB   . SER A 1 211 ? 26.742 37.806 37.034 1.00 22.82  ? 214 SER A CB   1 
ATOM   3384 O OG   . SER A 1 211 ? 27.891 37.399 36.314 1.00 27.90  ? 214 SER A OG   1 
ATOM   3385 H H    . SER A 1 211 ? 25.580 36.312 35.504 0.00 29.11  ? 214 SER A H    1 
ATOM   3386 H HA   . SER A 1 211 ? 26.514 35.961 37.932 0.00 26.95  ? 214 SER A HA   1 
ATOM   3387 H HB2  . SER A 1 211 ? 26.194 38.375 36.472 0.00 27.40  ? 214 SER A HB2  1 
ATOM   3388 H HB3  . SER A 1 211 ? 27.014 38.289 37.830 0.00 27.40  ? 214 SER A HB3  1 
ATOM   3389 H HG   . SER A 1 211 ? 27.663 36.978 35.624 0.00 33.49  ? 214 SER A HG   1 
ATOM   3390 N N    . ALA A 1 212 ? 23.704 37.488 37.758 1.00 21.40  ? 215 ALA A N    1 
ATOM   3391 C CA   . ALA A 1 212 ? 22.593 38.034 38.560 1.00 21.51  ? 215 ALA A CA   1 
ATOM   3392 C C    . ALA A 1 212 ? 21.701 36.968 39.117 1.00 21.55  ? 215 ALA A C    1 
ATOM   3393 O O    . ALA A 1 212 ? 20.884 37.227 40.015 1.00 23.92  ? 215 ALA A O    1 
ATOM   3394 C CB   . ALA A 1 212 ? 21.746 38.996 37.672 1.00 22.64  ? 215 ALA A CB   1 
ATOM   3395 H H    . ALA A 1 212 ? 23.587 37.531 36.907 0.00 25.69  ? 215 ALA A H    1 
ATOM   3396 H HA   . ALA A 1 212 ? 22.974 38.513 39.312 0.00 25.83  ? 215 ALA A HA   1 
ATOM   3397 H HB1  . ALA A 1 212 ? 21.023 39.362 38.205 0.00 27.18  ? 215 ALA A HB1  1 
ATOM   3398 H HB2  . ALA A 1 212 ? 22.315 39.712 37.350 0.00 27.18  ? 215 ALA A HB2  1 
ATOM   3399 H HB3  . ALA A 1 212 ? 21.384 38.498 36.922 0.00 27.18  ? 215 ALA A HB3  1 
ATOM   3400 N N    . LYS A 1 213 ? 21.826 35.729 38.604 1.00 22.01  ? 216 LYS A N    1 
ATOM   3401 C CA   . LYS A 1 213 ? 20.976 34.614 39.081 1.00 21.43  ? 216 LYS A CA   1 
ATOM   3402 C C    . LYS A 1 213 ? 21.839 33.582 39.847 1.00 22.47  ? 216 LYS A C    1 
ATOM   3403 O O    . LYS A 1 213 ? 21.567 33.386 41.043 1.00 26.08  ? 216 LYS A O    1 
ATOM   3404 C CB   . LYS A 1 213 ? 20.264 33.958 37.904 1.00 20.70  ? 216 LYS A CB   1 
ATOM   3405 C CG   . LYS A 1 213 ? 19.253 34.895 37.220 1.00 22.41  ? 216 LYS A CG   1 
ATOM   3406 C CD   . LYS A 1 213 ? 18.507 34.234 36.089 1.00 23.21  ? 216 LYS A CD   1 
ATOM   3407 C CE   . LYS A 1 213 ? 17.242 34.985 35.711 1.00 21.77  ? 216 LYS A CE   1 
ATOM   3408 N NZ   . LYS A 1 213 ? 17.561 36.202 34.973 1.00 20.62  ? 216 LYS A NZ   1 
ATOM   3409 H HA   . LYS A 1 213 ? 20.340 35.009 39.711 1.00 25.73  ? 216 LYS A HA   1 
ATOM   3410 H HB2  . LYS A 1 213 ? 20.933 33.652 37.258 1.00 24.85  ? 216 LYS A HB2  1 
ATOM   3411 H HB3  . LYS A 1 213 ? 19.814 33.147 38.217 1.00 24.85  ? 216 LYS A HB3  1 
ATOM   3412 H HG2  . LYS A 1 213 ? 18.596 35.226 37.865 1.00 26.90  ? 216 LYS A HG2  1 
ATOM   3413 H HG3  . LYS A 1 213 ? 19.702 35.689 36.865 1.00 26.90  ? 216 LYS A HG3  1 
ATOM   3414 H HD2  . LYS A 1 213 ? 19.095 34.166 35.309 1.00 27.86  ? 216 LYS A HD2  1 
ATOM   3415 H HD3  . LYS A 1 213 ? 18.282 33.316 36.342 1.00 27.86  ? 216 LYS A HD3  1 
ATOM   3416 H HE2  . LYS A 1 213 ? 16.681 34.436 35.125 1.00 26.13  ? 216 LYS A HE2  1 
ATOM   3417 H HE3  . LYS A 1 213 ? 16.754 35.258 36.514 1.00 26.13  ? 216 LYS A HE3  1 
ATOM   3418 H HZ2  . LYS A 1 213 ? 17.671 36.135 34.099 1.00 24.75  ? 216 LYS A HZ2  1 
ATOM   3419 N N    . VAL A 1 214 ? 22.803 32.949 39.166 1.00 21.69  ? 217 VAL A N    1 
ATOM   3420 C CA   . VAL A 1 214 ? 23.579 31.912 39.848 1.00 22.03  ? 217 VAL A CA   1 
ATOM   3421 C C    . VAL A 1 214 ? 24.585 32.557 40.786 1.00 21.76  ? 217 VAL A C    1 
ATOM   3422 O O    . VAL A 1 214 ? 24.793 32.064 41.909 1.00 26.28  ? 217 VAL A O    1 
ATOM   3423 C CB   . VAL A 1 214 ? 24.291 31.001 38.794 1.00 21.93  ? 217 VAL A CB   1 
ATOM   3424 C CG1  . VAL A 1 214 ? 25.097 29.918 39.529 1.00 25.81  ? 217 VAL A CG1  1 
ATOM   3425 C CG2  . VAL A 1 214 ? 23.266 30.377 37.880 1.00 27.16  ? 217 VAL A CG2  1 
ATOM   3426 H H    . VAL A 1 214 ? 23.014 33.097 38.345 0.00 26.04  ? 217 VAL A H    1 
ATOM   3427 H HA   . VAL A 1 214 ? 22.992 31.355 40.383 0.00 26.44  ? 217 VAL A HA   1 
ATOM   3428 H HB   . VAL A 1 214 ? 24.897 31.528 38.249 0.00 26.33  ? 217 VAL A HB   1 
ATOM   3429 H HG11 . VAL A 1 214 ? 25.407 29.262 38.885 0.00 30.99  ? 217 VAL A HG11 1 
ATOM   3430 H HG12 . VAL A 1 214 ? 25.856 30.332 39.969 0.00 30.99  ? 217 VAL A HG12 1 
ATOM   3431 H HG13 . VAL A 1 214 ? 24.527 29.491 40.187 0.00 30.99  ? 217 VAL A HG13 1 
ATOM   3432 H HG21 . VAL A 1 214 ? 23.690 29.674 37.363 0.00 32.61  ? 217 VAL A HG21 1 
ATOM   3433 H HG22 . VAL A 1 214 ? 22.549 30.005 38.417 0.00 32.61  ? 217 VAL A HG22 1 
ATOM   3434 H HG23 . VAL A 1 214 ? 22.915 31.059 37.286 0.00 32.61  ? 217 VAL A HG23 1 
ATOM   3435 N N    . GLY A 1 215 ? 25.227 33.659 40.372 1.00 24.06  ? 218 GLY A N    1 
ATOM   3436 C CA   . GLY A 1 215 ? 26.162 34.317 41.301 1.00 27.95  ? 218 GLY A CA   1 
ATOM   3437 C C    . GLY A 1 215 ? 25.458 34.849 42.539 1.00 29.69  ? 218 GLY A C    1 
ATOM   3438 O O    . GLY A 1 215 ? 25.872 34.593 43.681 1.00 27.53  ? 218 GLY A O    1 
ATOM   3439 H H    . GLY A 1 215 ? 25.146 34.027 39.600 0.00 28.89  ? 218 GLY A H    1 
ATOM   3440 H HA2  . GLY A 1 215 ? 26.839 33.681 41.582 0.00 33.55  ? 218 GLY A HA2  1 
ATOM   3441 H HA3  . GLY A 1 215 ? 26.594 35.060 40.850 0.00 33.55  ? 218 GLY A HA3  1 
ATOM   3442 N N    . PHE A 1 216 ? 24.391 35.617 42.321 1.00 25.50  ? 219 PHE A N    1 
ATOM   3443 C CA   . PHE A 1 216 ? 23.528 36.057 43.422 1.00 23.43  ? 219 PHE A CA   1 
ATOM   3444 C C    . PHE A 1 216 ? 23.127 34.922 44.325 1.00 25.97  ? 219 PHE A C    1 
ATOM   3445 O O    . PHE A 1 216 ? 23.208 35.030 45.551 1.00 27.54  ? 219 PHE A O    1 
ATOM   3446 C CB   . PHE A 1 216 ? 22.284 36.722 42.764 1.00 23.24  ? 219 PHE A CB   1 
ATOM   3447 C CG   . PHE A 1 216 ? 21.253 37.262 43.744 1.00 25.58  ? 219 PHE A CG   1 
ATOM   3448 C CD1  . PHE A 1 216 ? 20.302 36.423 44.315 1.00 26.54  ? 219 PHE A CD1  1 
ATOM   3449 C CD2  . PHE A 1 216 ? 21.169 38.628 43.993 1.00 27.23  ? 219 PHE A CD2  1 
ATOM   3450 C CE1  . PHE A 1 216 ? 19.334 36.921 45.181 1.00 29.53  ? 219 PHE A CE1  1 
ATOM   3451 C CE2  . PHE A 1 216 ? 20.191 39.140 44.845 1.00 30.22  ? 219 PHE A CE2  1 
ATOM   3452 C CZ   . PHE A 1 216 ? 19.268 38.291 45.441 1.00 27.24  ? 219 PHE A CZ   1 
ATOM   3453 H H    . PHE A 1 216 ? 24.142 35.897 41.547 0.00 30.61  ? 219 PHE A H    1 
ATOM   3454 H HA   . PHE A 1 216 ? 23.995 36.691 43.989 0.00 28.13  ? 219 PHE A HA   1 
ATOM   3455 H HB2  . PHE A 1 216 ? 22.585 37.466 42.219 0.00 27.90  ? 219 PHE A HB2  1 
ATOM   3456 H HB3  . PHE A 1 216 ? 21.840 36.062 42.209 0.00 27.90  ? 219 PHE A HB3  1 
ATOM   3457 H HD1  . PHE A 1 216 ? 20.313 35.515 44.115 0.00 31.86  ? 219 PHE A HD1  1 
ATOM   3458 H HD2  . PHE A 1 216 ? 21.773 39.207 43.587 0.00 32.69  ? 219 PHE A HD2  1 
ATOM   3459 H HE1  . PHE A 1 216 ? 18.730 36.341 45.587 0.00 35.45  ? 219 PHE A HE1  1 
ATOM   3460 H HE2  . PHE A 1 216 ? 20.156 40.054 45.014 0.00 36.27  ? 219 PHE A HE2  1 
ATOM   3461 H HZ   . PHE A 1 216 ? 18.614 38.631 46.007 0.00 32.70  ? 219 PHE A HZ   1 
ATOM   3462 N N    . GLY A 1 217 ? 22.660 33.795 43.743 1.00 24.70  ? 220 GLY A N    1 
ATOM   3463 C CA   . GLY A 1 217 ? 22.172 32.718 44.581 1.00 25.27  ? 220 GLY A CA   1 
ATOM   3464 C C    . GLY A 1 217 ? 23.268 32.040 45.382 1.00 26.17  ? 220 GLY A C    1 
ATOM   3465 O O    . GLY A 1 217 ? 23.040 31.599 46.514 1.00 29.30  ? 220 GLY A O    1 
ATOM   3466 H H    . GLY A 1 217 ? 22.621 33.649 42.896 0.00 29.65  ? 220 GLY A H    1 
ATOM   3467 H HA2  . GLY A 1 217 ? 21.518 33.072 45.204 0.00 30.33  ? 220 GLY A HA2  1 
ATOM   3468 H HA3  . GLY A 1 217 ? 21.748 32.048 44.023 0.00 30.33  ? 220 GLY A HA3  1 
ATOM   3469 N N    . LEU A 1 218 ? 24.482 31.933 44.807 1.00 23.73  ? 221 LEU A N    1 
ATOM   3470 C CA   . LEU A 1 218 ? 25.593 31.350 45.567 1.00 25.67  ? 221 LEU A CA   1 
ATOM   3471 C C    . LEU A 1 218 ? 25.918 32.176 46.805 1.00 34.41  ? 221 LEU A C    1 
ATOM   3472 O O    . LEU A 1 218 ? 26.189 31.623 47.876 1.00 36.55  ? 221 LEU A O    1 
ATOM   3473 C CB   . LEU A 1 218 ? 26.822 31.255 44.661 1.00 29.58  ? 221 LEU A CB   1 
ATOM   3474 C CG   . LEU A 1 218 ? 26.758 30.095 43.642 1.00 34.39  ? 221 LEU A CG   1 
ATOM   3475 C CD1  . LEU A 1 218 ? 27.867 30.218 42.614 1.00 35.24  ? 221 LEU A CD1  1 
ATOM   3476 C CD2  . LEU A 1 218 ? 26.853 28.753 44.380 1.00 36.68  ? 221 LEU A CD2  1 
ATOM   3477 H H    . LEU A 1 218 ? 24.677 32.182 44.007 0.00 28.49  ? 221 LEU A H    1 
ATOM   3478 H HA   . LEU A 1 218 ? 25.343 30.460 45.862 0.00 30.82  ? 221 LEU A HA   1 
ATOM   3479 H HB2  . LEU A 1 218 ? 26.907 32.083 44.163 0.00 35.51  ? 221 LEU A HB2  1 
ATOM   3480 H HB3  . LEU A 1 218 ? 27.607 31.119 45.215 0.00 35.51  ? 221 LEU A HB3  1 
ATOM   3481 H HG   . LEU A 1 218 ? 25.914 30.131 43.166 0.00 41.28  ? 221 LEU A HG   1 
ATOM   3482 H HD11 . LEU A 1 218 ? 27.774 29.506 41.963 0.00 42.30  ? 221 LEU A HD11 1 
ATOM   3483 H HD12 . LEU A 1 218 ? 27.796 31.080 42.175 0.00 42.30  ? 221 LEU A HD12 1 
ATOM   3484 H HD13 . LEU A 1 218 ? 28.723 30.146 43.064 0.00 42.30  ? 221 LEU A HD13 1 
ATOM   3485 H HD21 . LEU A 1 218 ? 27.014 28.047 43.734 0.00 44.03  ? 221 LEU A HD21 1 
ATOM   3486 H HD22 . LEU A 1 218 ? 27.585 28.792 45.015 0.00 44.03  ? 221 LEU A HD22 1 
ATOM   3487 H HD23 . LEU A 1 218 ? 26.019 28.589 44.847 0.00 44.03  ? 221 LEU A HD23 1 
ATOM   3488 N N    . ILE A 1 219 ? 25.893 33.503 46.679 1.00 26.33  ? 222 ILE A N    1 
ATOM   3489 C CA   . ILE A 1 219 ? 26.162 34.364 47.834 1.00 31.37  ? 222 ILE A CA   1 
ATOM   3490 C C    . ILE A 1 219 ? 25.069 34.197 48.888 1.00 31.83  ? 222 ILE A C    1 
ATOM   3491 O O    . ILE A 1 219 ? 25.357 34.009 50.090 1.00 32.96  ? 222 ILE A O    1 
ATOM   3492 C CB   . ILE A 1 219 ? 26.286 35.822 47.380 1.00 31.93  ? 222 ILE A CB   1 
ATOM   3493 C CG1  . ILE A 1 219 ? 27.465 35.992 46.429 1.00 32.53  ? 222 ILE A CG1  1 
ATOM   3494 C CG2  . ILE A 1 219 ? 26.430 36.756 48.571 1.00 36.59  ? 222 ILE A CG2  1 
ATOM   3495 C CD1  . ILE A 1 219 ? 27.428 37.309 45.639 1.00 38.28  ? 222 ILE A CD1  1 
ATOM   3496 H H    . ILE A 1 219 ? 25.727 33.925 45.948 0.00 31.60  ? 222 ILE A H    1 
ATOM   3497 H HA   . ILE A 1 219 ? 27.003 34.096 48.236 0.00 37.66  ? 222 ILE A HA   1 
ATOM   3498 H HB   . ILE A 1 219 ? 25.471 36.052 46.907 0.00 38.32  ? 222 ILE A HB   1 
ATOM   3499 H HG12 . ILE A 1 219 ? 28.287 35.976 46.944 0.00 39.05  ? 222 ILE A HG12 1 
ATOM   3500 H HG13 . ILE A 1 219 ? 27.461 35.262 45.790 0.00 39.05  ? 222 ILE A HG13 1 
ATOM   3501 H HG21 . ILE A 1 219 ? 26.796 37.601 48.267 0.00 43.92  ? 222 ILE A HG21 1 
ATOM   3502 H HG22 . ILE A 1 219 ? 25.557 36.898 48.969 0.00 43.92  ? 222 ILE A HG22 1 
ATOM   3503 H HG23 . ILE A 1 219 ? 27.027 36.351 49.219 0.00 43.92  ? 222 ILE A HG23 1 
ATOM   3504 H HD11 . ILE A 1 219 ? 28.144 37.305 44.984 0.00 45.95  ? 222 ILE A HD11 1 
ATOM   3505 H HD12 . ILE A 1 219 ? 26.571 37.386 45.192 0.00 45.95  ? 222 ILE A HD12 1 
ATOM   3506 H HD13 . ILE A 1 219 ? 27.548 38.050 46.254 0.00 45.95  ? 222 ILE A HD13 1 
ATOM   3507 N N    . LEU A 1 220 ? 23.807 34.202 48.452 1.00 27.96  ? 223 LEU A N    1 
ATOM   3508 C CA   . LEU A 1 220 ? 22.701 34.153 49.412 1.00 25.11  ? 223 LEU A CA   1 
ATOM   3509 C C    . LEU A 1 220 ? 22.644 32.809 50.133 1.00 29.97  ? 223 LEU A C    1 
ATOM   3510 O O    . LEU A 1 220 ? 22.513 32.767 51.357 1.00 31.52  ? 223 LEU A O    1 
ATOM   3511 C CB   . LEU A 1 220 ? 21.372 34.402 48.646 1.00 25.91  ? 223 LEU A CB   1 
ATOM   3512 C CG   . LEU A 1 220 ? 20.111 34.270 49.528 1.00 25.46  ? 223 LEU A CG   1 
ATOM   3513 C CD1  . LEU A 1 220 ? 20.085 35.338 50.591 1.00 31.89  ? 223 LEU A CD1  1 
ATOM   3514 C CD2  . LEU A 1 220 ? 18.881 34.377 48.622 1.00 30.47  ? 223 LEU A CD2  1 
ATOM   3515 H H    . LEU A 1 220 ? 23.569 34.234 47.626 0.00 33.57  ? 223 LEU A H    1 
ATOM   3516 H HA   . LEU A 1 220 ? 22.827 34.842 50.083 0.00 30.07  ? 223 LEU A HA   1 
ATOM   3517 H HB2  . LEU A 1 220 ? 21.387 35.301 48.282 0.00 31.11  ? 223 LEU A HB2  1 
ATOM   3518 H HB3  . LEU A 1 220 ? 21.301 33.754 47.928 0.00 31.11  ? 223 LEU A HB3  1 
ATOM   3519 H HG   . LEU A 1 220 ? 20.106 33.415 49.987 0.00 30.56  ? 223 LEU A HG   1 
ATOM   3520 H HD11 . LEU A 1 220 ? 19.265 35.255 51.102 0.00 38.28  ? 223 LEU A HD11 1 
ATOM   3521 H HD12 . LEU A 1 220 ? 20.852 35.221 51.174 0.00 38.28  ? 223 LEU A HD12 1 
ATOM   3522 H HD13 . LEU A 1 220 ? 20.123 36.208 50.165 0.00 38.28  ? 223 LEU A HD13 1 
ATOM   3523 H HD21 . LEU A 1 220 ? 18.081 34.297 49.165 0.00 36.57  ? 223 LEU A HD21 1 
ATOM   3524 H HD22 . LEU A 1 220 ? 18.892 35.238 48.174 0.00 36.57  ? 223 LEU A HD22 1 
ATOM   3525 H HD23 . LEU A 1 220 ? 18.909 33.663 47.966 0.00 36.57  ? 223 LEU A HD23 1 
ATOM   3526 N N    . LEU A 1 221 ? 22.710 31.701 49.389 1.00 29.77  ? 224 LEU A N    1 
ATOM   3527 C CA   . LEU A 1 221 ? 22.454 30.398 49.998 1.00 31.87  ? 224 LEU A CA   1 
ATOM   3528 C C    . LEU A 1 221 ? 23.632 29.883 50.804 1.00 35.35  ? 224 LEU A C    1 
ATOM   3529 O O    . LEU A 1 221 ? 23.485 28.857 51.479 1.00 38.00  ? 224 LEU A O    1 
ATOM   3530 C CB   . LEU A 1 221 ? 22.068 29.380 48.920 1.00 27.44  ? 224 LEU A CB   1 
ATOM   3531 C CG   . LEU A 1 221 ? 20.836 29.767 48.112 1.00 31.76  ? 224 LEU A CG   1 
ATOM   3532 C CD1  . LEU A 1 221 ? 20.580 28.758 46.994 1.00 32.55  ? 224 LEU A CD1  1 
ATOM   3533 C CD2  . LEU A 1 221 ? 19.619 29.864 49.025 1.00 34.98  ? 224 LEU A CD2  1 
ATOM   3534 H H    . LEU A 1 221 ? 22.897 31.680 48.550 0.00 35.73  ? 224 LEU A H    1 
ATOM   3535 H HA   . LEU A 1 221 ? 21.701 30.478 50.604 0.00 38.26  ? 224 LEU A HA   1 
ATOM   3536 H HB2  . LEU A 1 221 ? 22.809 29.287 48.302 0.00 32.94  ? 224 LEU A HB2  1 
ATOM   3537 H HB3  . LEU A 1 221 ? 21.885 28.529 49.349 0.00 32.94  ? 224 LEU A HB3  1 
ATOM   3538 H HG   . LEU A 1 221 ? 20.987 30.634 47.704 0.00 38.13  ? 224 LEU A HG   1 
ATOM   3539 H HD11 . LEU A 1 221 ? 19.785 29.023 46.506 0.00 39.07  ? 224 LEU A HD11 1 
ATOM   3540 H HD12 . LEU A 1 221 ? 21.346 28.746 46.399 0.00 39.07  ? 224 LEU A HD12 1 
ATOM   3541 H HD13 . LEU A 1 221 ? 20.451 27.880 47.385 0.00 39.07  ? 224 LEU A HD13 1 
ATOM   3542 H HD21 . LEU A 1 221 ? 18.818 29.909 48.480 0.00 41.99  ? 224 LEU A HD21 1 
ATOM   3543 H HD22 . LEU A 1 221 ? 19.588 29.080 49.594 0.00 41.99  ? 224 LEU A HD22 1 
ATOM   3544 H HD23 . LEU A 1 221 ? 19.694 30.664 49.568 0.00 41.99  ? 224 LEU A HD23 1 
ATOM   3545 N N    . ARG A 1 222 ? 24.783 30.549 50.750 1.00 43.23  ? 225 ARG A N    1 
ATOM   3546 C CA   . ARG A 1 222 ? 25.914 30.217 51.617 1.00 47.59  ? 225 ARG A CA   1 
ATOM   3547 C C    . ARG A 1 222 ? 25.924 31.046 52.894 1.00 47.39  ? 225 ARG A C    1 
ATOM   3548 O O    . ARG A 1 222 ? 26.815 30.858 53.731 1.00 51.24  ? 225 ARG A O    1 
ATOM   3549 C CB   . ARG A 1 222 ? 27.225 30.407 50.853 1.00 50.52  ? 225 ARG A CB   1 
ATOM   3550 C CG   . ARG A 1 222 ? 27.516 29.281 49.850 1.00 63.51  ? 225 ARG A CG   1 
ATOM   3551 C CD   . ARG A 1 222 ? 28.882 29.411 49.178 1.00 68.79  ? 225 ARG A CD   1 
ATOM   3552 N NE   . ARG A 1 222 ? 29.866 30.089 50.019 1.00 70.59  ? 225 ARG A NE   1 
ATOM   3553 C CZ   . ARG A 1 222 ? 30.543 29.508 50.998 1.00 89.27  ? 225 ARG A CZ   1 
ATOM   3554 N NH1  . ARG A 1 222 ? 30.386 28.223 51.282 1.00 86.43  ? 225 ARG A NH1  1 
ATOM   3555 N NH2  . ARG A 1 222 ? 31.401 30.233 51.713 1.00 96.94  ? 225 ARG A NH2  1 
ATOM   3556 H H    . ARG A 1 222 ? 24.935 31.205 50.215 1.00 51.81  ? 225 ARG A H    1 
ATOM   3557 H HA   . ARG A 1 222 ? 25.860 29.282 51.872 1.00 57.04  ? 225 ARG A HA   1 
ATOM   3558 H HB2  . ARG A 1 222 ? 27.182 31.241 50.359 1.00 60.56  ? 225 ARG A HB2  1 
ATOM   3559 H HB3  . ARG A 1 222 ? 27.957 30.435 51.489 1.00 60.56  ? 225 ARG A HB3  1 
ATOM   3560 H HG2  . ARG A 1 222 ? 27.494 28.430 50.317 1.00 76.22  ? 225 ARG A HG2  1 
ATOM   3561 H HG3  . ARG A 1 222 ? 26.840 29.296 49.155 1.00 76.22  ? 225 ARG A HG3  1 
ATOM   3562 H HD2  . ARG A 1 222 ? 29.221 28.525 48.975 1.00 82.56  ? 225 ARG A HD2  1 
ATOM   3563 H HD3  . ARG A 1 222 ? 28.784 29.924 48.360 1.00 82.56  ? 225 ARG A HD3  1 
ATOM   3564 H HE   . ARG A 1 222 ? 30.016 30.922 49.869 1.00 84.72  ? 225 ARG A HE   1 
ATOM   3565 H HH11 . ARG A 1 222 ? 29.834 27.746 50.826 1.00 103.72 ? 225 ARG A HH11 1 
ATOM   3566 H HH12 . ARG A 1 222 ? 30.836 27.866 51.922 1.00 103.72 ? 225 ARG A HH12 1 
ATOM   3567 H HH21 . ARG A 1 222 ? 31.510 31.067 51.536 1.00 116.34 ? 225 ARG A HH21 1 
ATOM   3568 H HH22 . ARG A 1 222 ? 31.846 29.867 52.351 1.00 116.34 ? 225 ARG A HH22 1 
ATOM   3569 N N    . SER A 1 223 ? 24.937 31.917 53.082 1.00 43.33  ? 226 SER A N    1 
ATOM   3570 C CA   . SER A 1 223 ? 24.895 32.828 54.214 1.00 49.67  ? 226 SER A CA   1 
ATOM   3571 C C    . SER A 1 223 ? 24.089 32.242 55.367 1.00 42.45  ? 226 SER A C    1 
ATOM   3572 O O    . SER A 1 223 ? 23.123 31.513 55.171 1.00 43.46  ? 226 SER A O    1 
ATOM   3573 C CB   . SER A 1 223 ? 24.264 34.162 53.784 1.00 54.68  ? 226 SER A CB   1 
ATOM   3574 O OG   . SER A 1 223 ? 23.816 34.896 54.915 1.00 62.07  ? 226 SER A OG   1 
ATOM   3575 H H    . SER A 1 223 ? 24.263 31.999 52.553 0.00 51.94  ? 226 SER A H    1 
ATOM   3576 H HA   . SER A 1 223 ? 25.799 32.985 54.532 0.00 59.62  ? 226 SER A HA   1 
ATOM   3577 H HB2  . SER A 1 223 ? 24.926 34.686 53.308 0.00 65.63  ? 226 SER A HB2  1 
ATOM   3578 H HB3  . SER A 1 223 ? 23.506 33.980 53.205 0.00 65.63  ? 226 SER A HB3  1 
ATOM   3579 H HG   . SER A 1 223 ? 23.306 35.516 54.671 0.00 74.50  ? 226 SER A HG   1 
ATOM   3580 N N    . ARG A 1 224 ? 24.506 32.573 56.598 1.00 44.53  ? 227 ARG A N    1 
ATOM   3581 C CA   . ARG A 1 224 ? 23.696 32.194 57.747 1.00 43.82  ? 227 ARG A CA   1 
ATOM   3582 C C    . ARG A 1 224 ? 22.438 33.039 57.884 1.00 40.67  ? 227 ARG A C    1 
ATOM   3583 O O    . ARG A 1 224 ? 21.558 32.693 58.681 1.00 43.75  ? 227 ARG A O    1 
ATOM   3584 C CB   . ARG A 1 224 ? 24.540 32.293 59.031 1.00 51.07  ? 227 ARG A CB   1 
ATOM   3585 C CG   . ARG A 1 224 ? 24.297 31.142 59.997 1.00 69.72  ? 227 ARG A CG   1 
ATOM   3586 C CD   . ARG A 1 224 ? 24.914 29.839 59.508 1.00 82.53  ? 227 ARG A CD   1 
ATOM   3587 N NE   . ARG A 1 224 ? 24.182 28.675 59.997 1.00 86.66  ? 227 ARG A NE   1 
ATOM   3588 C CZ   . ARG A 1 224 ? 24.391 27.430 59.589 1.00 103.23 ? 227 ARG A CZ   1 
ATOM   3589 N NH1  . ARG A 1 224 ? 25.314 27.144 58.683 1.00 115.85 ? 227 ARG A NH1  1 
ATOM   3590 N NH2  . ARG A 1 224 ? 23.658 26.446 60.105 1.00 94.96  ? 227 ARG A NH2  1 
ATOM   3591 H H    . ARG A 1 224 ? 25.229 33.002 56.780 0.00 53.37  ? 227 ARG A H    1 
ATOM   3592 H HA   . ARG A 1 224 ? 23.416 31.271 57.645 0.00 52.52  ? 227 ARG A HA   1 
ATOM   3593 H HB2  . ARG A 1 224 ? 25.480 32.288 58.790 0.00 61.30  ? 227 ARG A HB2  1 
ATOM   3594 H HB3  . ARG A 1 224 ? 24.319 33.119 59.489 0.00 61.30  ? 227 ARG A HB3  1 
ATOM   3595 H HG2  . ARG A 1 224 ? 24.691 31.359 60.856 0.00 83.67  ? 227 ARG A HG2  1 
ATOM   3596 H HG3  . ARG A 1 224 ? 23.341 31.005 60.095 0.00 83.67  ? 227 ARG A HG3  1 
ATOM   3597 H HD2  . ARG A 1 224 ? 24.899 29.822 58.538 0.00 99.04  ? 227 ARG A HD2  1 
ATOM   3598 H HD3  . ARG A 1 224 ? 25.828 29.779 59.826 0.00 99.04  ? 227 ARG A HD3  1 
ATOM   3599 H HE   . ARG A 1 224 ? 23.574 28.804 60.591 0.00 104.00 ? 227 ARG A HE   1 
ATOM   3600 H HH11 . ARG A 1 224 ? 25.795 27.772 58.346 0.00 139.03 ? 227 ARG A HH11 1 
ATOM   3601 H HH12 . ARG A 1 224 ? 25.433 26.330 58.433 0.00 139.03 ? 227 ARG A HH12 1 
ATOM   3602 H HH21 . ARG A 1 224 ? 23.058 26.621 60.695 0.00 113.97 ? 227 ARG A HH21 1 
ATOM   3603 H HH22 . ARG A 1 224 ? 23.785 25.635 59.848 0.00 113.97 ? 227 ARG A HH22 1 
ATOM   3604 N N    . ALA A 1 225 ? 22.301 34.112 57.095 1.00 41.84  ? 228 ALA A N    1 
ATOM   3605 C CA   . ALA A 1 225 ? 21.161 35.005 57.225 1.00 44.13  ? 228 ALA A CA   1 
ATOM   3606 C C    . ALA A 1 225 ? 19.842 34.337 56.856 1.00 49.25  ? 228 ALA A C    1 
ATOM   3607 O O    . ALA A 1 225 ? 18.783 34.800 57.289 1.00 46.91  ? 228 ALA A O    1 
ATOM   3608 C CB   . ALA A 1 225 ? 21.358 36.236 56.329 1.00 43.07  ? 228 ALA A CB   1 
ATOM   3609 H H    . ALA A 1 225 ? 22.857 34.339 56.479 0.00 50.22  ? 228 ALA A H    1 
ATOM   3610 H HA   . ALA A 1 225 ? 21.107 35.291 58.150 0.00 52.97  ? 228 ALA A HA   1 
ATOM   3611 H HB1  . ALA A 1 225 ? 20.612 36.843 56.459 0.00 51.69  ? 228 ALA A HB1  1 
ATOM   3612 H HB2  . ALA A 1 225 ? 22.188 36.674 56.574 0.00 51.69  ? 228 ALA A HB2  1 
ATOM   3613 H HB3  . ALA A 1 225 ? 21.395 35.950 55.403 0.00 51.69  ? 228 ALA A HB3  1 
ATOM   3614 N N    . ILE A 1 226 ? 19.876 33.257 56.073 1.00 35.28  ? 229 ILE A N    1 
ATOM   3615 C CA   . ILE A 1 226 ? 18.617 32.650 55.610 1.00 32.35  ? 229 ILE A CA   1 
ATOM   3616 C C    . ILE A 1 226 ? 18.007 31.728 56.650 1.00 36.37  ? 229 ILE A C    1 
ATOM   3617 O O    . ILE A 1 226 ? 16.879 31.271 56.469 1.00 41.09  ? 229 ILE A O    1 
ATOM   3618 C CB   . ILE A 1 226 ? 18.838 31.881 54.295 1.00 34.60  ? 229 ILE A CB   1 
ATOM   3619 C CG1  . ILE A 1 226 ? 19.803 30.704 54.508 1.00 38.79  ? 229 ILE A CG1  1 
ATOM   3620 C CG2  . ILE A 1 226 ? 19.353 32.821 53.217 1.00 36.41  ? 229 ILE A CG2  1 
ATOM   3621 C CD1  . ILE A 1 226 ? 19.861 29.766 53.299 1.00 37.84  ? 229 ILE A CD1  1 
ATOM   3622 H H    . ILE A 1 226 ? 20.592 32.864 55.803 0.00 42.35  ? 229 ILE A H    1 
ATOM   3623 H HA   . ILE A 1 226 ? 17.977 33.359 55.436 0.00 38.83  ? 229 ILE A HA   1 
ATOM   3624 H HB   . ILE A 1 226 ? 17.987 31.518 54.004 0.00 41.53  ? 229 ILE A HB   1 
ATOM   3625 H HG12 . ILE A 1 226 ? 20.695 31.051 54.664 0.00 46.56  ? 229 ILE A HG12 1 
ATOM   3626 H HG13 . ILE A 1 226 ? 19.508 30.189 55.275 0.00 46.56  ? 229 ILE A HG13 1 
ATOM   3627 H HG21 . ILE A 1 226 ? 19.386 32.344 52.373 0.00 43.70  ? 229 ILE A HG21 1 
ATOM   3628 H HG22 . ILE A 1 226 ? 18.752 33.579 53.145 0.00 43.70  ? 229 ILE A HG22 1 
ATOM   3629 H HG23 . ILE A 1 226 ? 20.241 33.125 53.461 0.00 43.70  ? 229 ILE A HG23 1 
ATOM   3630 H HD11 . ILE A 1 226 ? 20.429 29.010 53.514 0.00 45.42  ? 229 ILE A HD11 1 
ATOM   3631 H HD12 . ILE A 1 226 ? 18.964 29.459 53.095 0.00 45.42  ? 229 ILE A HD12 1 
ATOM   3632 H HD13 . ILE A 1 226 ? 20.226 30.250 52.542 0.00 45.42  ? 229 ILE A HD13 1 
ATOM   3633 N N    . PHE A 1 227 ? 18.738 31.421 57.731 1.00 40.78  ? 230 PHE A N    1 
ATOM   3634 C CA   . PHE A 1 227 ? 18.230 30.574 58.800 1.00 39.86  ? 230 PHE A CA   1 
ATOM   3635 C C    . PHE A 1 227 ? 17.740 31.429 59.957 1.00 47.14  ? 230 PHE A C    1 
ATOM   3636 O O    . PHE A 1 227 ? 18.327 32.469 60.273 1.00 41.94  ? 230 PHE A O    1 
ATOM   3637 C CB   . PHE A 1 227 ? 19.324 29.621 59.314 1.00 42.81  ? 230 PHE A CB   1 
ATOM   3638 C CG   . PHE A 1 227 ? 19.713 28.569 58.314 1.00 41.67  ? 230 PHE A CG   1 
ATOM   3639 C CD1  . PHE A 1 227 ? 19.045 27.360 58.278 1.00 51.27  ? 230 PHE A CD1  1 
ATOM   3640 C CD2  . PHE A 1 227 ? 20.731 28.798 57.407 1.00 50.94  ? 230 PHE A CD2  1 
ATOM   3641 C CE1  . PHE A 1 227 ? 19.391 26.389 57.360 1.00 49.76  ? 230 PHE A CE1  1 
ATOM   3642 C CE2  . PHE A 1 227 ? 21.079 27.833 56.478 1.00 54.83  ? 230 PHE A CE2  1 
ATOM   3643 C CZ   . PHE A 1 227 ? 20.411 26.629 56.454 1.00 57.00  ? 230 PHE A CZ   1 
ATOM   3644 H H    . PHE A 1 227 ? 19.541 31.699 57.862 0.00 48.94  ? 230 PHE A H    1 
ATOM   3645 H HA   . PHE A 1 227 ? 17.489 30.049 58.460 0.00 47.84  ? 230 PHE A HA   1 
ATOM   3646 H HB2  . PHE A 1 227 ? 20.116 30.138 59.527 0.00 51.38  ? 230 PHE A HB2  1 
ATOM   3647 H HB3  . PHE A 1 227 ? 18.998 29.169 60.109 0.00 51.38  ? 230 PHE A HB3  1 
ATOM   3648 H HD1  . PHE A 1 227 ? 18.355 27.198 58.879 0.00 61.54  ? 230 PHE A HD1  1 
ATOM   3649 H HD2  . PHE A 1 227 ? 21.186 29.609 57.421 0.00 61.14  ? 230 PHE A HD2  1 
ATOM   3650 H HE1  . PHE A 1 227 ? 18.940 25.576 57.350 0.00 59.72  ? 230 PHE A HE1  1 
ATOM   3651 H HE2  . PHE A 1 227 ? 21.764 27.998 55.871 0.00 65.80  ? 230 PHE A HE2  1 
ATOM   3652 H HZ   . PHE A 1 227 ? 20.643 25.979 55.831 0.00 68.41  ? 230 PHE A HZ   1 
ATOM   3653 N N    . GLY A 1 228 ? 16.669 30.981 60.604 1.00 45.63  ? 231 GLY A N    1 
ATOM   3654 C CA   . GLY A 1 228 ? 16.222 31.645 61.799 1.00 43.56  ? 231 GLY A CA   1 
ATOM   3655 C C    . GLY A 1 228 ? 17.238 31.503 62.923 1.00 46.50  ? 231 GLY A C    1 
ATOM   3656 O O    . GLY A 1 228 ? 18.051 30.582 62.947 1.00 56.00  ? 231 GLY A O    1 
ATOM   3657 H H    . GLY A 1 228 ? 16.196 30.302 60.368 0.00 54.77  ? 231 GLY A H    1 
ATOM   3658 H HA2  . GLY A 1 228 ? 16.091 32.589 61.617 0.00 52.28  ? 231 GLY A HA2  1 
ATOM   3659 H HA3  . GLY A 1 228 ? 15.381 31.260 62.091 0.00 52.28  ? 231 GLY A HA3  1 
ATOM   3660 N N    . GLU A 1 229 ? 17.204 32.453 63.856 1.00 57.19  ? 232 GLU A N    1 
ATOM   3661 C CA   . GLU A 1 229 ? 18.094 32.404 65.005 1.00 58.94  ? 232 GLU A CA   1 
ATOM   3662 C C    . GLU A 1 229 ? 17.613 31.325 65.966 1.00 61.61  ? 232 GLU A C    1 
ATOM   3663 O O    . GLU A 1 229 ? 16.516 31.427 66.526 1.00 65.40  ? 232 GLU A O    1 
ATOM   3664 C CB   . GLU A 1 229 ? 18.136 33.768 65.694 1.00 71.98  ? 232 GLU A CB   1 
ATOM   3665 C CG   . GLU A 1 229 ? 19.455 34.066 66.390 1.00 60.61  ? 232 GLU A CG   1 
ATOM   3666 C CD   . GLU A 1 229 ? 19.510 35.474 66.948 1.00 66.23  ? 232 GLU A CD   1 
ATOM   3667 O OE1  . GLU A 1 229 ? 20.562 35.835 67.526 1.00 48.45  ? 232 GLU A OE1  1 
ATOM   3668 O OE2  . GLU A 1 229 ? 18.507 36.210 66.814 1.00 68.44  ? 232 GLU A OE2  1 
ATOM   3669 H H    . GLU A 1 229 ? 16.675 33.131 63.845 0.00 68.64  ? 232 GLU A H    1 
ATOM   3670 H HA   . GLU A 1 229 ? 18.995 32.187 64.717 0.00 70.73  ? 232 GLU A HA   1 
ATOM   3671 H HB2  . GLU A 1 229 ? 17.991 34.458 65.028 0.00 86.39  ? 232 GLU A HB2  1 
ATOM   3672 H HB3  . GLU A 1 229 ? 17.435 33.800 66.363 0.00 86.39  ? 232 GLU A HB3  1 
ATOM   3673 H HG2  . GLU A 1 229 ? 19.572 33.445 67.127 0.00 72.75  ? 232 GLU A HG2  1 
ATOM   3674 H HG3  . GLU A 1 229 ? 20.180 33.965 65.753 0.00 72.75  ? 232 GLU A HG3  1 
ATOM   3675 N N    . ALA A 1 230 ? 18.428 30.290 66.160 1.00 55.18  ? 233 ALA A N    1 
ATOM   3676 C CA   . ALA A 1 230 ? 18.029 29.149 66.966 1.00 57.22  ? 233 ALA A CA   1 
ATOM   3677 C C    . ALA A 1 230 ? 19.227 28.604 67.723 1.00 63.13  ? 233 ALA A C    1 
ATOM   3678 O O    . ALA A 1 230 ? 20.380 28.802 67.336 1.00 70.54  ? 233 ALA A O    1 
ATOM   3679 C CB   . ALA A 1 230 ? 17.411 28.038 66.102 1.00 65.62  ? 233 ALA A CB   1 
ATOM   3680 H H    . ALA A 1 230 ? 19.220 30.229 65.832 0.00 66.22  ? 233 ALA A H    1 
ATOM   3681 H HA   . ALA A 1 230 ? 17.372 29.441 67.618 0.00 68.67  ? 233 ALA A HA   1 
ATOM   3682 H HB1  . ALA A 1 230 ? 17.147 27.301 66.676 0.00 78.76  ? 233 ALA A HB1  1 
ATOM   3683 H HB2  . ALA A 1 230 ? 16.635 28.392 65.640 0.00 78.76  ? 233 ALA A HB2  1 
ATOM   3684 H HB3  . ALA A 1 230 ? 18.070 27.735 65.458 0.00 78.76  ? 233 ALA A HB3  1 
ATOM   3685 N N    . GLU A 1 231 ? 18.932 27.910 68.823 1.00 60.82  ? 234 GLU A N    1 
ATOM   3686 C CA   . GLU A 1 231 ? 19.960 27.297 69.651 1.00 61.13  ? 234 GLU A CA   1 
ATOM   3687 C C    . GLU A 1 231 ? 20.311 25.902 69.138 1.00 77.94  ? 234 GLU A C    1 
ATOM   3688 O O    . GLU A 1 231 ? 19.507 24.975 69.236 1.00 84.67  ? 234 GLU A O    1 
ATOM   3689 C CB   . GLU A 1 231 ? 19.496 27.221 71.109 1.00 55.05  ? 234 GLU A CB   1 
ATOM   3690 C CG   . GLU A 1 231 ? 20.611 27.057 72.102 1.00 62.18  ? 234 GLU A CG   1 
ATOM   3691 C CD   . GLU A 1 231 ? 21.588 28.210 72.055 1.00 50.25  ? 234 GLU A CD   1 
ATOM   3692 O OE1  . GLU A 1 231 ? 21.125 29.360 71.901 1.00 61.51  ? 234 GLU A OE1  1 
ATOM   3693 O OE2  . GLU A 1 231 ? 22.801 27.971 72.191 1.00 53.87  ? 234 GLU A OE2  1 
ATOM   3694 H H    . GLU A 1 231 ? 18.133 27.781 69.112 0.00 73.00  ? 234 GLU A H    1 
ATOM   3695 H HA   . GLU A 1 231 ? 20.762 27.841 69.618 0.00 73.36  ? 234 GLU A HA   1 
ATOM   3696 H HB2  . GLU A 1 231 ? 19.026 28.041 71.328 0.00 66.07  ? 234 GLU A HB2  1 
ATOM   3697 H HB3  . GLU A 1 231 ? 18.901 26.461 71.207 0.00 66.07  ? 234 GLU A HB3  1 
ATOM   3698 H HG2  . GLU A 1 231 ? 20.238 27.012 72.996 0.00 74.63  ? 234 GLU A HG2  1 
ATOM   3699 H HG3  . GLU A 1 231 ? 21.097 26.241 71.904 0.00 74.63  ? 234 GLU A HG3  1 
HETATM 3700 C C46  . LI1 B 2 .   ? 4.738  61.321 20.282 1.00 74.77  ? 301 LI1 A C46  1 
HETATM 3701 C C47  . LI1 B 2 .   ? 4.094  61.262 21.663 1.00 69.36  ? 301 LI1 A C47  1 
HETATM 3702 C C48  . LI1 B 2 .   ? 5.036  60.876 22.798 1.00 63.15  ? 301 LI1 A C48  1 
HETATM 3703 C C49  . LI1 B 2 .   ? 5.661  59.539 22.461 1.00 73.30  ? 301 LI1 A C49  1 
HETATM 3704 C C50  . LI1 B 2 .   ? 4.127  60.695 24.014 1.00 62.74  ? 301 LI1 A C50  1 
HETATM 3705 C C51  . LI1 B 2 .   ? 4.849  60.459 25.335 1.00 60.53  ? 301 LI1 A C51  1 
HETATM 3706 C C52  . LI1 B 2 .   ? 3.979  60.700 26.559 1.00 71.13  ? 301 LI1 A C52  1 
HETATM 3707 C C53  . LI1 B 2 .   ? 4.762  61.045 27.815 1.00 67.86  ? 301 LI1 A C53  1 
HETATM 3708 C C55  . LI1 B 2 .   ? 5.842  60.033 28.158 1.00 62.02  ? 301 LI1 A C55  1 
HETATM 3709 C C56  . LI1 B 2 .   ? 6.979  60.599 28.993 1.00 81.47  ? 301 LI1 A C56  1 
HETATM 3710 C C57  . LI1 B 2 .   ? 8.165  59.649 29.131 1.00 69.78  ? 301 LI1 A C57  1 
HETATM 3711 C C58  . LI1 B 2 .   ? 9.213  60.037 30.163 1.00 75.31  ? 301 LI1 A C58  1 
HETATM 3712 C C59  . LI1 B 2 .   ? 8.995  61.445 30.688 1.00 91.41  ? 301 LI1 A C59  1 
HETATM 3713 C C60  . LI1 B 2 .   ? 9.281  59.044 31.311 1.00 60.81  ? 301 LI1 A C60  1 
HETATM 3714 H H461 . LI1 B 2 .   ? 5.631  61.693 20.346 1.00 89.74  ? 301 LI1 A H461 1 
HETATM 3715 H H462 . LI1 B 2 .   ? 4.817  60.419 19.934 1.00 89.74  ? 301 LI1 A H462 1 
HETATM 3716 H H471 . LI1 B 2 .   ? 3.705  62.131 21.848 1.00 83.24  ? 301 LI1 A H471 1 
HETATM 3717 H H472 . LI1 B 2 .   ? 3.360  60.628 21.623 1.00 83.24  ? 301 LI1 A H472 1 
HETATM 3718 H H48  . LI1 B 2 .   ? 5.731  61.535 22.951 1.00 75.79  ? 301 LI1 A H48  1 
HETATM 3719 C C50  . LI1 C 2 .   ? 24.133 21.874 24.645 1.00 63.46  ? 302 LI1 A C50  1 
HETATM 3720 C C51  . LI1 C 2 .   ? 23.271 22.711 25.587 1.00 46.56  ? 302 LI1 A C51  1 
HETATM 3721 C C52  . LI1 C 2 .   ? 23.453 22.366 27.056 1.00 58.60  ? 302 LI1 A C52  1 
HETATM 3722 C C53  . LI1 C 2 .   ? 22.480 21.313 27.568 1.00 62.32  ? 302 LI1 A C53  1 
HETATM 3723 C C55  . LI1 C 2 .   ? 22.013 21.545 28.996 1.00 64.49  ? 302 LI1 A C55  1 
HETATM 3724 C C56  . LI1 C 2 .   ? 22.400 20.438 29.969 1.00 61.75  ? 302 LI1 A C56  1 
HETATM 3725 C C57  . LI1 C 2 .   ? 23.790 20.617 30.579 1.00 62.55  ? 302 LI1 A C57  1 
HETATM 3726 C C58  . LI1 C 2 .   ? 23.873 20.479 32.096 1.00 59.66  ? 302 LI1 A C58  1 
HETATM 3727 C C45  . LI1 D 2 .   ? -2.705 30.978 18.330 1.00 66.32  ? 303 LI1 A C45  1 
HETATM 3728 C C46  . LI1 D 2 .   ? -1.295 30.927 18.900 1.00 65.21  ? 303 LI1 A C46  1 
HETATM 3729 C C47  . LI1 D 2 .   ? -1.231 30.226 20.252 1.00 63.90  ? 303 LI1 A C47  1 
HETATM 3730 C C48  . LI1 D 2 .   ? -2.018 30.906 21.370 1.00 47.98  ? 303 LI1 A C48  1 
HETATM 3731 C C50  . LI1 D 2 .   ? -1.265 30.838 22.697 1.00 42.96  ? 303 LI1 A C50  1 
HETATM 3732 C C51  . LI1 D 2 .   ? -2.078 31.242 23.923 1.00 46.09  ? 303 LI1 A C51  1 
HETATM 3733 C C52  . LI1 D 2 .   ? -1.471 30.795 25.240 1.00 50.59  ? 303 LI1 A C52  1 
HETATM 3734 C C53  . LI1 D 2 .   ? -2.455 30.818 26.399 1.00 47.33  ? 303 LI1 A C53  1 
HETATM 3735 C C55  . LI1 D 2 .   ? -1.822 30.571 27.756 1.00 51.95  ? 303 LI1 A C55  1 
HETATM 3736 C C56  . LI1 D 2 .   ? -1.765 31.804 28.648 1.00 67.23  ? 303 LI1 A C56  1 
HETATM 3737 C C57  . LI1 D 2 .   ? -3.083 32.566 28.740 1.00 64.42  ? 303 LI1 A C57  1 
HETATM 3738 C C58  . LI1 D 2 .   ? -3.025 33.906 29.469 1.00 62.27  ? 303 LI1 A C58  1 
HETATM 3739 H H451 . LI1 D 2 .   ? -2.724 31.595 17.580 1.00 79.60  ? 303 LI1 A H451 1 
HETATM 3740 H H452 . LI1 D 2 .   ? -2.919 30.102 17.970 1.00 79.60  ? 303 LI1 A H452 1 
HETATM 3741 H H461 . LI1 D 2 .   ? -0.967 31.835 18.989 1.00 78.27  ? 303 LI1 A H461 1 
HETATM 3742 H H462 . LI1 D 2 .   ? -0.724 30.466 18.267 1.00 78.27  ? 303 LI1 A H462 1 
HETATM 3743 C C45  . LI1 E 2 .   ? 26.428 59.621 53.649 1.00 74.66  ? 304 LI1 A C45  1 
HETATM 3744 C C46  . LI1 E 2 .   ? 25.333 59.912 52.630 1.00 68.74  ? 304 LI1 A C46  1 
HETATM 3745 C C47  . LI1 E 2 .   ? 24.570 58.664 52.196 1.00 64.11  ? 304 LI1 A C47  1 
HETATM 3746 C C48  . LI1 E 2 .   ? 23.675 58.845 50.967 1.00 67.92  ? 304 LI1 A C48  1 
HETATM 3747 C C50  . LI1 E 2 .   ? 24.518 59.086 49.715 1.00 64.09  ? 304 LI1 A C50  1 
HETATM 3748 C C51  . LI1 E 2 .   ? 23.798 59.797 48.574 1.00 63.15  ? 304 LI1 A C51  1 
HETATM 3749 C C52  . LI1 E 2 .   ? 23.192 58.848 47.552 1.00 79.73  ? 304 LI1 A C52  1 
HETATM 3750 C C53  . LI1 E 2 .   ? 22.678 59.542 46.300 1.00 75.51  ? 304 LI1 A C53  1 
HETATM 3751 C C55  . LI1 E 2 .   ? 23.553 59.336 45.076 1.00 65.93  ? 304 LI1 A C55  1 
HETATM 3752 C C56  . LI1 E 2 .   ? 23.224 60.265 43.923 1.00 61.59  ? 304 LI1 A C56  1 
HETATM 3753 C C57  . LI1 E 2 .   ? 23.135 59.563 42.574 1.00 64.51  ? 304 LI1 A C57  1 
HETATM 3754 C C58  . LI1 E 2 .   ? 22.864 60.458 41.375 1.00 63.84  ? 304 LI1 A C58  1 
HETATM 3755 C C59  . LI1 E 2 .   ? 22.738 59.655 40.091 1.00 68.59  ? 304 LI1 A C59  1 
HETATM 3756 H H451 . LI1 E 2 .   ? 26.087 59.022 54.330 1.00 89.60  ? 304 LI1 A H451 1 
HETATM 3757 H H452 . LI1 E 2 .   ? 27.147 59.150 53.198 1.00 89.60  ? 304 LI1 A H452 1 
HETATM 3758 H H461 . LI1 E 2 .   ? 24.716 60.551 53.019 1.00 82.50  ? 304 LI1 A H461 1 
HETATM 3759 H H462 . LI1 E 2 .   ? 25.741 60.328 51.854 1.00 82.50  ? 304 LI1 A H462 1 
HETATM 3760 H H471 . LI1 E 2 .   ? 24.032 58.368 52.946 1.00 76.95  ? 304 LI1 A H471 1 
HETATM 3761 H H472 . LI1 E 2 .   ? 25.218 57.964 52.022 1.00 76.95  ? 304 LI1 A H472 1 
HETATM 3762 C C46  . LI1 F 2 .   ? 27.458 50.740 45.211 1.00 79.32  ? 305 LI1 A C46  1 
HETATM 3763 C C47  . LI1 F 2 .   ? 26.823 51.948 44.536 1.00 99.41  ? 305 LI1 A C47  1 
HETATM 3764 C C48  . LI1 F 2 .   ? 26.221 51.679 43.154 1.00 91.37  ? 305 LI1 A C48  1 
HETATM 3765 C C50  . LI1 F 2 .   ? 27.290 51.779 42.064 1.00 90.45  ? 305 LI1 A C50  1 
HETATM 3766 C C51  . LI1 F 2 .   ? 26.759 51.856 40.636 1.00 79.17  ? 305 LI1 A C51  1 
HETATM 3767 C C52  . LI1 F 2 .   ? 27.843 51.698 39.582 1.00 83.55  ? 305 LI1 A C52  1 
HETATM 3768 C C53  . LI1 F 2 .   ? 27.456 52.231 38.213 1.00 86.95  ? 305 LI1 A C53  1 
HETATM 3769 C C55  . LI1 F 2 .   ? 26.146 51.677 37.684 1.00 80.09  ? 305 LI1 A C55  1 
HETATM 3770 C C56  . LI1 F 2 .   ? 26.124 51.499 36.175 1.00 73.02  ? 305 LI1 A C56  1 
HETATM 3771 C C57  . LI1 F 2 .   ? 27.065 50.409 35.678 1.00 72.31  ? 305 LI1 A C57  1 
HETATM 3772 C C58  . LI1 F 2 .   ? 27.198 50.298 34.168 1.00 76.42  ? 305 LI1 A C58  1 
HETATM 3773 C C59  . LI1 F 2 .   ? 26.088 51.055 33.459 1.00 67.10  ? 305 LI1 A C59  1 
HETATM 3774 C C60  . LI1 F 2 .   ? 27.235 48.849 33.713 1.00 74.19  ? 305 LI1 A C60  1 
HETATM 3775 H H461 . LI1 F 2 .   ? 27.992 50.244 44.572 1.00 95.19  ? 305 LI1 A H461 1 
HETATM 3776 H H462 . LI1 F 2 .   ? 28.050 51.051 45.914 1.00 95.19  ? 305 LI1 A H462 1 
HETATM 3777 H H471 . LI1 F 2 .   ? 27.499 52.640 44.464 1.00 119.31 ? 305 LI1 A H471 1 
HETATM 3778 H H472 . LI1 F 2 .   ? 26.133 52.290 45.126 1.00 119.31 ? 305 LI1 A H472 1 
HETATM 3779 C C18  . OLC G 3 .   ? 20.419 19.507 32.760 1.00 58.07  ? 306 OLC A C18  1 
HETATM 3780 C C10  . OLC G 3 .   ? 12.924 21.011 35.811 1.00 52.00  ? 306 OLC A C10  1 
HETATM 3781 C C9   . OLC G 3 .   ? 12.265 21.035 36.987 1.00 57.60  ? 306 OLC A C9   1 
HETATM 3782 C C17  . OLC G 3 .   ? 19.547 19.922 33.967 1.00 68.73  ? 306 OLC A C17  1 
HETATM 3783 C C11  . OLC G 3 .   ? 13.180 22.174 34.847 1.00 55.77  ? 306 OLC A C11  1 
HETATM 3784 C C8   . OLC G 3 .   ? 11.474 21.682 38.137 1.00 58.11  ? 306 OLC A C8   1 
HETATM 3785 C C24  . OLC G 3 .   ? 11.207 22.899 49.290 1.00 57.62  ? 306 OLC A C24  1 
HETATM 3786 C C16  . OLC G 3 .   ? 18.533 20.995 33.520 1.00 65.64  ? 306 OLC A C16  1 
HETATM 3787 C C12  . OLC G 3 .   ? 14.659 22.552 35.051 1.00 53.91  ? 306 OLC A C12  1 
HETATM 3788 C C7   . OLC G 3 .   ? 12.086 21.099 39.436 1.00 59.22  ? 306 OLC A C7   1 
HETATM 3789 C C15  . OLC G 3 .   ? 18.062 21.825 34.745 1.00 61.53  ? 306 OLC A C15  1 
HETATM 3790 C C13  . OLC G 3 .   ? 15.594 21.447 34.465 1.00 63.53  ? 306 OLC A C13  1 
HETATM 3791 C C6   . OLC G 3 .   ? 11.633 21.872 40.710 1.00 62.58  ? 306 OLC A C6   1 
HETATM 3792 C C14  . OLC G 3 .   ? 16.811 21.184 35.395 1.00 50.87  ? 306 OLC A C14  1 
HETATM 3793 C C5   . OLC G 3 .   ? 12.035 23.368 40.698 1.00 52.67  ? 306 OLC A C5   1 
HETATM 3794 C C4   . OLC G 3 .   ? 11.540 23.972 42.045 1.00 47.09  ? 306 OLC A C4   1 
HETATM 3795 C C3   . OLC G 3 .   ? 12.645 23.802 43.120 1.00 54.51  ? 306 OLC A C3   1 
HETATM 3796 C C2   . OLC G 3 .   ? 12.132 24.433 44.438 1.00 46.64  ? 306 OLC A C2   1 
HETATM 3797 C C21  . OLC G 3 .   ? 13.195 23.745 48.034 1.00 55.60  ? 306 OLC A C21  1 
HETATM 3798 C C1   . OLC G 3 .   ? 12.927 23.911 45.651 1.00 45.64  ? 306 OLC A C1   1 
HETATM 3799 C C22  . OLC G 3 .   ? 12.356 23.919 49.309 1.00 58.79  ? 306 OLC A C22  1 
HETATM 3800 O O19  . OLC G 3 .   ? 13.975 23.371 45.519 1.00 59.99  ? 306 OLC A O19  1 
HETATM 3801 O O25  . OLC G 3 .   ? 10.432 23.007 50.462 1.00 58.33  ? 306 OLC A O25  1 
HETATM 3802 O O23  . OLC G 3 .   ? 13.164 23.707 50.433 1.00 77.03  ? 306 OLC A O23  1 
HETATM 3803 O O20  . OLC G 3 .   ? 12.374 24.093 46.938 1.00 49.01  ? 306 OLC A O20  1 
HETATM 3804 H H18  . OLC G 3 .   ? 20.941 20.379 32.373 0.00 69.69  ? 306 OLC A H18  1 
HETATM 3805 H H18A . OLC G 3 .   ? 21.145 18.761 33.077 0.00 69.69  ? 306 OLC A H18A 1 
HETATM 3806 H H18B . OLC G 3 .   ? 19.785 19.088 31.982 0.00 69.69  ? 306 OLC A H18B 1 
HETATM 3807 H H10  . OLC G 3 .   ? 13.995 21.023 35.996 0.00 62.41  ? 306 OLC A H10  1 
HETATM 3808 H H9   . OLC G 3 .   ? 12.422 22.110 37.017 0.00 69.13  ? 306 OLC A H9   1 
HETATM 3809 H H17  . OLC G 3 .   ? 20.183 20.328 34.752 0.00 82.49  ? 306 OLC A H17  1 
HETATM 3810 H H17A . OLC G 3 .   ? 19.013 19.052 34.346 0.00 82.49  ? 306 OLC A H17A 1 
HETATM 3811 H H11  . OLC G 3 .   ? 13.004 21.862 33.817 0.00 66.93  ? 306 OLC A H11  1 
HETATM 3812 H H11A . OLC G 3 .   ? 12.533 23.019 35.087 0.00 66.93  ? 306 OLC A H11A 1 
HETATM 3813 H H8   . OLC G 3 .   ? 10.417 21.425 38.064 0.00 69.74  ? 306 OLC A H8   1 
HETATM 3814 H H8A  . OLC G 3 .   ? 11.586 22.766 38.115 0.00 69.74  ? 306 OLC A H8A  1 
HETATM 3815 H H24  . OLC G 3 .   ? 11.621 21.894 49.226 0.00 69.15  ? 306 OLC A H24  1 
HETATM 3816 H H24A . OLC G 3 .   ? 10.575 23.087 48.424 0.00 69.15  ? 306 OLC A H24A 1 
HETATM 3817 H H16  . OLC G 3 .   ? 19.004 21.658 32.795 0.00 78.78  ? 306 OLC A H16  1 
HETATM 3818 H H16A . OLC G 3 .   ? 17.671 20.509 33.062 0.00 78.78  ? 306 OLC A H16A 1 
HETATM 3819 H H12  . OLC G 3 .   ? 14.860 23.495 34.546 0.00 64.71  ? 306 OLC A H12  1 
HETATM 3820 H H12A . OLC G 3 .   ? 14.857 22.660 36.116 0.00 64.71  ? 306 OLC A H12A 1 
HETATM 3821 H H7   . OLC G 3 .   ? 11.777 20.058 39.531 0.00 71.07  ? 306 OLC A H7   1 
HETATM 3822 H H7A  . OLC G 3 .   ? 13.172 21.150 39.364 0.00 71.07  ? 306 OLC A H7A  1 
HETATM 3823 H H15  . OLC G 3 .   ? 17.818 22.835 34.420 0.00 73.85  ? 306 OLC A H15  1 
HETATM 3824 H H15A . OLC G 3 .   ? 18.865 21.864 35.479 0.00 73.85  ? 306 OLC A H15A 1 
HETATM 3825 H H13  . OLC G 3 .   ? 15.956 21.770 33.490 0.00 76.25  ? 306 OLC A H13  1 
HETATM 3826 H H13A . OLC G 3 .   ? 15.026 20.524 34.354 0.00 76.25  ? 306 OLC A H13A 1 
HETATM 3827 H H6   . OLC G 3 .   ? 10.547 21.807 40.787 0.00 75.10  ? 306 OLC A H6   1 
HETATM 3828 H H6A  . OLC G 3 .   ? 12.087 21.400 41.581 0.00 75.10  ? 306 OLC A H6A  1 
HETATM 3829 H H14  . OLC G 3 .   ? 16.633 21.632 36.373 0.00 61.05  ? 306 OLC A H14  1 
HETATM 3830 H H14A . OLC G 3 .   ? 16.963 20.111 35.510 0.00 61.05  ? 306 OLC A H14A 1 
HETATM 3831 H H5   . OLC G 3 .   ? 11.561 23.878 39.860 0.00 63.22  ? 306 OLC A H5   1 
HETATM 3832 H H5A  . OLC G 3 .   ? 13.118 23.465 40.617 0.00 63.22  ? 306 OLC A H5A  1 
HETATM 3833 H H4   . OLC G 3 .   ? 11.322 25.031 41.911 0.00 56.52  ? 306 OLC A H4   1 
HETATM 3834 H H4A  . OLC G 3 .   ? 10.636 23.453 42.366 0.00 56.52  ? 306 OLC A H4A  1 
HETATM 3835 H H3   . OLC G 3 .   ? 12.852 22.743 43.273 0.00 65.42  ? 306 OLC A H3   1 
HETATM 3836 H H3A  . OLC G 3 .   ? 13.555 24.307 42.797 0.00 65.42  ? 306 OLC A H3A  1 
HETATM 3837 H H2   . OLC G 3 .   ? 12.242 25.515 44.381 0.00 55.98  ? 306 OLC A H2   1 
HETATM 3838 H H2A  . OLC G 3 .   ? 11.081 24.182 44.568 0.00 55.98  ? 306 OLC A H2A  1 
HETATM 3839 H H21  . OLC G 3 .   ? 14.067 24.398 48.070 0.00 66.74  ? 306 OLC A H21  1 
HETATM 3840 H H21A . OLC G 3 .   ? 13.521 22.709 47.942 0.00 66.74  ? 306 OLC A H21A 1 
HETATM 3841 H H22  . OLC G 3 .   ? 11.948 24.929 49.352 0.00 70.56  ? 306 OLC A H22  1 
HETATM 3842 H HO25 . OLC G 3 .   ? 9.973  22.197 50.615 0.00 70.01  ? 306 OLC A HO25 1 
HETATM 3843 H HO23 . OLC G 3 .   ? 12.824 24.217 51.159 0.00 92.45  ? 306 OLC A HO23 1 
HETATM 3844 C C18  . OLC H 3 .   ? 6.189  32.382 41.970 1.00 68.97  ? 307 OLC A C18  1 
HETATM 3845 C C10  . OLC H 3 .   ? 8.028  29.486 32.766 1.00 59.43  ? 307 OLC A C10  1 
HETATM 3846 C C9   . OLC H 3 .   ? 8.084  29.103 31.474 1.00 66.07  ? 307 OLC A C9   1 
HETATM 3847 C C17  . OLC H 3 .   ? 6.055  32.622 40.453 1.00 64.29  ? 307 OLC A C17  1 
HETATM 3848 C C11  . OLC H 3 .   ? 6.783  29.541 33.665 1.00 49.95  ? 307 OLC A C11  1 
HETATM 3849 C C8   . OLC H 3 .   ? 7.513  28.598 30.141 1.00 54.36  ? 307 OLC A C8   1 
HETATM 3850 C C24  . OLC H 3 .   ? 3.215  33.151 18.751 1.00 85.14  ? 307 OLC A C24  1 
HETATM 3851 C C16  . OLC H 3 .   ? 5.956  31.259 39.727 1.00 57.04  ? 307 OLC A C16  1 
HETATM 3852 C C12  . OLC H 3 .   ? 7.220  29.829 35.137 1.00 51.89  ? 307 OLC A C12  1 
HETATM 3853 C C7   . OLC H 3 .   ? 7.466  29.652 29.016 1.00 75.43  ? 307 OLC A C7   1 
HETATM 3854 C C15  . OLC H 3 .   ? 6.219  31.479 38.217 1.00 51.30  ? 307 OLC A C15  1 
HETATM 3855 C C13  . OLC H 3 .   ? 6.035  30.440 35.924 1.00 44.75  ? 307 OLC A C13  1 
HETATM 3856 C C6   . OLC H 3 .   ? 6.007  30.125 28.773 1.00 67.70  ? 307 OLC A C6   1 
HETATM 3857 C C14  . OLC H 3 .   ? 6.178  30.141 37.443 1.00 52.97  ? 307 OLC A C14  1 
HETATM 3858 C C5   . OLC H 3 .   ? 6.035  31.279 27.726 1.00 64.14  ? 307 OLC A C5   1 
HETATM 3859 C C4   . OLC H 3 .   ? 4.679  31.367 26.960 1.00 67.14  ? 307 OLC A C4   1 
HETATM 3860 C C3   . OLC H 3 .   ? 4.935  31.595 25.444 1.00 61.80  ? 307 OLC A C3   1 
HETATM 3861 C C2   . OLC H 3 .   ? 3.702  31.129 24.624 1.00 77.70  ? 307 OLC A C2   1 
HETATM 3862 C C21  . OLC H 3 .   ? 3.034  32.570 21.190 1.00 70.72  ? 307 OLC A C21  1 
HETATM 3863 C C1   . OLC H 3 .   ? 3.416  32.149 23.497 1.00 73.99  ? 307 OLC A C1   1 
HETATM 3864 C C22  . OLC H 3 .   ? 3.390  32.040 19.796 1.00 74.13  ? 307 OLC A C22  1 
HETATM 3865 O O19  . OLC H 3 .   ? 2.896  33.186 23.753 1.00 86.75  ? 307 OLC A O19  1 
HETATM 3866 O O25  . OLC H 3 .   ? 4.475  33.691 18.419 1.00 86.66  ? 307 OLC A O25  1 
HETATM 3867 O O23  . OLC H 3 .   ? 4.719  31.605 19.795 1.00 85.39  ? 307 OLC A O23  1 
HETATM 3868 O O20  . OLC H 3 .   ? 3.765  31.845 22.162 1.00 70.53  ? 307 OLC A O20  1 
HETATM 3869 H H18  . OLC H 3 .   ? 6.306  33.336 42.479 0.00 82.78  ? 307 OLC A H18  1 
HETATM 3870 H H18A . OLC H 3 .   ? 5.295  31.882 42.338 0.00 82.78  ? 307 OLC A H18A 1 
HETATM 3871 H H18B . OLC H 3 .   ? 7.059  31.759 42.163 0.00 82.78  ? 307 OLC A H18B 1 
HETATM 3872 H H10  . OLC H 3 .   ? 8.371  28.675 33.403 0.00 71.32  ? 307 OLC A H10  1 
HETATM 3873 H H9   . OLC H 3 .   ? 7.134  28.596 31.619 0.00 79.30  ? 307 OLC A H9   1 
HETATM 3874 H H17  . OLC H 3 .   ? 5.157  33.206 40.255 0.00 77.16  ? 307 OLC A H17  1 
HETATM 3875 H H17A . OLC H 3 .   ? 6.927  33.165 40.092 0.00 77.16  ? 307 OLC A H17A 1 
HETATM 3876 H H11  . OLC H 3 .   ? 6.120  30.336 33.320 0.00 59.95  ? 307 OLC A H11  1 
HETATM 3877 H H11A . OLC H 3 .   ? 6.259  28.586 33.620 0.00 59.95  ? 307 OLC A H11A 1 
HETATM 3878 H H8   . OLC H 3 .   ? 6.496  28.247 30.320 0.00 65.24  ? 307 OLC A H8   1 
HETATM 3879 H H8A  . OLC H 3 .   ? 8.130  27.766 29.801 0.00 65.24  ? 307 OLC A H8A  1 
HETATM 3880 H H24  . OLC H 3 .   ? 2.580  33.936 19.159 0.00 102.18 ? 307 OLC A H24  1 
HETATM 3881 H H24A . OLC H 3 .   ? 2.752  32.736 17.857 0.00 102.18 ? 307 OLC A H24A 1 
HETATM 3882 H H16  . OLC H 3 .   ? 6.701  30.574 40.133 0.00 68.46  ? 307 OLC A H16  1 
HETATM 3883 H H16A . OLC H 3 .   ? 4.960  30.839 39.869 0.00 68.46  ? 307 OLC A H16A 1 
HETATM 3884 H H12  . OLC H 3 .   ? 7.527  28.898 35.611 0.00 62.28  ? 307 OLC A H12  1 
HETATM 3885 H H12A . OLC H 3 .   ? 8.054  30.529 35.137 0.00 62.28  ? 307 OLC A H12A 1 
HETATM 3886 H H7   . OLC H 3 .   ? 8.078  30.508 29.302 0.00 90.53  ? 307 OLC A H7   1 
HETATM 3887 H H7A  . OLC H 3 .   ? 7.859  29.214 28.099 0.00 90.53  ? 307 OLC A H7A  1 
HETATM 3888 H H15  . OLC H 3 .   ? 7.200  31.934 38.089 0.00 61.58  ? 307 OLC A H15  1 
HETATM 3889 H H15A . OLC H 3 .   ? 5.455  32.145 37.817 0.00 61.58  ? 307 OLC A H15A 1 
HETATM 3890 H H13  . OLC H 3 .   ? 5.103  30.010 35.560 0.00 53.71  ? 307 OLC A H13  1 
HETATM 3891 H H13A . OLC H 3 .   ? 6.021  31.518 35.771 0.00 53.71  ? 307 OLC A H13A 1 
HETATM 3892 H H6   . OLC H 3 .   ? 5.410  29.296 28.392 0.00 81.25  ? 307 OLC A H6   1 
HETATM 3893 H H6A  . OLC H 3 .   ? 5.575  30.484 29.707 0.00 81.25  ? 307 OLC A H6A  1 
HETATM 3894 H H14  . OLC H 3 .   ? 5.328  29.548 37.781 0.00 63.58  ? 307 OLC A H14  1 
HETATM 3895 H H14A . OLC H 3 .   ? 7.100  29.587 37.621 0.00 63.58  ? 307 OLC A H14A 1 
HETATM 3896 H H5   . OLC H 3 .   ? 6.217  32.222 28.240 0.00 76.97  ? 307 OLC A H5   1 
HETATM 3897 H H5A  . OLC H 3 .   ? 6.837  31.093 27.012 0.00 76.97  ? 307 OLC A H5A  1 
HETATM 3898 H H4   . OLC H 3 .   ? 4.126  30.438 27.097 0.00 80.58  ? 307 OLC A H4   1 
HETATM 3899 H H4A  . OLC H 3 .   ? 4.095  32.198 27.356 0.00 80.58  ? 307 OLC A H4A  1 
HETATM 3900 H H3   . OLC H 3 .   ? 5.111  32.655 25.263 0.00 74.17  ? 307 OLC A H3   1 
HETATM 3901 H H3A  . OLC H 3 .   ? 5.811  31.023 25.136 0.00 74.17  ? 307 OLC A H3A  1 
HETATM 3902 H H2   . OLC H 3 .   ? 3.905  30.153 24.186 0.00 93.26  ? 307 OLC A H2   1 
HETATM 3903 H H2A  . OLC H 3 .   ? 2.835  31.060 25.279 0.00 93.26  ? 307 OLC A H2A  1 
HETATM 3904 H H21  . OLC H 3 .   ? 3.289  33.627 21.255 0.00 84.88  ? 307 OLC A H21  1 
HETATM 3905 H H21A . OLC H 3 .   ? 1.966  32.443 21.367 0.00 84.88  ? 307 OLC A H21A 1 
HETATM 3906 H H22  . OLC H 3 .   ? 2.728  31.211 19.548 0.00 88.96  ? 307 OLC A H22  1 
HETATM 3907 H HO25 . OLC H 3 .   ? 5.102  33.469 19.093 0.00 104.01 ? 307 OLC A HO25 1 
HETATM 3908 H HO23 . OLC H 3 .   ? 5.099  31.743 20.653 0.00 102.49 ? 307 OLC A HO23 1 
HETATM 3909 C C18  . OLC I 3 .   ? 34.719 36.142 35.712 1.00 72.68  ? 308 OLC A C18  1 
HETATM 3910 C C10  . OLC I 3 .   ? 32.772 39.791 28.108 1.00 69.05  ? 308 OLC A C10  1 
HETATM 3911 C C9   . OLC I 3 .   ? 32.820 40.878 27.371 1.00 66.01  ? 308 OLC A C9   1 
HETATM 3912 C C17  . OLC I 3 .   ? 35.741 35.536 34.725 1.00 82.15  ? 308 OLC A C17  1 
HETATM 3913 C C11  . OLC I 3 .   ? 32.807 39.658 29.643 1.00 70.46  ? 308 OLC A C11  1 
HETATM 3914 C C8   . OLC I 3 .   ? 32.843 41.635 26.011 1.00 60.09  ? 308 OLC A C8   1 
HETATM 3915 C C24  . OLC I 3 .   ? 35.880 45.709 14.590 1.00 86.41  ? 308 OLC A C24  1 
HETATM 3916 C C16  . OLC I 3 .   ? 35.225 35.725 33.280 1.00 76.57  ? 308 OLC A C16  1 
HETATM 3917 C C12  . OLC I 3 .   ? 34.286 39.348 30.010 1.00 70.57  ? 308 OLC A C12  1 
HETATM 3918 C C7   . OLC I 3 .   ? 34.040 41.117 25.095 1.00 57.22  ? 308 OLC A C7   1 
HETATM 3919 C C15  . OLC I 3 .   ? 35.809 37.028 32.683 1.00 60.42  ? 308 OLC A C15  1 
HETATM 3920 C C13  . OLC I 3 .   ? 34.361 38.734 31.437 1.00 78.12  ? 308 OLC A C13  1 
HETATM 3921 C C6   . OLC I 3 .   ? 33.461 40.986 23.659 1.00 68.22  ? 308 OLC A C6   1 
HETATM 3922 C C14  . OLC I 3 .   ? 35.058 37.342 31.362 1.00 70.79  ? 308 OLC A C14  1 
HETATM 3923 C C5   . OLC I 3 .   ? 34.617 40.625 22.689 1.00 59.22  ? 308 OLC A C5   1 
HETATM 3924 C C4   . OLC I 3 .   ? 35.005 41.836 21.794 1.00 54.34  ? 308 OLC A C4   1 
HETATM 3925 C C3   . OLC I 3 .   ? 34.447 41.620 20.362 1.00 58.59  ? 308 OLC A C3   1 
HETATM 3926 C C2   . OLC I 3 .   ? 34.470 42.976 19.604 1.00 74.87  ? 308 OLC A C2   1 
HETATM 3927 C C21  . OLC I 3 .   ? 35.713 43.800 16.197 1.00 80.80  ? 308 OLC A C21  1 
HETATM 3928 C C1   . OLC I 3 .   ? 35.157 42.791 18.234 1.00 71.81  ? 308 OLC A C1   1 
HETATM 3929 C C22  . OLC I 3 .   ? 35.171 44.384 14.890 1.00 89.62  ? 308 OLC A C22  1 
HETATM 3930 O O19  . OLC I 3 .   ? 36.132 42.116 18.158 1.00 89.91  ? 308 OLC A O19  1 
HETATM 3931 O O25  . OLC I 3 .   ? 35.328 46.727 15.395 1.00 78.82  ? 308 OLC A O25  1 
HETATM 3932 O O23  . OLC I 3 .   ? 35.424 43.479 13.857 1.00 92.20  ? 308 OLC A O23  1 
HETATM 3933 O O20  . OLC I 3 .   ? 34.662 43.430 17.073 1.00 91.44  ? 308 OLC A O20  1 
HETATM 3934 H H18  . OLC I 3 .   ? 35.052 35.966 36.733 0.00 87.23  ? 308 OLC A H18  1 
HETATM 3935 H H18A . OLC I 3 .   ? 34.636 37.212 35.537 0.00 87.23  ? 308 OLC A H18A 1 
HETATM 3936 H H18B . OLC I 3 .   ? 33.748 35.674 35.561 0.00 87.23  ? 308 OLC A H18B 1 
HETATM 3937 H H10  . OLC I 3 .   ? 33.753 39.324 28.124 0.00 82.87  ? 308 OLC A H10  1 
HETATM 3938 H H9   . OLC I 3 .   ? 32.440 40.261 26.561 0.00 79.23  ? 308 OLC A H9   1 
HETATM 3939 H H17  . OLC I 3 .   ? 36.700 36.040 34.839 0.00 98.60  ? 308 OLC A H17  1 
HETATM 3940 H H17A . OLC I 3 .   ? 35.863 34.474 34.933 0.00 98.60  ? 308 OLC A H17A 1 
HETATM 3941 H H11  . OLC I 3 .   ? 32.487 40.590 30.112 0.00 84.57  ? 308 OLC A H11  1 
HETATM 3942 H H11A . OLC I 3 .   ? 32.156 38.845 29.968 0.00 84.57  ? 308 OLC A H11A 1 
HETATM 3943 H H8   . OLC I 3 .   ? 32.971 42.702 26.198 0.00 72.12  ? 308 OLC A H8   1 
HETATM 3944 H H8A  . OLC I 3 .   ? 31.898 41.468 25.493 0.00 72.12  ? 308 OLC A H8A  1 
HETATM 3945 H H24  . OLC I 3 .   ? 35.746 45.963 13.540 0.00 103.71 ? 308 OLC A H24  1 
HETATM 3946 H H24A . OLC I 3 .   ? 36.942 45.610 14.807 0.00 103.71 ? 308 OLC A H24A 1 
HETATM 3947 H H16  . OLC I 3 .   ? 35.536 34.877 32.671 0.00 91.89  ? 308 OLC A H16  1 
HETATM 3948 H H16A . OLC I 3 .   ? 34.137 35.787 33.289 0.00 91.89  ? 308 OLC A H16A 1 
HETATM 3949 H H12  . OLC I 3 .   ? 34.695 38.640 29.291 0.00 84.70  ? 308 OLC A H12  1 
HETATM 3950 H H12A . OLC I 3 .   ? 34.865 40.269 29.982 0.00 84.70  ? 308 OLC A H12A 1 
HETATM 3951 H H7   . OLC I 3 .   ? 34.863 41.832 25.108 0.00 68.68  ? 308 OLC A H7   1 
HETATM 3952 H H7A  . OLC I 3 .   ? 34.395 40.149 25.450 0.00 68.68  ? 308 OLC A H7A  1 
HETATM 3953 H H15  . OLC I 3 .   ? 36.870 36.896 32.479 0.00 72.52  ? 308 OLC A H15  1 
HETATM 3954 H H15A . OLC I 3 .   ? 35.673 37.848 33.386 0.00 72.52  ? 308 OLC A H15A 1 
HETATM 3955 H H13  . OLC I 3 .   ? 33.355 38.617 31.836 0.00 93.76  ? 308 OLC A H13  1 
HETATM 3956 H H13A . OLC I 3 .   ? 34.935 39.394 32.086 0.00 93.76  ? 308 OLC A H13A 1 
HETATM 3957 H H6   . OLC I 3 .   ? 32.706 40.201 23.638 0.00 81.87  ? 308 OLC A H6   1 
HETATM 3958 H H6A  . OLC I 3 .   ? 33.011 41.932 23.357 0.00 81.87  ? 308 OLC A H6A  1 
HETATM 3959 H H14  . OLC I 3 .   ? 34.304 36.574 31.189 0.00 84.96  ? 308 OLC A H14  1 
HETATM 3960 H H14A . OLC I 3 .   ? 35.771 37.343 30.537 0.00 84.96  ? 308 OLC A H14A 1 
HETATM 3961 H H5   . OLC I 3 .   ? 34.300 39.800 22.050 0.00 71.08  ? 308 OLC A H5   1 
HETATM 3962 H H5A  . OLC I 3 .   ? 35.487 40.321 23.271 0.00 71.08  ? 308 OLC A H5A  1 
HETATM 3963 H H4   . OLC I 3 .   ? 34.583 42.749 22.215 0.00 65.22  ? 308 OLC A H4   1 
HETATM 3964 H H4A  . OLC I 3 .   ? 36.091 41.924 21.752 0.00 65.22  ? 308 OLC A H4A  1 
HETATM 3965 H H3   . OLC I 3 .   ? 35.065 40.894 19.834 0.00 70.32  ? 308 OLC A H3   1 
HETATM 3966 H H3A  . OLC I 3 .   ? 33.423 41.251 20.420 0.00 70.32  ? 308 OLC A H3A  1 
HETATM 3967 H H2   . OLC I 3 .   ? 33.450 43.325 19.454 0.00 89.86  ? 308 OLC A H2   1 
HETATM 3968 H H2A  . OLC I 3 .   ? 35.022 43.709 20.190 0.00 89.86  ? 308 OLC A H2A  1 
HETATM 3969 H H21  . OLC I 3 .   ? 36.312 42.919 15.970 0.00 96.98  ? 308 OLC A H21  1 
HETATM 3970 H H21A . OLC I 3 .   ? 36.337 44.547 16.688 0.00 96.98  ? 308 OLC A H21A 1 
HETATM 3971 H H22  . OLC I 3 .   ? 34.098 44.560 14.979 0.00 107.55 ? 308 OLC A H22  1 
HETATM 3972 H HO25 . OLC I 3 .   ? 35.609 46.608 16.290 0.00 94.60  ? 308 OLC A HO25 1 
HETATM 3973 H HO23 . OLC I 3 .   ? 36.361 43.371 13.755 0.00 110.66 ? 308 OLC A HO23 1 
HETATM 3974 C C18  . OLC J 3 .   ? 3.649  38.562 36.511 1.00 59.79  ? 309 OLC A C18  1 
HETATM 3975 C C10  . OLC J 3 .   ? 5.116  37.203 43.891 1.00 71.10  ? 309 OLC A C10  1 
HETATM 3976 C C9   . OLC J 3 .   ? 4.558  38.177 44.646 1.00 69.06  ? 309 OLC A C9   1 
HETATM 3977 C C17  . OLC J 3 .   ? 4.401  39.307 37.633 1.00 67.18  ? 309 OLC A C17  1 
HETATM 3978 C C11  . OLC J 3 .   ? 6.499  37.166 43.223 1.00 65.03  ? 309 OLC A C11  1 
HETATM 3979 C C8   . OLC J 3 .   ? 4.499  39.533 45.367 1.00 73.68  ? 309 OLC A C8   1 
HETATM 3980 C C24  . OLC J 3 .   ? 4.613  36.136 56.230 1.00 97.67  ? 309 OLC A C24  1 
HETATM 3981 C C16  . OLC J 3 .   ? 3.733  39.043 39.008 1.00 71.49  ? 309 OLC A C16  1 
HETATM 3982 C C12  . OLC J 3 .   ? 6.355  37.388 41.708 1.00 64.76  ? 309 OLC A C12  1 
HETATM 3983 C C7   . OLC J 3 .   ? 3.120  39.735 46.050 1.00 71.31  ? 309 OLC A C7   1 
HETATM 3984 C C15  . OLC J 3 .   ? 3.684  37.530 39.366 1.00 86.10  ? 309 OLC A C15  1 
HETATM 3985 C C13  . OLC J 3 .   ? 5.333  36.442 41.015 1.00 68.62  ? 309 OLC A C13  1 
HETATM 3986 C C6   . OLC J 3 .   ? 3.279  40.047 47.573 1.00 70.26  ? 309 OLC A C6   1 
HETATM 3987 C C14  . OLC J 3 .   ? 5.124  36.981 39.574 1.00 63.04  ? 309 OLC A C14  1 
HETATM 3988 C C5   . OLC J 3 .   ? 3.922  38.849 48.333 1.00 66.13  ? 309 OLC A C5   1 
HETATM 3989 C C4   . OLC J 3 .   ? 4.718  39.362 49.573 1.00 68.32  ? 309 OLC A C4   1 
HETATM 3990 C C3   . OLC J 3 .   ? 4.367  38.541 50.848 1.00 79.51  ? 309 OLC A C3   1 
HETATM 3991 C C2   . OLC J 3 .   ? 5.624  38.415 51.757 1.00 95.90  ? 309 OLC A C2   1 
HETATM 3992 C C21  . OLC J 3 .   ? 3.818  37.162 54.084 1.00 101.22 ? 309 OLC A C21  1 
HETATM 3993 C C1   . OLC J 3 .   ? 5.274  38.807 53.212 1.00 88.16  ? 309 OLC A C1   1 
HETATM 3994 C C22  . OLC J 3 .   ? 3.832  35.885 54.933 1.00 101.03 ? 309 OLC A C22  1 
HETATM 3995 O O19  . OLC J 3 .   ? 5.178  39.951 53.518 1.00 91.84  ? 309 OLC A O19  1 
HETATM 3996 O O25  . OLC J 3 .   ? 4.605  34.964 57.016 1.00 98.59  ? 309 OLC A O25  1 
HETATM 3997 O O23  . OLC J 3 .   ? 2.517  35.518 55.230 1.00 98.14  ? 309 OLC A O23  1 
HETATM 3998 O O20  . OLC J 3 .   ? 5.077  37.803 54.184 1.00 99.56  ? 309 OLC A O20  1 
HETATM 3999 H H18  . OLC J 3 .   ? 3.896  37.504 36.549 0.00 71.76  ? 309 OLC A H18  1 
HETATM 4000 H H18A . OLC J 3 .   ? 2.577  38.689 36.646 0.00 71.76  ? 309 OLC A H18A 1 
HETATM 4001 H H18B . OLC J 3 .   ? 3.943  38.969 35.545 0.00 71.76  ? 309 OLC A H18B 1 
HETATM 4002 H H10  . OLC J 3 .   ? 4.718  37.258 42.881 0.00 85.33  ? 309 OLC A H10  1 
HETATM 4003 H H9   . OLC J 3 .   ? 5.276  38.876 44.227 0.00 82.89  ? 309 OLC A H9   1 
HETATM 4004 H H17  . OLC J 3 .   ? 4.384  40.376 37.427 0.00 80.63  ? 309 OLC A H17  1 
HETATM 4005 H H17A . OLC J 3 .   ? 5.433  38.960 37.664 0.00 80.63  ? 309 OLC A H17A 1 
HETATM 4006 H H11  . OLC J 3 .   ? 7.125  37.953 43.645 0.00 78.05  ? 309 OLC A H11  1 
HETATM 4007 H H11A . OLC J 3 .   ? 6.962  36.195 43.404 0.00 78.05  ? 309 OLC A H11A 1 
HETATM 4008 H H8   . OLC J 3 .   ? 4.659  40.331 44.642 0.00 88.42  ? 309 OLC A H8   1 
HETATM 4009 H H8A  . OLC J 3 .   ? 5.282  39.569 46.125 0.00 88.42  ? 309 OLC A H8A  1 
HETATM 4010 H H24  . OLC J 3 .   ? 4.144  36.948 56.784 0.00 117.21 ? 309 OLC A H24  1 
HETATM 4011 H H24A . OLC J 3 .   ? 5.640  36.406 55.990 0.00 117.21 ? 309 OLC A H24A 1 
HETATM 4012 H H16  . OLC J 3 .   ? 4.299  39.566 39.778 0.00 85.81  ? 309 OLC A H16  1 
HETATM 4013 H H16A . OLC J 3 .   ? 2.714  39.429 38.982 0.00 85.81  ? 309 OLC A H16A 1 
HETATM 4014 H H12  . OLC J 3 .   ? 6.034  38.415 41.542 0.00 77.73  ? 309 OLC A H12  1 
HETATM 4015 H H12A . OLC J 3 .   ? 7.329  37.233 41.246 0.00 77.73  ? 309 OLC A H12A 1 
HETATM 4016 H H7   . OLC J 3 .   ? 2.604  40.567 45.570 0.00 85.58  ? 309 OLC A H7   1 
HETATM 4017 H H7A  . OLC J 3 .   ? 2.530  38.826 45.934 0.00 85.58  ? 309 OLC A H7A  1 
HETATM 4018 H H15  . OLC J 3 .   ? 3.205  36.984 38.555 0.00 103.33 ? 309 OLC A H15  1 
HETATM 4019 H H15A . OLC J 3 .   ? 3.111  37.395 40.282 0.00 103.33 ? 309 OLC A H15A 1 
HETATM 4020 H H13  . OLC J 3 .   ? 4.389  36.448 41.558 0.00 82.36  ? 309 OLC A H13  1 
HETATM 4021 H H13A . OLC J 3 .   ? 5.725  35.426 40.982 0.00 82.36  ? 309 OLC A H13A 1 
HETATM 4022 H H6   . OLC J 3 .   ? 3.914  40.925 47.691 0.00 84.33  ? 309 OLC A H6   1 
HETATM 4023 H H6A  . OLC J 3 .   ? 2.296  40.250 47.998 0.00 84.33  ? 309 OLC A H6A  1 
HETATM 4024 H H14  . OLC J 3 .   ? 5.838  37.783 39.391 0.00 75.66  ? 309 OLC A H14  1 
HETATM 4025 H H14A . OLC J 3 .   ? 5.299  36.171 38.866 0.00 75.66  ? 309 OLC A H14A 1 
HETATM 4026 H H5   . OLC J 3 .   ? 3.137  38.169 48.665 0.00 79.37  ? 309 OLC A H5   1 
HETATM 4027 H H5A  . OLC J 3 .   ? 4.601  38.320 47.663 0.00 79.37  ? 309 OLC A H5A  1 
HETATM 4028 H H4   . OLC J 3 .   ? 5.786  39.270 49.374 0.00 82.00  ? 309 OLC A H4   1 
HETATM 4029 H H4A  . OLC J 3 .   ? 4.470  40.409 49.746 0.00 82.00  ? 309 OLC A H4A  1 
HETATM 4030 H H3   . OLC J 3 .   ? 3.573  39.046 51.397 0.00 95.43  ? 309 OLC A H3   1 
HETATM 4031 H H3A  . OLC J 3 .   ? 4.031  37.546 50.556 0.00 95.43  ? 309 OLC A H3A  1 
HETATM 4032 H H2   . OLC J 3 .   ? 5.980  37.386 51.738 0.00 115.09 ? 309 OLC A H2   1 
HETATM 4033 H H2A  . OLC J 3 .   ? 6.404  39.076 51.384 0.00 115.09 ? 309 OLC A H2A  1 
HETATM 4034 H H21  . OLC J 3 .   ? 3.621  36.906 53.043 0.00 121.48 ? 309 OLC A H21  1 
HETATM 4035 H H21A . OLC J 3 .   ? 3.039  37.832 54.448 0.00 121.48 ? 309 OLC A H21A 1 
HETATM 4036 H H22  . OLC J 3 .   ? 4.317  35.081 54.379 0.00 121.25 ? 309 OLC A H22  1 
HETATM 4037 H HO25 . OLC J 3 .   ? 3.814  34.475 56.844 0.00 118.32 ? 309 OLC A HO25 1 
HETATM 4038 H HO23 . OLC J 3 .   ? 2.235  35.967 56.016 0.00 117.78 ? 309 OLC A HO23 1 
HETATM 4039 C C18  . OLC K 3 .   ? 21.700 54.922 37.423 1.00 67.65  ? 310 OLC A C18  1 
HETATM 4040 C C10  . OLC K 3 .   ? 23.100 56.679 29.452 1.00 82.22  ? 310 OLC A C10  1 
HETATM 4041 C C9   . OLC K 3 .   ? 23.319 57.241 28.251 1.00 86.36  ? 310 OLC A C9   1 
HETATM 4042 C C17  . OLC K 3 .   ? 22.285 53.658 36.753 1.00 66.92  ? 310 OLC A C17  1 
HETATM 4043 C C11  . OLC K 3 .   ? 21.793 56.232 30.064 1.00 76.88  ? 310 OLC A C11  1 
HETATM 4044 C C8   . OLC K 3 .   ? 22.922 57.783 26.896 1.00 84.98  ? 310 OLC A C8   1 
HETATM 4045 C C24  . OLC K 3 .   ? 28.314 55.894 15.484 1.00 95.37  ? 310 OLC A C24  1 
HETATM 4046 C C16  . OLC K 3 .   ? 21.462 53.270 35.494 1.00 65.70  ? 310 OLC A C16  1 
HETATM 4047 C C12  . OLC K 3 .   ? 22.071 55.536 31.432 1.00 68.64  ? 310 OLC A C12  1 
HETATM 4048 C C7   . OLC K 3 .   ? 24.101 57.798 25.869 1.00 91.13  ? 310 OLC A C7   1 
HETATM 4049 C C15  . OLC K 3 .   ? 21.565 54.375 34.418 1.00 62.03  ? 310 OLC A C15  1 
HETATM 4050 C C13  . OLC K 3 .   ? 20.751 55.050 32.103 1.00 69.30  ? 310 OLC A C13  1 
HETATM 4051 C C6   . OLC K 3 .   ? 23.498 57.849 24.430 1.00 78.81  ? 310 OLC A C6   1 
HETATM 4052 C C14  . OLC K 3 .   ? 21.049 53.845 33.050 1.00 57.82  ? 310 OLC A C14  1 
HETATM 4053 C C5   . OLC K 3 .   ? 24.565 57.532 23.347 1.00 90.81  ? 310 OLC A C5   1 
HETATM 4054 C C4   . OLC K 3 .   ? 23.842 56.909 22.111 1.00 74.85  ? 310 OLC A C4   1 
HETATM 4055 C C3   . OLC K 3 .   ? 24.350 57.551 20.789 1.00 86.51  ? 310 OLC A C3   1 
HETATM 4056 C C2   . OLC K 3 .   ? 24.331 56.463 19.684 1.00 90.41  ? 310 OLC A C2   1 
HETATM 4057 C C21  . OLC K 3 .   ? 26.107 56.406 16.611 1.00 101.92 ? 310 OLC A C21  1 
HETATM 4058 C C1   . OLC K 3 .   ? 24.561 57.094 18.292 1.00 83.38  ? 310 OLC A C1   1 
HETATM 4059 C C22  . OLC K 3 .   ? 27.460 55.686 16.741 1.00 93.34  ? 310 OLC A C22  1 
HETATM 4060 O O19  . OLC K 3 .   ? 23.652 57.514 17.650 1.00 83.36  ? 310 OLC A O19  1 
HETATM 4061 O O25  . OLC K 3 .   ? 29.156 54.774 15.303 1.00 91.87  ? 310 OLC A O25  1 
HETATM 4062 O O23  . OLC K 3 .   ? 28.139 56.189 17.857 1.00 88.83  ? 310 OLC A O23  1 
HETATM 4063 O O20  . OLC K 3 .   ? 25.881 57.147 17.796 1.00 94.09  ? 310 OLC A O20  1 
HETATM 4064 H H18  . OLC K 3 .   ? 22.240 55.126 38.345 0.00 81.19  ? 310 OLC A H18  1 
HETATM 4065 H H18A . OLC K 3 .   ? 21.801 55.769 36.748 0.00 81.19  ? 310 OLC A H18A 1 
HETATM 4066 H H18B . OLC K 3 .   ? 20.648 54.759 37.647 0.00 81.19  ? 310 OLC A H18B 1 
HETATM 4067 H H10  . OLC K 3 .   ? 23.350 55.622 29.406 0.00 98.67  ? 310 OLC A H10  1 
HETATM 4068 H H17  . OLC K 3 .   ? 22.260 52.833 37.464 0.00 80.31  ? 310 OLC A H17  1 
HETATM 4069 H H17A . OLC K 3 .   ? 23.315 53.854 36.460 0.00 80.31  ? 310 OLC A H17A 1 
HETATM 4070 H H11  . OLC K 3 .   ? 21.298 55.529 29.392 0.00 92.27  ? 310 OLC A H11  1 
HETATM 4071 H H11A . OLC K 3 .   ? 21.149 57.099 30.221 0.00 92.27  ? 310 OLC A H11A 1 
HETATM 4072 H H8   . OLC K 3 .   ? 22.560 58.803 27.023 0.00 101.99 ? 310 OLC A H8   1 
HETATM 4073 H H8A  . OLC K 3 .   ? 22.263 57.498 28.222 0.00 103.65 ? 310 OLC A H8A  1 
HETATM 4074 H H24  . OLC K 3 .   ? 28.921 56.791 15.601 0.00 114.46 ? 310 OLC A H24  1 
HETATM 4075 H H24A . OLC K 3 .   ? 27.664 56.006 14.617 0.00 114.46 ? 310 OLC A H24A 1 
HETATM 4076 H H16  . OLC K 3 .   ? 20.417 53.139 35.775 0.00 78.86  ? 310 OLC A H16  1 
HETATM 4077 H H16A . OLC K 3 .   ? 21.848 52.335 35.087 0.00 78.86  ? 310 OLC A H16A 1 
HETATM 4078 H H12  . OLC K 3 .   ? 22.721 54.678 31.268 0.00 82.38  ? 310 OLC A H12  1 
HETATM 4079 H H12A . OLC K 3 .   ? 22.566 56.244 32.096 0.00 82.38  ? 310 OLC A H12A 1 
HETATM 4080 H H7   . OLC K 3 .   ? 24.725 58.676 26.038 0.00 109.37 ? 310 OLC A H7   1 
HETATM 4081 H H7A  . OLC K 3 .   ? 24.703 56.897 25.985 0.00 109.37 ? 310 OLC A H7A  1 
HETATM 4082 H H15  . OLC K 3 .   ? 22.605 54.680 34.316 0.00 74.45  ? 310 OLC A H15  1 
HETATM 4083 H H15A . OLC K 3 .   ? 20.963 55.230 34.722 0.00 74.45  ? 310 OLC A H15A 1 
HETATM 4084 H H13  . OLC K 3 .   ? 20.047 54.739 31.333 0.00 83.17  ? 310 OLC A H13  1 
HETATM 4085 H H13A . OLC K 3 .   ? 20.319 55.866 32.682 0.00 83.17  ? 310 OLC A H13A 1 
HETATM 4086 H H6   . OLC K 3 .   ? 22.694 57.116 24.359 0.00 94.58  ? 310 OLC A H6   1 
HETATM 4087 H H6A  . OLC K 3 .   ? 23.098 58.846 24.250 0.00 94.58  ? 310 OLC A H6A  1 
HETATM 4088 H H14  . OLC K 3 .   ? 20.136 53.270 33.204 0.00 69.40  ? 310 OLC A H14  1 
HETATM 4089 H H14A . OLC K 3 .   ? 21.808 53.207 32.598 0.00 69.40  ? 310 OLC A H14A 1 
HETATM 4090 H H5   . OLC K 3 .   ? 25.293 56.825 23.743 0.00 108.98 ? 310 OLC A H5   1 
HETATM 4091 H H5A  . OLC K 3 .   ? 25.073 58.450 23.051 0.00 108.98 ? 310 OLC A H5A  1 
HETATM 4092 H H4   . OLC K 3 .   ? 24.038 55.837 22.087 0.00 89.83  ? 310 OLC A H4   1 
HETATM 4093 H H4A  . OLC K 3 .   ? 22.769 57.080 22.202 0.00 89.83  ? 310 OLC A H4A  1 
HETATM 4094 H H3   . OLC K 3 .   ? 23.698 58.376 20.505 0.00 103.82 ? 310 OLC A H3   1 
HETATM 4095 H H3A  . OLC K 3 .   ? 25.366 57.921 20.925 0.00 103.82 ? 310 OLC A H3A  1 
HETATM 4096 H H2   . OLC K 3 .   ? 25.119 55.738 19.882 0.00 108.50 ? 310 OLC A H2   1 
HETATM 4097 H H2A  . OLC K 3 .   ? 23.365 55.960 19.694 0.00 108.50 ? 310 OLC A H2A  1 
HETATM 4098 H H21  . OLC K 3 .   ? 26.130 57.079 15.754 0.00 122.32 ? 310 OLC A H21  1 
HETATM 4099 H H21A . OLC K 3 .   ? 25.312 55.673 16.477 0.00 122.32 ? 310 OLC A H21A 1 
HETATM 4100 H H22  . OLC K 3 .   ? 27.280 54.618 16.860 0.00 112.01 ? 310 OLC A H22  1 
HETATM 4101 H HO25 . OLC K 3 .   ? 29.156 54.246 16.087 0.00 110.25 ? 310 OLC A HO25 1 
HETATM 4102 H HO23 . OLC K 3 .   ? 27.515 56.586 18.453 0.00 106.60 ? 310 OLC A HO23 1 
HETATM 4103 H H8B  . OLC K 3 .   ? 22.122 57.160 26.495 0.00 101.99 ? 310 OLC A H8B  1 
HETATM 4104 C C45  . LI1 L 2 .   ? 30.978 33.717 46.774 1.00 87.19  ? 311 LI1 A C45  1 
HETATM 4105 C C46  . LI1 L 2 .   ? 30.383 33.430 45.402 1.00 68.38  ? 311 LI1 A C46  1 
HETATM 4106 C C47  . LI1 L 2 .   ? 31.394 33.573 44.272 1.00 79.54  ? 311 LI1 A C47  1 
HETATM 4107 C C48  . LI1 L 2 .   ? 31.473 34.965 43.643 1.00 76.76  ? 311 LI1 A C48  1 
HETATM 4108 C C50  . LI1 L 2 .   ? 30.852 34.970 42.245 1.00 78.81  ? 311 LI1 A C50  1 
HETATM 4109 C C51  . LI1 L 2 .   ? 29.488 35.642 42.144 1.00 62.70  ? 311 LI1 A C51  1 
HETATM 4110 C C52  . LI1 L 2 .   ? 29.540 37.159 42.214 1.00 63.58  ? 311 LI1 A C52  1 
HETATM 4111 C C53  . LI1 L 2 .   ? 28.663 37.850 41.180 1.00 46.80  ? 311 LI1 A C53  1 
HETATM 4112 C C55  . LI1 L 2 .   ? 29.346 38.054 39.838 1.00 66.60  ? 311 LI1 A C55  1 
HETATM 4113 C C56  . LI1 L 2 .   ? 29.763 39.491 39.570 1.00 66.82  ? 311 LI1 A C56  1 
HETATM 4114 H H451 . LI1 L 2 .   ? 30.268 33.965 47.387 1.00 104.64 ? 311 LI1 A H451 1 
HETATM 4115 H H452 . LI1 L 2 .   ? 31.561 34.489 46.699 1.00 104.64 ? 311 LI1 A H452 1 
HETATM 4116 H H461 . LI1 L 2 .   ? 30.025 32.529 45.405 1.00 82.06  ? 311 LI1 A H461 1 
HETATM 4117 H H462 . LI1 L 2 .   ? 29.644 34.042 45.255 1.00 82.06  ? 311 LI1 A H462 1 
HETATM 4118 H H471 . LI1 L 2 .   ? 31.172 32.923 43.588 1.00 95.46  ? 311 LI1 A H471 1 
HETATM 4119 H H472 . LI1 L 2 .   ? 32.266 33.327 44.620 1.00 95.46  ? 311 LI1 A H472 1 
HETATM 4120 C C45  . LI1 M 2 .   ? 31.134 28.221 45.879 1.00 88.19  ? 312 LI1 A C45  1 
HETATM 4121 C C46  . LI1 M 2 .   ? 30.962 26.790 45.384 1.00 78.94  ? 312 LI1 A C46  1 
HETATM 4122 C C47  . LI1 M 2 .   ? 30.865 26.693 43.864 1.00 73.46  ? 312 LI1 A C47  1 
HETATM 4123 C C48  . LI1 M 2 .   ? 29.444 26.562 43.312 1.00 67.65  ? 312 LI1 A C48  1 
HETATM 4124 C C50  . LI1 M 2 .   ? 29.447 26.546 41.784 1.00 61.51  ? 312 LI1 A C50  1 
HETATM 4125 C C51  . LI1 M 2 .   ? 28.216 25.916 41.140 1.00 58.71  ? 312 LI1 A C51  1 
HETATM 4126 C C52  . LI1 M 2 .   ? 28.342 25.725 39.634 1.00 71.15  ? 312 LI1 A C52  1 
HETATM 4127 C C53  . LI1 M 2 .   ? 27.848 26.906 38.811 1.00 72.18  ? 312 LI1 A C53  1 
HETATM 4128 C C55  . LI1 M 2 .   ? 28.200 28.264 39.400 1.00 74.02  ? 312 LI1 A C55  1 
HETATM 4129 C C56  . LI1 M 2 .   ? 28.434 29.352 38.359 1.00 68.27  ? 312 LI1 A C56  1 
HETATM 4130 C C57  . LI1 M 2 .   ? 28.625 30.744 38.962 1.00 60.50  ? 312 LI1 A C57  1 
HETATM 4131 C C58  . LI1 M 2 .   ? 29.400 31.732 38.107 1.00 61.02  ? 312 LI1 A C58  1 
HETATM 4132 C C59  . LI1 M 2 .   ? 29.314 33.145 38.655 1.00 62.76  ? 312 LI1 A C59  1 
HETATM 4133 H H451 . LI1 M 2 .   ? 30.349 28.740 45.646 1.00 105.84 ? 312 LI1 A H451 1 
HETATM 4134 H H452 . LI1 M 2 .   ? 31.881 28.621 45.406 1.00 105.84 ? 312 LI1 A H452 1 
HETATM 4135 H H461 . LI1 M 2 .   ? 30.160 26.422 45.785 1.00 94.74  ? 312 LI1 A H461 1 
HETATM 4136 H H462 . LI1 M 2 .   ? 31.717 26.266 45.696 1.00 94.74  ? 312 LI1 A H462 1 
HETATM 4137 H H471 . LI1 M 2 .   ? 31.393 25.931 43.579 1.00 88.17  ? 312 LI1 A H471 1 
HETATM 4138 H H472 . LI1 M 2 .   ? 31.285 27.482 43.487 1.00 88.17  ? 312 LI1 A H472 1 
HETATM 4139 C C50  . LI1 N 2 .   ? 28.391 25.498 24.373 1.00 60.01  ? 313 LI1 A C50  1 
HETATM 4140 C C51  . LI1 N 2 .   ? 28.585 24.015 24.666 1.00 61.52  ? 313 LI1 A C51  1 
HETATM 4141 C C52  . LI1 N 2 .   ? 27.827 23.528 25.886 1.00 54.34  ? 313 LI1 A C52  1 
HETATM 4142 C C53  . LI1 N 2 .   ? 28.682 22.733 26.861 1.00 66.23  ? 313 LI1 A C53  1 
HETATM 4143 C C55  . LI1 N 2 .   ? 28.746 23.331 28.258 1.00 79.13  ? 313 LI1 A C55  1 
HETATM 4144 C C56  . LI1 N 2 .   ? 30.130 23.288 28.887 1.00 81.04  ? 313 LI1 A C56  1 
HETATM 4145 C C57  . LI1 N 2 .   ? 30.184 23.879 30.292 1.00 70.99  ? 313 LI1 A C57  1 
HETATM 4146 C C58  . LI1 N 2 .   ? 31.519 24.483 30.703 1.00 71.94  ? 313 LI1 A C58  1 
HETATM 4147 C C46  . LI1 O 2 .   ? 30.458 32.697 34.008 1.00 72.13  ? 314 LI1 A C46  1 
HETATM 4148 C C47  . LI1 O 2 .   ? 30.375 33.520 32.728 1.00 70.54  ? 314 LI1 A C47  1 
HETATM 4149 C C48  . LI1 O 2 .   ? 31.381 33.136 31.640 1.00 75.42  ? 314 LI1 A C48  1 
HETATM 4150 C C50  . LI1 O 2 .   ? 31.302 31.640 31.327 1.00 81.45  ? 314 LI1 A C50  1 
HETATM 4151 C C51  . LI1 O 2 .   ? 32.594 31.018 30.807 1.00 92.39  ? 314 LI1 A C51  1 
HETATM 4152 C C52  . LI1 O 2 .   ? 32.520 29.508 30.639 1.00 90.22  ? 314 LI1 A C52  1 
HETATM 4153 C C53  . LI1 O 2 .   ? 33.826 28.790 30.935 1.00 81.21  ? 314 LI1 A C53  1 
HETATM 4154 C C55  . LI1 O 2 .   ? 33.841 27.335 30.501 1.00 80.85  ? 314 LI1 A C55  1 
HETATM 4155 C C56  . LI1 O 2 .   ? 33.988 27.142 29.001 1.00 79.23  ? 314 LI1 A C56  1 
HETATM 4156 C C57  . LI1 O 2 .   ? 33.597 25.748 28.523 1.00 79.04  ? 314 LI1 A C57  1 
HETATM 4157 C C58  . LI1 O 2 .   ? 34.046 25.382 27.117 1.00 72.79  ? 314 LI1 A C58  1 
HETATM 4158 C C59  . LI1 O 2 .   ? 34.297 26.620 26.274 1.00 77.30  ? 314 LI1 A C59  1 
HETATM 4159 C C60  . LI1 O 2 .   ? 33.045 24.464 26.435 1.00 80.69  ? 314 LI1 A C60  1 
HETATM 4160 C C45  . LI1 P 2 .   ? 9.313  58.871 45.845 1.00 64.69  ? 315 LI1 A C45  1 
HETATM 4161 C C46  . LI1 P 2 .   ? 10.190 57.908 45.062 1.00 72.88  ? 315 LI1 A C46  1 
HETATM 4162 C C47  . LI1 P 2 .   ? 11.544 58.508 44.701 1.00 77.31  ? 315 LI1 A C47  1 
HETATM 4163 C C48  . LI1 P 2 .   ? 11.542 59.421 43.474 1.00 82.05  ? 315 LI1 A C48  1 
HETATM 4164 C C50  . LI1 P 2 .   ? 12.933 59.480 42.839 1.00 71.87  ? 315 LI1 A C50  1 
HETATM 4165 C C51  . LI1 P 2 .   ? 13.318 58.262 42.008 1.00 53.42  ? 315 LI1 A C51  1 
HETATM 4166 C C52  . LI1 P 2 .   ? 14.725 58.334 41.435 1.00 68.84  ? 315 LI1 A C52  1 
HETATM 4167 C C53  . LI1 P 2 .   ? 15.807 57.852 42.391 1.00 75.69  ? 315 LI1 A C53  1 
HETATM 4168 C C55  . LI1 P 2 .   ? 17.209 57.869 41.799 1.00 59.77  ? 315 LI1 A C55  1 
HETATM 4169 C C56  . LI1 P 2 .   ? 17.897 56.513 41.796 1.00 59.75  ? 315 LI1 A C56  1 
HETATM 4170 C C57  . LI1 P 2 .   ? 18.783 56.265 43.016 1.00 57.15  ? 315 LI1 A C57  1 
HETATM 4171 C C58  . LI1 P 2 .   ? 19.661 55.021 42.951 1.00 64.44  ? 315 LI1 A C58  1 
HETATM 4172 C C59  . LI1 P 2 .   ? 20.849 55.111 43.894 1.00 63.46  ? 315 LI1 A C59  1 
HETATM 4173 H H451 . LI1 P 2 .   ? 9.756  59.108 46.674 1.00 77.64  ? 315 LI1 A H451 1 
HETATM 4174 H H452 . LI1 P 2 .   ? 9.228  59.689 45.331 1.00 77.64  ? 315 LI1 A H452 1 
HETATM 4175 H H461 . LI1 P 2 .   ? 9.721  57.653 44.253 1.00 87.47  ? 315 LI1 A H461 1 
HETATM 4176 H H462 . LI1 P 2 .   ? 10.320 57.108 45.594 1.00 87.47  ? 315 LI1 A H462 1 
HETATM 4177 H H471 . LI1 P 2 .   ? 12.166 57.778 44.558 1.00 92.79  ? 315 LI1 A H471 1 
HETATM 4178 H H472 . LI1 P 2 .   ? 11.866 59.004 45.471 1.00 92.79  ? 315 LI1 A H472 1 
HETATM 4179 C C52  . LI1 Q 2 .   ? 26.511 18.751 43.763 1.00 70.68  ? 316 LI1 A C52  1 
HETATM 4180 C C53  . LI1 Q 2 .   ? 25.939 17.666 42.855 1.00 66.45  ? 316 LI1 A C53  1 
HETATM 4181 C C55  . LI1 Q 2 .   ? 25.036 18.218 41.758 1.00 56.79  ? 316 LI1 A C55  1 
HETATM 4182 C C56  . LI1 Q 2 .   ? 25.573 19.455 41.037 1.00 62.55  ? 316 LI1 A C56  1 
HETATM 4183 C C57  . LI1 Q 2 .   ? 25.290 19.383 39.536 1.00 64.18  ? 316 LI1 A C57  1 
HETATM 4184 C C58  . LI1 Q 2 .   ? 25.524 18.017 38.898 1.00 74.72  ? 316 LI1 A C58  1 
HETATM 4185 C C46  . LI1 R 2 .   ? 15.433 58.549 16.268 1.00 63.58  ? 317 LI1 A C46  1 
HETATM 4186 C C47  . LI1 R 2 .   ? 15.397 59.512 17.449 1.00 75.26  ? 317 LI1 A C47  1 
HETATM 4187 C C48  . LI1 R 2 .   ? 15.256 58.845 18.812 1.00 68.53  ? 317 LI1 A C48  1 
HETATM 4188 C C49  . LI1 R 2 .   ? 13.873 58.230 18.901 1.00 64.45  ? 317 LI1 A C49  1 
HETATM 4189 C C50  . LI1 R 2 .   ? 15.331 59.973 19.835 1.00 64.28  ? 317 LI1 A C50  1 
HETATM 4190 C C51  . LI1 R 2 .   ? 15.120 59.528 21.279 1.00 59.97  ? 317 LI1 A C51  1 
HETATM 4191 C C52  . LI1 R 2 .   ? 14.459 60.565 22.162 1.00 70.98  ? 317 LI1 A C52  1 
HETATM 4192 C C53  . LI1 R 2 .   ? 13.101 60.135 22.690 1.00 66.24  ? 317 LI1 A C53  1 
HETATM 4193 C C55  . LI1 R 2 .   ? 13.167 59.066 23.759 1.00 61.88  ? 317 LI1 A C55  1 
HETATM 4194 C C56  . LI1 R 2 .   ? 12.720 59.540 25.132 1.00 57.11  ? 317 LI1 A C56  1 
HETATM 4195 C C57  . LI1 R 2 .   ? 13.876 59.912 26.055 1.00 57.20  ? 317 LI1 A C57  1 
HETATM 4196 C C58  . LI1 R 2 .   ? 13.478 60.423 27.432 1.00 68.51  ? 317 LI1 A C58  1 
HETATM 4197 C C59  . LI1 R 2 .   ? 14.679 60.899 28.231 1.00 64.62  ? 317 LI1 A C59  1 
HETATM 4198 C C60  . LI1 R 2 .   ? 12.418 61.512 27.351 1.00 69.94  ? 317 LI1 A C60  1 
HETATM 4199 H H461 . LI1 R 2 .   ? 15.811 57.700 16.539 1.00 76.30  ? 317 LI1 A H461 1 
HETATM 4200 H H462 . LI1 R 2 .   ? 14.523 58.387 15.970 1.00 76.30  ? 317 LI1 A H462 1 
HETATM 4201 H H471 . LI1 R 2 .   ? 16.210 60.040 17.431 1.00 90.33  ? 317 LI1 A H471 1 
HETATM 4202 H H472 . LI1 R 2 .   ? 14.659 60.127 17.313 1.00 90.33  ? 317 LI1 A H472 1 
HETATM 4203 H H48  . LI1 R 2 .   ? 15.938 58.170 18.956 1.00 82.25  ? 317 LI1 A H48  1 
HETATM 4204 C C1   . RET S 4 .   ? 15.099 46.332 29.762 1.00 20.58  ? 318 RET A C1   1 
HETATM 4205 C C2   . RET S 4 .   ? 14.600 47.247 28.629 1.00 33.40  ? 318 RET A C2   1 
HETATM 4206 C C3   . RET S 4 .   ? 15.164 48.638 28.619 1.00 36.83  ? 318 RET A C3   1 
HETATM 4207 C C4   . RET S 4 .   ? 14.915 49.330 29.952 1.00 21.94  ? 318 RET A C4   1 
HETATM 4208 C C5   . RET S 4 .   ? 15.258 48.467 31.125 1.00 20.41  ? 318 RET A C5   1 
HETATM 4209 C C6   . RET S 4 .   ? 15.373 47.138 31.058 1.00 20.31  ? 318 RET A C6   1 
HETATM 4210 C C7   . RET S 4 .   ? 15.842 46.388 32.237 1.00 20.43  ? 318 RET A C7   1 
HETATM 4211 C C8   . RET S 4 .   ? 15.958 45.067 32.442 1.00 21.10  ? 318 RET A C8   1 
HETATM 4212 C C9   . RET S 4 .   ? 16.443 44.380 33.612 1.00 19.90  ? 318 RET A C9   1 
HETATM 4213 C C10  . RET S 4 .   ? 16.610 43.043 33.563 1.00 19.87  ? 318 RET A C10  1 
HETATM 4214 C C11  . RET S 4 .   ? 17.117 42.194 34.557 1.00 21.15  ? 318 RET A C11  1 
HETATM 4215 C C12  . RET S 4 .   ? 17.339 40.898 34.303 1.00 21.48  ? 318 RET A C12  1 
HETATM 4216 C C13  . RET S 4 .   ? 17.754 39.877 35.221 1.00 21.20  ? 318 RET A C13  1 
HETATM 4217 C C14  . RET S 4 .   ? 17.745 38.589 34.791 1.00 22.15  ? 318 RET A C14  1 
HETATM 4218 C C15  . RET S 4 .   ? 17.696 37.405 35.547 1.00 24.74  ? 318 RET A C15  1 
HETATM 4219 C C16  . RET S 4 .   ? 16.356 45.611 29.282 1.00 22.88  ? 318 RET A C16  1 
HETATM 4220 C C17  . RET S 4 .   ? 13.950 45.335 29.964 1.00 27.67  ? 318 RET A C17  1 
HETATM 4221 C C18  . RET S 4 .   ? 15.346 49.267 32.415 1.00 21.19  ? 318 RET A C18  1 
HETATM 4222 C C19  . RET S 4 .   ? 16.777 45.202 34.850 1.00 21.75  ? 318 RET A C19  1 
HETATM 4223 C C20  . RET S 4 .   ? 18.100 40.281 36.635 1.00 23.86  ? 318 RET A C20  1 
HETATM 4224 H H21  . RET S 4 .   ? 14.803 46.837 27.763 1.00 40.10  ? 318 RET A H21  1 
HETATM 4225 H H22  . RET S 4 .   ? 13.625 47.321 28.673 1.00 40.10  ? 318 RET A H22  1 
HETATM 4226 H H31  . RET S 4 .   ? 14.760 49.160 27.897 1.00 44.21  ? 318 RET A H31  1 
HETATM 4227 H H32  . RET S 4 .   ? 16.126 48.610 28.437 1.00 44.21  ? 318 RET A H32  1 
HETATM 4228 H H41  . RET S 4 .   ? 13.974 49.591 30.019 1.00 26.34  ? 318 RET A H41  1 
HETATM 4229 H H42  . RET S 4 .   ? 15.443 50.153 30.002 1.00 26.34  ? 318 RET A H42  1 
HETATM 4230 H H7   . RET S 4 .   ? 15.771 46.935 33.045 1.00 24.53  ? 318 RET A H7   1 
HETATM 4231 H H8   . RET S 4 .   ? 16.066 44.543 31.621 1.00 25.33  ? 318 RET A H8   1 
HETATM 4232 H H10  . RET S 4 .   ? 16.348 42.593 32.734 1.00 23.85  ? 318 RET A H10  1 
HETATM 4233 H H11  . RET S 4 .   ? 17.620 42.599 35.293 1.00 25.39  ? 318 RET A H11  1 
HETATM 4234 H H12  . RET S 4 .   ? 17.204 40.604 33.379 1.00 25.79  ? 318 RET A H12  1 
HETATM 4235 H H14  . RET S 4 .   ? 17.775 38.409 33.829 1.00 26.59  ? 318 RET A H14  1 
HETATM 4236 H H15  . RET S 4 .   ? 17.763 37.480 36.520 1.00 29.70  ? 318 RET A H15  1 
HETATM 4237 H H161 . RET S 4 .   ? 16.148 44.901 28.641 1.00 27.47  ? 318 RET A H161 1 
HETATM 4238 H H162 . RET S 4 .   ? 16.981 46.221 28.840 1.00 27.47  ? 318 RET A H162 1 
HETATM 4239 H H163 . RET S 4 .   ? 16.842 45.193 30.023 1.00 27.47  ? 318 RET A H163 1 
HETATM 4240 H H171 . RET S 4 .   ? 14.181 44.670 30.645 1.00 33.21  ? 318 RET A H171 1 
HETATM 4241 H H172 . RET S 4 .   ? 13.750 44.859 29.132 1.00 33.21  ? 318 RET A H172 1 
HETATM 4242 H H173 . RET S 4 .   ? 13.136 45.794 30.254 1.00 33.21  ? 318 RET A H173 1 
HETATM 4243 H H181 . RET S 4 .   ? 15.343 50.236 32.280 1.00 25.37  ? 318 RET A H181 1 
HETATM 4244 H H182 . RET S 4 .   ? 16.156 49.089 32.935 1.00 25.37  ? 318 RET A H182 1 
HETATM 4245 H H183 . RET S 4 .   ? 14.608 49.098 33.035 1.00 25.37  ? 318 RET A H183 1 
HETATM 4246 H H191 . RET S 4 .   ? 17.720 45.463 34.840 1.00 26.11  ? 318 RET A H191 1 
HETATM 4247 H H192 . RET S 4 .   ? 16.228 46.012 34.877 1.00 26.11  ? 318 RET A H192 1 
HETATM 4248 H H193 . RET S 4 .   ? 16.606 44.680 35.660 1.00 26.11  ? 318 RET A H193 1 
HETATM 4249 H H201 . RET S 4 .   ? 17.355 40.749 37.064 1.00 28.64  ? 318 RET A H201 1 
HETATM 4250 H H202 . RET S 4 .   ? 18.315 39.500 37.185 1.00 28.64  ? 318 RET A H202 1 
HETATM 4251 H H203 . RET S 4 .   ? 18.875 40.878 36.654 1.00 28.64  ? 318 RET A H203 1 
HETATM 4252 O O    . HOH T 5 .   ? 20.649 19.772 52.357 1.00 60.37  ? 401 HOH A O    1 
HETATM 4253 O O    . HOH T 5 .   ? 9.595  47.985 54.362 1.00 55.06  ? 402 HOH A O    1 
HETATM 4254 O O    . HOH T 5 .   ? 22.772 35.096 67.436 1.00 48.62  ? 403 HOH A O    1 
HETATM 4255 O O    . HOH T 5 .   ? 21.967 26.035 53.465 1.00 61.76  ? 404 HOH A O    1 
HETATM 4256 O O    . HOH T 5 .   ? 14.622 34.391 60.498 1.00 70.01  ? 405 HOH A O    1 
HETATM 4257 O O    . HOH T 5 .   ? 17.871 35.208 32.381 1.00 23.71  ? 406 HOH A O    1 
HETATM 4258 O O    . HOH T 5 .   ? 4.153  29.361 18.657 1.00 59.20  ? 407 HOH A O    1 
HETATM 4259 O O    . HOH T 5 .   ? 22.940 45.144 16.481 1.00 46.86  ? 408 HOH A O    1 
HETATM 4260 O O    . HOH T 5 .   ? 18.063 36.707 28.760 1.00 26.89  ? 409 HOH A O    1 
HETATM 4261 O O    . HOH T 5 .   ? 15.421 40.864 23.374 1.00 43.35  ? 410 HOH A O    1 
HETATM 4262 O O    . HOH T 5 .   ? 19.180 29.155 73.676 1.00 39.46  ? 411 HOH A O    1 
HETATM 4263 O O    . HOH T 5 .   ? 7.829  30.934 18.395 1.00 47.36  ? 412 HOH A O    1 
HETATM 4264 O O    . HOH T 5 .   ? 26.614 34.162 56.905 1.00 63.85  ? 413 HOH A O    1 
HETATM 4265 O O    . HOH T 5 .   ? 8.699  27.964 54.479 1.00 38.75  ? 414 HOH A O    1 
HETATM 4266 O O    . HOH T 5 .   ? 23.447 37.013 14.770 1.00 45.81  ? 415 HOH A O    1 
HETATM 4267 O O    . HOH T 5 .   ? 16.415 34.331 29.085 1.00 27.47  ? 416 HOH A O    1 
HETATM 4268 O O    . HOH T 5 .   ? 7.911  44.789 58.173 1.00 60.45  ? 417 HOH A O    1 
HETATM 4269 O O    . HOH T 5 .   ? 16.734 23.731 46.645 1.00 35.23  ? 418 HOH A O    1 
HETATM 4270 O O    . HOH T 5 .   ? 18.752 48.120 15.924 1.00 52.41  ? 419 HOH A O    1 
HETATM 4271 O O    . HOH T 5 .   ? 15.924 21.231 47.349 1.00 46.96  ? 420 HOH A O    1 
HETATM 4272 O O    . HOH T 5 .   ? 10.123 31.298 16.299 1.00 61.03  ? 421 HOH A O    1 
HETATM 4273 O O    . HOH T 5 .   ? 17.290 23.153 58.400 1.00 55.04  ? 422 HOH A O    1 
HETATM 4274 O O    . HOH T 5 .   ? 30.735 39.890 16.070 1.00 65.41  ? 423 HOH A O    1 
HETATM 4275 O O    . HOH T 5 .   ? 27.600 34.914 51.616 1.00 46.70  ? 424 HOH A O    1 
HETATM 4276 O O    . HOH T 5 .   ? 23.775 41.916 14.587 1.00 46.73  ? 425 HOH A O    1 
HETATM 4277 O O    . HOH T 5 .   ? 7.792  39.900 54.680 1.00 65.99  ? 426 HOH A O    1 
HETATM 4278 O O    . HOH T 5 .   ? 18.872 37.537 69.327 1.00 36.33  ? 427 HOH A O    1 
HETATM 4279 O O    . HOH T 5 .   ? 15.102 25.445 14.928 1.00 56.75  ? 428 HOH A O    1 
HETATM 4280 O O    . HOH T 5 .   ? 22.657 45.382 61.928 1.00 63.16  ? 429 HOH A O    1 
HETATM 4281 O O    . HOH T 5 .   ? 4.474  51.450 20.545 1.00 26.56  ? 430 HOH A O    1 
HETATM 4282 O O    . HOH T 5 .   ? 21.984 35.645 26.300 1.00 25.67  ? 431 HOH A O    1 
HETATM 4283 O O    . HOH T 5 .   ? 8.552  49.229 10.575 1.00 48.25  ? 432 HOH A O    1 
HETATM 4284 O O    . HOH T 5 .   ? 20.128 39.961 40.813 1.00 26.84  ? 433 HOH A O    1 
HETATM 4285 O O    . HOH T 5 .   ? 18.801 32.647 41.788 1.00 42.96  ? 434 HOH A O    1 
HETATM 4286 O O    . HOH T 5 .   ? 18.786 39.878 22.522 1.00 38.40  ? 435 HOH A O    1 
HETATM 4287 O O    . HOH T 5 .   ? 8.232  33.411 17.855 1.00 48.84  ? 436 HOH A O    1 
HETATM 4288 O O    . HOH T 5 .   ? 17.214 40.177 20.244 1.00 33.77  ? 437 HOH A O    1 
HETATM 4289 O O    . HOH T 5 .   ? 19.781 35.471 14.330 1.00 48.77  ? 438 HOH A O    1 
HETATM 4290 O O    . HOH T 5 .   ? 25.669 39.091 15.172 1.00 42.54  ? 439 HOH A O    1 
HETATM 4291 O O    . HOH T 5 .   ? 28.477 55.858 21.153 1.00 78.86  ? 440 HOH A O    1 
HETATM 4292 O O    . HOH T 5 .   ? 16.992 42.425 7.133  1.00 62.79  ? 441 HOH A O    1 
HETATM 4293 O O    . HOH T 5 .   ? 26.111 52.370 51.534 1.00 79.39  ? 442 HOH A O    1 
HETATM 4294 O O    . HOH T 5 .   ? 28.042 38.331 13.763 1.00 59.78  ? 443 HOH A O    1 
HETATM 4295 O O    . HOH T 5 .   ? 21.116 45.797 14.604 1.00 56.17  ? 444 HOH A O    1 
HETATM 4296 O O    . HOH T 5 .   ? 18.190 34.727 12.733 1.00 56.08  ? 445 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 1   ? 1.5166 1.1792 0.8330 -0.2608 -0.0180 -0.0599 4   GLY A N   
2    C CA  . GLY A 1   ? 1.4144 1.1361 0.8393 -0.2141 -0.0022 -0.0595 4   GLY A CA  
3    C C   . GLY A 1   ? 1.3508 1.0826 0.8170 -0.1627 0.0464  -0.0617 4   GLY A C   
4    O O   . GLY A 1   ? 1.0773 0.8944 0.6450 -0.1383 0.0405  -0.0395 4   GLY A O   
5    N N   . THR A 2   ? 1.2569 0.8963 0.6434 -0.1468 0.0980  -0.0855 5   THR A N   
6    C CA  . THR A 2   ? 0.9832 0.6324 0.4140 -0.0978 0.1480  -0.0807 5   THR A CA  
7    C C   . THR A 2   ? 1.0154 0.6863 0.4214 -0.1049 0.1471  -0.0637 5   THR A C   
8    O O   . THR A 2   ? 1.1657 0.8585 0.6213 -0.0664 0.1841  -0.0532 5   THR A O   
9    C CB  . THR A 2   ? 1.3418 0.8892 0.7099 -0.0730 0.2094  -0.1008 5   THR A CB  
10   O OG1 . THR A 2   ? 1.3914 0.8542 0.6490 -0.1088 0.2039  -0.1110 5   THR A OG1 
11   C CG2 . THR A 2   ? 1.2259 0.7660 0.6427 -0.0558 0.2162  -0.1101 5   THR A CG2 
18   N N   . GLY A 3   ? 1.1526 0.8220 0.4873 -0.1547 0.1045  -0.0558 6   GLY A N   
19   C CA  . GLY A 3   ? 1.0868 0.7854 0.4030 -0.1626 0.0996  -0.0341 6   GLY A CA  
20   C C   . GLY A 3   ? 0.9602 0.7768 0.4210 -0.1352 0.0853  -0.0030 6   GLY A C   
21   O O   . GLY A 3   ? 1.0321 0.8755 0.4982 -0.1282 0.0942  0.0161  6   GLY A O   
25   N N   . ARG A 4   ? 0.8239 0.7026 0.3933 -0.1210 0.0658  0.0024  7   ARG A N   
26   C CA  . ARG A 4   ? 0.6508 0.6228 0.3454 -0.0971 0.0566  0.0282  7   ARG A CA  
27   C C   . ARG A 4   ? 0.5382 0.5178 0.3077 -0.0519 0.0937  0.0189  7   ARG A C   
28   O O   . ARG A 4   ? 0.6017 0.5608 0.3875 -0.0406 0.1007  0.0017  7   ARG A O   
29   C CB  . ARG A 4   ? 0.5385 0.5659 0.2960 -0.1123 0.0143  0.0437  7   ARG A CB  
30   C CG  . ARG A 4   ? 0.5699 0.6211 0.2891 -0.1575 -0.0294 0.0714  7   ARG A CG  
31   C CD  . ARG A 4   ? 0.6508 0.7450 0.4332 -0.1675 -0.0614 0.0864  7   ARG A CD  
32   N NE  . ARG A 4   ? 0.8200 0.8555 0.5452 -0.1859 -0.0684 0.0586  7   ARG A NE  
33   C CZ  . ARG A 4   ? 0.7577 0.8093 0.5343 -0.1821 -0.0803 0.0578  7   ARG A CZ  
34   N NH1 . ARG A 4   ? 0.4436 0.5565 0.3248 -0.1547 -0.0790 0.0769  7   ARG A NH1 
35   N NH2 . ARG A 4   ? 0.7916 0.7866 0.5060 -0.2059 -0.0895 0.0363  7   ARG A NH2 
49   N N   . PRO A 5   ? 0.5019 0.5161 0.3246 -0.0283 0.1144  0.0345  8   PRO A N   
50   C CA  . PRO A 5   ? 0.5129 0.5361 0.4056 0.0076  0.1457  0.0321  8   PRO A CA  
51   C C   . PRO A 5   ? 0.5005 0.5620 0.4755 0.0145  0.1252  0.0304  8   PRO A C   
52   O O   . PRO A 5   ? 0.4489 0.5068 0.4631 0.0349  0.1423  0.0259  8   PRO A O   
53   C CB  . PRO A 5   ? 0.5019 0.5625 0.4379 0.0219  0.1623  0.0552  8   PRO A CB  
54   C CG  . PRO A 5   ? 0.7109 0.7976 0.6245 -0.0025 0.1344  0.0713  8   PRO A CG  
55   C CD  . PRO A 5   ? 0.5054 0.5535 0.3284 -0.0354 0.1096  0.0597  8   PRO A CD  
63   N N   . GLU A 6   ? 0.3843 0.4810 0.3857 -0.0020 0.0907  0.0381  9   GLU A N   
64   C CA  . GLU A 6   ? 0.3290 0.4499 0.3937 0.0040  0.0755  0.0356  9   GLU A CA  
65   C C   . GLU A 6   ? 0.3351 0.4246 0.3728 -0.0008 0.0674  0.0165  9   GLU A C   
66   O O   . GLU A 6   ? 0.2871 0.3903 0.3666 0.0036  0.0558  0.0138  9   GLU A O   
67   C CB  . GLU A 6   ? 0.3049 0.4645 0.4046 -0.0064 0.0529  0.0545  9   GLU A CB  
68   C CG  . GLU A 6   ? 0.2939 0.4558 0.3547 -0.0312 0.0277  0.0640  9   GLU A CG  
69   C CD  . GLU A 6   ? 0.3346 0.5054 0.3542 -0.0480 0.0231  0.0833  9   GLU A CD  
70   O OE1 . GLU A 6   ? 0.3743 0.5322 0.3728 -0.0389 0.0453  0.0807  9   GLU A OE1 
71   O OE2 . GLU A 6   ? 0.3214 0.5149 0.3309 -0.0713 -0.0032 0.1059  9   GLU A OE2 
78   N N   . TRP A 7   ? 0.3511 0.3894 0.3099 -0.0117 0.0757  0.0027  10  TRP A N   
79   C CA  . TRP A 7   ? 0.3708 0.3751 0.3015 -0.0197 0.0675  -0.0141 10  TRP A CA  
80   C C   . TRP A 7   ? 0.3692 0.3749 0.3517 0.0064  0.0829  -0.0203 10  TRP A C   
81   O O   . TRP A 7   ? 0.3590 0.3639 0.3555 0.0038  0.0680  -0.0267 10  TRP A O   
82   C CB  . TRP A 7   ? 0.4783 0.4084 0.3009 -0.0379 0.0809  -0.0303 10  TRP A CB  
83   C CG  . TRP A 7   ? 0.6209 0.4981 0.4159 -0.0118 0.1296  -0.0412 10  TRP A CG  
84   C CD1 . TRP A 7   ? 0.7592 0.6161 0.5263 0.0017  0.1641  -0.0357 10  TRP A CD1 
85   C CD2 . TRP A 7   ? 0.5830 0.4195 0.3790 0.0076  0.1557  -0.0532 10  TRP A CD2 
86   N NE1 . TRP A 7   ? 0.7731 0.5789 0.5272 0.0305  0.2137  -0.0413 10  TRP A NE1 
87   C CE2 . TRP A 7   ? 0.6805 0.4746 0.4543 0.0349  0.2092  -0.0508 10  TRP A CE2 
88   C CE3 . TRP A 7   ? 0.6474 0.4801 0.4643 0.0071  0.1425  -0.0613 10  TRP A CE3 
89   C CZ2 . TRP A 7   ? 0.8289 0.5799 0.6072 0.0630  0.2511  -0.0527 10  TRP A CZ2 
90   C CZ3 . TRP A 7   ? 0.8328 0.6233 0.6504 0.0324  0.1799  -0.0661 10  TRP A CZ3 
91   C CH2 . TRP A 7   ? 0.7474 0.4990 0.5490 0.0608  0.2343  -0.0601 10  TRP A CH2 
102  N N   . ILE A 8   ? 0.3783 0.3909 0.3940 0.0307  0.1115  -0.0129 11  ILE A N   
103  C CA  . ILE A 8   ? 0.3156 0.3354 0.3834 0.0526  0.1238  -0.0096 11  ILE A CA  
104  C C   . ILE A 8   ? 0.2735 0.3389 0.4023 0.0476  0.0914  -0.0044 11  ILE A C   
105  O O   . ILE A 8   ? 0.3014 0.3659 0.4501 0.0527  0.0852  -0.0067 11  ILE A O   
106  C CB  . ILE A 8   ? 0.3956 0.4262 0.5013 0.0778  0.1593  0.0092  11  ILE A CB  
107  C CG1 . ILE A 8   ? 0.4750 0.5352 0.6552 0.0959  0.1625  0.0258  11  ILE A CG1 
108  C CG2 . ILE A 8   ? 0.4119 0.4871 0.5549 0.0737  0.1510  0.0244  11  ILE A CG2 
109  C CD1 . ILE A 8   ? 0.6028 0.6187 0.7575 0.1086  0.1833  0.0186  11  ILE A CD1 
121  N N   . TRP A 9   ? 0.2676 0.3658 0.4207 0.0379  0.0743  0.0036  12  TRP A N   
122  C CA  . TRP A 9   ? 0.2049 0.3263 0.3975 0.0324  0.0513  0.0063  12  TRP A CA  
123  C C   . TRP A 9   ? 0.2345 0.3427 0.4021 0.0216  0.0336  -0.0027 12  TRP A C   
124  O O   . TRP A 9   ? 0.2380 0.3468 0.4222 0.0218  0.0220  -0.0050 12  TRP A O   
125  C CB  . TRP A 9   ? 0.2076 0.3539 0.4286 0.0273  0.0477  0.0185  12  TRP A CB  
126  C CG  . TRP A 9   ? 0.1911 0.3532 0.4382 0.0361  0.0657  0.0313  12  TRP A CG  
127  C CD1 . TRP A 9   ? 0.2564 0.4261 0.4969 0.0366  0.0785  0.0405  12  TRP A CD1 
128  C CD2 . TRP A 9   ? 0.2205 0.3939 0.5032 0.0450  0.0725  0.0421  12  TRP A CD2 
129  N NE1 . TRP A 9   ? 0.2622 0.4434 0.5317 0.0470  0.0952  0.0539  12  TRP A NE1 
130  C CE2 . TRP A 9   ? 0.2515 0.4315 0.5408 0.0504  0.0887  0.0557  12  TRP A CE2 
131  C CE3 . TRP A 9   ? 0.2840 0.4582 0.5832 0.0465  0.0625  0.0449  12  TRP A CE3 
132  C CZ2 . TRP A 9   ? 0.2795 0.4677 0.5971 0.0567  0.0947  0.0737  12  TRP A CZ2 
133  C CZ3 . TRP A 9   ? 0.2476 0.4342 0.5751 0.0517  0.0677  0.0651  12  TRP A CZ3 
134  C CH2 . TRP A 9   ? 0.3132 0.5066 0.6518 0.0568  0.0840  0.0799  12  TRP A CH2 
145  N N   . LEU A 10  ? 0.2113 0.3081 0.3375 0.0094  0.0298  -0.0040 13  LEU A N   
146  C CA  . LEU A 10  ? 0.1955 0.2852 0.3067 -0.0026 0.0124  -0.0056 13  LEU A CA  
147  C C   . LEU A 10  ? 0.2394 0.2989 0.3329 0.0012  0.0154  -0.0206 13  LEU A C   
148  O O   . LEU A 10  ? 0.2538 0.3131 0.3580 -0.0004 0.0036  -0.0210 13  LEU A O   
149  C CB  . LEU A 10  ? 0.2224 0.3122 0.2947 -0.0246 0.0010  0.0036  13  LEU A CB  
150  C CG  . LEU A 10  ? 0.2312 0.3579 0.3293 -0.0268 -0.0013 0.0268  13  LEU A CG  
151  C CD1 . LEU A 10  ? 0.2321 0.3624 0.2872 -0.0519 -0.0156 0.0406  13  LEU A CD1 
152  C CD2 . LEU A 10  ? 0.2659 0.4169 0.4141 -0.0202 -0.0062 0.0436  13  LEU A CD2 
164  N N   . ALA A 11  ? 0.2672 0.2963 0.3324 0.0086  0.0362  -0.0302 14  ALA A N   
165  C CA  . ALA A 11  ? 0.2845 0.2790 0.3346 0.0161  0.0466  -0.0411 14  ALA A CA  
166  C C   . ALA A 11  ? 0.2812 0.3019 0.3895 0.0337  0.0446  -0.0338 14  ALA A C   
167  O O   . ALA A 11  ? 0.2701 0.2815 0.3815 0.0348  0.0374  -0.0371 14  ALA A O   
168  C CB  . ALA A 11  ? 0.3837 0.3298 0.3876 0.0249  0.0812  -0.0487 14  ALA A CB  
174  N N   A LEU A 12  ? 0.2596 0.3126 0.4122 0.0442  0.0488  -0.0211 15  LEU A N   
175  N N   B LEU A 12  ? 0.2612 0.3141 0.4138 0.0442  0.0488  -0.0211 15  LEU A N   
176  C CA  A LEU A 12  ? 0.2659 0.3453 0.4671 0.0512  0.0386  -0.0099 15  LEU A CA  
177  C CA  B LEU A 12  ? 0.2662 0.3454 0.4672 0.0512  0.0384  -0.0100 15  LEU A CA  
178  C C   A LEU A 12  ? 0.2400 0.3247 0.4402 0.0386  0.0131  -0.0139 15  LEU A C   
179  C C   B LEU A 12  ? 0.2417 0.3259 0.4413 0.0385  0.0131  -0.0142 15  LEU A C   
180  O O   A LEU A 12  ? 0.2354 0.3184 0.4434 0.0403  0.0035  -0.0126 15  LEU A O   
181  O O   B LEU A 12  ? 0.2354 0.3176 0.4423 0.0402  0.0036  -0.0130 15  LEU A O   
182  C CB  A LEU A 12  ? 0.2598 0.3734 0.5066 0.0559  0.0427  0.0085  15  LEU A CB  
183  C CB  B LEU A 12  ? 0.2609 0.3748 0.5082 0.0556  0.0418  0.0084  15  LEU A CB  
184  C CG  A LEU A 12  ? 0.2962 0.4410 0.5913 0.0545  0.0267  0.0276  15  LEU A CG  
185  C CG  B LEU A 12  ? 0.2910 0.4052 0.5572 0.0758  0.0741  0.0231  15  LEU A CG  
186  C CD1 A LEU A 12  ? 0.2543 0.3925 0.5556 0.0675  0.0341  0.0362  15  LEU A CD1 
187  C CD1 B LEU A 12  ? 0.3570 0.5019 0.6542 0.0725  0.0731  0.0418  15  LEU A CD1 
188  C CD2 A LEU A 12  ? 0.2502 0.4180 0.5698 0.0518  0.0297  0.0474  15  LEU A CD2 
189  C CD2 B LEU A 12  ? 0.4001 0.5147 0.6869 0.0878  0.0790  0.0377  15  LEU A CD2 
212  N N   . GLY A 13  ? 0.1838 0.2713 0.3725 0.0279  0.0064  -0.0156 16  GLY A N   
213  C CA  . GLY A 13  ? 0.1779 0.2609 0.3633 0.0214  -0.0060 -0.0155 16  GLY A CA  
214  C C   . GLY A 13  ? 0.2509 0.3173 0.4184 0.0212  -0.0099 -0.0202 16  GLY A C   
215  O O   . GLY A 13  ? 0.2356 0.2933 0.4029 0.0225  -0.0159 -0.0196 16  GLY A O   
219  N N   . THR A 14  ? 0.2043 0.2603 0.3496 0.0163  -0.0065 -0.0243 17  THR A N   
220  C CA  . THR A 14  ? 0.2232 0.2610 0.3518 0.0112  -0.0118 -0.0274 17  THR A CA  
221  C C   . THR A 14  ? 0.2751 0.3004 0.4112 0.0237  -0.0077 -0.0323 17  THR A C   
222  O O   . THR A 14  ? 0.2583 0.2778 0.3969 0.0247  -0.0142 -0.0301 17  THR A O   
223  C CB  . THR A 14  ? 0.2428 0.2592 0.3319 -0.0042 -0.0109 -0.0331 17  THR A CB  
224  O OG1 . THR A 14  ? 0.2403 0.2767 0.3248 -0.0192 -0.0200 -0.0214 17  THR A OG1 
225  C CG2 . THR A 14  ? 0.3107 0.3051 0.3819 -0.0163 -0.0198 -0.0346 17  THR A CG2 
233  N N   . ALA A 15  ? 0.2482 0.2714 0.3920 0.0351  0.0058  -0.0335 18  ALA A N   
234  C CA  . ALA A 15  ? 0.2774 0.2956 0.4377 0.0490  0.0119  -0.0291 18  ALA A CA  
235  C C   . ALA A 15  ? 0.2602 0.3021 0.4455 0.0492  -0.0061 -0.0190 18  ALA A C   
236  O O   . ALA A 15  ? 0.2883 0.3236 0.4744 0.0531  -0.0112 -0.0158 18  ALA A O   
237  C CB  . ALA A 15  ? 0.3103 0.3284 0.4863 0.0647  0.0357  -0.0214 18  ALA A CB  
243  N N   . LEU A 16  ? 0.2098 0.2715 0.4064 0.0420  -0.0156 -0.0145 19  LEU A N   
244  C CA  . LEU A 16  ? 0.2300 0.2991 0.4315 0.0347  -0.0336 -0.0069 19  LEU A CA  
245  C C   . LEU A 16  ? 0.2441 0.2871 0.4140 0.0301  -0.0377 -0.0142 19  LEU A C   
246  O O   . LEU A 16  ? 0.2755 0.3084 0.4329 0.0279  -0.0473 -0.0104 19  LEU A O   
247  C CB  . LEU A 16  ? 0.2319 0.3166 0.4448 0.0230  -0.0415 -0.0012 19  LEU A CB  
248  C CG  . LEU A 16  ? 0.2317 0.3502 0.4886 0.0287  -0.0371 0.0160  19  LEU A CG  
249  C CD1 . LEU A 16  ? 0.3086 0.4419 0.5782 0.0141  -0.0449 0.0221  19  LEU A CD1 
250  C CD2 . LEU A 16  ? 0.3221 0.4626 0.6087 0.0318  -0.0482 0.0379  19  LEU A CD2 
262  N N   . MET A 17  ? 0.2083 0.2420 0.3668 0.0290  -0.0292 -0.0193 20  MET A N   
263  C CA  . MET A 17  ? 0.2188 0.2316 0.3590 0.0297  -0.0260 -0.0172 20  MET A CA  
264  C C   . MET A 17  ? 0.2378 0.2440 0.3777 0.0358  -0.0265 -0.0165 20  MET A C   
265  O O   . MET A 17  ? 0.2808 0.2695 0.4070 0.0393  -0.0252 -0.0123 20  MET A O   
266  C CB  . MET A 17  ? 0.2398 0.2571 0.3849 0.0281  -0.0164 -0.0103 20  MET A CB  
267  C CG  . MET A 17  ? 0.2253 0.2438 0.3711 0.0246  -0.0108 -0.0085 20  MET A CG  
268  S SD  . MET A 17  ? 0.2760 0.2506 0.3871 0.0220  -0.0039 -0.0107 20  MET A SD  
269  C CE  . MET A 17  ? 0.2620 0.2361 0.3792 0.0169  0.0071  -0.0073 20  MET A CE  
279  N N   . GLY A 18  ? 0.2665 0.2778 0.4147 0.0369  -0.0244 -0.0204 21  GLY A N   
280  C CA  . GLY A 18  ? 0.2922 0.2891 0.4377 0.0408  -0.0223 -0.0202 21  GLY A CA  
281  C C   . GLY A 18  ? 0.3098 0.3067 0.4616 0.0509  -0.0250 -0.0150 21  GLY A C   
282  O O   . GLY A 18  ? 0.3099 0.2953 0.4561 0.0549  -0.0257 -0.0101 21  GLY A O   
286  N N   . LEU A 19  ? 0.2821 0.2965 0.4503 0.0543  -0.0274 -0.0104 22  LEU A N   
287  C CA  . LEU A 19  ? 0.2782 0.3050 0.4609 0.0599  -0.0358 0.0046  22  LEU A CA  
288  C C   . LEU A 19  ? 0.3463 0.3644 0.5012 0.0491  -0.0523 0.0072  22  LEU A C   
289  O O   . LEU A 19  ? 0.3495 0.3626 0.4960 0.0514  -0.0591 0.0170  22  LEU A O   
290  C CB  . LEU A 19  ? 0.2956 0.3535 0.5134 0.0630  -0.0365 0.0191  22  LEU A CB  
291  C CG  . LEU A 19  ? 0.4438 0.4977 0.6824 0.0798  -0.0095 0.0211  22  LEU A CG  
292  C CD1 . LEU A 19  ? 0.5735 0.6609 0.8473 0.0833  -0.0055 0.0415  22  LEU A CD1 
293  C CD2 . LEU A 19  ? 0.5676 0.6032 0.8065 0.0935  0.0053  0.0282  22  LEU A CD2 
305  N N   . GLY A 20  ? 0.2617 0.2702 0.3951 0.0371  -0.0556 -0.0007 23  GLY A N   
306  C CA  . GLY A 20  ? 0.2980 0.2752 0.3855 0.0262  -0.0620 -0.0018 23  GLY A CA  
307  C C   . GLY A 20  ? 0.3569 0.3058 0.4229 0.0368  -0.0478 -0.0025 23  GLY A C   
308  O O   . GLY A 20  ? 0.3619 0.2858 0.3920 0.0344  -0.0516 0.0021  23  GLY A O   
312  N N   . THR A 21  ? 0.3045 0.2579 0.3915 0.0461  -0.0327 -0.0044 24  THR A N   
313  C CA  . THR A 21  ? 0.3286 0.2641 0.4095 0.0554  -0.0195 0.0026  24  THR A CA  
314  C C   . THR A 21  ? 0.3311 0.2665 0.4146 0.0620  -0.0248 0.0084  24  THR A C   
315  O O   . THR A 21  ? 0.3574 0.2689 0.4152 0.0672  -0.0186 0.0155  24  THR A O   
316  C CB  . THR A 21  ? 0.3185 0.2703 0.4304 0.0559  -0.0119 0.0064  24  THR A CB  
317  O OG1 . THR A 21  ? 0.2812 0.2381 0.3954 0.0516  -0.0061 0.0075  24  THR A OG1 
318  C CG2 . THR A 21  ? 0.3801 0.3222 0.4988 0.0630  0.0003  0.0222  24  THR A CG2 
326  N N   . LEU A 22  ? 0.3038 0.2608 0.4167 0.0644  -0.0305 0.0077  25  LEU A N   
327  C CA  . LEU A 22  ? 0.2995 0.2565 0.4229 0.0739  -0.0304 0.0172  25  LEU A CA  
328  C C   . LEU A 22  ? 0.3342 0.2928 0.4377 0.0718  -0.0448 0.0291  25  LEU A C   
329  O O   . LEU A 22  ? 0.3755 0.3232 0.4682 0.0785  -0.0436 0.0400  25  LEU A O   
330  C CB  . LEU A 22  ? 0.3706 0.3398 0.5251 0.0796  -0.0245 0.0163  25  LEU A CB  
331  C CG  . LEU A 22  ? 0.5448 0.4972 0.7004 0.0751  -0.0125 0.0044  25  LEU A CG  
332  C CD1 . LEU A 22  ? 0.5163 0.4651 0.6820 0.0793  -0.0004 -0.0007 25  LEU A CD1 
333  C CD2 . LEU A 22  ? 0.6681 0.6002 0.8208 0.0760  -0.0058 0.0091  25  LEU A CD2 
345  N N   . TYR A 23  ? 0.3008 0.2731 0.3976 0.0591  -0.0610 0.0302  26  TYR A N   
346  C CA  . TYR A 23  ? 0.3683 0.3419 0.4377 0.0463  -0.0835 0.0451  26  TYR A CA  
347  C C   . TYR A 23  ? 0.3795 0.3021 0.3794 0.0401  -0.0791 0.0392  26  TYR A C   
348  O O   . TYR A 23  ? 0.4133 0.3249 0.3869 0.0397  -0.0862 0.0522  26  TYR A O   
349  C CB  . TYR A 23  ? 0.3273 0.3234 0.4013 0.0259  -0.1055 0.0497  26  TYR A CB  
350  C CG  . TYR A 23  ? 0.3421 0.3412 0.3831 0.0014  -0.1379 0.0690  26  TYR A CG  
351  C CD1 . TYR A 23  ? 0.4999 0.5418 0.5795 0.0046  -0.1545 0.1016  26  TYR A CD1 
352  C CD2 . TYR A 23  ? 0.4231 0.3778 0.3898 -0.0275 -0.1517 0.0578  26  TYR A CD2 
353  C CE1 . TYR A 23  ? 0.5305 0.5817 0.5789 -0.0247 -0.1919 0.1261  26  TYR A CE1 
354  C CE2 . TYR A 23  ? 0.5286 0.4770 0.4482 -0.0601 -0.1874 0.0752  26  TYR A CE2 
355  C CZ  . TYR A 23  ? 0.5838 0.5863 0.5467 -0.0605 -0.2113 0.1110  26  TYR A CZ  
356  O OH  . TYR A 23  ? 0.6818 0.6852 0.5983 -0.0990 -0.2540 0.1350  26  TYR A OH  
366  N N   . PHE A 24  ? 0.3908 0.2790 0.3599 0.0375  -0.0626 0.0229  27  PHE A N   
367  C CA  . PHE A 24  ? 0.4370 0.2641 0.3348 0.0364  -0.0464 0.0198  27  PHE A CA  
368  C C   . PHE A 24  ? 0.4722 0.2929 0.3818 0.0582  -0.0266 0.0298  27  PHE A C   
369  O O   . PHE A 24  ? 0.5341 0.3123 0.3877 0.0597  -0.0177 0.0355  27  PHE A O   
370  C CB  . PHE A 24  ? 0.4279 0.2204 0.3043 0.0368  -0.0221 0.0077  27  PHE A CB  
371  C CG  . PHE A 24  ? 0.4551 0.2390 0.3072 0.0131  -0.0378 -0.0026 27  PHE A CG  
372  C CD1 . PHE A 24  ? 0.5046 0.2913 0.3264 -0.0144 -0.0728 0.0006  27  PHE A CD1 
373  C CD2 . PHE A 24  ? 0.4503 0.2257 0.3124 0.0157  -0.0193 -0.0104 27  PHE A CD2 
374  C CE1 . PHE A 24  ? 0.5985 0.3776 0.4007 -0.0413 -0.0897 -0.0058 27  PHE A CE1 
375  C CE2 . PHE A 24  ? 0.5427 0.3062 0.3825 -0.0071 -0.0318 -0.0194 27  PHE A CE2 
376  C CZ  . PHE A 24  ? 0.5795 0.3440 0.3893 -0.0369 -0.0679 -0.0180 27  PHE A CZ  
386  N N   . LEU A 25  ? 0.3879 0.2445 0.3641 0.0725  -0.0186 0.0324  28  LEU A N   
387  C CA  . LEU A 25  ? 0.4413 0.2932 0.4347 0.0888  -0.0018 0.0443  28  LEU A CA  
388  C C   . LEU A 25  ? 0.4735 0.3299 0.4600 0.0919  -0.0138 0.0564  28  LEU A C   
389  O O   . LEU A 25  ? 0.5503 0.3802 0.5093 0.1010  -0.0010 0.0675  28  LEU A O   
390  C CB  . LEU A 25  ? 0.5693 0.4523 0.6249 0.0926  0.0022  0.0438  28  LEU A CB  
391  C CG  . LEU A 25  ? 0.6708 0.5569 0.7431 0.0956  0.0146  0.0534  28  LEU A CG  
392  C CD1 . LEU A 25  ? 0.6108 0.4859 0.6703 0.0966  0.0349  0.0622  28  LEU A CD1 
393  C CD2 . LEU A 25  ? 0.7919 0.7019 0.9006 0.0858  0.0094  0.0487  28  LEU A CD2 
405  N N   . VAL A 26  ? 0.4457 0.3373 0.4609 0.0868  -0.0352 0.0598  29  VAL A N   
406  C CA  . VAL A 26  ? 0.4501 0.3549 0.4701 0.0915  -0.0462 0.0801  29  VAL A CA  
407  C C   . VAL A 26  ? 0.5362 0.4157 0.4843 0.0756  -0.0633 0.0881  29  VAL A C   
408  O O   . VAL A 26  ? 0.5432 0.4088 0.4651 0.0807  -0.0627 0.1040  29  VAL A O   
409  C CB  . VAL A 26  ? 0.4771 0.4287 0.5559 0.0939  -0.0581 0.0909  29  VAL A CB  
410  C CG1 . VAL A 26  ? 0.5547 0.5280 0.6475 0.1001  -0.0692 0.1216  29  VAL A CG1 
411  C CG2 . VAL A 26  ? 0.6047 0.5590 0.7304 0.1066  -0.0365 0.0796  29  VAL A CG2 
421  N N   . LYS A 27  ? 0.4704 0.3386 0.3788 0.0527  -0.0798 0.0779  30  LYS A N   
422  C CA  . LYS A 27  ? 0.5505 0.3790 0.3697 0.0272  -0.0993 0.0823  30  LYS A CA  
423  C C   . LYS A 27  ? 0.6282 0.3855 0.3722 0.0365  -0.0690 0.0758  30  LYS A C   
424  O O   . LYS A 27  ? 0.7585 0.4819 0.4318 0.0254  -0.0782 0.0868  30  LYS A O   
425  C CB  . LYS A 27  ? 0.5998 0.4145 0.3844 -0.0019 -0.1169 0.0682  30  LYS A CB  
426  C CG  . LYS A 27  ? 0.7835 0.5769 0.4908 -0.0423 -0.1557 0.0791  30  LYS A CG  
427  C CD  . LYS A 27  ? 0.8721 0.6301 0.5295 -0.0741 -0.1665 0.0604  30  LYS A CD  
428  C CE  . LYS A 27  ? 1.0973 0.8608 0.7058 -0.1244 -0.2203 0.0791  30  LYS A CE  
429  N NZ  . LYS A 27  ? 1.2451 1.0840 0.9383 -0.1385 -0.2493 0.0936  30  LYS A NZ  
443  N N   . GLY A 28  ? 0.6146 0.3948 0.3820 0.0878  -0.0873 0.1094  31  GLY A N   
444  C CA  . GLY A 28  ? 0.6737 0.4513 0.4138 0.0753  -0.0726 0.1159  31  GLY A CA  
445  C C   . GLY A 28  ? 0.8163 0.5537 0.5184 0.0693  -0.0614 0.1359  31  GLY A C   
446  O O   . GLY A 28  ? 0.7637 0.4966 0.4388 0.0587  -0.0480 0.1420  31  GLY A O   
450  N N   . MET A 29  ? 0.7801 0.4875 0.4801 0.0754  -0.0655 0.1455  32  MET A N   
451  C CA  . MET A 29  ? 0.9496 0.6215 0.6220 0.0685  -0.0532 0.1626  32  MET A CA  
452  C C   . MET A 29  ? 0.9160 0.5811 0.5502 0.0782  -0.0592 0.1720  32  MET A C   
453  O O   . MET A 29  ? 1.1615 0.8339 0.7965 0.0964  -0.0780 0.1694  32  MET A O   
454  C CB  . MET A 29  ? 1.0392 0.6957 0.7351 0.0720  -0.0559 0.1642  32  MET A CB  
455  C CG  . MET A 29  ? 1.1748 0.8239 0.8943 0.0547  -0.0399 0.1617  32  MET A CG  
456  S SD  . MET A 29  ? 1.4111 1.0452 1.1594 0.0600  -0.0441 0.1608  32  MET A SD  
457  C CE  . MET A 29  ? 1.2526 0.8496 0.9683 0.0573  -0.0342 0.1800  32  MET A CE  
467  N N   . GLY A 30  ? 0.9925 0.6452 0.5944 0.0657  -0.0427 0.1818  33  GLY A N   
468  C CA  . GLY A 30  ? 1.0768 0.7211 0.6388 0.0728  -0.0460 0.1920  33  GLY A CA  
469  C C   . GLY A 30  ? 1.1523 0.8214 0.6943 0.0753  -0.0498 0.1848  33  GLY A C   
470  O O   . GLY A 30  ? 1.2365 0.8994 0.7415 0.0769  -0.0479 0.1932  33  GLY A O   
474  N N   . VAL A 31  ? 0.9200 0.6173 0.4850 0.0760  -0.0552 0.1691  34  VAL A N   
475  C CA  . VAL A 31  ? 0.9282 0.6502 0.4757 0.0766  -0.0564 0.1602  34  VAL A CA  
476  C C   . VAL A 31  ? 0.9278 0.6411 0.4489 0.0561  -0.0311 0.1669  34  VAL A C   
477  O O   . VAL A 31  ? 0.9665 0.6776 0.5097 0.0373  -0.0120 0.1658  34  VAL A O   
478  C CB  . VAL A 31  ? 0.9958 0.7625 0.5987 0.0749  -0.0615 0.1362  34  VAL A CB  
479  C CG1 . VAL A 31  ? 0.9083 0.7081 0.5082 0.0706  -0.0580 0.1226  34  VAL A CG1 
480  C CG2 . VAL A 31  ? 0.9072 0.6835 0.5339 0.0946  -0.0854 0.1281  34  VAL A CG2 
490  N N   . SER A 32  ? 0.9424 0.6589 0.4263 0.0580  -0.0300 0.1702  35  SER A N   
491  C CA  . SER A 32  ? 0.9574 0.6670 0.4149 0.0387  -0.0053 0.1759  35  SER A CA  
492  C C   . SER A 32  ? 1.1037 0.8457 0.5536 0.0339  -0.0006 0.1608  35  SER A C   
493  O O   . SER A 32  ? 1.0518 0.7964 0.4932 0.0147  0.0226  0.1596  35  SER A O   
494  C CB  . SER A 32  ? 1.1443 0.8289 0.5646 0.0412  -0.0028 0.1936  35  SER A CB  
495  O OG  . SER A 32  ? 1.2471 0.9400 0.6507 0.0623  -0.0263 0.1935  35  SER A OG  
501  N N   . ASP A 33  ? 0.9402 0.7143 0.4057 0.0491  -0.0209 0.1452  36  ASP A N   
502  C CA  . ASP A 33  ? 0.9528 0.7659 0.4264 0.0441  -0.0170 0.1260  36  ASP A CA  
503  C C   . ASP A 33  ? 0.7322 0.5701 0.2578 0.0256  -0.0003 0.1109  36  ASP A C   
504  O O   . ASP A 33  ? 0.6841 0.5326 0.2560 0.0276  -0.0071 0.1033  36  ASP A O   
505  C CB  . ASP A 33  ? 0.8691 0.7118 0.3580 0.0637  -0.0423 0.1100  36  ASP A CB  
506  C CG  . ASP A 33  ? 0.7835 0.6663 0.2834 0.0588  -0.0385 0.0882  36  ASP A CG  
507  O OD1 . ASP A 33  ? 0.9443 0.8263 0.3991 0.0579  -0.0335 0.0908  36  ASP A OD1 
508  O OD2 . ASP A 33  ? 0.7584 0.6722 0.3107 0.0559  -0.0397 0.0687  36  ASP A OD2 
513  N N   . PRO A 34  ? 0.7626 0.6112 0.2815 0.0084  0.0209  0.1056  37  PRO A N   
514  C CA  . PRO A 34  ? 0.7917 0.6627 0.3603 -0.0076 0.0357  0.0917  37  PRO A CA  
515  C C   . PRO A 34  ? 0.7031 0.6119 0.3229 -0.0004 0.0231  0.0704  37  PRO A C   
516  O O   . PRO A 34  ? 0.6736 0.5929 0.3381 -0.0062 0.0263  0.0635  37  PRO A O   
517  C CB  . PRO A 34  ? 0.8699 0.7483 0.4170 -0.0247 0.0590  0.0878  37  PRO A CB  
518  C CG  . PRO A 34  ? 0.9266 0.7925 0.4151 -0.0168 0.0550  0.0967  37  PRO A CG  
519  C CD  . PRO A 34  ? 0.8744 0.7149 0.3391 0.0032  0.0326  0.1119  37  PRO A CD  
527  N N   . ASP A 35  ? 0.7256 0.6545 0.3396 0.0121  0.0089  0.0594  38  ASP A N   
528  C CA  . ASP A 35  ? 0.6395 0.6008 0.3023 0.0186  -0.0021 0.0392  38  ASP A CA  
529  C C   . ASP A 35  ? 0.5751 0.5279 0.2652 0.0289  -0.0173 0.0428  38  ASP A C   
530  O O   . ASP A 35  ? 0.5318 0.4983 0.2678 0.0260  -0.0166 0.0338  38  ASP A O   
531  C CB  . ASP A 35  ? 0.6578 0.6413 0.3076 0.0294  -0.0137 0.0254  38  ASP A CB  
532  C CG  . ASP A 35  ? 0.9745 0.9846 0.6300 0.0185  0.0007  0.0090  38  ASP A CG  
533  O OD1 . ASP A 35  ? 1.3485 1.3826 1.0046 0.0258  -0.0076 -0.0073 38  ASP A OD1 
534  O OD2 . ASP A 35  ? 1.0346 1.0430 0.6959 0.0028  0.0205  0.0107  38  ASP A OD2 
539  N N   . ALA A 36  ? 0.5808 0.5101 0.2423 0.0416  -0.0310 0.0563  39  ALA A N   
540  C CA  . ALA A 36  ? 0.5572 0.4789 0.2447 0.0514  -0.0450 0.0585  39  ALA A CA  
541  C C   . ALA A 36  ? 0.5370 0.4436 0.2461 0.0396  -0.0328 0.0666  39  ALA A C   
542  O O   . ALA A 36  ? 0.4986 0.4123 0.2458 0.0419  -0.0385 0.0608  39  ALA A O   
543  C CB  . ALA A 36  ? 0.5993 0.4975 0.2511 0.0680  -0.0618 0.0714  39  ALA A CB  
549  N N   . LYS A 37  ? 0.5967 0.4833 0.2816 0.0262  -0.0154 0.0789  40  LYS A N   
550  C CA  . LYS A 37  ? 0.5493 0.4246 0.2564 0.0138  -0.0032 0.0839  40  LYS A CA  
551  C C   . LYS A 37  ? 0.5072 0.4131 0.2628 0.0064  0.0019  0.0673  40  LYS A C   
552  O O   . LYS A 37  ? 0.5542 0.4588 0.3393 0.0039  0.0019  0.0670  40  LYS A O   
553  C CB  . LYS A 37  ? 0.6340 0.4865 0.3086 -0.0015 0.0172  0.0964  40  LYS A CB  
554  C CG  . LYS A 37  ? 0.7858 0.5977 0.4127 0.0047  0.0144  0.1173  40  LYS A CG  
555  C CD  . LYS A 37  ? 0.9157 0.7064 0.5043 -0.0111 0.0368  0.1285  40  LYS A CD  
556  C CE  . LYS A 37  ? 1.0481 0.8170 0.6488 -0.0267 0.0536  0.1357  40  LYS A CE  
557  N NZ  . LYS A 37  ? 1.0902 0.8400 0.6568 -0.0446 0.0784  0.1444  40  LYS A NZ  
571  N N   . LYS A 38  ? 0.4812 0.4141 0.2448 0.0030  0.0068  0.0536  41  LYS A N   
572  C CA  . LYS A 38  ? 0.4333 0.3940 0.2431 -0.0012 0.0099  0.0383  41  LYS A CA  
573  C C   . LYS A 38  ? 0.4129 0.3804 0.2534 0.0102  -0.0055 0.0330  41  LYS A C   
574  O O   . LYS A 38  ? 0.3833 0.3552 0.2549 0.0073  -0.0041 0.0306  41  LYS A O   
575  C CB  . LYS A 38  ? 0.4793 0.4669 0.2927 -0.0029 0.0142  0.0230  41  LYS A CB  
576  C CG  . LYS A 38  ? 0.7844 0.7781 0.5889 -0.0178 0.0336  0.0203  41  LYS A CG  
577  C CD  . LYS A 38  ? 0.8623 0.8687 0.6423 -0.0161 0.0351  0.0124  41  LYS A CD  
578  C CE  . LYS A 38  ? 1.0897 1.1131 0.8735 -0.0304 0.0544  0.0023  41  LYS A CE  
579  N NZ  . LYS A 38  ? 1.2263 1.2327 0.9607 -0.0390 0.0672  0.0125  41  LYS A NZ  
593  N N   . PHE A 39  ? 0.4068 0.3772 0.2389 0.0235  -0.0203 0.0296  42  PHE A N   
594  C CA  . PHE A 39  ? 0.3759 0.3551 0.2393 0.0330  -0.0330 0.0219  42  PHE A CA  
595  C C   . PHE A 39  ? 0.3726 0.3313 0.2408 0.0355  -0.0377 0.0326  42  PHE A C   
596  O O   . PHE A 39  ? 0.3636 0.3291 0.2642 0.0360  -0.0397 0.0276  42  PHE A O   
597  C CB  . PHE A 39  ? 0.4104 0.3994 0.2648 0.0462  -0.0476 0.0134  42  PHE A CB  
598  C CG  . PHE A 39  ? 0.3827 0.3970 0.2428 0.0444  -0.0440 -0.0022 42  PHE A CG  
599  C CD1 . PHE A 39  ? 0.3787 0.4136 0.2796 0.0422  -0.0411 -0.0169 42  PHE A CD1 
600  C CD2 . PHE A 39  ? 0.4603 0.4764 0.2850 0.0449  -0.0428 -0.0023 42  PHE A CD2 
601  C CE1 . PHE A 39  ? 0.4293 0.4866 0.3380 0.0407  -0.0373 -0.0327 42  PHE A CE1 
602  C CE2 . PHE A 39  ? 0.4676 0.5086 0.2990 0.0431  -0.0393 -0.0189 42  PHE A CE2 
603  C CZ  . PHE A 39  ? 0.5078 0.5694 0.3831 0.0409  -0.0365 -0.0346 42  PHE A CZ  
613  N N   . TYR A 40  ? 0.4092 0.3415 0.2449 0.0368  -0.0386 0.0476  43  TYR A N   
614  C CA  . TYR A 40  ? 0.4060 0.3181 0.2484 0.0386  -0.0420 0.0566  43  TYR A CA  
615  C C   . TYR A 40  ? 0.4185 0.3313 0.2831 0.0252  -0.0288 0.0571  43  TYR A C   
616  O O   . TYR A 40  ? 0.3913 0.3035 0.2802 0.0263  -0.0319 0.0555  43  TYR A O   
617  C CB  . TYR A 40  ? 0.4534 0.3337 0.2558 0.0425  -0.0441 0.0731  43  TYR A CB  
618  C CG  . TYR A 40  ? 0.4760 0.3509 0.2676 0.0608  -0.0635 0.0736  43  TYR A CG  
619  C CD1 . TYR A 40  ? 0.5149 0.3837 0.3273 0.0691  -0.0738 0.0728  43  TYR A CD1 
620  C CD2 . TYR A 40  ? 0.5261 0.4045 0.2883 0.0698  -0.0715 0.0732  43  TYR A CD2 
621  C CE1 . TYR A 40  ? 0.5571 0.4234 0.3624 0.0870  -0.0926 0.0711  43  TYR A CE1 
622  C CE2 . TYR A 40  ? 0.5805 0.4567 0.3333 0.0882  -0.0913 0.0720  43  TYR A CE2 
623  C CZ  . TYR A 40  ? 0.5728 0.4438 0.3500 0.0966  -0.1017 0.0704  43  TYR A CZ  
624  O OH  . TYR A 40  ? 0.6416 0.5134 0.4126 0.1158  -0.1222 0.0670  43  TYR A OH  
634  N N   . ALA A 41  ? 0.4070 0.3231 0.2641 0.0127  -0.0141 0.0578  44  ALA A N   
635  C CA  . ALA A 41  ? 0.4004 0.3209 0.2804 0.0005  -0.0026 0.0560  44  ALA A CA  
636  C C   . ALA A 41  ? 0.3667 0.3119 0.2845 0.0028  -0.0063 0.0437  44  ALA A C   
637  O O   . ALA A 41  ? 0.3587 0.3033 0.2972 0.0017  -0.0072 0.0434  44  ALA A O   
638  C CB  . ALA A 41  ? 0.4187 0.3416 0.2858 -0.0134 0.0142  0.0563  44  ALA A CB  
644  N N   . ILE A 42  ? 0.3338 0.2997 0.2604 0.0060  -0.0079 0.0334  45  ILE A N   
645  C CA  . ILE A 42  ? 0.3088 0.2946 0.2698 0.0087  -0.0103 0.0228  45  ILE A CA  
646  C C   . ILE A 42  ? 0.3187 0.2990 0.2928 0.0174  -0.0212 0.0232  45  ILE A C   
647  O O   . ILE A 42  ? 0.3272 0.3112 0.3235 0.0165  -0.0209 0.0216  45  ILE A O   
648  C CB  . ILE A 42  ? 0.3330 0.3385 0.2995 0.0116  -0.0104 0.0111  45  ILE A CB  
649  C CG1 . ILE A 42  ? 0.3719 0.3865 0.3307 0.0020  0.0022  0.0082  45  ILE A CG1 
650  C CG2 . ILE A 42  ? 0.3501 0.3701 0.3508 0.0161  -0.0137 0.0018  45  ILE A CG2 
651  C CD1 . ILE A 42  ? 0.4265 0.4576 0.3827 0.0045  0.0026  -0.0030 45  ILE A CD1 
663  N N   . THR A 43  ? 0.3123 0.2847 0.2727 0.0263  -0.0312 0.0245  46  THR A N   
664  C CA  . THR A 43  ? 0.2998 0.2723 0.2772 0.0349  -0.0413 0.0207  46  THR A CA  
665  C C   . THR A 43  ? 0.3795 0.3352 0.3581 0.0341  -0.0424 0.0287  46  THR A C   
666  O O   . THR A 43  ? 0.3595 0.3181 0.3589 0.0375  -0.0463 0.0245  46  THR A O   
667  C CB  . THR A 43  ? 0.3131 0.2861 0.2772 0.0457  -0.0528 0.0170  46  THR A CB  
668  O OG1 . THR A 43  ? 0.3270 0.3175 0.2906 0.0453  -0.0508 0.0076  46  THR A OG1 
669  C CG2 . THR A 43  ? 0.3898 0.3675 0.3768 0.0541  -0.0626 0.0091  46  THR A CG2 
677  N N   . THR A 44  ? 0.3080 0.2455 0.2651 0.0292  -0.0380 0.0395  47  THR A N   
678  C CA  . THR A 44  ? 0.2987 0.2196 0.2585 0.0276  -0.0380 0.0458  47  THR A CA  
679  C C   . THR A 44  ? 0.3456 0.2758 0.3261 0.0180  -0.0291 0.0430  47  THR A C   
680  O O   . THR A 44  ? 0.3181 0.2454 0.3128 0.0184  -0.0308 0.0421  47  THR A O   
681  C CB  . THR A 44  ? 0.3266 0.2225 0.2571 0.0249  -0.0347 0.0580  47  THR A CB  
682  O OG1 . THR A 44  ? 0.4010 0.2870 0.3073 0.0360  -0.0447 0.0620  47  THR A OG1 
683  C CG2 . THR A 44  ? 0.4004 0.2773 0.3358 0.0236  -0.0347 0.0631  47  THR A CG2 
691  N N   . LEU A 45  ? 0.3089 0.2515 0.2914 0.0103  -0.0203 0.0405  48  LEU A N   
692  C CA  . LEU A 45  ? 0.2870 0.2412 0.2891 0.0031  -0.0139 0.0367  48  LEU A CA  
693  C C   . LEU A 45  ? 0.2820 0.2487 0.3071 0.0089  -0.0191 0.0305  48  LEU A C   
694  O O   . LEU A 45  ? 0.2896 0.2599 0.3275 0.0063  -0.0176 0.0295  48  LEU A O   
695  C CB  . LEU A 45  ? 0.2991 0.2673 0.3018 -0.0045 -0.0047 0.0331  48  LEU A CB  
696  C CG  . LEU A 45  ? 0.3850 0.3441 0.3722 -0.0153 0.0056  0.0374  48  LEU A CG  
697  C CD1 . LEU A 45  ? 0.4391 0.4160 0.4290 -0.0213 0.0143  0.0308  48  LEU A CD1 
698  C CD2 . LEU A 45  ? 0.3982 0.3534 0.3960 -0.0228 0.0100  0.0377  48  LEU A CD2 
710  N N   . VAL A 46  ? 0.2429 0.2167 0.2733 0.0165  -0.0245 0.0257  49  VAL A N   
711  C CA  . VAL A 46  ? 0.2373 0.2211 0.2888 0.0205  -0.0265 0.0199  49  VAL A CA  
712  C C   . VAL A 46  ? 0.2910 0.2665 0.3492 0.0224  -0.0297 0.0213  49  VAL A C   
713  O O   . VAL A 46  ? 0.2498 0.2297 0.3192 0.0202  -0.0269 0.0208  49  VAL A O   
714  C CB  . VAL A 46  ? 0.2363 0.2275 0.2927 0.0269  -0.0304 0.0129  49  VAL A CB  
715  C CG1 . VAL A 46  ? 0.2725 0.2680 0.3501 0.0308  -0.0316 0.0074  49  VAL A CG1 
716  C CG2 . VAL A 46  ? 0.2640 0.2678 0.3209 0.0245  -0.0253 0.0087  49  VAL A CG2 
726  N N   . PRO A 47  ? 0.2585 0.2228 0.3103 0.0268  -0.0357 0.0224  50  PRO A N   
727  C CA  . PRO A 47  ? 0.2344 0.1924 0.2949 0.0277  -0.0375 0.0218  50  PRO A CA  
728  C C   . PRO A 47  ? 0.2784 0.2291 0.3344 0.0209  -0.0332 0.0266  50  PRO A C   
729  O O   . PRO A 47  ? 0.2716 0.2222 0.3371 0.0198  -0.0324 0.0246  50  PRO A O   
730  C CB  . PRO A 47  ? 0.2792 0.2284 0.3353 0.0358  -0.0462 0.0203  50  PRO A CB  
731  C CG  . PRO A 47  ? 0.3293 0.2732 0.3640 0.0373  -0.0484 0.0251  50  PRO A CG  
732  C CD  . PRO A 47  ? 0.2775 0.2358 0.3149 0.0330  -0.0424 0.0227  50  PRO A CD  
740  N N   . ALA A 48  ? 0.2596 0.2043 0.3016 0.0154  -0.0294 0.0318  51  ALA A N   
741  C CA  . ALA A 48  ? 0.2614 0.2001 0.3022 0.0074  -0.0240 0.0340  51  ALA A CA  
742  C C   . ALA A 48  ? 0.2522 0.2082 0.3070 0.0032  -0.0201 0.0296  51  ALA A C   
743  O O   . ALA A 48  ? 0.2562 0.2125 0.3173 0.0000  -0.0190 0.0276  51  ALA A O   
744  C CB  . ALA A 48  ? 0.2585 0.1876 0.2826 0.0008  -0.0183 0.0395  51  ALA A CB  
750  N N   . ILE A 49  ? 0.2291 0.1995 0.2883 0.0037  -0.0185 0.0276  52  ILE A N   
751  C CA  . ILE A 49  ? 0.2068 0.1929 0.2782 0.0026  -0.0167 0.0242  52  ILE A CA  
752  C C   . ILE A 49  ? 0.2282 0.2144 0.3075 0.0080  -0.0200 0.0230  52  ILE A C   
753  O O   . ILE A 49  ? 0.2531 0.2447 0.3369 0.0067  -0.0195 0.0216  52  ILE A O   
754  C CB  . ILE A 49  ? 0.2094 0.2088 0.2851 0.0041  -0.0149 0.0220  52  ILE A CB  
755  C CG1 . ILE A 49  ? 0.2177 0.2193 0.2865 -0.0033 -0.0093 0.0216  52  ILE A CG1 
756  C CG2 . ILE A 49  ? 0.2523 0.2661 0.3406 0.0068  -0.0154 0.0194  52  ILE A CG2 
757  C CD1 . ILE A 49  ? 0.2784 0.2913 0.3493 -0.0019 -0.0070 0.0183  52  ILE A CD1 
769  N N   . ALA A 50  ? 0.2111 0.1930 0.2923 0.0138  -0.0228 0.0224  53  ALA A N   
770  C CA  . ALA A 50  ? 0.2405 0.2223 0.3301 0.0173  -0.0234 0.0204  53  ALA A CA  
771  C C   . ALA A 50  ? 0.2327 0.2074 0.3214 0.0151  -0.0239 0.0195  53  ALA A C   
772  O O   . ALA A 50  ? 0.2600 0.2379 0.3527 0.0149  -0.0220 0.0181  53  ALA A O   
773  C CB  . ALA A 50  ? 0.2583 0.2379 0.3535 0.0227  -0.0254 0.0170  53  ALA A CB  
779  N N   . PHE A 51  ? 0.2118 0.1759 0.2945 0.0139  -0.0260 0.0202  54  PHE A N   
780  C CA  . PHE A 51  ? 0.2215 0.1783 0.3052 0.0116  -0.0260 0.0183  54  PHE A CA  
781  C C   . PHE A 51  ? 0.2492 0.2144 0.3339 0.0056  -0.0223 0.0170  54  PHE A C   
782  O O   . PHE A 51  ? 0.2470 0.2143 0.3357 0.0049  -0.0214 0.0132  54  PHE A O   
783  C CB  . PHE A 51  ? 0.2527 0.1936 0.3276 0.0111  -0.0281 0.0213  54  PHE A CB  
784  C CG  . PHE A 51  ? 0.2834 0.2156 0.3602 0.0072  -0.0267 0.0190  54  PHE A CG  
785  C CD1 . PHE A 51  ? 0.3071 0.2351 0.3922 0.0111  -0.0292 0.0138  54  PHE A CD1 
786  C CD2 . PHE A 51  ? 0.3085 0.2381 0.3812 -0.0010 -0.0219 0.0201  54  PHE A CD2 
787  C CE1 . PHE A 51  ? 0.3207 0.2408 0.4093 0.0075  -0.0275 0.0101  54  PHE A CE1 
788  C CE2 . PHE A 51  ? 0.3503 0.2720 0.4270 -0.0053 -0.0199 0.0160  54  PHE A CE2 
789  C CZ  . PHE A 51  ? 0.3600 0.2765 0.4441 -0.0006 -0.0229 0.0113  54  PHE A CZ  
799  N N   . THR A 52  ? 0.2465 0.2177 0.3278 0.0011  -0.0202 0.0186  55  THR A N   
800  C CA  . THR A 52  ? 0.2130 0.1952 0.2971 -0.0042 -0.0180 0.0149  55  THR A CA  
801  C C   . THR A 52  ? 0.2519 0.2467 0.3388 0.0000  -0.0192 0.0140  55  THR A C   
802  O O   . THR A 52  ? 0.2226 0.2243 0.3100 -0.0018 -0.0192 0.0101  55  THR A O   
803  C CB  . THR A 52  ? 0.2422 0.2319 0.3259 -0.0101 -0.0150 0.0143  55  THR A CB  
804  O OG1 . THR A 52  ? 0.3229 0.3233 0.4080 -0.0063 -0.0157 0.0161  55  THR A OG1 
805  C CG2 . THR A 52  ? 0.3067 0.2794 0.3829 -0.0147 -0.0119 0.0175  55  THR A CG2 
813  N N   . MET A 53  ? 0.2072 0.2042 0.2950 0.0058  -0.0200 0.0175  56  MET A N   
814  C CA  . MET A 53  ? 0.1974 0.2022 0.2852 0.0101  -0.0202 0.0186  56  MET A CA  
815  C C   . MET A 53  ? 0.2392 0.2366 0.3261 0.0118  -0.0183 0.0183  56  MET A C   
816  O O   . MET A 53  ? 0.2372 0.2392 0.3193 0.0128  -0.0174 0.0186  56  MET A O   
817  C CB  . MET A 53  ? 0.2339 0.2423 0.3246 0.0153  -0.0203 0.0220  56  MET A CB  
818  C CG  . MET A 53  ? 0.2444 0.2644 0.3378 0.0136  -0.0213 0.0205  56  MET A CG  
819  S SD  . MET A 53  ? 0.3139 0.3512 0.4078 0.0141  -0.0244 0.0175  56  MET A SD  
820  C CE  . MET A 53  ? 0.3996 0.4382 0.4934 0.0040  -0.0230 0.0109  56  MET A CE  
830  N N   . TYR A 54  ? 0.2240 0.2112 0.3149 0.0123  -0.0177 0.0167  57  TYR A N   
831  C CA  . TYR A 54  ? 0.2323 0.2146 0.3255 0.0123  -0.0149 0.0132  57  TYR A CA  
832  C C   . TYR A 54  ? 0.2494 0.2336 0.3398 0.0079  -0.0145 0.0089  57  TYR A C   
833  O O   . TYR A 54  ? 0.2367 0.2233 0.3242 0.0072  -0.0112 0.0066  57  TYR A O   
834  C CB  . TYR A 54  ? 0.2064 0.1805 0.3079 0.0143  -0.0161 0.0096  57  TYR A CB  
835  C CG  . TYR A 54  ? 0.2057 0.1796 0.3135 0.0177  -0.0133 0.0094  57  TYR A CG  
836  C CD1 . TYR A 54  ? 0.2251 0.2007 0.3343 0.0204  -0.0149 0.0120  57  TYR A CD1 
837  C CD2 . TYR A 54  ? 0.2374 0.2097 0.3509 0.0170  -0.0074 0.0053  57  TYR A CD2 
838  C CE1 . TYR A 54  ? 0.2170 0.1921 0.3343 0.0227  -0.0113 0.0102  57  TYR A CE1 
839  C CE2 . TYR A 54  ? 0.2868 0.2576 0.4077 0.0184  -0.0027 0.0042  57  TYR A CE2 
840  C CZ  . TYR A 54  ? 0.2488 0.2208 0.3726 0.0214  -0.0049 0.0063  57  TYR A CZ  
841  O OH  . TYR A 54  ? 0.2316 0.2016 0.3650 0.0221  0.0008  0.0037  57  TYR A OH  
851  N N   . LEU A 55  ? 0.2065 0.1889 0.2974 0.0044  -0.0169 0.0070  58  LEU A N   
852  C CA  . LEU A 55  ? 0.2151 0.1996 0.3059 -0.0004 -0.0160 0.0008  58  LEU A CA  
853  C C   . LEU A 55  ? 0.2394 0.2386 0.3238 -0.0015 -0.0158 0.0000  58  LEU A C   
854  O O   . LEU A 55  ? 0.2492 0.2529 0.3309 -0.0034 -0.0141 -0.0055 58  LEU A O   
855  C CB  . LEU A 55  ? 0.2281 0.2057 0.3208 -0.0049 -0.0170 -0.0005 58  LEU A CB  
856  C CG  . LEU A 55  ? 0.2382 0.2161 0.3341 -0.0109 -0.0153 -0.0088 58  LEU A CG  
857  C CD1 . LEU A 55  ? 0.2997 0.2707 0.4009 -0.0092 -0.0142 -0.0147 58  LEU A CD1 
858  C CD2 . LEU A 55  ? 0.2840 0.2511 0.3813 -0.0161 -0.0143 -0.0085 58  LEU A CD2 
870  N N   . SER A 56  ? 0.1927 0.2005 0.2745 0.0006  -0.0180 0.0045  59  SER A N   
871  C CA  . SER A 56  ? 0.2024 0.2254 0.2780 0.0019  -0.0201 0.0034  59  SER A CA  
872  C C   . SER A 56  ? 0.2461 0.2679 0.3118 0.0069  -0.0182 0.0074  59  SER A C   
873  O O   . SER A 56  ? 0.2725 0.3038 0.3290 0.0076  -0.0194 0.0051  59  SER A O   
874  C CB  . SER A 56  ? 0.2347 0.2680 0.3123 0.0048  -0.0235 0.0065  59  SER A CB  
875  O OG  . SER A 56  ? 0.3115 0.3407 0.3864 0.0120  -0.0235 0.0144  59  SER A OG  
881  N N   . MET A 57  ? 0.2234 0.2334 0.2903 0.0099  -0.0146 0.0127  60  MET A N   
882  C CA  . MET A 57  ? 0.2325 0.2379 0.2898 0.0125  -0.0097 0.0163  60  MET A CA  
883  C C   . MET A 57  ? 0.2599 0.2631 0.3163 0.0076  -0.0050 0.0089  60  MET A C   
884  O O   . MET A 57  ? 0.2671 0.2729 0.3104 0.0077  -0.0017 0.0091  60  MET A O   
885  C CB  . MET A 57  ? 0.2296 0.2235 0.2921 0.0157  -0.0057 0.0218  60  MET A CB  
886  C CG  . MET A 57  ? 0.2607 0.2574 0.3251 0.0207  -0.0098 0.0276  60  MET A CG  
887  S SD  . MET A 57  ? 0.3061 0.2893 0.3757 0.0248  -0.0035 0.0334  60  MET A SD  
888  C CE  . MET A 57  ? 0.3171 0.2992 0.4034 0.0215  -0.0056 0.0259  60  MET A CE  
898  N N   . LEU A 58  ? 0.2252 0.2234 0.2945 0.0040  -0.0047 0.0023  61  LEU A N   
899  C CA  . LEU A 58  ? 0.2094 0.2063 0.2817 -0.0002 -0.0004 -0.0069 61  LEU A CA  
900  C C   . LEU A 58  ? 0.2860 0.2941 0.3499 -0.0035 -0.0017 -0.0127 61  LEU A C   
901  O O   . LEU A 58  ? 0.3176 0.3288 0.3746 -0.0057 0.0033  -0.0178 61  LEU A O   
902  C CB  . LEU A 58  ? 0.2498 0.2387 0.3382 -0.0013 -0.0026 -0.0126 61  LEU A CB  
903  C CG  . LEU A 58  ? 0.3176 0.3048 0.4140 -0.0044 0.0007  -0.0238 61  LEU A CG  
904  C CD1 . LEU A 58  ? 0.3313 0.3176 0.4296 -0.0044 0.0086  -0.0268 61  LEU A CD1 
905  C CD2 . LEU A 58  ? 0.3668 0.3440 0.4770 -0.0030 -0.0038 -0.0274 61  LEU A CD2 
917  N N   . LEU A 59  ? 0.2566 0.2725 0.3217 -0.0045 -0.0078 -0.0137 62  LEU A N   
918  C CA  . LEU A 59  ? 0.2479 0.2771 0.3089 -0.0084 -0.0094 -0.0227 62  LEU A CA  
919  C C   . LEU A 59  ? 0.2889 0.3311 0.3320 -0.0040 -0.0120 -0.0188 62  LEU A C   
920  O O   . LEU A 59  ? 0.3293 0.3858 0.3668 -0.0061 -0.0143 -0.0272 62  LEU A O   
921  C CB  . LEU A 59  ? 0.2853 0.3180 0.3573 -0.0125 -0.0135 -0.0273 62  LEU A CB  
922  C CG  . LEU A 59  ? 0.2813 0.2980 0.3670 -0.0160 -0.0115 -0.0300 62  LEU A CG  
923  C CD1 . LEU A 59  ? 0.3109 0.3285 0.4045 -0.0217 -0.0129 -0.0338 62  LEU A CD1 
924  C CD2 . LEU A 59  ? 0.3437 0.3554 0.4346 -0.0187 -0.0074 -0.0396 62  LEU A CD2 
936  N N   . GLY A 60  ? 0.3604 0.3402 0.3014 -0.0202 0.0113  -0.0836 63  GLY A N   
937  C CA  . GLY A 60  ? 0.3992 0.3807 0.3094 -0.0172 0.0065  -0.0806 63  GLY A CA  
938  C C   . GLY A 60  ? 0.3987 0.3910 0.3098 -0.0161 -0.0092 -0.0766 63  GLY A C   
939  O O   . GLY A 60  ? 0.4314 0.4255 0.3175 -0.0119 -0.0157 -0.0730 63  GLY A O   
943  N N   . TYR A 61  ? 0.3227 0.3217 0.2612 -0.0194 -0.0153 -0.0772 64  TYR A N   
944  C CA  . TYR A 61  ? 0.3433 0.3543 0.2867 -0.0190 -0.0290 -0.0753 64  TYR A CA  
945  C C   . TYR A 61  ? 0.3610 0.3748 0.3020 -0.0136 -0.0307 -0.0604 64  TYR A C   
946  O O   . TYR A 61  ? 0.3847 0.4068 0.3170 -0.0100 -0.0414 -0.0579 64  TYR A O   
947  C CB  . TYR A 61  ? 0.3353 0.3505 0.3092 -0.0251 -0.0313 -0.0799 64  TYR A CB  
948  C CG  . TYR A 61  ? 0.3282 0.3576 0.3125 -0.0261 -0.0437 -0.0807 64  TYR A CG  
949  C CD1 . TYR A 61  ? 0.3675 0.4055 0.3504 -0.0290 -0.0536 -0.0940 64  TYR A CD1 
950  C CD2 . TYR A 61  ? 0.3865 0.4214 0.3838 -0.0242 -0.0451 -0.0695 64  TYR A CD2 
951  C CE1 . TYR A 61  ? 0.4928 0.5462 0.4900 -0.0300 -0.0651 -0.0963 64  TYR A CE1 
952  C CE2 . TYR A 61  ? 0.3877 0.4369 0.3976 -0.0250 -0.0551 -0.0712 64  TYR A CE2 
953  C CZ  . TYR A 61  ? 0.3922 0.4511 0.4034 -0.0279 -0.0650 -0.0845 64  TYR A CZ  
954  O OH  . TYR A 61  ? 0.4700 0.5455 0.4989 -0.0289 -0.0750 -0.0878 64  TYR A OH  
964  N N   . GLY A 62  ? 0.3030 0.3104 0.2522 -0.0126 -0.0210 -0.0517 65  GLY A N   
965  C CA  . GLY A 62  ? 0.3338 0.3436 0.2864 -0.0085 -0.0222 -0.0390 65  GLY A CA  
966  C C   . GLY A 62  ? 0.3694 0.3717 0.2975 -0.0033 -0.0173 -0.0313 65  GLY A C   
967  O O   . GLY A 62  ? 0.3350 0.3342 0.2680 -0.0009 -0.0126 -0.0215 65  GLY A O   
971  N N   . LEU A 63  ? 0.3844 0.3823 0.2860 -0.0019 -0.0176 -0.0361 66  LEU A N   
972  C CA  . LEU A 63  ? 0.3662 0.3530 0.2385 0.0029  -0.0110 -0.0284 66  LEU A CA  
973  C C   . LEU A 63  ? 0.4328 0.4224 0.2790 0.0086  -0.0243 -0.0275 66  LEU A C   
974  O O   . LEU A 63  ? 0.4730 0.4701 0.3143 0.0075  -0.0347 -0.0386 66  LEU A O   
975  C CB  . LEU A 63  ? 0.4192 0.3952 0.2789 -0.0001 0.0036  -0.0349 66  LEU A CB  
976  C CG  . LEU A 63  ? 0.4608 0.4224 0.2868 0.0033  0.0145  -0.0287 66  LEU A CG  
977  C CD1 . LEU A 63  ? 0.4856 0.4402 0.3179 0.0049  0.0242  -0.0157 66  LEU A CD1 
978  C CD2 . LEU A 63  ? 0.5297 0.4836 0.3469 -0.0006 0.0285  -0.0391 66  LEU A CD2 
990  N N   . THR A 64  ? 0.3889 0.3719 0.2180 0.0154  -0.0247 -0.0147 67  THR A N   
991  C CA  . THR A 64  ? 0.4615 0.4435 0.2592 0.0233  -0.0371 -0.0123 67  THR A CA  
992  C C   . THR A 64  ? 0.4574 0.4194 0.2216 0.0286  -0.0257 0.0001  67  THR A C   
993  O O   . THR A 64  ? 0.4891 0.4408 0.2613 0.0257  -0.0094 0.0071  67  THR A O   
994  C CB  . THR A 64  ? 0.4758 0.4721 0.2903 0.0284  -0.0540 -0.0086 67  THR A CB  
995  O OG1 . THR A 64  ? 0.5286 0.5280 0.3168 0.0363  -0.0700 -0.0100 67  THR A OG1 
996  C CG2 . THR A 64  ? 0.4990 0.4891 0.3231 0.0320  -0.0480 0.0061  67  THR A CG2 
1004 N N   . MET A 65  ? 0.5031 0.4589 0.2289 0.0362  -0.0344 0.0023  68  MET A N   
1005 C CA  . MET A 65  ? 0.5687 0.5020 0.2558 0.0425  -0.0240 0.0160  68  MET A CA  
1006 C C   . MET A 65  ? 0.7371 0.6688 0.4181 0.0531  -0.0365 0.0296  68  MET A C   
1007 O O   . MET A 65  ? 0.6895 0.6346 0.3692 0.0595  -0.0579 0.0259  68  MET A O   
1008 C CB  . MET A 65  ? 0.6672 0.5902 0.3080 0.0453  -0.0240 0.0106  68  MET A CB  
1009 C CG  . MET A 65  ? 0.8596 0.7833 0.5044 0.0357  -0.0114 -0.0044 68  MET A CG  
1010 S SD  . MET A 65  ? 0.8240 0.7359 0.4906 0.0268  0.0184  -0.0002 68  MET A SD  
1011 C CE  . MET A 65  ? 0.8888 0.7717 0.5018 0.0315  0.0367  0.0125  68  MET A CE  
1021 N N   . VAL A 66  ? 0.6102 0.5257 0.2898 0.0548  -0.0231 0.0442  69  VAL A N   
1022 C CA  . VAL A 66  ? 0.5991 0.5092 0.2741 0.0652  -0.0320 0.0583  69  VAL A CA  
1023 C C   . VAL A 66  ? 0.6709 0.5515 0.2990 0.0718  -0.0203 0.0730  69  VAL A C   
1024 O O   . VAL A 66  ? 0.6812 0.5450 0.3047 0.0653  0.0030  0.0773  69  VAL A O   
1025 C CB  . VAL A 66  ? 0.5485 0.4638 0.2657 0.0615  -0.0262 0.0627  69  VAL A CB  
1026 C CG1 . VAL A 66  ? 0.6466 0.5541 0.3581 0.0730  -0.0345 0.0768  69  VAL A CG1 
1027 C CG2 . VAL A 66  ? 0.5142 0.4558 0.2738 0.0550  -0.0358 0.0493  69  VAL A CG2 
1037 N N   . PRO A 67  ? 0.6501 0.5226 0.2425 0.0850  -0.0351 0.0814  70  PRO A N   
1038 C CA  . PRO A 67  ? 0.7116 0.5518 0.2556 0.0921  -0.0228 0.0981  70  PRO A CA  
1039 C C   . PRO A 67  ? 0.8992 0.7241 0.4558 0.0961  -0.0148 0.1148  70  PRO A C   
1040 O O   . PRO A 67  ? 0.8750 0.7109 0.4529 0.1035  -0.0312 0.1178  70  PRO A O   
1041 C CB  . PRO A 67  ? 0.8065 0.6463 0.3082 0.1061  -0.0461 0.0992  70  PRO A CB  
1042 C CG  . PRO A 67  ? 0.7665 0.6377 0.3070 0.1093  -0.0719 0.0891  70  PRO A CG  
1043 C CD  . PRO A 67  ? 0.7181 0.6105 0.3106 0.0941  -0.0640 0.0749  70  PRO A CD  
1051 N N   . PHE A 68  ? 0.8467 0.6469 0.3932 0.0904  0.0118  0.1241  71  PHE A N   
1052 C CA  . PHE A 68  ? 0.8588 0.6368 0.4068 0.0948  0.0223  0.1414  71  PHE A CA  
1053 C C   . PHE A 68  ? 0.8956 0.6453 0.4219 0.0874  0.0526  0.1489  71  PHE A C   
1054 O O   . PHE A 68  ? 0.9005 0.6521 0.4278 0.0767  0.0684  0.1393  71  PHE A O   
1055 C CB  . PHE A 68  ? 0.8515 0.6462 0.4570 0.0893  0.0214  0.1373  71  PHE A CB  
1056 C CG  . PHE A 68  ? 0.6819 0.4905 0.3266 0.0733  0.0365  0.1238  71  PHE A CG  
1057 C CD1 . PHE A 68  ? 0.8196 0.6102 0.4692 0.0644  0.0632  0.1276  71  PHE A CD1 
1058 C CD2 . PHE A 68  ? 0.6050 0.4437 0.2819 0.0678  0.0239  0.1076  71  PHE A CD2 
1059 C CE1 . PHE A 68  ? 0.7270 0.5318 0.4146 0.0512  0.0747  0.1146  71  PHE A CE1 
1060 C CE2 . PHE A 68  ? 0.6608 0.5111 0.3722 0.0550  0.0360  0.0961  71  PHE A CE2 
1061 C CZ  . PHE A 68  ? 0.6248 0.4588 0.3417 0.0472  0.0605  0.0994  71  PHE A CZ  
1071 N N   . GLY A 69  ? 0.9853 0.7137 0.5021 0.0915  0.0598  0.1629  72  GLY A N   
1072 C CA  . GLY A 69  ? 1.0227 0.7268 0.5228 0.0843  0.0870  0.1685  72  GLY A CA  
1073 C C   . GLY A 69  ? 1.1421 0.8417 0.6006 0.0844  0.0890  0.1647  72  GLY A C   
1074 O O   . GLY A 69  ? 1.1823 0.8701 0.6334 0.0749  0.1135  0.1624  72  GLY A O   
1078 N N   . GLY A 70  ? 0.9981 0.7084 0.4320 0.0947  0.0637  0.1624  73  GLY A N   
1079 C CA  . GLY A 70  ? 1.0445 0.7509 0.4374 0.0958  0.0635  0.1582  73  GLY A CA  
1080 C C   . GLY A 70  ? 1.1473 0.8667 0.5418 0.0859  0.0714  0.1413  73  GLY A C   
1081 O O   . GLY A 70  ? 1.1175 0.8310 0.4794 0.0846  0.0772  0.1370  73  GLY A O   
1085 N N   . GLU A 71  ? 0.9796 0.7157 0.4105 0.0791  0.0722  0.1314  74  GLU A N   
1086 C CA  . GLU A 71  ? 0.9838 0.7326 0.4200 0.0699  0.0792  0.1144  74  GLU A CA  
1087 C C   . GLU A 71  ? 0.8090 0.5853 0.2689 0.0722  0.0546  0.1024  74  GLU A C   
1088 O O   . GLU A 71  ? 0.8877 0.6750 0.3732 0.0776  0.0379  0.1069  74  GLU A O   
1089 C CB  . GLU A 71  ? 1.0455 0.7872 0.5092 0.0566  0.1098  0.1122  74  GLU A CB  
1092 N N   . GLN A 72  ? 0.9013 0.6948 0.3676 0.0656  0.0517  0.0838  75  GLN A N   
1093 C CA  . GLN A 72  ? 0.8807 0.7070 0.3933 0.0614  0.0328  0.0678  75  GLN A CA  
1094 C C   . GLN A 72  ? 0.8289 0.6646 0.3922 0.0484  0.0500  0.0606  75  GLN A C   
1095 O O   . GLN A 72  ? 0.8605 0.6923 0.4239 0.0401  0.0687  0.0523  75  GLN A O   
1096 C CB  . GLN A 72  ? 0.9233 0.7623 0.4170 0.0618  0.0189  0.0511  75  GLN A CB  
1097 C CG  . GLN A 72  ? 1.2728 1.0993 0.7069 0.0747  0.0046  0.0565  75  GLN A CG  
1098 C CD  . GLN A 72  ? 1.3778 1.2235 0.8210 0.0848  -0.0280 0.0552  75  GLN A CD  
1099 O OE1 . GLN A 72  ? 1.3807 1.2536 0.8606 0.0804  -0.0434 0.0396  75  GLN A OE1 
1100 N NE2 . GLN A 72  ? 1.2721 1.1091 0.6986 0.0952  -0.0373 0.0702  75  GLN A NE2 
1109 N N   . ASN A 73  ? 0.6341 0.4818 0.2393 0.0473  0.0437  0.0634  76  ASN A N   
1110 C CA  . ASN A 73  ? 0.5784 0.4333 0.2297 0.0367  0.0584  0.0584  76  ASN A CA  
1111 C C   . ASN A 73  ? 0.6057 0.4875 0.2958 0.0316  0.0450  0.0430  76  ASN A C   
1112 O O   . ASN A 73  ? 0.5509 0.4477 0.2521 0.0360  0.0243  0.0415  76  ASN A O   
1113 C CB  . ASN A 73  ? 0.5650 0.4135 0.2368 0.0386  0.0618  0.0713  76  ASN A CB  
1114 C CG  . ASN A 73  ? 0.6751 0.4933 0.3087 0.0438  0.0761  0.0884  76  ASN A CG  
1115 O OD1 . ASN A 73  ? 0.8329 0.6350 0.4635 0.0373  0.1006  0.0911  76  ASN A OD1 
1116 N ND2 . ASN A 73  ? 0.7242 0.5340 0.3287 0.0560  0.0608  0.0998  76  ASN A ND2 
1123 N N   . PRO A 74  ? 0.5683 0.4563 0.2810 0.0226  0.0569  0.0314  77  PRO A N   
1124 C CA  . PRO A 74  ? 0.5139 0.4241 0.2637 0.0180  0.0455  0.0185  77  PRO A CA  
1125 C C   . PRO A 74  ? 0.5265 0.4465 0.3153 0.0169  0.0410  0.0226  77  PRO A C   
1126 O O   . PRO A 74  ? 0.5350 0.4494 0.3419 0.0135  0.0547  0.0266  77  PRO A O   
1127 C CB  . PRO A 74  ? 0.6269 0.5363 0.3867 0.0102  0.0618  0.0069  77  PRO A CB  
1128 C CG  . PRO A 74  ? 0.6615 0.5514 0.4032 0.0089  0.0846  0.0141  77  PRO A CG  
1129 C CD  . PRO A 74  ? 0.6241 0.4979 0.3273 0.0167  0.0819  0.0293  77  PRO A CD  
1137 N N   . ILE A 75  ? 0.4126 0.3480 0.2158 0.0195  0.0220  0.0204  78  ILE A N   
1138 C CA  . ILE A 75  ? 0.3798 0.3250 0.2167 0.0189  0.0169  0.0233  78  ILE A CA  
1139 C C   . ILE A 75  ? 0.3899 0.3522 0.2541 0.0141  0.0084  0.0118  78  ILE A C   
1140 O O   . ILE A 75  ? 0.3789 0.3507 0.2384 0.0152  -0.0047 0.0055  78  ILE A O   
1141 C CB  . ILE A 75  ? 0.4583 0.4044 0.2878 0.0272  0.0038  0.0331  78  ILE A CB  
1142 C CG1 . ILE A 75  ? 0.4722 0.3974 0.2741 0.0326  0.0131  0.0465  78  ILE A CG1 
1143 C CG2 . ILE A 75  ? 0.4445 0.4028 0.3096 0.0261  -0.0017 0.0335  78  ILE A CG2 
1144 C CD1 . ILE A 75  ? 0.5426 0.4571 0.3617 0.0280  0.0313  0.0517  78  ILE A CD1 
1156 N N   . TYR A 76  ? 0.3338 0.2989 0.2257 0.0090  0.0162  0.0085  79  TYR A N   
1157 C CA  . TYR A 76  ? 0.3069 0.2848 0.2246 0.0051  0.0094  0.0000  79  TYR A CA  
1158 C C   . TYR A 76  ? 0.3152 0.3027 0.2487 0.0074  -0.0018 0.0044  79  TYR A C   
1159 O O   . TYR A 76  ? 0.3383 0.3265 0.2896 0.0072  0.0012  0.0084  79  TYR A O   
1160 C CB  . TYR A 76  ? 0.3099 0.2862 0.2490 0.0007  0.0205  -0.0043 79  TYR A CB  
1161 C CG  . TYR A 76  ? 0.3046 0.2753 0.2348 -0.0023 0.0303  -0.0127 79  TYR A CG  
1162 C CD1 . TYR A 76  ? 0.3183 0.2936 0.2504 -0.0045 0.0251  -0.0228 79  TYR A CD1 
1163 C CD2 . TYR A 76  ? 0.4076 0.3679 0.3289 -0.0031 0.0458  -0.0112 79  TYR A CD2 
1164 C CE1 . TYR A 76  ? 0.3144 0.2844 0.2400 -0.0070 0.0348  -0.0318 79  TYR A CE1 
1165 C CE2 . TYR A 76  ? 0.3537 0.3093 0.2680 -0.0058 0.0565  -0.0199 79  TYR A CE2 
1166 C CZ  . TYR A 76  ? 0.3702 0.3309 0.2863 -0.0074 0.0502  -0.0306 79  TYR A CZ  
1167 O OH  . TYR A 76  ? 0.4081 0.3638 0.3173 -0.0097 0.0613  -0.0404 79  TYR A OH  
1177 N N   . TRP A 77  ? 0.3104 0.3067 0.2390 0.0094  -0.0146 0.0022  80  TRP A N   
1178 C CA  . TRP A 77  ? 0.2871 0.2934 0.2320 0.0115  -0.0237 0.0054  80  TRP A CA  
1179 C C   . TRP A 77  ? 0.2708 0.2845 0.2415 0.0063  -0.0237 0.0005  80  TRP A C   
1180 O O   . TRP A 77  ? 0.2637 0.2832 0.2494 0.0072  -0.0265 0.0037  80  TRP A O   
1181 C CB  . TRP A 77  ? 0.2898 0.3056 0.2260 0.0155  -0.0379 0.0033  80  TRP A CB  
1182 C CG  . TRP A 77  ? 0.3040 0.3268 0.2400 0.0111  -0.0435 -0.0086 80  TRP A CG  
1183 C CD1 . TRP A 77  ? 0.3609 0.3796 0.2737 0.0115  -0.0451 -0.0144 80  TRP A CD1 
1184 C CD2 . TRP A 77  ? 0.3171 0.3506 0.2773 0.0051  -0.0471 -0.0168 80  TRP A CD2 
1185 N NE1 . TRP A 77  ? 0.4452 0.4725 0.3683 0.0060  -0.0504 -0.0269 80  TRP A NE1 
1186 C CE2 . TRP A 77  ? 0.3493 0.3850 0.3022 0.0018  -0.0510 -0.0280 80  TRP A CE2 
1187 C CE3 . TRP A 77  ? 0.3529 0.3929 0.3386 0.0021  -0.0463 -0.0157 80  TRP A CE3 
1188 C CZ2 . TRP A 77  ? 0.3935 0.4368 0.3665 -0.0049 -0.0537 -0.0378 80  TRP A CZ2 
1189 C CZ3 . TRP A 77  ? 0.3675 0.4141 0.3704 -0.0043 -0.0482 -0.0242 80  TRP A CZ3 
1190 C CH2 . TRP A 77  ? 0.3687 0.4168 0.3664 -0.0079 -0.0518 -0.0352 80  TRP A CH2 
1201 N N   . ALA A 78  ? 0.2574 0.2693 0.2324 0.0014  -0.0198 -0.0072 81  ALA A N   
1202 C CA  . ALA A 78  ? 0.2463 0.2622 0.2426 -0.0026 -0.0201 -0.0104 81  ALA A CA  
1203 C C   . ALA A 78  ? 0.2362 0.2494 0.2451 -0.0016 -0.0152 -0.0047 81  ALA A C   
1204 O O   . ALA A 78  ? 0.2570 0.2734 0.2797 -0.0031 -0.0170 -0.0046 81  ALA A O   
1205 C CB  . ALA A 78  ? 0.3190 0.3308 0.3176 -0.0069 -0.0163 -0.0189 81  ALA A CB  
1211 N N   . ARG A 79  ? 0.2479 0.2547 0.2517 0.0007  -0.0086 -0.0006 82  ARG A N   
1212 C CA  . ARG A 79  ? 0.2421 0.2477 0.2591 0.0016  -0.0055 0.0028  82  ARG A CA  
1213 C C   . ARG A 79  ? 0.2501 0.2617 0.2730 0.0036  -0.0113 0.0071  82  ARG A C   
1214 O O   . ARG A 79  ? 0.2406 0.2537 0.2751 0.0033  -0.0117 0.0072  82  ARG A O   
1215 C CB  . ARG A 79  ? 0.3090 0.3071 0.3211 0.0030  0.0030  0.0062  82  ARG A CB  
1216 C CG  . ARG A 79  ? 0.3059 0.2985 0.3155 0.0007  0.0115  0.0015  82  ARG A CG  
1217 C CD  . ARG A 79  ? 0.3407 0.3264 0.3534 0.0006  0.0223  0.0040  82  ARG A CD  
1218 N NE  . ARG A 79  ? 0.3201 0.3002 0.3285 -0.0019 0.0332  -0.0006 82  ARG A NE  
1219 C CZ  . ARG A 79  ? 0.3147 0.2975 0.3388 -0.0039 0.0362  -0.0085 82  ARG A CZ  
1220 N NH1 . ARG A 79  ? 0.3578 0.3473 0.4006 -0.0031 0.0287  -0.0115 82  ARG A NH1 
1221 N NH2 . ARG A 79  ? 0.4003 0.3783 0.4208 -0.0060 0.0476  -0.0133 82  ARG A NH2 
1235 N N   . TYR A 80  ? 0.2534 0.2681 0.2677 0.0065  -0.0158 0.0104  83  TYR A N   
1236 C CA  . TYR A 80  ? 0.1974 0.2183 0.2198 0.0091  -0.0202 0.0138  83  TYR A CA  
1237 C C   . TYR A 80  ? 0.2314 0.2611 0.2645 0.0062  -0.0245 0.0100  83  TYR A C   
1238 O O   . TYR A 80  ? 0.2480 0.2813 0.2908 0.0067  -0.0245 0.0114  83  TYR A O   
1239 C CB  . TYR A 80  ? 0.2198 0.2414 0.2315 0.0146  -0.0247 0.0184  83  TYR A CB  
1240 C CG  . TYR A 80  ? 0.2612 0.2701 0.2597 0.0168  -0.0177 0.0235  83  TYR A CG  
1241 C CD1 . TYR A 80  ? 0.2861 0.2885 0.2903 0.0188  -0.0122 0.0281  83  TYR A CD1 
1242 C CD2 . TYR A 80  ? 0.2990 0.3013 0.2801 0.0162  -0.0149 0.0227  83  TYR A CD2 
1243 C CE1 . TYR A 80  ? 0.3169 0.3062 0.3111 0.0194  -0.0035 0.0324  83  TYR A CE1 
1244 C CE2 . TYR A 80  ? 0.2887 0.2777 0.2569 0.0173  -0.0056 0.0275  83  TYR A CE2 
1245 C CZ  . TYR A 80  ? 0.3302 0.3128 0.3066 0.0185  0.0005  0.0326  83  TYR A CZ  
1246 O OH  . TYR A 80  ? 0.3412 0.3094 0.3074 0.0184  0.0118  0.0371  83  TYR A OH  
1256 N N   . ALA A 81  ? 0.2071 0.2394 0.2386 0.0027  -0.0271 0.0046  84  ALA A N   
1257 C CA  . ALA A 81  ? 0.2038 0.2420 0.2476 -0.0016 -0.0286 0.0009  84  ALA A CA  
1258 C C   . ALA A 81  ? 0.2726 0.3038 0.3222 -0.0036 -0.0232 0.0019  84  ALA A C   
1259 O O   . ALA A 81  ? 0.2751 0.3083 0.3323 -0.0051 -0.0222 0.0029  84  ALA A O   
1260 C CB  . ALA A 81  ? 0.2234 0.2642 0.2655 -0.0055 -0.0319 -0.0065 84  ALA A CB  
1266 N N   . ASP A 82  ? 0.2122 0.2350 0.2579 -0.0033 -0.0198 0.0014  85  ASP A N   
1267 C CA  . ASP A 82  ? 0.2130 0.2296 0.2636 -0.0029 -0.0171 0.0026  85  ASP A CA  
1268 C C   . ASP A 82  ? 0.2130 0.2312 0.2656 0.0002  -0.0172 0.0067  85  ASP A C   
1269 O O   . ASP A 82  ? 0.2311 0.2488 0.2860 0.0000  -0.0171 0.0083  85  ASP A O   
1270 C CB  . ASP A 82  ? 0.2090 0.2196 0.2583 -0.0021 -0.0141 0.0000  85  ASP A CB  
1271 C CG  . ASP A 82  ? 0.2282 0.2338 0.2844 0.0003  -0.0134 0.0002  85  ASP A CG  
1272 O OD1 . ASP A 82  ? 0.2516 0.2575 0.3095 0.0022  -0.0154 0.0031  85  ASP A OD1 
1273 O OD2 . ASP A 82  ? 0.2418 0.2439 0.3014 0.0006  -0.0110 -0.0035 85  ASP A OD2 
1278 N N   . TRP A 83  ? 0.1991 0.2179 0.2497 0.0030  -0.0163 0.0083  86  TRP A N   
1279 C CA  . TRP A 83  ? 0.2117 0.2305 0.2657 0.0058  -0.0158 0.0104  86  TRP A CA  
1280 C C   . TRP A 83  ? 0.2303 0.2549 0.2862 0.0065  -0.0172 0.0122  86  TRP A C   
1281 O O   . TRP A 83  ? 0.2332 0.2573 0.2909 0.0080  -0.0165 0.0126  86  TRP A O   
1282 C CB  . TRP A 83  ? 0.2009 0.2172 0.2537 0.0079  -0.0131 0.0118  86  TRP A CB  
1283 C CG  . TRP A 83  ? 0.1972 0.2083 0.2511 0.0067  -0.0090 0.0092  86  TRP A CG  
1284 C CD1 . TRP A 83  ? 0.2237 0.2332 0.2823 0.0055  -0.0089 0.0053  86  TRP A CD1 
1285 C CD2 . TRP A 83  ? 0.2042 0.2103 0.2550 0.0070  -0.0031 0.0105  86  TRP A CD2 
1286 N NE1 . TRP A 83  ? 0.2241 0.2302 0.2858 0.0047  -0.0033 0.0026  86  TRP A NE1 
1287 C CE2 . TRP A 83  ? 0.2171 0.2206 0.2729 0.0050  0.0012  0.0060  86  TRP A CE2 
1288 C CE3 . TRP A 83  ? 0.2610 0.2633 0.3044 0.0090  -0.0006 0.0154  86  TRP A CE3 
1289 C CZ2 . TRP A 83  ? 0.2519 0.2497 0.3070 0.0038  0.0100  0.0056  86  TRP A CZ2 
1290 C CZ3 . TRP A 83  ? 0.2713 0.2654 0.3107 0.0082  0.0077  0.0166  86  TRP A CZ3 
1291 C CH2 . TRP A 83  ? 0.2641 0.2564 0.3097 0.0050  0.0138  0.0114  86  TRP A CH2 
1302 N N   . LEU A 84  ? 0.2119 0.2430 0.2682 0.0056  -0.0193 0.0123  87  LEU A N   
1303 C CA  . LEU A 84  ? 0.2037 0.2424 0.2664 0.0060  -0.0197 0.0126  87  LEU A CA  
1304 C C   . LEU A 84  ? 0.2180 0.2549 0.2825 0.0031  -0.0164 0.0121  87  LEU A C   
1305 O O   . LEU A 84  ? 0.2591 0.2987 0.3265 0.0042  -0.0137 0.0126  87  LEU A O   
1306 C CB  . LEU A 84  ? 0.2245 0.2723 0.2910 0.0050  -0.0239 0.0106  87  LEU A CB  
1307 C CG  . LEU A 84  ? 0.3807 0.4396 0.4594 0.0051  -0.0241 0.0092  87  LEU A CG  
1308 C CD1 . LEU A 84  ? 0.4168 0.4775 0.4980 0.0112  -0.0243 0.0119  87  LEU A CD1 
1309 C CD2 . LEU A 84  ? 0.4744 0.5442 0.5601 0.0034  -0.0300 0.0047  87  LEU A CD2 
1321 N N   . PHE A 85  ? 0.2296 0.2604 0.2912 -0.0002 -0.0156 0.0113  88  PHE A N   
1322 C CA  . PHE A 85  ? 0.2370 0.2622 0.2966 -0.0024 -0.0117 0.0126  88  PHE A CA  
1323 C C   . PHE A 85  ? 0.2610 0.2764 0.3122 0.0010  -0.0124 0.0143  88  PHE A C   
1324 O O   . PHE A 85  ? 0.2899 0.3007 0.3347 0.0020  -0.0101 0.0163  88  PHE A O   
1325 C CB  . PHE A 85  ? 0.2727 0.2951 0.3351 -0.0078 -0.0102 0.0110  88  PHE A CB  
1326 C CG  . PHE A 85  ? 0.2753 0.3093 0.3489 -0.0116 -0.0104 0.0074  88  PHE A CG  
1327 C CD1 . PHE A 85  ? 0.3581 0.3981 0.4396 -0.0139 -0.0056 0.0073  88  PHE A CD1 
1328 C CD2 . PHE A 85  ? 0.3037 0.3431 0.3799 -0.0124 -0.0154 0.0033  88  PHE A CD2 
1329 C CE1 . PHE A 85  ? 0.4565 0.5101 0.5532 -0.0172 -0.0069 0.0022  88  PHE A CE1 
1330 C CE2 . PHE A 85  ? 0.3822 0.4342 0.4697 -0.0151 -0.0182 -0.0015 88  PHE A CE2 
1331 C CZ  . PHE A 85  ? 0.3864 0.4463 0.4862 -0.0174 -0.0143 -0.0023 88  PHE A CZ  
1341 N N   . THR A 86  ? 0.2165 0.2290 0.2676 0.0030  -0.0155 0.0129  89  THR A N   
1342 C CA  . THR A 86  ? 0.2101 0.2152 0.2569 0.0066  -0.0178 0.0130  89  THR A CA  
1343 C C   . THR A 86  ? 0.2610 0.2687 0.3075 0.0104  -0.0194 0.0117  89  THR A C   
1344 O O   . THR A 86  ? 0.2628 0.2657 0.3032 0.0137  -0.0222 0.0114  89  THR A O   
1345 C CB  . THR A 86  ? 0.2232 0.2252 0.2744 0.0073  -0.0198 0.0103  89  THR A CB  
1346 O OG1 . THR A 86  ? 0.2193 0.2267 0.2759 0.0069  -0.0188 0.0079  89  THR A OG1 
1347 C CG2 . THR A 86  ? 0.2303 0.2275 0.2816 0.0040  -0.0183 0.0102  89  THR A CG2 
1355 N N   . THR A 87  ? 0.2398 0.2536 0.2918 0.0104  -0.0182 0.0107  90  THR A N   
1356 C CA  . THR A 87  ? 0.2221 0.2367 0.2759 0.0135  -0.0191 0.0082  90  THR A CA  
1357 C C   . THR A 87  ? 0.2500 0.2649 0.2970 0.0147  -0.0176 0.0087  90  THR A C   
1358 O O   . THR A 87  ? 0.2441 0.2564 0.2867 0.0176  -0.0201 0.0057  90  THR A O   
1359 C CB  . THR A 87  ? 0.2163 0.2336 0.2775 0.0137  -0.0171 0.0075  90  THR A CB  
1360 O OG1 . THR A 87  ? 0.2385 0.2599 0.2997 0.0130  -0.0153 0.0108  90  THR A OG1 
1361 C CG2 . THR A 87  ? 0.2355 0.2505 0.3013 0.0126  -0.0165 0.0062  90  THR A CG2 
1369 N N   . PRO A 88  ? 0.2354 0.2535 0.2815 0.0125  -0.0136 0.0112  91  PRO A N   
1370 C CA  . PRO A 88  ? 0.2679 0.2852 0.3068 0.0133  -0.0099 0.0111  91  PRO A CA  
1371 C C   . PRO A 88  ? 0.2830 0.2907 0.3069 0.0139  -0.0103 0.0132  91  PRO A C   
1372 O O   . PRO A 88  ? 0.3227 0.3264 0.3347 0.0166  -0.0094 0.0121  91  PRO A O   
1373 C CB  . PRO A 88  ? 0.3423 0.3670 0.3888 0.0102  -0.0047 0.0124  91  PRO A CB  
1374 C CG  . PRO A 88  ? 0.4042 0.4321 0.4580 0.0076  -0.0074 0.0135  91  PRO A CG  
1375 C CD  . PRO A 88  ? 0.2614 0.2856 0.3146 0.0096  -0.0121 0.0128  91  PRO A CD  
1383 N N   . LEU A 89  ? 0.2774 0.2797 0.2998 0.0122  -0.0118 0.0161  92  LEU A N   
1384 C CA  . LEU A 89  ? 0.2542 0.2445 0.2612 0.0144  -0.0131 0.0194  92  LEU A CA  
1385 C C   . LEU A 89  ? 0.2990 0.2866 0.3002 0.0206  -0.0216 0.0161  92  LEU A C   
1386 O O   . LEU A 89  ? 0.3402 0.3197 0.3239 0.0248  -0.0239 0.0173  92  LEU A O   
1387 C CB  . LEU A 89  ? 0.2867 0.2711 0.2967 0.0118  -0.0133 0.0223  92  LEU A CB  
1388 C CG  . LEU A 89  ? 0.3026 0.2869 0.3162 0.0051  -0.0048 0.0250  92  LEU A CG  
1389 C CD1 . LEU A 89  ? 0.3107 0.2887 0.3290 0.0025  -0.0054 0.0259  92  LEU A CD1 
1390 C CD2 . LEU A 89  ? 0.3593 0.3343 0.3577 0.0044  0.0029  0.0296  92  LEU A CD2 
1402 N N   . LEU A 90  ? 0.2663 0.2605 0.2818 0.0215  -0.0266 0.0112  93  LEU A N   
1403 C CA  . LEU A 90  ? 0.2348 0.2289 0.2501 0.0269  -0.0350 0.0058  93  LEU A CA  
1404 C C   . LEU A 90  ? 0.2472 0.2436 0.2560 0.0289  -0.0351 0.0015  93  LEU A C   
1405 O O   . LEU A 90  ? 0.3074 0.3006 0.3056 0.0341  -0.0422 -0.0020 93  LEU A O   
1406 C CB  . LEU A 90  ? 0.2514 0.2524 0.2868 0.0260  -0.0372 0.0008  93  LEU A CB  
1407 C CG  . LEU A 90  ? 0.2865 0.2846 0.3278 0.0254  -0.0382 0.0026  93  LEU A CG  
1408 C CD1 . LEU A 90  ? 0.2736 0.2783 0.3329 0.0225  -0.0354 -0.0014 93  LEU A CD1 
1409 C CD2 . LEU A 90  ? 0.2894 0.2823 0.3266 0.0318  -0.0472 0.0013  93  LEU A CD2 
1421 N N   . LEU A 91  ? 0.2729 0.2748 0.2880 0.0257  -0.0281 0.0009  94  LEU A N   
1422 C CA  . LEU A 91  ? 0.2650 0.2683 0.2747 0.0275  -0.0268 -0.0039 94  LEU A CA  
1423 C C   . LEU A 91  ? 0.2938 0.2897 0.2800 0.0292  -0.0237 -0.0008 94  LEU A C   
1424 O O   . LEU A 91  ? 0.3302 0.3236 0.3036 0.0329  -0.0263 -0.0058 94  LEU A O   
1425 C CB  . LEU A 91  ? 0.2534 0.2633 0.2762 0.0247  -0.0195 -0.0044 94  LEU A CB  
1426 C CG  . LEU A 91  ? 0.2926 0.3064 0.3339 0.0238  -0.0211 -0.0071 94  LEU A CG  
1427 C CD1 . LEU A 91  ? 0.3304 0.3482 0.3815 0.0228  -0.0148 -0.0055 94  LEU A CD1 
1428 C CD2 . LEU A 91  ? 0.3181 0.3317 0.3644 0.0261  -0.0263 -0.0157 94  LEU A CD2 
1440 N N   A LEU A 92  ? 0.3014 0.2925 0.2809 0.0263  -0.0177 0.0069  95  LEU A N   
1441 N N   B LEU A 92  ? 0.3028 0.2940 0.2824 0.0263  -0.0175 0.0069  95  LEU A N   
1442 C CA  A LEU A 92  ? 0.3524 0.3335 0.3083 0.0272  -0.0122 0.0112  95  LEU A CA  
1443 C CA  B LEU A 92  ? 0.3539 0.3350 0.3094 0.0273  -0.0123 0.0111  95  LEU A CA  
1444 C C   A LEU A 92  ? 0.3738 0.3438 0.3083 0.0338  -0.0217 0.0122  95  LEU A C   
1445 C C   B LEU A 92  ? 0.3752 0.3456 0.3100 0.0340  -0.0221 0.0117  95  LEU A C   
1446 O O   A LEU A 92  ? 0.3978 0.3598 0.3078 0.0375  -0.0208 0.0121  95  LEU A O   
1447 O O   B LEU A 92  ? 0.4024 0.3656 0.3136 0.0379  -0.0220 0.0108  95  LEU A O   
1448 C CB  A LEU A 92  ? 0.3271 0.3051 0.2852 0.0215  -0.0029 0.0187  95  LEU A CB  
1449 C CB  B LEU A 92  ? 0.3322 0.3091 0.2880 0.0219  -0.0030 0.0189  95  LEU A CB  
1450 C CG  A LEU A 92  ? 0.3270 0.2943 0.2644 0.0200  0.0080  0.0240  95  LEU A CG  
1451 C CG  B LEU A 92  ? 0.4149 0.4019 0.3866 0.0160  0.0075  0.0182  95  LEU A CG  
1452 C CD1 A LEU A 92  ? 0.4656 0.4394 0.4021 0.0192  0.0166  0.0190  95  LEU A CD1 
1453 C CD1 B LEU A 92  ? 0.5299 0.5117 0.5025 0.0103  0.0154  0.0244  95  LEU A CD1 
1454 C CD2 A LEU A 92  ? 0.3559 0.3204 0.3013 0.0133  0.0164  0.0300  95  LEU A CD2 
1455 C CD2 B LEU A 92  ? 0.4406 0.4296 0.4049 0.0169  0.0153  0.0145  95  LEU A CD2 
1478 N N   . ASP A 93  ? 0.3181 0.2872 0.2606 0.0361  -0.0310 0.0127  96  ASP A N   
1479 C CA  . ASP A 93  ? 0.3494 0.3101 0.2756 0.0441  -0.0429 0.0125  96  ASP A CA  
1480 C C   . ASP A 93  ? 0.3974 0.3632 0.3180 0.0489  -0.0508 0.0024  96  ASP A C   
1481 O O   . ASP A 93  ? 0.4320 0.3890 0.3263 0.0555  -0.0568 0.0023  96  ASP A O   
1482 C CB  . ASP A 93  ? 0.3955 0.3594 0.3406 0.0459  -0.0518 0.0112  96  ASP A CB  
1483 C CG  . ASP A 93  ? 0.3512 0.3019 0.2877 0.0471  -0.0512 0.0205  96  ASP A CG  
1484 O OD1 . ASP A 93  ? 0.3674 0.3034 0.2789 0.0485  -0.0465 0.0287  96  ASP A OD1 
1485 O OD2 . ASP A 93  ? 0.3863 0.3400 0.3410 0.0471  -0.0550 0.0194  96  ASP A OD2 
1490 N N   . LEU A 94  ? 0.3424 0.3214 0.2870 0.0460  -0.0513 -0.0065 97  LEU A N   
1491 C CA  . LEU A 94  ? 0.3460 0.3300 0.2892 0.0495  -0.0582 -0.0179 97  LEU A CA  
1492 C C   . LEU A 94  ? 0.3923 0.3717 0.3136 0.0496  -0.0504 -0.0188 97  LEU A C   
1493 O O   . LEU A 94  ? 0.4207 0.3967 0.3222 0.0552  -0.0574 -0.0253 97  LEU A O   
1494 C CB  . LEU A 94  ? 0.3279 0.3243 0.3030 0.0454  -0.0577 -0.0264 97  LEU A CB  
1495 C CG  . LEU A 94  ? 0.3694 0.3712 0.3677 0.0450  -0.0640 -0.0280 97  LEU A CG  
1496 C CD1 . LEU A 94  ? 0.4106 0.4207 0.4367 0.0393  -0.0580 -0.0329 97  LEU A CD1 
1497 C CD2 . LEU A 94  ? 0.4632 0.4667 0.4602 0.0520  -0.0795 -0.0362 97  LEU A CD2 
1509 N N   . ALA A 95  ? 0.3743 0.3545 0.2995 0.0439  -0.0362 -0.0136 98  ALA A N   
1510 C CA  . ALA A 95  ? 0.4041 0.3815 0.3129 0.0435  -0.0264 -0.0156 98  ALA A CA  
1511 C C   . ALA A 95  ? 0.4532 0.4157 0.3243 0.0474  -0.0246 -0.0094 98  ALA A C   
1512 O O   . ALA A 95  ? 0.4719 0.4298 0.3202 0.0507  -0.0231 -0.0146 98  ALA A O   
1513 C CB  . ALA A 95  ? 0.3761 0.3594 0.3020 0.0369  -0.0122 -0.0116 98  ALA A CB  
1519 N N   . LEU A 96  ? 0.4086 0.3617 0.2712 0.0472  -0.0239 0.0018  99  LEU A N   
1520 C CA  . LEU A 96  ? 0.4945 0.4295 0.3188 0.0513  -0.0211 0.0097  99  LEU A CA  
1521 C C   . LEU A 96  ? 0.5295 0.4585 0.3305 0.0615  -0.0382 0.0050  99  LEU A C   
1522 O O   . LEU A 96  ? 0.5643 0.4798 0.3276 0.0667  -0.0374 0.0071  99  LEU A O   
1523 C CB  . LEU A 96  ? 0.5476 0.4724 0.3716 0.0485  -0.0162 0.0227  99  LEU A CB  
1524 C CG  . LEU A 96  ? 0.6326 0.5619 0.4751 0.0384  0.0013  0.0271  99  LEU A CG  
1525 C CD1 . LEU A 96  ? 0.6212 0.5378 0.4612 0.0357  0.0055  0.0386  99  LEU A CD1 
1526 C CD2 . LEU A 96  ? 0.7561 0.6830 0.5844 0.0352  0.0176  0.0263  99  LEU A CD2 
1538 N N   . LEU A 97  ? 0.4649 0.4041 0.2878 0.0646  -0.0539 -0.0020 100 LEU A N   
1539 C CA  . LEU A 97  ? 0.5151 0.4521 0.3220 0.0747  -0.0728 -0.0086 100 LEU A CA  
1540 C C   . LEU A 97  ? 0.5560 0.4952 0.3455 0.0774  -0.0746 -0.0205 100 LEU A C   
1541 O O   . LEU A 97  ? 0.6227 0.5523 0.3779 0.0863  -0.0848 -0.0223 100 LEU A O   
1542 C CB  . LEU A 97  ? 0.5217 0.4730 0.3645 0.0755  -0.0864 -0.0164 100 LEU A CB  
1543 C CG  . LEU A 97  ? 0.6689 0.6207 0.5065 0.0861  -0.1080 -0.0223 100 LEU A CG  
1544 C CD1 . LEU A 97  ? 0.6309 0.5645 0.4406 0.0937  -0.1123 -0.0083 100 LEU A CD1 
1545 C CD2 . LEU A 97  ? 0.5701 0.5389 0.4519 0.0838  -0.1157 -0.0312 100 LEU A CD2 
1557 N N   . VAL A 98  ? 0.4415 0.6611 0.3208 0.0625  -0.1116 0.0318  101 VAL A N   
1558 C CA  . VAL A 98  ? 0.4257 0.6526 0.2862 0.0337  -0.1127 0.0165  101 VAL A CA  
1559 C C   . VAL A 98  ? 0.4865 0.6635 0.3244 0.0312  -0.1007 0.0145  101 VAL A C   
1560 O O   . VAL A 98  ? 0.5429 0.7091 0.3561 0.0124  -0.0968 0.0007  101 VAL A O   
1561 C CB  . VAL A 98  ? 0.4688 0.6977 0.3379 0.0062  -0.1112 -0.0029 101 VAL A CB  
1562 C CG1 . VAL A 98  ? 0.5733 0.8647 0.4682 0.0067  -0.1224 0.0020  101 VAL A CG1 
1563 C CG2 . VAL A 98  ? 0.4682 0.6416 0.3478 0.0075  -0.0962 -0.0096 101 VAL A CG2 
1573 N N   . ASP A 99  ? 0.4467 0.5920 0.2874 0.0484  -0.0938 0.0288  102 ASP A N   
1574 C CA  . ASP A 99  ? 0.4839 0.5971 0.3080 0.0455  -0.0818 0.0319  102 ASP A CA  
1575 C C   . ASP A 99  ? 0.5602 0.6520 0.3862 0.0324  -0.0686 0.0160  102 ASP A C   
1576 O O   . ASP A 99  ? 0.5282 0.6092 0.3289 0.0278  -0.0592 0.0099  102 ASP A O   
1577 C CB  . ASP A 99  ? 0.6010 0.7291 0.3939 0.0455  -0.0850 0.0362  102 ASP A CB  
1578 C CG  . ASP A 99  ? 0.8224 0.9264 0.6001 0.0490  -0.0731 0.0485  102 ASP A CG  
1579 O OD1 . ASP A 99  ? 0.8215 0.9033 0.6126 0.0524  -0.0675 0.0607  102 ASP A OD1 
1580 O OD2 . ASP A 99  ? 0.9328 1.0419 0.6824 0.0458  -0.0694 0.0466  102 ASP A OD2 
1585 N N   . ALA A 100 ? 0.4452 0.5281 0.2959 0.0304  -0.0665 0.0104  103 ALA A N   
1586 C CA  . ALA A 100 ? 0.4322 0.4923 0.2831 0.0231  -0.0532 -0.0021 103 ALA A CA  
1587 C C   . ALA A 100 ? 0.4957 0.5417 0.3420 0.0309  -0.0382 0.0084  103 ALA A C   
1588 O O   . ALA A 100 ? 0.4741 0.5242 0.3295 0.0354  -0.0390 0.0261  103 ALA A O   
1589 C CB  . ALA A 100 ? 0.4466 0.5030 0.3268 0.0219  -0.0544 -0.0056 103 ALA A CB  
1595 N N   . ASP A 101 ? 0.5185 0.5471 0.3453 0.0323  -0.0232 -0.0012 104 ASP A N   
1596 C CA  . ASP A 101 ? 0.5575 0.5870 0.3827 0.0445  -0.0062 0.0112  104 ASP A CA  
1597 C C   . ASP A 101 ? 0.4924 0.5305 0.3539 0.0462  -0.0035 0.0225  104 ASP A C   
1598 O O   . ASP A 101 ? 0.4247 0.4546 0.3048 0.0411  -0.0096 0.0149  104 ASP A O   
1599 C CB  . ASP A 101 ? 0.6376 0.6402 0.4242 0.0540  0.0122  -0.0015 104 ASP A CB  
1600 C CG  . ASP A 101 ? 0.6128 0.5842 0.3957 0.0514  0.0165  -0.0173 104 ASP A CG  
1601 O OD1 . ASP A 101 ? 0.7357 0.7045 0.5312 0.0659  0.0303  -0.0103 104 ASP A OD1 
1602 O OD2 . ASP A 101 ? 0.8399 0.7935 0.6063 0.0335  0.0059  -0.0346 104 ASP A OD2 
1607 N N   . GLN A 102 ? 0.4712 0.5316 0.3413 0.0513  0.0060  0.0420  105 GLN A N   
1608 C CA  . GLN A 102 ? 0.4558 0.5333 0.3575 0.0456  0.0050  0.0562  105 GLN A CA  
1609 C C   . GLN A 102 ? 0.4493 0.5212 0.3617 0.0550  0.0145  0.0483  105 GLN A C   
1610 O O   . GLN A 102 ? 0.3978 0.4715 0.3342 0.0469  0.0074  0.0506  105 GLN A O   
1611 C CB  . GLN A 102 ? 0.6366 0.7524 0.5432 0.0440  0.0135  0.0813  105 GLN A CB  
1612 C CG  . GLN A 102 ? 0.6646 0.7800 0.5685 0.0243  0.0001  0.0959  105 GLN A CG  
1613 C CD  . GLN A 102 ? 0.9558 1.1101 0.8549 0.0196  0.0096  0.1199  105 GLN A CD  
1614 O OE1 . GLN A 102 ? 0.9197 1.1180 0.8323 0.0267  0.0241  0.1328  105 GLN A OE1 
1615 N NE2 . GLN A 102 ? 1.0751 1.2183 0.9540 0.0094  0.0025  0.1286  105 GLN A NE2 
1624 N N   . GLY A 103 ? 0.4006 0.4597 0.2882 0.0736  0.0318  0.0402  106 GLY A N   
1625 C CA  . GLY A 103 ? 0.4249 0.4688 0.3136 0.0863  0.0429  0.0344  106 GLY A CA  
1626 C C   . GLY A 103 ? 0.4620 0.4731 0.3547 0.0722  0.0305  0.0153  106 GLY A C   
1627 O O   . GLY A 103 ? 0.4208 0.4310 0.3324 0.0730  0.0310  0.0162  106 GLY A O   
1631 N N   . THR A 104 ? 0.4130 0.4052 0.2890 0.0583  0.0188  0.0001  107 THR A N   
1632 C CA  . THR A 104 ? 0.4363 0.4120 0.3180 0.0433  0.0072  -0.0149 107 THR A CA  
1633 C C   . THR A 104 ? 0.4111 0.4101 0.3322 0.0363  -0.0070 -0.0061 107 THR A C   
1634 O O   . THR A 104 ? 0.4023 0.3953 0.3384 0.0316  -0.0105 -0.0118 107 THR A O   
1635 C CB  . THR A 104 ? 0.4707 0.4378 0.3258 0.0287  -0.0028 -0.0292 107 THR A CB  
1636 O OG1 . THR A 104 ? 0.5498 0.4799 0.3545 0.0323  0.0113  -0.0403 107 THR A OG1 
1637 C CG2 . THR A 104 ? 0.5446 0.5123 0.4099 0.0106  -0.0153 -0.0409 107 THR A CG2 
1645 N N   . ILE A 105 ? 0.3547 0.3731 0.2857 0.0352  -0.0144 0.0078  108 ILE A N   
1646 C CA  . ILE A 105 ? 0.3288 0.3518 0.2818 0.0292  -0.0262 0.0160  108 ILE A CA  
1647 C C   . ILE A 105 ? 0.3955 0.4229 0.3672 0.0288  -0.0208 0.0230  108 ILE A C   
1648 O O   . ILE A 105 ? 0.3590 0.3787 0.3434 0.0248  -0.0271 0.0197  108 ILE A O   
1649 C CB  . ILE A 105 ? 0.3517 0.3790 0.2975 0.0260  -0.0332 0.0308  108 ILE A CB  
1650 C CG1 . ILE A 105 ? 0.3970 0.4243 0.3256 0.0294  -0.0409 0.0254  108 ILE A CG1 
1651 C CG2 . ILE A 105 ? 0.4977 0.5110 0.4505 0.0189  -0.0423 0.0393  108 ILE A CG2 
1652 C CD1 . ILE A 105 ? 0.4411 0.4654 0.3546 0.0290  -0.0460 0.0416  108 ILE A CD1 
1664 N N   . LEU A 106 ? 0.3459 0.3922 0.3189 0.0344  -0.0087 0.0348  109 LEU A N   
1665 C CA  A LEU A 106 ? 0.2981 0.3622 0.2900 0.0350  -0.0041 0.0450  109 LEU A CA  
1666 C CA  B LEU A 106 ? 0.2990 0.3636 0.2906 0.0355  -0.0035 0.0451  109 LEU A CA  
1667 C C   . LEU A 106 ? 0.3652 0.4096 0.3589 0.0433  0.0012  0.0314  109 LEU A C   
1668 O O   . LEU A 106 ? 0.3420 0.3889 0.3519 0.0378  -0.0037 0.0334  109 LEU A O   
1669 C CB  A LEU A 106 ? 0.3627 0.4661 0.3565 0.0454  0.0102  0.0637  109 LEU A CB  
1670 C CB  B LEU A 106 ? 0.3627 0.4642 0.3543 0.0480  0.0120  0.0624  109 LEU A CB  
1671 C CG  A LEU A 106 ? 0.3534 0.4922 0.3693 0.0468  0.0141  0.0789  109 LEU A CG  
1672 C CG  B LEU A 106 ? 0.3354 0.4740 0.3317 0.0349  0.0089  0.0840  109 LEU A CG  
1673 C CD1 A LEU A 106 ? 0.4659 0.6117 0.4953 0.0177  -0.0037 0.0871  109 LEU A CD1 
1674 C CD1 B LEU A 106 ? 0.4341 0.6062 0.4215 0.0560  0.0281  0.0958  109 LEU A CD1 
1675 C CD2 A LEU A 106 ? 0.3723 0.5654 0.3921 0.0634  0.0304  0.1010  109 LEU A CD2 
1676 C CD2 B LEU A 106 ? 0.4732 0.6429 0.4904 0.0144  0.0005  0.1013  109 LEU A CD2 
1699 N N   . ALA A 107 ? 0.3540 0.3734 0.3248 0.0535  0.0111  0.0177  110 ALA A N   
1700 C CA  . ALA A 107 ? 0.3803 0.3710 0.3435 0.0566  0.0167  0.0050  110 ALA A CA  
1701 C C   . ALA A 107 ? 0.3465 0.3328 0.3261 0.0405  0.0015  -0.0041 110 ALA A C   
1702 O O   . ALA A 107 ? 0.3501 0.3307 0.3397 0.0404  0.0027  -0.0053 110 ALA A O   
1703 C CB  . ALA A 107 ? 0.4703 0.4211 0.3917 0.0607  0.0272  -0.0104 110 ALA A CB  
1709 N N   . LEU A 108 ? 0.2919 0.2828 0.2716 0.0306  -0.0113 -0.0091 111 LEU A N   
1710 C CA  . LEU A 108 ? 0.3096 0.3035 0.3020 0.0227  -0.0233 -0.0153 111 LEU A CA  
1711 C C   . LEU A 108 ? 0.3374 0.3360 0.3478 0.0235  -0.0288 -0.0056 111 LEU A C   
1712 O O   . LEU A 108 ? 0.3251 0.3202 0.3449 0.0223  -0.0305 -0.0097 111 LEU A O   
1713 C CB  . LEU A 108 ? 0.3147 0.3208 0.3010 0.0198  -0.0343 -0.0174 111 LEU A CB  
1714 C CG  . LEU A 108 ? 0.4335 0.4437 0.4030 0.0099  -0.0362 -0.0299 111 LEU A CG  
1715 C CD1 . LEU A 108 ? 0.5047 0.5415 0.4741 0.0117  -0.0489 -0.0260 111 LEU A CD1 
1716 C CD2 . LEU A 108 ? 0.5185 0.5277 0.4915 -0.0020 -0.0359 -0.0401 111 LEU A CD2 
1728 N N   . VAL A 109 ? 0.2845 0.2883 0.2942 0.0221  -0.0320 0.0074  112 VAL A N   
1729 C CA  . VAL A 109 ? 0.2885 0.2866 0.3023 0.0153  -0.0389 0.0160  112 VAL A CA  
1730 C C   . VAL A 109 ? 0.3343 0.3430 0.3612 0.0141  -0.0330 0.0199  112 VAL A C   
1731 O O   . VAL A 109 ? 0.2903 0.2900 0.3200 0.0097  -0.0378 0.0188  112 VAL A O   
1732 C CB  . VAL A 109 ? 0.3283 0.3257 0.3302 0.0059  -0.0439 0.0303  112 VAL A CB  
1733 C CG1 . VAL A 109 ? 0.3747 0.3612 0.3709 -0.0104 -0.0508 0.0399  112 VAL A CG1 
1734 C CG2 . VAL A 109 ? 0.4254 0.4044 0.4092 0.0114  -0.0507 0.0277  112 VAL A CG2 
1744 N N   . GLY A 110 ? 0.2699 0.2975 0.3010 0.0216  -0.0211 0.0257  113 GLY A N   
1745 C CA  . GLY A 110 ? 0.2516 0.2941 0.2933 0.0270  -0.0140 0.0326  113 GLY A CA  
1746 C C   . GLY A 110 ? 0.2980 0.3179 0.3396 0.0319  -0.0110 0.0193  113 GLY A C   
1747 O O   . GLY A 110 ? 0.2746 0.2985 0.3247 0.0296  -0.0132 0.0225  113 GLY A O   
1751 N N   . ALA A 111 ? 0.2502 0.2473 0.2788 0.0353  -0.0062 0.0050  114 ALA A N   
1752 C CA  . ALA A 111 ? 0.2731 0.2508 0.2992 0.0330  -0.0041 -0.0064 114 ALA A CA  
1753 C C   . ALA A 111 ? 0.2391 0.2219 0.2781 0.0248  -0.0162 -0.0095 114 ALA A C   
1754 O O   . ALA A 111 ? 0.2798 0.2581 0.3234 0.0240  -0.0147 -0.0120 114 ALA A O   
1755 C CB  . ALA A 111 ? 0.3153 0.2712 0.3198 0.0276  -0.0002 -0.0206 114 ALA A CB  
1761 N N   . ASP A 112 ? 0.2346 0.2224 0.2736 0.0219  -0.0265 -0.0089 115 ASP A N   
1762 C CA  . ASP A 112 ? 0.2284 0.2124 0.2688 0.0220  -0.0351 -0.0110 115 ASP A CA  
1763 C C   . ASP A 112 ? 0.2514 0.2283 0.2913 0.0184  -0.0377 -0.0036 115 ASP A C   
1764 O O   . ASP A 112 ? 0.2469 0.2162 0.2857 0.0202  -0.0392 -0.0074 115 ASP A O   
1765 C CB  . ASP A 112 ? 0.2510 0.2321 0.2807 0.0256  -0.0431 -0.0092 115 ASP A CB  
1766 C CG  . ASP A 112 ? 0.3221 0.2946 0.3442 0.0355  -0.0483 -0.0109 115 ASP A CG  
1767 O OD1 . ASP A 112 ? 0.3522 0.2988 0.3597 0.0353  -0.0512 -0.0071 115 ASP A OD1 
1768 O OD2 . ASP A 112 ? 0.4256 0.4185 0.4526 0.0435  -0.0487 -0.0154 115 ASP A OD2 
1773 N N   . GLY A 113 ? 0.2548 0.2387 0.2934 0.0113  -0.0390 0.0079  116 GLY A N   
1774 C CA  . GLY A 113 ? 0.2457 0.2321 0.2822 0.0007  -0.0436 0.0167  116 GLY A CA  
1775 C C   . GLY A 113 ? 0.2484 0.2463 0.2969 0.0066  -0.0368 0.0163  116 GLY A C   
1776 O O   . GLY A 113 ? 0.2748 0.2665 0.3182 0.0010  -0.0414 0.0167  116 GLY A O   
1780 N N   . ILE A 114 ? 0.2111 0.2197 0.2683 0.0185  -0.0247 0.0164  117 ILE A N   
1781 C CA  . ILE A 114 ? 0.2108 0.2197 0.2716 0.0269  -0.0160 0.0169  117 ILE A CA  
1782 C C   . ILE A 114 ? 0.2530 0.2416 0.3112 0.0247  -0.0174 0.0037  117 ILE A C   
1783 O O   . ILE A 114 ? 0.2509 0.2391 0.3098 0.0249  -0.0169 0.0053  117 ILE A O   
1784 C CB  . ILE A 114 ? 0.2400 0.2440 0.2945 0.0423  -0.0005 0.0184  117 ILE A CB  
1785 C CG1 . ILE A 114 ? 0.2756 0.3149 0.3357 0.0513  0.0036  0.0372  117 ILE A CG1 
1786 C CG2 . ILE A 114 ? 0.3044 0.2899 0.3513 0.0508  0.0099  0.0168  117 ILE A CG2 
1787 C CD1 . ILE A 114 ? 0.3562 0.3845 0.3999 0.0748  0.0224  0.0401  117 ILE A CD1 
1799 N N   . MET A 115 ? 0.2202 0.1999 0.2755 0.0229  -0.0193 -0.0073 118 MET A N   
1800 C CA  . MET A 115 ? 0.2247 0.2016 0.2811 0.0217  -0.0195 -0.0163 118 MET A CA  
1801 C C   . MET A 115 ? 0.2523 0.2255 0.3045 0.0236  -0.0265 -0.0151 118 MET A C   
1802 O O   . MET A 115 ? 0.2529 0.2258 0.3052 0.0250  -0.0236 -0.0167 118 MET A O   
1803 C CB  . MET A 115 ? 0.2407 0.2259 0.2968 0.0195  -0.0220 -0.0240 118 MET A CB  
1804 C CG  . MET A 115 ? 0.2453 0.2475 0.3064 0.0206  -0.0236 -0.0287 118 MET A CG  
1805 S SD  . MET A 115 ? 0.2658 0.2985 0.3297 0.0180  -0.0287 -0.0325 118 MET A SD  
1806 C CE  . MET A 115 ? 0.3024 0.3265 0.3574 0.0384  -0.0366 -0.0266 118 MET A CE  
1816 N N   . ILE A 116 ? 0.2343 0.1968 0.2747 0.0231  -0.0352 -0.0125 119 ILE A N   
1817 C CA  . ILE A 116 ? 0.2501 0.1909 0.2702 0.0246  -0.0407 -0.0132 119 ILE A CA  
1818 C C   . ILE A 116 ? 0.2801 0.2200 0.2960 0.0135  -0.0430 -0.0068 119 ILE A C   
1819 O O   . ILE A 116 ? 0.3024 0.2297 0.3051 0.0151  -0.0434 -0.0097 119 ILE A O   
1820 C CB  . ILE A 116 ? 0.2871 0.2002 0.2817 0.0251  -0.0482 -0.0118 119 ILE A CB  
1821 C CG1 . ILE A 116 ? 0.3060 0.2296 0.3060 0.0402  -0.0461 -0.0155 119 ILE A CG1 
1822 C CG2 . ILE A 116 ? 0.3847 0.2554 0.3411 0.0274  -0.0520 -0.0141 119 ILE A CG2 
1823 C CD1 . ILE A 116 ? 0.3121 0.2553 0.3198 0.0566  -0.0403 -0.0209 119 ILE A CD1 
1835 N N   . GLY A 117 ? 0.2358 0.1952 0.2616 0.0035  -0.0444 0.0038  120 GLY A N   
1836 C CA  . GLY A 117 ? 0.2397 0.2133 0.2630 -0.0079 -0.0486 0.0139  120 GLY A CA  
1837 C C   . GLY A 117 ? 0.2569 0.2409 0.2908 0.0023  -0.0403 0.0134  120 GLY A C   
1838 O O   . GLY A 117 ? 0.2783 0.2610 0.3008 -0.0039 -0.0447 0.0157  120 GLY A O   
1842 N N   . THR A 118 ? 0.2279 0.2173 0.2769 0.0153  -0.0284 0.0109  121 THR A N   
1843 C CA  . THR A 118 ? 0.2247 0.2143 0.2764 0.0228  -0.0193 0.0115  121 THR A CA  
1844 C C   . THR A 118 ? 0.2631 0.2375 0.3072 0.0229  -0.0194 0.0004  121 THR A C   
1845 O O   . THR A 118 ? 0.2585 0.2331 0.2987 0.0246  -0.0159 0.0025  121 THR A O   
1846 C CB  . THR A 118 ? 0.2528 0.2366 0.3081 0.0330  -0.0051 0.0121  121 THR A CB  
1847 O OG1 . THR A 118 ? 0.2692 0.2407 0.3241 0.0292  -0.0040 0.0000  121 THR A OG1 
1848 C CG2 . THR A 118 ? 0.3220 0.3238 0.3802 0.0427  -0.0006 0.0264  121 THR A CG2 
1856 N N   . GLY A 119 ? 0.2337 0.2000 0.2750 0.0243  -0.0219 -0.0092 122 GLY A N   
1857 C CA  . GLY A 119 ? 0.2544 0.2154 0.2865 0.0307  -0.0207 -0.0161 122 GLY A CA  
1858 C C   . GLY A 119 ? 0.3282 0.2697 0.3352 0.0296  -0.0271 -0.0153 122 GLY A C   
1859 O O   . GLY A 119 ? 0.3047 0.2442 0.3029 0.0353  -0.0227 -0.0176 122 GLY A O   
1863 N N   . LEU A 120 ? 0.2750 0.2004 0.2651 0.0190  -0.0375 -0.0120 123 LEU A N   
1864 C CA  . LEU A 120 ? 0.2909 0.1900 0.2463 0.0091  -0.0458 -0.0119 123 LEU A CA  
1865 C C   . LEU A 120 ? 0.3029 0.2254 0.2656 0.0012  -0.0462 -0.0038 123 LEU A C   
1866 O O   . LEU A 120 ? 0.3210 0.2277 0.2593 0.0008  -0.0471 -0.0070 123 LEU A O   
1867 C CB  . LEU A 120 ? 0.3141 0.1935 0.2476 -0.0102 -0.0581 -0.0079 123 LEU A CB  
1868 C CG  . LEU A 120 ? 0.3712 0.2201 0.2603 -0.0336 -0.0701 -0.0064 123 LEU A CG  
1869 C CD1 . LEU A 120 ? 0.4562 0.2446 0.2929 -0.0224 -0.0679 -0.0192 123 LEU A CD1 
1870 C CD2 . LEU A 120 ? 0.5238 0.3598 0.3949 -0.0597 -0.0818 0.0003  123 LEU A CD2 
1882 N N   . VAL A 121 ? 0.2558 0.2149 0.2475 -0.0012 -0.0441 0.0079  124 VAL A N   
1883 C CA  . VAL A 121 ? 0.2415 0.2264 0.2391 -0.0017 -0.0428 0.0190  124 VAL A CA  
1884 C C   . VAL A 121 ? 0.2840 0.2600 0.2822 0.0121  -0.0312 0.0132  124 VAL A C   
1885 O O   . VAL A 121 ? 0.2946 0.2715 0.2789 0.0106  -0.0324 0.0158  124 VAL A O   
1886 C CB  . VAL A 121 ? 0.2426 0.2643 0.2668 0.0050  -0.0373 0.0340  124 VAL A CB  
1887 C CG1 . VAL A 121 ? 0.2667 0.3145 0.2952 0.0141  -0.0322 0.0483  124 VAL A CG1 
1888 C CG2 . VAL A 121 ? 0.3093 0.3554 0.3345 -0.0117 -0.0491 0.0443  124 VAL A CG2 
1898 N N   . GLY A 122 ? 0.2582 0.2289 0.2707 0.0223  -0.0205 0.0062  125 GLY A N   
1899 C CA  . GLY A 122 ? 0.2941 0.2624 0.3063 0.0293  -0.0098 0.0025  125 GLY A CA  
1900 C C   . GLY A 122 ? 0.3159 0.2713 0.3054 0.0325  -0.0120 -0.0052 125 GLY A C   
1901 O O   . GLY A 122 ? 0.3140 0.2719 0.2953 0.0358  -0.0064 -0.0035 125 GLY A O   
1905 N N   . ALA A 123 ? 0.2931 0.2290 0.2655 0.0348  -0.0184 -0.0134 126 ALA A N   
1906 C CA  . ALA A 123 ? 0.3134 0.2251 0.2520 0.0452  -0.0172 -0.0210 126 ALA A CA  
1907 C C   . ALA A 123 ? 0.3816 0.2730 0.2861 0.0350  -0.0246 -0.0196 126 ALA A C   
1908 O O   . ALA A 123 ? 0.3811 0.2551 0.2561 0.0452  -0.0197 -0.0247 126 ALA A O   
1909 C CB  . ALA A 123 ? 0.3852 0.2665 0.3006 0.0536  -0.0211 -0.0281 126 ALA A CB  
1915 N N   . LEU A 124 ? 0.3320 0.2304 0.2374 0.0147  -0.0365 -0.0115 127 LEU A N   
1916 C CA  . LEU A 124 ? 0.3572 0.2447 0.2285 -0.0023 -0.0474 -0.0086 127 LEU A CA  
1917 C C   . LEU A 124 ? 0.3454 0.2750 0.2380 -0.0041 -0.0457 0.0051  127 LEU A C   
1918 O O   . LEU A 124 ? 0.3789 0.3129 0.2472 -0.0196 -0.0562 0.0106  127 LEU A O   
1919 C CB  . LEU A 124 ? 0.3957 0.2735 0.2494 -0.0295 -0.0643 -0.0048 127 LEU A CB  
1920 C CG  . LEU A 124 ? 0.4446 0.2659 0.2620 -0.0298 -0.0669 -0.0166 127 LEU A CG  
1921 C CD1 . LEU A 124 ? 0.5353 0.3521 0.3362 -0.0645 -0.0839 -0.0095 127 LEU A CD1 
1922 C CD2 . LEU A 124 ? 0.5056 0.2641 0.2602 -0.0212 -0.0642 -0.0300 127 LEU A CD2 
1934 N N   . THR A 125 ? 0.3287 0.2847 0.2594 0.0106  -0.0329 0.0114  128 THR A N   
1935 C CA  . THR A 125 ? 0.2968 0.2835 0.2418 0.0146  -0.0285 0.0269  128 THR A CA  
1936 C C   . THR A 125 ? 0.3466 0.3255 0.2721 0.0208  -0.0219 0.0252  128 THR A C   
1937 O O   . THR A 125 ? 0.3742 0.3370 0.2957 0.0302  -0.0115 0.0151  128 THR A O   
1938 C CB  . THR A 125 ? 0.3143 0.3111 0.2916 0.0272  -0.0152 0.0325  128 THR A CB  
1939 O OG1 . THR A 125 ? 0.3527 0.3674 0.3448 0.0239  -0.0213 0.0402  128 THR A OG1 
1940 C CG2 . THR A 125 ? 0.3656 0.3726 0.3453 0.0388  -0.0039 0.0467  128 THR A CG2 
1948 N N   . LYS A 126 ? 0.3325 0.3309 0.2453 0.0154  -0.0285 0.0374  129 LYS A N   
1949 C CA  . LYS A 126 ? 0.3991 0.3892 0.2863 0.0191  -0.0243 0.0361  129 LYS A CA  
1950 C C   . LYS A 126 ? 0.4303 0.4318 0.3346 0.0347  -0.0075 0.0472  129 LYS A C   
1951 O O   . LYS A 126 ? 0.4798 0.4734 0.3664 0.0395  0.0003  0.0452  129 LYS A O   
1952 C CB  . LYS A 126 ? 0.4318 0.4388 0.2909 0.0022  -0.0413 0.0448  129 LYS A CB  
1953 C CG  . LYS A 126 ? 0.5390 0.5196 0.3624 -0.0223 -0.0589 0.0328  129 LYS A CG  
1954 C CD  . LYS A 126 ? 0.6784 0.6916 0.4798 -0.0491 -0.0791 0.0461  129 LYS A CD  
1955 C CE  . LYS A 126 ? 1.1654 1.1275 0.8997 -0.0772 -0.0940 0.0301  129 LYS A CE  
1956 N NZ  . LYS A 126 ? 1.3154 1.2630 1.0368 -0.1060 -0.1091 0.0268  129 LYS A NZ  
1970 N N   . VAL A 127 ? 0.3602 0.3738 0.2906 0.0428  -0.0005 0.0592  130 VAL A N   
1971 C CA  . VAL A 127 ? 0.3460 0.3520 0.2802 0.0553  0.0171  0.0698  130 VAL A CA  
1972 C C   . VAL A 127 ? 0.4011 0.3846 0.3467 0.0524  0.0293  0.0571  130 VAL A C   
1973 O O   . VAL A 127 ? 0.3741 0.3521 0.3356 0.0506  0.0291  0.0522  130 VAL A O   
1974 C CB  . VAL A 127 ? 0.3698 0.3879 0.3122 0.0694  0.0211  0.0901  130 VAL A CB  
1975 C CG1 . VAL A 127 ? 0.4040 0.3919 0.3356 0.0816  0.0414  0.0998  130 VAL A CG1 
1976 C CG2 . VAL A 127 ? 0.4410 0.5018 0.3760 0.0716  0.0076  0.1073  130 VAL A CG2 
1986 N N   . TYR A 128 ? 0.3517 0.4617 0.2593 0.0155  0.0030  0.0656  131 TYR A N   
1987 C CA  . TYR A 128 ? 0.3294 0.4455 0.2530 0.0186  0.0183  0.0605  131 TYR A CA  
1988 C C   . TYR A 128 ? 0.3150 0.4211 0.2747 0.0114  0.0200  0.0714  131 TYR A C   
1989 O O   . TYR A 128 ? 0.3138 0.4136 0.2920 0.0121  0.0228  0.0610  131 TYR A O   
1990 C CB  . TYR A 128 ? 0.3538 0.4982 0.2595 0.0202  0.0328  0.0704  131 TYR A CB  
1991 C CG  . TYR A 128 ? 0.3893 0.5536 0.3128 0.0235  0.0488  0.0684  131 TYR A CG  
1992 C CD1 . TYR A 128 ? 0.4241 0.5866 0.3457 0.0368  0.0531  0.0469  131 TYR A CD1 
1993 C CD2 . TYR A 128 ? 0.4127 0.5987 0.3554 0.0124  0.0584  0.0907  131 TYR A CD2 
1994 C CE1 . TYR A 128 ? 0.4361 0.6255 0.3783 0.0418  0.0671  0.0488  131 TYR A CE1 
1995 C CE2 . TYR A 128 ? 0.4035 0.6175 0.3670 0.0125  0.0711  0.0924  131 TYR A CE2 
1996 C CZ  . TYR A 128 ? 0.5314 0.7506 0.4960 0.0286  0.0755  0.0720  131 TYR A CZ  
1997 O OH  . TYR A 128 ? 0.4909 0.7460 0.4799 0.0307  0.0875  0.0773  131 TYR A OH  
2007 N N   A SER A 129 ? 0.3439 0.4454 0.3102 0.0049  0.0183  0.0931  132 SER A N   
2008 N N   B SER A 129 ? 0.3439 0.4453 0.3101 0.0049  0.0183  0.0931  132 SER A N   
2009 C CA  A SER A 129 ? 0.3169 0.3992 0.3083 -0.0019 0.0210  0.1013  132 SER A CA  
2010 C CA  B SER A 129 ? 0.3176 0.3995 0.3089 -0.0019 0.0207  0.1015  132 SER A CA  
2011 C C   A SER A 129 ? 0.3205 0.3798 0.3277 0.0026  0.0141  0.0890  132 SER A C   
2012 C C   B SER A 129 ? 0.3216 0.3813 0.3286 0.0027  0.0141  0.0884  132 SER A C   
2013 O O   A SER A 129 ? 0.3309 0.3743 0.3531 -0.0016 0.0172  0.0850  132 SER A O   
2014 O O   B SER A 129 ? 0.3288 0.3740 0.3508 -0.0014 0.0173  0.0833  132 SER A O   
2015 C CB  A SER A 129 ? 0.3926 0.4646 0.3828 -0.0071 0.0207  0.1271  132 SER A CB  
2016 C CB  B SER A 129 ? 0.3910 0.4618 0.3812 -0.0062 0.0198  0.1270  132 SER A CB  
2017 O OG  A SER A 129 ? 0.4126 0.4756 0.4015 0.0014  0.0107  0.1333  132 SER A OG  
2018 O OG  B SER A 129 ? 0.4317 0.5238 0.4095 -0.0137 0.0275  0.1425  132 SER A OG  
2029 N N   . TYR A 130 ? 0.3065 0.3662 0.3092 0.0093  0.0042  0.0839  133 TYR A N   
2030 C CA  . TYR A 130 ? 0.2816 0.3269 0.3007 0.0133  -0.0007 0.0752  133 TYR A CA  
2031 C C   . TYR A 130 ? 0.2912 0.3346 0.3142 0.0131  0.0010  0.0549  133 TYR A C   
2032 O O   . TYR A 130 ? 0.2829 0.3137 0.3201 0.0144  0.0002  0.0492  133 TYR A O   
2033 C CB  . TYR A 130 ? 0.2848 0.3390 0.3026 0.0168  -0.0133 0.0786  133 TYR A CB  
2034 C CG  . TYR A 130 ? 0.3604 0.4210 0.3805 0.0205  -0.0174 0.1020  133 TYR A CG  
2035 C CD1 . TYR A 130 ? 0.3726 0.4184 0.3972 0.0229  -0.0089 0.1179  133 TYR A CD1 
2036 C CD2 . TYR A 130 ? 0.3652 0.4452 0.3827 0.0205  -0.0312 0.1094  133 TYR A CD2 
2037 C CE1 . TYR A 130 ? 0.4396 0.4885 0.4662 0.0295  -0.0124 0.1419  133 TYR A CE1 
2038 C CE2 . TYR A 130 ? 0.3720 0.4641 0.3948 0.0259  -0.0360 0.1343  133 TYR A CE2 
2039 C CZ  . TYR A 130 ? 0.4525 0.5279 0.4799 0.0326  -0.0256 0.1507  133 TYR A CZ  
2040 O OH  . TYR A 130 ? 0.5396 0.6243 0.5721 0.0412  -0.0301 0.1780  133 TYR A OH  
2050 N N   . ARG A 131 ? 0.2545 0.3106 0.2632 0.0139  0.0041  0.0448  134 ARG A N   
2051 C CA  . ARG A 131 ? 0.2314 0.2852 0.2452 0.0172  0.0061  0.0285  134 ARG A CA  
2052 C C   . ARG A 131 ? 0.3078 0.3576 0.3420 0.0123  0.0116  0.0308  134 ARG A C   
2053 O O   . ARG A 131 ? 0.2598 0.3019 0.3035 0.0136  0.0096  0.0214  134 ARG A O   
2054 C CB  . ARG A 131 ? 0.2866 0.3555 0.2821 0.0241  0.0128  0.0201  134 ARG A CB  
2055 C CG  . ARG A 131 ? 0.3128 0.3773 0.2771 0.0277  0.0057  0.0132  134 ARG A CG  
2056 C CD  . ARG A 131 ? 0.3304 0.4070 0.2689 0.0387  0.0164  0.0041  134 ARG A CD  
2057 N NE  . ARG A 131 ? 0.3200 0.3880 0.2605 0.0506  0.0209  -0.0119 134 ARG A NE  
2058 C CZ  . ARG A 131 ? 0.3706 0.4094 0.2920 0.0558  0.0123  -0.0291 134 ARG A CZ  
2059 N NH1 . ARG A 131 ? 0.3399 0.3586 0.2399 0.0467  -0.0029 -0.0334 134 ARG A NH1 
2060 N NH2 . ARG A 131 ? 0.3852 0.4146 0.3086 0.0695  0.0178  -0.0406 134 ARG A NH2 
2074 N N   . PHE A 132 ? 0.2502 0.3028 0.2883 0.0042  0.0172  0.0442  135 PHE A N   
2075 C CA  . PHE A 132 ? 0.2503 0.2963 0.3019 -0.0056 0.0197  0.0457  135 PHE A CA  
2076 C C   . PHE A 132 ? 0.3009 0.3145 0.3561 -0.0069 0.0162  0.0455  135 PHE A C   
2077 O O   . PHE A 132 ? 0.2631 0.2651 0.3232 -0.0136 0.0158  0.0402  135 PHE A O   
2078 C CB  . PHE A 132 ? 0.2691 0.3282 0.3214 -0.0179 0.0257  0.0612  135 PHE A CB  
2079 C CG  . PHE A 132 ? 0.2452 0.3436 0.2945 -0.0133 0.0331  0.0624  135 PHE A CG  
2080 C CD1 . PHE A 132 ? 0.3010 0.4243 0.3627 -0.0109 0.0366  0.0560  135 PHE A CD1 
2081 C CD2 . PHE A 132 ? 0.3171 0.4282 0.3499 -0.0088 0.0369  0.0704  135 PHE A CD2 
2082 C CE1 . PHE A 132 ? 0.3380 0.4991 0.3967 -0.0009 0.0467  0.0574  135 PHE A CE1 
2083 C CE2 . PHE A 132 ? 0.3598 0.5061 0.3844 -0.0010 0.0467  0.0700  135 PHE A CE2 
2084 C CZ  . PHE A 132 ? 0.3268 0.4978 0.3652 0.0046  0.0528  0.0631  135 PHE A CZ  
2094 N N   . VAL A 133 ? 0.2551 0.2566 0.3066 0.0006  0.0140  0.0514  136 VAL A N   
2095 C CA  . VAL A 133 ? 0.2614 0.2371 0.3166 0.0063  0.0137  0.0508  136 VAL A CA  
2096 C C   . VAL A 133 ? 0.2721 0.2519 0.3333 0.0103  0.0110  0.0371  136 VAL A C   
2097 O O   . VAL A 133 ? 0.2719 0.2349 0.3336 0.0097  0.0130  0.0311  136 VAL A O   
2098 C CB  . VAL A 133 ? 0.3136 0.2879 0.3692 0.0170  0.0121  0.0641  136 VAL A CB  
2099 C CG1 . VAL A 133 ? 0.3537 0.3089 0.4158 0.0286  0.0150  0.0645  136 VAL A CG1 
2100 C CG2 . VAL A 133 ? 0.3716 0.3368 0.4196 0.0131  0.0149  0.0810  136 VAL A CG2 
2110 N N   . TRP A 134 ? 0.2348 0.2343 0.2966 0.0135  0.0057  0.0318  137 TRP A N   
2111 C CA  . TRP A 134 ? 0.2155 0.2158 0.2825 0.0157  0.0021  0.0215  137 TRP A CA  
2112 C C   . TRP A 134 ? 0.2406 0.2413 0.3089 0.0111  0.0042  0.0130  137 TRP A C   
2113 O O   . TRP A 134 ? 0.2546 0.2487 0.3263 0.0112  0.0033  0.0079  137 TRP A O   
2114 C CB  . TRP A 134 ? 0.1953 0.2066 0.2573 0.0173  -0.0057 0.0175  137 TRP A CB  
2115 C CG  . TRP A 134 ? 0.1973 0.2147 0.2611 0.0186  -0.0114 0.0280  137 TRP A CG  
2116 C CD1 . TRP A 134 ? 0.2528 0.2801 0.3062 0.0175  -0.0162 0.0347  137 TRP A CD1 
2117 C CD2 . TRP A 134 ? 0.2368 0.2571 0.3151 0.0217  -0.0131 0.0359  137 TRP A CD2 
2118 N NE1 . TRP A 134 ? 0.2387 0.2765 0.3015 0.0188  -0.0227 0.0474  137 TRP A NE1 
2119 C CE2 . TRP A 134 ? 0.2147 0.2508 0.2952 0.0222  -0.0201 0.0489  137 TRP A CE2 
2120 C CE3 . TRP A 134 ? 0.2710 0.2868 0.3602 0.0248  -0.0087 0.0348  137 TRP A CE3 
2121 C CZ2 . TRP A 134 ? 0.2686 0.3206 0.3673 0.0266  -0.0224 0.0626  137 TRP A CZ2 
2122 C CZ3 . TRP A 134 ? 0.2820 0.3115 0.3861 0.0301  -0.0088 0.0470  137 TRP A CZ3 
2123 C CH2 . TRP A 134 ? 0.2813 0.3310 0.3928 0.0315  -0.0154 0.0617  137 TRP A CH2 
2134 N N   . TRP A 135 ? 0.2113 0.2255 0.2779 0.0073  0.0069  0.0137  138 TRP A N   
2135 C CA  . TRP A 135 ? 0.1788 0.2028 0.2519 0.0024  0.0077  0.0100  138 TRP A CA  
2136 C C   . TRP A 135 ? 0.2558 0.2617 0.3284 -0.0081 0.0073  0.0109  138 TRP A C   
2137 O O   . TRP A 135 ? 0.2461 0.2532 0.3211 -0.0115 0.0041  0.0057  138 TRP A O   
2138 C CB  . TRP A 135 ? 0.2235 0.2737 0.2987 -0.0001 0.0127  0.0158  138 TRP A CB  
2139 C CG  . TRP A 135 ? 0.2112 0.2838 0.2992 -0.0066 0.0129  0.0174  138 TRP A CG  
2140 C CD1 . TRP A 135 ? 0.1977 0.2932 0.2940 0.0041  0.0136  0.0136  138 TRP A CD1 
2141 C CD2 . TRP A 135 ? 0.2161 0.2907 0.3100 -0.0253 0.0109  0.0247  138 TRP A CD2 
2142 N NE1 . TRP A 135 ? 0.2326 0.3534 0.3441 -0.0064 0.0121  0.0207  138 TRP A NE1 
2143 C CE2 . TRP A 135 ? 0.2357 0.3434 0.3448 -0.0274 0.0091  0.0268  138 TRP A CE2 
2144 C CE3 . TRP A 135 ? 0.2755 0.3240 0.3615 -0.0412 0.0096  0.0304  138 TRP A CE3 
2145 C CZ2 . TRP A 135 ? 0.3016 0.4230 0.4196 -0.0490 0.0038  0.0351  138 TRP A CZ2 
2146 C CZ3 . TRP A 135 ? 0.3107 0.3618 0.4002 -0.0628 0.0047  0.0358  138 TRP A CZ3 
2147 C CH2 . TRP A 135 ? 0.3092 0.3993 0.4153 -0.0687 0.0008  0.0384  138 TRP A CH2 
2158 N N   . ALA A 136 ? 0.2635 0.2484 0.3292 -0.0127 0.0099  0.0172  139 ALA A N   
2159 C CA  . ALA A 136 ? 0.2924 0.2482 0.3486 -0.0227 0.0096  0.0150  139 ALA A CA  
2160 C C   . ALA A 136 ? 0.3107 0.2484 0.3606 -0.0132 0.0104  0.0068  139 ALA A C   
2161 O O   . ALA A 136 ? 0.3124 0.2372 0.3525 -0.0201 0.0084  -0.0004 139 ALA A O   
2162 C CB  . ALA A 136 ? 0.3020 0.2304 0.3486 -0.0275 0.0129  0.0244  139 ALA A CB  
2168 N N   . ILE A 137 ? 0.2420 0.1830 0.2969 0.0016  0.0129  0.0092  140 ILE A N   
2169 C CA  . ILE A 137 ? 0.2675 0.2010 0.3201 0.0109  0.0156  0.0051  140 ILE A CA  
2170 C C   . ILE A 137 ? 0.2979 0.2477 0.3542 0.0073  0.0103  -0.0015 140 ILE A C   
2171 O O   . ILE A 137 ? 0.3084 0.2492 0.3557 0.0072  0.0116  -0.0066 140 ILE A O   
2172 C CB  . ILE A 137 ? 0.3010 0.2458 0.3645 0.0242  0.0175  0.0140  140 ILE A CB  
2173 C CG1 . ILE A 137 ? 0.3273 0.2539 0.3867 0.0319  0.0235  0.0230  140 ILE A CG1 
2174 C CG2 . ILE A 137 ? 0.3339 0.2861 0.4019 0.0318  0.0200  0.0132  140 ILE A CG2 
2175 C CD1 . ILE A 137 ? 0.3838 0.3330 0.4579 0.0418  0.0217  0.0364  140 ILE A CD1 
2187 N N   . SER A 138 ? 0.2317 0.2041 0.2986 0.0062  0.0049  -0.0012 141 SER A N   
2188 C CA  . SER A 138 ? 0.2419 0.2259 0.3126 0.0059  -0.0001 -0.0051 141 SER A CA  
2189 C C   . SER A 138 ? 0.2743 0.2597 0.3401 -0.0040 -0.0026 -0.0080 141 SER A C   
2190 O O   . SER A 138 ? 0.2531 0.2400 0.3153 -0.0051 -0.0059 -0.0101 141 SER A O   
2191 C CB  . SER A 138 ? 0.2337 0.2331 0.3114 0.0104  -0.0035 -0.0052 141 SER A CB  
2192 O OG  . SER A 138 ? 0.2309 0.2373 0.3120 0.0135  -0.0079 -0.0075 141 SER A OG  
2198 N N   . THR A 139 ? 0.2127 0.2010 0.2784 -0.0134 -0.0026 -0.0060 142 THR A N   
2199 C CA  . THR A 139 ? 0.2387 0.2329 0.3012 -0.0286 -0.0083 -0.0064 142 THR A CA  
2200 C C   . THR A 139 ? 0.3195 0.2811 0.3586 -0.0354 -0.0086 -0.0134 142 THR A C   
2201 O O   . THR A 139 ? 0.3092 0.2744 0.3400 -0.0447 -0.0156 -0.0164 142 THR A O   
2202 C CB  . THR A 139 ? 0.2667 0.2723 0.3355 -0.0411 -0.0083 0.0005  142 THR A CB  
2203 O OG1 . THR A 139 ? 0.2581 0.2981 0.3448 -0.0315 -0.0058 0.0059  142 THR A OG1 
2204 C CG2 . THR A 139 ? 0.3300 0.3440 0.3965 -0.0627 -0.0173 0.0024  142 THR A CG2 
2212 N N   . ALA A 140 ? 0.3187 0.2488 0.3448 -0.0291 -0.0009 -0.0157 143 ALA A N   
2213 C CA  . ALA A 140 ? 0.3396 0.2346 0.3382 -0.0294 0.0023  -0.0243 143 ALA A CA  
2214 C C   . ALA A 140 ? 0.3556 0.2620 0.3514 -0.0202 0.0032  -0.0270 143 ALA A C   
2215 O O   . ALA A 140 ? 0.3939 0.2854 0.3653 -0.0265 0.0012  -0.0345 143 ALA A O   
2216 C CB  . ALA A 140 ? 0.3856 0.2471 0.3738 -0.0166 0.0134  -0.0237 143 ALA A CB  
2222 N N   . ALA A 141 ? 0.2787 0.2088 0.2954 -0.0077 0.0053  -0.0206 144 ALA A N   
2223 C CA  . ALA A 141 ? 0.2793 0.2217 0.2957 -0.0022 0.0051  -0.0192 144 ALA A CA  
2224 C C   . ALA A 141 ? 0.3069 0.2658 0.3228 -0.0127 -0.0060 -0.0193 144 ALA A C   
2225 O O   . ALA A 141 ? 0.3161 0.2744 0.3164 -0.0144 -0.0075 -0.0206 144 ALA A O   
2226 C CB  . ALA A 141 ? 0.2419 0.2034 0.2812 0.0077  0.0059  -0.0107 144 ALA A CB  
2232 N N   . MET A 142 ? 0.2883 0.2663 0.3212 -0.0181 -0.0131 -0.0160 145 MET A N   
2233 C CA  . MET A 142 ? 0.2679 0.2688 0.3052 -0.0255 -0.0236 -0.0125 145 MET A CA  
2234 C C   . MET A 142 ? 0.2973 0.2873 0.3103 -0.0432 -0.0300 -0.0179 145 MET A C   
2235 O O   . MET A 142 ? 0.3362 0.3381 0.3411 -0.0483 -0.0382 -0.0158 145 MET A O   
2236 C CB  . MET A 142 ? 0.2696 0.2979 0.3307 -0.0257 -0.0270 -0.0065 145 MET A CB  
2237 C CG  . MET A 142 ? 0.2859 0.3469 0.3587 -0.0277 -0.0370 0.0013  145 MET A CG  
2238 S SD  . MET A 142 ? 0.3131 0.4156 0.4152 -0.0248 -0.0374 0.0107  145 MET A SD  
2239 C CE  . MET A 142 ? 0.4079 0.5181 0.5047 -0.0538 -0.0444 0.0124  145 MET A CE  
2249 N N   . LEU A 143 ? 0.2925 0.2574 0.2912 -0.0539 -0.0280 -0.0242 146 LEU A N   
2250 C CA  . LEU A 143 ? 0.3751 0.3197 0.3434 -0.0746 -0.0364 -0.0316 146 LEU A CA  
2251 C C   . LEU A 143 ? 0.4163 0.3343 0.3495 -0.0690 -0.0320 -0.0412 146 LEU A C   
2252 O O   . LEU A 143 ? 0.4282 0.3419 0.3349 -0.0841 -0.0423 -0.0461 146 LEU A O   
2253 C CB  . LEU A 143 ? 0.3935 0.3049 0.3494 -0.0877 -0.0350 -0.0362 146 LEU A CB  
2254 C CG  . LEU A 143 ? 0.4850 0.4287 0.4723 -0.0985 -0.0401 -0.0242 146 LEU A CG  
2255 C CD1 . LEU A 143 ? 0.5040 0.4104 0.4789 -0.1102 -0.0371 -0.0254 146 LEU A CD1 
2256 C CD2 . LEU A 143 ? 0.4664 0.4501 0.4644 -0.1196 -0.0566 -0.0164 146 LEU A CD2 
2268 N N   . TYR A 144 ? 0.3655 0.2698 0.2974 -0.0480 -0.0169 -0.0427 147 TYR A N   
2269 C CA  . TYR A 144 ? 0.3910 0.2815 0.2937 -0.0393 -0.0097 -0.0482 147 TYR A CA  
2270 C C   . TYR A 144 ? 0.3832 0.3079 0.2921 -0.0418 -0.0188 -0.0397 147 TYR A C   
2271 O O   . TYR A 144 ? 0.4205 0.3389 0.2970 -0.0486 -0.0227 -0.0444 147 TYR A O   
2272 C CB  . TYR A 144 ? 0.3993 0.2839 0.3104 -0.0157 0.0085  -0.0454 147 TYR A CB  
2273 C CG  . TYR A 144 ? 0.4463 0.3271 0.3321 -0.0045 0.0192  -0.0473 147 TYR A CG  
2274 C CD1 . TYR A 144 ? 0.5323 0.3723 0.3721 -0.0002 0.0291  -0.0618 147 TYR A CD1 
2275 C CD2 . TYR A 144 ? 0.4828 0.3976 0.3862 0.0012  0.0196  -0.0345 147 TYR A CD2 
2276 C CE1 . TYR A 144 ? 0.5561 0.3962 0.3694 0.0126  0.0418  -0.0633 147 TYR A CE1 
2277 C CE2 . TYR A 144 ? 0.5214 0.4387 0.4019 0.0104  0.0306  -0.0331 147 TYR A CE2 
2278 C CZ  . TYR A 144 ? 0.5517 0.4345 0.3872 0.0172  0.0427  -0.0477 147 TYR A CZ  
2279 O OH  . TYR A 144 ? 0.7074 0.5955 0.5164 0.0289  0.0566  -0.0463 147 TYR A OH  
2289 N N   . ILE A 145 ? 0.3220 0.2803 0.2695 -0.0354 -0.0226 -0.0266 148 ILE A N   
2290 C CA  . ILE A 145 ? 0.3058 0.2918 0.2602 -0.0353 -0.0314 -0.0157 148 ILE A CA  
2291 C C   . ILE A 145 ? 0.3394 0.3392 0.2818 -0.0536 -0.0481 -0.0155 148 ILE A C   
2292 O O   . ILE A 145 ? 0.3763 0.3835 0.2977 -0.0585 -0.0548 -0.0125 148 ILE A O   
2293 C CB  . ILE A 145 ? 0.3086 0.3168 0.3021 -0.0243 -0.0329 -0.0039 148 ILE A CB  
2294 C CG1 . ILE A 145 ? 0.3097 0.3080 0.3104 -0.0116 -0.0207 -0.0015 148 ILE A CG1 
2295 C CG2 . ILE A 145 ? 0.3413 0.3742 0.3436 -0.0233 -0.0441 0.0090  148 ILE A CG2 
2296 C CD1 . ILE A 145 ? 0.3595 0.3651 0.3904 -0.0036 -0.0219 0.0042  148 ILE A CD1 
2308 N N   . LEU A 146 ? 0.3621 0.3707 0.3189 -0.0654 -0.0558 -0.0160 149 LEU A N   
2309 C CA  . LEU A 146 ? 0.3514 0.3836 0.3040 -0.0860 -0.0742 -0.0116 149 LEU A CA  
2310 C C   . LEU A 146 ? 0.5166 0.5174 0.4176 -0.1045 -0.0799 -0.0252 149 LEU A C   
2311 O O   . LEU A 146 ? 0.4471 0.4665 0.3323 -0.1190 -0.0957 -0.0210 149 LEU A O   
2312 C CB  . LEU A 146 ? 0.3694 0.4213 0.3492 -0.0973 -0.0797 -0.0072 149 LEU A CB  
2313 C CG  . LEU A 146 ? 0.3890 0.4707 0.4131 -0.0774 -0.0729 0.0041  149 LEU A CG  
2314 C CD1 . LEU A 146 ? 0.5124 0.6250 0.5614 -0.0904 -0.0784 0.0118  149 LEU A CD1 
2315 C CD2 . LEU A 146 ? 0.5315 0.6422 0.5734 -0.0607 -0.0765 0.0171  149 LEU A CD2 
2327 N N   . TYR A 147 ? 0.4049 0.3559 0.2763 -0.1035 -0.0677 -0.0417 150 TYR A N   
2328 C CA  . TYR A 147 ? 0.5224 0.4311 0.3352 -0.1166 -0.0700 -0.0585 150 TYR A CA  
2329 C C   . TYR A 147 ? 0.5102 0.4268 0.2974 -0.1073 -0.0676 -0.0572 150 TYR A C   
2330 O O   . TYR A 147 ? 0.5824 0.4961 0.3313 -0.1247 -0.0811 -0.0620 150 TYR A O   
2331 C CB  . TYR A 147 ? 0.5397 0.3913 0.3284 -0.1066 -0.0522 -0.0744 150 TYR A CB  
2332 C CG  . TYR A 147 ? 0.7045 0.5029 0.4257 -0.1092 -0.0476 -0.0946 150 TYR A CG  
2333 C CD1 . TYR A 147 ? 0.8480 0.6351 0.5485 -0.0831 -0.0273 -0.0988 150 TYR A CD1 
2334 C CD2 . TYR A 147 ? 1.0191 0.7786 0.6957 -0.1381 -0.0630 -0.1089 150 TYR A CD2 
2335 C CE1 . TYR A 147 ? 0.9604 0.6985 0.5948 -0.0809 -0.0195 -0.1183 150 TYR A CE1 
2336 C CE2 . TYR A 147 ? 1.0377 0.7396 0.6435 -0.1392 -0.0582 -0.1307 150 TYR A CE2 
2337 C CZ  . TYR A 147 ? 1.1507 0.8421 0.7346 -0.1080 -0.0349 -0.1360 150 TYR A CZ  
2338 O OH  . TYR A 147 ? 1.3379 0.9768 0.8539 -0.1031 -0.0264 -0.1567 150 TYR A OH  
2348 N N   . VAL A 148 ? 0.4596 0.3876 0.2665 -0.0819 -0.0513 -0.0492 151 VAL A N   
2349 C CA  . VAL A 148 ? 0.4733 0.4110 0.2571 -0.0735 -0.0469 -0.0443 151 VAL A CA  
2350 C C   . VAL A 148 ? 0.4601 0.4397 0.2539 -0.0856 -0.0677 -0.0285 151 VAL A C   
2351 O O   . VAL A 148 ? 0.5321 0.5146 0.2884 -0.0929 -0.0743 -0.0283 151 VAL A O   
2352 C CB  . VAL A 148 ? 0.4706 0.4187 0.2822 -0.0486 -0.0278 -0.0339 151 VAL A CB  
2353 C CG1 . VAL A 148 ? 0.4867 0.4565 0.2855 -0.0428 -0.0256 -0.0208 151 VAL A CG1 
2354 C CG2 . VAL A 148 ? 0.5377 0.4505 0.3349 -0.0341 -0.0067 -0.0469 151 VAL A CG2 
2364 N N   . LEU A 149 ? 0.4482 0.4625 0.2930 -0.0849 -0.0773 -0.0135 152 LEU A N   
2365 C CA  . LEU A 149 ? 0.4442 0.5017 0.3039 -0.0909 -0.0960 0.0052  152 LEU A CA  
2366 C C   . LEU A 149 ? 0.5439 0.6082 0.3723 -0.1187 -0.1171 0.0006  152 LEU A C   
2367 O O   . LEU A 149 ? 0.5163 0.6106 0.3362 -0.1254 -0.1325 0.0140  152 LEU A O   
2368 C CB  . LEU A 149 ? 0.4048 0.4947 0.3223 -0.0807 -0.0994 0.0202  152 LEU A CB  
2369 C CG  . LEU A 149 ? 0.4397 0.5250 0.3861 -0.0564 -0.0847 0.0275  152 LEU A CG  
2370 C CD1 . LEU A 149 ? 0.4734 0.5859 0.4663 -0.0460 -0.0891 0.0393  152 LEU A CD1 
2371 C CD2 . LEU A 149 ? 0.4766 0.5646 0.4118 -0.0475 -0.0829 0.0403  152 LEU A CD2 
2383 N N   . PHE A 150 ? 0.5689 0.6043 0.3777 -0.1373 -0.1199 -0.0169 153 PHE A N   
2384 C CA  . PHE A 150 ? 0.5622 0.5993 0.3376 -0.1705 -0.1435 -0.0221 153 PHE A CA  
2385 C C   . PHE A 150 ? 0.8887 0.8744 0.5882 -0.1804 -0.1414 -0.0443 153 PHE A C   
2386 O O   . PHE A 150 ? 1.0167 1.0144 0.6831 -0.1963 -0.1580 -0.0422 153 PHE A O   
2387 C CB  . PHE A 150 ? 0.7392 0.7710 0.5324 -0.1910 -0.1510 -0.0267 153 PHE A CB  
2388 C CG  . PHE A 150 ? 0.7710 0.8699 0.6234 -0.1965 -0.1655 -0.0025 153 PHE A CG  
2389 C CD1 . PHE A 150 ? 0.7217 0.8384 0.6265 -0.1787 -0.1527 0.0059  153 PHE A CD1 
2390 C CD2 . PHE A 150 ? 0.7014 0.8425 0.5619 -0.2089 -0.1829 0.0130  153 PHE A CD2 
2391 C CE1 . PHE A 150 ? 0.8703 1.0510 0.8279 -0.1791 -0.1625 0.0282  153 PHE A CE1 
2392 C CE2 . PHE A 150 ? 0.9158 1.1182 0.8339 -0.2049 -0.1886 0.0368  153 PHE A CE2 
2393 C CZ  . PHE A 150 ? 0.7309 0.9534 0.6960 -0.1893 -0.1781 0.0440  153 PHE A CZ  
2403 N N   . PHE A 151 ? 0.8823 0.8107 0.5540 -0.1682 -0.1198 -0.0649 154 PHE A N   
2404 C CA  . PHE A 151 ? 1.0862 0.9564 0.6803 -0.1741 -0.1146 -0.0896 154 PHE A CA  
2405 C C   . PHE A 151 ? 1.1209 0.9857 0.6928 -0.1446 -0.0911 -0.0902 154 PHE A C   
2406 O O   . PHE A 151 ? 1.3370 1.1508 0.8468 -0.1383 -0.0772 -0.1117 154 PHE A O   
2407 C CB  . PHE A 151 ? 0.9905 0.7965 0.5645 -0.1775 -0.1050 -0.1111 154 PHE A CB  
2408 C CG  . PHE A 151 ? 1.0216 0.8390 0.6301 -0.2030 -0.1231 -0.1043 154 PHE A CG  
2409 C CD1 . PHE A 151 ? 0.8687 0.7218 0.5360 -0.2039 -0.1260 -0.0892 154 PHE A CD1 
2410 C CD2 . PHE A 151 ? 1.0392 0.8347 0.6204 -0.2268 -0.1370 -0.1114 154 PHE A CD2 
2411 C CE1 . PHE A 151 ? 0.9928 0.8637 0.6931 -0.2254 -0.1392 -0.0795 154 PHE A CE1 
2412 C CE2 . PHE A 151 ? 1.1673 0.9777 0.7798 -0.2514 -0.1523 -0.1014 154 PHE A CE2 
2413 C CZ  . PHE A 151 ? 1.1242 0.9747 0.7970 -0.2497 -0.1522 -0.0845 154 PHE A CZ  
2423 N N   . GLY A 152 ? 1.2790 0.5167 0.9171 -0.0102 -0.1194 -0.1327 155 GLY A N   
2424 C CA  . GLY A 152 ? 1.2904 0.5943 0.9005 0.0514  -0.0819 -0.1378 155 GLY A CA  
2425 C C   . GLY A 152 ? 1.1877 0.6058 0.8210 0.0459  -0.0626 -0.1116 155 GLY A C   
2426 O O   . GLY A 152 ? 1.2289 0.6878 0.8127 0.0837  -0.0617 -0.1320 155 GLY A O   
2430 N N   . PHE A 153 ? 1.1108 0.5817 0.8148 0.0036  -0.0490 -0.0663 156 PHE A N   
2431 C CA  . PHE A 153 ? 1.0133 0.5917 0.7442 -0.0008 -0.0314 -0.0379 156 PHE A CA  
2432 C C   . PHE A 153 ? 1.2476 0.8347 0.9533 -0.0308 -0.0625 -0.0556 156 PHE A C   
2433 O O   . PHE A 153 ? 1.0562 0.7099 0.7397 -0.0114 -0.0563 -0.0604 156 PHE A O   
2434 C CB  . PHE A 153 ? 0.9053 0.5276 0.7091 -0.0263 -0.0135 0.0122  156 PHE A CB  
2435 C CG  . PHE A 153 ? 0.8478 0.4935 0.6835 0.0077  0.0145  0.0390  156 PHE A CG  
2436 C CD1 . PHE A 153 ? 0.8884 0.5103 0.6977 0.0514  0.0269  0.0234  156 PHE A CD1 
2437 C CD2 . PHE A 153 ? 0.8329 0.5244 0.7243 -0.0009 0.0231  0.0819  156 PHE A CD2 
2438 C CE1 . PHE A 153 ? 0.8358 0.4840 0.6849 0.0780  0.0482  0.0565  156 PHE A CE1 
2439 C CE2 . PHE A 153 ? 0.7834 0.4878 0.7091 0.0269  0.0367  0.1098  156 PHE A CE2 
2440 C CZ  . PHE A 153 ? 0.8448 0.5304 0.7551 0.0627  0.0498  0.1003  156 PHE A CZ  
2450 N N   . THR A 154 ? 1.1931 0.7194 0.9082 -0.0796 -0.0978 -0.0588 157 THR A N   
2451 C CA  . THR A 154 ? 1.2581 0.7891 0.9583 -0.1143 -0.1347 -0.0692 157 THR A CA  
2452 C C   . THR A 154 ? 1.2717 0.7716 0.8876 -0.0741 -0.1590 -0.1231 157 THR A C   
2453 O O   . THR A 154 ? 1.2581 0.8023 0.8542 -0.0787 -0.1716 -0.1308 157 THR A O   
2454 C CB  . THR A 154 ? 1.1886 0.6504 0.9165 -0.1711 -0.1775 -0.0585 157 THR A CB  
2455 O OG1 . THR A 154 ? 1.0863 0.5946 0.8865 -0.1985 -0.1515 -0.0040 157 THR A OG1 
2456 C CG2 . THR A 154 ? 1.3128 0.7744 1.0310 -0.2106 -0.2248 -0.0648 157 THR A CG2 
2464 N N   . SER A 155 ? 1.5418 0.9666 1.1014 -0.0277 -0.1664 -0.1615 158 SER A N   
2465 C CA  . SER A 155 ? 1.7592 1.1468 1.2221 0.0261  -0.1939 -0.2173 158 SER A CA  
2466 C C   . SER A 155 ? 1.7164 1.2223 1.1612 0.0784  -0.1497 -0.2084 158 SER A C   
2467 O O   . SER A 155 ? 1.6640 1.1833 1.0460 0.1063  -0.1704 -0.2388 158 SER A O   
2468 C CB  . SER A 155 ? 1.7080 0.9925 1.1109 0.0735  -0.2096 -0.2582 158 SER A CB  
2471 N N   . LYS A 156 ? 1.4856 1.0783 0.9872 0.0928  -0.0936 -0.1631 159 LYS A N   
2472 C CA  . LYS A 156 ? 1.5196 1.2335 1.0191 0.1391  -0.0548 -0.1414 159 LYS A CA  
2473 C C   . LYS A 156 ? 1.3946 1.1955 0.9412 0.0961  -0.0503 -0.1100 159 LYS A C   
2474 O O   . LYS A 156 ? 1.3591 1.2354 0.8768 0.1257  -0.0429 -0.1119 159 LYS A O   
2475 C CB  . LYS A 156 ? 1.3472 1.1179 0.8978 0.1680  -0.0076 -0.0978 159 LYS A CB  
2476 C CG  . LYS A 156 ? 1.4461 1.3169 0.9687 0.2424  0.0247  -0.0839 159 LYS A CG  
2477 C CD  . LYS A 156 ? 1.2282 1.1474 0.8082 0.2683  0.0630  -0.0348 159 LYS A CD  
2478 C CE  . LYS A 156 ? 1.1179 1.1890 0.7361 0.3066  0.0982  0.0230  159 LYS A CE  
2479 N NZ  . LYS A 156 ? 0.9969 1.1471 0.6502 0.2709  0.0950  0.0471  159 LYS A NZ  
2493 N N   . ALA A 157 ? 1.2976 1.0935 0.9133 0.0318  -0.0543 -0.0798 160 ALA A N   
2494 C CA  . ALA A 157 ? 1.0668 0.9438 0.7254 -0.0062 -0.0510 -0.0494 160 ALA A CA  
2495 C C   . ALA A 157 ? 1.2815 1.1518 0.8862 -0.0143 -0.0851 -0.0838 160 ALA A C   
2496 O O   . ALA A 157 ? 1.0546 1.0122 0.6643 -0.0122 -0.0747 -0.0701 160 ALA A O   
2497 C CB  . ALA A 157 ? 0.9705 0.8320 0.6951 -0.0637 -0.0555 -0.0168 160 ALA A CB  
2503 N N   . GLU A 158 ? 1.2206 0.9826 0.7742 -0.0242 -0.1319 -0.1278 161 GLU A N   
2504 C CA  . GLU A 158 ? 1.4050 1.1399 0.9072 -0.0358 -0.1788 -0.1621 161 GLU A CA  
2505 C C   . GLU A 158 ? 1.4337 1.2086 0.8557 0.0351  -0.1729 -0.1952 161 GLU A C   
2506 O O   . GLU A 158 ? 1.4264 1.1899 0.8006 0.0334  -0.2101 -0.2239 161 GLU A O   
2507 C CB  . GLU A 158 ? 1.5774 1.1722 1.0462 -0.0606 -0.2428 -0.1987 161 GLU A CB  
2508 C CG  . GLU A 158 ? 1.6412 1.2121 1.1934 -0.1366 -0.2558 -0.1570 161 GLU A CG  
2509 C CD  . GLU A 158 ? 1.8466 1.2955 1.3813 -0.1762 -0.3328 -0.1799 161 GLU A CD  
2510 O OE1 . GLU A 158 ? 2.0785 1.4439 1.5274 -0.1425 -0.3832 -0.2368 161 GLU A OE1 
2511 O OE2 . GLU A 158 ? 1.7099 1.1471 1.3167 -0.2380 -0.3472 -0.1377 161 GLU A OE2 
2518 N N   . SER A 159 ? 1.3367 1.1638 0.7442 0.0996  -0.1287 -0.1874 162 SER A N   
2519 C CA  . SER A 159 ? 1.4127 1.3064 0.7505 0.1769  -0.1134 -0.2047 162 SER A CA  
2520 C C   . SER A 159 ? 1.2974 1.3473 0.6993 0.1834  -0.0599 -0.1448 162 SER A C   
2521 O O   . SER A 159 ? 1.3455 1.4794 0.7105 0.2524  -0.0337 -0.1385 162 SER A O   
2522 C CB  . SER A 159 ? 1.5298 1.3811 0.7988 0.2570  -0.1057 -0.2335 162 SER A CB  
2523 O OG  . SER A 159 ? 1.4140 1.3045 0.7539 0.2569  -0.0597 -0.1868 162 SER A OG  
2529 N N   . MET A 160 ? 1.1906 1.2831 0.6864 0.1174  -0.0466 -0.0976 163 MET A N   
2530 C CA  . MET A 160 ? 1.0791 1.3035 0.6444 0.1160  -0.0077 -0.0380 163 MET A CA  
2531 C C   . MET A 160 ? 0.9890 1.2602 0.5750 0.0693  -0.0214 -0.0293 163 MET A C   
2532 O O   . MET A 160 ? 1.0557 1.2657 0.5992 0.0435  -0.0593 -0.0685 163 MET A O   
2533 C CB  . MET A 160 ? 0.9791 1.2073 0.6305 0.0897  0.0136  0.0094  163 MET A CB  
2534 C CG  . MET A 160 ? 1.2501 1.4159 0.8847 0.1254  0.0226  -0.0015 163 MET A CG  
2535 S SD  . MET A 160 ? 1.0184 1.2051 0.7528 0.1076  0.0469  0.0600  163 MET A SD  
2536 C CE  . MET A 160 ? 0.7871 1.1300 0.5729 0.1432  0.0768  0.1253  163 MET A CE  
2546 N N   . ARG A 161 ? 0.8837 1.2612 0.5385 0.0575  0.0042  0.0250  164 ARG A N   
2547 C CA  . ARG A 161 ? 0.8452 1.2748 0.5239 0.0155  -0.0059 0.0376  164 ARG A CA  
2548 C C   . ARG A 161 ? 0.8362 1.1858 0.5285 -0.0479 -0.0358 0.0231  164 ARG A C   
2549 O O   . ARG A 161 ? 0.8151 1.1052 0.5377 -0.0672 -0.0365 0.0313  164 ARG A O   
2550 C CB  . ARG A 161 ? 0.7355 1.2703 0.4966 0.0069  0.0178  0.1021  164 ARG A CB  
2551 C CG  . ARG A 161 ? 0.7113 1.3452 0.4844 0.0633  0.0464  0.1384  164 ARG A CG  
2552 C CD  . ARG A 161 ? 0.8242 1.5058 0.6915 0.0528  0.0574  0.2045  164 ARG A CD  
2553 N NE  . ARG A 161 ? 0.6924 1.4012 0.6137 0.0049  0.0423  0.2317  164 ARG A NE  
2554 C CZ  . ARG A 161 ? 0.6389 1.3742 0.6368 -0.0089 0.0358  0.2843  164 ARG A CZ  
2555 N NH1 . ARG A 161 ? 0.5325 1.2753 0.5736 0.0146  0.0424  0.3218  164 ARG A NH1 
2556 N NH2 . ARG A 161 ? 0.5561 1.3070 0.5862 -0.0445 0.0169  0.3002  164 ARG A NH2 
2570 N N   . PRO A 162 ? 0.6702 0.6340 0.3205 0.0231  -0.1741 -0.0279 165 PRO A N   
2571 C CA  . PRO A 162 ? 0.6447 0.6180 0.3204 0.0074  -0.1859 -0.0339 165 PRO A CA  
2572 C C   . PRO A 162 ? 0.6953 0.6919 0.4189 0.0078  -0.1815 -0.0240 165 PRO A C   
2573 O O   . PRO A 162 ? 0.6097 0.6067 0.3550 -0.0022 -0.1819 -0.0293 165 PRO A O   
2574 C CB  . PRO A 162 ? 0.6606 0.6492 0.3247 -0.0006 -0.2066 -0.0352 165 PRO A CB  
2575 C CG  . PRO A 162 ? 0.7934 0.7665 0.4133 0.0084  -0.2059 -0.0363 165 PRO A CG  
2576 C CD  . PRO A 162 ? 0.7246 0.6903 0.3430 0.0252  -0.1856 -0.0274 165 PRO A CD  
2584 N N   . GLU A 163 ? 0.6035 0.6173 0.3421 0.0186  -0.1770 -0.0097 166 GLU A N   
2585 C CA  . GLU A 163 ? 0.6296 0.6609 0.4100 0.0194  -0.1721 -0.0011 166 GLU A CA  
2586 C C   . GLU A 163 ? 0.5631 0.5813 0.3543 0.0212  -0.1552 -0.0026 166 GLU A C   
2587 O O   . GLU A 163 ? 0.5869 0.6137 0.4091 0.0171  -0.1524 -0.0013 166 GLU A O   
2588 C CB  . GLU A 163 ? 0.6858 0.7328 0.4748 0.0302  -0.1712 0.0144  166 GLU A CB  
2589 C CG  . GLU A 163 ? 0.7682 0.8037 0.5412 0.0412  -0.1566 0.0223  166 GLU A CG  
2590 C CD  . GLU A 163 ? 0.9593 0.9864 0.6928 0.0465  -0.1603 0.0217  166 GLU A CD  
2591 O OE1 . GLU A 163 ? 0.8296 0.8509 0.5421 0.0402  -0.1714 0.0107  166 GLU A OE1 
2592 O OE2 . GLU A 163 ? 1.0713 1.0969 0.7930 0.0560  -0.1520 0.0323  166 GLU A OE2 
2599 N N   . VAL A 164 ? 0.5977 0.5972 0.3635 0.0282  -0.1437 -0.0048 167 VAL A N   
2600 C CA  . VAL A 164 ? 0.5620 0.5516 0.3364 0.0303  -0.1288 -0.0066 167 VAL A CA  
2601 C C   . VAL A 164 ? 0.5009 0.4766 0.2753 0.0204  -0.1320 -0.0194 167 VAL A C   
2602 O O   . VAL A 164 ? 0.5127 0.4906 0.3117 0.0170  -0.1262 -0.0196 167 VAL A O   
2603 C CB  . VAL A 164 ? 0.6077 0.5852 0.3548 0.0419  -0.1156 -0.0045 167 VAL A CB  
2604 C CG1 . VAL A 164 ? 0.6494 0.6185 0.4030 0.0449  -0.1014 -0.0070 167 VAL A CG1 
2605 C CG2 . VAL A 164 ? 0.6423 0.6343 0.3937 0.0495  -0.1103 0.0100  167 VAL A CG2 
2615 N N   . ALA A 165 ? 0.6224 0.5819 0.3674 0.0147  -0.1415 -0.0301 168 ALA A N   
2616 C CA  . ALA A 165 ? 0.6235 0.5638 0.3630 0.0037  -0.1443 -0.0426 168 ALA A CA  
2617 C C   . ALA A 165 ? 0.5842 0.5437 0.3604 -0.0094 -0.1527 -0.0420 168 ALA A C   
2618 O O   . ALA A 165 ? 0.5871 0.5390 0.3771 -0.0147 -0.1472 -0.0456 168 ALA A O   
2619 C CB  . ALA A 165 ? 0.6361 0.5541 0.3342 -0.0024 -0.1547 -0.0544 168 ALA A CB  
2625 N N   . SER A 166 ? 0.5518 0.5373 0.3437 -0.0137 -0.1656 -0.0366 169 SER A N   
2626 C CA  . SER A 166 ? 0.5587 0.5659 0.3846 -0.0254 -0.1739 -0.0357 169 SER A CA  
2627 C C   . SER A 166 ? 0.5548 0.5748 0.4159 -0.0195 -0.1625 -0.0272 169 SER A C   
2628 O O   . SER A 166 ? 0.5288 0.5526 0.4120 -0.0280 -0.1613 -0.0297 169 SER A O   
2629 C CB  . SER A 166 ? 0.7051 0.7400 0.5378 -0.0289 -0.1905 -0.0310 169 SER A CB  
2630 O OG  . SER A 166 ? 0.7737 0.8254 0.6175 -0.0146 -0.1870 -0.0179 169 SER A OG  
2636 N N   . THR A 167 ? 0.5096 0.5350 0.3747 -0.0061 -0.1536 -0.0171 170 THR A N   
2637 C CA  . THR A 167 ? 0.4541 0.4879 0.3482 -0.0018 -0.1427 -0.0100 170 THR A CA  
2638 C C   . THR A 167 ? 0.4896 0.5055 0.3821 -0.0029 -0.1306 -0.0155 170 THR A C   
2639 O O   . THR A 167 ? 0.4541 0.4756 0.3712 -0.0067 -0.1262 -0.0150 170 THR A O   
2640 C CB  . THR A 167 ? 0.4412 0.4804 0.3351 0.0102  -0.1360 0.0015  170 THR A CB  
2641 O OG1 . THR A 167 ? 0.4992 0.5548 0.3958 0.0126  -0.1470 0.0079  170 THR A OG1 
2642 C CG2 . THR A 167 ? 0.4737 0.5176 0.3933 0.0128  -0.1245 0.0078  170 THR A CG2 
2650 N N   . PHE A 168 ? 0.4503 0.4453 0.3135 0.0020  -0.1246 -0.0201 171 PHE A N   
2651 C CA  . PHE A 168 ? 0.4626 0.4407 0.3222 0.0033  -0.1132 -0.0246 171 PHE A CA  
2652 C C   . PHE A 168 ? 0.4604 0.4298 0.3262 -0.0094 -0.1184 -0.0333 171 PHE A C   
2653 O O   . PHE A 168 ? 0.4778 0.4472 0.3616 -0.0112 -0.1113 -0.0328 171 PHE A O   
2654 C CB  . PHE A 168 ? 0.4915 0.4475 0.3145 0.0125  -0.1064 -0.0286 171 PHE A CB  
2655 C CG  . PHE A 168 ? 0.5503 0.4874 0.3666 0.0157  -0.0953 -0.0332 171 PHE A CG  
2656 C CD1 . PHE A 168 ? 0.5356 0.4830 0.3700 0.0227  -0.0831 -0.0261 171 PHE A CD1 
2657 C CD2 . PHE A 168 ? 0.5963 0.5049 0.3874 0.0111  -0.0978 -0.0445 171 PHE A CD2 
2658 C CE1 . PHE A 168 ? 0.5577 0.4901 0.3862 0.0272  -0.0734 -0.0291 171 PHE A CE1 
2659 C CE2 . PHE A 168 ? 0.6176 0.5063 0.4006 0.0158  -0.0872 -0.0477 171 PHE A CE2 
2660 C CZ  . PHE A 168 ? 0.5668 0.4693 0.3698 0.0247  -0.0752 -0.0395 171 PHE A CZ  
2670 N N   . LYS A 169 ? 0.5102 0.4718 0.3598 -0.0195 -0.1309 -0.0412 172 LYS A N   
2671 C CA  . LYS A 169 ? 0.5150 0.4666 0.3679 -0.0344 -0.1359 -0.0495 172 LYS A CA  
2672 C C   . LYS A 169 ? 0.5341 0.5106 0.4276 -0.0406 -0.1363 -0.0440 172 LYS A C   
2673 O O   . LYS A 169 ? 0.5085 0.4765 0.4114 -0.0465 -0.1309 -0.0466 172 LYS A O   
2674 C CB  . LYS A 169 ? 0.4925 0.4389 0.3249 -0.0474 -0.1518 -0.0575 172 LYS A CB  
2677 N N   . VAL A 170 ? 0.4476 0.4537 0.3641 -0.0381 -0.1417 -0.0358 173 VAL A N   
2678 C CA  . VAL A 170 ? 0.4049 0.4348 0.3585 -0.0419 -0.1413 -0.0304 173 VAL A CA  
2679 C C   . VAL A 170 ? 0.3951 0.4205 0.3614 -0.0340 -0.1264 -0.0263 173 VAL A C   
2680 O O   . VAL A 170 ? 0.3779 0.4062 0.3627 -0.0397 -0.1224 -0.0269 173 VAL A O   
2681 C CB  . VAL A 170 ? 0.4354 0.4947 0.4067 -0.0373 -0.1491 -0.0218 173 VAL A CB  
2682 C CG1 . VAL A 170 ? 0.4452 0.5265 0.4522 -0.0368 -0.1456 -0.0155 173 VAL A CG1 
2683 C CG2 . VAL A 170 ? 0.5031 0.5733 0.4656 -0.0473 -0.1659 -0.0255 173 VAL A CG2 
2693 N N   . LEU A 171 ? 0.3585 0.3790 0.3153 -0.0215 -0.1181 -0.0214 174 LEU A N   
2694 C CA  . LEU A 171 ? 0.3836 0.4034 0.3525 -0.0154 -0.1050 -0.0170 174 LEU A CA  
2695 C C   . LEU A 171 ? 0.4029 0.4024 0.3605 -0.0168 -0.0975 -0.0230 174 LEU A C   
2696 O O   . LEU A 171 ? 0.3864 0.3882 0.3593 -0.0169 -0.0899 -0.0211 174 LEU A O   
2697 C CB  . LEU A 171 ? 0.3716 0.3929 0.3321 -0.0041 -0.0986 -0.0100 174 LEU A CB  
2698 C CG  . LEU A 171 ? 0.3851 0.4230 0.3571 -0.0009 -0.1032 -0.0020 174 LEU A CG  
2699 C CD1 . LEU A 171 ? 0.4737 0.5091 0.4326 0.0079  -0.0966 0.0048  174 LEU A CD1 
2700 C CD2 . LEU A 171 ? 0.3865 0.4372 0.3876 -0.0026 -0.1005 0.0021  174 LEU A CD2 
2712 N N   A ARG A 172 ? 0.3849 0.3627 0.3131 -0.0169 -0.0991 -0.0299 175 ARG A N   
2713 N N   B ARG A 172 ? 0.3888 0.3666 0.3174 -0.0172 -0.0993 -0.0300 175 ARG A N   
2714 C CA  A ARG A 172 ? 0.4259 0.3794 0.3394 -0.0172 -0.0922 -0.0356 175 ARG A CA  
2715 C CA  B ARG A 172 ? 0.4278 0.3816 0.3419 -0.0171 -0.0919 -0.0354 175 ARG A CA  
2716 C C   A ARG A 172 ? 0.4309 0.3840 0.3608 -0.0306 -0.0953 -0.0390 175 ARG A C   
2717 C C   B ARG A 172 ? 0.4356 0.3872 0.3641 -0.0307 -0.0953 -0.0394 175 ARG A C   
2718 O O   A ARG A 172 ? 0.4238 0.3704 0.3604 -0.0296 -0.0868 -0.0381 175 ARG A O   
2719 O O   B ARG A 172 ? 0.4222 0.3648 0.3547 -0.0299 -0.0869 -0.0392 175 ARG A O   
2720 C CB  A ARG A 172 ? 0.5365 0.4624 0.4116 -0.0156 -0.0946 -0.0436 175 ARG A CB  
2721 C CB  B ARG A 172 ? 0.5294 0.4558 0.4050 -0.0139 -0.0930 -0.0427 175 ARG A CB  
2722 C CG  A ARG A 172 ? 0.5439 0.4365 0.3975 -0.0177 -0.0894 -0.0511 175 ARG A CG  
2723 C CG  B ARG A 172 ? 0.5383 0.4346 0.3932 -0.0098 -0.0837 -0.0477 175 ARG A CG  
2724 C CD  A ARG A 172 ? 0.5820 0.4450 0.3985 -0.0235 -0.0967 -0.0616 175 ARG A CD  
2725 C CD  B ARG A 172 ? 0.6257 0.4946 0.4610 -0.0238 -0.0913 -0.0582 175 ARG A CD  
2726 N NE  A ARG A 172 ? 0.6584 0.5267 0.4823 -0.0434 -0.1113 -0.0668 175 ARG A NE  
2727 N NE  B ARG A 172 ? 0.5895 0.4408 0.3915 -0.0243 -0.0983 -0.0652 175 ARG A NE  
2728 C CZ  A ARG A 172 ? 0.6356 0.4832 0.4306 -0.0536 -0.1212 -0.0762 175 ARG A CZ  
2729 C CZ  B ARG A 172 ? 0.6934 0.5480 0.4918 -0.0393 -0.1129 -0.0705 175 ARG A CZ  
2730 N NH1 A ARG A 172 ? 0.7231 0.5392 0.4774 -0.0447 -0.1174 -0.0823 175 ARG A NH1 
2731 N NH1 B ARG A 172 ? 0.5996 0.4773 0.4278 -0.0544 -0.1220 -0.0690 175 ARG A NH1 
2732 N NH2 A ARG A 172 ? 0.7366 0.5964 0.5433 -0.0734 -0.1351 -0.0794 175 ARG A NH2 
2733 N NH2 B ARG A 172 ? 0.6707 0.5070 0.4344 -0.0386 -0.1185 -0.0772 175 ARG A NH2 
2760 N N   . ASN A 173 ? 0.4354 0.3967 0.3712 -0.0435 -0.1077 -0.0423 176 ASN A N   
2761 C CA  . ASN A 173 ? 0.4626 0.4264 0.4143 -0.0581 -0.1108 -0.0449 176 ASN A CA  
2762 C C   . ASN A 173 ? 0.4218 0.4094 0.4077 -0.0561 -0.1050 -0.0375 176 ASN A C   
2763 O O   . ASN A 173 ? 0.4125 0.3947 0.4072 -0.0620 -0.0998 -0.0382 176 ASN A O   
2764 C CB  . ASN A 173 ? 0.4800 0.4563 0.4339 -0.0726 -0.1262 -0.0484 176 ASN A CB  
2765 C CG  . ASN A 173 ? 0.5948 0.5417 0.5114 -0.0793 -0.1326 -0.0581 176 ASN A CG  
2766 O OD1 . ASN A 173 ? 0.5756 0.4896 0.4644 -0.0727 -0.1242 -0.0625 176 ASN A OD1 
2767 N ND2 . ASN A 173 ? 0.6244 0.5830 0.5385 -0.0917 -0.1473 -0.0613 176 ASN A ND2 
2774 N N   . VAL A 174 ? 0.3594 0.3703 0.3624 -0.0479 -0.1052 -0.0304 177 VAL A N   
2775 C CA  . VAL A 174 ? 0.3054 0.3341 0.3359 -0.0448 -0.0987 -0.0242 177 VAL A CA  
2776 C C   . VAL A 174 ? 0.3425 0.3575 0.3684 -0.0384 -0.0862 -0.0233 177 VAL A C   
2777 O O   . VAL A 174 ? 0.3478 0.3658 0.3883 -0.0417 -0.0807 -0.0222 177 VAL A O   
2778 C CB  . VAL A 174 ? 0.3375 0.3857 0.3799 -0.0360 -0.1003 -0.0171 177 VAL A CB  
2779 C CG1 . VAL A 174 ? 0.3964 0.4541 0.4587 -0.0311 -0.0914 -0.0116 177 VAL A CG1 
2780 C CG2 . VAL A 174 ? 0.3498 0.4182 0.4030 -0.0411 -0.1125 -0.0160 177 VAL A CG2 
2790 N N   . THR A 175 ? 0.3431 0.3457 0.3490 -0.0288 -0.0813 -0.0228 178 THR A N   
2791 C CA  . THR A 175 ? 0.3518 0.3470 0.3538 -0.0212 -0.0699 -0.0205 178 THR A CA  
2792 C C   . THR A 175 ? 0.3647 0.3406 0.3583 -0.0255 -0.0662 -0.0249 178 THR A C   
2793 O O   . THR A 175 ? 0.3681 0.3461 0.3719 -0.0244 -0.0590 -0.0222 178 THR A O   
2794 C CB  . THR A 175 ? 0.3864 0.3753 0.3678 -0.0101 -0.0660 -0.0188 178 THR A CB  
2795 O OG1 . THR A 175 ? 0.3799 0.3856 0.3693 -0.0070 -0.0685 -0.0133 178 THR A OG1 
2796 C CG2 . THR A 175 ? 0.3886 0.3748 0.3665 -0.0015 -0.0547 -0.0154 178 THR A CG2 
2804 N N   . VAL A 176 ? 0.3431 0.2973 0.3152 -0.0306 -0.0709 -0.0317 179 VAL A N   
2805 C CA  . VAL A 176 ? 0.3589 0.2875 0.3173 -0.0340 -0.0661 -0.0356 179 VAL A CA  
2806 C C   . VAL A 176 ? 0.3804 0.3185 0.3619 -0.0458 -0.0665 -0.0345 179 VAL A C   
2807 O O   . VAL A 176 ? 0.4322 0.3601 0.4135 -0.0446 -0.0585 -0.0329 179 VAL A O   
2808 C CB  . VAL A 176 ? 0.4844 0.3830 0.4114 -0.0392 -0.0714 -0.0441 179 VAL A CB  
2809 C CG1 . VAL A 176 ? 0.5784 0.4478 0.4923 -0.0472 -0.0681 -0.0483 179 VAL A CG1 
2810 C CG2 . VAL A 176 ? 0.5579 0.4433 0.4584 -0.0237 -0.0668 -0.0445 179 VAL A CG2 
2820 N N   . VAL A 177 ? 0.3532 0.3120 0.3544 -0.0567 -0.0754 -0.0346 180 VAL A N   
2821 C CA  . VAL A 177 ? 0.3280 0.2993 0.3519 -0.0677 -0.0753 -0.0331 180 VAL A CA  
2822 C C   . VAL A 177 ? 0.3393 0.3277 0.3838 -0.0596 -0.0667 -0.0265 180 VAL A C   
2823 O O   . VAL A 177 ? 0.3676 0.3525 0.4183 -0.0625 -0.0601 -0.0249 180 VAL A O   
2824 C CB  . VAL A 177 ? 0.4112 0.4062 0.4524 -0.0791 -0.0869 -0.0336 180 VAL A CB  
2825 C CG1 . VAL A 177 ? 0.4464 0.4614 0.5152 -0.0882 -0.0851 -0.0302 180 VAL A CG1 
2826 C CG2 . VAL A 177 ? 0.4775 0.4547 0.4968 -0.0910 -0.0965 -0.0409 180 VAL A CG2 
2836 N N   . LEU A 178 ? 0.2776 0.2833 0.3311 -0.0501 -0.0664 -0.0225 181 LEU A N   
2837 C CA  . LEU A 178 ? 0.2844 0.3048 0.3555 -0.0448 -0.0592 -0.0173 181 LEU A CA  
2838 C C   . LEU A 178 ? 0.2887 0.2968 0.3485 -0.0373 -0.0498 -0.0156 181 LEU A C   
2839 O O   . LEU A 178 ? 0.2850 0.2968 0.3541 -0.0378 -0.0436 -0.0132 181 LEU A O   
2840 C CB  . LEU A 178 ? 0.2644 0.3014 0.3444 -0.0378 -0.0612 -0.0135 181 LEU A CB  
2841 C CG  . LEU A 178 ? 0.3384 0.3928 0.4331 -0.0417 -0.0697 -0.0128 181 LEU A CG  
2842 C CD1 . LEU A 178 ? 0.3251 0.3886 0.4225 -0.0328 -0.0704 -0.0083 181 LEU A CD1 
2843 C CD2 . LEU A 178 ? 0.3705 0.4395 0.4874 -0.0476 -0.0679 -0.0115 181 LEU A CD2 
2855 N N   . TRP A 179 ? 0.2551 0.2500 0.2940 -0.0293 -0.0483 -0.0163 182 TRP A N   
2856 C CA  . TRP A 179 ? 0.2809 0.2703 0.3111 -0.0201 -0.0393 -0.0130 182 TRP A CA  
2857 C C   . TRP A 179 ? 0.2863 0.2577 0.3090 -0.0229 -0.0347 -0.0142 182 TRP A C   
2858 O O   . TRP A 179 ? 0.3022 0.2764 0.3276 -0.0181 -0.0276 -0.0101 182 TRP A O   
2859 C CB  . TRP A 179 ? 0.2802 0.2620 0.2901 -0.0095 -0.0376 -0.0125 182 TRP A CB  
2860 C CG  . TRP A 179 ? 0.2619 0.2622 0.2781 -0.0054 -0.0390 -0.0088 182 TRP A CG  
2861 C CD1 . TRP A 179 ? 0.2825 0.2961 0.3128 -0.0107 -0.0449 -0.0083 182 TRP A CD1 
2862 C CD2 . TRP A 179 ? 0.2631 0.2704 0.2705 0.0049  -0.0337 -0.0041 182 TRP A CD2 
2863 N NE1 . TRP A 179 ? 0.2899 0.3139 0.3184 -0.0051 -0.0438 -0.0038 182 TRP A NE1 
2864 C CE2 . TRP A 179 ? 0.2721 0.2943 0.2879 0.0032  -0.0371 -0.0012 182 TRP A CE2 
2865 C CE3 . TRP A 179 ? 0.3333 0.3366 0.3267 0.0157  -0.0264 -0.0014 182 TRP A CE3 
2866 C CZ2 . TRP A 179 ? 0.3158 0.3493 0.3269 0.0096  -0.0332 0.0042  182 TRP A CZ2 
2867 C CZ3 . TRP A 179 ? 0.3381 0.3576 0.3290 0.0235  -0.0225 0.0045  182 TRP A CZ3 
2868 C CH2 . TRP A 179 ? 0.2877 0.3217 0.2876 0.0190  -0.0261 0.0070  182 TRP A CH2 
2879 N N   . SER A 180 ? 0.3064 0.2582 0.3180 -0.0312 -0.0389 -0.0196 183 SER A N   
2880 C CA  . SER A 180 ? 0.3278 0.2568 0.3286 -0.0352 -0.0342 -0.0205 183 SER A CA  
2881 C C   . SER A 180 ? 0.3271 0.2700 0.3493 -0.0423 -0.0312 -0.0171 183 SER A C   
2882 O O   . SER A 180 ? 0.3401 0.2681 0.3549 -0.0421 -0.0247 -0.0151 183 SER A O   
2883 C CB  . SER A 180 ? 0.3757 0.2806 0.3603 -0.0470 -0.0406 -0.0275 183 SER A CB  
2884 O OG  . SER A 180 ? 0.4717 0.3574 0.4300 -0.0388 -0.0416 -0.0311 183 SER A OG  
2890 N N   . ALA A 181 ? 0.2926 0.2621 0.3393 -0.0473 -0.0349 -0.0159 184 ALA A N   
2891 C CA  . ALA A 181 ? 0.2757 0.2587 0.3416 -0.0528 -0.0309 -0.0128 184 ALA A CA  
2892 C C   . ALA A 181 ? 0.2703 0.2606 0.3383 -0.0429 -0.0230 -0.0079 184 ALA A C   
2893 O O   . ALA A 181 ? 0.2996 0.2911 0.3733 -0.0457 -0.0176 -0.0053 184 ALA A O   
2894 C CB  . ALA A 181 ? 0.2754 0.2845 0.3654 -0.0586 -0.0364 -0.0127 184 ALA A CB  
2900 N N   . TYR A 182 ? 0.2466 0.2424 0.3090 -0.0325 -0.0223 -0.0063 185 TYR A N   
2901 C CA  . TYR A 182 ? 0.2460 0.2535 0.3118 -0.0256 -0.0163 -0.0016 185 TYR A CA  
2902 C C   . TYR A 182 ? 0.2529 0.2475 0.3066 -0.0212 -0.0095 0.0016  185 TYR A C   
2903 O O   . TYR A 182 ? 0.2707 0.2741 0.3317 -0.0219 -0.0051 0.0047  185 TYR A O   
2904 C CB  . TYR A 182 ? 0.2284 0.2456 0.2899 -0.0173 -0.0172 0.0002  185 TYR A CB  
2905 C CG  . TYR A 182 ? 0.2182 0.2500 0.2925 -0.0205 -0.0220 -0.0007 185 TYR A CG  
2906 C CD1 . TYR A 182 ? 0.2550 0.2842 0.3297 -0.0233 -0.0286 -0.0038 185 TYR A CD1 
2907 C CD2 . TYR A 182 ? 0.2141 0.2606 0.2975 -0.0205 -0.0199 0.0019  185 TYR A CD2 
2908 C CE1 . TYR A 182 ? 0.2570 0.2979 0.3415 -0.0241 -0.0324 -0.0033 185 TYR A CE1 
2909 C CE2 . TYR A 182 ? 0.2123 0.2664 0.3035 -0.0224 -0.0232 0.0015  185 TYR A CE2 
2910 C CZ  . TYR A 182 ? 0.2002 0.2518 0.2924 -0.0232 -0.0291 -0.0005 185 TYR A CZ  
2911 O OH  . TYR A 182 ? 0.2215 0.2794 0.3200 -0.0233 -0.0319 0.0003  185 TYR A OH  
2921 N N   . PRO A 183 ? 0.2851 0.2579 0.3187 -0.0157 -0.0077 0.0013  186 PRO A N   
2922 C CA  . PRO A 183 ? 0.2662 0.2248 0.2868 -0.0096 -0.0004 0.0057  186 PRO A CA  
2923 C C   . PRO A 183 ? 0.2779 0.2274 0.3034 -0.0204 0.0017  0.0057  186 PRO A C   
2924 O O   . PRO A 183 ? 0.3155 0.2621 0.3370 -0.0168 0.0079  0.0106  186 PRO A O   
2925 C CB  . PRO A 183 ? 0.3263 0.2576 0.3212 -0.0010 0.0009  0.0043  186 PRO A CB  
2926 C CG  . PRO A 183 ? 0.3529 0.2813 0.3475 -0.0073 -0.0068 -0.0024 186 PRO A CG  
2927 C CD  . PRO A 183 ? 0.2950 0.2550 0.3133 -0.0113 -0.0113 -0.0020 186 PRO A CD  
2935 N N   . VAL A 184 ? 0.2986 0.2452 0.3327 -0.0340 -0.0033 0.0008  187 VAL A N   
2936 C CA  . VAL A 184 ? 0.3039 0.2467 0.3453 -0.0460 -0.0008 0.0018  187 VAL A CA  
2937 C C   . VAL A 184 ? 0.2866 0.2561 0.3484 -0.0464 0.0022  0.0051  187 VAL A C   
2938 O O   . VAL A 184 ? 0.3081 0.2753 0.3697 -0.0481 0.0086  0.0091  187 VAL A O   
2939 C CB  . VAL A 184 ? 0.3331 0.2726 0.3807 -0.0610 -0.0078 -0.0034 187 VAL A CB  
2940 C CG1 . VAL A 184 ? 0.3684 0.3087 0.4262 -0.0752 -0.0046 -0.0014 187 VAL A CG1 
2941 C CG2 . VAL A 184 ? 0.3811 0.2894 0.4036 -0.0619 -0.0109 -0.0079 187 VAL A CG2 
2951 N N   . VAL A 185 ? 0.2422 0.2346 0.3193 -0.0451 -0.0018 0.0033  188 VAL A N   
2952 C CA  . VAL A 185 ? 0.2281 0.2416 0.3207 -0.0449 0.0014  0.0053  188 VAL A CA  
2953 C C   . VAL A 185 ? 0.2823 0.2965 0.3652 -0.0363 0.0072  0.0098  188 VAL A C   
2954 O O   . VAL A 185 ? 0.2958 0.3160 0.3824 -0.0377 0.0124  0.0124  188 VAL A O   
2955 C CB  . VAL A 185 ? 0.2614 0.2925 0.3665 -0.0434 -0.0036 0.0027  188 VAL A CB  
2956 C CG1 . VAL A 185 ? 0.2864 0.3330 0.4014 -0.0419 0.0006  0.0040  188 VAL A CG1 
2957 C CG2 . VAL A 185 ? 0.3011 0.3363 0.4176 -0.0513 -0.0096 -0.0004 188 VAL A CG2 
2967 N N   . TRP A 186 ? 0.2606 0.2709 0.3307 -0.0270 0.0063  0.0111  189 TRP A N   
2968 C CA  . TRP A 186 ? 0.2476 0.2639 0.3094 -0.0184 0.0107  0.0164  189 TRP A CA  
2969 C C   . TRP A 186 ? 0.2787 0.2793 0.3296 -0.0172 0.0170  0.0209  189 TRP A C   
2970 O O   . TRP A 186 ? 0.2892 0.2982 0.3396 -0.0153 0.0212  0.0250  189 TRP A O   
2971 C CB  . TRP A 186 ? 0.2452 0.2624 0.2965 -0.0081 0.0088  0.0180  189 TRP A CB  
2972 C CG  . TRP A 186 ? 0.2532 0.2872 0.2998 0.0009  0.0111  0.0239  189 TRP A CG  
2973 C CD1 . TRP A 186 ? 0.2868 0.3430 0.3400 0.0009  0.0081  0.0244  189 TRP A CD1 
2974 C CD2 . TRP A 186 ? 0.2372 0.2679 0.2707 0.0111  0.0163  0.0309  189 TRP A CD2 
2975 N NE1 . TRP A 186 ? 0.2544 0.3254 0.3015 0.0088  0.0104  0.0310  189 TRP A NE1 
2976 C CE2 . TRP A 186 ? 0.2778 0.3349 0.3132 0.0166  0.0153  0.0354  189 TRP A CE2 
2977 C CE3 . TRP A 186 ? 0.2777 0.2860 0.2974 0.0158  0.0216  0.0344  189 TRP A CE3 
2978 C CZ2 . TRP A 186 ? 0.2787 0.3444 0.3044 0.0279  0.0189  0.0437  189 TRP A CZ2 
2979 C CZ3 . TRP A 186 ? 0.3502 0.3622 0.3583 0.0282  0.0260  0.0426  189 TRP A CZ3 
2980 C CH2 . TRP A 186 ? 0.3271 0.3697 0.3389 0.0350  0.0245  0.0475  189 TRP A CH2 
2991 N N   . LEU A 187 ? 0.3012 0.2767 0.3408 -0.0187 0.0176  0.0201  190 LEU A N   
2992 C CA  . LEU A 187 ? 0.3022 0.2563 0.3268 -0.0169 0.0242  0.0250  190 LEU A CA  
2993 C C   . LEU A 187 ? 0.3960 0.3548 0.4312 -0.0277 0.0279  0.0264  190 LEU A C   
2994 O O   . LEU A 187 ? 0.3595 0.3146 0.3869 -0.0241 0.0342  0.0324  190 LEU A O   
2995 C CB  . LEU A 187 ? 0.3727 0.2942 0.3802 -0.0187 0.0236  0.0225  190 LEU A CB  
2996 C CG  . LEU A 187 ? 0.4123 0.3020 0.3980 -0.0161 0.0309  0.0276  190 LEU A CG  
2997 C CD1 . LEU A 187 ? 0.4652 0.3541 0.4351 0.0038  0.0358  0.0350  190 LEU A CD1 
2998 C CD2 . LEU A 187 ? 0.5010 0.3548 0.4692 -0.0227 0.0292  0.0226  190 LEU A CD2 
3010 N N   . ILE A 188 ? 0.3263 0.2957 0.3797 -0.0398 0.0246  0.0216  191 ILE A N   
3011 C CA  . ILE A 188 ? 0.3090 0.2855 0.3735 -0.0495 0.0294  0.0236  191 ILE A CA  
3012 C C   . ILE A 188 ? 0.3158 0.3181 0.3929 -0.0467 0.0311  0.0238  191 ILE A C   
3013 O O   . ILE A 188 ? 0.3577 0.3668 0.4412 -0.0516 0.0368  0.0262  191 ILE A O   
3014 C CB  . ILE A 188 ? 0.3240 0.3012 0.4021 -0.0642 0.0259  0.0197  191 ILE A CB  
3015 C CG1 . ILE A 188 ? 0.4063 0.4068 0.5029 -0.0644 0.0192  0.0146  191 ILE A CG1 
3016 C CG2 . ILE A 188 ? 0.4947 0.4420 0.5560 -0.0692 0.0234  0.0181  191 ILE A CG2 
3017 C CD1 . ILE A 188 ? 0.6115 0.6160 0.7206 -0.0769 0.0135  0.0112  191 ILE A CD1 
3029 N N   . GLY A 189 ? 0.3253 0.3407 0.4041 -0.0394 0.0270  0.0215  192 GLY A N   
3030 C CA  . GLY A 189 ? 0.2795 0.3145 0.3666 -0.0381 0.0279  0.0203  192 GLY A CA  
3031 C C   . GLY A 189 ? 0.2838 0.3232 0.3588 -0.0313 0.0313  0.0246  192 GLY A C   
3032 O O   . GLY A 189 ? 0.3503 0.3791 0.4120 -0.0269 0.0348  0.0302  192 GLY A O   
3036 N N   A SER A 190 ? 0.3184 0.3729 0.3965 -0.0306 0.0300  0.0221  193 SER A N   
3037 N N   B SER A 190 ? 0.3200 0.3745 0.3980 -0.0306 0.0300  0.0221  193 SER A N   
3038 C CA  A SER A 190 ? 0.3515 0.4140 0.4185 -0.0269 0.0324  0.0254  193 SER A CA  
3039 C CA  B SER A 190 ? 0.3524 0.4150 0.4195 -0.0269 0.0323  0.0254  193 SER A CA  
3040 C C   A SER A 190 ? 0.3902 0.4551 0.4458 -0.0188 0.0295  0.0303  193 SER A C   
3041 C C   B SER A 190 ? 0.3891 0.4548 0.4449 -0.0189 0.0293  0.0301  193 SER A C   
3042 O O   A SER A 190 ? 0.4370 0.5070 0.4816 -0.0141 0.0318  0.0359  193 SER A O   
3043 O O   B SER A 190 ? 0.4314 0.5037 0.4766 -0.0146 0.0312  0.0352  193 SER A O   
3044 C CB  A SER A 190 ? 0.3681 0.4426 0.4383 -0.0301 0.0309  0.0203  193 SER A CB  
3045 C CB  B SER A 190 ? 0.3681 0.4425 0.4386 -0.0302 0.0311  0.0203  193 SER A CB  
3046 O OG  A SER A 190 ? 0.3888 0.4681 0.4620 -0.0301 0.0244  0.0173  193 SER A OG  
3047 O OG  B SER A 190 ? 0.3817 0.4551 0.4578 -0.0339 0.0368  0.0181  193 SER A OG  
3058 N N   . GLU A 191 ? 0.2979 0.3613 0.3554 -0.0160 0.0247  0.0291  194 GLU A N   
3059 C CA  . GLU A 191 ? 0.3260 0.3939 0.3734 -0.0062 0.0231  0.0345  194 GLU A CA  
3060 C C   . GLU A 191 ? 0.3571 0.4065 0.3919 0.0018  0.0278  0.0405  194 GLU A C   
3061 O O   . GLU A 191 ? 0.3367 0.3910 0.3606 0.0130  0.0287  0.0473  194 GLU A O   
3062 C CB  . GLU A 191 ? 0.3093 0.3800 0.3610 -0.0048 0.0179  0.0317  194 GLU A CB  
3063 C CG  . GLU A 191 ? 0.3302 0.4180 0.3900 -0.0109 0.0133  0.0278  194 GLU A CG  
3064 C CD  . GLU A 191 ? 0.4545 0.5351 0.5253 -0.0195 0.0122  0.0207  194 GLU A CD  
3065 O OE1 . GLU A 191 ? 0.4080 0.4752 0.4823 -0.0214 0.0146  0.0193  194 GLU A OE1 
3066 O OE2 . GLU A 191 ? 0.4977 0.5861 0.5731 -0.0242 0.0090  0.0173  194 GLU A OE2 
3073 N N   . GLY A 192 ? 0.3345 0.3626 0.3697 -0.0037 0.0310  0.0387  195 GLY A N   
3074 C CA  . GLY A 192 ? 0.3483 0.3512 0.3685 0.0018  0.0356  0.0435  195 GLY A CA  
3075 C C   . GLY A 192 ? 0.3974 0.3895 0.4130 -0.0027 0.0422  0.0475  195 GLY A C   
3076 O O   . GLY A 192 ? 0.3823 0.3857 0.3929 0.0017  0.0451  0.0528  195 GLY A O   
3080 N N   . ALA A 193 ? 0.3489 0.3206 0.3659 -0.0125 0.0445  0.0454  196 ALA A N   
3081 C CA  . ALA A 193 ? 0.4170 0.3758 0.4286 -0.0181 0.0518  0.0502  196 ALA A CA  
3082 C C   . ALA A 193 ? 0.4393 0.4195 0.4664 -0.0266 0.0539  0.0486  196 ALA A C   
3083 O O   . ALA A 193 ? 0.4654 0.4406 0.4875 -0.0296 0.0610  0.0539  196 ALA A O   
3084 C CB  . ALA A 193 ? 0.4986 0.4292 0.5062 -0.0284 0.0530  0.0486  196 ALA A CB  
3090 N N   . GLY A 194 ? 0.3825 0.3838 0.4262 -0.0298 0.0489  0.0418  197 GLY A N   
3091 C CA  . GLY A 194 ? 0.4000 0.4195 0.4546 -0.0346 0.0519  0.0400  197 GLY A CA  
3092 C C   . GLY A 194 ? 0.4415 0.4597 0.5084 -0.0457 0.0566  0.0395  197 GLY A C   
3093 O O   . GLY A 194 ? 0.4387 0.4666 0.5086 -0.0479 0.0630  0.0413  197 GLY A O   
3097 N N   . ILE A 195 ? 0.3196 0.3280 0.3933 -0.0533 0.0536  0.0374  198 ILE A N   
3098 C CA  . ILE A 195 ? 0.3486 0.3610 0.4365 -0.0659 0.0573  0.0378  198 ILE A CA  
3099 C C   . ILE A 195 ? 0.4766 0.5141 0.5865 -0.0678 0.0548  0.0324  198 ILE A C   
3100 O O   . ILE A 195 ? 0.4566 0.5085 0.5796 -0.0732 0.0605  0.0340  198 ILE A O   
3101 C CB  . ILE A 195 ? 0.4503 0.4415 0.5344 -0.0755 0.0543  0.0378  198 ILE A CB  
3102 C CG1 . ILE A 195 ? 0.6124 0.5729 0.6701 -0.0699 0.0572  0.0429  198 ILE A CG1 
3103 C CG2 . ILE A 195 ? 0.6696 0.6677 0.7682 -0.0911 0.0583  0.0398  198 ILE A CG2 
3104 C CD1 . ILE A 195 ? 0.6142 0.5682 0.6612 -0.0693 0.0670  0.0512  198 ILE A CD1 
3116 N N   . VAL A 196 ? 0.3688 0.4116 0.4826 -0.0628 0.0470  0.0269  199 VAL A N   
3117 C CA  . VAL A 196 ? 0.3287 0.3914 0.4602 -0.0621 0.0445  0.0222  199 VAL A CA  
3118 C C   . VAL A 196 ? 0.3478 0.4171 0.4728 -0.0531 0.0463  0.0203  199 VAL A C   
3119 O O   . VAL A 196 ? 0.3655 0.4277 0.4766 -0.0477 0.0431  0.0201  199 VAL A O   
3120 C CB  . VAL A 196 ? 0.4162 0.4778 0.5534 -0.0629 0.0346  0.0177  199 VAL A CB  
3121 C CG1 . VAL A 196 ? 0.4343 0.5138 0.5862 -0.0592 0.0320  0.0139  199 VAL A CG1 
3122 C CG2 . VAL A 196 ? 0.4422 0.4978 0.5849 -0.0745 0.0321  0.0187  199 VAL A CG2 
3132 N N   . PRO A 197 ? 0.2744 0.3572 0.4079 -0.0515 0.0515  0.0190  200 PRO A N   
3133 C CA  . PRO A 197 ? 0.3143 0.3986 0.4373 -0.0448 0.0532  0.0161  200 PRO A CA  
3134 C C   . PRO A 197 ? 0.3365 0.4198 0.4590 -0.0414 0.0452  0.0109  200 PRO A C   
3135 O O   . PRO A 197 ? 0.3121 0.3975 0.4458 -0.0423 0.0398  0.0093  200 PRO A O   
3136 C CB  . PRO A 197 ? 0.3937 0.4893 0.5250 -0.0433 0.0618  0.0156  200 PRO A CB  
3137 C CG  . PRO A 197 ? 0.4654 0.5719 0.6170 -0.0487 0.0628  0.0182  200 PRO A CG  
3138 C CD  . PRO A 197 ? 0.3630 0.4597 0.5136 -0.0561 0.0573  0.0210  200 PRO A CD  
3146 N N   . LEU A 198 ? 0.3154 0.3960 0.4237 -0.0383 0.0447  0.0087  201 LEU A N   
3147 C CA  . LEU A 198 ? 0.2575 0.3359 0.3624 -0.0370 0.0374  0.0048  201 LEU A CA  
3148 C C   . LEU A 198 ? 0.3069 0.3869 0.4230 -0.0351 0.0367  0.0010  201 LEU A C   
3149 O O   . LEU A 198 ? 0.2998 0.3779 0.4189 -0.0348 0.0300  -0.0006 201 LEU A O   
3150 C CB  . LEU A 198 ? 0.2943 0.3715 0.3819 -0.0371 0.0374  0.0031  201 LEU A CB  
3151 C CG  . LEU A 198 ? 0.3417 0.4171 0.4233 -0.0385 0.0307  -0.0003 201 LEU A CG  
3152 C CD1 . LEU A 198 ? 0.3650 0.4429 0.4507 -0.0382 0.0237  0.0026  201 LEU A CD1 
3153 C CD2 . LEU A 198 ? 0.4198 0.4965 0.4836 -0.0416 0.0305  -0.0015 201 LEU A CD2 
3165 N N   A ASN A 199 ? 0.2920 0.3757 0.4135 -0.0325 0.0439  0.0000  202 ASN A N   
3166 N N   B ASN A 199 ? 0.2963 0.3799 0.4174 -0.0325 0.0440  0.0000  202 ASN A N   
3167 C CA  A ASN A 199 ? 0.3071 0.3924 0.4378 -0.0277 0.0438  -0.0026 202 ASN A CA  
3168 C CA  B ASN A 199 ? 0.3089 0.3948 0.4400 -0.0277 0.0443  -0.0024 202 ASN A CA  
3169 C C   A ASN A 199 ? 0.3448 0.4395 0.4943 -0.0288 0.0384  -0.0001 202 ASN A C   
3170 C C   B ASN A 199 ? 0.3438 0.4382 0.4929 -0.0290 0.0383  -0.0001 202 ASN A C   
3171 O O   A ASN A 199 ? 0.3048 0.3984 0.4584 -0.0258 0.0331  -0.0016 202 ASN A O   
3172 O O   B ASN A 199 ? 0.3020 0.3945 0.4541 -0.0264 0.0326  -0.0017 202 ASN A O   
3173 C CB  A ASN A 199 ? 0.3748 0.4634 0.5064 -0.0219 0.0541  -0.0035 202 ASN A CB  
3174 C CB  B ASN A 199 ? 0.3758 0.4673 0.5103 -0.0225 0.0549  -0.0024 202 ASN A CB  
3175 C CG  A ASN A 199 ? 0.3733 0.4777 0.5208 -0.0233 0.0599  0.0015  202 ASN A CG  
3176 C CG  B ASN A 199 ? 0.3356 0.4268 0.4755 -0.0139 0.0569  -0.0047 202 ASN A CG  
3177 O OD1 A ASN A 199 ? 0.3968 0.5021 0.5420 -0.0294 0.0609  0.0049  202 ASN A OD1 
3178 O OD1 B ASN A 199 ? 0.3496 0.4340 0.4888 -0.0124 0.0502  -0.0064 202 ASN A OD1 
3179 N ND2 A ASN A 199 ? 0.4941 0.6118 0.6576 -0.0175 0.0643  0.0029  202 ASN A ND2 
3180 N ND2 B ASN A 199 ? 0.5093 0.6078 0.6536 -0.0068 0.0669  -0.0040 202 ASN A ND2 
3193 N N   . ILE A 200 ? 0.2984 0.4009 0.4575 -0.0341 0.0393  0.0037  203 ILE A N   
3194 C CA  . ILE A 200 ? 0.2296 0.3398 0.4036 -0.0380 0.0328  0.0053  203 ILE A CA  
3195 C C   . ILE A 200 ? 0.2801 0.3788 0.4449 -0.0401 0.0239  0.0039  203 ILE A C   
3196 O O   . ILE A 200 ? 0.2718 0.3728 0.4429 -0.0400 0.0168  0.0030  203 ILE A O   
3197 C CB  . ILE A 200 ? 0.2838 0.4028 0.4680 -0.0458 0.0365  0.0095  203 ILE A CB  
3198 C CG1 . ILE A 200 ? 0.3422 0.4773 0.5376 -0.0426 0.0463  0.0118  203 ILE A CG1 
3199 C CG2 . ILE A 200 ? 0.3502 0.4749 0.5463 -0.0530 0.0284  0.0104  203 ILE A CG2 
3200 C CD1 . ILE A 200 ? 0.3898 0.5397 0.5996 -0.0346 0.0459  0.0112  203 ILE A CD1 
3212 N N   . GLU A 201 ? 0.2321 0.3200 0.3816 -0.0411 0.0243  0.0044  204 GLU A N   
3213 C CA  . GLU A 201 ? 0.2572 0.3363 0.3972 -0.0409 0.0173  0.0038  204 GLU A CA  
3214 C C   . GLU A 201 ? 0.3171 0.3964 0.4560 -0.0371 0.0126  0.0010  204 GLU A C   
3215 O O   . GLU A 201 ? 0.2607 0.3378 0.3997 -0.0368 0.0060  0.0005  204 GLU A O   
3216 C CB  . GLU A 201 ? 0.2924 0.3648 0.4167 -0.0398 0.0196  0.0059  204 GLU A CB  
3217 C CG  . GLU A 201 ? 0.3372 0.4044 0.4518 -0.0372 0.0138  0.0063  204 GLU A CG  
3218 C CD  . GLU A 201 ? 0.4013 0.4679 0.5019 -0.0341 0.0159  0.0096  204 GLU A CD  
3219 O OE1 . GLU A 201 ? 0.3650 0.4320 0.4616 -0.0344 0.0213  0.0119  204 GLU A OE1 
3220 O OE2 . GLU A 201 ? 0.4971 0.5655 0.5910 -0.0308 0.0120  0.0106  204 GLU A OE2 
3227 N N   . THR A 202 ? 0.2381 0.3174 0.3735 -0.0343 0.0163  -0.0008 205 THR A N   
3228 C CA  . THR A 202 ? 0.2165 0.2912 0.3475 -0.0319 0.0127  -0.0031 205 THR A CA  
3229 C C   . THR A 202 ? 0.2427 0.3214 0.3863 -0.0286 0.0095  -0.0031 205 THR A C   
3230 O O   . THR A 202 ? 0.2360 0.3110 0.3772 -0.0273 0.0039  -0.0033 205 THR A O   
3231 C CB  . THR A 202 ? 0.2568 0.3253 0.3773 -0.0308 0.0181  -0.0058 205 THR A CB  
3232 O OG1 . THR A 202 ? 0.2703 0.3384 0.3784 -0.0346 0.0197  -0.0053 205 THR A OG1 
3233 C CG2 . THR A 202 ? 0.2493 0.3080 0.3616 -0.0303 0.0149  -0.0079 205 THR A CG2 
3241 N N   . LEU A 203 ? 0.2205 0.3089 0.3776 -0.0267 0.0134  -0.0021 206 LEU A N   
3242 C CA  . LEU A 203 ? 0.2268 0.3256 0.3987 -0.0234 0.0095  -0.0007 206 LEU A CA  
3243 C C   . LEU A 203 ? 0.2148 0.3151 0.3890 -0.0284 0.0006  0.0000  206 LEU A C   
3244 O O   . LEU A 203 ? 0.2336 0.3346 0.4094 -0.0256 -0.0057 0.0002  206 LEU A O   
3245 C CB  . LEU A 203 ? 0.1983 0.3135 0.3864 -0.0223 0.0154  0.0016  206 LEU A CB  
3246 C CG  . LEU A 203 ? 0.2331 0.3677 0.4407 -0.0209 0.0109  0.0045  206 LEU A CG  
3247 C CD1 . LEU A 203 ? 0.2670 0.4002 0.4746 -0.0103 0.0086  0.0049  206 LEU A CD1 
3248 C CD2 . LEU A 203 ? 0.3122 0.4672 0.5364 -0.0211 0.0181  0.0078  206 LEU A CD2 
3260 N N   . LEU A 204 ? 0.2358 0.3340 0.4076 -0.0354 0.0003  0.0004  207 LEU A N   
3261 C CA  . LEU A 204 ? 0.2385 0.3339 0.4089 -0.0401 -0.0074 0.0001  207 LEU A CA  
3262 C C   . LEU A 204 ? 0.1893 0.2741 0.3461 -0.0367 -0.0122 -0.0011 207 LEU A C   
3263 O O   . LEU A 204 ? 0.2470 0.3324 0.4040 -0.0364 -0.0191 -0.0015 207 LEU A O   
3264 C CB  . LEU A 204 ? 0.2091 0.2976 0.3746 -0.0472 -0.0054 0.0007  207 LEU A CB  
3265 C CG  . LEU A 204 ? 0.2516 0.3509 0.4304 -0.0535 -0.0010 0.0028  207 LEU A CG  
3266 C CD1 . LEU A 204 ? 0.2917 0.3776 0.4603 -0.0602 0.0022  0.0040  207 LEU A CD1 
3267 C CD2 . LEU A 204 ? 0.3767 0.4911 0.5712 -0.0585 -0.0075 0.0031  207 LEU A CD2 
3279 N N   . PHE A 205 ? 0.1980 0.2756 0.3430 -0.0346 -0.0087 -0.0011 208 PHE A N   
3280 C CA  . PHE A 205 ? 0.1968 0.2687 0.3306 -0.0323 -0.0125 -0.0011 208 PHE A CA  
3281 C C   . PHE A 205 ? 0.2069 0.2800 0.3434 -0.0290 -0.0153 -0.0011 208 PHE A C   
3282 O O   . PHE A 205 ? 0.2151 0.2855 0.3460 -0.0276 -0.0201 -0.0005 208 PHE A O   
3283 C CB  . PHE A 205 ? 0.2113 0.2808 0.3339 -0.0320 -0.0085 -0.0001 208 PHE A CB  
3284 C CG  . PHE A 205 ? 0.2153 0.2818 0.3300 -0.0319 -0.0072 0.0016  208 PHE A CG  
3285 C CD1 . PHE A 205 ? 0.2216 0.2822 0.3311 -0.0305 -0.0106 0.0018  208 PHE A CD1 
3286 C CD2 . PHE A 205 ? 0.2428 0.3109 0.3524 -0.0321 -0.0021 0.0032  208 PHE A CD2 
3287 C CE1 . PHE A 205 ? 0.2546 0.3084 0.3535 -0.0280 -0.0082 0.0038  208 PHE A CE1 
3288 C CE2 . PHE A 205 ? 0.2573 0.3220 0.3579 -0.0295 -0.0004 0.0061  208 PHE A CE2 
3289 C CZ  . PHE A 205 ? 0.2841 0.3406 0.3794 -0.0269 -0.0029 0.0065  208 PHE A CZ  
3299 N N   . MET A 206 ? 0.2138 0.2892 0.3569 -0.0264 -0.0116 -0.0014 209 MET A N   
3300 C CA  . MET A 206 ? 0.2349 0.3071 0.3775 -0.0215 -0.0135 -0.0007 209 MET A CA  
3301 C C   . MET A 206 ? 0.2006 0.2811 0.3528 -0.0190 -0.0202 0.0009  209 MET A C   
3302 O O   . MET A 206 ? 0.2361 0.3124 0.3829 -0.0161 -0.0247 0.0023  209 MET A O   
3303 C CB  . MET A 206 ? 0.2911 0.3603 0.4353 -0.0171 -0.0068 -0.0014 209 MET A CB  
3304 C CG  . MET A 206 ? 0.2945 0.3544 0.4339 -0.0108 -0.0076 -0.0002 209 MET A CG  
3305 S SD  . MET A 206 ? 0.4513 0.5243 0.6074 -0.0007 -0.0086 0.0029  209 MET A SD  
3306 C CE  . MET A 206 ? 0.2600 0.3274 0.4142 0.0042  0.0027  0.0009  209 MET A CE  
3316 N N   . VAL A 207 ? 0.1884 0.2813 0.3538 -0.0211 -0.0212 0.0010  210 VAL A N   
3317 C CA  . VAL A 207 ? 0.2076 0.3116 0.3819 -0.0212 -0.0291 0.0023  210 VAL A CA  
3318 C C   . VAL A 207 ? 0.2070 0.3025 0.3689 -0.0250 -0.0357 0.0009  210 VAL A C   
3319 O O   . VAL A 207 ? 0.2135 0.3104 0.3728 -0.0223 -0.0424 0.0020  210 VAL A O   
3320 C CB  . VAL A 207 ? 0.2213 0.3421 0.4121 -0.0264 -0.0291 0.0028  210 VAL A CB  
3321 C CG1 . VAL A 207 ? 0.2725 0.4064 0.4711 -0.0296 -0.0390 0.0037  210 VAL A CG1 
3322 C CG2 . VAL A 207 ? 0.2725 0.4050 0.4762 -0.0197 -0.0218 0.0051  210 VAL A CG2 
3332 N N   . LEU A 208 ? 0.1967 0.2832 0.3493 -0.0298 -0.0335 -0.0011 211 LEU A N   
3333 C CA  . LEU A 208 ? 0.1802 0.2572 0.3186 -0.0310 -0.0381 -0.0023 211 LEU A CA  
3334 C C   . LEU A 208 ? 0.2209 0.2930 0.3492 -0.0257 -0.0387 -0.0006 211 LEU A C   
3335 O O   . LEU A 208 ? 0.2415 0.3116 0.3626 -0.0241 -0.0444 -0.0004 211 LEU A O   
3336 C CB  . LEU A 208 ? 0.2067 0.2737 0.3355 -0.0340 -0.0338 -0.0036 211 LEU A CB  
3337 C CG  . LEU A 208 ? 0.2316 0.2976 0.3653 -0.0413 -0.0335 -0.0050 211 LEU A CG  
3338 C CD1 . LEU A 208 ? 0.2707 0.3238 0.3922 -0.0412 -0.0275 -0.0048 211 LEU A CD1 
3339 C CD2 . LEU A 208 ? 0.3160 0.3792 0.4464 -0.0465 -0.0417 -0.0075 211 LEU A CD2 
3351 N N   . ASP A 209 ? 0.1935 0.2630 0.3193 -0.0240 -0.0329 0.0007  212 ASP A N   
3352 C CA  . ASP A 209 ? 0.1868 0.2516 0.3023 -0.0219 -0.0329 0.0029  212 ASP A CA  
3353 C C   . ASP A 209 ? 0.2362 0.3008 0.3533 -0.0179 -0.0371 0.0051  212 ASP A C   
3354 O O   . ASP A 209 ? 0.2253 0.2867 0.3331 -0.0163 -0.0403 0.0072  212 ASP A O   
3355 C CB  . ASP A 209 ? 0.2006 0.2625 0.3129 -0.0239 -0.0267 0.0035  212 ASP A CB  
3356 C CG  . ASP A 209 ? 0.2578 0.3221 0.3651 -0.0266 -0.0233 0.0033  212 ASP A CG  
3357 O OD1 . ASP A 209 ? 0.2462 0.3115 0.3489 -0.0254 -0.0247 0.0036  212 ASP A OD1 
3358 O OD2 . ASP A 209 ? 0.2241 0.2884 0.3297 -0.0295 -0.0190 0.0031  212 ASP A OD2 
3363 N N   . VAL A 210 ? 0.2191 0.2871 0.3469 -0.0149 -0.0363 0.0054  213 VAL A N   
3364 C CA  . VAL A 210 ? 0.2123 0.2796 0.3405 -0.0085 -0.0397 0.0088  213 VAL A CA  
3365 C C   . VAL A 210 ? 0.2377 0.3131 0.3669 -0.0080 -0.0484 0.0093  213 VAL A C   
3366 O O   . VAL A 210 ? 0.2391 0.3110 0.3600 -0.0042 -0.0524 0.0125  213 VAL A O   
3367 C CB  . VAL A 210 ? 0.2301 0.3018 0.3701 -0.0027 -0.0362 0.0097  213 VAL A CB  
3368 C CG1 . VAL A 210 ? 0.3042 0.3776 0.4457 0.0067  -0.0401 0.0145  213 VAL A CG1 
3369 C CG2 . VAL A 210 ? 0.2677 0.3258 0.4006 -0.0031 -0.0277 0.0084  213 VAL A CG2 
3379 N N   . SER A 211 ? 0.2333 0.3179 0.3701 -0.0127 -0.0515 0.0063  214 SER A N   
3380 C CA  . SER A 211 ? 0.2090 0.2998 0.3442 -0.0146 -0.0606 0.0056  214 SER A CA  
3381 C C   . SER A 211 ? 0.2366 0.3156 0.3528 -0.0153 -0.0625 0.0045  214 SER A C   
3382 O O   . SER A 211 ? 0.2500 0.3295 0.3583 -0.0130 -0.0689 0.0057  214 SER A O   
3383 C CB  . SER A 211 ? 0.2077 0.3069 0.3525 -0.0226 -0.0628 0.0021  214 SER A CB  
3384 O OG  . SER A 211 ? 0.2602 0.3754 0.4243 -0.0213 -0.0611 0.0042  214 SER A OG  
3390 N N   . ALA A 212 ? 0.2116 0.2817 0.3198 -0.0175 -0.0564 0.0028  215 ALA A N   
3391 C CA  . ALA A 212 ? 0.2218 0.2832 0.3123 -0.0165 -0.0567 0.0022  215 ALA A CA  
3392 C C   . ALA A 212 ? 0.2259 0.2852 0.3079 -0.0123 -0.0549 0.0068  215 ALA A C   
3393 O O   . ALA A 212 ? 0.2618 0.3174 0.3296 -0.0101 -0.0554 0.0077  215 ALA A O   
3394 C CB  . ALA A 212 ? 0.2396 0.2953 0.3254 -0.0183 -0.0503 0.0002  215 ALA A CB  
3400 N N   . LYS A 213 ? 0.2290 0.2891 0.3179 -0.0113 -0.0520 0.0101  216 LYS A N   
3401 C CA  . LYS A 213 ? 0.2267 0.2816 0.3061 -0.0097 -0.0498 0.0151  216 LYS A CA  
3402 C C   . LYS A 213 ? 0.2402 0.2933 0.3203 -0.0045 -0.0541 0.0189  216 LYS A C   
3403 O O   . LYS A 213 ? 0.2901 0.3415 0.3593 -0.0018 -0.0575 0.0221  216 LYS A O   
3404 C CB  . LYS A 213 ? 0.2179 0.2697 0.2988 -0.0137 -0.0426 0.0160  216 LYS A CB  
3405 C CG  . LYS A 213 ? 0.2386 0.2953 0.3175 -0.0173 -0.0386 0.0142  216 LYS A CG  
3406 C CD  . LYS A 213 ? 0.2488 0.3052 0.3279 -0.0228 -0.0330 0.0152  216 LYS A CD  
3407 C CE  . LYS A 213 ? 0.2286 0.2946 0.3038 -0.0249 -0.0298 0.0162  216 LYS A CE  
3408 N NZ  . LYS A 213 ? 0.2115 0.2801 0.2917 -0.0230 -0.0289 0.0126  216 LYS A NZ  
3419 N N   . VAL A 214 ? 0.2263 0.2800 0.3177 -0.0019 -0.0532 0.0192  217 VAL A N   
3420 C CA  . VAL A 214 ? 0.2314 0.2830 0.3224 0.0057  -0.0563 0.0242  217 VAL A CA  
3421 C C   . VAL A 214 ? 0.2215 0.2872 0.3179 0.0088  -0.0657 0.0240  217 VAL A C   
3422 O O   . VAL A 214 ? 0.2812 0.3469 0.3702 0.0143  -0.0708 0.0286  217 VAL A O   
3423 C CB  . VAL A 214 ? 0.2288 0.2759 0.3284 0.0101  -0.0510 0.0251  217 VAL A CB  
3424 C CG1 . VAL A 214 ? 0.2797 0.3235 0.3775 0.0212  -0.0536 0.0315  217 VAL A CG1 
3425 C CG2 . VAL A 214 ? 0.3034 0.3345 0.3941 0.0046  -0.0429 0.0242  217 VAL A CG2 
3435 N N   . GLY A 215 ? 0.2428 0.3206 0.3508 0.0044  -0.0684 0.0191  218 GLY A N   
3436 C CA  . GLY A 215 ? 0.2862 0.3779 0.3978 0.0041  -0.0786 0.0183  218 GLY A CA  
3437 C C   . GLY A 215 ? 0.3167 0.4019 0.4095 0.0022  -0.0835 0.0171  218 GLY A C   
3438 O O   . GLY A 215 ? 0.2898 0.3799 0.3764 0.0061  -0.0912 0.0201  218 GLY A O   
3442 N N   . PHE A 216 ? 0.2705 0.3454 0.3531 -0.0025 -0.0790 0.0131  219 PHE A N   
3443 C CA  . PHE A 216 ? 0.2537 0.3206 0.3160 -0.0020 -0.0808 0.0124  219 PHE A CA  
3444 C C   . PHE A 216 ? 0.2904 0.3540 0.3423 0.0043  -0.0810 0.0193  219 PHE A C   
3445 O O   . PHE A 216 ? 0.3146 0.3784 0.3535 0.0068  -0.0872 0.0203  219 PHE A O   
3446 C CB  . PHE A 216 ? 0.2564 0.3146 0.3120 -0.0046 -0.0724 0.0098  219 PHE A CB  
3447 C CG  . PHE A 216 ? 0.2955 0.3463 0.3301 -0.0020 -0.0715 0.0093  219 PHE A CG  
3448 C CD1 . PHE A 216 ? 0.3112 0.3610 0.3361 0.0019  -0.0676 0.0154  219 PHE A CD1 
3449 C CD2 . PHE A 216 ? 0.3228 0.3661 0.3460 -0.0036 -0.0729 0.0031  219 PHE A CD2 
3450 C CE1 . PHE A 216 ? 0.3567 0.4025 0.3628 0.0055  -0.0653 0.0157  219 PHE A CE1 
3451 C CE2 . PHE A 216 ? 0.3704 0.4055 0.3722 0.0012  -0.0704 0.0026  219 PHE A CE2 
3452 C CZ  . PHE A 216 ? 0.3340 0.3726 0.3283 0.0063  -0.0663 0.0091  219 PHE A CZ  
3462 N N   . GLY A 217 ? 0.2750 0.3335 0.3301 0.0062  -0.0740 0.0243  220 GLY A N   
3463 C CA  . GLY A 217 ? 0.2886 0.3402 0.3313 0.0107  -0.0730 0.0316  220 GLY A CA  
3464 C C   . GLY A 217 ? 0.2984 0.3540 0.3418 0.0180  -0.0804 0.0364  220 GLY A C   
3465 O O   . GLY A 217 ? 0.3441 0.3962 0.3730 0.0222  -0.0831 0.0416  220 GLY A O   
3469 N N   . LEU A 218 ? 0.2587 0.3239 0.3191 0.0206  -0.0835 0.0357  221 LEU A N   
3470 C CA  . LEU A 218 ? 0.2792 0.3538 0.3423 0.0293  -0.0912 0.0413  221 LEU A CA  
3471 C C   . LEU A 218 ? 0.3892 0.4744 0.4436 0.0279  -0.1021 0.0394  221 LEU A C   
3472 O O   . LEU A 218 ? 0.4190 0.5063 0.4635 0.0349  -0.1079 0.0455  221 LEU A O   
3473 C CB  . LEU A 218 ? 0.3167 0.4054 0.4020 0.0324  -0.0919 0.0408  221 LEU A CB  
3474 C CG  . LEU A 218 ? 0.3807 0.4561 0.4700 0.0382  -0.0818 0.0444  221 LEU A CG  
3475 C CD1 . LEU A 218 ? 0.3791 0.4698 0.4902 0.0409  -0.0805 0.0427  221 LEU A CD1 
3476 C CD2 . LEU A 218 ? 0.4176 0.4812 0.4950 0.0499  -0.0815 0.0540  221 LEU A CD2 
3488 N N   . ILE A 219 ? 0.2850 0.3748 0.3405 0.0190  -0.1051 0.0309  222 ILE A N   
3489 C CA  . ILE A 219 ? 0.3514 0.4465 0.3941 0.0158  -0.1154 0.0273  222 ILE A CA  
3490 C C   . ILE A 219 ? 0.3703 0.4514 0.3876 0.0190  -0.1135 0.0296  222 ILE A C   
3491 O O   . ILE A 219 ? 0.3879 0.4726 0.3918 0.0231  -0.1213 0.0328  222 ILE A O   
3492 C CB  . ILE A 219 ? 0.3574 0.4529 0.4027 0.0047  -0.1172 0.0173  222 ILE A CB  
3493 C CG1 . ILE A 219 ? 0.3508 0.4636 0.4217 0.0006  -0.1196 0.0162  222 ILE A CG1 
3494 C CG2 . ILE A 219 ? 0.4234 0.5173 0.4494 0.0000  -0.1271 0.0120  222 ILE A CG2 
3495 C CD1 . ILE A 219 ? 0.4240 0.5321 0.4984 -0.0110 -0.1174 0.0075  222 ILE A CD1 
3507 N N   . LEU A 220 ? 0.3281 0.3958 0.3387 0.0177  -0.1028 0.0291  223 LEU A N   
3508 C CA  . LEU A 220 ? 0.3029 0.3608 0.2904 0.0203  -0.0994 0.0317  223 LEU A CA  
3509 C C   . LEU A 220 ? 0.3678 0.4232 0.3478 0.0275  -0.0992 0.0422  223 LEU A C   
3510 O O   . LEU A 220 ? 0.3941 0.4482 0.3553 0.0314  -0.1034 0.0452  223 LEU A O   
3511 C CB  . LEU A 220 ? 0.3160 0.3662 0.3024 0.0172  -0.0876 0.0303  223 LEU A CB  
3512 C CG  . LEU A 220 ? 0.3190 0.3636 0.2846 0.0204  -0.0818 0.0346  223 LEU A CG  
3513 C CD1 . LEU A 220 ? 0.4083 0.4499 0.3534 0.0225  -0.0867 0.0291  223 LEU A CD1 
3514 C CD2 . LEU A 220 ? 0.3812 0.4253 0.3511 0.0172  -0.0706 0.0350  223 LEU A CD2 
3526 N N   . LEU A 221 ? 0.3625 0.4143 0.3541 0.0295  -0.0938 0.0481  224 LEU A N   
3527 C CA  . LEU A 221 ? 0.3960 0.4384 0.3765 0.0356  -0.0911 0.0588  224 LEU A CA  
3528 C C   . LEU A 221 ? 0.4382 0.4875 0.4175 0.0448  -0.1008 0.0644  224 LEU A C   
3529 O O   . LEU A 221 ? 0.4791 0.5191 0.4456 0.0514  -0.0995 0.0742  224 LEU A O   
3530 C CB  . LEU A 221 ? 0.3412 0.3715 0.3298 0.0337  -0.0815 0.0626  224 LEU A CB  
3531 C CG  . LEU A 221 ? 0.3966 0.4236 0.3866 0.0241  -0.0724 0.0585  224 LEU A CG  
3532 C CD1 . LEU A 221 ? 0.4085 0.4231 0.4051 0.0204  -0.0645 0.0611  224 LEU A CD1 
3533 C CD2 . LEU A 221 ? 0.4441 0.4693 0.4156 0.0221  -0.0685 0.0624  224 LEU A CD2 
3545 N N   . ARG A 222 ? 0.3520 0.7222 0.5683 0.0674  -0.0639 0.1189  225 ARG A N   
3546 C CA  . ARG A 222 ? 0.3863 0.7806 0.6411 0.0971  -0.0982 0.1460  225 ARG A CA  
3547 C C   . ARG A 222 ? 0.3939 0.7864 0.6202 0.0748  -0.1471 0.1610  225 ARG A C   
3548 O O   . ARG A 222 ? 0.4257 0.8441 0.6769 0.0941  -0.1825 0.1855  225 ARG A O   
3549 C CB  . ARG A 222 ? 0.3596 0.8462 0.7137 0.1137  -0.0959 0.1539  225 ARG A CB  
3550 C CG  . ARG A 222 ? 0.5148 0.9948 0.9034 0.1442  -0.0485 0.1472  225 ARG A CG  
3551 C CD  . ARG A 222 ? 0.5194 1.0833 1.0111 0.1624  -0.0455 0.1567  225 ARG A CD  
3552 N NE  . ARG A 222 ? 0.5082 1.1311 1.0428 0.1647  -0.0964 0.1778  225 ARG A NE  
3553 C CZ  . ARG A 222 ? 0.7431 1.3619 1.2870 0.1931  -0.1252 0.2028  225 ARG A CZ  
3554 N NH1 . ARG A 222 ? 0.7241 1.3005 1.2592 0.2335  -0.1089 0.2224  225 ARG A NH1 
3555 N NH2 . ARG A 222 ? 0.8283 1.4746 1.3804 0.1792  -0.1649 0.2032  225 ARG A NH2 
3569 N N   . SER A 223 ? 0.3708 0.7316 0.5441 0.0337  -0.1478 0.1484  226 SER A N   
3570 C CA  . SER A 223 ? 0.4626 0.8180 0.6068 0.0024  -0.1853 0.1594  226 SER A CA  
3571 C C   . SER A 223 ? 0.4337 0.6875 0.4916 0.0010  -0.1980 0.1625  226 SER A C   
3572 O O   . SER A 223 ? 0.4885 0.6673 0.4953 0.0083  -0.1699 0.1471  226 SER A O   
3573 C CB  . SER A 223 ? 0.5230 0.8945 0.6603 -0.0430 -0.1709 0.1464  226 SER A CB  
3574 O OG  . SER A 223 ? 0.6540 0.9691 0.7353 -0.0765 -0.1832 0.1457  226 SER A OG  
3580 N N   . ARG A 224 ? 0.4672 0.7183 0.5064 -0.0112 -0.2394 0.1805  227 ARG A N   
3581 C CA  . ARG A 224 ? 0.5228 0.6687 0.4733 -0.0200 -0.2483 0.1794  227 ARG A CA  
3582 C C   . ARG A 224 ? 0.5225 0.6042 0.4186 -0.0667 -0.2251 0.1573  227 ARG A C   
3583 O O   . ARG A 224 ? 0.6168 0.6020 0.4436 -0.0750 -0.2193 0.1484  227 ARG A O   
3584 C CB  . ARG A 224 ? 0.6135 0.7668 0.5603 -0.0179 -0.2770 0.1894  227 ARG A CB  
3585 C CG  . ARG A 224 ? 0.8957 0.9709 0.7823 0.0100  -0.2888 0.2010  227 ARG A CG  
3586 C CD  . ARG A 224 ? 1.0394 1.1347 0.9614 0.0699  -0.2924 0.2247  227 ARG A CD  
3587 N NE  . ARG A 224 ? 1.1529 1.1384 1.0014 0.0963  -0.2823 0.2283  227 ARG A NE  
3588 C CZ  . ARG A 224 ? 1.3636 1.3309 1.2277 0.1485  -0.2549 0.2339  227 ARG A CZ  
3589 N NH1 . ARG A 224 ? 1.4653 1.5178 1.4187 0.1797  -0.2411 0.2437  227 ARG A NH1 
3590 N NH2 . ARG A 224 ? 1.3211 1.1775 1.1095 0.1687  -0.2340 0.2274  227 ARG A NH2 
3604 N N   . ALA A 225 ? 0.5090 0.6395 0.4411 -0.0940 -0.2044 0.1474  228 ALA A N   
3605 C CA  . ALA A 225 ? 0.5681 0.6444 0.4642 -0.1346 -0.1772 0.1330  228 ALA A CA  
3606 C C   . ALA A 225 ? 0.6749 0.6777 0.5187 -0.1326 -0.1548 0.1187  228 ALA A C   
3607 O O   . ALA A 225 ? 0.6764 0.6145 0.4916 -0.1593 -0.1338 0.1046  228 ALA A O   
3608 C CB  . ALA A 225 ? 0.5144 0.6605 0.4615 -0.1547 -0.1542 0.1315  228 ALA A CB  
3614 N N   . ILE A 226 ? 0.4953 0.5053 0.3399 -0.0990 -0.1474 0.1159  229 ILE A N   
3615 C CA  . ILE A 226 ? 0.4958 0.4392 0.2941 -0.0982 -0.1121 0.0932  229 ILE A CA  
3616 C C   . ILE A 226 ? 0.6106 0.4404 0.3310 -0.0894 -0.1160 0.0864  229 ILE A C   
3617 O O   . ILE A 226 ? 0.7070 0.4712 0.3829 -0.0939 -0.0869 0.0639  229 ILE A O   
3618 C CB  . ILE A 226 ? 0.4943 0.4868 0.3334 -0.0680 -0.0820 0.0807  229 ILE A CB  
3619 C CG1 . ILE A 226 ? 0.5416 0.5346 0.3979 -0.0226 -0.0894 0.0888  229 ILE A CG1 
3620 C CG2 . ILE A 226 ? 0.4591 0.5553 0.3689 -0.0787 -0.0749 0.0851  229 ILE A CG2 
3621 C CD1 . ILE A 226 ? 0.5135 0.5287 0.3957 0.0032  -0.0485 0.0726  229 ILE A CD1 
3633 N N   . PHE A 227 ? 0.7557 0.5228 0.2708 -0.0026 -0.1104 0.0125  230 PHE A N   
3634 C CA  . PHE A 227 ? 0.7543 0.5029 0.2574 -0.0200 -0.1215 0.0241  230 PHE A CA  
3635 C C   . PHE A 227 ? 0.8439 0.6063 0.3411 -0.0362 -0.1034 0.0302  230 PHE A C   
3636 O O   . PHE A 227 ? 0.7718 0.5494 0.2724 -0.0339 -0.0907 0.0239  230 PHE A O   
3637 C CB  . PHE A 227 ? 0.7977 0.5303 0.2985 -0.0173 -0.1428 0.0256  230 PHE A CB  
3638 C CG  . PHE A 227 ? 0.7852 0.5036 0.2943 -0.0002 -0.1651 0.0184  230 PHE A CG  
3639 C CD1 . PHE A 227 ? 0.9170 0.6083 0.4229 -0.0054 -0.1869 0.0250  230 PHE A CD1 
3640 C CD2 . PHE A 227 ? 0.8927 0.6275 0.4153 0.0216  -0.1652 0.0053  230 PHE A CD2 
3641 C CE1 . PHE A 227 ? 0.8983 0.5764 0.4158 0.0128  -0.2097 0.0148  230 PHE A CE1 
3642 C CE2 . PHE A 227 ? 0.9402 0.6688 0.4741 0.0407  -0.1848 -0.0040 230 PHE A CE2 
3643 C CZ  . PHE A 227 ? 0.9783 0.6772 0.5102 0.0374  -0.2075 -0.0012 230 PHE A CZ  
3653 N N   . GLY A 228 ? 0.8286 0.5874 0.3178 -0.0520 -0.1040 0.0425  231 GLY A N   
3654 C CA  . GLY A 228 ? 0.7973 0.5753 0.2824 -0.0639 -0.0892 0.0477  231 GLY A CA  
3655 C C   . GLY A 228 ? 0.8371 0.6143 0.3155 -0.0660 -0.0963 0.0498  231 GLY A C   
3656 O O   . GLY A 228 ? 0.9647 0.7229 0.4402 -0.0633 -0.1149 0.0527  231 GLY A O   
3660 N N   . GLU A 229 ? 0.9658 0.7648 0.4423 -0.0688 -0.0823 0.0464  232 GLU A N   
3661 C CA  . GLU A 229 ? 0.9895 0.7918 0.4580 -0.0699 -0.0883 0.0472  232 GLU A CA  
3662 C C   . GLU A 229 ? 1.0276 0.8279 0.4856 -0.0819 -0.0978 0.0661  232 GLU A C   
3663 O O   . GLU A 229 ? 1.0702 0.8891 0.5255 -0.0904 -0.0884 0.0753  232 GLU A O   
3664 C CB  . GLU A 229 ? 1.1469 0.9729 0.6152 -0.0673 -0.0733 0.0358  232 GLU A CB  
3665 C CG  . GLU A 229 ? 1.0044 0.8305 0.4681 -0.0626 -0.0800 0.0276  232 GLU A CG  
3666 C CD  . GLU A 229 ? 1.0696 0.9141 0.5327 -0.0595 -0.0689 0.0132  232 GLU A CD  
3667 O OE1 . GLU A 229 ? 0.8456 0.6906 0.3048 -0.0562 -0.0751 0.0044  232 GLU A OE1 
3668 O OE2 . GLU A 229 ? 1.0922 0.9496 0.5585 -0.0597 -0.0558 0.0097  232 GLU A OE2 
3675 N N   . ALA A 230 ? 0.9544 0.7342 0.4078 -0.0820 -0.1168 0.0729  233 ALA A N   
3676 C CA  . ALA A 230 ? 0.9852 0.7583 0.4306 -0.0944 -0.1290 0.0942  233 ALA A CA  
3677 C C   . ALA A 230 ? 1.0653 0.8296 0.5037 -0.0908 -0.1431 0.0962  233 ALA A C   
3678 O O   . ALA A 230 ? 1.1609 0.9166 0.6026 -0.0787 -0.1484 0.0816  233 ALA A O   
3679 C CB  . ALA A 230 ? 1.0993 0.8449 0.5492 -0.1010 -0.1447 0.1057  233 ALA A CB  
3685 N N   . GLU A 231 ? 1.0370 0.8069 0.4669 -0.1010 -0.1487 0.1156  234 GLU A N   
3686 C CA  . GLU A 231 ? 1.0458 0.8088 0.4680 -0.0982 -0.1624 0.1206  234 GLU A CA  
3687 C C   . GLU A 231 ? 1.2704 0.9945 0.6965 -0.1001 -0.1881 0.1305  234 GLU A C   
3688 O O   . GLU A 231 ? 1.3590 1.0709 0.7873 -0.1134 -0.1984 0.1516  234 GLU A O   
3689 C CB  . GLU A 231 ? 0.9631 0.7542 0.3743 -0.1059 -0.1561 0.1378  234 GLU A CB  
3690 C CG  . GLU A 231 ? 1.0553 0.8514 0.4560 -0.0988 -0.1636 0.1369  234 GLU A CG  
3691 C CD  . GLU A 231 ? 0.9005 0.7082 0.3007 -0.0847 -0.1557 0.1102  234 GLU A CD  
3692 O OE1 . GLU A 231 ? 1.0353 0.8633 0.4385 -0.0819 -0.1390 0.0970  234 GLU A OE1 
3693 O OE2 . GLU A 231 ? 0.9503 0.7475 0.3489 -0.0767 -0.1671 0.1029  234 GLU A OE2 
4204 C C1  . RET S .   ? 0.2369 0.2752 0.2699 0.0169  0.0019  0.0204  318 RET A C1  
4205 C C2  . RET S .   ? 0.4027 0.4387 0.4278 0.0246  0.0078  0.0261  318 RET A C2  
4206 C C3  . RET S .   ? 0.4619 0.4659 0.4715 0.0279  0.0113  0.0250  318 RET A C3  
4207 C C4  . RET S .   ? 0.2857 0.2699 0.2780 0.0361  0.0116  0.0226  318 RET A C4  
4208 C C5  . RET S .   ? 0.2618 0.2523 0.2613 0.0294  0.0053  0.0171  318 RET A C5  
4209 C C6  . RET S .   ? 0.2462 0.2609 0.2645 0.0211  0.0010  0.0165  318 RET A C6  
4210 C C7  . RET S .   ? 0.2458 0.2619 0.2685 0.0153  -0.0050 0.0117  318 RET A C7  
4211 C C8  . RET S .   ? 0.2435 0.2777 0.2805 0.0086  -0.0090 0.0112  318 RET A C8  
4212 C C9  . RET S .   ? 0.2277 0.2614 0.2669 0.0045  -0.0146 0.0077  318 RET A C9  
4213 C C10 . RET S .   ? 0.2179 0.2665 0.2705 -0.0018 -0.0175 0.0082  318 RET A C10 
4214 C C11 . RET S .   ? 0.2326 0.2823 0.2887 -0.0053 -0.0228 0.0063  318 RET A C11 
4215 C C12 . RET S .   ? 0.2296 0.2893 0.2971 -0.0108 -0.0243 0.0072  318 RET A C12 
4216 C C13 . RET S .   ? 0.2248 0.2857 0.2949 -0.0129 -0.0288 0.0070  318 RET A C13 
4217 C C14 . RET S .   ? 0.2323 0.2993 0.3099 -0.0172 -0.0284 0.0088  318 RET A C14 
4218 C C15 . RET S .   ? 0.2651 0.3328 0.3419 -0.0183 -0.0306 0.0110  318 RET A C15 
4219 C C16 . RET S .   ? 0.2610 0.2996 0.3088 0.0033  -0.0014 0.0157  318 RET A C16 
4220 C C17 . RET S .   ? 0.3155 0.3815 0.3542 0.0194  0.0011  0.0247  318 RET A C17 
4221 C C18 . RET S .   ? 0.2872 0.2515 0.2665 0.0345  0.0050  0.0127  318 RET A C18 
4222 C C19 . RET S .   ? 0.2631 0.2766 0.2865 0.0074  -0.0171 0.0034  318 RET A C19 
4223 C C20 . RET S .   ? 0.2643 0.3171 0.3252 -0.0099 -0.0336 0.0050  318 RET A C20 
# 
