data_9F9G
# 
_entry.id   9F9G 
# 
_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   9F9G         pdb_00009f9g 10.2210/pdb9f9g/pdb 
WWPDB D_1292135920 ?            ?                   
# 
_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                        9F9G 
_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                                                                        25303.887 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    46 ? ? ? ? 
# 
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       
;ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM
RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
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   ILE 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   ILE 1   4   4   ILE ILE 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  301 302 LI1 LI1 A . 
C 2 LI1 1  302 303 LI1 LI1 A . 
D 2 LI1 1  303 305 LI1 LI1 A . 
E 2 LI1 1  304 306 LI1 LI1 A . 
F 2 LI1 1  305 307 LI1 LI1 A . 
G 2 LI1 1  306 308 LI1 LI1 A . 
H 3 OLC 1  307 309 OLC OLC A . 
I 3 OLC 1  308 310 OLC OLC A . 
J 3 OLC 1  309 312 OLC OLC A . 
K 3 OLC 1  310 313 OLC OLC A . 
L 3 OLC 1  311 314 OLC OLC A . 
M 2 LI1 1  312 316 LI1 LI1 A . 
N 2 LI1 1  313 317 LI1 LI1 A . 
O 2 LI1 1  314 318 LI1 LI1 A . 
P 2 LI1 1  315 319 LI1 LI1 A . 
Q 2 LI1 1  316 320 LI1 LI1 A . 
R 2 LI1 1  317 321 LI1 LI1 A . 
S 4 RET 1  318 216 RET LYR A . 
T 5 HOH 1  401 480 HOH HOH A . 
T 5 HOH 2  402 441 HOH HOH A . 
T 5 HOH 3  403 482 HOH HOH A . 
T 5 HOH 4  404 403 HOH HOH A . 
T 5 HOH 5  405 404 HOH HOH A . 
T 5 HOH 6  406 486 HOH HOH A . 
T 5 HOH 7  407 493 HOH HOH A . 
T 5 HOH 8  408 402 HOH HOH A . 
T 5 HOH 9  409 511 HOH HOH A . 
T 5 HOH 10 410 434 HOH HOH A . 
T 5 HOH 11 411 401 HOH HOH A . 
T 5 HOH 12 412 400 HOH HOH A . 
T 5 HOH 13 413 495 HOH HOH A . 
T 5 HOH 14 414 411 HOH HOH A . 
T 5 HOH 15 415 414 HOH HOH A . 
T 5 HOH 16 416 504 HOH HOH A . 
T 5 HOH 17 417 456 HOH HOH A . 
T 5 HOH 18 418 485 HOH HOH A . 
T 5 HOH 19 419 510 HOH HOH A . 
T 5 HOH 20 420 407 HOH HOH A . 
T 5 HOH 21 421 477 HOH HOH A . 
T 5 HOH 22 422 412 HOH HOH A . 
T 5 HOH 23 423 409 HOH HOH A . 
T 5 HOH 24 424 502 HOH HOH A . 
T 5 HOH 25 425 417 HOH HOH A . 
T 5 HOH 26 426 478 HOH HOH A . 
T 5 HOH 27 427 421 HOH HOH A . 
T 5 HOH 28 428 487 HOH HOH A . 
T 5 HOH 29 429 479 HOH HOH A . 
T 5 HOH 30 430 416 HOH HOH A . 
T 5 HOH 31 431 415 HOH HOH A . 
T 5 HOH 32 432 419 HOH HOH A . 
T 5 HOH 33 433 503 HOH HOH A . 
T 5 HOH 34 434 505 HOH HOH A . 
T 5 HOH 35 435 509 HOH HOH A . 
T 5 HOH 36 436 507 HOH HOH A . 
T 5 HOH 37 437 420 HOH HOH A . 
T 5 HOH 38 438 418 HOH HOH A . 
T 5 HOH 39 439 413 HOH HOH A . 
T 5 HOH 40 440 422 HOH HOH A . 
T 5 HOH 41 441 475 HOH HOH A . 
T 5 HOH 42 442 496 HOH HOH A . 
T 5 HOH 43 443 506 HOH HOH A . 
T 5 HOH 44 444 501 HOH HOH A . 
T 5 HOH 45 445 484 HOH HOH A . 
T 5 HOH 46 446 476 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 N 1 A LI1 301 ? C1  ? B LI1 1 C1  
2   1 N 1 A LI1 301 ? C2  ? B LI1 1 C2  
3   1 N 1 A LI1 301 ? C3  ? B LI1 1 C3  
4   1 N 1 A LI1 301 ? O1  ? B LI1 1 O1  
5   1 N 1 A LI1 301 ? O2  ? B LI1 1 O2  
6   1 N 1 A LI1 301 ? O3  ? B LI1 1 O3  
7   1 N 1 A LI1 301 ? C41 ? B LI1 1 C41 
8   1 N 1 A LI1 301 ? C42 ? B LI1 1 C42 
9   1 N 1 A LI1 301 ? C43 ? B LI1 1 C43 
10  1 N 1 A LI1 301 ? C44 ? B LI1 1 C44 
11  1 N 1 A LI1 301 ? C45 ? B LI1 1 C45 
12  1 N 1 A LI1 301 ? C46 ? B LI1 1 C46 
13  1 N 1 A LI1 301 ? C47 ? B LI1 1 C47 
14  1 N 1 A LI1 301 ? C48 ? B LI1 1 C48 
15  1 N 1 A LI1 301 ? C49 ? B LI1 1 C49 
16  1 N 1 A LI1 301 ? C50 ? B LI1 1 C50 
17  1 N 1 A LI1 301 ? C51 ? B LI1 1 C51 
18  1 N 1 A LI1 301 ? C59 ? B LI1 1 C59 
19  1 N 1 A LI1 301 ? C60 ? B LI1 1 C60 
20  1 N 1 A LI1 301 ? C11 ? B LI1 1 C11 
21  1 N 1 A LI1 301 ? C12 ? B LI1 1 C12 
22  1 N 1 A LI1 301 ? C13 ? B LI1 1 C13 
23  1 N 1 A LI1 301 ? C14 ? B LI1 1 C14 
24  1 N 1 A LI1 301 ? C15 ? B LI1 1 C15 
25  1 N 1 A LI1 301 ? C16 ? B LI1 1 C16 
26  1 N 1 A LI1 301 ? C17 ? B LI1 1 C17 
27  1 N 1 A LI1 301 ? C18 ? B LI1 1 C18 
28  1 N 1 A LI1 301 ? C19 ? B LI1 1 C19 
29  1 N 1 A LI1 301 ? C20 ? B LI1 1 C20 
30  1 N 1 A LI1 301 ? C21 ? B LI1 1 C21 
31  1 N 1 A LI1 301 ? C22 ? B LI1 1 C22 
32  1 N 1 A LI1 301 ? C23 ? B LI1 1 C23 
33  1 N 1 A LI1 301 ? C24 ? B LI1 1 C24 
34  1 N 1 A LI1 301 ? C25 ? B LI1 1 C25 
35  1 N 1 A LI1 301 ? C26 ? B LI1 1 C26 
36  1 N 1 A LI1 301 ? C27 ? B LI1 1 C27 
37  1 N 1 A LI1 301 ? C28 ? B LI1 1 C28 
38  1 N 1 A LI1 301 ? C29 ? B LI1 1 C29 
39  1 N 1 A LI1 301 ? C30 ? B LI1 1 C30 
40  1 N 1 A LI1 302 ? C1  ? C LI1 1 C1  
41  1 N 1 A LI1 302 ? C2  ? C LI1 1 C2  
42  1 N 1 A LI1 302 ? C3  ? C LI1 1 C3  
43  1 N 1 A LI1 302 ? O1  ? C LI1 1 O1  
44  1 N 1 A LI1 302 ? O2  ? C LI1 1 O2  
45  1 N 1 A LI1 302 ? O3  ? C LI1 1 O3  
46  1 N 1 A LI1 302 ? C41 ? C LI1 1 C41 
47  1 N 1 A LI1 302 ? C42 ? C LI1 1 C42 
48  1 N 1 A LI1 302 ? C43 ? C LI1 1 C43 
49  1 N 1 A LI1 302 ? C44 ? C LI1 1 C44 
50  1 N 1 A LI1 302 ? C45 ? C LI1 1 C45 
51  1 N 1 A LI1 302 ? C11 ? C LI1 1 C11 
52  1 N 1 A LI1 302 ? C12 ? C LI1 1 C12 
53  1 N 1 A LI1 302 ? C13 ? C LI1 1 C13 
54  1 N 1 A LI1 302 ? C14 ? C LI1 1 C14 
55  1 N 1 A LI1 302 ? C15 ? C LI1 1 C15 
56  1 N 1 A LI1 302 ? C16 ? C LI1 1 C16 
57  1 N 1 A LI1 302 ? C17 ? C LI1 1 C17 
58  1 N 1 A LI1 302 ? C18 ? C LI1 1 C18 
59  1 N 1 A LI1 302 ? C19 ? C LI1 1 C19 
60  1 N 1 A LI1 302 ? C20 ? C LI1 1 C20 
61  1 N 1 A LI1 302 ? C21 ? C LI1 1 C21 
62  1 N 1 A LI1 302 ? C22 ? C LI1 1 C22 
63  1 N 1 A LI1 302 ? C23 ? C LI1 1 C23 
64  1 N 1 A LI1 302 ? C24 ? C LI1 1 C24 
65  1 N 1 A LI1 302 ? C25 ? C LI1 1 C25 
66  1 N 1 A LI1 302 ? C26 ? C LI1 1 C26 
67  1 N 1 A LI1 302 ? C27 ? C LI1 1 C27 
68  1 N 1 A LI1 302 ? C28 ? C LI1 1 C28 
69  1 N 1 A LI1 302 ? C29 ? C LI1 1 C29 
70  1 N 1 A LI1 302 ? C30 ? C LI1 1 C30 
71  1 N 1 A LI1 303 ? C1  ? D LI1 1 C1  
72  1 N 1 A LI1 303 ? C2  ? D LI1 1 C2  
73  1 N 1 A LI1 303 ? C3  ? D LI1 1 C3  
74  1 N 1 A LI1 303 ? O1  ? D LI1 1 O1  
75  1 N 1 A LI1 303 ? O2  ? D LI1 1 O2  
76  1 N 1 A LI1 303 ? O3  ? D LI1 1 O3  
77  1 N 1 A LI1 303 ? C41 ? D LI1 1 C41 
78  1 N 1 A LI1 303 ? C42 ? D LI1 1 C42 
79  1 N 1 A LI1 303 ? C43 ? D LI1 1 C43 
80  1 N 1 A LI1 303 ? C44 ? D LI1 1 C44 
81  1 N 1 A LI1 303 ? C45 ? D LI1 1 C45 
82  1 N 1 A LI1 303 ? C46 ? D LI1 1 C46 
83  1 N 1 A LI1 303 ? C47 ? D LI1 1 C47 
84  1 N 1 A LI1 303 ? C48 ? D LI1 1 C48 
85  1 N 1 A LI1 303 ? C49 ? D LI1 1 C49 
86  1 N 1 A LI1 303 ? C59 ? D LI1 1 C59 
87  1 N 1 A LI1 303 ? C60 ? D LI1 1 C60 
88  1 N 1 A LI1 303 ? C11 ? D LI1 1 C11 
89  1 N 1 A LI1 303 ? C12 ? D LI1 1 C12 
90  1 N 1 A LI1 303 ? C13 ? D LI1 1 C13 
91  1 N 1 A LI1 303 ? C14 ? D LI1 1 C14 
92  1 N 1 A LI1 303 ? C15 ? D LI1 1 C15 
93  1 N 1 A LI1 303 ? C16 ? D LI1 1 C16 
94  1 N 1 A LI1 303 ? C17 ? D LI1 1 C17 
95  1 N 1 A LI1 303 ? C18 ? D LI1 1 C18 
96  1 N 1 A LI1 303 ? C19 ? D LI1 1 C19 
97  1 N 1 A LI1 303 ? C20 ? D LI1 1 C20 
98  1 N 1 A LI1 303 ? C21 ? D LI1 1 C21 
99  1 N 1 A LI1 303 ? C22 ? D LI1 1 C22 
100 1 N 1 A LI1 303 ? C23 ? D LI1 1 C23 
101 1 N 1 A LI1 303 ? C24 ? D LI1 1 C24 
102 1 N 1 A LI1 303 ? C25 ? D LI1 1 C25 
103 1 N 1 A LI1 303 ? C26 ? D LI1 1 C26 
104 1 N 1 A LI1 303 ? C27 ? D LI1 1 C27 
105 1 N 1 A LI1 303 ? C28 ? D LI1 1 C28 
106 1 N 1 A LI1 303 ? C29 ? D LI1 1 C29 
107 1 N 1 A LI1 303 ? C30 ? D LI1 1 C30 
108 1 N 1 A LI1 304 ? C1  ? E LI1 1 C1  
109 1 N 1 A LI1 304 ? C2  ? E LI1 1 C2  
110 1 N 1 A LI1 304 ? C3  ? E LI1 1 C3  
111 1 N 1 A LI1 304 ? O1  ? E LI1 1 O1  
112 1 N 1 A LI1 304 ? O2  ? E LI1 1 O2  
113 1 N 1 A LI1 304 ? O3  ? E LI1 1 O3  
114 1 N 1 A LI1 304 ? C41 ? E LI1 1 C41 
115 1 N 1 A LI1 304 ? C42 ? E LI1 1 C42 
116 1 N 1 A LI1 304 ? C43 ? E LI1 1 C43 
117 1 N 1 A LI1 304 ? C44 ? E LI1 1 C44 
118 1 N 1 A LI1 304 ? C49 ? E LI1 1 C49 
119 1 N 1 A LI1 304 ? C59 ? E LI1 1 C59 
120 1 N 1 A LI1 304 ? C60 ? E LI1 1 C60 
121 1 N 1 A LI1 304 ? C11 ? E LI1 1 C11 
122 1 N 1 A LI1 304 ? C12 ? E LI1 1 C12 
123 1 N 1 A LI1 304 ? C13 ? E LI1 1 C13 
124 1 N 1 A LI1 304 ? C14 ? E LI1 1 C14 
125 1 N 1 A LI1 304 ? C15 ? E LI1 1 C15 
126 1 N 1 A LI1 304 ? C16 ? E LI1 1 C16 
127 1 N 1 A LI1 304 ? C17 ? E LI1 1 C17 
128 1 N 1 A LI1 304 ? C18 ? E LI1 1 C18 
129 1 N 1 A LI1 304 ? C19 ? E LI1 1 C19 
130 1 N 1 A LI1 304 ? C20 ? E LI1 1 C20 
131 1 N 1 A LI1 304 ? C21 ? E LI1 1 C21 
132 1 N 1 A LI1 304 ? C22 ? E LI1 1 C22 
133 1 N 1 A LI1 304 ? C23 ? E LI1 1 C23 
134 1 N 1 A LI1 304 ? C24 ? E LI1 1 C24 
135 1 N 1 A LI1 304 ? C25 ? E LI1 1 C25 
136 1 N 1 A LI1 304 ? C26 ? E LI1 1 C26 
137 1 N 1 A LI1 304 ? C27 ? E LI1 1 C27 
138 1 N 1 A LI1 304 ? C28 ? E LI1 1 C28 
139 1 N 1 A LI1 304 ? C29 ? E LI1 1 C29 
140 1 N 1 A LI1 304 ? C30 ? E LI1 1 C30 
141 1 N 1 A LI1 305 ? C1  ? F LI1 1 C1  
142 1 N 1 A LI1 305 ? C2  ? F LI1 1 C2  
143 1 N 1 A LI1 305 ? C3  ? F LI1 1 C3  
144 1 N 1 A LI1 305 ? O1  ? F LI1 1 O1  
145 1 N 1 A LI1 305 ? O2  ? F LI1 1 O2  
146 1 N 1 A LI1 305 ? O3  ? F LI1 1 O3  
147 1 N 1 A LI1 305 ? C41 ? F LI1 1 C41 
148 1 N 1 A LI1 305 ? C42 ? F LI1 1 C42 
149 1 N 1 A LI1 305 ? C43 ? F LI1 1 C43 
150 1 N 1 A LI1 305 ? C44 ? F LI1 1 C44 
151 1 N 1 A LI1 305 ? C49 ? F LI1 1 C49 
152 1 N 1 A LI1 305 ? C60 ? F LI1 1 C60 
153 1 N 1 A LI1 305 ? C11 ? F LI1 1 C11 
154 1 N 1 A LI1 305 ? C12 ? F LI1 1 C12 
155 1 N 1 A LI1 305 ? C13 ? F LI1 1 C13 
156 1 N 1 A LI1 305 ? C14 ? F LI1 1 C14 
157 1 N 1 A LI1 305 ? C15 ? F LI1 1 C15 
158 1 N 1 A LI1 305 ? C16 ? F LI1 1 C16 
159 1 N 1 A LI1 305 ? C17 ? F LI1 1 C17 
160 1 N 1 A LI1 305 ? C18 ? F LI1 1 C18 
161 1 N 1 A LI1 305 ? C19 ? F LI1 1 C19 
162 1 N 1 A LI1 305 ? C20 ? F LI1 1 C20 
163 1 N 1 A LI1 305 ? C21 ? F LI1 1 C21 
164 1 N 1 A LI1 305 ? C22 ? F LI1 1 C22 
165 1 N 1 A LI1 305 ? C23 ? F LI1 1 C23 
166 1 N 1 A LI1 305 ? C24 ? F LI1 1 C24 
167 1 N 1 A LI1 305 ? C25 ? F LI1 1 C25 
168 1 N 1 A LI1 305 ? C26 ? F LI1 1 C26 
169 1 N 1 A LI1 305 ? C27 ? F LI1 1 C27 
170 1 N 1 A LI1 305 ? C28 ? F LI1 1 C28 
171 1 N 1 A LI1 305 ? C29 ? F LI1 1 C29 
172 1 N 1 A LI1 305 ? C30 ? F LI1 1 C30 
173 1 N 1 A LI1 306 ? C1  ? G LI1 1 C1  
174 1 N 1 A LI1 306 ? C2  ? G LI1 1 C2  
175 1 N 1 A LI1 306 ? C3  ? G LI1 1 C3  
176 1 N 1 A LI1 306 ? O1  ? G LI1 1 O1  
177 1 N 1 A LI1 306 ? O2  ? G LI1 1 O2  
178 1 N 1 A LI1 306 ? O3  ? G LI1 1 O3  
179 1 N 1 A LI1 306 ? C41 ? G LI1 1 C41 
180 1 N 1 A LI1 306 ? C42 ? G LI1 1 C42 
181 1 N 1 A LI1 306 ? C43 ? G LI1 1 C43 
182 1 N 1 A LI1 306 ? C44 ? G LI1 1 C44 
183 1 N 1 A LI1 306 ? C45 ? G LI1 1 C45 
184 1 N 1 A LI1 306 ? C49 ? G LI1 1 C49 
185 1 N 1 A LI1 306 ? C11 ? G LI1 1 C11 
186 1 N 1 A LI1 306 ? C12 ? G LI1 1 C12 
187 1 N 1 A LI1 306 ? C13 ? G LI1 1 C13 
188 1 N 1 A LI1 306 ? C14 ? G LI1 1 C14 
189 1 N 1 A LI1 306 ? C15 ? G LI1 1 C15 
190 1 N 1 A LI1 306 ? C16 ? G LI1 1 C16 
191 1 N 1 A LI1 306 ? C17 ? G LI1 1 C17 
192 1 N 1 A LI1 306 ? C18 ? G LI1 1 C18 
193 1 N 1 A LI1 306 ? C19 ? G LI1 1 C19 
194 1 N 1 A LI1 306 ? C20 ? G LI1 1 C20 
195 1 N 1 A LI1 306 ? C21 ? G LI1 1 C21 
196 1 N 1 A LI1 306 ? C22 ? G LI1 1 C22 
197 1 N 1 A LI1 306 ? C23 ? G LI1 1 C23 
198 1 N 1 A LI1 306 ? C24 ? G LI1 1 C24 
199 1 N 1 A LI1 306 ? C25 ? G LI1 1 C25 
200 1 N 1 A LI1 306 ? C26 ? G LI1 1 C26 
201 1 N 1 A LI1 306 ? C27 ? G LI1 1 C27 
202 1 N 1 A LI1 306 ? C28 ? G LI1 1 C28 
203 1 N 1 A LI1 306 ? C29 ? G LI1 1 C29 
204 1 N 1 A LI1 306 ? C30 ? G LI1 1 C30 
205 1 N 1 A LI1 312 ? C1  ? M LI1 1 C1  
206 1 N 1 A LI1 312 ? C2  ? M LI1 1 C2  
207 1 N 1 A LI1 312 ? C3  ? M LI1 1 C3  
208 1 N 1 A LI1 312 ? O1  ? M LI1 1 O1  
209 1 N 1 A LI1 312 ? O2  ? M LI1 1 O2  
210 1 N 1 A LI1 312 ? O3  ? M LI1 1 O3  
211 1 N 1 A LI1 312 ? C41 ? M LI1 1 C41 
212 1 N 1 A LI1 312 ? C42 ? M LI1 1 C42 
213 1 N 1 A LI1 312 ? C43 ? M LI1 1 C43 
214 1 N 1 A LI1 312 ? C44 ? M LI1 1 C44 
215 1 N 1 A LI1 312 ? C49 ? M LI1 1 C49 
216 1 N 1 A LI1 312 ? C57 ? M LI1 1 C57 
217 1 N 1 A LI1 312 ? C58 ? M LI1 1 C58 
218 1 N 1 A LI1 312 ? C59 ? M LI1 1 C59 
219 1 N 1 A LI1 312 ? C60 ? M LI1 1 C60 
220 1 N 1 A LI1 312 ? C11 ? M LI1 1 C11 
221 1 N 1 A LI1 312 ? C12 ? M LI1 1 C12 
222 1 N 1 A LI1 312 ? C13 ? M LI1 1 C13 
223 1 N 1 A LI1 312 ? C14 ? M LI1 1 C14 
224 1 N 1 A LI1 312 ? C15 ? M LI1 1 C15 
225 1 N 1 A LI1 312 ? C16 ? M LI1 1 C16 
226 1 N 1 A LI1 312 ? C17 ? M LI1 1 C17 
227 1 N 1 A LI1 312 ? C18 ? M LI1 1 C18 
228 1 N 1 A LI1 312 ? C19 ? M LI1 1 C19 
229 1 N 1 A LI1 312 ? C20 ? M LI1 1 C20 
230 1 N 1 A LI1 312 ? C21 ? M LI1 1 C21 
231 1 N 1 A LI1 312 ? C22 ? M LI1 1 C22 
232 1 N 1 A LI1 312 ? C23 ? M LI1 1 C23 
233 1 N 1 A LI1 312 ? C24 ? M LI1 1 C24 
234 1 N 1 A LI1 312 ? C25 ? M LI1 1 C25 
235 1 N 1 A LI1 312 ? C26 ? M LI1 1 C26 
236 1 N 1 A LI1 312 ? C27 ? M LI1 1 C27 
237 1 N 1 A LI1 312 ? C28 ? M LI1 1 C28 
238 1 N 1 A LI1 312 ? C29 ? M LI1 1 C29 
239 1 N 1 A LI1 312 ? C30 ? M LI1 1 C30 
240 1 N 1 A LI1 313 ? C1  ? N LI1 1 C1  
241 1 N 1 A LI1 313 ? C2  ? N LI1 1 C2  
242 1 N 1 A LI1 313 ? C3  ? N LI1 1 C3  
243 1 N 1 A LI1 313 ? O1  ? N LI1 1 O1  
244 1 N 1 A LI1 313 ? O2  ? N LI1 1 O2  
245 1 N 1 A LI1 313 ? O3  ? N LI1 1 O3  
246 1 N 1 A LI1 313 ? C41 ? N LI1 1 C41 
247 1 N 1 A LI1 313 ? C42 ? N LI1 1 C42 
248 1 N 1 A LI1 313 ? C43 ? N LI1 1 C43 
249 1 N 1 A LI1 313 ? C44 ? N LI1 1 C44 
250 1 N 1 A LI1 313 ? C49 ? N LI1 1 C49 
251 1 N 1 A LI1 313 ? C60 ? N LI1 1 C60 
252 1 N 1 A LI1 313 ? C11 ? N LI1 1 C11 
253 1 N 1 A LI1 313 ? C12 ? N LI1 1 C12 
254 1 N 1 A LI1 313 ? C13 ? N LI1 1 C13 
255 1 N 1 A LI1 313 ? C14 ? N LI1 1 C14 
256 1 N 1 A LI1 313 ? C15 ? N LI1 1 C15 
257 1 N 1 A LI1 313 ? C16 ? N LI1 1 C16 
258 1 N 1 A LI1 313 ? C17 ? N LI1 1 C17 
259 1 N 1 A LI1 313 ? C18 ? N LI1 1 C18 
260 1 N 1 A LI1 313 ? C19 ? N LI1 1 C19 
261 1 N 1 A LI1 313 ? C20 ? N LI1 1 C20 
262 1 N 1 A LI1 313 ? C21 ? N LI1 1 C21 
263 1 N 1 A LI1 313 ? C22 ? N LI1 1 C22 
264 1 N 1 A LI1 313 ? C23 ? N LI1 1 C23 
265 1 N 1 A LI1 313 ? C24 ? N LI1 1 C24 
266 1 N 1 A LI1 313 ? C25 ? N LI1 1 C25 
267 1 N 1 A LI1 313 ? C26 ? N LI1 1 C26 
268 1 N 1 A LI1 313 ? C27 ? N LI1 1 C27 
269 1 N 1 A LI1 313 ? C28 ? N LI1 1 C28 
270 1 N 1 A LI1 313 ? C29 ? N LI1 1 C29 
271 1 N 1 A LI1 313 ? C30 ? N LI1 1 C30 
272 1 N 1 A LI1 314 ? C1  ? O LI1 1 C1  
273 1 N 1 A LI1 314 ? C2  ? O LI1 1 C2  
274 1 N 1 A LI1 314 ? C3  ? O LI1 1 C3  
275 1 N 1 A LI1 314 ? O1  ? O LI1 1 O1  
276 1 N 1 A LI1 314 ? O2  ? O LI1 1 O2  
277 1 N 1 A LI1 314 ? O3  ? O LI1 1 O3  
278 1 N 1 A LI1 314 ? C41 ? O LI1 1 C41 
279 1 N 1 A LI1 314 ? C42 ? O LI1 1 C42 
280 1 N 1 A LI1 314 ? C43 ? O LI1 1 C43 
281 1 N 1 A LI1 314 ? C44 ? O LI1 1 C44 
282 1 N 1 A LI1 314 ? C45 ? O LI1 1 C45 
283 1 N 1 A LI1 314 ? C46 ? O LI1 1 C46 
284 1 N 1 A LI1 314 ? C47 ? O LI1 1 C47 
285 1 N 1 A LI1 314 ? C48 ? O LI1 1 C48 
286 1 N 1 A LI1 314 ? C49 ? O LI1 1 C49 
287 1 N 1 A LI1 314 ? C59 ? O LI1 1 C59 
288 1 N 1 A LI1 314 ? C60 ? O LI1 1 C60 
289 1 N 1 A LI1 314 ? C11 ? O LI1 1 C11 
290 1 N 1 A LI1 314 ? C12 ? O LI1 1 C12 
291 1 N 1 A LI1 314 ? C13 ? O LI1 1 C13 
292 1 N 1 A LI1 314 ? C14 ? O LI1 1 C14 
293 1 N 1 A LI1 314 ? C15 ? O LI1 1 C15 
294 1 N 1 A LI1 314 ? C16 ? O LI1 1 C16 
295 1 N 1 A LI1 314 ? C17 ? O LI1 1 C17 
296 1 N 1 A LI1 314 ? C18 ? O LI1 1 C18 
297 1 N 1 A LI1 314 ? C19 ? O LI1 1 C19 
298 1 N 1 A LI1 314 ? C20 ? O LI1 1 C20 
299 1 N 1 A LI1 314 ? C21 ? O LI1 1 C21 
300 1 N 1 A LI1 314 ? C22 ? O LI1 1 C22 
301 1 N 1 A LI1 314 ? C23 ? O LI1 1 C23 
302 1 N 1 A LI1 314 ? C24 ? O LI1 1 C24 
303 1 N 1 A LI1 314 ? C25 ? O LI1 1 C25 
304 1 N 1 A LI1 314 ? C26 ? O LI1 1 C26 
305 1 N 1 A LI1 314 ? C27 ? O LI1 1 C27 
306 1 N 1 A LI1 314 ? C28 ? O LI1 1 C28 
307 1 N 1 A LI1 314 ? C29 ? O LI1 1 C29 
308 1 N 1 A LI1 314 ? C30 ? O LI1 1 C30 
309 1 N 1 A LI1 315 ? C1  ? P LI1 1 C1  
310 1 N 1 A LI1 315 ? C2  ? P LI1 1 C2  
311 1 N 1 A LI1 315 ? C3  ? P LI1 1 C3  
312 1 N 1 A LI1 315 ? O1  ? P LI1 1 O1  
313 1 N 1 A LI1 315 ? O2  ? P LI1 1 O2  
314 1 N 1 A LI1 315 ? O3  ? P LI1 1 O3  
315 1 N 1 A LI1 315 ? C41 ? P LI1 1 C41 
316 1 N 1 A LI1 315 ? C42 ? P LI1 1 C42 
317 1 N 1 A LI1 315 ? C43 ? P LI1 1 C43 
318 1 N 1 A LI1 315 ? C44 ? P LI1 1 C44 
319 1 N 1 A LI1 315 ? C45 ? P LI1 1 C45 
320 1 N 1 A LI1 315 ? C49 ? P LI1 1 C49 
321 1 N 1 A LI1 315 ? C11 ? P LI1 1 C11 
322 1 N 1 A LI1 315 ? C12 ? P LI1 1 C12 
323 1 N 1 A LI1 315 ? C13 ? P LI1 1 C13 
324 1 N 1 A LI1 315 ? C14 ? P LI1 1 C14 
325 1 N 1 A LI1 315 ? C15 ? P LI1 1 C15 
326 1 N 1 A LI1 315 ? C16 ? P LI1 1 C16 
327 1 N 1 A LI1 315 ? C17 ? P LI1 1 C17 
328 1 N 1 A LI1 315 ? C18 ? P LI1 1 C18 
329 1 N 1 A LI1 315 ? C19 ? P LI1 1 C19 
330 1 N 1 A LI1 315 ? C20 ? P LI1 1 C20 
331 1 N 1 A LI1 315 ? C21 ? P LI1 1 C21 
332 1 N 1 A LI1 315 ? C22 ? P LI1 1 C22 
333 1 N 1 A LI1 315 ? C23 ? P LI1 1 C23 
334 1 N 1 A LI1 315 ? C24 ? P LI1 1 C24 
335 1 N 1 A LI1 315 ? C25 ? P LI1 1 C25 
336 1 N 1 A LI1 315 ? C26 ? P LI1 1 C26 
337 1 N 1 A LI1 315 ? C27 ? P LI1 1 C27 
338 1 N 1 A LI1 315 ? C28 ? P LI1 1 C28 
339 1 N 1 A LI1 315 ? C29 ? P LI1 1 C29 
340 1 N 1 A LI1 315 ? C30 ? P LI1 1 C30 
341 1 N 1 A LI1 316 ? C1  ? Q LI1 1 C1  
342 1 N 1 A LI1 316 ? C2  ? Q LI1 1 C2  
343 1 N 1 A LI1 316 ? C3  ? Q LI1 1 C3  
344 1 N 1 A LI1 316 ? O1  ? Q LI1 1 O1  
345 1 N 1 A LI1 316 ? O2  ? Q LI1 1 O2  
346 1 N 1 A LI1 316 ? O3  ? Q LI1 1 O3  
347 1 N 1 A LI1 316 ? C41 ? Q LI1 1 C41 
348 1 N 1 A LI1 316 ? C42 ? Q LI1 1 C42 
349 1 N 1 A LI1 316 ? C43 ? Q LI1 1 C43 
350 1 N 1 A LI1 316 ? C44 ? Q LI1 1 C44 
351 1 N 1 A LI1 316 ? C49 ? Q LI1 1 C49 
352 1 N 1 A LI1 316 ? C60 ? Q LI1 1 C60 
353 1 N 1 A LI1 316 ? C11 ? Q LI1 1 C11 
354 1 N 1 A LI1 316 ? C12 ? Q LI1 1 C12 
355 1 N 1 A LI1 316 ? C13 ? Q LI1 1 C13 
356 1 N 1 A LI1 316 ? C14 ? Q LI1 1 C14 
357 1 N 1 A LI1 316 ? C15 ? Q LI1 1 C15 
358 1 N 1 A LI1 316 ? C16 ? Q LI1 1 C16 
359 1 N 1 A LI1 316 ? C17 ? Q LI1 1 C17 
360 1 N 1 A LI1 316 ? C18 ? Q LI1 1 C18 
361 1 N 1 A LI1 316 ? C19 ? Q LI1 1 C19 
362 1 N 1 A LI1 316 ? C20 ? Q LI1 1 C20 
363 1 N 1 A LI1 316 ? C21 ? Q LI1 1 C21 
364 1 N 1 A LI1 316 ? C22 ? Q LI1 1 C22 
365 1 N 1 A LI1 316 ? C23 ? Q LI1 1 C23 
366 1 N 1 A LI1 316 ? C24 ? Q LI1 1 C24 
367 1 N 1 A LI1 316 ? C25 ? Q LI1 1 C25 
368 1 N 1 A LI1 316 ? C26 ? Q LI1 1 C26 
369 1 N 1 A LI1 316 ? C27 ? Q LI1 1 C27 
370 1 N 1 A LI1 316 ? C28 ? Q LI1 1 C28 
371 1 N 1 A LI1 316 ? C29 ? Q LI1 1 C29 
372 1 N 1 A LI1 316 ? C30 ? Q LI1 1 C30 
373 1 N 1 A LI1 317 ? C1  ? R LI1 1 C1  
374 1 N 1 A LI1 317 ? C2  ? R LI1 1 C2  
375 1 N 1 A LI1 317 ? C3  ? R LI1 1 C3  
376 1 N 1 A LI1 317 ? O1  ? R LI1 1 O1  
377 1 N 1 A LI1 317 ? O2  ? R LI1 1 O2  
378 1 N 1 A LI1 317 ? O3  ? R LI1 1 O3  
379 1 N 1 A LI1 317 ? C41 ? R LI1 1 C41 
380 1 N 1 A LI1 317 ? C42 ? R LI1 1 C42 
381 1 N 1 A LI1 317 ? C43 ? R LI1 1 C43 
382 1 N 1 A LI1 317 ? C44 ? R LI1 1 C44 
383 1 N 1 A LI1 317 ? C45 ? R LI1 1 C45 
384 1 N 1 A LI1 317 ? C46 ? R LI1 1 C46 
385 1 N 1 A LI1 317 ? C47 ? R LI1 1 C47 
386 1 N 1 A LI1 317 ? C48 ? R LI1 1 C48 
387 1 N 1 A LI1 317 ? C49 ? R LI1 1 C49 
388 1 N 1 A LI1 317 ? C50 ? R LI1 1 C50 
389 1 N 1 A LI1 317 ? C51 ? R LI1 1 C51 
390 1 N 1 A LI1 317 ? C59 ? R LI1 1 C59 
391 1 N 1 A LI1 317 ? C60 ? R LI1 1 C60 
392 1 N 1 A LI1 317 ? C11 ? R LI1 1 C11 
393 1 N 1 A LI1 317 ? C12 ? R LI1 1 C12 
394 1 N 1 A LI1 317 ? C13 ? R LI1 1 C13 
395 1 N 1 A LI1 317 ? C14 ? R LI1 1 C14 
396 1 N 1 A LI1 317 ? C15 ? R LI1 1 C15 
397 1 N 1 A LI1 317 ? C16 ? R LI1 1 C16 
398 1 N 1 A LI1 317 ? C17 ? R LI1 1 C17 
399 1 N 1 A LI1 317 ? C18 ? R LI1 1 C18 
400 1 N 1 A LI1 317 ? C19 ? R LI1 1 C19 
401 1 N 1 A LI1 317 ? C20 ? R LI1 1 C20 
402 1 N 1 A LI1 317 ? C21 ? R LI1 1 C21 
403 1 N 1 A LI1 317 ? C22 ? R LI1 1 C22 
404 1 N 1 A LI1 317 ? C23 ? R LI1 1 C23 
405 1 N 1 A LI1 317 ? C24 ? R LI1 1 C24 
406 1 N 1 A LI1 317 ? C25 ? R LI1 1 C25 
407 1 N 1 A LI1 317 ? C26 ? R LI1 1 C26 
408 1 N 1 A LI1 317 ? C27 ? R LI1 1 C27 
409 1 N 1 A LI1 317 ? C28 ? R LI1 1 C28 
410 1 N 1 A LI1 317 ? C29 ? R LI1 1 C29 
411 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                     9F9G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.320 
_cell.length_a_esd                 ? 
_cell.length_b                     62.320 
_cell.length_b_esd                 ? 
_cell.length_c                     111.100 
_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                         9F9G 
_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                   9F9G 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.50 
_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                     298 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'CS-PAD CXI-1' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-06-03 
_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   1.3 
_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                        'SLAC LCLS BEAMLINE CXI' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.3 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   CXI 
_diffrn_source.pdbx_synchrotron_site       'SLAC LCLS' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F9G 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.44 
_reflns.d_resolution_low                               20.06 
_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                                     45078 
_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                                1371 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.13 
_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                                   0.0301 
_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                                    1.44 
_reflns_shell.d_res_low                                     1.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.87 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4511 
_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                                  0.87 
_reflns_shell.pdbx_R_split                                  1.11 
_reflns_shell.percent_possible_all                          ? 
_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                                 9F9G 
_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                            1.44 
_refine.ls_d_res_low                             20.06 
_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                     44100 
_refine.ls_number_reflns_R_free                  1987 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 4.51 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1497 
_refine.ls_R_factor_R_free                       0.1721 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1486 
_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                          1.33 
_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                 20.07 
_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                            0.21 
_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                       1.44 
_refine_hist.d_res_low                        20.06 
_refine_hist.number_atoms_solvent             46 
_refine_hist.number_atoms_total               2107 
_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        1807 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         254 
_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' ? 0.022  ? 2171 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.947  ? 2887 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.230 ? 848  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.135  ? 315  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.015  ? 341  ? 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' 1.44 1.48  . . 141 2988 100.00 . . . . 0.3903 . . . . . . . . . . . 0.4514 
'X-RAY DIFFRACTION' 1.48 1.52  . . 144 3008 100.00 . . . . 0.2526 . . . . . . . . . . . 0.2853 
'X-RAY DIFFRACTION' 1.52 1.56  . . 138 2989 100.00 . . . . 0.1970 . . . . . . . . . . . 0.2207 
'X-RAY DIFFRACTION' 1.56 1.61  . . 139 3009 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 1.61 1.67  . . 141 2988 100.00 . . . . 0.2107 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 1.67 1.74  . . 147 3010 100.00 . . . . 0.1605 . . . . . . . . . . . 0.2130 
'X-RAY DIFFRACTION' 1.74 1.81  . . 138 2998 100.00 . . . . 0.1282 . . . . . . . . . . . 0.1493 
'X-RAY DIFFRACTION' 1.81 1.91  . . 137 3001 100.00 . . . . 0.1281 . . . . . . . . . . . 0.1592 
'X-RAY DIFFRACTION' 1.91 2.03  . . 143 3009 100.00 . . . . 0.1291 . . . . . . . . . . . 0.1630 
'X-RAY DIFFRACTION' 2.03 2.19  . . 139 3012 100.00 . . . . 0.1164 . . . . . . . . . . . 0.1395 
'X-RAY DIFFRACTION' 2.19 2.41  . . 144 3017 100.00 . . . . 0.1215 . . . . . . . . . . . 0.1380 
'X-RAY DIFFRACTION' 2.41 2.75  . . 137 3013 100.00 . . . . 0.1413 . . . . . . . . . . . 0.1623 
'X-RAY DIFFRACTION' 2.75 3.47  . . 151 3025 100.00 . . . . 0.1519 . . . . . . . . . . . 0.1563 
'X-RAY DIFFRACTION' 3.47 20.06 . . 148 3046 100.00 . . . . 0.1537 . . . . . . . . . . . 0.1855 
# 
_struct.entry_id                     9F9G 
_struct.title                        'Laser excitation effects on BR: Reprocessed Dark from Nogly et al.' 
_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        9F9G 
_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 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
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   
;ITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM
RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_struct_ref.pdbx_align_begin           17 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F9G 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_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                  17 
_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       4 
_struct_ref_seq.pdbx_auth_seq_align_end       234 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 19590 ? 
1 MORE         -250  ? 
1 'SSA (A^2)'  28920 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z        1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_665 -y+1,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 31.1600000000  0.8660254038  
-0.5000000000 0.0000000000 53.9707031638 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_565 -x+y,-x+1,z  -0.5000000000 0.8660254038  0.0000000000 -31.1600000000 -0.8660254038 
-0.5000000000 0.0000000000 53.9707031638 0.0000000000 0.0000000000 1.0000000000 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   ? MET A 29  ? GLU A 9   MET A 32  1 ? 24 
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               1.350 
_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                   9F9G 
_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_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CE1 A TYR 79  ? ? CZ  A TYR 79  ? ? 1.301 1.381 -0.080 0.013 N 
2 1 CE3 A TRP 182 ? ? CZ3 A TRP 182 ? ? 1.486 1.380 0.106  0.017 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A TYR 57  ? ? CG A TYR 57  ? ? CD1 A TYR 57  ? ? 124.83 121.00 3.83   0.60 N 
2 1 CB A TYR 64  ? ? CG A TYR 64  ? ? CD1 A TYR 64  ? ? 117.37 121.00 -3.63  0.60 N 
3 1 CB A PHE 88  ? ? CG A PHE 88  ? ? CD2 A PHE 88  ? ? 116.50 120.80 -4.30  0.70 N 
4 1 CB A ASP 96  ? ? CG A ASP 96  ? ? OD1 A ASP 96  ? ? 123.99 118.30 5.69   0.90 N 
5 1 CG A MET 209 ? ? SD A MET 209 ? ? CE  A MET 209 ? ? 81.25  100.20 -18.95 1.60 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    MET 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     163 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -111.52 
_pdbx_validate_torsion.psi             -169.78 
# 
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 23.5671 27.0338 29.5755 0.1417 ? 0.0250  ? -0.0145 ? 0.1811 ? -0.0165 ? 0.2815 ? 2.6411 ? 1.8662  
? -2.7985 ? 7.4287 ? -5.7472 ? 5.5488 ? -0.1610 ? 0.0690  ? -0.1798 ? -0.2602 ? -0.0383 ? -0.4132 ? 0.4376  ? 0.3083  ? 0.1283  ? 
2 'X-RAY DIFFRACTION' ? refined 15.1110 27.7038 41.1205 0.2359 ? 0.0128  ? -0.0352 ? 0.1904 ? 0.0242  ? 0.2307 ? 1.6660 ? -0.1958 
? 0.0497  ? 1.9552 ? 1.1900  ? 2.3534 ? -0.0237 ? -0.2863 ? -0.0822 ? 0.3969  ? 0.0650  ? -0.0576 ? 0.4148  ? -0.1883 ? 0.0201  ? 
3 'X-RAY DIFFRACTION' ? refined 12.7625 38.7229 27.8666 0.1741 ? 0.0032  ? -0.0062 ? 0.1784 ? 0.0095  ? 0.2173 ? 1.8063 ? -0.2339 
? 0.2546  ? 2.0993 ? 0.8944  ? 3.8471 ? -0.0282 ? 0.1646  ? 0.0588  ? -0.2038 ? -0.0206 ? -0.0650 ? -0.1630 ? -0.1567 ? 0.0514  ? 
4 'X-RAY DIFFRACTION' ? refined 7.5348  45.8530 37.1586 0.2033 ? 0.0117  ? -0.0146 ? 0.1938 ? -0.0073 ? 0.2261 ? 1.6991 ? -0.1033 
? -0.0212 ? 2.0664 ? -1.8876 ? 5.8493 ? 0.1085  ? -0.2017 ? 0.0126  ? 0.1586  ? 0.1582  ? 0.0513  ? 0.0711  ? -0.1436 ? -0.2447 ? 
5 'X-RAY DIFFRACTION' ? refined 13.0776 53.1062 32.7964 0.1954 ? -0.0153 ? -0.0079 ? 0.1750 ? -0.0177 ? 0.2525 ? 2.8093 ? -0.1921 
? 0.1925  ? 2.5119 ? -1.9882 ? 2.0136 ? 0.0148  ? -0.0753 ? 0.2606  ? 0.2241  ? -0.0374 ? -0.1320 ? -0.4792 ? 0.2274  ? 0.0360  ? 
6 'X-RAY DIFFRACTION' ? refined 17.6008 46.5214 57.6937 1.2221 ? -0.1134 ? -0.0596 ? 0.8253 ? -0.1373 ? 0.6151 ? 6.1991 ? -3.8361 
? 5.3057  ? 2.6694 ? -3.5812 ? 4.8416 ? -0.7252 ? -1.8965 ? 1.1991  ? 1.3881  ? 0.2067  ? -0.3373 ? -2.5507 ? -0.2152 ? 0.6404  ? 
7 'X-RAY DIFFRACTION' ? refined 22.9027 42.0320 35.3948 0.1751 ? -0.0279 ? -0.0562 ? 0.2146 ? -0.0054 ? 0.2708 ? 1.0523 ? -0.1144 
? -0.4253 ? 1.4639 ? -0.7973 ? 3.0069 ? -0.0220 ? -0.1050 ? 0.0472  ? 0.1975  ? 0.0359  ? -0.2660 ? -0.2458 ? 0.1042  ? -0.0017 ? 
8 'X-RAY DIFFRACTION' ? refined 24.7329 31.8551 53.9968 0.5077 ? -0.0092 ? -0.1807 ? 0.6334 ? 0.0720  ? 0.4284 ? 8.6293 ? -4.7389 
? -6.3285 ? 8.5322 ? 5.9889  ? 5.7948 ? -0.6180 ? -0.2890 ? 0.7057  ? 0.9577  ? 0.7909  ? -1.4020 ? 0.4303  ? 1.5108  ? -0.0755 ? 
9 'X-RAY DIFFRACTION' ? refined 18.9572 29.9782 64.6507 0.7801 ? -0.0644 ? -0.0827 ? 0.5162 ? 0.0500  ? 0.2578 ? 4.0773 ? -1.9348 
? 2.0970  ? 0.9181 ? -0.9951 ? 1.0785 ? 0.9930  ? -0.2998 ? -0.4717 ? 0.5281  ? -0.3824 ? -0.1626 ? 0.4865  ? 0.3063  ? -0.6551 ? 
# 
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                    9F9G 
_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]   0.016046 
_atom_sites.fract_transf_matrix[1][2]   0.009264 
_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]   0.018529 
_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]   0.009001 
_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    . ILE A 1 1   ? 20.338 24.941 14.169 1.00 97.15  ? 4   ILE A N    1 
ATOM   2    C CA   . ILE A 1 1   ? 20.531 25.865 15.282 1.00 96.39  ? 4   ILE A CA   1 
ATOM   3    C C    . ILE A 1 1   ? 21.886 26.562 15.156 1.00 84.77  ? 4   ILE A C    1 
ATOM   4    O O    . ILE A 1 1   ? 22.020 27.752 15.453 1.00 73.53  ? 4   ILE A O    1 
ATOM   5    C CB   . ILE A 1 1   ? 20.349 25.166 16.660 1.00 94.82  ? 4   ILE A CB   1 
ATOM   6    C CG1  . ILE A 1 1   ? 21.366 24.045 16.845 1.00 96.45  ? 4   ILE A CG1  1 
ATOM   7    C CG2  . ILE A 1 1   ? 18.934 24.610 16.818 1.00 77.32  ? 4   ILE A CG2  1 
ATOM   8    C CD1  . ILE A 1 1   ? 21.135 23.245 18.109 1.00 91.86  ? 4   ILE A CD1  1 
ATOM   9    N N    . THR A 1 2   ? 22.886 25.817 14.686 1.00 73.92  ? 5   THR A N    1 
ATOM   10   C CA   . THR A 1 2   ? 24.231 26.358 14.544 1.00 55.70  ? 5   THR A CA   1 
ATOM   11   C C    . THR A 1 2   ? 24.341 27.380 13.415 1.00 60.22  ? 5   THR A C    1 
ATOM   12   O O    . THR A 1 2   ? 25.437 27.915 13.179 1.00 65.43  ? 5   THR A O    1 
ATOM   13   C CB   . THR A 1 2   ? 25.189 25.200 14.296 1.00 71.06  ? 5   THR A CB   1 
ATOM   14   O OG1  . THR A 1 2   ? 24.660 24.381 13.248 1.00 76.46  ? 5   THR A OG1  1 
ATOM   15   C CG2  . THR A 1 2   ? 25.324 24.364 15.583 1.00 63.69  ? 5   THR A CG2  1 
ATOM   16   H HA   . THR A 1 2   ? 24.492 26.810 15.361 0.00 66.84  ? 5   THR A HA   1 
ATOM   17   H HB   . THR A 1 2   ? 26.066 25.528 14.042 0.00 85.27  ? 5   THR A HB   1 
ATOM   18   H HG1  . THR A 1 2   ? 25.205 23.770 13.059 0.00 91.76  ? 5   THR A HG1  1 
ATOM   19   H HG21 . THR A 1 2   ? 25.939 23.628 15.438 0.00 76.43  ? 5   THR A HG21 1 
ATOM   20   H HG22 . THR A 1 2   ? 25.662 24.918 16.305 0.00 76.43  ? 5   THR A HG22 1 
ATOM   21   H HG23 . THR A 1 2   ? 24.460 24.006 15.839 0.00 76.43  ? 5   THR A HG23 1 
ATOM   22   N N    . GLY A 1 3   ? 23.256 27.659 12.692 1.00 69.95  ? 6   GLY A N    1 
ATOM   23   C CA   . GLY A 1 3   ? 23.318 28.644 11.630 1.00 59.87  ? 6   GLY A CA   1 
ATOM   24   C C    . GLY A 1 3   ? 23.414 30.078 12.121 1.00 47.79  ? 6   GLY A C    1 
ATOM   25   O O    . GLY A 1 3   ? 23.779 30.959 11.351 1.00 62.62  ? 6   GLY A O    1 
ATOM   26   H H    . GLY A 1 3   ? 22.485 27.294 12.800 0.00 83.94  ? 6   GLY A H    1 
ATOM   27   H HA2  . GLY A 1 3   ? 24.096 28.464 11.080 0.00 71.85  ? 6   GLY A HA2  1 
ATOM   28   H HA3  . GLY A 1 3   ? 22.521 28.568 11.083 0.00 71.85  ? 6   GLY A HA3  1 
ATOM   29   N N    . ARG A 1 4   ? 23.076 30.320 13.382 1.00 44.87  ? 7   ARG A N    1 
ATOM   30   C CA   . ARG A 1 4   ? 23.101 31.671 13.952 1.00 37.67  ? 7   ARG A CA   1 
ATOM   31   C C    . ARG A 1 4   ? 24.378 31.805 14.771 1.00 31.87  ? 7   ARG A C    1 
ATOM   32   O O    . ARG A 1 4   ? 24.562 31.012 15.713 1.00 38.33  ? 7   ARG A O    1 
ATOM   33   C CB   . ARG A 1 4   ? 21.880 31.826 14.891 1.00 34.11  ? 7   ARG A CB   1 
ATOM   34   C CG   . ARG A 1 4   ? 20.483 31.901 14.192 1.00 37.20  ? 7   ARG A CG   1 
ATOM   35   C CD   . ARG A 1 4   ? 19.323 31.767 15.191 1.00 46.69  ? 7   ARG A CD   1 
ATOM   36   N NE   . ARG A 1 4   ? 19.004 30.367 15.502 1.00 48.00  ? 7   ARG A NE   1 
ATOM   37   C CZ   . ARG A 1 4   ? 18.612 29.917 16.699 1.00 47.18  ? 7   ARG A CZ   1 
ATOM   38   N NH1  . ARG A 1 4   ? 18.588 30.701 17.800 1.00 33.69  ? 7   ARG A NH1  1 
ATOM   39   N NH2  . ARG A 1 4   ? 18.318 28.632 16.818 1.00 49.10  ? 7   ARG A NH2  1 
ATOM   40   H H    . ARG A 1 4   ? 22.824 29.715 13.939 0.00 53.84  ? 7   ARG A H    1 
ATOM   41   H HA   . ARG A 1 4   ? 23.074 32.357 13.267 0.00 45.20  ? 7   ARG A HA   1 
ATOM   42   H HB2  . ARG A 1 4   ? 21.860 31.064 15.491 0.00 40.93  ? 7   ARG A HB2  1 
ATOM   43   H HB3  . ARG A 1 4   ? 21.991 32.645 15.400 0.00 40.93  ? 7   ARG A HB3  1 
ATOM   44   H HG2  . ARG A 1 4   ? 20.397 32.757 13.743 0.00 44.64  ? 7   ARG A HG2  1 
ATOM   45   H HG3  . ARG A 1 4   ? 20.410 31.180 13.547 0.00 44.64  ? 7   ARG A HG3  1 
ATOM   46   H HD2  . ARG A 1 4   ? 19.565 32.211 16.018 0.00 56.03  ? 7   ARG A HD2  1 
ATOM   47   H HD3  . ARG A 1 4   ? 18.530 32.179 14.813 0.00 56.03  ? 7   ARG A HD3  1 
ATOM   48   H HE   . ARG A 1 4   ? 19.074 29.793 14.866 0.00 57.60  ? 7   ARG A HE   1 
ATOM   49   H HH11 . ARG A 1 4   ? 18.831 31.524 17.748 0.00 40.43  ? 7   ARG A HH11 1 
ATOM   50   H HH12 . ARG A 1 4   ? 18.330 30.376 18.553 0.00 40.43  ? 7   ARG A HH12 1 
ATOM   51   H HH21 . ARG A 1 4   ? 18.381 28.111 16.137 0.00 58.93  ? 7   ARG A HH21 1 
ATOM   52   H HH22 . ARG A 1 4   ? 18.063 28.318 17.577 0.00 58.93  ? 7   ARG A HH22 1 
ATOM   53   N N    . PRO A 1 5   ? 25.173 32.860 14.572 1.00 32.12  ? 8   PRO A N    1 
ATOM   54   C CA   . PRO A 1 5   ? 26.455 32.944 15.287 1.00 32.48  ? 8   PRO A CA   1 
ATOM   55   C C    . PRO A 1 5   ? 26.343 32.990 16.762 1.00 33.09  ? 8   PRO A C    1 
ATOM   56   O O    . PRO A 1 5   ? 27.226 32.454 17.451 1.00 34.14  ? 8   PRO A O    1 
ATOM   57   C CB   . PRO A 1 5   ? 27.113 34.210 14.744 1.00 37.39  ? 8   PRO A CB   1 
ATOM   58   C CG   . PRO A 1 5   ? 26.030 34.961 13.995 1.00 48.72  ? 8   PRO A CG   1 
ATOM   59   C CD   . PRO A 1 5   ? 25.005 33.932 13.576 1.00 35.39  ? 8   PRO A CD   1 
ATOM   60   H HA   . PRO A 1 5   ? 26.988 32.174 15.035 0.00 38.98  ? 8   PRO A HA   1 
ATOM   61   H HB2  . PRO A 1 5   ? 27.452 34.742 15.480 0.00 44.87  ? 8   PRO A HB2  1 
ATOM   62   H HB3  . PRO A 1 5   ? 27.838 33.968 14.146 0.00 44.87  ? 8   PRO A HB3  1 
ATOM   63   H HG2  . PRO A 1 5   ? 25.629 35.622 14.581 0.00 58.47  ? 8   PRO A HG2  1 
ATOM   64   H HG3  . PRO A 1 5   ? 26.414 35.395 13.218 0.00 58.47  ? 8   PRO A HG3  1 
ATOM   65   H HD2  . PRO A 1 5   ? 24.109 34.302 13.615 0.00 42.47  ? 8   PRO A HD2  1 
ATOM   66   H HD3  . PRO A 1 5   ? 25.190 33.604 12.682 0.00 42.47  ? 8   PRO A HD3  1 
ATOM   67   N N    . GLU A 1 6   ? 25.229 33.534 17.304 1.00 27.63  ? 9   GLU A N    1 
ATOM   68   C CA   . GLU A 1 6   ? 25.072 33.641 18.756 1.00 26.02  ? 9   GLU A CA   1 
ATOM   69   C C    . GLU A 1 6   ? 24.707 32.326 19.425 1.00 23.86  ? 9   GLU A C    1 
ATOM   70   O O    . GLU A 1 6   ? 24.571 32.251 20.653 1.00 24.04  ? 9   GLU A O    1 
ATOM   71   C CB   . GLU A 1 6   ? 23.935 34.663 19.069 1.00 27.29  ? 9   GLU A CB   1 
ATOM   72   C CG   . GLU A 1 6   ? 22.529 34.257 18.671 1.00 26.61  ? 9   GLU A CG   1 
ATOM   73   C CD   . GLU A 1 6   ? 22.100 34.629 17.264 1.00 26.25  ? 9   GLU A CD   1 
ATOM   74   O OE1  . GLU A 1 6   ? 23.037 34.941 16.423 1.00 28.10  ? 9   GLU A OE1  1 
ATOM   75   O OE2  . GLU A 1 6   ? 20.941 34.593 16.945 1.00 29.77  ? 9   GLU A OE2  1 
ATOM   76   H H    . GLU A 1 6   ? 24.566 33.840 16.851 0.00 33.16  ? 9   GLU A H    1 
ATOM   77   H HA   . GLU A 1 6   ? 25.912 33.949 19.129 0.00 31.23  ? 9   GLU A HA   1 
ATOM   78   H HB2  . GLU A 1 6   ? 23.925 34.819 20.027 0.00 32.75  ? 9   GLU A HB2  1 
ATOM   79   H HB3  . GLU A 1 6   ? 24.135 35.489 18.601 0.00 32.75  ? 9   GLU A HB3  1 
ATOM   80   H HG2  . GLU A 1 6   ? 22.459 33.292 18.745 0.00 31.93  ? 9   GLU A HG2  1 
ATOM   81   H HG3  . GLU A 1 6   ? 21.906 34.682 19.282 0.00 31.93  ? 9   GLU A HG3  1 
ATOM   82   N N    . TRP A 1 7   ? 24.615 31.204 18.663 1.00 24.90  ? 10  TRP A N    1 
ATOM   83   C CA   . TRP A 1 7   ? 24.183 29.944 19.234 1.00 25.27  ? 10  TRP A CA   1 
ATOM   84   C C    . TRP A 1 7   ? 25.085 29.510 20.369 1.00 24.28  ? 10  TRP A C    1 
ATOM   85   O O    . TRP A 1 7   ? 24.645 28.911 21.318 1.00 24.62  ? 10  TRP A O    1 
ATOM   86   C CB   . TRP A 1 7   ? 24.086 28.868 18.105 1.00 31.46  ? 10  TRP A CB   1 
ATOM   87   C CG   . TRP A 1 7   ? 25.406 28.191 17.764 1.00 34.08  ? 10  TRP A CG   1 
ATOM   88   C CD1  . TRP A 1 7   ? 26.251 28.578 16.799 1.00 39.65  ? 10  TRP A CD1  1 
ATOM   89   C CD2  . TRP A 1 7   ? 26.000 27.064 18.418 1.00 34.23  ? 10  TRP A CD2  1 
ATOM   90   N NE1  . TRP A 1 7   ? 27.352 27.721 16.742 1.00 43.29  ? 10  TRP A NE1  1 
ATOM   91   C CE2  . TRP A 1 7   ? 27.235 26.819 17.754 1.00 37.72  ? 10  TRP A CE2  1 
ATOM   92   C CE3  . TRP A 1 7   ? 25.625 26.250 19.483 1.00 39.45  ? 10  TRP A CE3  1 
ATOM   93   C CZ2  . TRP A 1 7   ? 28.069 25.760 18.116 1.00 49.31  ? 10  TRP A CZ2  1 
ATOM   94   C CZ3  . TRP A 1 7   ? 26.457 25.214 19.849 1.00 48.30  ? 10  TRP A CZ3  1 
ATOM   95   C CH2  . TRP A 1 7   ? 27.667 24.996 19.186 1.00 45.60  ? 10  TRP A CH2  1 
ATOM   96   H H    . TRP A 1 7   ? 24.799 31.166 17.823 0.00 29.88  ? 10  TRP A H    1 
ATOM   97   H HA   . TRP A 1 7   ? 23.297 30.044 19.614 0.00 30.32  ? 10  TRP A HA   1 
ATOM   98   H HB2  . TRP A 1 7   ? 23.467 28.177 18.389 0.00 37.75  ? 10  TRP A HB2  1 
ATOM   99   H HB3  . TRP A 1 7   ? 23.759 29.295 17.298 0.00 37.75  ? 10  TRP A HB3  1 
ATOM   100  H HD1  . TRP A 1 7   ? 26.122 29.313 16.244 0.00 47.58  ? 10  TRP A HD1  1 
ATOM   101  H HE1  . TRP A 1 7   ? 27.991 27.757 16.168 0.00 51.94  ? 10  TRP A HE1  1 
ATOM   102  H HE3  . TRP A 1 7   ? 24.829 26.403 19.939 0.00 47.34  ? 10  TRP A HE3  1 
ATOM   103  H HZ2  . TRP A 1 7   ? 28.858 25.580 17.657 0.00 59.17  ? 10  TRP A HZ2  1 
ATOM   104  H HZ3  . TRP A 1 7   ? 26.209 24.652 20.547 0.00 57.96  ? 10  TRP A HZ3  1 
ATOM   105  H HH2  . TRP A 1 7   ? 28.220 24.309 19.479 0.00 54.72  ? 10  TRP A HH2  1 
ATOM   106  N N    . ILE A 1 8   ? 26.426 29.765 20.232 1.00 25.96  ? 11  ILE A N    1 
ATOM   107  C CA   . ILE A 1 8   ? 27.314 29.220 21.249 1.00 26.27  ? 11  ILE A CA   1 
ATOM   108  C C    . ILE A 1 8   ? 26.998 29.846 22.607 1.00 23.80  ? 11  ILE A C    1 
ATOM   109  O O    . ILE A 1 8   ? 27.114 29.182 23.653 1.00 24.44  ? 11  ILE A O    1 
ATOM   110  C CB   . ILE A 1 8   ? 28.790 29.468 20.814 1.00 31.05  ? 11  ILE A CB   1 
ATOM   111  C CG1  . ILE A 1 8   ? 29.721 28.883 21.889 1.00 36.09  ? 11  ILE A CG1  1 
ATOM   112  C CG2  . ILE A 1 8   ? 28.989 30.939 20.555 1.00 32.94  ? 11  ILE A CG2  1 
ATOM   113  C CD1  . ILE A 1 8   ? 29.564 27.387 22.066 1.00 47.21  ? 11  ILE A CD1  1 
ATOM   114  H H    . ILE A 1 8   ? 26.795 30.217 19.601 0.00 31.15  ? 11  ILE A H    1 
ATOM   115  H HA   . ILE A 1 8   ? 27.178 28.263 21.334 0.00 31.53  ? 11  ILE A HA   1 
ATOM   116  H HB   . ILE A 1 8   ? 29.004 29.017 19.983 0.00 37.25  ? 11  ILE A HB   1 
ATOM   117  H HG12 . ILE A 1 8   ? 30.641 29.058 21.636 0.00 43.31  ? 11  ILE A HG12 1 
ATOM   118  H HG13 . ILE A 1 8   ? 29.524 29.306 22.739 0.00 43.31  ? 11  ILE A HG13 1 
ATOM   119  H HG21 . ILE A 1 8   ? 29.903 31.088 20.266 0.00 39.53  ? 11  ILE A HG21 1 
ATOM   120  H HG22 . ILE A 1 8   ? 28.372 31.223 19.862 0.00 39.53  ? 11  ILE A HG22 1 
ATOM   121  H HG23 . ILE A 1 8   ? 28.817 31.430 21.373 0.00 39.53  ? 11  ILE A HG23 1 
ATOM   122  H HD11 . ILE A 1 8   ? 30.241 27.069 22.682 0.00 56.65  ? 11  ILE A HD11 1 
ATOM   123  H HD12 . ILE A 1 8   ? 28.680 27.202 22.421 0.00 56.65  ? 11  ILE A HD12 1 
ATOM   124  H HD13 . ILE A 1 8   ? 29.671 26.954 21.204 0.00 56.65  ? 11  ILE A HD13 1 
ATOM   125  N N    . TRP A 1 9   ? 26.616 31.109 22.653 1.00 22.33  ? 12  TRP A N    1 
ATOM   126  C CA   . TRP A 1 9   ? 26.339 31.730 23.942 1.00 22.76  ? 12  TRP A CA   1 
ATOM   127  C C    . TRP A 1 9   ? 25.010 31.288 24.491 1.00 23.23  ? 12  TRP A C    1 
ATOM   128  O O    . TRP A 1 9   ? 24.870 31.184 25.701 1.00 23.00  ? 12  TRP A O    1 
ATOM   129  C CB   . TRP A 1 9   ? 26.386 33.276 23.822 1.00 22.64  ? 12  TRP A CB   1 
ATOM   130  C CG   . TRP A 1 9   ? 27.635 33.761 23.087 1.00 24.28  ? 12  TRP A CG   1 
ATOM   131  C CD1  . TRP A 1 9   ? 27.634 34.532 21.922 1.00 28.17  ? 12  TRP A CD1  1 
ATOM   132  C CD2  . TRP A 1 9   ? 28.974 33.493 23.402 1.00 27.20  ? 12  TRP A CD2  1 
ATOM   133  N NE1  . TRP A 1 9   ? 28.944 34.741 21.554 1.00 30.41  ? 12  TRP A NE1  1 
ATOM   134  C CE2  . TRP A 1 9   ? 29.772 34.126 22.445 1.00 28.99  ? 12  TRP A CE2  1 
ATOM   135  C CE3  . TRP A 1 9   ? 29.579 32.781 24.441 1.00 27.91  ? 12  TRP A CE3  1 
ATOM   136  C CZ2  . TRP A 1 9   ? 31.201 34.028 22.472 1.00 32.15  ? 12  TRP A CZ2  1 
ATOM   137  C CZ3  . TRP A 1 9   ? 30.952 32.697 24.468 1.00 33.08  ? 12  TRP A CZ3  1 
ATOM   138  C CH2  . TRP A 1 9   ? 31.736 33.319 23.488 1.00 31.53  ? 12  TRP A CH2  1 
ATOM   139  H H    . TRP A 1 9   ? 26.510 31.621 21.970 0.00 26.80  ? 12  TRP A H    1 
ATOM   140  H HA   . TRP A 1 9   ? 27.030 31.471 24.572 0.00 27.31  ? 12  TRP A HA   1 
ATOM   141  H HB2  . TRP A 1 9   ? 25.608 33.580 23.330 0.00 27.16  ? 12  TRP A HB2  1 
ATOM   142  H HB3  . TRP A 1 9   ? 26.388 33.664 24.711 0.00 27.16  ? 12  TRP A HB3  1 
ATOM   143  H HD1  . TRP A 1 9   ? 26.882 34.847 21.474 0.00 33.80  ? 12  TRP A HD1  1 
ATOM   144  H HE1  . TRP A 1 9   ? 29.200 35.191 20.868 0.00 36.49  ? 12  TRP A HE1  1 
ATOM   145  H HE3  . TRP A 1 9   ? 29.065 32.373 25.100 0.00 33.49  ? 12  TRP A HE3  1 
ATOM   146  H HZ2  . TRP A 1 9   ? 31.732 34.432 21.824 0.00 38.58  ? 12  TRP A HZ2  1 
ATOM   147  H HZ3  . TRP A 1 9   ? 31.367 32.218 25.149 0.00 39.69  ? 12  TRP A HZ3  1 
ATOM   148  H HH2  . TRP A 1 9   ? 32.661 33.241 23.540 0.00 37.83  ? 12  TRP A HH2  1 
ATOM   149  N N    . LEU A 1 10  ? 24.040 31.007 23.620 1.00 20.38  ? 13  LEU A N    1 
ATOM   150  C CA   . LEU A 1 10  ? 22.784 30.421 24.086 1.00 20.68  ? 13  LEU A CA   1 
ATOM   151  C C    . LEU A 1 10  ? 23.012 29.033 24.630 1.00 22.12  ? 13  LEU A C    1 
ATOM   152  O O    . LEU A 1 10  ? 22.415 28.672 25.666 1.00 21.18  ? 13  LEU A O    1 
ATOM   153  C CB   . LEU A 1 10  ? 21.774 30.411 22.932 1.00 20.47  ? 13  LEU A CB   1 
ATOM   154  C CG   . LEU A 1 10  ? 21.410 31.835 22.370 1.00 20.49  ? 13  LEU A CG   1 
ATOM   155  C CD1  . LEU A 1 10  ? 20.443 31.649 21.223 1.00 23.80  ? 13  LEU A CD1  1 
ATOM   156  C CD2  . LEU A 1 10  ? 20.691 32.635 23.479 1.00 25.40  ? 13  LEU A CD2  1 
ATOM   157  H H    . LEU A 1 10  ? 24.083 31.143 22.772 0.00 24.46  ? 13  LEU A H    1 
ATOM   158  H HA   . LEU A 1 10  ? 22.413 30.958 24.804 0.00 24.81  ? 13  LEU A HA   1 
ATOM   159  H HB2  . LEU A 1 10  ? 22.147 29.894 22.201 0.00 24.56  ? 13  LEU A HB2  1 
ATOM   160  H HB3  . LEU A 1 10  ? 20.953 30.000 23.245 0.00 24.56  ? 13  LEU A HB3  1 
ATOM   161  H HG   . LEU A 1 10  ? 22.204 32.309 22.078 0.00 24.59  ? 13  LEU A HG   1 
ATOM   162  H HD11 . LEU A 1 10  ? 20.197 32.520 20.873 0.00 28.56  ? 13  LEU A HD11 1 
ATOM   163  H HD12 . LEU A 1 10  ? 20.872 31.123 20.531 0.00 28.56  ? 13  LEU A HD12 1 
ATOM   164  H HD13 . LEU A 1 10  ? 19.653 31.188 21.547 0.00 28.56  ? 13  LEU A HD13 1 
ATOM   165  H HD21 . LEU A 1 10  ? 20.324 33.447 23.096 0.00 30.48  ? 13  LEU A HD21 1 
ATOM   166  H HD22 . LEU A 1 10  ? 19.977 32.091 23.849 0.00 30.48  ? 13  LEU A HD22 1 
ATOM   167  H HD23 . LEU A 1 10  ? 21.331 32.857 24.174 0.00 30.48  ? 13  LEU A HD23 1 
ATOM   168  N N    . ALA A 1 11  ? 23.895 28.242 24.018 1.00 21.71  ? 14  ALA A N    1 
ATOM   169  C CA   . ALA A 1 11  ? 24.134 26.903 24.514 1.00 20.87  ? 14  ALA A CA   1 
ATOM   170  C C    . ALA A 1 11  ? 24.844 27.002 25.879 1.00 23.44  ? 14  ALA A C    1 
ATOM   171  O O    . ALA A 1 11  ? 24.553 26.249 26.797 1.00 22.46  ? 14  ALA A O    1 
ATOM   172  C CB   . ALA A 1 11  ? 25.024 26.192 23.484 1.00 26.00  ? 14  ALA A CB   1 
ATOM   173  H H    . ALA A 1 11  ? 24.357 28.459 23.327 0.00 26.05  ? 14  ALA A H    1 
ATOM   174  H HA   . ALA A 1 11  ? 23.315 26.397 24.627 0.00 25.04  ? 14  ALA A HA   1 
ATOM   175  H HB1  . ALA A 1 11  ? 25.202 25.289 23.791 0.00 31.20  ? 14  ALA A HB1  1 
ATOM   176  H HB2  . ALA A 1 11  ? 24.562 26.166 22.632 0.00 31.20  ? 14  ALA A HB2  1 
ATOM   177  H HB3  . ALA A 1 11  ? 25.857 26.681 23.395 0.00 31.20  ? 14  ALA A HB3  1 
ATOM   178  N N    A LEU A 1 12  ? 25.866 27.875 25.983 0.59 23.78  ? 15  LEU A N    1 
ATOM   179  N N    B LEU A 1 12  ? 25.864 27.876 25.998 0.41 23.77  ? 15  LEU A N    1 
ATOM   180  C CA   A LEU A 1 12  ? 26.569 27.980 27.250 0.59 25.28  ? 15  LEU A CA   1 
ATOM   181  C CA   B LEU A 1 12  ? 26.548 27.984 27.282 0.41 25.14  ? 15  LEU A CA   1 
ATOM   182  C C    A LEU A 1 12  ? 25.652 28.494 28.338 0.59 23.70  ? 15  LEU A C    1 
ATOM   183  C C    B LEU A 1 12  ? 25.611 28.479 28.351 0.41 23.70  ? 15  LEU A C    1 
ATOM   184  O O    A LEU A 1 12  ? 25.695 27.981 29.467 0.59 23.12  ? 15  LEU A O    1 
ATOM   185  O O    B LEU A 1 12  ? 25.627 27.976 29.482 0.41 23.12  ? 15  LEU A O    1 
ATOM   186  C CB   A LEU A 1 12  ? 27.804 28.885 27.051 0.59 26.48  ? 15  LEU A CB   1 
ATOM   187  C CB   B LEU A 1 12  ? 27.745 28.937 27.164 0.41 26.47  ? 15  LEU A CB   1 
ATOM   188  C CG   A LEU A 1 12  ? 28.760 29.024 28.202 0.59 27.81  ? 15  LEU A CG   1 
ATOM   189  C CG   B LEU A 1 12  ? 28.863 28.272 26.401 0.41 24.55  ? 15  LEU A CG   1 
ATOM   190  C CD1  A LEU A 1 12  ? 29.302 27.709 28.699 0.59 32.54  ? 15  LEU A CD1  1 
ATOM   191  C CD1  B LEU A 1 12  ? 29.848 29.373 25.993 0.41 33.25  ? 15  LEU A CD1  1 
ATOM   192  C CD2  A LEU A 1 12  ? 29.895 29.958 27.764 0.59 29.86  ? 15  LEU A CD2  1 
ATOM   193  C CD2  B LEU A 1 12  ? 29.601 27.200 27.194 0.41 32.76  ? 15  LEU A CD2  1 
ATOM   194  H H    A LEU A 1 12  ? 26.150 28.389 25.356 0.59 28.54  ? 15  LEU A H    1 
ATOM   195  H H    B LEU A 1 12  ? 26.159 28.390 25.374 0.41 28.52  ? 15  LEU A H    1 
ATOM   196  H HA   A LEU A 1 12  ? 26.880 27.109 27.542 0.59 30.33  ? 15  LEU A HA   1 
ATOM   197  H HA   B LEU A 1 12  ? 26.875 27.106 27.534 0.41 30.17  ? 15  LEU A HA   1 
ATOM   198  H HB2  A LEU A 1 12  ? 28.313 28.530 26.305 0.59 31.77  ? 15  LEU A HB2  1 
ATOM   199  H HB2  B LEU A 1 12  ? 27.477 29.739 26.689 0.41 31.76  ? 15  LEU A HB2  1 
ATOM   200  H HB3  A LEU A 1 12  ? 27.487 29.777 26.841 0.59 31.77  ? 15  LEU A HB3  1 
ATOM   201  H HB3  B LEU A 1 12  ? 28.066 29.167 28.050 0.41 31.76  ? 15  LEU A HB3  1 
ATOM   202  H HG   A LEU A 1 12  ? 28.283 29.395 28.961 0.59 33.38  ? 15  LEU A HG   1 
ATOM   203  H HG   B LEU A 1 12  ? 28.484 27.811 25.636 0.41 29.46  ? 15  LEU A HG   1 
ATOM   204  H HD11 A LEU A 1 12  ? 30.051 27.880 29.292 0.59 39.05  ? 15  LEU A HD11 1 
ATOM   205  H HD11 B LEU A 1 12  ? 30.584 28.972 25.505 0.41 39.90  ? 15  LEU A HD11 1 
ATOM   206  H HD12 A LEU A 1 12  ? 28.602 27.239 29.179 0.59 39.05  ? 15  LEU A HD12 1 
ATOM   207  H HD12 B LEU A 1 12  ? 29.388 30.015 25.430 0.41 39.90  ? 15  LEU A HD12 1 
ATOM   208  H HD13 A LEU A 1 12  ? 29.595 27.181 27.940 0.59 39.05  ? 15  LEU A HD13 1 
ATOM   209  H HD13 B LEU A 1 12  ? 30.180 29.811 26.792 0.41 39.90  ? 15  LEU A HD13 1 
ATOM   210  H HD21 A LEU A 1 12  ? 30.313 30.338 28.553 0.59 35.83  ? 15  LEU A HD21 1 
ATOM   211  H HD21 B LEU A 1 12  ? 30.352 26.881 26.669 0.41 39.31  ? 15  LEU A HD21 1 
ATOM   212  H HD22 A LEU A 1 12  ? 30.547 29.448 27.258 0.59 35.83  ? 15  LEU A HD22 1 
ATOM   213  H HD22 B LEU A 1 12  ? 29.919 27.585 28.025 0.41 39.31  ? 15  LEU A HD22 1 
ATOM   214  H HD23 A LEU A 1 12  ? 29.527 30.665 27.212 0.59 35.83  ? 15  LEU A HD23 1 
ATOM   215  H HD23 B LEU A 1 12  ? 28.992 26.468 27.379 0.41 39.31  ? 15  LEU A HD23 1 
ATOM   216  N N    . GLY A 1 13  ? 24.760 29.443 28.016 1.00 21.07  ? 16  GLY A N    1 
ATOM   217  C CA   . GLY A 1 13  ? 23.774 29.901 28.974 1.00 21.03  ? 16  GLY A CA   1 
ATOM   218  C C    . GLY A 1 13  ? 22.864 28.791 29.453 1.00 21.96  ? 16  GLY A C    1 
ATOM   219  O O    . GLY A 1 13  ? 22.568 28.683 30.640 1.00 20.45  ? 16  GLY A O    1 
ATOM   220  H H    . GLY A 1 13  ? 24.715 29.828 27.248 0.00 25.28  ? 16  GLY A H    1 
ATOM   221  H HA2  . GLY A 1 13  ? 24.228 30.276 29.745 0.00 25.24  ? 16  GLY A HA2  1 
ATOM   222  H HA3  . GLY A 1 13  ? 23.226 30.589 28.566 0.00 25.24  ? 16  GLY A HA3  1 
ATOM   223  N N    . THR A 1 14  ? 22.374 27.992 28.534 1.00 19.59  ? 17  THR A N    1 
ATOM   224  C CA   . THR A 1 14  ? 21.514 26.861 28.869 1.00 20.77  ? 17  THR A CA   1 
ATOM   225  C C    . THR A 1 14  ? 22.212 25.958 29.827 1.00 23.85  ? 17  THR A C    1 
ATOM   226  O O    . THR A 1 14  ? 21.614 25.571 30.859 1.00 22.11  ? 17  THR A O    1 
ATOM   227  C CB   . THR A 1 14  ? 21.128 26.131 27.582 1.00 20.06  ? 17  THR A CB   1 
ATOM   228  O OG1  . THR A 1 14  ? 20.339 27.031 26.694 1.00 20.60  ? 17  THR A OG1  1 
ATOM   229  C CG2  . THR A 1 14  ? 20.130 24.976 27.970 1.00 22.56  ? 17  THR A CG2  1 
ATOM   230  H H    . THR A 1 14  ? 22.521 28.077 27.691 0.00 23.51  ? 17  THR A H    1 
ATOM   231  H HA   . THR A 1 14  ? 20.696 27.166 29.292 0.00 24.92  ? 17  THR A HA   1 
ATOM   232  H HB   . THR A 1 14  ? 21.929 25.815 27.136 0.00 24.07  ? 17  THR A HB   1 
ATOM   233  H HG1  . THR A 1 14  ? 20.798 27.702 26.484 0.00 24.72  ? 17  THR A HG1  1 
ATOM   234  H HG21 . THR A 1 14  ? 19.745 24.587 27.169 0.00 27.07  ? 17  THR A HG21 1 
ATOM   235  H HG22 . THR A 1 14  ? 20.599 24.283 28.462 0.00 27.07  ? 17  THR A HG22 1 
ATOM   236  H HG23 . THR A 1 14  ? 19.416 25.327 28.524 0.00 27.07  ? 17  THR A HG23 1 
ATOM   237  N N    . ALA A 1 15  ? 23.472 25.575 29.490 1.00 21.52  ? 18  ALA A N    1 
ATOM   238  C CA   . ALA A 1 15  ? 24.212 24.649 30.358 1.00 22.13  ? 18  ALA A CA   1 
ATOM   239  C C    . ALA A 1 15  ? 24.391 25.251 31.738 1.00 24.82  ? 18  ALA A C    1 
ATOM   240  O O    . ALA A 1 15  ? 24.274 24.532 32.741 1.00 25.21  ? 18  ALA A O    1 
ATOM   241  C CB   . ALA A 1 15  ? 25.571 24.394 29.692 1.00 25.15  ? 18  ALA A CB   1 
ATOM   242  H H    . ALA A 1 15  ? 23.897 25.832 28.789 0.00 25.82  ? 18  ALA A H    1 
ATOM   243  H HA   . ALA A 1 15  ? 23.737 23.810 30.464 0.00 26.55  ? 18  ALA A HA   1 
ATOM   244  H HB1  . ALA A 1 15  ? 26.081 23.778 30.242 0.00 30.18  ? 18  ALA A HB1  1 
ATOM   245  H HB2  . ALA A 1 15  ? 25.425 24.011 28.813 0.00 30.18  ? 18  ALA A HB2  1 
ATOM   246  H HB3  . ALA A 1 15  ? 26.046 25.236 29.611 0.00 30.18  ? 18  ALA A HB3  1 
ATOM   247  N N    . LEU A 1 16  ? 24.803 26.512 31.845 1.00 21.44  ? 19  LEU A N    1 
ATOM   248  C CA   . LEU A 1 16  ? 25.121 27.063 33.157 1.00 23.32  ? 19  LEU A CA   1 
ATOM   249  C C    . LEU A 1 16  ? 23.847 27.211 34.002 1.00 21.65  ? 19  LEU A C    1 
ATOM   250  O O    . LEU A 1 16  ? 23.907 26.999 35.236 1.00 23.88  ? 19  LEU A O    1 
ATOM   251  C CB   . LEU A 1 16  ? 25.888 28.386 32.937 1.00 25.11  ? 19  LEU A CB   1 
ATOM   252  C CG   . LEU A 1 16  ? 27.294 28.238 32.281 1.00 24.20  ? 19  LEU A CG   1 
ATOM   253  C CD1  . LEU A 1 16  ? 27.849 29.626 31.899 1.00 34.28  ? 19  LEU A CD1  1 
ATOM   254  C CD2  . LEU A 1 16  ? 28.180 27.532 33.293 1.00 34.41  ? 19  LEU A CD2  1 
ATOM   255  H H    . LEU A 1 16  ? 24.903 27.058 31.188 0.00 25.73  ? 19  LEU A H    1 
ATOM   256  H HA   . LEU A 1 16  ? 25.703 26.478 33.667 0.00 27.99  ? 19  LEU A HA   1 
ATOM   257  H HB2  . LEU A 1 16  ? 25.356 28.955 32.359 0.00 30.13  ? 19  LEU A HB2  1 
ATOM   258  H HB3  . LEU A 1 16  ? 26.013 28.814 33.799 0.00 30.13  ? 19  LEU A HB3  1 
ATOM   259  H HG   . LEU A 1 16  ? 27.264 27.721 31.460 0.00 29.04  ? 19  LEU A HG   1 
ATOM   260  H HD11 . LEU A 1 16  ? 28.727 29.517 31.501 0.00 41.14  ? 19  LEU A HD11 1 
ATOM   261  H HD12 . LEU A 1 16  ? 27.247 30.042 31.262 0.00 41.14  ? 19  LEU A HD12 1 
ATOM   262  H HD13 . LEU A 1 16  ? 27.913 30.171 32.698 0.00 41.14  ? 19  LEU A HD13 1 
ATOM   263  H HD21 . LEU A 1 16  ? 29.100 27.574 32.990 0.00 41.29  ? 19  LEU A HD21 1 
ATOM   264  H HD22 . LEU A 1 16  ? 28.093 27.975 34.151 0.00 41.29  ? 19  LEU A HD22 1 
ATOM   265  H HD23 . LEU A 1 16  ? 27.898 26.607 33.367 0.00 41.29  ? 19  LEU A HD23 1 
ATOM   266  N N    . MET A 1 17  ? 22.745 27.595 33.359 1.00 20.20  ? 20  MET A N    1 
ATOM   267  C CA   . MET A 1 17  ? 21.501 27.662 34.151 1.00 21.30  ? 20  MET A CA   1 
ATOM   268  C C    . MET A 1 17  ? 21.035 26.294 34.595 1.00 23.49  ? 20  MET A C    1 
ATOM   269  O O    . MET A 1 17  ? 20.557 26.156 35.733 1.00 21.98  ? 20  MET A O    1 
ATOM   270  C CB   . MET A 1 17  ? 20.356 28.342 33.329 1.00 19.25  ? 20  MET A CB   1 
ATOM   271  C CG   . MET A 1 17  ? 20.679 29.793 32.984 1.00 19.72  ? 20  MET A CG   1 
ATOM   272  S SD   . MET A 1 17  ? 20.810 30.841 34.525 1.00 21.31  ? 20  MET A SD   1 
ATOM   273  C CE   . MET A 1 17  ? 21.044 32.438 33.569 1.00 23.37  ? 20  MET A CE   1 
ATOM   274  H H    . MET A 1 17  ? 22.687 27.807 32.528 0.00 24.25  ? 20  MET A H    1 
ATOM   275  H HA   . MET A 1 17  ? 21.693 28.208 34.929 0.00 25.56  ? 20  MET A HA   1 
ATOM   276  H HB2  . MET A 1 17  ? 20.228 27.855 32.500 0.00 23.10  ? 20  MET A HB2  1 
ATOM   277  H HB3  . MET A 1 17  ? 19.539 28.329 33.851 0.00 23.10  ? 20  MET A HB3  1 
ATOM   278  H HG2  . MET A 1 17  ? 21.527 29.832 32.515 0.00 23.66  ? 20  MET A HG2  1 
ATOM   279  H HG3  . MET A 1 17  ? 19.974 30.156 32.426 0.00 23.66  ? 20  MET A HG3  1 
ATOM   280  H HE1  . MET A 1 17  ? 21.136 33.171 34.197 0.00 28.05  ? 20  MET A HE1  1 
ATOM   281  H HE2  . MET A 1 17  ? 21.844 32.366 33.025 0.00 28.05  ? 20  MET A HE2  1 
ATOM   282  H HE3  . MET A 1 17  ? 20.270 32.582 33.002 0.00 28.05  ? 20  MET A HE3  1 
ATOM   283  N N    . GLY A 1 18  ? 21.238 25.309 33.756 1.00 22.36  ? 21  GLY A N    1 
ATOM   284  C CA   . GLY A 1 18  ? 20.887 23.902 34.124 1.00 23.49  ? 21  GLY A CA   1 
ATOM   285  C C    . GLY A 1 18  ? 21.720 23.428 35.301 1.00 24.71  ? 21  GLY A C    1 
ATOM   286  O O    . GLY A 1 18  ? 21.179 22.844 36.257 1.00 24.71  ? 21  GLY A O    1 
ATOM   287  H H    . GLY A 1 18  ? 21.572 25.395 32.969 0.00 26.84  ? 21  GLY A H    1 
ATOM   288  H HA2  . GLY A 1 18  ? 19.949 23.851 34.364 0.00 28.19  ? 21  GLY A HA2  1 
ATOM   289  H HA3  . GLY A 1 18  ? 21.052 23.316 33.368 0.00 28.19  ? 21  GLY A HA3  1 
ATOM   290  N N    . LEU A 1 19  ? 23.051 23.584 35.211 1.00 24.77  ? 22  LEU A N    1 
ATOM   291  C CA   . LEU A 1 19  ? 23.957 23.179 36.288 1.00 24.29  ? 22  LEU A CA   1 
ATOM   292  C C    . LEU A 1 19  ? 23.647 23.940 37.565 1.00 27.05  ? 22  LEU A C    1 
ATOM   293  O O    . LEU A 1 19  ? 23.669 23.361 38.673 1.00 28.05  ? 22  LEU A O    1 
ATOM   294  C CB   . LEU A 1 19  ? 25.394 23.411 35.814 1.00 28.75  ? 22  LEU A CB   1 
ATOM   295  C CG   . LEU A 1 19  ? 25.896 22.437 34.797 1.00 31.76  ? 22  LEU A CG   1 
ATOM   296  C CD1  . LEU A 1 19  ? 27.259 22.902 34.338 1.00 40.42  ? 22  LEU A CD1  1 
ATOM   297  C CD2  . LEU A 1 19  ? 26.061 21.005 35.411 1.00 39.67  ? 22  LEU A CD2  1 
ATOM   298  H H    . LEU A 1 19  ? 23.455 23.923 34.531 1.00 29.73  ? 22  LEU A H    1 
ATOM   299  H HA   . LEU A 1 19  ? 23.854 22.236 36.494 1.00 29.15  ? 22  LEU A HA   1 
ATOM   300  H HB2  . LEU A 1 19  ? 25.446 24.296 35.419 1.00 34.50  ? 22  LEU A HB2  1 
ATOM   301  H HB3  . LEU A 1 19  ? 25.982 23.356 36.584 1.00 34.50  ? 22  LEU A HB3  1 
ATOM   302  H HG   . LEU A 1 19  ? 25.263 22.389 34.063 1.00 38.11  ? 22  LEU A HG   1 
ATOM   303  H HD11 . LEU A 1 19  ? 27.601 22.275 33.681 1.00 48.50  ? 22  LEU A HD11 1 
ATOM   304  H HD12 . LEU A 1 19  ? 27.176 23.783 33.942 1.00 48.50  ? 22  LEU A HD12 1 
ATOM   305  H HD13 . LEU A 1 19  ? 27.855 22.937 35.103 1.00 48.50  ? 22  LEU A HD13 1 
ATOM   306  H HD21 . LEU A 1 19  ? 26.455 20.420 34.745 1.00 47.61  ? 22  LEU A HD21 1 
ATOM   307  H HD22 . LEU A 1 19  ? 26.639 21.059 36.187 1.00 47.61  ? 22  LEU A HD22 1 
ATOM   308  H HD23 . LEU A 1 19  ? 25.188 20.670 35.671 1.00 47.61  ? 22  LEU A HD23 1 
ATOM   309  N N    . GLY A 1 20  ? 23.405 25.262 37.478 1.00 25.00  ? 23  GLY A N    1 
ATOM   310  C CA   . GLY A 1 20  ? 23.043 26.032 38.685 1.00 22.75  ? 23  GLY A CA   1 
ATOM   311  C C    . GLY A 1 20  ? 21.773 25.525 39.329 1.00 22.83  ? 23  GLY A C    1 
ATOM   312  O O    . GLY A 1 20  ? 21.713 25.358 40.565 1.00 24.37  ? 23  GLY A O    1 
ATOM   313  H H    . GLY A 1 20  ? 23.442 25.724 36.754 0.00 30.00  ? 23  GLY A H    1 
ATOM   314  H HA2  . GLY A 1 20  ? 23.762 25.968 39.334 0.00 27.31  ? 23  GLY A HA2  1 
ATOM   315  H HA3  . GLY A 1 20  ? 22.915 26.963 38.446 0.00 27.31  ? 23  GLY A HA3  1 
ATOM   316  N N    . THR A 1 21  ? 20.752 25.212 38.508 1.00 23.22  ? 24  THR A N    1 
ATOM   317  C CA   . THR A 1 21  ? 19.503 24.623 39.064 1.00 25.08  ? 24  THR A CA   1 
ATOM   318  C C    . THR A 1 21  ? 19.773 23.328 39.829 1.00 24.64  ? 24  THR A C    1 
ATOM   319  O O    . THR A 1 21  ? 19.317 23.193 40.979 1.00 24.40  ? 24  THR A O    1 
ATOM   320  C CB   . THR A 1 21  ? 18.552 24.338 37.886 1.00 22.46  ? 24  THR A CB   1 
ATOM   321  O OG1  . THR A 1 21  ? 18.219 25.584 37.263 1.00 22.36  ? 24  THR A OG1  1 
ATOM   322  C CG2  . THR A 1 21  ? 17.176 23.787 38.459 1.00 24.80  ? 24  THR A CG2  1 
ATOM   323  H H    . THR A 1 21  ? 20.752 25.323 37.656 0.00 27.86  ? 24  THR A H    1 
ATOM   324  H HA   . THR A 1 21  ? 19.100 25.250 39.684 0.00 30.09  ? 24  THR A HA   1 
ATOM   325  H HB   . THR A 1 21  ? 18.965 23.713 37.270 0.00 26.96  ? 24  THR A HB   1 
ATOM   326  H HG1  . THR A 1 21  ? 18.911 25.944 36.953 0.00 26.84  ? 24  THR A HG1  1 
ATOM   327  H HG21 . THR A 1 21  ? 16.511 23.757 37.754 0.00 29.76  ? 24  THR A HG21 1 
ATOM   328  H HG22 . THR A 1 21  ? 17.299 22.893 38.814 0.00 29.76  ? 24  THR A HG22 1 
ATOM   329  H HG23 . THR A 1 21  ? 16.857 24.366 39.169 0.00 29.76  ? 24  THR A HG23 1 
ATOM   330  N N    . LEU A 1 22  ? 20.535 22.394 39.241 1.00 24.31  ? 25  LEU A N    1 
ATOM   331  C CA   . LEU A 1 22  ? 20.781 21.084 39.876 1.00 22.49  ? 25  LEU A CA   1 
ATOM   332  C C    . LEU A 1 22  ? 21.597 21.294 41.127 1.00 25.06  ? 25  LEU A C    1 
ATOM   333  O O    . LEU A 1 22  ? 21.296 20.636 42.141 1.00 28.05  ? 25  LEU A O    1 
ATOM   334  C CB   . LEU A 1 22  ? 21.532 20.183 38.907 1.00 28.33  ? 25  LEU A CB   1 
ATOM   335  C CG   . LEU A 1 22  ? 20.616 19.788 37.770 1.00 35.94  ? 25  LEU A CG   1 
ATOM   336  C CD1  . LEU A 1 22  ? 21.465 19.069 36.782 1.00 36.15  ? 25  LEU A CD1  1 
ATOM   337  C CD2  . LEU A 1 22  ? 19.421 18.891 38.166 1.00 46.24  ? 25  LEU A CD2  1 
ATOM   338  H H    . LEU A 1 22  ? 20.922 22.490 38.479 1.00 29.18  ? 25  LEU A H    1 
ATOM   339  H HA   . LEU A 1 22  ? 19.943 20.650 40.100 1.00 26.99  ? 25  LEU A HA   1 
ATOM   340  H HB2  . LEU A 1 22  ? 22.296 20.658 38.545 1.00 34.00  ? 25  LEU A HB2  1 
ATOM   341  H HB3  . LEU A 1 22  ? 21.826 19.382 39.367 1.00 34.00  ? 25  LEU A HB3  1 
ATOM   342  H HG   . LEU A 1 22  ? 20.205 20.592 37.416 1.00 43.13  ? 25  LEU A HG   1 
ATOM   343  H HD11 . LEU A 1 22  ? 20.903 18.741 36.063 1.00 43.38  ? 25  LEU A HD11 1 
ATOM   344  H HD12 . LEU A 1 22  ? 22.129 19.682 36.431 1.00 43.38  ? 25  LEU A HD12 1 
ATOM   345  H HD13 . LEU A 1 22  ? 21.903 18.325 37.225 1.00 43.38  ? 25  LEU A HD13 1 
ATOM   346  H HD21 . LEU A 1 22  ? 18.941 18.633 37.364 1.00 55.49  ? 25  LEU A HD21 1 
ATOM   347  H HD22 . LEU A 1 22  ? 19.756 18.102 38.620 1.00 55.49  ? 25  LEU A HD22 1 
ATOM   348  H HD23 . LEU A 1 22  ? 18.835 19.389 38.757 1.00 55.49  ? 25  LEU A HD23 1 
ATOM   349  N N    . TYR A 1 23  ? 22.567 22.202 41.125 1.00 23.71  ? 26  TYR A N    1 
ATOM   350  C CA   . TYR A 1 23  ? 23.338 22.405 42.352 1.00 27.36  ? 26  TYR A CA   1 
ATOM   351  C C    . TYR A 1 23  ? 22.437 22.880 43.485 1.00 25.06  ? 26  TYR A C    1 
ATOM   352  O O    . TYR A 1 23  ? 22.516 22.384 44.582 1.00 26.74  ? 26  TYR A O    1 
ATOM   353  C CB   . TYR A 1 23  ? 24.515 23.357 42.095 1.00 27.89  ? 26  TYR A CB   1 
ATOM   354  C CG   . TYR A 1 23  ? 25.292 23.672 43.306 1.00 28.92  ? 26  TYR A CG   1 
ATOM   355  C CD1  . TYR A 1 23  ? 26.150 22.716 43.872 1.00 35.54  ? 26  TYR A CD1  1 
ATOM   356  C CD2  . TYR A 1 23  ? 25.259 24.902 43.883 1.00 33.26  ? 26  TYR A CD2  1 
ATOM   357  C CE1  . TYR A 1 23  ? 26.861 23.003 45.016 1.00 40.93  ? 26  TYR A CE1  1 
ATOM   358  C CE2  . TYR A 1 23  ? 25.980 25.208 45.004 1.00 38.91  ? 26  TYR A CE2  1 
ATOM   359  C CZ   . TYR A 1 23  ? 26.815 24.262 45.554 1.00 39.34  ? 26  TYR A CZ   1 
ATOM   360  O OH   . TYR A 1 23  ? 27.556 24.505 46.702 1.00 50.44  ? 26  TYR A OH   1 
ATOM   361  H H    . TYR A 1 23  ? 22.791 22.695 40.456 0.00 28.45  ? 26  TYR A H    1 
ATOM   362  H HA   . TYR A 1 23  ? 23.728 21.561 42.632 0.00 32.84  ? 26  TYR A HA   1 
ATOM   363  H HB2  . TYR A 1 23  ? 25.116 22.946 41.454 0.00 33.47  ? 26  TYR A HB2  1 
ATOM   364  H HB3  . TYR A 1 23  ? 24.170 24.191 41.738 0.00 33.47  ? 26  TYR A HB3  1 
ATOM   365  H HD1  . TYR A 1 23  ? 26.238 21.882 43.471 0.00 42.65  ? 26  TYR A HD1  1 
ATOM   366  H HD2  . TYR A 1 23  ? 24.725 25.560 43.501 0.00 39.91  ? 26  TYR A HD2  1 
ATOM   367  H HE1  . TYR A 1 23  ? 27.373 22.342 45.424 0.00 49.12  ? 26  TYR A HE1  1 
ATOM   368  H HE2  . TYR A 1 23  ? 25.907 26.050 45.392 0.00 46.69  ? 26  TYR A HE2  1 
ATOM   369  H HH   . TYR A 1 23  ? 27.410 25.284 46.979 0.00 60.53  ? 26  TYR A HH   1 
ATOM   370  N N    . PHE A 1 24  ? 21.583 23.906 43.211 1.00 25.54  ? 27  PHE A N    1 
ATOM   371  C CA   . PHE A 1 24  ? 20.777 24.462 44.310 1.00 25.81  ? 27  PHE A CA   1 
ATOM   372  C C    . PHE A 1 24  ? 19.729 23.457 44.750 1.00 26.29  ? 27  PHE A C    1 
ATOM   373  O O    . PHE A 1 24  ? 19.382 23.397 45.931 1.00 28.08  ? 27  PHE A O    1 
ATOM   374  C CB   . PHE A 1 24  ? 20.042 25.734 43.780 1.00 23.62  ? 27  PHE A CB   1 
ATOM   375  C CG   . PHE A 1 24  ? 20.950 26.898 43.510 1.00 24.60  ? 27  PHE A CG   1 
ATOM   376  C CD1  . PHE A 1 24  ? 22.195 27.053 44.110 1.00 30.06  ? 27  PHE A CD1  1 
ATOM   377  C CD2  . PHE A 1 24  ? 20.513 27.918 42.699 1.00 25.18  ? 27  PHE A CD2  1 
ATOM   378  C CE1  . PHE A 1 24  ? 22.983 28.167 43.776 1.00 34.53  ? 27  PHE A CE1  1 
ATOM   379  C CE2  . PHE A 1 24  ? 21.311 29.032 42.364 1.00 26.78  ? 27  PHE A CE2  1 
ATOM   380  C CZ   . PHE A 1 24  ? 22.522 29.184 42.948 1.00 30.15  ? 27  PHE A CZ   1 
ATOM   381  H H    . PHE A 1 24  ? 21.466 24.269 42.440 0.00 30.65  ? 27  PHE A H    1 
ATOM   382  H HA   . PHE A 1 24  ? 21.346 24.692 45.061 0.00 30.97  ? 27  PHE A HA   1 
ATOM   383  H HB2  . PHE A 1 24  ? 19.594 25.510 42.950 0.00 28.33  ? 27  PHE A HB2  1 
ATOM   384  H HB3  . PHE A 1 24  ? 19.392 26.015 44.443 0.00 28.33  ? 27  PHE A HB3  1 
ATOM   385  H HD1  . PHE A 1 24  ? 22.502 26.427 44.725 0.00 36.07  ? 27  PHE A HD1  1 
ATOM   386  H HD2  . PHE A 1 24  ? 19.651 27.872 42.355 0.00 30.22  ? 27  PHE A HD2  1 
ATOM   387  H HE1  . PHE A 1 24  ? 23.844 28.227 44.121 0.00 41.44  ? 27  PHE A HE1  1 
ATOM   388  H HE2  . PHE A 1 24  ? 21.007 29.657 41.746 0.00 32.13  ? 27  PHE A HE2  1 
ATOM   389  H HZ   . PHE A 1 24  ? 23.031 29.947 42.800 0.00 36.18  ? 27  PHE A HZ   1 
ATOM   390  N N    . LEU A 1 25  ? 19.232 22.659 43.806 1.00 25.14  ? 28  LEU A N    1 
ATOM   391  C CA   . LEU A 1 25  ? 18.286 21.599 44.201 1.00 29.62  ? 28  LEU A CA   1 
ATOM   392  C C    . LEU A 1 25  ? 18.926 20.561 45.134 1.00 32.24  ? 28  LEU A C    1 
ATOM   393  O O    . LEU A 1 25  ? 18.350 20.202 46.185 1.00 34.63  ? 28  LEU A O    1 
ATOM   394  C CB   . LEU A 1 25  ? 17.826 20.889 42.930 1.00 37.05  ? 28  LEU A CB   1 
ATOM   395  C CG   . LEU A 1 25  ? 16.557 20.037 43.139 1.00 47.82  ? 28  LEU A CG   1 
ATOM   396  C CD1  . LEU A 1 25  ? 15.372 20.983 43.273 1.00 43.42  ? 28  LEU A CD1  1 
ATOM   397  C CD2  . LEU A 1 25  ? 16.366 19.117 41.965 1.00 58.82  ? 28  LEU A CD2  1 
ATOM   398  H H    . LEU A 1 25  ? 19.415 22.702 42.967 0.00 30.16  ? 28  LEU A H    1 
ATOM   399  H HA   . LEU A 1 25  ? 17.542 22.005 44.673 0.00 35.55  ? 28  LEU A HA   1 
ATOM   400  H HB2  . LEU A 1 25  ? 17.632 21.555 42.251 0.00 44.46  ? 28  LEU A HB2  1 
ATOM   401  H HB3  . LEU A 1 25  ? 18.535 20.301 42.625 0.00 44.46  ? 28  LEU A HB3  1 
ATOM   402  H HG   . LEU A 1 25  ? 16.629 19.492 43.938 0.00 57.38  ? 28  LEU A HG   1 
ATOM   403  H HD11 . LEU A 1 25  ? 14.557 20.460 43.335 0.00 52.10  ? 28  LEU A HD11 1 
ATOM   404  H HD12 . LEU A 1 25  ? 15.484 21.518 44.074 0.00 52.10  ? 28  LEU A HD12 1 
ATOM   405  H HD13 . LEU A 1 25  ? 15.338 21.558 42.493 0.00 52.10  ? 28  LEU A HD13 1 
ATOM   406  H HD21 . LEU A 1 25  ? 15.567 18.587 42.107 0.00 70.58  ? 28  LEU A HD21 1 
ATOM   407  H HD22 . LEU A 1 25  ? 16.272 19.649 41.159 0.00 70.58  ? 28  LEU A HD22 1 
ATOM   408  H HD23 . LEU A 1 25  ? 17.140 18.537 41.890 0.00 70.58  ? 28  LEU A HD23 1 
ATOM   409  N N    . VAL A 1 26  ? 20.134 20.098 44.834 1.00 29.59  ? 29  VAL A N    1 
ATOM   410  C CA   . VAL A 1 26  ? 20.782 19.123 45.711 1.00 30.73  ? 29  VAL A CA   1 
ATOM   411  C C    . VAL A 1 26  ? 21.086 19.751 47.062 1.00 30.94  ? 29  VAL A C    1 
ATOM   412  O O    . VAL A 1 26  ? 20.857 19.115 48.126 1.00 36.70  ? 29  VAL A O    1 
ATOM   413  C CB   . VAL A 1 26  ? 22.053 18.565 45.044 1.00 33.10  ? 29  VAL A CB   1 
ATOM   414  C CG1  . VAL A 1 26  ? 22.810 17.724 46.027 1.00 39.39  ? 29  VAL A CG1  1 
ATOM   415  C CG2  . VAL A 1 26  ? 21.623 17.754 43.837 1.00 42.69  ? 29  VAL A CG2  1 
ATOM   416  H H    . VAL A 1 26  ? 20.593 20.325 44.143 0.00 35.50  ? 29  VAL A H    1 
ATOM   417  H HA   . VAL A 1 26  ? 20.172 18.383 45.856 0.00 36.88  ? 29  VAL A HA   1 
ATOM   418  H HB   . VAL A 1 26  ? 22.646 19.276 44.755 0.00 39.72  ? 29  VAL A HB   1 
ATOM   419  H HG11 . VAL A 1 26  ? 23.523 17.259 45.562 0.00 47.26  ? 29  VAL A HG11 1 
ATOM   420  H HG12 . VAL A 1 26  ? 23.181 18.298 46.714 0.00 47.26  ? 29  VAL A HG12 1 
ATOM   421  H HG13 . VAL A 1 26  ? 22.202 17.081 46.426 0.00 47.26  ? 29  VAL A HG13 1 
ATOM   422  H HG21 . VAL A 1 26  ? 22.409 17.376 43.414 0.00 51.23  ? 29  VAL A HG21 1 
ATOM   423  H HG22 . VAL A 1 26  ? 21.030 17.044 44.130 0.00 51.23  ? 29  VAL A HG22 1 
ATOM   424  H HG23 . VAL A 1 26  ? 21.159 18.336 43.215 0.00 51.23  ? 29  VAL A HG23 1 
ATOM   425  N N    . LYS A 1 27  ? 21.620 21.007 47.053 1.00 29.75  ? 30  LYS A N    1 
ATOM   426  C CA   . LYS A 1 27  ? 21.985 21.696 48.283 1.00 32.65  ? 30  LYS A CA   1 
ATOM   427  C C    . LYS A 1 27  ? 20.792 21.865 49.213 1.00 32.52  ? 30  LYS A C    1 
ATOM   428  O O    . LYS A 1 27  ? 20.953 21.790 50.468 1.00 38.75  ? 30  LYS A O    1 
ATOM   429  C CB   . LYS A 1 27  ? 22.621 23.040 47.942 1.00 34.43  ? 30  LYS A CB   1 
ATOM   430  C CG   . LYS A 1 27  ? 23.436 23.753 49.051 1.00 43.51  ? 30  LYS A CG   1 
ATOM   431  C CD   . LYS A 1 27  ? 24.298 24.964 48.474 1.00 47.06  ? 30  LYS A CD   1 
ATOM   432  C CE   . LYS A 1 27  ? 25.159 25.655 49.585 1.00 59.31  ? 30  LYS A CE   1 
ATOM   433  N NZ   . LYS A 1 27  ? 24.385 26.173 50.759 1.00 63.94  ? 30  LYS A NZ   1 
ATOM   434  H H    . LYS A 1 27  ? 21.773 21.465 46.341 0.00 35.70  ? 30  LYS A H    1 
ATOM   435  H HA   . LYS A 1 27  ? 22.640 21.165 48.763 0.00 39.19  ? 30  LYS A HA   1 
ATOM   436  H HB2  . LYS A 1 27  ? 23.226 22.901 47.196 0.00 41.31  ? 30  LYS A HB2  1 
ATOM   437  H HB3  . LYS A 1 27  ? 21.910 23.647 47.683 0.00 41.31  ? 30  LYS A HB3  1 
ATOM   438  H HG2  . LYS A 1 27  ? 22.827 24.105 49.718 0.00 52.21  ? 30  LYS A HG2  1 
ATOM   439  H HG3  . LYS A 1 27  ? 24.043 23.117 49.459 0.00 52.21  ? 30  LYS A HG3  1 
ATOM   440  H HD2  . LYS A 1 27  ? 24.899 24.631 47.789 0.00 56.47  ? 30  LYS A HD2  1 
ATOM   441  H HD3  . LYS A 1 27  ? 23.701 25.629 48.096 0.00 56.47  ? 30  LYS A HD3  1 
ATOM   442  H HE2  . LYS A 1 27  ? 25.800 25.010 49.922 0.00 71.18  ? 30  LYS A HE2  1 
ATOM   443  H HE3  . LYS A 1 27  ? 25.623 26.409 49.189 0.00 71.18  ? 30  LYS A HE3  1 
ATOM   444  H HZ1  . LYS A 1 27  ? 24.939 26.543 51.349 0.00 76.73  ? 30  LYS A HZ1  1 
ATOM   445  H HZ2  . LYS A 1 27  ? 23.798 26.785 50.491 0.00 76.73  ? 30  LYS A HZ2  1 
ATOM   446  H HZ3  . LYS A 1 27  ? 23.947 25.506 51.153 0.00 76.73  ? 30  LYS A HZ3  1 
ATOM   447  N N    . GLY A 1 28  ? 19.597 22.118 48.641 1.00 35.27  ? 31  GLY A N    1 
ATOM   448  C CA   . GLY A 1 28  ? 18.447 22.364 49.488 1.00 37.35  ? 31  GLY A CA   1 
ATOM   449  C C    . GLY A 1 28  ? 17.780 21.105 49.982 1.00 47.30  ? 31  GLY A C    1 
ATOM   450  O O    . GLY A 1 28  ? 16.838 21.207 50.774 1.00 40.45  ? 31  GLY A O    1 
ATOM   451  H H    . GLY A 1 28  ? 19.448 22.147 47.794 0.00 42.33  ? 31  GLY A H    1 
ATOM   452  H HA2  . GLY A 1 28  ? 18.729 22.878 50.261 0.00 44.83  ? 31  GLY A HA2  1 
ATOM   453  H HA3  . GLY A 1 28  ? 17.792 22.876 48.990 0.00 44.83  ? 31  GLY A HA3  1 
ATOM   454  N N    . MET A 1 29  ? 18.264 19.927 49.540 1.00 44.73  ? 32  MET A N    1 
ATOM   455  C CA   . MET A 1 29  ? 17.818 18.656 50.106 1.00 45.30  ? 32  MET A CA   1 
ATOM   456  C C    . MET A 1 29  ? 18.063 18.598 51.594 1.00 48.06  ? 32  MET A C    1 
ATOM   457  O O    . MET A 1 29  ? 19.187 18.788 52.088 1.00 58.15  ? 32  MET A O    1 
ATOM   458  C CB   . MET A 1 29  ? 18.594 17.490 49.473 1.00 48.72  ? 32  MET A CB   1 
ATOM   459  C CG   . MET A 1 29  ? 18.360 17.327 48.018 1.00 56.22  ? 32  MET A CG   1 
ATOM   460  S SD   . MET A 1 29  ? 18.354 15.609 47.419 1.00 76.23  ? 32  MET A SD   1 
ATOM   461  C CE   . MET A 1 29  ? 17.487 14.683 48.697 1.00 55.98  ? 32  MET A CE   1 
ATOM   462  H H    . MET A 1 29  ? 18.849 19.846 48.916 0.00 53.68  ? 32  MET A H    1 
ATOM   463  H HA   . MET A 1 29  ? 16.871 18.574 49.914 0.00 54.36  ? 32  MET A HA   1 
ATOM   464  H HB2  . MET A 1 29  ? 19.543 17.642 49.604 0.00 58.46  ? 32  MET A HB2  1 
ATOM   465  H HB3  . MET A 1 29  ? 18.327 16.666 49.910 0.00 58.46  ? 32  MET A HB3  1 
ATOM   466  H HG2  . MET A 1 29  ? 17.497 17.711 47.802 0.00 67.47  ? 32  MET A HG2  1 
ATOM   467  H HG3  . MET A 1 29  ? 19.062 17.796 47.540 0.00 67.47  ? 32  MET A HG3  1 
ATOM   468  H HE1  . MET A 1 29  ? 17.391 13.762 48.410 0.00 67.17  ? 32  MET A HE1  1 
ATOM   469  H HE2  . MET A 1 29  ? 18.001 14.722 49.519 0.00 67.17  ? 32  MET A HE2  1 
ATOM   470  H HE3  . MET A 1 29  ? 16.612 15.079 48.836 0.00 67.17  ? 32  MET A HE3  1 
ATOM   471  N N    . GLY A 1 30  ? 17.022 18.264 52.316 1.00 57.83  ? 33  GLY A N    1 
ATOM   472  C CA   . GLY A 1 30  ? 17.155 18.052 53.711 1.00 57.44  ? 33  GLY A CA   1 
ATOM   473  C C    . GLY A 1 30  ? 17.071 19.293 54.541 1.00 60.77  ? 33  GLY A C    1 
ATOM   474  O O    . GLY A 1 30  ? 16.877 19.183 55.760 1.00 64.59  ? 33  GLY A O    1 
ATOM   475  H H    . GLY A 1 30  ? 16.227 18.156 52.008 0.00 69.39  ? 33  GLY A H    1 
ATOM   476  H HA2  . GLY A 1 30  ? 16.452 17.451 54.002 0.00 68.92  ? 33  GLY A HA2  1 
ATOM   477  H HA3  . GLY A 1 30  ? 18.016 17.638 53.882 0.00 68.92  ? 33  GLY A HA3  1 
ATOM   478  N N    . VAL A 1 31  ? 17.192 20.479 53.940 1.00 46.50  ? 34  VAL A N    1 
ATOM   479  C CA   . VAL A 1 31  ? 16.973 21.666 54.757 1.00 49.63  ? 34  VAL A CA   1 
ATOM   480  C C    . VAL A 1 31  ? 15.573 21.576 55.333 1.00 48.56  ? 34  VAL A C    1 
ATOM   481  O O    . VAL A 1 31  ? 14.597 21.361 54.602 1.00 56.41  ? 34  VAL A O    1 
ATOM   482  C CB   . VAL A 1 31  ? 17.165 22.939 53.920 1.00 51.96  ? 34  VAL A CB   1 
ATOM   483  C CG1  . VAL A 1 31  ? 16.757 24.166 54.761 1.00 46.17  ? 34  VAL A CG1  1 
ATOM   484  C CG2  . VAL A 1 31  ? 18.604 23.014 53.474 1.00 54.91  ? 34  VAL A CG2  1 
ATOM   485  H H    . VAL A 1 31  ? 17.387 20.611 53.113 0.00 55.80  ? 34  VAL A H    1 
ATOM   486  H HA   . VAL A 1 31  ? 17.618 21.699 55.481 0.00 59.55  ? 34  VAL A HA   1 
ATOM   487  H HB   . VAL A 1 31  ? 16.606 22.928 53.127 0.00 62.35  ? 34  VAL A HB   1 
ATOM   488  H HG11 . VAL A 1 31  ? 17.069 24.970 54.319 0.00 55.40  ? 34  VAL A HG11 1 
ATOM   489  H HG12 . VAL A 1 31  ? 15.790 24.186 54.842 0.00 55.40  ? 34  VAL A HG12 1 
ATOM   490  H HG13 . VAL A 1 31  ? 17.160 24.094 55.641 0.00 55.40  ? 34  VAL A HG13 1 
ATOM   491  H HG21 . VAL A 1 31  ? 18.738 23.836 52.978 0.00 65.90  ? 34  VAL A HG21 1 
ATOM   492  H HG22 . VAL A 1 31  ? 19.178 23.002 54.256 0.00 65.90  ? 34  VAL A HG22 1 
ATOM   493  H HG23 . VAL A 1 31  ? 18.799 22.250 52.909 0.00 65.90  ? 34  VAL A HG23 1 
ATOM   494  N N    . SER A 1 32  ? 15.456 21.743 56.650 1.00 48.19  ? 35  SER A N    1 
ATOM   495  C CA   . SER A 1 32  ? 14.149 21.670 57.268 1.00 53.78  ? 35  SER A CA   1 
ATOM   496  C C    . SER A 1 32  ? 13.678 22.967 57.886 1.00 59.57  ? 35  SER A C    1 
ATOM   497  O O    . SER A 1 32  ? 12.486 23.068 58.202 1.00 56.03  ? 35  SER A O    1 
ATOM   498  C CB   . SER A 1 32  ? 14.091 20.533 58.299 1.00 60.46  ? 35  SER A CB   1 
ATOM   499  O OG   . SER A 1 32  ? 15.006 20.730 59.357 1.00 61.37  ? 35  SER A OG   1 
ATOM   500  H H    . SER A 1 32  ? 16.108 21.897 57.188 0.00 57.83  ? 35  SER A H    1 
ATOM   501  H HA   . SER A 1 32  ? 13.502 21.446 56.581 0.00 64.54  ? 35  SER A HA   1 
ATOM   502  H HB2  . SER A 1 32  ? 13.194 20.492 58.666 0.00 72.56  ? 35  SER A HB2  1 
ATOM   503  H HB3  . SER A 1 32  ? 14.306 19.698 57.853 0.00 72.56  ? 35  SER A HB3  1 
ATOM   504  H HG   . SER A 1 32  ? 14.944 20.102 59.912 0.00 73.65  ? 35  SER A HG   1 
ATOM   505  N N    . ASP A 1 33  ? 14.561 23.984 58.023 1.00 39.78  ? 36  ASP A N    1 
ATOM   506  C CA   . ASP A 1 33  ? 14.150 25.242 58.674 1.00 43.14  ? 36  ASP A CA   1 
ATOM   507  C C    . ASP A 1 33  ? 13.157 25.966 57.747 1.00 37.60  ? 36  ASP A C    1 
ATOM   508  O O    . ASP A 1 33  ? 13.463 26.210 56.604 1.00 38.00  ? 36  ASP A O    1 
ATOM   509  C CB   . ASP A 1 33  ? 15.384 26.129 58.838 1.00 41.98  ? 36  ASP A CB   1 
ATOM   510  C CG   . ASP A 1 33  ? 15.056 27.484 59.420 1.00 44.76  ? 36  ASP A CG   1 
ATOM   511  O OD1  . ASP A 1 33  ? 14.851 27.532 60.640 1.00 52.14  ? 36  ASP A OD1  1 
ATOM   512  O OD2  . ASP A 1 33  ? 15.033 28.468 58.692 1.00 43.51  ? 36  ASP A OD2  1 
ATOM   513  H H    . ASP A 1 33  ? 15.377 23.968 57.753 0.00 47.73  ? 36  ASP A H    1 
ATOM   514  H HA   . ASP A 1 33  ? 13.742 25.069 59.537 0.00 51.77  ? 36  ASP A HA   1 
ATOM   515  H HB2  . ASP A 1 33  ? 16.012 25.691 59.433 0.00 50.38  ? 36  ASP A HB2  1 
ATOM   516  H HB3  . ASP A 1 33  ? 15.791 26.267 57.968 0.00 50.38  ? 36  ASP A HB3  1 
ATOM   517  N N    . PRO A 1 34  ? 11.987 26.372 58.252 1.00 38.73  ? 37  PRO A N    1 
ATOM   518  C CA   . PRO A 1 34  ? 10.989 26.964 57.336 1.00 40.39  ? 37  PRO A CA   1 
ATOM   519  C C    . PRO A 1 34  ? 11.464 28.231 56.649 1.00 37.65  ? 37  PRO A C    1 
ATOM   520  O O    . PRO A 1 34  ? 11.135 28.462 55.489 1.00 36.16  ? 37  PRO A O    1 
ATOM   521  C CB   . PRO A 1 34  ? 9.771  27.238 58.243 1.00 43.95  ? 37  PRO A CB   1 
ATOM   522  C CG   . PRO A 1 34  ? 10.025 26.533 59.469 1.00 54.46  ? 37  PRO A CG   1 
ATOM   523  C CD   . PRO A 1 34  ? 11.432 26.118 59.587 1.00 45.17  ? 37  PRO A CD   1 
ATOM   524  H HA   . PRO A 1 34  ? 10.750 26.304 56.667 0.00 48.47  ? 37  PRO A HA   1 
ATOM   525  H HB2  . PRO A 1 34  ? 9.692  28.191 58.405 0.00 52.74  ? 37  PRO A HB2  1 
ATOM   526  H HB3  . PRO A 1 34  ? 8.965  26.907 57.816 0.00 52.74  ? 37  PRO A HB3  1 
ATOM   527  H HG2  . PRO A 1 34  ? 9.801  27.121 60.207 0.00 65.35  ? 37  PRO A HG2  1 
ATOM   528  H HG3  . PRO A 1 34  ? 9.456  25.747 59.487 0.00 65.35  ? 37  PRO A HG3  1 
ATOM   529  H HD2  . PRO A 1 34  ? 11.891 26.649 60.256 0.00 54.20  ? 37  PRO A HD2  1 
ATOM   530  H HD3  . PRO A 1 34  ? 11.494 25.176 59.811 0.00 54.20  ? 37  PRO A HD3  1 
ATOM   531  N N    . ASP A 1 35  ? 12.237 29.079 57.323 1.00 37.31  ? 38  ASP A N    1 
ATOM   532  C CA   . ASP A 1 35  ? 12.703 30.294 56.674 1.00 33.10  ? 38  ASP A CA   1 
ATOM   533  C C    . ASP A 1 35  ? 13.689 29.956 55.570 1.00 31.78  ? 38  ASP A C    1 
ATOM   534  O O    . ASP A 1 35  ? 13.587 30.453 54.428 1.00 32.03  ? 38  ASP A O    1 
ATOM   535  C CB   . ASP A 1 35  ? 13.407 31.219 57.665 1.00 39.42  ? 38  ASP A CB   1 
ATOM   536  C CG   . ASP A 1 35  ? 12.431 31.923 58.578 1.00 52.73  ? 38  ASP A CG   1 
ATOM   537  O OD1  . ASP A 1 35  ? 11.311 32.208 58.111 1.00 61.28  ? 38  ASP A OD1  1 
ATOM   538  O OD2  . ASP A 1 35  ? 12.786 32.200 59.735 1.00 54.96  ? 38  ASP A OD2  1 
ATOM   539  H H    . ASP A 1 35  ? 12.498 28.976 58.136 0.00 44.77  ? 38  ASP A H    1 
ATOM   540  H HA   . ASP A 1 35  ? 11.926 30.751 56.316 0.00 39.72  ? 38  ASP A HA   1 
ATOM   541  H HB2  . ASP A 1 35  ? 14.012 30.696 58.214 0.00 47.31  ? 38  ASP A HB2  1 
ATOM   542  H HB3  . ASP A 1 35  ? 13.903 31.893 57.174 0.00 47.31  ? 38  ASP A HB3  1 
ATOM   543  N N    . ALA A 1 36  ? 14.637 29.040 55.859 1.00 33.05  ? 39  ALA A N    1 
ATOM   544  C CA   . ALA A 1 36  ? 15.594 28.633 54.826 1.00 30.65  ? 39  ALA A CA   1 
ATOM   545  C C    . ALA A 1 36  ? 14.890 28.009 53.633 1.00 29.51  ? 39  ALA A C    1 
ATOM   546  O O    . ALA A 1 36  ? 15.305 28.218 52.480 1.00 27.80  ? 39  ALA A O    1 
ATOM   547  C CB   . ALA A 1 36  ? 16.673 27.703 55.407 1.00 32.58  ? 39  ALA A CB   1 
ATOM   548  H H    . ALA A 1 36  ? 14.738 28.654 56.621 0.00 39.66  ? 39  ALA A H    1 
ATOM   549  H HA   . ALA A 1 36  ? 16.058 29.423 54.507 0.00 36.78  ? 39  ALA A HA   1 
ATOM   550  H HB1  . ALA A 1 36  ? 17.298 27.466 54.704 0.00 39.10  ? 39  ALA A HB1  1 
ATOM   551  H HB2  . ALA A 1 36  ? 17.138 28.166 56.121 0.00 39.10  ? 39  ALA A HB2  1 
ATOM   552  H HB3  . ALA A 1 36  ? 16.247 26.903 55.754 0.00 39.10  ? 39  ALA A HB3  1 
ATOM   553  N N    . LYS A 1 37  ? 13.852 27.187 53.886 1.00 30.62  ? 40  LYS A N    1 
ATOM   554  C CA   . LYS A 1 37  ? 13.114 26.597 52.745 1.00 29.70  ? 40  LYS A CA   1 
ATOM   555  C C    . LYS A 1 37  ? 12.562 27.639 51.789 1.00 29.21  ? 40  LYS A C    1 
ATOM   556  O O    . LYS A 1 37  ? 12.502 27.398 50.550 1.00 29.43  ? 40  LYS A O    1 
ATOM   557  C CB   . LYS A 1 37  ? 11.936 25.740 53.288 1.00 32.57  ? 40  LYS A CB   1 
ATOM   558  C CG   . LYS A 1 37  ? 12.357 24.393 53.796 1.00 39.11  ? 40  LYS A CG   1 
ATOM   559  C CD   . LYS A 1 37  ? 11.362 23.794 54.751 1.00 54.07  ? 40  LYS A CD   1 
ATOM   560  C CE   . LYS A 1 37  ? 10.725 22.561 54.169 1.00 56.22  ? 40  LYS A CE   1 
ATOM   561  N NZ   . LYS A 1 37  ? 9.578  22.126 55.005 1.00 52.08  ? 40  LYS A NZ   1 
ATOM   562  H H    . LYS A 1 37  ? 13.567 26.965 54.666 0.00 36.75  ? 40  LYS A H    1 
ATOM   563  H HA   . LYS A 1 37  ? 13.738 26.044 52.248 0.00 35.64  ? 40  LYS A HA   1 
ATOM   564  H HB2  . LYS A 1 37  ? 11.516 26.215 54.022 0.00 39.09  ? 40  LYS A HB2  1 
ATOM   565  H HB3  . LYS A 1 37  ? 11.295 25.600 52.573 0.00 39.09  ? 40  LYS A HB3  1 
ATOM   566  H HG2  . LYS A 1 37  ? 12.453 23.787 53.044 0.00 46.93  ? 40  LYS A HG2  1 
ATOM   567  H HG3  . LYS A 1 37  ? 13.204 24.480 54.261 0.00 46.93  ? 40  LYS A HG3  1 
ATOM   568  H HD2  . LYS A 1 37  ? 11.812 23.546 55.573 0.00 64.88  ? 40  LYS A HD2  1 
ATOM   569  H HD3  . LYS A 1 37  ? 10.663 24.441 54.936 0.00 64.88  ? 40  LYS A HD3  1 
ATOM   570  H HE2  . LYS A 1 37  ? 10.401 22.753 53.275 0.00 67.46  ? 40  LYS A HE2  1 
ATOM   571  H HE3  . LYS A 1 37  ? 11.375 21.842 54.138 0.00 67.46  ? 40  LYS A HE3  1 
ATOM   572  H HZ1  . LYS A 1 37  ? 9.146  21.458 54.606 0.00 62.49  ? 40  LYS A HZ1  1 
ATOM   573  H HZ2  . LYS A 1 37  ? 9.869  21.849 55.799 0.00 62.49  ? 40  LYS A HZ2  1 
ATOM   574  H HZ3  . LYS A 1 37  ? 9.015  22.804 55.125 0.00 62.49  ? 40  LYS A HZ3  1 
ATOM   575  N N    . LYS A 1 38  ? 12.039 28.756 52.290 1.00 27.97  ? 41  LYS A N    1 
ATOM   576  C CA   . LYS A 1 38  ? 11.534 29.798 51.409 1.00 28.88  ? 41  LYS A CA   1 
ATOM   577  C C    . LYS A 1 38  ? 12.631 30.310 50.532 1.00 25.53  ? 41  LYS A C    1 
ATOM   578  O O    . LYS A 1 38  ? 12.463 30.470 49.339 1.00 24.00  ? 41  LYS A O    1 
ATOM   579  C CB   . LYS A 1 38  ? 11.008 30.970 52.271 1.00 34.40  ? 41  LYS A CB   1 
ATOM   580  C CG   . LYS A 1 38  ? 9.641  30.730 52.920 1.00 46.50  ? 41  LYS A CG   1 
ATOM   581  C CD   . LYS A 1 38  ? 9.085  32.013 53.549 1.00 58.07  ? 41  LYS A CD   1 
ATOM   582  C CE   . LYS A 1 38  ? 10.111 32.789 54.340 1.00 57.42  ? 41  LYS A CE   1 
ATOM   583  N NZ   . LYS A 1 38  ? 9.516  33.294 55.633 1.00 68.61  ? 41  LYS A NZ   1 
ATOM   584  H H    . LYS A 1 38  ? 11.966 28.931 53.128 0.00 33.55  ? 41  LYS A H    1 
ATOM   585  H HA   . LYS A 1 38  ? 10.817 29.439 50.863 0.00 34.66  ? 41  LYS A HA   1 
ATOM   586  H HB2  . LYS A 1 38  ? 11.644 31.137 52.984 0.00 41.28  ? 41  LYS A HB2  1 
ATOM   587  H HB3  . LYS A 1 38  ? 10.928 31.755 51.707 0.00 41.28  ? 41  LYS A HB3  1 
ATOM   588  H HG2  . LYS A 1 38  ? 9.014  30.424 52.246 0.00 55.80  ? 41  LYS A HG2  1 
ATOM   589  H HG3  . LYS A 1 38  ? 9.730  30.062 53.618 0.00 55.80  ? 41  LYS A HG3  1 
ATOM   590  H HD2  . LYS A 1 38  ? 8.755  32.591 52.843 0.00 69.68  ? 41  LYS A HD2  1 
ATOM   591  H HD3  . LYS A 1 38  ? 8.361  31.780 54.151 0.00 69.68  ? 41  LYS A HD3  1 
ATOM   592  H HE2  . LYS A 1 38  ? 10.862 32.213 54.550 0.00 68.91  ? 41  LYS A HE2  1 
ATOM   593  H HE3  . LYS A 1 38  ? 10.413 33.551 53.821 0.00 68.91  ? 41  LYS A HE3  1 
ATOM   594  H HZ1  . LYS A 1 38  ? 10.126 33.755 56.089 0.00 82.33  ? 41  LYS A HZ1  1 
ATOM   595  H HZ2  . LYS A 1 38  ? 8.822  33.825 55.462 0.00 82.33  ? 41  LYS A HZ2  1 
ATOM   596  H HZ3  . LYS A 1 38  ? 9.241  32.609 56.129 0.00 82.33  ? 41  LYS A HZ3  1 
ATOM   597  N N    . PHE A 1 39  ? 13.816 30.620 51.081 1.00 25.02  ? 42  PHE A N    1 
ATOM   598  C CA   . PHE A 1 39  ? 14.876 31.138 50.232 1.00 23.66  ? 42  PHE A CA   1 
ATOM   599  C C    . PHE A 1 39  ? 15.372 30.101 49.236 1.00 23.67  ? 42  PHE A C    1 
ATOM   600  O O    . PHE A 1 39  ? 15.713 30.444 48.089 1.00 23.00  ? 42  PHE A O    1 
ATOM   601  C CB   . PHE A 1 39  ? 16.065 31.566 51.139 1.00 25.94  ? 42  PHE A CB   1 
ATOM   602  C CG   . PHE A 1 39  ? 15.753 32.795 51.900 1.00 25.98  ? 42  PHE A CG   1 
ATOM   603  C CD1  . PHE A 1 39  ? 15.665 34.017 51.222 1.00 26.79  ? 42  PHE A CD1  1 
ATOM   604  C CD2  . PHE A 1 39  ? 15.553 32.783 53.234 1.00 28.80  ? 42  PHE A CD2  1 
ATOM   605  C CE1  . PHE A 1 39  ? 15.411 35.180 51.922 1.00 28.93  ? 42  PHE A CE1  1 
ATOM   606  C CE2  . PHE A 1 39  ? 15.334 33.962 53.963 1.00 30.72  ? 42  PHE A CE2  1 
ATOM   607  C CZ   . PHE A 1 39  ? 15.223 35.169 53.297 1.00 34.10  ? 42  PHE A CZ   1 
ATOM   608  H H    . PHE A 1 39  ? 14.016 30.539 51.913 0.00 30.02  ? 42  PHE A H    1 
ATOM   609  H HA   . PHE A 1 39  ? 14.532 31.896 49.733 0.00 28.39  ? 42  PHE A HA   1 
ATOM   610  H HB2  . PHE A 1 39  ? 16.258 30.856 51.770 0.00 31.12  ? 42  PHE A HB2  1 
ATOM   611  H HB3  . PHE A 1 39  ? 16.844 31.739 50.586 0.00 31.12  ? 42  PHE A HB3  1 
ATOM   612  H HD1  . PHE A 1 39  ? 15.777 34.045 50.299 0.00 32.15  ? 42  PHE A HD1  1 
ATOM   613  H HD2  . PHE A 1 39  ? 15.561 31.969 53.684 0.00 34.56  ? 42  PHE A HD2  1 
ATOM   614  H HE1  . PHE A 1 39  ? 15.365 35.987 51.462 0.00 34.72  ? 42  PHE A HE1  1 
ATOM   615  H HE2  . PHE A 1 39  ? 15.264 33.932 54.890 0.00 36.86  ? 42  PHE A HE2  1 
ATOM   616  H HZ   . PHE A 1 39  ? 15.028 35.953 53.758 0.00 40.92  ? 42  PHE A HZ   1 
ATOM   617  N N    . TYR A 1 40  ? 15.508 28.838 49.623 1.00 24.02  ? 43  TYR A N    1 
ATOM   618  C CA   . TYR A 1 40  ? 15.891 27.804 48.645 1.00 24.30  ? 43  TYR A CA   1 
ATOM   619  C C    . TYR A 1 40  ? 14.857 27.687 47.539 1.00 24.42  ? 43  TYR A C    1 
ATOM   620  O O    . TYR A 1 40  ? 15.223 27.503 46.380 1.00 24.14  ? 43  TYR A O    1 
ATOM   621  C CB   . TYR A 1 40  ? 16.138 26.464 49.319 1.00 25.68  ? 43  TYR A CB   1 
ATOM   622  C CG   . TYR A 1 40  ? 17.555 26.256 49.764 1.00 25.74  ? 43  TYR A CG   1 
ATOM   623  C CD1  . TYR A 1 40  ? 18.509 25.829 48.829 1.00 30.47  ? 43  TYR A CD1  1 
ATOM   624  C CD2  . TYR A 1 40  ? 17.865 26.552 51.021 1.00 29.12  ? 43  TYR A CD2  1 
ATOM   625  C CE1  . TYR A 1 40  ? 19.815 25.626 49.230 1.00 31.17  ? 43  TYR A CE1  1 
ATOM   626  C CE2  . TYR A 1 40  ? 19.204 26.328 51.485 1.00 32.58  ? 43  TYR A CE2  1 
ATOM   627  C CZ   . TYR A 1 40  ? 20.136 25.906 50.493 1.00 32.36  ? 43  TYR A CZ   1 
ATOM   628  O OH   . TYR A 1 40  ? 21.471 25.719 51.019 1.00 38.93  ? 43  TYR A OH   1 
ATOM   629  H H    . TYR A 1 40  ? 15.390 28.550 50.425 0.00 28.82  ? 43  TYR A H    1 
ATOM   630  H HA   . TYR A 1 40  ? 16.733 28.065 48.241 0.00 29.16  ? 43  TYR A HA   1 
ATOM   631  H HB2  . TYR A 1 40  ? 15.571 26.401 50.104 0.00 30.82  ? 43  TYR A HB2  1 
ATOM   632  H HB3  . TYR A 1 40  ? 15.919 25.756 48.694 0.00 30.82  ? 43  TYR A HB3  1 
ATOM   633  H HD1  . TYR A 1 40  ? 18.263 25.683 47.944 0.00 36.56  ? 43  TYR A HD1  1 
ATOM   634  H HD2  . TYR A 1 40  ? 17.221 26.900 51.595 0.00 34.95  ? 43  TYR A HD2  1 
ATOM   635  H HE1  . TYR A 1 40  ? 20.453 25.302 48.636 0.00 37.40  ? 43  TYR A HE1  1 
ATOM   636  H HE2  . TYR A 1 40  ? 19.448 26.450 52.374 0.00 39.09  ? 43  TYR A HE2  1 
ATOM   637  H HH   . TYR A 1 40  ? 21.490 25.926 51.833 0.00 46.71  ? 43  TYR A HH   1 
ATOM   638  N N    . ALA A 1 41  ? 13.540 27.717 47.876 1.00 23.13  ? 44  ALA A N    1 
ATOM   639  C CA   . ALA A 1 41  ? 12.525 27.591 46.776 1.00 22.39  ? 44  ALA A CA   1 
ATOM   640  C C    . ALA A 1 41  ? 12.622 28.719 45.819 1.00 24.31  ? 44  ALA A C    1 
ATOM   641  O O    . ALA A 1 41  ? 12.658 28.516 44.584 1.00 23.49  ? 44  ALA A O    1 
ATOM   642  C CB   . ALA A 1 41  ? 11.141 27.554 47.413 1.00 23.76  ? 44  ALA A CB   1 
ATOM   643  H H    . ALA A 1 41  ? 13.225 27.803 48.672 0.00 27.75  ? 44  ALA A H    1 
ATOM   644  H HA   . ALA A 1 41  ? 12.681 26.773 46.279 0.00 26.86  ? 44  ALA A HA   1 
ATOM   645  H HB1  . ALA A 1 41  ? 10.474 27.466 46.713 0.00 28.52  ? 44  ALA A HB1  1 
ATOM   646  H HB2  . ALA A 1 41  ? 11.090 26.796 48.015 0.00 28.52  ? 44  ALA A HB2  1 
ATOM   647  H HB3  . ALA A 1 41  ? 10.997 28.378 47.904 0.00 28.52  ? 44  ALA A HB3  1 
ATOM   648  N N    . ILE A 1 42  ? 12.666 29.958 46.310 1.00 21.61  ? 45  ILE A N    1 
ATOM   649  C CA   . ILE A 1 42  ? 12.700 31.130 45.413 1.00 22.77  ? 45  ILE A CA   1 
ATOM   650  C C    . ILE A 1 42  ? 13.948 31.060 44.564 1.00 21.68  ? 45  ILE A C    1 
ATOM   651  O O    . ILE A 1 42  ? 13.917 31.284 43.337 1.00 22.94  ? 45  ILE A O    1 
ATOM   652  C CB   . ILE A 1 42  ? 12.673 32.419 46.268 1.00 21.60  ? 45  ILE A CB   1 
ATOM   653  C CG1  . ILE A 1 42  ? 11.363 32.621 46.979 1.00 23.98  ? 45  ILE A CG1  1 
ATOM   654  C CG2  . ILE A 1 42  ? 13.026 33.615 45.295 1.00 24.04  ? 45  ILE A CG2  1 
ATOM   655  C CD1  . ILE A 1 42  ? 11.423 33.712 48.078 1.00 30.51  ? 45  ILE A CD1  1 
ATOM   656  H H    . ILE A 1 42  ? 12.676 30.153 47.148 0.00 25.93  ? 45  ILE A H    1 
ATOM   657  H HA   . ILE A 1 42  ? 11.928 31.130 44.827 0.00 27.33  ? 45  ILE A HA   1 
ATOM   658  H HB   . ILE A 1 42  ? 13.323 32.357 46.985 0.00 25.92  ? 45  ILE A HB   1 
ATOM   659  H HG12 . ILE A 1 42  ? 10.692 32.887 46.331 0.00 28.78  ? 45  ILE A HG12 1 
ATOM   660  H HG13 . ILE A 1 42  ? 11.104 31.787 47.401 0.00 28.78  ? 45  ILE A HG13 1 
ATOM   661  H HG21 . ILE A 1 42  ? 12.742 34.448 45.702 0.00 28.85  ? 45  ILE A HG21 1 
ATOM   662  H HG22 . ILE A 1 42  ? 13.985 33.629 45.147 0.00 28.85  ? 45  ILE A HG22 1 
ATOM   663  H HG23 . ILE A 1 42  ? 12.563 33.484 44.452 0.00 28.85  ? 45  ILE A HG23 1 
ATOM   664  H HD11 . ILE A 1 42  ? 10.584 33.717 48.564 0.00 36.61  ? 45  ILE A HD11 1 
ATOM   665  H HD12 . ILE A 1 42  ? 12.155 33.511 48.683 0.00 36.61  ? 45  ILE A HD12 1 
ATOM   666  H HD13 . ILE A 1 42  ? 11.568 34.575 47.659 0.00 36.61  ? 45  ILE A HD13 1 
ATOM   667  N N    . THR A 1 43  ? 15.091 30.766 45.184 1.00 20.59  ? 46  THR A N    1 
ATOM   668  C CA   . THR A 1 43  ? 16.412 30.890 44.559 1.00 21.61  ? 46  THR A CA   1 
ATOM   669  C C    . THR A 1 43  ? 16.644 29.784 43.573 1.00 27.24  ? 46  THR A C    1 
ATOM   670  O O    . THR A 1 43  ? 17.352 30.009 42.584 1.00 26.91  ? 46  THR A O    1 
ATOM   671  C CB   . THR A 1 43  ? 17.484 31.001 45.589 1.00 23.38  ? 46  THR A CB   1 
ATOM   672  O OG1  . THR A 1 43  ? 17.134 32.057 46.477 1.00 23.50  ? 46  THR A OG1  1 
ATOM   673  C CG2  . THR A 1 43  ? 18.824 31.364 44.913 1.00 30.28  ? 46  THR A CG2  1 
ATOM   674  H H    . THR A 1 43  ? 15.134 30.483 45.995 0.00 24.70  ? 46  THR A H    1 
ATOM   675  H HA   . THR A 1 43  ? 16.462 31.721 44.062 0.00 25.93  ? 46  THR A HA   1 
ATOM   676  H HB   . THR A 1 43  ? 17.586 30.164 46.067 0.00 28.06  ? 46  THR A HB   1 
ATOM   677  H HG1  . THR A 1 43  ? 16.443 31.851 46.909 0.00 28.20  ? 46  THR A HG1  1 
ATOM   678  H HG21 . THR A 1 43  ? 19.496 31.548 45.588 0.00 36.33  ? 46  THR A HG21 1 
ATOM   679  H HG22 . THR A 1 43  ? 19.126 30.627 44.360 0.00 36.33  ? 46  THR A HG22 1 
ATOM   680  H HG23 . THR A 1 43  ? 18.712 32.151 44.357 0.00 36.33  ? 46  THR A HG23 1 
ATOM   681  N N    . THR A 1 44  ? 16.033 28.587 43.778 1.00 21.89  ? 47  THR A N    1 
ATOM   682  C CA   . THR A 1 44  ? 16.204 27.482 42.847 1.00 21.52  ? 47  THR A CA   1 
ATOM   683  C C    . THR A 1 44  ? 15.291 27.675 41.621 1.00 22.23  ? 47  THR A C    1 
ATOM   684  O O    . THR A 1 44  ? 15.660 27.340 40.489 1.00 21.68  ? 47  THR A O    1 
ATOM   685  C CB   . THR A 1 44  ? 15.859 26.157 43.520 1.00 20.55  ? 47  THR A CB   1 
ATOM   686  O OG1  . THR A 1 44  ? 16.785 26.026 44.661 1.00 23.73  ? 47  THR A OG1  1 
ATOM   687  C CG2  . THR A 1 44  ? 16.100 24.944 42.560 1.00 23.79  ? 47  THR A CG2  1 
ATOM   688  H H    . THR A 1 44  ? 15.523 28.408 44.447 0.00 26.27  ? 47  THR A H    1 
ATOM   689  H HA   . THR A 1 44  ? 17.131 27.441 42.567 0.00 25.83  ? 47  THR A HA   1 
ATOM   690  H HB   . THR A 1 44  ? 14.926 26.140 43.785 0.00 24.67  ? 47  THR A HB   1 
ATOM   691  H HG1  . THR A 1 44  ? 16.654 26.648 45.210 0.00 28.47  ? 47  THR A HG1  1 
ATOM   692  H HG21 . THR A 1 44  ? 15.956 24.111 43.035 0.00 28.55  ? 47  THR A HG21 1 
ATOM   693  H HG22 . THR A 1 44  ? 15.486 24.989 41.810 0.00 28.55  ? 47  THR A HG22 1 
ATOM   694  H HG23 . THR A 1 44  ? 17.009 24.962 42.224 0.00 28.55  ? 47  THR A HG23 1 
ATOM   695  N N    A LEU A 1 45  ? 14.093 28.228 41.814 0.72 19.60  ? 48  LEU A N    1 
ATOM   696  N N    B LEU A 1 45  ? 14.112 28.253 41.809 0.28 19.65  ? 48  LEU A N    1 
ATOM   697  C CA   A LEU A 1 45  ? 13.166 28.503 40.716 0.72 20.33  ? 48  LEU A CA   1 
ATOM   698  C CA   B LEU A 1 45  ? 13.180 28.484 40.711 0.28 20.47  ? 48  LEU A CA   1 
ATOM   699  C C    A LEU A 1 45  ? 13.787 29.419 39.721 0.72 20.23  ? 48  LEU A C    1 
ATOM   700  C C    B LEU A 1 45  ? 13.701 29.528 39.735 0.28 20.56  ? 48  LEU A C    1 
ATOM   701  O O    A LEU A 1 45  ? 13.515 29.256 38.522 0.72 20.30  ? 48  LEU A O    1 
ATOM   702  O O    B LEU A 1 45  ? 13.304 29.537 38.555 0.28 20.85  ? 48  LEU A O    1 
ATOM   703  C CB   A LEU A 1 45  ? 11.852 29.059 41.248 0.72 20.98  ? 48  LEU A CB   1 
ATOM   704  C CB   B LEU A 1 45  ? 11.834 28.839 41.345 0.28 19.84  ? 48  LEU A CB   1 
ATOM   705  C CG   A LEU A 1 45  ? 10.884 28.057 41.783 0.72 21.58  ? 48  LEU A CG   1 
ATOM   706  C CG   B LEU A 1 45  ? 10.646 29.102 40.451 0.28 22.51  ? 48  LEU A CG   1 
ATOM   707  C CD1  A LEU A 1 45  ? 9.731  28.778 42.456 0.72 27.24  ? 48  LEU A CD1  1 
ATOM   708  C CD1  B LEU A 1 45  ? 10.286 27.844 39.667 0.28 20.59  ? 48  LEU A CD1  1 
ATOM   709  C CD2  A LEU A 1 45  ? 10.281 27.201 40.655 0.72 24.32  ? 48  LEU A CD2  1 
ATOM   710  C CD2  B LEU A 1 45  ? 9.456  29.575 41.233 0.28 20.30  ? 48  LEU A CD2  1 
ATOM   711  H H    A LEU A 1 45  ? 13.786 28.457 42.584 0.72 23.53  ? 48  LEU A H    1 
ATOM   712  H H    B LEU A 1 45  ? 13.823 28.526 42.572 0.28 23.58  ? 48  LEU A H    1 
ATOM   713  H HA   A LEU A 1 45  ? 12.954 27.671 40.264 0.72 24.40  ? 48  LEU A HA   1 
ATOM   714  H HA   B LEU A 1 45  ? 13.041 27.696 40.163 0.28 24.57  ? 48  LEU A HA   1 
ATOM   715  H HB2  A LEU A 1 45  ? 12.055 29.675 41.969 0.72 25.18  ? 48  LEU A HB2  1 
ATOM   716  H HB2  B LEU A 1 45  ? 11.582 28.102 41.924 0.28 23.81  ? 48  LEU A HB2  1 
ATOM   717  H HB3  A LEU A 1 45  ? 11.409 29.528 40.525 0.72 25.18  ? 48  LEU A HB3  1 
ATOM   718  H HB3  B LEU A 1 45  ? 11.964 29.644 41.871 0.28 23.81  ? 48  LEU A HB3  1 
ATOM   719  H HG   A LEU A 1 45  ? 11.358 27.486 42.407 0.72 25.90  ? 48  LEU A HG   1 
ATOM   720  H HG   B LEU A 1 45  ? 10.886 29.806 39.828 0.28 27.01  ? 48  LEU A HG   1 
ATOM   721  H HD11 A LEU A 1 45  ? 9.079  28.124 42.752 0.72 32.69  ? 48  LEU A HD11 1 
ATOM   722  H HD11 B LEU A 1 45  ? 9.610  28.065 39.007 0.28 24.71  ? 48  LEU A HD11 1 
ATOM   723  H HD12 A LEU A 1 45  ? 10.070 29.275 43.217 0.72 32.69  ? 48  LEU A HD12 1 
ATOM   724  H HD12 B LEU A 1 45  ? 11.082 27.508 39.226 0.28 24.71  ? 48  LEU A HD12 1 
ATOM   725  H HD13 A LEU A 1 45  ? 9.324  29.386 41.819 0.72 32.69  ? 48  LEU A HD13 1 
ATOM   726  H HD13 B LEU A 1 45  ? 9.942  27.176 40.281 0.28 24.71  ? 48  LEU A HD13 1 
ATOM   727  H HD21 A LEU A 1 45  ? 9.789  26.463 41.048 0.72 29.18  ? 48  LEU A HD21 1 
ATOM   728  H HD21 B LEU A 1 45  ? 8.702  29.677 40.631 0.28 24.36  ? 48  LEU A HD21 1 
ATOM   729  H HD22 A LEU A 1 45  ? 9.685  27.751 40.124 0.72 29.18  ? 48  LEU A HD22 1 
ATOM   730  H HD22 B LEU A 1 45  ? 9.247  28.920 41.917 0.28 24.36  ? 48  LEU A HD22 1 
ATOM   731  H HD23 A LEU A 1 45  ? 10.999 26.860 40.099 0.72 29.18  ? 48  LEU A HD23 1 
ATOM   732  H HD23 B LEU A 1 45  ? 9.667  30.427 41.646 0.28 24.36  ? 48  LEU A HD23 1 
ATOM   733  N N    . VAL A 1 46  ? 14.596 30.423 40.134 1.00 18.94  ? 49  VAL A N    1 
ATOM   734  C CA   . VAL A 1 46  ? 15.083 31.433 39.211 1.00 19.74  ? 49  VAL A CA   1 
ATOM   735  C C    . VAL A 1 46  ? 15.960 30.820 38.147 1.00 18.93  ? 49  VAL A C    1 
ATOM   736  O O    . VAL A 1 46  ? 15.591 31.041 36.932 1.00 18.92  ? 49  VAL A O    1 
ATOM   737  C CB   . VAL A 1 46  ? 15.790 32.490 40.047 1.00 19.02  ? 49  VAL A CB   1 
ATOM   738  C CG1  . VAL A 1 46  ? 16.664 33.417 39.109 1.00 21.53  ? 49  VAL A CG1  1 
ATOM   739  C CG2  . VAL A 1 46  ? 14.822 33.362 40.854 1.00 21.87  ? 49  VAL A CG2  1 
ATOM   740  H H    . VAL A 1 46  ? 14.871 30.533 40.941 0.00 22.73  ? 49  VAL A H    1 
ATOM   741  H HA   . VAL A 1 46  ? 14.359 31.849 38.718 0.00 23.69  ? 49  VAL A HA   1 
ATOM   742  H HB   . VAL A 1 46  ? 16.353 32.022 40.684 0.00 22.82  ? 49  VAL A HB   1 
ATOM   743  H HG11 . VAL A 1 46  ? 16.972 34.182 39.620 0.00 25.84  ? 49  VAL A HG11 1 
ATOM   744  H HG12 . VAL A 1 46  ? 17.423 32.910 38.782 0.00 25.84  ? 49  VAL A HG12 1 
ATOM   745  H HG13 . VAL A 1 46  ? 16.119 33.715 38.364 0.00 25.84  ? 49  VAL A HG13 1 
ATOM   746  H HG21 . VAL A 1 46  ? 15.332 33.993 41.384 0.00 26.25  ? 49  VAL A HG21 1 
ATOM   747  H HG22 . VAL A 1 46  ? 14.241 33.839 40.241 0.00 26.25  ? 49  VAL A HG22 1 
ATOM   748  H HG23 . VAL A 1 46  ? 14.294 32.793 41.435 0.00 26.25  ? 49  VAL A HG23 1 
ATOM   749  N N    . PRO A 1 47  ? 16.990 30.047 38.339 1.00 17.86  ? 50  PRO A N    1 
ATOM   750  C CA   . PRO A 1 47  ? 17.715 29.457 37.201 1.00 19.81  ? 50  PRO A CA   1 
ATOM   751  C C    . PRO A 1 47  ? 16.937 28.361 36.508 1.00 20.75  ? 50  PRO A C    1 
ATOM   752  O O    . PRO A 1 47  ? 17.182 28.101 35.315 1.00 19.61  ? 50  PRO A O    1 
ATOM   753  C CB   . PRO A 1 47  ? 19.045 28.924 37.849 1.00 20.68  ? 50  PRO A CB   1 
ATOM   754  C CG   . PRO A 1 47  ? 18.619 28.685 39.334 1.00 23.62  ? 50  PRO A CG   1 
ATOM   755  C CD   . PRO A 1 47  ? 17.651 29.821 39.645 1.00 19.23  ? 50  PRO A CD   1 
ATOM   756  H HA   . PRO A 1 47  ? 17.947 30.140 36.553 0.00 23.77  ? 50  PRO A HA   1 
ATOM   757  H HB2  . PRO A 1 47  ? 19.327 28.100 37.422 0.00 24.82  ? 50  PRO A HB2  1 
ATOM   758  H HB3  . PRO A 1 47  ? 19.748 29.589 37.782 0.00 24.82  ? 50  PRO A HB3  1 
ATOM   759  H HG2  . PRO A 1 47  ? 18.183 27.823 39.419 0.00 28.35  ? 50  PRO A HG2  1 
ATOM   760  H HG3  . PRO A 1 47  ? 19.397 28.722 39.913 0.00 28.35  ? 50  PRO A HG3  1 
ATOM   761  H HD2  . PRO A 1 47  ? 17.007 29.555 40.319 0.00 23.07  ? 50  PRO A HD2  1 
ATOM   762  H HD3  . PRO A 1 47  ? 18.127 30.615 39.935 0.00 23.07  ? 50  PRO A HD3  1 
ATOM   763  N N    . ALA A 1 48  ? 15.935 27.748 37.151 1.00 17.08  ? 51  ALA A N    1 
ATOM   764  C CA   . ALA A 1 48  ? 15.141 26.730 36.455 1.00 18.39  ? 51  ALA A CA   1 
ATOM   765  C C    . ALA A 1 48  ? 14.295 27.385 35.363 1.00 17.80  ? 51  ALA A C    1 
ATOM   766  O O    . ALA A 1 48  ? 14.217 26.844 34.207 1.00 18.79  ? 51  ALA A O    1 
ATOM   767  C CB   . ALA A 1 48  ? 14.174 26.070 37.481 1.00 19.33  ? 51  ALA A CB   1 
ATOM   768  H H    . ALA A 1 48  ? 15.702 27.898 37.965 0.00 20.50  ? 51  ALA A H    1 
ATOM   769  H HA   . ALA A 1 48  ? 15.729 26.063 36.067 0.00 22.07  ? 51  ALA A HA   1 
ATOM   770  H HB1  . ALA A 1 48  ? 13.651 25.389 37.030 0.00 23.20  ? 51  ALA A HB1  1 
ATOM   771  H HB2  . ALA A 1 48  ? 14.696 25.668 38.193 0.00 23.20  ? 51  ALA A HB2  1 
ATOM   772  H HB3  . ALA A 1 48  ? 13.587 26.751 37.845 0.00 23.20  ? 51  ALA A HB3  1 
ATOM   773  N N    . ILE A 1 49  ? 13.676 28.546 35.641 1.00 18.22  ? 52  ILE A N    1 
ATOM   774  C CA   . ILE A 1 49  ? 12.877 29.236 34.582 1.00 16.49  ? 52  ILE A CA   1 
ATOM   775  C C    . ILE A 1 49  ? 13.867 29.759 33.561 1.00 18.51  ? 52  ILE A C    1 
ATOM   776  O O    . ILE A 1 49  ? 13.607 29.642 32.345 1.00 18.92  ? 52  ILE A O    1 
ATOM   777  C CB   . ILE A 1 49  ? 12.179 30.405 35.312 1.00 17.45  ? 52  ILE A CB   1 
ATOM   778  C CG1  . ILE A 1 49  ? 11.081 29.859 36.160 1.00 17.99  ? 52  ILE A CG1  1 
ATOM   779  C CG2  . ILE A 1 49  ? 11.507 31.326 34.255 1.00 21.09  ? 52  ILE A CG2  1 
ATOM   780  C CD1  . ILE A 1 49  ? 10.512 30.979 37.190 1.00 21.93  ? 52  ILE A CD1  1 
ATOM   781  H H    . ILE A 1 49  ? 13.695 28.948 36.401 0.00 21.86  ? 52  ILE A H    1 
ATOM   782  H HA   . ILE A 1 49  ? 12.229 28.666 34.139 0.00 19.79  ? 52  ILE A HA   1 
ATOM   783  H HB   . ILE A 1 49  ? 12.832 30.886 35.843 0.00 20.94  ? 52  ILE A HB   1 
ATOM   784  H HG12 . ILE A 1 49  ? 10.351 29.568 35.591 0.00 21.59  ? 52  ILE A HG12 1 
ATOM   785  H HG13 . ILE A 1 49  ? 11.418 29.111 36.677 0.00 21.59  ? 52  ILE A HG13 1 
ATOM   786  H HG21 . ILE A 1 49  ? 10.902 31.936 34.706 0.00 25.31  ? 52  ILE A HG21 1 
ATOM   787  H HG22 . ILE A 1 49  ? 12.195 31.827 33.790 0.00 25.31  ? 52  ILE A HG22 1 
ATOM   788  H HG23 . ILE A 1 49  ? 11.014 30.777 33.625 0.00 25.31  ? 52  ILE A HG23 1 
ATOM   789  H HD11 . ILE A 1 49  ? 9.914  30.551 37.823 0.00 26.32  ? 52  ILE A HD11 1 
ATOM   790  H HD12 . ILE A 1 49  ? 11.257 31.383 37.661 0.00 26.32  ? 52  ILE A HD12 1 
ATOM   791  H HD13 . ILE A 1 49  ? 10.032 31.656 36.688 0.00 26.32  ? 52  ILE A HD13 1 
ATOM   792  N N    . ALA A 1 50  ? 14.995 30.292 33.957 1.00 18.27  ? 53  ALA A N    1 
ATOM   793  C CA   . ALA A 1 50  ? 15.959 30.758 32.921 1.00 17.81  ? 53  ALA A CA   1 
ATOM   794  C C    . ALA A 1 50  ? 16.474 29.641 32.079 1.00 19.37  ? 53  ALA A C    1 
ATOM   795  O O    . ALA A 1 50  ? 16.631 29.883 30.858 1.00 18.96  ? 53  ALA A O    1 
ATOM   796  C CB   . ALA A 1 50  ? 17.094 31.572 33.631 1.00 19.52  ? 53  ALA A CB   1 
ATOM   797  H H    . ALA A 1 50  ? 15.240 30.402 34.774 0.00 21.92  ? 53  ALA A H    1 
ATOM   798  H HA   . ALA A 1 50  ? 15.515 31.352 32.296 0.00 21.37  ? 53  ALA A HA   1 
ATOM   799  H HB1  . ALA A 1 50  ? 17.719 31.892 32.962 0.00 23.43  ? 53  ALA A HB1  1 
ATOM   800  H HB2  . ALA A 1 50  ? 16.697 32.324 34.100 0.00 23.43  ? 53  ALA A HB2  1 
ATOM   801  H HB3  . ALA A 1 50  ? 17.551 30.994 34.261 0.00 23.43  ? 53  ALA A HB3  1 
ATOM   802  N N    . PHE A 1 51  ? 16.721 28.467 32.618 1.00 17.96  ? 54  PHE A N    1 
ATOM   803  C CA   . PHE A 1 51  ? 17.096 27.308 31.781 1.00 17.41  ? 54  PHE A CA   1 
ATOM   804  C C    . PHE A 1 51  ? 16.076 27.082 30.703 1.00 19.05  ? 54  PHE A C    1 
ATOM   805  O O    . PHE A 1 51  ? 16.459 26.896 29.495 1.00 18.87  ? 54  PHE A O    1 
ATOM   806  C CB   . PHE A 1 51  ? 17.218 26.024 32.686 1.00 19.02  ? 54  PHE A CB   1 
ATOM   807  C CG   . PHE A 1 51  ? 17.283 24.751 31.902 1.00 19.66  ? 54  PHE A CG   1 
ATOM   808  C CD1  . PHE A 1 51  ? 18.414 24.302 31.264 1.00 25.22  ? 54  PHE A CD1  1 
ATOM   809  C CD2  . PHE A 1 51  ? 16.147 24.002 31.803 1.00 22.05  ? 54  PHE A CD2  1 
ATOM   810  C CE1  . PHE A 1 51  ? 18.400 23.111 30.582 1.00 25.34  ? 54  PHE A CE1  1 
ATOM   811  C CE2  . PHE A 1 51  ? 16.136 22.788 31.082 1.00 25.70  ? 54  PHE A CE2  1 
ATOM   812  C CZ   . PHE A 1 51  ? 17.273 22.408 30.459 1.00 24.99  ? 54  PHE A CZ   1 
ATOM   813  H H    . PHE A 1 51  ? 16.682 28.297 33.460 0.00 21.55  ? 54  PHE A H    1 
ATOM   814  H HA   . PHE A 1 51  ? 17.956 27.479 31.365 0.00 20.89  ? 54  PHE A HA   1 
ATOM   815  H HB2  . PHE A 1 51  ? 18.028 26.089 33.215 0.00 22.82  ? 54  PHE A HB2  1 
ATOM   816  H HB3  . PHE A 1 51  ? 16.443 25.976 33.268 0.00 22.82  ? 54  PHE A HB3  1 
ATOM   817  H HD1  . PHE A 1 51  ? 19.194 24.809 31.294 0.00 30.26  ? 54  PHE A HD1  1 
ATOM   818  H HD2  . PHE A 1 51  ? 15.368 24.296 32.217 0.00 26.46  ? 54  PHE A HD2  1 
ATOM   819  H HE1  . PHE A 1 51  ? 19.186 22.790 30.201 0.00 30.41  ? 54  PHE A HE1  1 
ATOM   820  H HE2  . PHE A 1 51  ? 15.368 22.265 31.037 0.00 30.84  ? 54  PHE A HE2  1 
ATOM   821  H HZ   . PHE A 1 51  ? 17.269 21.641 29.934 0.00 29.99  ? 54  PHE A HZ   1 
ATOM   822  N N    . THR A 1 52  ? 14.768 27.040 31.035 1.00 17.93  ? 55  THR A N    1 
ATOM   823  C CA   . THR A 1 52  ? 13.755 26.759 29.990 1.00 17.93  ? 55  THR A CA   1 
ATOM   824  C C    . THR A 1 52  ? 13.786 27.817 28.916 1.00 18.13  ? 55  THR A C    1 
ATOM   825  O O    . THR A 1 52  ? 13.570 27.500 27.717 1.00 18.25  ? 55  THR A O    1 
ATOM   826  C CB   . THR A 1 52  ? 12.346 26.587 30.588 1.00 19.92  ? 55  THR A CB   1 
ATOM   827  O OG1  . THR A 1 52  ? 11.875 27.820 31.094 1.00 22.18  ? 55  THR A OG1  1 
ATOM   828  C CG2  . THR A 1 52  ? 12.408 25.476 31.649 1.00 22.38  ? 55  THR A CG2  1 
ATOM   829  H H    . THR A 1 52  ? 14.452 27.165 31.825 0.00 21.52  ? 55  THR A H    1 
ATOM   830  H HA   . THR A 1 52  ? 13.968 25.907 29.579 0.00 21.52  ? 55  THR A HA   1 
ATOM   831  H HB   . THR A 1 52  ? 11.697 26.317 29.920 0.00 23.91  ? 55  THR A HB   1 
ATOM   832  H HG1  . THR A 1 52  ? 11.110 27.720 31.426 0.00 26.61  ? 55  THR A HG1  1 
ATOM   833  H HG21 . THR A 1 52  ? 11.512 25.250 31.945 0.00 26.86  ? 55  THR A HG21 1 
ATOM   834  H HG22 . THR A 1 52  ? 12.826 24.684 31.277 0.00 26.86  ? 55  THR A HG22 1 
ATOM   835  H HG23 . THR A 1 52  ? 12.925 25.776 32.413 0.00 26.86  ? 55  THR A HG23 1 
ATOM   836  N N    . MET A 1 53  ? 13.951 29.128 29.239 1.00 16.60  ? 56  MET A N    1 
ATOM   837  C CA   . MET A 1 53  ? 13.916 30.139 28.243 1.00 16.49  ? 56  MET A CA   1 
ATOM   838  C C    . MET A 1 53  ? 15.162 30.181 27.436 1.00 17.80  ? 56  MET A C    1 
ATOM   839  O O    . MET A 1 53  ? 15.058 30.483 26.230 1.00 17.67  ? 56  MET A O    1 
ATOM   840  C CB   . MET A 1 53  ? 13.531 31.474 28.979 1.00 18.43  ? 56  MET A CB   1 
ATOM   841  C CG   . MET A 1 53  ? 12.069 31.558 29.438 1.00 25.41  ? 56  MET A CG   1 
ATOM   842  S SD   . MET A 1 53  ? 10.805 31.267 28.169 1.00 25.51  ? 56  MET A SD   1 
ATOM   843  C CE   . MET A 1 53  ? 10.697 29.420 28.141 1.00 26.76  ? 56  MET A CE   1 
ATOM   844  H H    . MET A 1 53  ? 14.082 29.423 30.036 0.00 19.92  ? 56  MET A H    1 
ATOM   845  H HA   . MET A 1 53  ? 13.230 29.979 27.575 0.00 19.79  ? 56  MET A HA   1 
ATOM   846  H HB2  . MET A 1 53  ? 14.090 31.563 29.767 0.00 22.12  ? 56  MET A HB2  1 
ATOM   847  H HB3  . MET A 1 53  ? 13.690 32.216 28.375 0.00 22.12  ? 56  MET A HB3  1 
ATOM   848  H HG2  . MET A 1 53  ? 11.932 30.894 30.132 0.00 30.49  ? 56  MET A HG2  1 
ATOM   849  H HG3  . MET A 1 53  ? 11.915 32.447 29.794 0.00 30.49  ? 56  MET A HG3  1 
ATOM   850  H HE1  . MET A 1 53  ? 10.006 29.154 27.514 0.00 32.12  ? 56  MET A HE1  1 
ATOM   851  H HE2  . MET A 1 53  ? 11.552 29.058 27.863 0.00 32.12  ? 56  MET A HE2  1 
ATOM   852  H HE3  . MET A 1 53  ? 10.476 29.103 29.030 0.00 32.12  ? 56  MET A HE3  1 
ATOM   853  N N    . TYR A 1 54  ? 16.341 29.974 28.043 1.00 17.88  ? 57  TYR A N    1 
ATOM   854  C CA   . TYR A 1 54  ? 17.545 29.819 27.214 1.00 17.98  ? 57  TYR A CA   1 
ATOM   855  C C    . TYR A 1 54  ? 17.365 28.657 26.282 1.00 18.22  ? 57  TYR A C    1 
ATOM   856  O O    . TYR A 1 54  ? 17.752 28.815 25.096 1.00 18.00  ? 57  TYR A O    1 
ATOM   857  C CB   . TYR A 1 54  ? 18.765 29.602 28.136 1.00 17.06  ? 57  TYR A CB   1 
ATOM   858  C CG   . TYR A 1 54  ? 19.446 30.911 28.418 1.00 17.61  ? 57  TYR A CG   1 
ATOM   859  C CD1  . TYR A 1 54  ? 19.111 31.778 29.467 1.00 18.18  ? 57  TYR A CD1  1 
ATOM   860  C CD2  . TYR A 1 54  ? 20.485 31.362 27.590 1.00 20.29  ? 57  TYR A CD2  1 
ATOM   861  C CE1  . TYR A 1 54  ? 19.724 33.063 29.615 1.00 19.28  ? 57  TYR A CE1  1 
ATOM   862  C CE2  . TYR A 1 54  ? 21.121 32.598 27.761 1.00 19.86  ? 57  TYR A CE2  1 
ATOM   863  C CZ   . TYR A 1 54  ? 20.752 33.449 28.739 1.00 17.77  ? 57  TYR A CZ   1 
ATOM   864  O OH   . TYR A 1 54  ? 21.282 34.727 28.933 1.00 20.14  ? 57  TYR A OH   1 
ATOM   865  H H    . TYR A 1 54  ? 16.465 29.923 28.893 0.00 21.45  ? 57  TYR A H    1 
ATOM   866  H HA   . TYR A 1 54  ? 17.705 30.617 26.687 0.00 21.58  ? 57  TYR A HA   1 
ATOM   867  H HB2  . TYR A 1 54  ? 18.473 29.217 28.977 0.00 20.48  ? 57  TYR A HB2  1 
ATOM   868  H HB3  . TYR A 1 54  ? 19.399 29.009 27.702 0.00 20.48  ? 57  TYR A HB3  1 
ATOM   869  H HD1  . TYR A 1 54  ? 18.470 31.510 30.086 0.00 21.81  ? 57  TYR A HD1  1 
ATOM   870  H HD2  . TYR A 1 54  ? 20.765 30.814 26.893 0.00 24.34  ? 57  TYR A HD2  1 
ATOM   871  H HE1  . TYR A 1 54  ? 19.442 33.640 30.288 0.00 23.13  ? 57  TYR A HE1  1 
ATOM   872  H HE2  . TYR A 1 54  ? 21.813 32.836 27.188 0.00 23.84  ? 57  TYR A HE2  1 
ATOM   873  H HH   . TYR A 1 54  ? 20.936 35.082 29.611 0.00 24.16  ? 57  TYR A HH   1 
ATOM   874  N N    . LEU A 1 55  ? 16.815 27.537 26.711 1.00 18.04  ? 58  LEU A N    1 
ATOM   875  C CA   . LEU A 1 55  ? 16.684 26.424 25.761 1.00 16.79  ? 58  LEU A CA   1 
ATOM   876  C C    . LEU A 1 55  ? 15.735 26.838 24.639 1.00 18.26  ? 58  LEU A C    1 
ATOM   877  O O    . LEU A 1 55  ? 15.983 26.481 23.447 1.00 18.89  ? 58  LEU A O    1 
ATOM   878  C CB   . LEU A 1 55  ? 16.206 25.175 26.521 1.00 18.67  ? 58  LEU A CB   1 
ATOM   879  C CG   . LEU A 1 55  ? 15.952 23.971 25.648 1.00 18.65  ? 58  LEU A CG   1 
ATOM   880  C CD1  . LEU A 1 55  ? 17.294 23.446 25.082 1.00 24.00  ? 58  LEU A CD1  1 
ATOM   881  C CD2  . LEU A 1 55  ? 15.380 22.894 26.508 1.00 21.62  ? 58  LEU A CD2  1 
ATOM   882  H H    . LEU A 1 55  ? 16.521 27.392 27.506 0.00 21.65  ? 58  LEU A H    1 
ATOM   883  H HA   . LEU A 1 55  ? 17.534 26.191 25.356 0.00 20.15  ? 58  LEU A HA   1 
ATOM   884  H HB2  . LEU A 1 55  ? 16.885 24.930 27.169 0.00 22.40  ? 58  LEU A HB2  1 
ATOM   885  H HB3  . LEU A 1 55  ? 15.376 25.389 26.975 0.00 22.40  ? 58  LEU A HB3  1 
ATOM   886  H HG   . LEU A 1 55  ? 15.354 24.204 24.920 0.00 22.38  ? 58  LEU A HG   1 
ATOM   887  H HD11 . LEU A 1 55  ? 17.130 22.624 24.593 0.00 28.80  ? 58  LEU A HD11 1 
ATOM   888  H HD12 . LEU A 1 55  ? 17.669 24.115 24.488 0.00 28.80  ? 58  LEU A HD12 1 
ATOM   889  H HD13 . LEU A 1 55  ? 17.903 23.277 25.818 0.00 28.80  ? 58  LEU A HD13 1 
ATOM   890  H HD21 . LEU A 1 55  ? 15.239 22.100 25.968 0.00 25.95  ? 58  LEU A HD21 1 
ATOM   891  H HD22 . LEU A 1 55  ? 16.002 22.699 27.226 0.00 25.95  ? 58  LEU A HD22 1 
ATOM   892  H HD23 . LEU A 1 55  ? 14.535 23.198 26.875 0.00 25.95  ? 58  LEU A HD23 1 
ATOM   893  N N    . SER A 1 56  ? 14.654 27.578 24.929 1.00 16.33  ? 59  SER A N    1 
ATOM   894  C CA   . SER A 1 56  ? 13.760 27.978 23.859 1.00 16.95  ? 59  SER A CA   1 
ATOM   895  C C    . SER A 1 56  ? 14.410 28.902 22.863 1.00 19.93  ? 59  SER A C    1 
ATOM   896  O O    . SER A 1 56  ? 14.108 28.834 21.679 1.00 19.99  ? 59  SER A O    1 
ATOM   897  C CB   . SER A 1 56  ? 12.537 28.664 24.490 1.00 20.51  ? 59  SER A CB   1 
ATOM   898  O OG   . SER A 1 56  ? 12.732 30.038 24.718 1.00 24.06  ? 59  SER A OG   1 
ATOM   899  H H    . SER A 1 56  ? 14.431 27.848 25.715 0.00 19.59  ? 59  SER A H    1 
ATOM   900  H HA   . SER A 1 56  ? 13.485 27.188 23.367 0.00 20.34  ? 59  SER A HA   1 
ATOM   901  H HB2  . SER A 1 56  ? 11.782 28.557 23.890 0.00 24.61  ? 59  SER A HB2  1 
ATOM   902  H HB3  . SER A 1 56  ? 12.349 28.235 25.339 0.00 24.61  ? 59  SER A HB3  1 
ATOM   903  H HG   . SER A 1 56  ? 13.368 30.152 25.255 0.00 28.88  ? 59  SER A HG   1 
ATOM   904  N N    . MET A 1 57  ? 15.386 29.719 23.293 1.00 18.01  ? 60  MET A N    1 
ATOM   905  C CA   . MET A 1 57  ? 16.124 30.558 22.321 1.00 18.38  ? 60  MET A CA   1 
ATOM   906  C C    . MET A 1 57  ? 17.119 29.722 21.541 1.00 18.30  ? 60  MET A C    1 
ATOM   907  O O    . MET A 1 57  ? 17.166 29.923 20.283 1.00 20.70  ? 60  MET A O    1 
ATOM   908  C CB   . MET A 1 57  ? 16.856 31.655 23.124 1.00 19.16  ? 60  MET A CB   1 
ATOM   909  C CG   . MET A 1 57  ? 15.857 32.589 23.791 1.00 18.09  ? 60  MET A CG   1 
ATOM   910  S SD   . MET A 1 57  ? 16.692 34.131 24.411 1.00 22.79  ? 60  MET A SD   1 
ATOM   911  C CE   . MET A 1 57  ? 17.256 33.589 25.928 1.00 23.69  ? 60  MET A CE   1 
ATOM   912  H H    . MET A 1 57  ? 15.635 29.807 24.111 0.00 21.61  ? 60  MET A H    1 
ATOM   913  H HA   . MET A 1 57  ? 15.513 30.969 21.690 0.00 22.05  ? 60  MET A HA   1 
ATOM   914  H HB2  . MET A 1 57  ? 17.401 31.243 23.812 0.00 22.99  ? 60  MET A HB2  1 
ATOM   915  H HB3  . MET A 1 57  ? 17.415 32.176 22.525 0.00 22.99  ? 60  MET A HB3  1 
ATOM   916  H HG2  . MET A 1 57  ? 15.176 32.846 23.149 0.00 21.71  ? 60  MET A HG2  1 
ATOM   917  H HG3  . MET A 1 57  ? 15.447 32.138 24.545 0.00 21.71  ? 60  MET A HG3  1 
ATOM   918  H HE1  . MET A 1 57  ? 17.666 34.333 26.396 0.00 28.43  ? 60  MET A HE1  1 
ATOM   919  H HE2  . MET A 1 57  ? 16.506 33.249 26.440 0.00 28.43  ? 60  MET A HE2  1 
ATOM   920  H HE3  . MET A 1 57  ? 17.908 32.884 25.790 0.00 28.43  ? 60  MET A HE3  1 
ATOM   921  N N    . LEU A 1 58  ? 17.806 28.770 22.148 1.00 19.05  ? 61  LEU A N    1 
ATOM   922  C CA   . LEU A 1 58  ? 18.736 27.884 21.419 1.00 19.03  ? 61  LEU A CA   1 
ATOM   923  C C    . LEU A 1 58  ? 18.008 27.170 20.326 1.00 21.51  ? 61  LEU A C    1 
ATOM   924  O O    . LEU A 1 58  ? 18.538 27.042 19.206 1.00 23.23  ? 61  LEU A O    1 
ATOM   925  C CB   . LEU A 1 58  ? 19.332 26.920 22.496 1.00 21.34  ? 61  LEU A CB   1 
ATOM   926  C CG   . LEU A 1 58  ? 20.264 25.904 21.842 1.00 21.23  ? 61  LEU A CG   1 
ATOM   927  C CD1  . LEU A 1 58  ? 21.516 26.690 21.306 1.00 28.22  ? 61  LEU A CD1  1 
ATOM   928  C CD2  . LEU A 1 58  ? 20.683 24.873 22.864 1.00 26.48  ? 61  LEU A CD2  1 
ATOM   929  H H    . LEU A 1 58  ? 17.761 28.603 22.990 0.00 22.86  ? 61  LEU A H    1 
ATOM   930  H HA   . LEU A 1 58  ? 19.463 28.357 20.986 0.00 22.84  ? 61  LEU A HA   1 
ATOM   931  H HB2  . LEU A 1 58  ? 19.838 27.432 23.146 0.00 25.61  ? 61  LEU A HB2  1 
ATOM   932  H HB3  . LEU A 1 58  ? 18.613 26.442 22.938 0.00 25.61  ? 61  LEU A HB3  1 
ATOM   933  H HG   . LEU A 1 58  ? 19.831 25.438 21.110 0.00 25.48  ? 61  LEU A HG   1 
ATOM   934  H HD11 . LEU A 1 58  ? 22.185 26.054 21.009 0.00 33.87  ? 61  LEU A HD11 1 
ATOM   935  H HD12 . LEU A 1 58  ? 21.243 27.253 20.565 0.00 33.87  ? 61  LEU A HD12 1 
ATOM   936  H HD13 . LEU A 1 58  ? 21.875 27.238 22.022 0.00 33.87  ? 61  LEU A HD13 1 
ATOM   937  H HD21 . LEU A 1 58  ? 21.262 24.222 22.438 0.00 31.78  ? 61  LEU A HD21 1 
ATOM   938  H HD22 . LEU A 1 58  ? 21.158 25.316 23.584 0.00 31.78  ? 61  LEU A HD22 1 
ATOM   939  H HD23 . LEU A 1 58  ? 19.891 24.433 23.212 0.00 31.78  ? 61  LEU A HD23 1 
ATOM   940  N N    . LEU A 1 59  ? 16.790 26.631 20.620 1.00 19.55  ? 62  LEU A N    1 
ATOM   941  C CA   . LEU A 1 59  ? 16.107 25.805 19.587 1.00 19.66  ? 62  LEU A CA   1 
ATOM   942  C C    . LEU A 1 59  ? 15.345 26.669 18.592 1.00 22.22  ? 62  LEU A C    1 
ATOM   943  O O    . LEU A 1 59  ? 14.738 26.087 17.664 1.00 27.71  ? 62  LEU A O    1 
ATOM   944  C CB   . LEU A 1 59  ? 15.120 24.815 20.315 1.00 21.68  ? 62  LEU A CB   1 
ATOM   945  C CG   . LEU A 1 59  ? 15.740 23.876 21.284 1.00 21.35  ? 62  LEU A CG   1 
ATOM   946  C CD1  . LEU A 1 59  ? 14.679 22.917 21.942 1.00 26.76  ? 62  LEU A CD1  1 
ATOM   947  C CD2  . LEU A 1 59  ? 16.821 22.988 20.574 1.00 26.77  ? 62  LEU A CD2  1 
ATOM   948  H H    . LEU A 1 59  ? 16.367 26.725 21.363 0.00 23.46  ? 62  LEU A H    1 
ATOM   949  H HA   . LEU A 1 59  ? 16.750 25.278 19.087 0.00 23.59  ? 62  LEU A HA   1 
ATOM   950  H HB2  . LEU A 1 59  ? 14.468 25.342 20.802 0.00 26.01  ? 62  LEU A HB2  1 
ATOM   951  H HB3  . LEU A 1 59  ? 14.676 24.279 19.639 0.00 26.01  ? 62  LEU A HB3  1 
ATOM   952  H HG   . LEU A 1 59  ? 16.148 24.415 21.980 0.00 25.62  ? 62  LEU A HG   1 
ATOM   953  H HD11 . LEU A 1 59  ? 15.131 22.324 22.563 0.00 32.11  ? 62  LEU A HD11 1 
ATOM   954  H HD12 . LEU A 1 59  ? 14.021 23.450 22.414 0.00 32.11  ? 62  LEU A HD12 1 
ATOM   955  H HD13 . LEU A 1 59  ? 14.247 22.398 21.245 0.00 32.11  ? 62  LEU A HD13 1 
ATOM   956  H HD21 . LEU A 1 59  ? 17.112 22.294 21.186 0.00 32.13  ? 62  LEU A HD21 1 
ATOM   957  H HD22 . LEU A 1 59  ? 16.429 22.586 19.782 0.00 32.13  ? 62  LEU A HD22 1 
ATOM   958  H HD23 . LEU A 1 59  ? 17.573 23.545 20.323 0.00 32.13  ? 62  LEU A HD23 1 
ATOM   959  N N    . GLY A 1 60  ? 15.255 27.971 18.807 1.00 22.36  ? 63  GLY A N    1 
ATOM   960  C CA   . GLY A 1 60  ? 14.658 28.863 17.816 1.00 24.74  ? 63  GLY A CA   1 
ATOM   961  C C    . GLY A 1 60  ? 13.232 29.235 18.125 1.00 24.17  ? 63  GLY A C    1 
ATOM   962  O O    . GLY A 1 60  ? 12.643 30.095 17.403 1.00 27.91  ? 63  GLY A O    1 
ATOM   963  H H    . GLY A 1 60  ? 15.532 28.366 19.519 0.00 26.83  ? 63  GLY A H    1 
ATOM   964  H HA2  . GLY A 1 60  ? 15.179 29.679 17.770 0.00 29.69  ? 63  GLY A HA2  1 
ATOM   965  H HA3  . GLY A 1 60  ? 14.675 28.428 16.949 0.00 29.69  ? 63  GLY A HA3  1 
ATOM   966  N N    . TYR A 1 61  ? 12.617 28.663 19.168 1.00 21.61  ? 64  TYR A N    1 
ATOM   967  C CA   . TYR A 1 61  ? 11.235 28.995 19.450 1.00 21.95  ? 64  TYR A CA   1 
ATOM   968  C C    . TYR A 1 61  ? 11.088 30.391 19.988 1.00 21.77  ? 64  TYR A C    1 
ATOM   969  O O    . TYR A 1 61  ? 10.110 31.073 19.682 1.00 23.96  ? 64  TYR A O    1 
ATOM   970  C CB   . TYR A 1 61  ? 10.658 27.914 20.488 1.00 22.42  ? 64  TYR A CB   1 
ATOM   971  C CG   . TYR A 1 61  ? 9.166  28.105 20.792 1.00 21.79  ? 64  TYR A CG   1 
ATOM   972  C CD1  . TYR A 1 61  ? 8.280  27.506 19.962 1.00 28.05  ? 64  TYR A CD1  1 
ATOM   973  C CD2  . TYR A 1 61  ? 8.782  28.856 21.826 1.00 23.04  ? 64  TYR A CD2  1 
ATOM   974  C CE1  . TYR A 1 61  ? 6.861  27.688 20.159 1.00 32.56  ? 64  TYR A CE1  1 
ATOM   975  C CE2  . TYR A 1 61  ? 7.395  29.027 22.057 1.00 25.17  ? 64  TYR A CE2  1 
ATOM   976  C CZ   . TYR A 1 61  ? 6.516  28.494 21.235 1.00 31.12  ? 64  TYR A CZ   1 
ATOM   977  O OH   . TYR A 1 61  ? 5.126  28.660 21.440 1.00 37.76  ? 64  TYR A OH   1 
ATOM   978  H H    . TYR A 1 61  ? 12.976 28.097 19.707 0.00 25.93  ? 64  TYR A H    1 
ATOM   979  H HA   . TYR A 1 61  ? 10.713 28.957 18.633 0.00 26.34  ? 64  TYR A HA   1 
ATOM   980  H HB2  . TYR A 1 61  ? 10.775 27.027 20.114 0.00 26.91  ? 64  TYR A HB2  1 
ATOM   981  H HB3  . TYR A 1 61  ? 11.146 27.990 21.323 0.00 26.91  ? 64  TYR A HB3  1 
ATOM   982  H HD1  . TYR A 1 61  ? 8.586  26.975 19.262 0.00 33.66  ? 64  TYR A HD1  1 
ATOM   983  H HD2  . TYR A 1 61  ? 9.411  29.257 22.382 0.00 27.65  ? 64  TYR A HD2  1 
ATOM   984  H HE1  . TYR A 1 61  ? 6.225  27.295 19.606 0.00 39.08  ? 64  TYR A HE1  1 
ATOM   985  H HE2  . TYR A 1 61  ? 7.105  29.518 22.792 0.00 30.20  ? 64  TYR A HE2  1 
ATOM   986  H HH   . TYR A 1 61  ? 4.989  29.090 22.149 0.00 45.32  ? 64  TYR A HH   1 
ATOM   987  N N    . GLY A 1 62  ? 12.022 30.823 20.726 1.00 20.38  ? 65  GLY A N    1 
ATOM   988  C CA   . GLY A 1 62  ? 11.928 32.101 21.499 1.00 21.81  ? 65  GLY A CA   1 
ATOM   989  C C    . GLY A 1 62  ? 12.428 33.282 20.675 1.00 21.15  ? 65  GLY A C    1 
ATOM   990  O O    . GLY A 1 62  ? 12.798 34.272 21.308 1.00 21.46  ? 65  GLY A O    1 
ATOM   991  H H    . GLY A 1 62  ? 12.771 30.416 20.835 0.00 24.46  ? 65  GLY A H    1 
ATOM   992  H HA2  . GLY A 1 62  ? 11.005 32.265 21.747 0.00 26.17  ? 65  GLY A HA2  1 
ATOM   993  H HA3  . GLY A 1 62  ? 12.465 32.035 22.304 0.00 26.17  ? 65  GLY A HA3  1 
ATOM   994  N N    . LEU A 1 63  ? 12.456 33.170 19.311 1.00 24.41  ? 66  LEU A N    1 
ATOM   995  C CA   . LEU A 1 63  ? 12.931 34.249 18.420 1.00 23.07  ? 66  LEU A CA   1 
ATOM   996  C C    . LEU A 1 63  ? 11.790 34.638 17.529 1.00 27.67  ? 66  LEU A C    1 
ATOM   997  O O    . LEU A 1 63  ? 11.035 33.758 17.042 1.00 29.41  ? 66  LEU A O    1 
ATOM   998  C CB   . LEU A 1 63  ? 14.087 33.688 17.602 1.00 27.30  ? 66  LEU A CB   1 
ATOM   999  C CG   . LEU A 1 63  ? 14.701 34.542 16.529 1.00 25.19  ? 66  LEU A CG   1 
ATOM   1000 C CD1  . LEU A 1 63  ? 15.428 35.736 17.106 1.00 31.40  ? 66  LEU A CD1  1 
ATOM   1001 C CD2  . LEU A 1 63  ? 15.715 33.682 15.827 1.00 35.29  ? 66  LEU A CD2  1 
ATOM   1002 H H    . LEU A 1 63  ? 12.200 32.467 18.886 0.00 29.29  ? 66  LEU A H    1 
ATOM   1003 H HA   . LEU A 1 63  ? 13.223 35.042 18.895 0.00 27.69  ? 66  LEU A HA   1 
ATOM   1004 H HB2  . LEU A 1 63  ? 14.801 33.468 18.220 0.00 32.76  ? 66  LEU A HB2  1 
ATOM   1005 H HB3  . LEU A 1 63  ? 13.769 32.883 17.163 0.00 32.76  ? 66  LEU A HB3  1 
ATOM   1006 H HG   . LEU A 1 63  ? 14.009 34.875 15.936 0.00 30.23  ? 66  LEU A HG   1 
ATOM   1007 H HD11 . LEU A 1 63  ? 15.832 36.239 16.382 0.00 37.68  ? 66  LEU A HD11 1 
ATOM   1008 H HD12 . LEU A 1 63  ? 14.792 36.293 17.582 0.00 37.68  ? 66  LEU A HD12 1 
ATOM   1009 H HD13 . LEU A 1 63  ? 16.114 35.423 17.716 0.00 37.68  ? 66  LEU A HD13 1 
ATOM   1010 H HD21 . LEU A 1 63  ? 16.138 34.202 15.127 0.00 42.34  ? 66  LEU A HD21 1 
ATOM   1011 H HD22 . LEU A 1 63  ? 16.380 33.390 16.470 0.00 42.34  ? 66  LEU A HD22 1 
ATOM   1012 H HD23 . LEU A 1 63  ? 15.265 32.913 15.443 0.00 42.34  ? 66  LEU A HD23 1 
ATOM   1013 N N    . THR A 1 64  ? 11.606 35.953 17.257 1.00 23.78  ? 67  THR A N    1 
ATOM   1014 C CA   . THR A 1 64  ? 10.697 36.406 16.210 1.00 23.89  ? 67  THR A CA   1 
ATOM   1015 C C    . THR A 1 64  ? 11.388 37.475 15.385 1.00 25.27  ? 67  THR A C    1 
ATOM   1016 O O    . THR A 1 64  ? 12.436 37.987 15.810 1.00 28.98  ? 67  THR A O    1 
ATOM   1017 C CB   . THR A 1 64  ? 9.380  36.932 16.849 1.00 26.47  ? 67  THR A CB   1 
ATOM   1018 O OG1  . THR A 1 64  ? 8.392  36.964 15.835 1.00 31.95  ? 67  THR A OG1  1 
ATOM   1019 C CG2  . THR A 1 64  ? 9.583  38.303 17.626 1.00 27.19  ? 67  THR A CG2  1 
ATOM   1020 H H    . THR A 1 64  ? 12.004 36.592 17.673 0.00 28.54  ? 67  THR A H    1 
ATOM   1021 H HA   . THR A 1 64  ? 10.474 35.682 15.604 0.00 28.67  ? 67  THR A HA   1 
ATOM   1022 H HB   . THR A 1 64  ? 9.064  36.343 17.552 0.00 31.76  ? 67  THR A HB   1 
ATOM   1023 H HG1  . THR A 1 64  ? 7.697  37.338 16.123 0.00 38.35  ? 67  THR A HG1  1 
ATOM   1024 H HG21 . THR A 1 64  ? 8.749  38.580 18.035 0.00 32.62  ? 67  THR A HG21 1 
ATOM   1025 H HG22 . THR A 1 64  ? 10.253 38.195 18.319 0.00 32.62  ? 67  THR A HG22 1 
ATOM   1026 H HG23 . THR A 1 64  ? 9.876  38.993 17.010 0.00 32.62  ? 67  THR A HG23 1 
ATOM   1027 N N    . MET A 1 65  ? 10.844 37.855 14.232 1.00 28.11  ? 68  MET A N    1 
ATOM   1028 C CA   . MET A 1 65  ? 11.423 38.930 13.422 1.00 30.62  ? 68  MET A CA   1 
ATOM   1029 C C    . MET A 1 65  ? 10.496 40.138 13.503 1.00 35.77  ? 68  MET A C    1 
ATOM   1030 O O    . MET A 1 65  ? 9.279  39.993 13.317 1.00 36.46  ? 68  MET A O    1 
ATOM   1031 C CB   . MET A 1 65  ? 11.483 38.493 11.968 1.00 34.07  ? 68  MET A CB   1 
ATOM   1032 C CG   . MET A 1 65  ? 12.439 37.312 11.656 1.00 42.72  ? 68  MET A CG   1 
ATOM   1033 S SD   . MET A 1 65  ? 14.157 37.672 12.135 1.00 46.74  ? 68  MET A SD   1 
ATOM   1034 C CE   . MET A 1 65  ? 14.960 36.052 12.161 1.00 60.94  ? 68  MET A CE   1 
ATOM   1035 H H    . MET A 1 65  ? 10.135 37.505 13.895 0.00 33.73  ? 68  MET A H    1 
ATOM   1036 H HA   . MET A 1 65  ? 12.311 39.150 13.745 0.00 36.74  ? 68  MET A HA   1 
ATOM   1037 H HB2  . MET A 1 65  ? 10.592 38.221 11.696 0.00 40.88  ? 68  MET A HB2  1 
ATOM   1038 H HB3  . MET A 1 65  ? 11.776 39.248 11.435 0.00 40.88  ? 68  MET A HB3  1 
ATOM   1039 H HG2  . MET A 1 65  ? 12.146 36.528 12.146 0.00 51.26  ? 68  MET A HG2  1 
ATOM   1040 H HG3  . MET A 1 65  ? 12.422 37.133 10.703 0.00 51.26  ? 68  MET A HG3  1 
ATOM   1041 H HE1  . MET A 1 65  ? 15.887 36.164 12.423 0.00 73.13  ? 68  MET A HE1  1 
ATOM   1042 H HE2  . MET A 1 65  ? 14.502 35.483 12.799 0.00 73.13  ? 68  MET A HE2  1 
ATOM   1043 H HE3  . MET A 1 65  ? 14.912 35.661 11.275 0.00 73.13  ? 68  MET A HE3  1 
ATOM   1044 N N    . VAL A 1 66  ? 11.048 41.313 13.794 1.00 30.72  ? 69  VAL A N    1 
ATOM   1045 C CA   . VAL A 1 66  ? 10.251 42.541 13.936 1.00 28.32  ? 69  VAL A CA   1 
ATOM   1046 C C    . VAL A 1 66  ? 10.761 43.485 12.876 1.00 32.57  ? 69  VAL A C    1 
ATOM   1047 O O    . VAL A 1 66  ? 11.961 43.759 12.836 1.00 33.92  ? 69  VAL A O    1 
ATOM   1048 C CB   . VAL A 1 66  ? 10.390 43.162 15.339 1.00 29.01  ? 69  VAL A CB   1 
ATOM   1049 C CG1  . VAL A 1 66  ? 9.526  44.462 15.362 1.00 37.31  ? 69  VAL A CG1  1 
ATOM   1050 C CG2  . VAL A 1 66  ? 9.940  42.203 16.450 1.00 29.93  ? 69  VAL A CG2  1 
ATOM   1051 H H    . VAL A 1 66  ? 11.892 41.429 13.917 0.00 36.87  ? 69  VAL A H    1 
ATOM   1052 H HA   . VAL A 1 66  ? 9.308  42.369 13.782 0.00 33.98  ? 69  VAL A HA   1 
ATOM   1053 H HB   . VAL A 1 66  ? 11.323 43.359 15.516 0.00 34.81  ? 69  VAL A HB   1 
ATOM   1054 H HG11 . VAL A 1 66  ? 9.452  44.776 16.277 0.00 44.77  ? 69  VAL A HG11 1 
ATOM   1055 H HG12 . VAL A 1 66  ? 9.956  45.137 14.815 0.00 44.77  ? 69  VAL A HG12 1 
ATOM   1056 H HG13 . VAL A 1 66  ? 8.645  44.261 15.009 0.00 44.77  ? 69  VAL A HG13 1 
ATOM   1057 H HG21 . VAL A 1 66  ? 10.057 42.638 17.309 0.00 35.91  ? 69  VAL A HG21 1 
ATOM   1058 H HG22 . VAL A 1 66  ? 9.005  41.981 16.316 0.00 35.91  ? 69  VAL A HG22 1 
ATOM   1059 H HG23 . VAL A 1 66  ? 10.480 41.398 16.411 0.00 35.91  ? 69  VAL A HG23 1 
ATOM   1060 N N    . PRO A 1 67  ? 9.897  44.042 12.017 1.00 34.29  ? 70  PRO A N    1 
ATOM   1061 C CA   . PRO A 1 67  ? 10.342 44.988 11.014 1.00 34.42  ? 70  PRO A CA   1 
ATOM   1062 C C    . PRO A 1 67  ? 10.450 46.366 11.657 1.00 48.30  ? 70  PRO A C    1 
ATOM   1063 O O    . PRO A 1 67  ? 9.502  46.845 12.262 1.00 49.36  ? 70  PRO A O    1 
ATOM   1064 C CB   . PRO A 1 67  ? 9.226  44.947 9.974  1.00 39.93  ? 70  PRO A CB   1 
ATOM   1065 C CG   . PRO A 1 67  ? 7.997  44.592 10.795 1.00 40.39  ? 70  PRO A CG   1 
ATOM   1066 C CD   . PRO A 1 67  ? 8.475  43.669 11.881 1.00 35.06  ? 70  PRO A CD   1 
ATOM   1067 H HA   . PRO A 1 67  ? 11.181 44.723 10.606 0.00 41.30  ? 70  PRO A HA   1 
ATOM   1068 H HB2  . PRO A 1 67  ? 9.129  45.814 9.550  0.00 47.92  ? 70  PRO A HB2  1 
ATOM   1069 H HB3  . PRO A 1 67  ? 9.413  44.269 9.306  0.00 47.92  ? 70  PRO A HB3  1 
ATOM   1070 H HG2  . PRO A 1 67  ? 7.613  45.398 11.174 0.00 48.47  ? 70  PRO A HG2  1 
ATOM   1071 H HG3  . PRO A 1 67  ? 7.345  44.148 10.230 0.00 48.47  ? 70  PRO A HG3  1 
ATOM   1072 H HD2  . PRO A 1 67  ? 7.993  43.826 12.708 0.00 42.08  ? 70  PRO A HD2  1 
ATOM   1073 H HD3  . PRO A 1 67  ? 8.383  42.741 11.615 0.00 42.08  ? 70  PRO A HD3  1 
ATOM   1074 N N    . PHE A 1 68  ? 11.640 46.953 11.605 1.00 38.74  ? 71  PHE A N    1 
ATOM   1075 C CA   . PHE A 1 68  ? 11.805 48.375 11.927 1.00 39.24  ? 71  PHE A CA   1 
ATOM   1076 C C    . PHE A 1 68  ? 13.062 48.831 11.198 1.00 43.56  ? 71  PHE A C    1 
ATOM   1077 O O    . PHE A 1 68  ? 13.951 48.030 10.868 1.00 49.55  ? 71  PHE A O    1 
ATOM   1078 C CB   . PHE A 1 68  ? 11.781 48.694 13.416 1.00 45.17  ? 71  PHE A CB   1 
ATOM   1079 C CG   . PHE A 1 68  ? 12.841 48.004 14.236 1.00 40.11  ? 71  PHE A CG   1 
ATOM   1080 C CD1  . PHE A 1 68  ? 14.146 48.529 14.290 1.00 42.76  ? 71  PHE A CD1  1 
ATOM   1081 C CD2  . PHE A 1 68  ? 12.545 46.905 14.923 1.00 31.80  ? 71  PHE A CD2  1 
ATOM   1082 C CE1  . PHE A 1 68  ? 15.094 47.919 15.092 1.00 39.61  ? 71  PHE A CE1  1 
ATOM   1083 C CE2  . PHE A 1 68  ? 13.503 46.254 15.707 1.00 35.37  ? 71  PHE A CE2  1 
ATOM   1084 C CZ   . PHE A 1 68  ? 14.815 46.805 15.764 1.00 38.48  ? 71  PHE A CZ   1 
ATOM   1085 H H    . PHE A 1 68  ? 12.370 46.554 11.388 0.00 46.49  ? 71  PHE A H    1 
ATOM   1086 H HA   . PHE A 1 68  ? 11.054 48.890 11.593 0.00 47.09  ? 71  PHE A HA   1 
ATOM   1087 H HB2  . PHE A 1 68  ? 11.906 49.650 13.527 0.00 54.20  ? 71  PHE A HB2  1 
ATOM   1088 H HB3  . PHE A 1 68  ? 10.919 48.429 13.773 0.00 54.20  ? 71  PHE A HB3  1 
ATOM   1089 H HD1  . PHE A 1 68  ? 14.369 49.282 13.791 0.00 51.31  ? 71  PHE A HD1  1 
ATOM   1090 H HD2  . PHE A 1 68  ? 11.682 46.562 14.881 0.00 38.17  ? 71  PHE A HD2  1 
ATOM   1091 H HE1  . PHE A 1 68  ? 15.942 48.294 15.162 0.00 47.53  ? 71  PHE A HE1  1 
ATOM   1092 H HE2  . PHE A 1 68  ? 13.288 45.482 16.179 0.00 42.45  ? 71  PHE A HE2  1 
ATOM   1093 H HZ   . PHE A 1 68  ? 15.474 46.388 16.270 0.00 46.17  ? 71  PHE A HZ   1 
ATOM   1094 N N    . GLY A 1 69  ? 13.121 50.126 10.927 1.00 57.86  ? 72  GLY A N    1 
ATOM   1095 C CA   . GLY A 1 69  ? 14.267 50.625 10.200 1.00 52.00  ? 72  GLY A CA   1 
ATOM   1096 C C    . GLY A 1 69  ? 14.474 49.965 8.856  1.00 62.95  ? 72  GLY A C    1 
ATOM   1097 O O    . GLY A 1 69  ? 15.617 49.860 8.379  1.00 58.57  ? 72  GLY A O    1 
ATOM   1098 H H    . GLY A 1 69  ? 12.531 50.713 11.145 0.00 69.44  ? 72  GLY A H    1 
ATOM   1099 H HA2  . GLY A 1 69  ? 14.157 51.577 10.053 0.00 62.40  ? 72  GLY A HA2  1 
ATOM   1100 H HA3  . GLY A 1 69  ? 15.065 50.477 10.732 0.00 62.40  ? 72  GLY A HA3  1 
ATOM   1101 N N    . GLY A 1 70  ? 13.402 49.503 8.228  1.00 51.82  ? 73  GLY A N    1 
ATOM   1102 C CA   . GLY A 1 70  ? 13.539 48.973 6.903  1.00 49.59  ? 73  GLY A CA   1 
ATOM   1103 C C    . GLY A 1 70  ? 14.167 47.616 6.815  1.00 59.41  ? 73  GLY A C    1 
ATOM   1104 O O    . GLY A 1 70  ? 14.470 47.164 5.705  1.00 67.35  ? 73  GLY A O    1 
ATOM   1105 H H    . GLY A 1 70  ? 12.604 49.489 8.549  0.00 62.19  ? 73  GLY A H    1 
ATOM   1106 H HA2  . GLY A 1 70  ? 12.658 48.915 6.501  0.00 59.51  ? 73  GLY A HA2  1 
ATOM   1107 H HA3  . GLY A 1 70  ? 14.084 49.583 6.382  0.00 59.51  ? 73  GLY A HA3  1 
ATOM   1108 N N    . GLU A 1 71  ? 14.344 46.946 7.940  1.00 49.86  ? 74  GLU A N    1 
ATOM   1109 C CA   . GLU A 1 71  ? 14.947 45.624 7.983  1.00 49.83  ? 74  GLU A CA   1 
ATOM   1110 C C    . GLU A 1 71  ? 14.000 44.696 8.717  1.00 42.66  ? 74  GLU A C    1 
ATOM   1111 O O    . GLU A 1 71  ? 13.098 45.140 9.427  1.00 47.80  ? 74  GLU A O    1 
ATOM   1112 C CB   . GLU A 1 71  ? 16.260 45.661 8.761  1.00 50.92  ? 74  GLU A CB   1 
ATOM   1113 C CG   . GLU A 1 71  ? 17.201 46.779 8.303  1.00 61.79  ? 74  GLU A CG   1 
ATOM   1114 C CD   . GLU A 1 71  ? 18.639 46.539 8.714  1.00 83.39  ? 74  GLU A CD   1 
ATOM   1115 O OE1  . GLU A 1 71  ? 18.884 45.550 9.455  1.00 86.10  ? 74  GLU A OE1  1 
ATOM   1116 O OE2  . GLU A 1 71  ? 19.515 47.351 8.320  1.00 89.10  ? 74  GLU A OE2  1 
ATOM   1117 H H    . GLU A 1 71  ? 14.116 47.244 8.714  0.00 59.83  ? 74  GLU A H    1 
ATOM   1118 H HA   . GLU A 1 71  ? 15.104 45.300 7.082  0.00 59.80  ? 74  GLU A HA   1 
ATOM   1119 N N    . GLN A 1 72  ? 14.225 43.385 8.556  1.00 38.99  ? 75  GLN A N    1 
ATOM   1120 C CA   . GLN A 1 72  ? 13.617 42.417 9.491  1.00 35.01  ? 75  GLN A CA   1 
ATOM   1121 C C    . GLN A 1 72  ? 14.611 42.102 10.597 1.00 37.89  ? 75  GLN A C    1 
ATOM   1122 O O    . GLN A 1 72  ? 15.693 41.547 10.347 1.00 46.71  ? 75  GLN A O    1 
ATOM   1123 C CB   . GLN A 1 72  ? 13.213 41.149 8.747  1.00 49.50  ? 75  GLN A CB   1 
ATOM   1124 C CG   . GLN A 1 72  ? 12.489 41.453 7.455  1.00 66.69  ? 75  GLN A CG   1 
ATOM   1125 C CD   . GLN A 1 72  ? 11.026 41.785 7.685  1.00 60.81  ? 75  GLN A CD   1 
ATOM   1126 O OE1  . GLN A 1 72  ? 10.428 41.375 8.690  1.00 62.15  ? 75  GLN A OE1  1 
ATOM   1127 N NE2  . GLN A 1 72  ? 10.449 42.571 6.768  1.00 71.07  ? 75  GLN A NE2  1 
ATOM   1128 H H    . GLN A 1 72  ? 14.709 43.040 7.934  0.00 46.79  ? 75  GLN A H    1 
ATOM   1129 H HA   . GLN A 1 72  ? 12.824 42.802 9.896  0.00 42.01  ? 75  GLN A HA   1 
ATOM   1130 H HB2  . GLN A 1 72  ? 14.009 40.637 8.535  0.00 59.40  ? 75  GLN A HB2  1 
ATOM   1131 H HB3  . GLN A 1 72  ? 12.621 40.625 9.310  0.00 59.40  ? 75  GLN A HB3  1 
ATOM   1132 H HG2  . GLN A 1 72  ? 12.909 42.215 7.026  0.00 80.03  ? 75  GLN A HG2  1 
ATOM   1133 H HG3  . GLN A 1 72  ? 12.535 40.677 6.874  0.00 80.03  ? 75  GLN A HG3  1 
ATOM   1134 H HE21 . GLN A 1 72  ? 10.905 42.856 6.097  0.00 85.28  ? 75  GLN A HE21 1 
ATOM   1135 H HE22 . GLN A 1 72  ? 9.621  42.791 6.849  0.00 85.28  ? 75  GLN A HE22 1 
ATOM   1136 N N    . ASN A 1 73  ? 14.274 42.467 11.820 1.00 30.85  ? 76  ASN A N    1 
ATOM   1137 C CA   . ASN A 1 73  ? 15.276 42.349 12.840 1.00 29.91  ? 76  ASN A CA   1 
ATOM   1138 C C    . ASN A 1 73  ? 14.971 41.170 13.762 1.00 29.11  ? 76  ASN A C    1 
ATOM   1139 O O    . ASN A 1 73  ? 13.868 41.029 14.283 1.00 27.43  ? 76  ASN A O    1 
ATOM   1140 C CB   . ASN A 1 73  ? 15.252 43.633 13.716 1.00 33.31  ? 76  ASN A CB   1 
ATOM   1141 C CG   . ASN A 1 73  ? 15.558 44.870 12.937 1.00 35.50  ? 76  ASN A CG   1 
ATOM   1142 O OD1  . ASN A 1 73  ? 16.737 45.190 12.732 1.00 44.19  ? 76  ASN A OD1  1 
ATOM   1143 N ND2  . ASN A 1 73  ? 14.527 45.496 12.356 1.00 36.69  ? 76  ASN A ND2  1 
ATOM   1144 H H    . ASN A 1 73  ? 13.507 42.771 12.065 0.00 37.02  ? 76  ASN A H    1 
ATOM   1145 H HA   . ASN A 1 73  ? 16.148 42.218 12.436 0.00 35.89  ? 76  ASN A HA   1 
ATOM   1146 H HB2  . ASN A 1 73  ? 14.369 43.734 14.105 0.00 39.97  ? 76  ASN A HB2  1 
ATOM   1147 H HB3  . ASN A 1 73  ? 15.916 43.550 14.419 0.00 39.97  ? 76  ASN A HB3  1 
ATOM   1148 H HD21 . ASN A 1 73  ? 14.661 46.212 11.898 0.00 44.03  ? 76  ASN A HD21 1 
ATOM   1149 H HD22 . ASN A 1 73  ? 13.731 45.183 12.441 0.00 44.03  ? 76  ASN A HD22 1 
ATOM   1150 N N    . PRO A 1 74  ? 15.969 40.371 14.171 1.00 28.38  ? 77  PRO A N    1 
ATOM   1151 C CA   . PRO A 1 74  ? 15.731 39.229 15.043 1.00 26.83  ? 77  PRO A CA   1 
ATOM   1152 C C    . PRO A 1 74  ? 15.602 39.681 16.481 1.00 30.20  ? 77  PRO A C    1 
ATOM   1153 O O    . PRO A 1 74  ? 16.493 40.348 17.022 1.00 34.27  ? 77  PRO A O    1 
ATOM   1154 C CB   . PRO A 1 74  ? 16.988 38.361 14.839 1.00 32.02  ? 77  PRO A CB   1 
ATOM   1155 C CG   . PRO A 1 74  ? 18.024 39.273 14.231 1.00 42.06  ? 77  PRO A CG   1 
ATOM   1156 C CD   . PRO A 1 74  ? 17.318 40.371 13.514 1.00 35.27  ? 77  PRO A CD   1 
ATOM   1157 H HA   . PRO A 1 74  ? 14.937 38.742 14.773 0.00 32.20  ? 77  PRO A HA   1 
ATOM   1158 H HB2  . PRO A 1 74  ? 17.291 38.018 15.694 0.00 38.42  ? 77  PRO A HB2  1 
ATOM   1159 H HB3  . PRO A 1 74  ? 16.784 37.626 14.240 0.00 38.42  ? 77  PRO A HB3  1 
ATOM   1160 H HG2  . PRO A 1 74  ? 18.579 39.639 14.938 0.00 50.47  ? 77  PRO A HG2  1 
ATOM   1161 H HG3  . PRO A 1 74  ? 18.569 38.765 13.611 0.00 50.47  ? 77  PRO A HG3  1 
ATOM   1162 H HD2  . PRO A 1 74  ? 17.769 41.219 13.644 0.00 42.33  ? 77  PRO A HD2  1 
ATOM   1163 H HD3  . PRO A 1 74  ? 17.244 40.177 12.566 0.00 42.33  ? 77  PRO A HD3  1 
ATOM   1164 N N    . ILE A 1 75  ? 14.432 39.433 17.093 1.00 22.63  ? 78  ILE A N    1 
ATOM   1165 C CA   . ILE A 1 75  ? 14.233 39.810 18.471 1.00 21.76  ? 78  ILE A CA   1 
ATOM   1166 C C    . ILE A 1 75  ? 13.936 38.569 19.269 1.00 22.98  ? 78  ILE A C    1 
ATOM   1167 O O    . ILE A 1 75  ? 12.948 37.846 19.012 1.00 22.92  ? 78  ILE A O    1 
ATOM   1168 C CB   . ILE A 1 75  ? 13.040 40.835 18.533 1.00 22.39  ? 78  ILE A CB   1 
ATOM   1169 C CG1  . ILE A 1 75  ? 13.332 42.123 17.728 1.00 26.18  ? 78  ILE A CG1  1 
ATOM   1170 C CG2  . ILE A 1 75  ? 12.706 41.061 20.049 1.00 24.73  ? 78  ILE A CG2  1 
ATOM   1171 C CD1  . ILE A 1 75  ? 14.437 43.078 18.384 1.00 29.97  ? 78  ILE A CD1  1 
ATOM   1172 H H    . ILE A 1 75  ? 13.757 39.052 16.721 0.00 27.15  ? 78  ILE A H    1 
ATOM   1173 H HA   . ILE A 1 75  ? 15.036 40.196 18.855 0.00 26.12  ? 78  ILE A HA   1 
ATOM   1174 H HB   . ILE A 1 75  ? 12.252 40.481 18.093 0.00 26.87  ? 78  ILE A HB   1 
ATOM   1175 H HG12 . ILE A 1 75  ? 13.647 41.872 16.846 0.00 31.41  ? 78  ILE A HG12 1 
ATOM   1176 H HG13 . ILE A 1 75  ? 12.510 42.633 17.654 0.00 31.41  ? 78  ILE A HG13 1 
ATOM   1177 H HG21 . ILE A 1 75  ? 12.158 41.857 20.136 0.00 29.68  ? 78  ILE A HG21 1 
ATOM   1178 H HG22 . ILE A 1 75  ? 12.224 40.289 20.385 0.00 29.68  ? 78  ILE A HG22 1 
ATOM   1179 H HG23 . ILE A 1 75  ? 13.534 41.174 20.542 0.00 29.68  ? 78  ILE A HG23 1 
ATOM   1180 H HD11 . ILE A 1 75  ? 14.555 43.858 17.820 0.00 35.96  ? 78  ILE A HD11 1 
ATOM   1181 H HD12 . ILE A 1 75  ? 14.138 43.350 19.266 0.00 35.96  ? 78  ILE A HD12 1 
ATOM   1182 H HD13 . ILE A 1 75  ? 15.274 42.592 18.454 0.00 35.96  ? 78  ILE A HD13 1 
ATOM   1183 N N    . TYR A 1 76  ? 14.786 38.309 20.254 1.00 19.50  ? 79  TYR A N    1 
ATOM   1184 C CA   . TYR A 1 76  ? 14.569 37.180 21.181 1.00 18.96  ? 79  TYR A CA   1 
ATOM   1185 C C    . TYR A 1 76  ? 13.570 37.568 22.250 1.00 20.25  ? 79  TYR A C    1 
ATOM   1186 O O    . TYR A 1 76  ? 13.919 38.136 23.311 1.00 22.68  ? 79  TYR A O    1 
ATOM   1187 C CB   . TYR A 1 76  ? 15.931 36.775 21.794 1.00 22.54  ? 79  TYR A CB   1 
ATOM   1188 C CG   . TYR A 1 76  ? 16.778 35.934 20.881 1.00 20.18  ? 79  TYR A CG   1 
ATOM   1189 C CD1  . TYR A 1 76  ? 16.494 34.576 20.667 1.00 21.53  ? 79  TYR A CD1  1 
ATOM   1190 C CD2  . TYR A 1 76  ? 17.849 36.465 20.223 1.00 25.87  ? 79  TYR A CD2  1 
ATOM   1191 C CE1  . TYR A 1 76  ? 17.305 33.797 19.830 1.00 20.01  ? 79  TYR A CE1  1 
ATOM   1192 C CE2  . TYR A 1 76  ? 18.630 35.649 19.352 1.00 26.06  ? 79  TYR A CE2  1 
ATOM   1193 C CZ   . TYR A 1 76  ? 18.315 34.325 19.203 1.00 21.13  ? 79  TYR A CZ   1 
ATOM   1194 O OH   . TYR A 1 76  ? 19.104 33.550 18.351 1.00 24.45  ? 79  TYR A OH   1 
ATOM   1195 H H    . TYR A 1 76  ? 15.497 38.766 20.414 0.00 23.40  ? 79  TYR A H    1 
ATOM   1196 H HA   . TYR A 1 76  ? 14.181 36.433 20.699 0.00 22.75  ? 79  TYR A HA   1 
ATOM   1197 H HB2  . TYR A 1 76  ? 16.430 37.580 22.004 0.00 27.05  ? 79  TYR A HB2  1 
ATOM   1198 H HB3  . TYR A 1 76  ? 15.770 36.265 22.603 0.00 27.05  ? 79  TYR A HB3  1 
ATOM   1199 H HD1  . TYR A 1 76  ? 15.759 34.189 21.085 0.00 25.84  ? 79  TYR A HD1  1 
ATOM   1200 H HD2  . TYR A 1 76  ? 18.070 37.360 20.342 0.00 31.04  ? 79  TYR A HD2  1 
ATOM   1201 H HE1  . TYR A 1 76  ? 17.118 32.892 19.722 0.00 24.01  ? 79  TYR A HE1  1 
ATOM   1202 H HE2  . TYR A 1 76  ? 19.349 36.014 18.889 0.00 31.27  ? 79  TYR A HE2  1 
ATOM   1203 H HH   . TYR A 1 76  ? 19.691 34.030 17.989 0.00 29.34  ? 79  TYR A HH   1 
ATOM   1204 N N    . TRP A 1 77  ? 12.288 37.242 22.023 1.00 19.21  ? 80  TRP A N    1 
ATOM   1205 C CA   . TRP A 1 77  ? 11.271 37.672 22.973 1.00 18.77  ? 80  TRP A CA   1 
ATOM   1206 C C    . TRP A 1 77  ? 11.255 36.816 24.193 1.00 18.54  ? 80  TRP A C    1 
ATOM   1207 O O    . TRP A 1 77  ? 10.704 37.239 25.216 1.00 18.58  ? 80  TRP A O    1 
ATOM   1208 C CB   . TRP A 1 77  ? 9.856  37.632 22.292 1.00 21.83  ? 80  TRP A CB   1 
ATOM   1209 C CG   . TRP A 1 77  ? 9.486  36.182 21.810 1.00 20.78  ? 80  TRP A CG   1 
ATOM   1210 C CD1  . TRP A 1 77  ? 9.677  35.682 20.555 1.00 25.88  ? 80  TRP A CD1  1 
ATOM   1211 C CD2  . TRP A 1 77  ? 8.893  35.116 22.575 1.00 19.86  ? 80  TRP A CD2  1 
ATOM   1212 N NE1  . TRP A 1 77  ? 9.198  34.356 20.489 1.00 27.00  ? 80  TRP A NE1  1 
ATOM   1213 C CE2  . TRP A 1 77  ? 8.722  34.021 21.732 1.00 24.58  ? 80  TRP A CE2  1 
ATOM   1214 C CE3  . TRP A 1 77  ? 8.517  35.000 23.910 1.00 24.14  ? 80  TRP A CE3  1 
ATOM   1215 C CZ2  . TRP A 1 77  ? 8.196  32.798 22.171 1.00 29.83  ? 80  TRP A CZ2  1 
ATOM   1216 C CZ3  . TRP A 1 77  ? 7.941  33.772 24.340 1.00 28.27  ? 80  TRP A CZ3  1 
ATOM   1217 C CH2  . TRP A 1 77  ? 7.813  32.705 23.450 1.00 27.32  ? 80  TRP A CH2  1 
ATOM   1218 H H    . TRP A 1 77  ? 12.000 36.790 21.350 0.00 23.06  ? 80  TRP A H    1 
ATOM   1219 H HA   . TRP A 1 77  ? 11.450 38.587 23.241 0.00 22.52  ? 80  TRP A HA   1 
ATOM   1220 H HB2  . TRP A 1 77  ? 9.186  37.923 22.929 0.00 26.20  ? 80  TRP A HB2  1 
ATOM   1221 H HB3  . TRP A 1 77  ? 9.856  38.219 21.519 0.00 26.20  ? 80  TRP A HB3  1 
ATOM   1222 H HD1  . TRP A 1 77  ? 10.066 36.145 19.849 0.00 31.06  ? 80  TRP A HD1  1 
ATOM   1223 H HE1  . TRP A 1 77  ? 9.203  33.849 19.795 0.00 32.40  ? 80  TRP A HE1  1 
ATOM   1224 H HE3  . TRP A 1 77  ? 8.639  35.706 24.504 0.00 28.97  ? 80  TRP A HE3  1 
ATOM   1225 H HZ2  . TRP A 1 77  ? 8.116  32.075 21.592 0.00 35.80  ? 80  TRP A HZ2  1 
ATOM   1226 H HZ3  . TRP A 1 77  ? 7.649  33.679 25.218 0.00 33.92  ? 80  TRP A HZ3  1 
ATOM   1227 H HH2  . TRP A 1 77  ? 7.451  31.905 23.755 0.00 32.79  ? 80  TRP A HH2  1 
ATOM   1228 N N    . ALA A 1 78  ? 11.898 35.589 24.136 1.00 17.47  ? 81  ALA A N    1 
ATOM   1229 C CA   . ALA A 1 78  ? 11.827 34.762 25.340 1.00 18.05  ? 81  ALA A CA   1 
ATOM   1230 C C    . ALA A 1 78  ? 12.551 35.352 26.497 1.00 17.20  ? 81  ALA A C    1 
ATOM   1231 O O    . ALA A 1 78  ? 12.227 34.970 27.637 1.00 20.55  ? 81  ALA A O    1 
ATOM   1232 C CB   . ALA A 1 78  ? 12.370 33.335 24.983 1.00 23.54  ? 81  ALA A CB   1 
ATOM   1233 H H    . ALA A 1 78  ? 12.332 35.269 23.466 0.00 20.96  ? 81  ALA A H    1 
ATOM   1234 H HA   . ALA A 1 78  ? 10.906 34.675 25.630 0.00 21.66  ? 81  ALA A HA   1 
ATOM   1235 H HB1  . ALA A 1 78  ? 12.351 32.782 25.780 0.00 28.24  ? 81  ALA A HB1  1 
ATOM   1236 H HB2  . ALA A 1 78  ? 11.808 32.945 24.296 0.00 28.24  ? 81  ALA A HB2  1 
ATOM   1237 H HB3  . ALA A 1 78  ? 13.281 33.415 24.659 0.00 28.24  ? 81  ALA A HB3  1 
ATOM   1238 N N    . ARG A 1 79  ? 13.457 36.293 26.275 1.00 18.10  ? 82  ARG A N    1 
ATOM   1239 C CA   . ARG A 1 79  ? 14.133 36.990 27.389 1.00 18.52  ? 82  ARG A CA   1 
ATOM   1240 C C    . ARG A 1 79  ? 13.079 37.622 28.295 1.00 18.69  ? 82  ARG A C    1 
ATOM   1241 O O    . ARG A 1 79  ? 13.244 37.565 29.502 1.00 18.31  ? 82  ARG A O    1 
ATOM   1242 C CB   . ARG A 1 79  ? 15.078 38.082 26.876 1.00 19.49  ? 82  ARG A CB   1 
ATOM   1243 C CG   . ARG A 1 79  ? 16.267 37.569 26.086 1.00 20.77  ? 82  ARG A CG   1 
ATOM   1244 C CD   . ARG A 1 79  ? 17.288 38.678 25.949 1.00 21.21  ? 82  ARG A CD   1 
ATOM   1245 N NE   . ARG A 1 79  ? 18.355 38.330 25.029 1.00 22.81  ? 82  ARG A NE   1 
ATOM   1246 C CZ   . ARG A 1 79  ? 19.250 37.373 25.232 1.00 24.16  ? 82  ARG A CZ   1 
ATOM   1247 N NH1  . ARG A 1 79  ? 19.318 36.753 26.394 1.00 27.53  ? 82  ARG A NH1  1 
ATOM   1248 N NH2  . ARG A 1 79  ? 20.098 37.059 24.272 1.00 31.64  ? 82  ARG A NH2  1 
ATOM   1249 H H    . ARG A 1 79  ? 13.722 36.555 25.443 0.00 21.73  ? 82  ARG A H    1 
ATOM   1250 H HA   . ARG A 1 79  ? 14.649 36.331 27.908 0.00 22.23  ? 82  ARG A HA   1 
ATOM   1251 H HB2  . ARG A 1 79  ? 14.564 38.694 26.309 0.00 23.39  ? 82  ARG A HB2  1 
ATOM   1252 H HB3  . ARG A 1 79  ? 15.408 38.592 27.645 0.00 23.39  ? 82  ARG A HB3  1 
ATOM   1253 H HG2  . ARG A 1 79  ? 16.670 36.804 26.548 0.00 24.93  ? 82  ARG A HG2  1 
ATOM   1254 H HG3  . ARG A 1 79  ? 15.975 37.280 25.195 0.00 24.93  ? 82  ARG A HG3  1 
ATOM   1255 H HD2  . ARG A 1 79  ? 16.840 39.491 25.631 0.00 25.46  ? 82  ARG A HD2  1 
ATOM   1256 H HD3  . ARG A 1 79  ? 17.673 38.872 26.830 0.00 25.46  ? 82  ARG A HD3  1 
ATOM   1257 H HE   . ARG A 1 79  ? 18.415 38.785 24.287 0.00 27.38  ? 82  ARG A HE   1 
ATOM   1258 H HH11 . ARG A 1 79  ? 18.787 36.990 27.054 0.00 33.03  ? 82  ARG A HH11 1 
ATOM   1259 H HH12 . ARG A 1 79  ? 19.899 36.101 26.506 0.00 33.03  ? 82  ARG A HH12 1 
ATOM   1260 H HH21 . ARG A 1 79  ? 20.049 37.466 23.494 0.00 37.96  ? 82  ARG A HH21 1 
ATOM   1261 H HH22 . ARG A 1 79  ? 20.709 36.443 24.413 0.00 37.96  ? 82  ARG A HH22 1 
ATOM   1262 N N    . TYR A 1 80  ? 12.028 38.210 27.725 1.00 18.58  ? 83  TYR A N    1 
ATOM   1263 C CA   . TYR A 1 80  ? 11.063 38.926 28.579 1.00 18.58  ? 83  TYR A CA   1 
ATOM   1264 C C    . TYR A 1 80  ? 10.188 37.968 29.319 1.00 16.89  ? 83  TYR A C    1 
ATOM   1265 O O    . TYR A 1 80  ? 9.707  38.319 30.438 1.00 19.78  ? 83  TYR A O    1 
ATOM   1266 C CB   . TYR A 1 80  ? 10.199 39.907 27.717 1.00 19.56  ? 83  TYR A CB   1 
ATOM   1267 C CG   . TYR A 1 80  ? 11.129 40.840 26.964 1.00 18.82  ? 83  TYR A CG   1 
ATOM   1268 C CD1  . TYR A 1 80  ? 11.571 42.021 27.560 1.00 20.19  ? 83  TYR A CD1  1 
ATOM   1269 C CD2  . TYR A 1 80  ? 11.582 40.537 25.674 1.00 20.37  ? 83  TYR A CD2  1 
ATOM   1270 C CE1  . TYR A 1 80  ? 12.536 42.795 26.869 1.00 22.55  ? 83  TYR A CE1  1 
ATOM   1271 C CE2  . TYR A 1 80  ? 12.539 41.308 25.007 1.00 22.52  ? 83  TYR A CE2  1 
ATOM   1272 C CZ   . TYR A 1 80  ? 12.969 42.425 25.604 1.00 22.93  ? 83  TYR A CZ   1 
ATOM   1273 O OH   . TYR A 1 80  ? 13.951 43.104 24.900 1.00 24.27  ? 83  TYR A OH   1 
ATOM   1274 H H    . TYR A 1 80  ? 11.844 38.204 26.885 0.00 22.29  ? 83  TYR A H    1 
ATOM   1275 H HA   . TYR A 1 80  ? 11.544 39.464 29.227 0.00 22.30  ? 83  TYR A HA   1 
ATOM   1276 H HB2  . TYR A 1 80  ? 9.667  39.406 27.079 0.00 23.48  ? 83  TYR A HB2  1 
ATOM   1277 H HB3  . TYR A 1 80  ? 9.620  40.431 28.292 0.00 23.48  ? 83  TYR A HB3  1 
ATOM   1278 H HD1  . TYR A 1 80  ? 11.242 42.293 28.386 0.00 24.23  ? 83  TYR A HD1  1 
ATOM   1279 H HD2  . TYR A 1 80  ? 11.232 39.791 25.243 0.00 24.45  ? 83  TYR A HD2  1 
ATOM   1280 H HE1  . TYR A 1 80  ? 12.884 43.560 27.268 0.00 27.07  ? 83  TYR A HE1  1 
ATOM   1281 H HE2  . TYR A 1 80  ? 12.866 41.053 24.175 0.00 27.03  ? 83  TYR A HE2  1 
ATOM   1282 H HH   . TYR A 1 80  ? 14.048 42.761 24.140 0.00 29.13  ? 83  TYR A HH   1 
ATOM   1283 N N    . ALA A 1 81  ? 9.891  36.761 28.748 1.00 17.00  ? 84  ALA A N    1 
ATOM   1284 C CA   . ALA A 1 81  ? 9.087  35.806 29.525 1.00 16.40  ? 84  ALA A CA   1 
ATOM   1285 C C    . ALA A 1 81  ? 9.921  35.281 30.707 1.00 17.19  ? 84  ALA A C    1 
ATOM   1286 O O    . ALA A 1 81  ? 9.312  35.112 31.786 1.00 21.54  ? 84  ALA A O    1 
ATOM   1287 C CB   . ALA A 1 81  ? 8.712  34.693 28.520 1.00 21.00  ? 84  ALA A CB   1 
ATOM   1288 H H    . ALA A 1 81  ? 10.132 36.501 27.965 0.00 20.40  ? 84  ALA A H    1 
ATOM   1289 H HA   . ALA A 1 81  ? 8.280  36.185 29.906 0.00 19.68  ? 84  ALA A HA   1 
ATOM   1290 H HB1  . ALA A 1 81  ? 8.178  34.023 28.976 0.00 25.20  ? 84  ALA A HB1  1 
ATOM   1291 H HB2  . ALA A 1 81  ? 8.202  35.083 27.793 0.00 25.20  ? 84  ALA A HB2  1 
ATOM   1292 H HB3  . ALA A 1 81  ? 9.525  34.291 28.176 0.00 25.20  ? 84  ALA A HB3  1 
ATOM   1293 N N    . ASP A 1 82  ? 11.220 35.115 30.545 1.00 16.52  ? 85  ASP A N    1 
ATOM   1294 C CA   . ASP A 1 82  ? 12.050 34.770 31.689 1.00 17.22  ? 85  ASP A CA   1 
ATOM   1295 C C    . ASP A 1 82  ? 12.027 35.885 32.710 1.00 15.97  ? 85  ASP A C    1 
ATOM   1296 O O    . ASP A 1 82  ? 11.603 35.657 33.859 1.00 17.11  ? 85  ASP A O    1 
ATOM   1297 C CB   . ASP A 1 82  ? 13.449 34.615 31.118 1.00 17.62  ? 85  ASP A CB   1 
ATOM   1298 C CG   . ASP A 1 82  ? 14.595 34.455 32.087 1.00 18.79  ? 85  ASP A CG   1 
ATOM   1299 O OD1  . ASP A 1 82  ? 14.454 34.768 33.267 1.00 19.34  ? 85  ASP A OD1  1 
ATOM   1300 O OD2  . ASP A 1 82  ? 15.671 33.978 31.619 1.00 18.67  ? 85  ASP A OD2  1 
ATOM   1301 H H    . ASP A 1 82  ? 11.642 35.193 29.799 0.00 19.83  ? 85  ASP A H    1 
ATOM   1302 H HA   . ASP A 1 82  ? 11.750 33.962 32.135 0.00 20.67  ? 85  ASP A HA   1 
ATOM   1303 H HB2  . ASP A 1 82  ? 13.452 33.827 30.552 0.00 21.15  ? 85  ASP A HB2  1 
ATOM   1304 H HB3  . ASP A 1 82  ? 13.641 35.405 30.589 0.00 21.15  ? 85  ASP A HB3  1 
ATOM   1305 N N    . TRP A 1 83  ? 12.320 37.088 32.290 1.00 16.44  ? 86  TRP A N    1 
ATOM   1306 C CA   . TRP A 1 83  ? 12.539 38.133 33.292 1.00 17.45  ? 86  TRP A CA   1 
ATOM   1307 C C    . TRP A 1 83  ? 11.227 38.546 33.962 1.00 17.79  ? 86  TRP A C    1 
ATOM   1308 O O    . TRP A 1 83  ? 11.233 38.981 35.128 1.00 18.33  ? 86  TRP A O    1 
ATOM   1309 C CB   . TRP A 1 83  ? 13.116 39.402 32.600 1.00 18.07  ? 86  TRP A CB   1 
ATOM   1310 C CG   . TRP A 1 83  ? 14.441 39.176 31.945 1.00 15.82  ? 86  TRP A CG   1 
ATOM   1311 C CD1  . TRP A 1 83  ? 15.292 38.161 32.198 1.00 18.97  ? 86  TRP A CD1  1 
ATOM   1312 C CD2  . TRP A 1 83  ? 15.067 40.034 30.963 1.00 16.59  ? 86  TRP A CD2  1 
ATOM   1313 N NE1  . TRP A 1 83  ? 16.509 38.311 31.399 1.00 18.90  ? 86  TRP A NE1  1 
ATOM   1314 C CE2  . TRP A 1 83  ? 16.292 39.439 30.630 1.00 17.96  ? 86  TRP A CE2  1 
ATOM   1315 C CE3  . TRP A 1 83  ? 14.597 41.143 30.292 1.00 19.61  ? 86  TRP A CE3  1 
ATOM   1316 C CZ2  . TRP A 1 83  ? 17.205 40.063 29.706 1.00 18.98  ? 86  TRP A CZ2  1 
ATOM   1317 C CZ3  . TRP A 1 83  ? 15.434 41.769 29.340 1.00 19.74  ? 86  TRP A CZ3  1 
ATOM   1318 C CH2  . TRP A 1 83  ? 16.714 41.193 29.033 1.00 20.91  ? 86  TRP A CH2  1 
ATOM   1319 H H    . TRP A 1 83  ? 12.397 37.331 31.469 0.00 19.73  ? 86  TRP A H    1 
ATOM   1320 H HA   . TRP A 1 83  ? 13.161 37.792 33.954 0.00 20.95  ? 86  TRP A HA   1 
ATOM   1321 H HB2  . TRP A 1 83  ? 12.494 39.696 31.917 0.00 21.69  ? 86  TRP A HB2  1 
ATOM   1322 H HB3  . TRP A 1 83  ? 13.229 40.097 33.267 0.00 21.69  ? 86  TRP A HB3  1 
ATOM   1323 H HD1  . TRP A 1 83  ? 15.129 37.466 32.795 0.00 22.77  ? 86  TRP A HD1  1 
ATOM   1324 H HE1  . TRP A 1 83  ? 17.207 37.807 31.407 0.00 22.68  ? 86  TRP A HE1  1 
ATOM   1325 H HE3  . TRP A 1 83  ? 13.744 41.473 30.462 0.00 23.53  ? 86  TRP A HE3  1 
ATOM   1326 H HZ2  . TRP A 1 83  ? 18.064 39.738 29.565 0.00 22.77  ? 86  TRP A HZ2  1 
ATOM   1327 H HZ3  . TRP A 1 83  ? 15.158 42.549 28.915 0.00 23.69  ? 86  TRP A HZ3  1 
ATOM   1328 H HH2  . TRP A 1 83  ? 17.234 41.581 28.367 0.00 25.09  ? 86  TRP A HH2  1 
ATOM   1329 N N    . LEU A 1 84  ? 10.034 38.399 33.287 1.00 15.68  ? 87  LEU A N    1 
ATOM   1330 C CA   . LEU A 1 84  ? 8.754  38.653 33.955 1.00 17.24  ? 87  LEU A CA   1 
ATOM   1331 C C    . LEU A 1 84  ? 8.626  37.859 35.254 1.00 17.80  ? 87  LEU A C    1 
ATOM   1332 O O    . LEU A 1 84  ? 8.044  38.372 36.210 1.00 19.07  ? 87  LEU A O    1 
ATOM   1333 C CB   . LEU A 1 84  ? 7.613  38.293 32.926 1.00 19.71  ? 87  LEU A CB   1 
ATOM   1334 C CG   . LEU A 1 84  ? 6.283  38.560 33.480 1.00 25.09  ? 87  LEU A CG   1 
ATOM   1335 C CD1  . LEU A 1 84  ? 6.084  40.030 33.663 1.00 34.50  ? 87  LEU A CD1  1 
ATOM   1336 C CD2  . LEU A 1 84  ? 5.286  38.019 32.390 1.00 31.75  ? 87  LEU A CD2  1 
ATOM   1337 H H    . LEU A 1 84  ? 9.963  38.158 32.465 0.00 18.81  ? 87  LEU A H    1 
ATOM   1338 H HA   . LEU A 1 84  ? 8.673  39.586 34.207 0.00 20.69  ? 87  LEU A HA   1 
ATOM   1339 H HB2  . LEU A 1 84  ? 7.723  38.829 32.125 0.00 23.65  ? 87  LEU A HB2  1 
ATOM   1340 H HB3  . LEU A 1 84  ? 7.668  37.351 32.704 0.00 23.65  ? 87  LEU A HB3  1 
ATOM   1341 H HG   . LEU A 1 84  ? 6.147  38.145 34.346 0.00 30.11  ? 87  LEU A HG   1 
ATOM   1342 H HD11 . LEU A 1 84  ? 5.162  40.195 33.914 0.00 41.40  ? 87  LEU A HD11 1 
ATOM   1343 H HD12 . LEU A 1 84  ? 6.679  40.345 34.361 0.00 41.40  ? 87  LEU A HD12 1 
ATOM   1344 H HD13 . LEU A 1 84  ? 6.285  40.482 32.828 0.00 41.40  ? 87  LEU A HD13 1 
ATOM   1345 H HD21 . LEU A 1 84  ? 4.376  38.188 32.683 0.00 38.10  ? 87  LEU A HD21 1 
ATOM   1346 H HD22 . LEU A 1 84  ? 5.454  38.478 31.552 0.00 38.10  ? 87  LEU A HD22 1 
ATOM   1347 H HD23 . LEU A 1 84  ? 5.426  37.066 32.279 0.00 38.10  ? 87  LEU A HD23 1 
ATOM   1348 N N    . PHE A 1 85  ? 9.081  36.593 35.271 1.00 18.05  ? 88  PHE A N    1 
ATOM   1349 C CA   . PHE A 1 85  ? 8.980  35.827 36.513 1.00 19.35  ? 88  PHE A CA   1 
ATOM   1350 C C    . PHE A 1 85  ? 10.229 35.801 37.338 1.00 18.96  ? 88  PHE A C    1 
ATOM   1351 O O    . PHE A 1 85  ? 10.138 35.812 38.617 1.00 21.71  ? 88  PHE A O    1 
ATOM   1352 C CB   . PHE A 1 85  ? 8.654  34.373 36.135 1.00 23.42  ? 88  PHE A CB   1 
ATOM   1353 C CG   . PHE A 1 85  ? 7.273  34.233 35.460 1.00 24.83  ? 88  PHE A CG   1 
ATOM   1354 C CD1  . PHE A 1 85  ? 6.135  34.415 36.192 1.00 29.52  ? 88  PHE A CD1  1 
ATOM   1355 C CD2  . PHE A 1 85  ? 7.273  34.015 34.150 1.00 24.13  ? 88  PHE A CD2  1 
ATOM   1356 C CE1  . PHE A 1 85  ? 4.882  34.325 35.571 1.00 32.61  ? 88  PHE A CE1  1 
ATOM   1357 C CE2  . PHE A 1 85  ? 6.021  33.896 33.485 1.00 33.21  ? 88  PHE A CE2  1 
ATOM   1358 C CZ   . PHE A 1 85  ? 4.858  34.116 34.209 1.00 32.34  ? 88  PHE A CZ   1 
ATOM   1359 H H    . PHE A 1 85  ? 9.435  36.182 34.604 0.00 21.66  ? 88  PHE A H    1 
ATOM   1360 H HA   . PHE A 1 85  ? 8.284  36.216 37.066 0.00 23.22  ? 88  PHE A HA   1 
ATOM   1361 H HB2  . PHE A 1 85  ? 9.326  34.049 35.515 0.00 28.11  ? 88  PHE A HB2  1 
ATOM   1362 H HB3  . PHE A 1 85  ? 8.653  33.830 36.938 0.00 28.11  ? 88  PHE A HB3  1 
ATOM   1363 H HD1  . PHE A 1 85  ? 6.191  34.599 37.102 0.00 35.42  ? 88  PHE A HD1  1 
ATOM   1364 H HD2  . PHE A 1 85  ? 8.072  33.941 33.679 0.00 28.95  ? 88  PHE A HD2  1 
ATOM   1365 H HE1  . PHE A 1 85  ? 4.095  34.403 36.060 0.00 39.13  ? 88  PHE A HE1  1 
ATOM   1366 H HE2  . PHE A 1 85  ? 5.983  33.676 32.582 0.00 39.85  ? 88  PHE A HE2  1 
ATOM   1367 H HZ   . PHE A 1 85  ? 4.042  34.122 33.764 0.00 38.81  ? 88  PHE A HZ   1 
ATOM   1368 N N    . THR A 1 86  ? 11.380 35.946 36.747 1.00 17.79  ? 89  THR A N    1 
ATOM   1369 C CA   . THR A 1 86  ? 12.599 35.785 37.559 1.00 17.32  ? 89  THR A CA   1 
ATOM   1370 C C    . THR A 1 86  ? 12.969 37.061 38.264 1.00 19.05  ? 89  THR A C    1 
ATOM   1371 O O    . THR A 1 86  ? 13.530 37.040 39.389 1.00 18.36  ? 89  THR A O    1 
ATOM   1372 C CB   . THR A 1 86  ? 13.802 35.228 36.751 1.00 16.55  ? 89  THR A CB   1 
ATOM   1373 O OG1  . THR A 1 86  ? 14.108 36.105 35.701 1.00 17.69  ? 89  THR A OG1  1 
ATOM   1374 C CG2  . THR A 1 86  ? 13.506 33.793 36.241 1.00 18.95  ? 89  THR A CG2  1 
ATOM   1375 H H    . THR A 1 86  ? 11.500 36.129 35.916 0.00 21.35  ? 89  THR A H    1 
ATOM   1376 H HA   . THR A 1 86  ? 12.411 35.105 38.224 0.00 20.79  ? 89  THR A HA   1 
ATOM   1377 H HB   . THR A 1 86  ? 14.586 35.159 37.318 0.00 19.86  ? 89  THR A HB   1 
ATOM   1378 H HG1  . THR A 1 86  ? 14.749 35.802 35.250 0.00 21.22  ? 89  THR A HG1  1 
ATOM   1379 H HG21 . THR A 1 86  ? 14.254 33.467 35.716 0.00 22.74  ? 89  THR A HG21 1 
ATOM   1380 H HG22 . THR A 1 86  ? 13.366 33.196 36.993 0.00 22.74  ? 89  THR A HG22 1 
ATOM   1381 H HG23 . THR A 1 86  ? 12.710 33.795 35.688 0.00 22.74  ? 89  THR A HG23 1 
ATOM   1382 N N    . THR A 1 87  ? 12.685 38.235 37.711 1.00 18.42  ? 90  THR A N    1 
ATOM   1383 C CA   . THR A 1 87  ? 13.095 39.509 38.365 1.00 18.59  ? 90  THR A CA   1 
ATOM   1384 C C    . THR A 1 87  ? 12.241 39.734 39.624 1.00 18.41  ? 90  THR A C    1 
ATOM   1385 O O    . THR A 1 87  ? 12.829 40.147 40.622 1.00 19.40  ? 90  THR A O    1 
ATOM   1386 C CB   . THR A 1 87  ? 13.157 40.689 37.382 1.00 18.77  ? 90  THR A CB   1 
ATOM   1387 O OG1  . THR A 1 87  ? 11.922 40.861 36.695 1.00 18.96  ? 90  THR A OG1  1 
ATOM   1388 C CG2  . THR A 1 87  ? 14.261 40.511 36.363 1.00 20.53  ? 90  THR A CG2  1 
ATOM   1389 H H    . THR A 1 87  ? 12.221 38.352 36.935 0.00 22.11  ? 90  THR A H    1 
ATOM   1390 H HA   . THR A 1 87  ? 14.018 39.366 38.680 0.00 22.31  ? 90  THR A HA   1 
ATOM   1391 H HB   . THR A 1 87  ? 13.343 41.507 37.903 0.00 22.52  ? 90  THR A HB   1 
ATOM   1392 H HG1  . THR A 1 87  ? 11.345 41.168 37.229 0.00 22.75  ? 90  THR A HG1  1 
ATOM   1393 H HG21 . THR A 1 87  ? 14.333 41.313 35.816 0.00 24.63  ? 90  THR A HG21 1 
ATOM   1394 H HG22 . THR A 1 87  ? 15.106 40.354 36.822 0.00 24.63  ? 90  THR A HG22 1 
ATOM   1395 H HG23 . THR A 1 87  ? 14.056 39.747 35.793 0.00 24.63  ? 90  THR A HG23 1 
ATOM   1396 N N    . PRO A 1 88  ? 10.910 39.476 39.666 1.00 18.06  ? 91  PRO A N    1 
ATOM   1397 C CA   . PRO A 1 88  ? 10.232 39.657 40.931 1.00 18.72  ? 91  PRO A CA   1 
ATOM   1398 C C    . PRO A 1 88  ? 10.677 38.613 41.939 1.00 21.05  ? 91  PRO A C    1 
ATOM   1399 O O    . PRO A 1 88  ? 10.694 38.951 43.141 1.00 21.89  ? 91  PRO A O    1 
ATOM   1400 C CB   . PRO A 1 88  ? 8.714  39.550 40.631 1.00 23.52  ? 91  PRO A CB   1 
ATOM   1401 C CG   . PRO A 1 88  ? 8.705  38.954 39.234 1.00 30.96  ? 91  PRO A CG   1 
ATOM   1402 C CD   . PRO A 1 88  ? 10.023 39.190 38.499 1.00 19.30  ? 91  PRO A CD   1 
ATOM   1403 H HA   . PRO A 1 88  ? 10.385 40.558 41.257 0.00 22.46  ? 91  PRO A HA   1 
ATOM   1404 H HB2  . PRO A 1 88  ? 8.280  38.966 41.271 0.00 28.22  ? 91  PRO A HB2  1 
ATOM   1405 H HB3  . PRO A 1 88  ? 8.300  40.427 40.648 0.00 28.22  ? 91  PRO A HB3  1 
ATOM   1406 H HG2  . PRO A 1 88  ? 8.550  38.000 39.314 0.00 37.15  ? 91  PRO A HG2  1 
ATOM   1407 H HG3  . PRO A 1 88  ? 7.983  39.367 38.735 0.00 37.15  ? 91  PRO A HG3  1 
ATOM   1408 H HD2  . PRO A 1 88  ? 10.310 38.400 38.015 0.00 23.16  ? 91  PRO A HD2  1 
ATOM   1409 H HD3  . PRO A 1 88  ? 9.968  39.947 37.896 0.00 23.16  ? 91  PRO A HD3  1 
ATOM   1410 N N    . LEU A 1 89  ? 11.052 37.388 41.525 1.00 20.29  ? 92  LEU A N    1 
ATOM   1411 C CA   . LEU A 1 89  ? 11.553 36.398 42.505 1.00 19.29  ? 92  LEU A CA   1 
ATOM   1412 C C    . LEU A 1 89  ? 12.845 36.889 43.120 1.00 21.16  ? 92  LEU A C    1 
ATOM   1413 O O    . LEU A 1 89  ? 13.049 36.778 44.346 1.00 21.51  ? 92  LEU A O    1 
ATOM   1414 C CB   . LEU A 1 89  ? 11.773 35.012 41.840 1.00 20.74  ? 92  LEU A CB   1 
ATOM   1415 C CG   . LEU A 1 89  ? 10.407 34.285 41.593 1.00 21.31  ? 92  LEU A CG   1 
ATOM   1416 C CD1  . LEU A 1 89  ? 10.709 33.085 40.738 1.00 23.18  ? 92  LEU A CD1  1 
ATOM   1417 C CD2  . LEU A 1 89  ? 9.708  33.905 42.858 1.00 27.70  ? 92  LEU A CD2  1 
ATOM   1418 H H    . LEU A 1 89  ? 11.028 37.111 40.711 0.00 24.35  ? 92  LEU A H    1 
ATOM   1419 H HA   . LEU A 1 89  ? 10.886 36.280 43.199 0.00 23.15  ? 92  LEU A HA   1 
ATOM   1420 H HB2  . LEU A 1 89  ? 12.217 35.132 40.986 0.00 24.89  ? 92  LEU A HB2  1 
ATOM   1421 H HB3  . LEU A 1 89  ? 12.316 34.458 42.422 0.00 24.89  ? 92  LEU A HB3  1 
ATOM   1422 H HG   . LEU A 1 89  ? 9.782  34.879 41.149 0.00 25.57  ? 92  LEU A HG   1 
ATOM   1423 H HD11 . LEU A 1 89  ? 9.878  32.633 40.522 0.00 27.82  ? 92  LEU A HD11 1 
ATOM   1424 H HD12 . LEU A 1 89  ? 11.146 33.380 39.923 0.00 27.82  ? 92  LEU A HD12 1 
ATOM   1425 H HD13 . LEU A 1 89  ? 11.294 32.487 41.228 0.00 27.82  ? 92  LEU A HD13 1 
ATOM   1426 H HD21 . LEU A 1 89  ? 8.996  33.280 42.649 0.00 33.24  ? 92  LEU A HD21 1 
ATOM   1427 H HD22 . LEU A 1 89  ? 10.347 33.490 43.459 0.00 33.24  ? 92  LEU A HD22 1 
ATOM   1428 H HD23 . LEU A 1 89  ? 9.339  34.703 43.267 0.00 33.24  ? 92  LEU A HD23 1 
ATOM   1429 N N    . LEU A 1 90  ? 13.728 37.487 42.345 1.00 20.41  ? 93  LEU A N    1 
ATOM   1430 C CA   . LEU A 1 90  ? 14.974 37.994 42.932 1.00 19.57  ? 93  LEU A CA   1 
ATOM   1431 C C    . LEU A 1 90  ? 14.667 39.135 43.915 1.00 18.84  ? 93  LEU A C    1 
ATOM   1432 O O    . LEU A 1 90  ? 15.321 39.206 45.029 1.00 20.66  ? 93  LEU A O    1 
ATOM   1433 C CB   . LEU A 1 90  ? 15.905 38.464 41.810 1.00 20.62  ? 93  LEU A CB   1 
ATOM   1434 C CG   . LEU A 1 90  ? 16.482 37.267 41.005 1.00 20.12  ? 93  LEU A CG   1 
ATOM   1435 C CD1  . LEU A 1 90  ? 17.072 37.834 39.671 1.00 23.80  ? 93  LEU A CD1  1 
ATOM   1436 C CD2  . LEU A 1 90  ? 17.608 36.503 41.817 1.00 22.40  ? 93  LEU A CD2  1 
ATOM   1437 H H    . LEU A 1 90  ? 13.642 37.613 41.498 0.00 24.49  ? 93  LEU A H    1 
ATOM   1438 H HA   . LEU A 1 90  ? 15.429 37.290 43.419 0.00 23.48  ? 93  LEU A HA   1 
ATOM   1439 H HB2  . LEU A 1 90  ? 15.408 39.032 41.200 0.00 24.75  ? 93  LEU A HB2  1 
ATOM   1440 H HB3  . LEU A 1 90  ? 16.645 38.958 42.195 0.00 24.75  ? 93  LEU A HB3  1 
ATOM   1441 H HG   . LEU A 1 90  ? 15.782 36.620 40.824 0.00 24.14  ? 93  LEU A HG   1 
ATOM   1442 H HD11 . LEU A 1 90  ? 17.431 37.101 39.148 0.00 28.56  ? 93  LEU A HD11 1 
ATOM   1443 H HD12 . LEU A 1 90  ? 16.366 38.278 39.177 0.00 28.56  ? 93  LEU A HD12 1 
ATOM   1444 H HD13 . LEU A 1 90  ? 17.777 38.466 39.882 0.00 28.56  ? 93  LEU A HD13 1 
ATOM   1445 H HD21 . LEU A 1 90  ? 18.026 35.847 41.237 0.00 26.88  ? 93  LEU A HD21 1 
ATOM   1446 H HD22 . LEU A 1 90  ? 18.269 37.145 42.121 0.00 26.88  ? 93  LEU A HD22 1 
ATOM   1447 H HD23 . LEU A 1 90  ? 17.202 36.061 42.579 0.00 26.88  ? 93  LEU A HD23 1 
ATOM   1448 N N    . LEU A 1 91  ? 13.766 40.015 43.588 1.00 19.91  ? 94  LEU A N    1 
ATOM   1449 C CA   . LEU A 1 91  ? 13.374 41.065 44.503 1.00 21.46  ? 94  LEU A CA   1 
ATOM   1450 C C    . LEU A 1 91  ? 12.701 40.505 45.758 1.00 21.96  ? 94  LEU A C    1 
ATOM   1451 O O    . LEU A 1 91  ? 12.970 41.029 46.863 1.00 24.07  ? 94  LEU A O    1 
ATOM   1452 C CB   . LEU A 1 91  ? 12.406 42.091 43.838 1.00 22.88  ? 94  LEU A CB   1 
ATOM   1453 C CG   . LEU A 1 91  ? 13.059 42.906 42.747 1.00 22.54  ? 94  LEU A CG   1 
ATOM   1454 C CD1  . LEU A 1 91  ? 11.995 43.876 42.097 1.00 27.22  ? 94  LEU A CD1  1 
ATOM   1455 C CD2  . LEU A 1 91  ? 14.268 43.710 43.248 1.00 27.07  ? 94  LEU A CD2  1 
ATOM   1456 H H    . LEU A 1 91  ? 13.355 40.036 42.833 0.00 23.89  ? 94  LEU A H    1 
ATOM   1457 H HA   . LEU A 1 91  ? 14.186 41.536 44.749 0.00 25.75  ? 94  LEU A HA   1 
ATOM   1458 H HB2  . LEU A 1 91  ? 11.661 41.609 43.445 0.00 27.45  ? 94  LEU A HB2  1 
ATOM   1459 H HB3  . LEU A 1 91  ? 12.084 42.704 44.517 0.00 27.45  ? 94  LEU A HB3  1 
ATOM   1460 H HG   . LEU A 1 91  ? 13.396 42.291 42.077 0.00 27.05  ? 94  LEU A HG   1 
ATOM   1461 H HD11 . LEU A 1 91  ? 12.423 44.388 41.393 0.00 32.66  ? 94  LEU A HD11 1 
ATOM   1462 H HD12 . LEU A 1 91  ? 11.271 43.347 41.727 0.00 32.66  ? 94  LEU A HD12 1 
ATOM   1463 H HD13 . LEU A 1 91  ? 11.654 44.474 42.780 0.00 32.66  ? 94  LEU A HD13 1 
ATOM   1464 H HD21 . LEU A 1 91  ? 14.548 44.326 42.553 0.00 32.48  ? 94  LEU A HD21 1 
ATOM   1465 H HD22 . LEU A 1 91  ? 14.011 44.203 44.043 0.00 32.48  ? 94  LEU A HD22 1 
ATOM   1466 H HD23 . LEU A 1 91  ? 14.990 43.098 43.458 0.00 32.48  ? 94  LEU A HD23 1 
ATOM   1467 N N    . LEU A 1 92  ? 11.962 39.418 45.664 1.00 22.30  ? 95  LEU A N    1 
ATOM   1468 C CA   . LEU A 1 92  ? 11.353 38.816 46.838 1.00 22.61  ? 95  LEU A CA   1 
ATOM   1469 C C    . LEU A 1 92  ? 12.424 38.229 47.730 1.00 24.00  ? 95  LEU A C    1 
ATOM   1470 O O    . LEU A 1 92  ? 12.337 38.372 48.977 1.00 24.62  ? 95  LEU A O    1 
ATOM   1471 C CB   . LEU A 1 92  ? 10.346 37.733 46.454 1.00 23.01  ? 95  LEU A CB   1 
ATOM   1472 C CG   . LEU A 1 92  ? 9.486  37.089 47.442 1.00 31.25  ? 95  LEU A CG   1 
ATOM   1473 C CD1  . LEU A 1 92  ? 8.538  38.179 48.038 1.00 38.23  ? 95  LEU A CD1  1 
ATOM   1474 C CD2  . LEU A 1 92  ? 8.686  36.008 46.784 1.00 35.59  ? 95  LEU A CD2  1 
ATOM   1475 H H    . LEU A 1 92  ? 11.794 39.003 44.930 1.00 26.77  ? 95  LEU A H    1 
ATOM   1476 H HA   . LEU A 1 92  ? 10.863 39.503 47.316 1.00 27.13  ? 95  LEU A HA   1 
ATOM   1477 H HB2  . LEU A 1 92  ? 9.745  38.129 45.805 1.00 27.61  ? 95  LEU A HB2  1 
ATOM   1478 H HB3  . LEU A 1 92  ? 10.853 37.015 46.043 1.00 27.61  ? 95  LEU A HB3  1 
ATOM   1479 H HG   . LEU A 1 92  ? 10.010 36.686 48.152 1.00 37.50  ? 95  LEU A HG   1 
ATOM   1480 H HD11 . LEU A 1 92  ? 7.968  37.769 48.708 1.00 45.88  ? 95  LEU A HD11 1 
ATOM   1481 H HD12 . LEU A 1 92  ? 9.075  38.877 48.443 1.00 45.88  ? 95  LEU A HD12 1 
ATOM   1482 H HD13 . LEU A 1 92  ? 7.996  38.549 47.324 1.00 45.88  ? 95  LEU A HD13 1 
ATOM   1483 H HD21 . LEU A 1 92  ? 8.099  35.605 47.442 1.00 42.71  ? 95  LEU A HD21 1 
ATOM   1484 H HD22 . LEU A 1 92  ? 8.161  36.397 46.067 1.00 42.71  ? 95  LEU A HD22 1 
ATOM   1485 H HD23 . LEU A 1 92  ? 9.291  35.340 46.427 1.00 42.71  ? 95  LEU A HD23 1 
ATOM   1486 N N    . ASP A 1 93  ? 13.469 37.621 47.215 1.00 23.12  ? 96  ASP A N    1 
ATOM   1487 C CA   . ASP A 1 93  ? 14.570 37.182 48.092 1.00 22.40  ? 96  ASP A CA   1 
ATOM   1488 C C    . ASP A 1 93  ? 15.128 38.351 48.893 1.00 26.72  ? 96  ASP A C    1 
ATOM   1489 O O    . ASP A 1 93  ? 15.380 38.230 50.106 1.00 28.27  ? 96  ASP A O    1 
ATOM   1490 C CB   . ASP A 1 93  ? 15.730 36.643 47.234 1.00 23.63  ? 96  ASP A CB   1 
ATOM   1491 C CG   . ASP A 1 93  ? 15.782 35.130 47.094 1.00 22.99  ? 96  ASP A CG   1 
ATOM   1492 O OD1  . ASP A 1 93  ? 15.194 34.370 47.811 1.00 24.24  ? 96  ASP A OD1  1 
ATOM   1493 O OD2  . ASP A 1 93  ? 16.522 34.707 46.148 1.00 25.39  ? 96  ASP A OD2  1 
ATOM   1494 H H    . ASP A 1 93  ? 13.579 37.447 46.380 0.00 27.75  ? 96  ASP A H    1 
ATOM   1495 H HA   . ASP A 1 93  ? 14.224 36.496 48.684 0.00 26.88  ? 96  ASP A HA   1 
ATOM   1496 H HB2  . ASP A 1 93  ? 15.648 37.013 46.341 0.00 28.36  ? 96  ASP A HB2  1 
ATOM   1497 H HB3  . ASP A 1 93  ? 16.566 36.926 47.635 0.00 28.36  ? 96  ASP A HB3  1 
ATOM   1498 N N    . LEU A 1 94  ? 15.394 39.502 48.255 1.00 23.92  ? 97  LEU A N    1 
ATOM   1499 C CA   . LEU A 1 94  ? 15.862 40.650 49.002 1.00 25.74  ? 97  LEU A CA   1 
ATOM   1500 C C    . LEU A 1 94  ? 14.864 41.147 50.038 1.00 23.01  ? 97  LEU A C    1 
ATOM   1501 O O    . LEU A 1 94  ? 15.228 41.471 51.195 1.00 26.50  ? 97  LEU A O    1 
ATOM   1502 C CB   . LEU A 1 94  ? 16.225 41.820 48.055 1.00 26.80  ? 97  LEU A CB   1 
ATOM   1503 C CG   . LEU A 1 94  ? 17.403 41.541 47.130 1.00 26.51  ? 97  LEU A CG   1 
ATOM   1504 C CD1  . LEU A 1 94  ? 17.490 42.667 46.077 1.00 37.45  ? 97  LEU A CD1  1 
ATOM   1505 C CD2  . LEU A 1 94  ? 18.728 41.409 47.911 1.00 32.27  ? 97  LEU A CD2  1 
ATOM   1506 H H    . LEU A 1 94  ? 15.310 39.630 47.409 0.00 28.71  ? 97  LEU A H    1 
ATOM   1507 H HA   . LEU A 1 94  ? 16.658 40.353 49.470 0.00 30.89  ? 97  LEU A HA   1 
ATOM   1508 H HB2  . LEU A 1 94  ? 15.455 42.017 47.499 0.00 32.16  ? 97  LEU A HB2  1 
ATOM   1509 H HB3  . LEU A 1 94  ? 16.451 42.594 48.594 0.00 32.16  ? 97  LEU A HB3  1 
ATOM   1510 H HG   . LEU A 1 94  ? 17.267 40.691 46.683 0.00 31.81  ? 97  LEU A HG   1 
ATOM   1511 H HD11 . LEU A 1 94  ? 18.211 42.467 45.460 0.00 44.94  ? 97  LEU A HD11 1 
ATOM   1512 H HD12 . LEU A 1 94  ? 16.648 42.716 45.598 0.00 44.94  ? 97  LEU A HD12 1 
ATOM   1513 H HD13 . LEU A 1 94  ? 17.664 43.508 46.528 0.00 44.94  ? 97  LEU A HD13 1 
ATOM   1514 H HD21 . LEU A 1 94  ? 19.464 41.368 47.281 0.00 38.73  ? 97  LEU A HD21 1 
ATOM   1515 H HD22 . LEU A 1 94  ? 18.832 42.181 48.490 0.00 38.73  ? 97  LEU A HD22 1 
ATOM   1516 H HD23 . LEU A 1 94  ? 18.702 40.598 48.443 0.00 38.73  ? 97  LEU A HD23 1 
ATOM   1517 N N    . ALA A 1 95  ? 13.586 41.297 49.675 1.00 24.99  ? 98  ALA A N    1 
ATOM   1518 C CA   . ALA A 1 95  ? 12.597 41.800 50.587 1.00 25.23  ? 98  ALA A CA   1 
ATOM   1519 C C    . ALA A 1 95  ? 12.397 40.866 51.799 1.00 28.74  ? 98  ALA A C    1 
ATOM   1520 O O    . ALA A 1 95  ? 12.172 41.330 52.924 1.00 31.38  ? 98  ALA A O    1 
ATOM   1521 C CB   . ALA A 1 95  ? 11.271 42.001 49.803 1.00 29.41  ? 98  ALA A CB   1 
ATOM   1522 H H    . ALA A 1 95  ? 13.276 41.110 48.895 0.00 29.99  ? 98  ALA A H    1 
ATOM   1523 H HA   . ALA A 1 95  ? 12.886 42.654 50.947 0.00 30.27  ? 98  ALA A HA   1 
ATOM   1524 H HB1  . ALA A 1 95  ? 10.597 42.351 50.407 0.00 35.29  ? 98  ALA A HB1  1 
ATOM   1525 H HB2  . ALA A 1 95  ? 11.424 42.627 49.079 0.00 35.29  ? 98  ALA A HB2  1 
ATOM   1526 H HB3  . ALA A 1 95  ? 10.983 41.146 49.446 0.00 35.29  ? 98  ALA A HB3  1 
ATOM   1527 N N    . LEU A 1 96  ? 12.477 39.556 51.583 1.00 26.81  ? 99  LEU A N    1 
ATOM   1528 C CA   . LEU A 1 96  ? 12.273 38.663 52.721 1.00 29.76  ? 99  LEU A CA   1 
ATOM   1529 C C    . LEU A 1 96  ? 13.431 38.723 53.681 1.00 31.18  ? 99  LEU A C    1 
ATOM   1530 O O    . LEU A 1 96  ? 13.265 38.496 54.873 1.00 33.87  ? 99  LEU A O    1 
ATOM   1531 C CB   . LEU A 1 96  ? 12.107 37.228 52.213 1.00 33.66  ? 99  LEU A CB   1 
ATOM   1532 C CG   . LEU A 1 96  ? 10.798 37.070 51.471 1.00 34.32  ? 99  LEU A CG   1 
ATOM   1533 C CD1  . LEU A 1 96  ? 10.739 35.592 51.039 1.00 41.08  ? 99  LEU A CD1  1 
ATOM   1534 C CD2  . LEU A 1 96  ? 9.511  37.417 52.274 1.00 50.85  ? 99  LEU A CD2  1 
ATOM   1535 H H    . LEU A 1 96  ? 12.640 39.178 50.828 0.00 32.17  ? 99  LEU A H    1 
ATOM   1536 H HA   . LEU A 1 96  ? 11.468 38.929 53.193 0.00 35.71  ? 99  LEU A HA   1 
ATOM   1537 H HB2  . LEU A 1 96  ? 12.833 37.015 51.607 0.00 40.40  ? 99  LEU A HB2  1 
ATOM   1538 H HB3  . LEU A 1 96  ? 12.112 36.617 52.965 0.00 40.40  ? 99  LEU A HB3  1 
ATOM   1539 H HG   . LEU A 1 96  ? 10.788 37.704 50.736 0.00 41.18  ? 99  LEU A HG   1 
ATOM   1540 H HD11 . LEU A 1 96  ? 9.874  35.415 50.638 0.00 49.30  ? 99  LEU A HD11 1 
ATOM   1541 H HD12 . LEU A 1 96  ? 11.444 35.423 50.395 0.00 49.30  ? 99  LEU A HD12 1 
ATOM   1542 H HD13 . LEU A 1 96  ? 10.863 35.030 51.820 0.00 49.30  ? 99  LEU A HD13 1 
ATOM   1543 H HD21 . LEU A 1 96  ? 8.736  37.119 51.773 0.00 61.02  ? 99  LEU A HD21 1 
ATOM   1544 H HD22 . LEU A 1 96  ? 9.543  36.967 53.132 0.00 61.02  ? 99  LEU A HD22 1 
ATOM   1545 H HD23 . LEU A 1 96  ? 9.471  38.377 52.405 0.00 61.02  ? 99  LEU A HD23 1 
ATOM   1546 N N    . LEU A 1 97  ? 14.601 38.959 53.167 1.00 31.25  ? 100 LEU A N    1 
ATOM   1547 C CA   . LEU A 1 97  ? 15.791 39.020 53.980 1.00 35.18  ? 100 LEU A CA   1 
ATOM   1548 C C    . LEU A 1 97  ? 15.701 40.152 54.963 1.00 31.22  ? 100 LEU A C    1 
ATOM   1549 O O    . LEU A 1 97  ? 16.049 39.985 56.142 1.00 35.95  ? 100 LEU A O    1 
ATOM   1550 C CB   . LEU A 1 97  ? 16.956 39.200 53.003 1.00 36.13  ? 100 LEU A CB   1 
ATOM   1551 C CG   . LEU A 1 97  ? 18.369 39.049 53.420 1.00 45.72  ? 100 LEU A CG   1 
ATOM   1552 C CD1  . LEU A 1 97  ? 18.592 37.625 53.937 1.00 41.83  ? 100 LEU A CD1  1 
ATOM   1553 C CD2  . LEU A 1 97  ? 19.281 39.375 52.249 1.00 41.42  ? 100 LEU A CD2  1 
ATOM   1554 H H    . LEU A 1 97  ? 14.746 39.092 52.330 0.00 37.50  ? 100 LEU A H    1 
ATOM   1555 H HA   . LEU A 1 97  ? 15.925 38.216 54.506 0.00 42.21  ? 100 LEU A HA   1 
ATOM   1556 H HB2  . LEU A 1 97  ? 16.825 38.552 52.292 0.00 43.35  ? 100 LEU A HB2  1 
ATOM   1557 H HB3  . LEU A 1 97  ? 16.885 40.100 52.648 0.00 43.35  ? 100 LEU A HB3  1 
ATOM   1558 H HG   . LEU A 1 97  ? 18.586 39.662 54.139 0.00 54.86  ? 100 LEU A HG   1 
ATOM   1559 H HD11 . LEU A 1 97  ? 19.536 37.502 54.127 0.00 50.20  ? 100 LEU A HD11 1 
ATOM   1560 H HD12 . LEU A 1 97  ? 18.073 37.497 54.746 0.00 50.20  ? 100 LEU A HD12 1 
ATOM   1561 H HD13 . LEU A 1 97  ? 18.307 36.994 53.258 0.00 50.20  ? 100 LEU A HD13 1 
ATOM   1562 H HD21 . LEU A 1 97  ? 20.204 39.255 52.525 0.00 49.70  ? 100 LEU A HD21 1 
ATOM   1563 H HD22 . LEU A 1 97  ? 19.076 38.777 51.513 0.00 49.70  ? 100 LEU A HD22 1 
ATOM   1564 H HD23 . LEU A 1 97  ? 19.133 40.295 51.980 0.00 49.70  ? 100 LEU A HD23 1 
ATOM   1565 N N    . VAL A 1 98  ? 15.077 41.261 54.577 1.00 32.67  ? 101 VAL A N    1 
ATOM   1566 C CA   . VAL A 1 98  ? 14.949 42.442 55.450 1.00 36.50  ? 101 VAL A CA   1 
ATOM   1567 C C    . VAL A 1 98  ? 13.567 42.537 56.093 1.00 34.78  ? 101 VAL A C    1 
ATOM   1568 O O    . VAL A 1 98  ? 13.274 43.538 56.782 1.00 41.56  ? 101 VAL A O    1 
ATOM   1569 C CB   . VAL A 1 98  ? 15.306 43.739 54.703 1.00 36.95  ? 101 VAL A CB   1 
ATOM   1570 C CG1  . VAL A 1 98  ? 16.632 43.591 53.969 1.00 47.14  ? 101 VAL A CG1  1 
ATOM   1571 C CG2  . VAL A 1 98  ? 14.281 44.093 53.680 1.00 37.47  ? 101 VAL A CG2  1 
ATOM   1572 H H    . VAL A 1 98  ? 14.713 41.362 53.805 0.00 39.20  ? 101 VAL A H    1 
ATOM   1573 H HA   . VAL A 1 98  ? 15.587 42.342 56.174 0.00 43.80  ? 101 VAL A HA   1 
ATOM   1574 H HB   . VAL A 1 98  ? 15.356 44.439 55.374 0.00 44.34  ? 101 VAL A HB   1 
ATOM   1575 H HG11 . VAL A 1 98  ? 16.869 44.442 53.570 0.00 56.57  ? 101 VAL A HG11 1 
ATOM   1576 H HG12 . VAL A 1 98  ? 17.315 43.320 54.602 0.00 56.57  ? 101 VAL A HG12 1 
ATOM   1577 H HG13 . VAL A 1 98  ? 16.536 42.917 53.278 0.00 56.57  ? 101 VAL A HG13 1 
ATOM   1578 H HG21 . VAL A 1 98  ? 14.603 44.843 53.155 0.00 44.96  ? 101 VAL A HG21 1 
ATOM   1579 H HG22 . VAL A 1 98  ? 14.132 43.326 53.104 0.00 44.96  ? 101 VAL A HG22 1 
ATOM   1580 H HG23 . VAL A 1 98  ? 13.456 44.334 54.129 0.00 44.96  ? 101 VAL A HG23 1 
ATOM   1581 N N    . ASP A 1 99  ? 12.726 41.532 55.933 1.00 34.81  ? 102 ASP A N    1 
ATOM   1582 C CA   . ASP A 1 99  ? 11.369 41.528 56.477 1.00 33.14  ? 102 ASP A CA   1 
ATOM   1583 C C    . ASP A 1 99  ? 10.601 42.788 56.051 1.00 35.03  ? 102 ASP A C    1 
ATOM   1584 O O    . ASP A 1 99  ? 9.983  43.500 56.864 1.00 36.76  ? 102 ASP A O    1 
ATOM   1585 C CB   . ASP A 1 99  ? 11.377 41.383 57.982 1.00 39.29  ? 102 ASP A CB   1 
ATOM   1586 C CG   . ASP A 1 99  ? 10.075 40.842 58.506 1.00 51.38  ? 102 ASP A CG   1 
ATOM   1587 O OD1  . ASP A 1 99  ? 9.363  40.131 57.770 1.00 52.75  ? 102 ASP A OD1  1 
ATOM   1588 O OD2  . ASP A 1 99  ? 9.761  41.146 59.655 1.00 54.55  ? 102 ASP A OD2  1 
ATOM   1589 H H    . ASP A 1 99  ? 12.918 40.814 55.499 0.00 41.78  ? 102 ASP A H    1 
ATOM   1590 H HA   . ASP A 1 99  ? 10.903 40.760 56.110 0.00 39.76  ? 102 ASP A HA   1 
ATOM   1591 H HB2  . ASP A 1 99  ? 12.085 40.772 58.239 0.00 47.15  ? 102 ASP A HB2  1 
ATOM   1592 H HB3  . ASP A 1 99  ? 11.528 42.253 58.385 0.00 47.15  ? 102 ASP A HB3  1 
ATOM   1593 N N    . ALA A 1 100 ? 10.620 43.051 54.783 1.00 31.41  ? 103 ALA A N    1 
ATOM   1594 C CA   . ALA A 1 100 ? 9.983  44.246 54.239 1.00 32.99  ? 103 ALA A CA   1 
ATOM   1595 C C    . ALA A 1 100 ? 8.488  44.164 54.461 1.00 36.93  ? 103 ALA A C    1 
ATOM   1596 O O    . ALA A 1 100 ? 7.899  43.086 54.458 1.00 34.44  ? 103 ALA A O    1 
ATOM   1597 C CB   . ALA A 1 100 ? 10.291 44.358 52.752 1.00 32.17  ? 103 ALA A CB   1 
ATOM   1598 H H    . ALA A 1 100 ? 10.997 42.556 54.190 0.00 37.69  ? 103 ALA A H    1 
ATOM   1599 H HA   . ALA A 1 100 ? 10.319 45.043 54.678 0.00 39.59  ? 103 ALA A HA   1 
ATOM   1600 H HB1  . ALA A 1 100 ? 9.856  45.150 52.398 0.00 38.61  ? 103 ALA A HB1  1 
ATOM   1601 H HB2  . ALA A 1 100 ? 11.251 44.427 52.632 0.00 38.61  ? 103 ALA A HB2  1 
ATOM   1602 H HB3  . ALA A 1 100 ? 9.957  43.567 52.300 0.00 38.61  ? 103 ALA A HB3  1 
ATOM   1603 N N    . ASP A 1 101 ? 7.872  45.329 54.705 1.00 33.85  ? 104 ASP A N    1 
ATOM   1604 C CA   . ASP A 1 101 ? 6.421  45.359 54.832 1.00 37.46  ? 104 ASP A CA   1 
ATOM   1605 C C    . ASP A 1 101 ? 5.724  45.031 53.512 1.00 30.09  ? 104 ASP A C    1 
ATOM   1606 O O    . ASP A 1 101 ? 6.269  45.156 52.400 1.00 28.53  ? 104 ASP A O    1 
ATOM   1607 C CB   . ASP A 1 101 ? 5.993  46.745 55.321 1.00 37.70  ? 104 ASP A CB   1 
ATOM   1608 C CG   . ASP A 1 101 ? 6.210  47.805 54.296 1.00 47.08  ? 104 ASP A CG   1 
ATOM   1609 O OD1  . ASP A 1 101 ? 7.326  48.359 54.284 1.00 57.33  ? 104 ASP A OD1  1 
ATOM   1610 O OD2  . ASP A 1 101 ? 5.292  48.067 53.486 1.00 49.27  ? 104 ASP A OD2  1 
ATOM   1611 H H    . ASP A 1 101 ? 8.265  46.088 54.796 0.00 40.62  ? 104 ASP A H    1 
ATOM   1612 H HA   . ASP A 1 101 ? 6.138  44.686 55.470 0.00 44.95  ? 104 ASP A HA   1 
ATOM   1613 H HB2  . ASP A 1 101 ? 5.048  46.726 55.539 1.00 45.25  ? 104 ASP A HB2  1 
ATOM   1614 H HB3  . ASP A 1 101 ? 6.511  46.977 56.108 1.00 45.25  ? 104 ASP A HB3  1 
ATOM   1615 N N    . GLN A 1 102 ? 4.453  44.588 53.620 1.00 33.31  ? 105 GLN A N    1 
ATOM   1616 C CA   . GLN A 1 102 ? 3.767  44.081 52.443 1.00 32.85  ? 105 GLN A CA   1 
ATOM   1617 C C    . GLN A 1 102 ? 3.519  45.180 51.423 1.00 31.40  ? 105 GLN A C    1 
ATOM   1618 O O    . GLN A 1 102 ? 3.548  44.918 50.188 1.00 29.70  ? 105 GLN A O    1 
ATOM   1619 C CB   . GLN A 1 102 ? 2.413  43.478 52.893 1.00 38.67  ? 105 GLN A CB   1 
ATOM   1620 C CG   . GLN A 1 102 ? 2.521  42.390 53.919 1.00 53.22  ? 105 GLN A CG   1 
ATOM   1621 C CD   . GLN A 1 102 ? 1.232  41.614 54.042 1.00 69.26  ? 105 GLN A CD   1 
ATOM   1622 O OE1  . GLN A 1 102 ? 0.204  42.001 53.476 1.00 68.30  ? 105 GLN A OE1  1 
ATOM   1623 N NE2  . GLN A 1 102 ? 1.274  40.515 54.788 1.00 87.50  ? 105 GLN A NE2  1 
ATOM   1624 H H    . GLN A 1 102 ? 3.991  44.575 54.345 0.00 39.97  ? 105 GLN A H    1 
ATOM   1625 H HA   . GLN A 1 102 ? 4.308  43.396 52.019 0.00 39.42  ? 105 GLN A HA   1 
ATOM   1626 H HB2  . GLN A 1 102 ? 1.872  44.187 53.274 0.00 46.41  ? 105 GLN A HB2  1 
ATOM   1627 H HB3  . GLN A 1 102 ? 1.969  43.104 52.116 0.00 46.41  ? 105 GLN A HB3  1 
ATOM   1628 H HG2  . GLN A 1 102 ? 3.224  41.774 53.661 0.00 63.86  ? 105 GLN A HG2  1 
ATOM   1629 H HG3  . GLN A 1 102 ? 2.724  42.782 54.783 0.00 63.86  ? 105 GLN A HG3  1 
ATOM   1630 H HE21 . GLN A 1 102 ? 2.009  40.280 55.168 0.00 105.01 ? 105 GLN A HE21 1 
ATOM   1631 H HE22 . GLN A 1 102 ? 0.566  40.037 54.890 0.00 105.01 ? 105 GLN A HE22 1 
ATOM   1632 N N    . GLY A 1 103 ? 3.281  46.425 51.850 1.00 31.01  ? 106 GLY A N    1 
ATOM   1633 C CA   . GLY A 1 103 ? 3.088  47.507 50.866 1.00 29.99  ? 106 GLY A CA   1 
ATOM   1634 C C    . GLY A 1 103 ? 4.329  47.765 50.024 1.00 29.30  ? 106 GLY A C    1 
ATOM   1635 O O    . GLY A 1 103 ? 4.248  47.989 48.816 1.00 28.24  ? 106 GLY A O    1 
ATOM   1636 H H    . GLY A 1 103 ? 3.227  46.667 52.673 0.00 37.21  ? 106 GLY A H    1 
ATOM   1637 H HA2  . GLY A 1 103 ? 2.360  47.270 50.269 0.00 35.99  ? 106 GLY A HA2  1 
ATOM   1638 H HA3  . GLY A 1 103 ? 2.860  48.327 51.332 0.00 35.99  ? 106 GLY A HA3  1 
ATOM   1639 N N    . THR A 1 104 ? 5.505  47.698 50.634 1.00 29.71  ? 107 THR A N    1 
ATOM   1640 C CA   . THR A 1 104 ? 6.721  47.866 49.875 1.00 29.67  ? 107 THR A CA   1 
ATOM   1641 C C    . THR A 1 104 ? 6.947  46.712 48.932 1.00 26.98  ? 107 THR A C    1 
ATOM   1642 O O    . THR A 1 104 ? 7.409  46.929 47.796 1.00 25.90  ? 107 THR A O    1 
ATOM   1643 C CB   . THR A 1 104 ? 7.880  48.078 50.835 1.00 31.87  ? 107 THR A CB   1 
ATOM   1644 O OG1  . THR A 1 104 ? 7.528  49.164 51.724 1.00 34.22  ? 107 THR A OG1  1 
ATOM   1645 C CG2  . THR A 1 104 ? 9.167  48.470 50.087 1.00 36.09  ? 107 THR A CG2  1 
ATOM   1646 H H    . THR A 1 104 ? 5.619  47.557 51.474 0.00 35.66  ? 107 THR A H    1 
ATOM   1647 H HA   . THR A 1 104 ? 6.661  48.658 49.318 0.00 35.60  ? 107 THR A HA   1 
ATOM   1648 H HB   . THR A 1 104 ? 8.053  47.258 51.323 0.00 38.25  ? 107 THR A HB   1 
ATOM   1649 H HG1  . THR A 1 104 ? 8.132  49.274 52.297 0.00 41.07  ? 107 THR A HG1  1 
ATOM   1650 H HG21 . THR A 1 104 ? 9.895  48.586 50.718 0.00 43.31  ? 107 THR A HG21 1 
ATOM   1651 H HG22 . THR A 1 104 ? 9.407  47.775 49.454 0.00 43.31  ? 107 THR A HG22 1 
ATOM   1652 H HG23 . THR A 1 104 ? 9.031  49.301 49.606 0.00 43.31  ? 107 THR A HG23 1 
ATOM   1653 N N    . ILE A 1 105 ? 6.620  45.492 49.329 1.00 25.01  ? 108 ILE A N    1 
ATOM   1654 C CA   . ILE A 1 105 ? 6.793  44.352 48.388 1.00 25.13  ? 108 ILE A CA   1 
ATOM   1655 C C    . ILE A 1 105 ? 5.902  44.545 47.190 1.00 26.90  ? 108 ILE A C    1 
ATOM   1656 O O    . ILE A 1 105 ? 6.326  44.333 46.042 1.00 24.47  ? 108 ILE A O    1 
ATOM   1657 C CB   . ILE A 1 105 ? 6.534  43.031 49.155 1.00 26.53  ? 108 ILE A CB   1 
ATOM   1658 C CG1  . ILE A 1 105 ? 7.570  42.816 50.217 1.00 32.37  ? 108 ILE A CG1  1 
ATOM   1659 C CG2  . ILE A 1 105 ? 6.557  41.900 48.082 1.00 31.34  ? 108 ILE A CG2  1 
ATOM   1660 C CD1  . ILE A 1 105 ? 7.216  41.508 51.018 1.00 34.54  ? 108 ILE A CD1  1 
ATOM   1661 H H    . ILE A 1 105 ? 6.306  45.287 50.103 0.00 30.01  ? 108 ILE A H    1 
ATOM   1662 H HA   . ILE A 1 105 ? 7.701  44.315 48.048 0.00 30.15  ? 108 ILE A HA   1 
ATOM   1663 H HB   . ILE A 1 105 ? 5.681  43.051 49.618 0.00 31.84  ? 108 ILE A HB   1 
ATOM   1664 H HG12 . ILE A 1 105 ? 8.444  42.710 49.809 0.00 38.85  ? 108 ILE A HG12 1 
ATOM   1665 H HG13 . ILE A 1 105 ? 7.578  43.569 50.828 0.00 38.85  ? 108 ILE A HG13 1 
ATOM   1666 H HG21 . ILE A 1 105 ? 6.563  41.040 48.531 0.00 37.61  ? 108 ILE A HG21 1 
ATOM   1667 H HG22 . ILE A 1 105 ? 5.768  41.977 47.525 0.00 37.61  ? 108 ILE A HG22 1 
ATOM   1668 H HG23 . ILE A 1 105 ? 7.356  41.995 47.540 0.00 37.61  ? 108 ILE A HG23 1 
ATOM   1669 H HD11 . ILE A 1 105 ? 7.678  41.525 51.871 0.00 41.44  ? 108 ILE A HD11 1 
ATOM   1670 H HD12 . ILE A 1 105 ? 6.257  41.475 51.161 0.00 41.44  ? 108 ILE A HD12 1 
ATOM   1671 H HD13 . ILE A 1 105 ? 7.500  40.736 50.503 0.00 41.44  ? 108 ILE A HD13 1 
ATOM   1672 N N    . LEU A 1 106 ? 4.637  44.913 47.390 1.00 25.35  ? 109 LEU A N    1 
ATOM   1673 C CA   A LEU A 1 106 ? 3.739  45.142 46.265 0.54 24.95  ? 109 LEU A CA   1 
ATOM   1674 C CA   B LEU A 1 106 ? 3.713  45.176 46.285 0.46 25.03  ? 109 LEU A CA   1 
ATOM   1675 C C    . LEU A 1 106 ? 4.239  46.249 45.374 1.00 24.07  ? 109 LEU A C    1 
ATOM   1676 O O    . LEU A 1 106 ? 4.203  46.098 44.126 1.00 25.58  ? 109 LEU A O    1 
ATOM   1677 C CB   A LEU A 1 106 ? 2.303  45.411 46.767 0.54 28.36  ? 109 LEU A CB   1 
ATOM   1678 C CB   B LEU A 1 106 ? 2.339  45.614 46.834 0.46 28.43  ? 109 LEU A CB   1 
ATOM   1679 C CG   A LEU A 1 106 ? 1.326  45.634 45.624 0.54 31.24  ? 109 LEU A CG   1 
ATOM   1680 C CG   B LEU A 1 106 ? 1.432  44.549 47.404 0.46 35.32  ? 109 LEU A CG   1 
ATOM   1681 C CD1  A LEU A 1 106 ? 1.263  44.436 44.740 0.54 36.54  ? 109 LEU A CD1  1 
ATOM   1682 C CD1  B LEU A 1 106 ? 0.459  45.164 48.383 0.46 35.66  ? 109 LEU A CD1  1 
ATOM   1683 C CD2  A LEU A 1 106 ? -0.028 45.967 46.177 0.54 34.98  ? 109 LEU A CD2  1 
ATOM   1684 C CD2  B LEU A 1 106 ? 0.684  43.897 46.279 0.46 40.03  ? 109 LEU A CD2  1 
ATOM   1685 H H    A LEU A 1 106 ? 4.278  45.037 48.162 0.54 30.42  ? 109 LEU A H    1 
ATOM   1686 H H    B LEU A 1 106 ? 4.282  45.020 48.167 0.46 30.42  ? 109 LEU A H    1 
ATOM   1687 H HA   A LEU A 1 106 ? 3.704  44.337 45.724 0.54 29.94  ? 109 LEU A HA   1 
ATOM   1688 H HA   B LEU A 1 106 ? 3.610  44.354 45.780 0.46 30.04  ? 109 LEU A HA   1 
ATOM   1689 H HB2  A LEU A 1 106 ? 1.999  44.647 47.281 0.54 34.03  ? 109 LEU A HB2  1 
ATOM   1690 H HB2  B LEU A 1 106 ? 2.496  46.255 47.544 0.46 34.12  ? 109 LEU A HB2  1 
ATOM   1691 H HB3  A LEU A 1 106 ? 2.306  46.205 47.323 0.54 34.03  ? 109 LEU A HB3  1 
ATOM   1692 H HB3  B LEU A 1 106 ? 1.852  46.035 46.108 0.46 34.12  ? 109 LEU A HB3  1 
ATOM   1693 H HG   A LEU A 1 106 ? 1.628  46.377 45.079 0.54 37.49  ? 109 LEU A HG   1 
ATOM   1694 H HG   B LEU A 1 106 ? 1.954  43.882 47.876 0.46 42.39  ? 109 LEU A HG   1 
ATOM   1695 H HD11 A LEU A 1 106 ? 0.494  44.516 44.155 0.54 43.85  ? 109 LEU A HD11 1 
ATOM   1696 H HD11 B LEU A 1 106 ? -0.105 44.465 48.749 0.46 42.79  ? 109 LEU A HD11 1 
ATOM   1697 H HD12 A LEU A 1 106 ? 2.076  44.390 44.213 0.54 43.85  ? 109 LEU A HD12 1 
ATOM   1698 H HD12 B LEU A 1 106 ? 0.958  45.594 49.095 0.46 42.79  ? 109 LEU A HD12 1 
ATOM   1699 H HD13 A LEU A 1 106 ? 1.180  43.642 45.290 0.54 43.85  ? 109 LEU A HD13 1 
ATOM   1700 H HD13 B LEU A 1 106 ? -0.085 45.819 47.918 0.46 42.79  ? 109 LEU A HD13 1 
ATOM   1701 H HD21 A LEU A 1 106 ? -0.617 46.211 45.445 0.54 41.98  ? 109 LEU A HD21 1 
ATOM   1702 H HD21 B LEU A 1 106 ? 0.128  43.189 46.639 0.46 48.03  ? 109 LEU A HD21 1 
ATOM   1703 H HD22 A LEU A 1 106 ? -0.380 45.191 46.640 0.54 41.98  ? 109 LEU A HD22 1 
ATOM   1704 H HD22 B LEU A 1 106 ? 0.131  44.562 45.840 0.46 48.03  ? 109 LEU A HD22 1 
ATOM   1705 H HD23 A LEU A 1 106 ? 0.057  46.711 46.794 0.54 41.98  ? 109 LEU A HD23 1 
ATOM   1706 H HD23 B LEU A 1 106 ? 1.322  43.529 45.648 0.46 48.03  ? 109 LEU A HD23 1 
ATOM   1707 N N    . ALA A 1 107 ? 4.742  47.356 45.928 1.00 24.27  ? 110 ALA A N    1 
ATOM   1708 C CA   . ALA A 1 107 ? 5.293  48.435 45.071 1.00 25.88  ? 110 ALA A CA   1 
ATOM   1709 C C    . ALA A 1 107 ? 6.455  47.936 44.247 1.00 24.82  ? 110 ALA A C    1 
ATOM   1710 O O    . ALA A 1 107 ? 6.535  48.263 43.037 1.00 25.22  ? 110 ALA A O    1 
ATOM   1711 C CB   . ALA A 1 107 ? 5.764  49.581 45.988 1.00 27.06  ? 110 ALA A CB   1 
ATOM   1712 H H    . ALA A 1 107 ? 4.780  47.512 46.773 0.00 29.13  ? 110 ALA A H    1 
ATOM   1713 H HA   . ALA A 1 107 ? 4.607  48.754 44.464 0.00 31.05  ? 110 ALA A HA   1 
ATOM   1714 H HB1  . ALA A 1 107 ? 6.212  50.252 45.450 0.00 32.47  ? 110 ALA A HB1  1 
ATOM   1715 H HB2  . ALA A 1 107 ? 4.992  49.971 46.428 0.00 32.47  ? 110 ALA A HB2  1 
ATOM   1716 H HB3  . ALA A 1 107 ? 6.377  49.225 46.650 0.00 32.47  ? 110 ALA A HB3  1 
ATOM   1717 N N    . LEU A 1 108 ? 7.345  47.116 44.789 1.00 23.25  ? 111 LEU A N    1 
ATOM   1718 C CA   . LEU A 1 108 ? 8.522  46.631 44.053 1.00 23.83  ? 111 LEU A CA   1 
ATOM   1719 C C    . LEU A 1 108 ? 8.096  45.682 42.979 1.00 22.76  ? 111 LEU A C    1 
ATOM   1720 O O    . LEU A 1 108 ? 8.583  45.801 41.812 1.00 22.18  ? 111 LEU A O    1 
ATOM   1721 C CB   . LEU A 1 108 ? 9.483  45.921 45.023 1.00 22.67  ? 111 LEU A CB   1 
ATOM   1722 C CG   . LEU A 1 108 ? 10.367 46.751 45.909 1.00 30.44  ? 111 LEU A CG   1 
ATOM   1723 C CD1  . LEU A 1 108 ? 11.081 45.855 46.922 1.00 35.15  ? 111 LEU A CD1  1 
ATOM   1724 C CD2  . LEU A 1 108 ? 11.415 47.446 45.023 1.00 38.66  ? 111 LEU A CD2  1 
ATOM   1725 H H    . LEU A 1 108 ? 7.298  46.817 45.594 0.00 27.90  ? 111 LEU A H    1 
ATOM   1726 H HA   . LEU A 1 108 ? 8.986  47.382 43.652 0.00 28.60  ? 111 LEU A HA   1 
ATOM   1727 H HB2  . LEU A 1 108 ? 8.946  45.368 45.612 0.00 27.21  ? 111 LEU A HB2  1 
ATOM   1728 H HB3  . LEU A 1 108 ? 10.073 45.363 44.492 0.00 27.21  ? 111 LEU A HB3  1 
ATOM   1729 H HG   . LEU A 1 108 ? 9.842  47.407 46.392 0.00 36.53  ? 111 LEU A HG   1 
ATOM   1730 H HD11 . LEU A 1 108 ? 11.781 46.366 47.357 0.00 42.18  ? 111 LEU A HD11 1 
ATOM   1731 H HD12 . LEU A 1 108 ? 10.438 45.549 47.580 0.00 42.18  ? 111 LEU A HD12 1 
ATOM   1732 H HD13 . LEU A 1 108 ? 11.465 45.096 46.457 0.00 42.18  ? 111 LEU A HD13 1 
ATOM   1733 H HD21 . LEU A 1 108 ? 12.041 47.923 45.590 0.00 46.40  ? 111 LEU A HD21 1 
ATOM   1734 H HD22 . LEU A 1 108 ? 11.885 46.775 44.503 0.00 46.40  ? 111 LEU A HD22 1 
ATOM   1735 H HD23 . LEU A 1 108 ? 10.965 48.069 44.431 0.00 46.40  ? 111 LEU A HD23 1 
ATOM   1736 N N    . VAL A 1 109 ? 7.226  44.742 43.286 1.00 22.30  ? 112 VAL A N    1 
ATOM   1737 C CA   . VAL A 1 109 ? 6.810  43.780 42.260 1.00 21.51  ? 112 VAL A CA   1 
ATOM   1738 C C    . VAL A 1 109 ? 6.033  44.460 41.187 1.00 24.01  ? 112 VAL A C    1 
ATOM   1739 O O    . VAL A 1 109 ? 6.212  44.215 39.982 1.00 21.86  ? 112 VAL A O    1 
ATOM   1740 C CB   . VAL A 1 109 ? 6.039  42.617 42.925 1.00 22.22  ? 112 VAL A CB   1 
ATOM   1741 C CG1  . VAL A 1 109 ? 5.410  41.709 41.849 1.00 27.22  ? 112 VAL A CG1  1 
ATOM   1742 C CG2  . VAL A 1 109 ? 7.007  41.847 43.791 1.00 27.74  ? 112 VAL A CG2  1 
ATOM   1743 H H    . VAL A 1 109 ? 6.866  44.632 44.059 0.00 26.76  ? 112 VAL A H    1 
ATOM   1744 H HA   . VAL A 1 109 ? 7.595  43.404 41.834 0.00 25.82  ? 112 VAL A HA   1 
ATOM   1745 H HB   . VAL A 1 109 ? 5.314  42.953 43.474 0.00 26.67  ? 112 VAL A HB   1 
ATOM   1746 H HG11 . VAL A 1 109 ? 5.136  40.874 42.260 0.00 32.67  ? 112 VAL A HG11 1 
ATOM   1747 H HG12 . VAL A 1 109 ? 4.640  42.158 41.467 0.00 32.67  ? 112 VAL A HG12 1 
ATOM   1748 H HG13 . VAL A 1 109 ? 6.068  41.536 41.157 0.00 32.67  ? 112 VAL A HG13 1 
ATOM   1749 H HG21 . VAL A 1 109 ? 6.576  41.036 44.103 0.00 33.29  ? 112 VAL A HG21 1 
ATOM   1750 H HG22 . VAL A 1 109 ? 7.792  41.624 43.267 0.00 33.29  ? 112 VAL A HG22 1 
ATOM   1751 H HG23 . VAL A 1 109 ? 7.261  42.398 44.548 0.00 33.29  ? 112 VAL A HG23 1 
ATOM   1752 N N    . GLY A 1 110 ? 5.149  45.417 41.521 1.00 21.59  ? 113 GLY A N    1 
ATOM   1753 C CA   . GLY A 1 110 ? 4.407  46.081 40.480 1.00 22.28  ? 113 GLY A CA   1 
ATOM   1754 C C    . GLY A 1 110 ? 5.295  46.967 39.615 1.00 21.84  ? 113 GLY A C    1 
ATOM   1755 O O    . GLY A 1 110 ? 5.159  46.984 38.354 1.00 20.35  ? 113 GLY A O    1 
ATOM   1756 H H    . GLY A 1 110 ? 4.977  45.681 42.321 0.00 25.91  ? 113 GLY A H    1 
ATOM   1757 H HA2  . GLY A 1 110 ? 3.988  45.418 39.910 0.00 26.73  ? 113 GLY A HA2  1 
ATOM   1758 H HA3  . GLY A 1 110 ? 3.718  46.635 40.879 0.00 26.73  ? 113 GLY A HA3  1 
ATOM   1759 N N    . ALA A 1 111 ? 6.256  47.704 40.213 1.00 19.45  ? 114 ALA A N    1 
ATOM   1760 C CA   . ALA A 1 111 ? 7.172  48.449 39.364 1.00 19.70  ? 114 ALA A CA   1 
ATOM   1761 C C    . ALA A 1 111 ? 8.010  47.534 38.455 1.00 19.87  ? 114 ALA A C    1 
ATOM   1762 O O    . ALA A 1 111 ? 8.286  47.872 37.291 1.00 19.09  ? 114 ALA A O    1 
ATOM   1763 C CB   . ALA A 1 111 ? 8.157  49.338 40.230 1.00 21.89  ? 114 ALA A CB   1 
ATOM   1764 H H    . ALA A 1 111 ? 6.381  47.778 41.061 0.00 23.34  ? 114 ALA A H    1 
ATOM   1765 H HA   . ALA A 1 111 ? 6.624  49.026 38.809 0.00 23.64  ? 114 ALA A HA   1 
ATOM   1766 H HB1  . ALA A 1 111 ? 8.749  49.825 39.635 0.00 26.26  ? 114 ALA A HB1  1 
ATOM   1767 H HB2  . ALA A 1 111 ? 7.637  49.961 40.761 0.00 26.26  ? 114 ALA A HB2  1 
ATOM   1768 H HB3  . ALA A 1 111 ? 8.675  48.760 40.812 0.00 26.26  ? 114 ALA A HB3  1 
ATOM   1769 N N    . ASP A 1 112 ? 8.396  46.374 38.955 1.00 20.44  ? 115 ASP A N    1 
ATOM   1770 C CA   . ASP A 1 112 ? 9.158  45.400 38.151 1.00 17.70  ? 115 ASP A CA   1 
ATOM   1771 C C    . ASP A 1 112 ? 8.309  44.933 36.982 1.00 17.87  ? 115 ASP A C    1 
ATOM   1772 O O    . ASP A 1 112 ? 8.825  44.799 35.856 1.00 17.16  ? 115 ASP A O    1 
ATOM   1773 C CB   . ASP A 1 112 ? 9.646  44.215 39.102 1.00 17.63  ? 115 ASP A CB   1 
ATOM   1774 C CG   . ASP A 1 112 ? 10.646 43.392 38.427 1.00 22.56  ? 115 ASP A CG   1 
ATOM   1775 O OD1  . ASP A 1 112 ? 10.191 42.588 37.611 1.00 23.42  ? 115 ASP A OD1  1 
ATOM   1776 O OD2  . ASP A 1 112 ? 11.850 43.566 38.596 1.00 29.50  ? 115 ASP A OD2  1 
ATOM   1777 H H    . ASP A 1 112 ? 8.237  46.114 39.759 0.00 24.53  ? 115 ASP A H    1 
ATOM   1778 H HA   . ASP A 1 112 ? 9.960  45.793 37.773 0.00 21.24  ? 115 ASP A HA   1 
ATOM   1779 H HB2  . ASP A 1 112 ? 10.043 44.586 39.905 0.00 21.15  ? 115 ASP A HB2  1 
ATOM   1780 H HB3  . ASP A 1 112 ? 8.889  43.653 39.334 0.00 21.15  ? 115 ASP A HB3  1 
ATOM   1781 N N    . GLY A 1 113 ? 7.042  44.580 37.224 1.00 18.08  ? 116 GLY A N    1 
ATOM   1782 C CA   . GLY A 1 113 ? 6.120  44.212 36.124 1.00 19.05  ? 116 GLY A CA   1 
ATOM   1783 C C    . GLY A 1 113 ? 6.063  45.274 35.045 1.00 19.65  ? 116 GLY A C    1 
ATOM   1784 O O    . GLY A 1 113 ? 6.071  44.965 33.872 1.00 19.97  ? 116 GLY A O    1 
ATOM   1785 H H    . GLY A 1 113 ? 6.686  44.543 38.006 0.00 21.69  ? 116 GLY A H    1 
ATOM   1786 H HA2  . GLY A 1 113 ? 6.416  43.381 35.721 0.00 22.87  ? 116 GLY A HA2  1 
ATOM   1787 H HA3  . GLY A 1 113 ? 5.227  44.090 36.481 0.00 22.87  ? 116 GLY A HA3  1 
ATOM   1788 N N    . ILE A 1 114 ? 5.912  46.535 35.452 1.00 17.93  ? 117 ILE A N    1 
ATOM   1789 C CA   . ILE A 1 114 ? 5.882  47.652 34.512 1.00 18.75  ? 117 ILE A CA   1 
ATOM   1790 C C    . ILE A 1 114 ? 7.219  47.736 33.779 1.00 18.72  ? 117 ILE A C    1 
ATOM   1791 O O    . ILE A 1 114 ? 7.236  47.860 32.533 1.00 18.31  ? 117 ILE A O    1 
ATOM   1792 C CB   . ILE A 1 114 ? 5.527  48.934 35.269 1.00 18.02  ? 117 ILE A CB   1 
ATOM   1793 C CG1  . ILE A 1 114 ? 4.020  48.832 35.674 1.00 21.36  ? 117 ILE A CG1  1 
ATOM   1794 C CG2  . ILE A 1 114 ? 5.766  50.110 34.295 1.00 21.37  ? 117 ILE A CG2  1 
ATOM   1795 C CD1  . ILE A 1 114 ? 3.628  50.016 36.643 1.00 26.44  ? 117 ILE A CD1  1 
ATOM   1796 H H    . ILE A 1 114 ? 5.825  46.772 36.275 0.00 21.52  ? 117 ILE A H    1 
ATOM   1797 H HA   . ILE A 1 114 ? 5.198  47.514 33.839 0.00 22.50  ? 117 ILE A HA   1 
ATOM   1798 H HB   . ILE A 1 114 ? 6.061  49.062 36.068 0.00 21.63  ? 117 ILE A HB   1 
ATOM   1799 H HG12 . ILE A 1 114 ? 3.466  48.884 34.880 0.00 25.63  ? 117 ILE A HG12 1 
ATOM   1800 H HG13 . ILE A 1 114 ? 3.864  47.991 36.133 0.00 25.63  ? 117 ILE A HG13 1 
ATOM   1801 H HG21 . ILE A 1 114 ? 5.337  50.905 34.650 0.00 25.64  ? 117 ILE A HG21 1 
ATOM   1802 H HG22 . ILE A 1 114 ? 6.720  50.259 34.208 0.00 25.64  ? 117 ILE A HG22 1 
ATOM   1803 H HG23 . ILE A 1 114 ? 5.386  49.887 33.431 0.00 25.64  ? 117 ILE A HG23 1 
ATOM   1804 H HD11 . ILE A 1 114 ? 2.742  49.851 37.001 0.00 31.73  ? 117 ILE A HD11 1 
ATOM   1805 H HD12 . ILE A 1 114 ? 4.274  50.060 37.365 0.00 31.73  ? 117 ILE A HD12 1 
ATOM   1806 H HD13 . ILE A 1 114 ? 3.634  50.847 36.143 0.00 31.73  ? 117 ILE A HD13 1 
ATOM   1807 N N    . MET A 1 115 ? 8.359  47.562 34.444 1.00 16.96  ? 118 MET A N    1 
ATOM   1808 C CA   . MET A 1 115 ? 9.670  47.600 33.760 1.00 17.12  ? 118 MET A CA   1 
ATOM   1809 C C    . MET A 1 115 ? 9.728  46.527 32.712 1.00 18.84  ? 118 MET A C    1 
ATOM   1810 O O    . MET A 1 115 ? 10.121 46.791 31.536 1.00 17.78  ? 118 MET A O    1 
ATOM   1811 C CB   . MET A 1 115 ? 10.726 47.409 34.865 1.00 17.45  ? 118 MET A CB   1 
ATOM   1812 C CG   . MET A 1 115 ? 12.139 47.392 34.282 1.00 17.46  ? 118 MET A CG   1 
ATOM   1813 S SD   . MET A 1 115 ? 13.378 47.115 35.597 1.00 20.67  ? 118 MET A SD   1 
ATOM   1814 C CE   . MET A 1 115 ? 13.190 45.311 35.792 1.00 25.01  ? 118 MET A CE   1 
ATOM   1815 H H    . MET A 1 115 ? 8.411  47.418 35.290 0.00 20.35  ? 118 MET A H    1 
ATOM   1816 H HA   . MET A 1 115 ? 9.835  48.443 33.309 0.00 20.54  ? 118 MET A HA   1 
ATOM   1817 H HB2  . MET A 1 115 ? 10.664 48.141 35.499 0.00 20.94  ? 118 MET A HB2  1 
ATOM   1818 H HB3  . MET A 1 115 ? 10.570 46.565 35.317 0.00 20.94  ? 118 MET A HB3  1 
ATOM   1819 H HG2  . MET A 1 115 ? 12.212 46.675 33.633 0.00 20.95  ? 118 MET A HG2  1 
ATOM   1820 H HG3  . MET A 1 115 ? 12.325 48.244 33.858 0.00 20.95  ? 118 MET A HG3  1 
ATOM   1821 H HE1  . MET A 1 115 ? 13.801 45.003 36.479 0.00 30.02  ? 118 MET A HE1  1 
ATOM   1822 H HE2  . MET A 1 115 ? 12.276 45.115 36.049 0.00 30.02  ? 118 MET A HE2  1 
ATOM   1823 H HE3  . MET A 1 115 ? 13.396 44.879 34.948 0.00 30.02  ? 118 MET A HE3  1 
ATOM   1824 N N    . ILE A 1 116 ? 9.400  45.259 33.044 1.00 16.55  ? 119 ILE A N    1 
ATOM   1825 C CA   . ILE A 1 116 ? 9.570  44.238 31.998 1.00 19.49  ? 119 ILE A CA   1 
ATOM   1826 C C    . ILE A 1 116 ? 8.481  44.374 30.932 1.00 18.03  ? 119 ILE A C    1 
ATOM   1827 O O    . ILE A 1 116 ? 8.777  44.168 29.736 1.00 18.80  ? 119 ILE A O    1 
ATOM   1828 C CB   . ILE A 1 116 ? 9.526  42.886 32.728 1.00 17.26  ? 119 ILE A CB   1 
ATOM   1829 C CG1  . ILE A 1 116 ? 10.648 42.722 33.731 1.00 19.17  ? 119 ILE A CG1  1 
ATOM   1830 C CG2  . ILE A 1 116 ? 9.554  41.764 31.611 1.00 21.40  ? 119 ILE A CG2  1 
ATOM   1831 C CD1  . ILE A 1 116 ? 12.049 42.995 33.223 1.00 20.22  ? 119 ILE A CD1  1 
ATOM   1832 H H    . ILE A 1 116 ? 9.103  44.991 33.805 0.00 19.86  ? 119 ILE A H    1 
ATOM   1833 H HA   . ILE A 1 116 ? 10.410 44.339 31.525 0.00 23.39  ? 119 ILE A HA   1 
ATOM   1834 H HB   . ILE A 1 116 ? 8.717  42.825 33.259 0.00 20.72  ? 119 ILE A HB   1 
ATOM   1835 H HG12 . ILE A 1 116 ? 10.488 43.333 34.466 0.00 23.01  ? 119 ILE A HG12 1 
ATOM   1836 H HG13 . ILE A 1 116 ? 10.635 41.806 34.052 0.00 23.01  ? 119 ILE A HG13 1 
ATOM   1837 H HG21 . ILE A 1 116 ? 9.773  40.914 32.023 0.00 25.68  ? 119 ILE A HG21 1 
ATOM   1838 H HG22 . ILE A 1 116 ? 8.681  41.714 31.191 0.00 25.68  ? 119 ILE A HG22 1 
ATOM   1839 H HG23 . ILE A 1 116 ? 10.226 41.994 30.949 0.00 25.68  ? 119 ILE A HG23 1 
ATOM   1840 H HD11 . ILE A 1 116 ? 12.690 42.681 33.880 0.00 24.26  ? 119 ILE A HD11 1 
ATOM   1841 H HD12 . ILE A 1 116 ? 12.178 42.525 32.384 0.00 24.26  ? 119 ILE A HD12 1 
ATOM   1842 H HD13 . ILE A 1 116 ? 12.156 43.949 33.087 0.00 24.26  ? 119 ILE A HD13 1 
ATOM   1843 N N    . GLY A 1 117 ? 7.243  44.659 31.280 1.00 17.57  ? 120 GLY A N    1 
ATOM   1844 C CA   . GLY A 1 117 ? 6.173  44.745 30.264 1.00 18.63  ? 120 GLY A CA   1 
ATOM   1845 C C    . GLY A 1 117 ? 6.434  45.861 29.282 1.00 19.67  ? 120 GLY A C    1 
ATOM   1846 O O    . GLY A 1 117 ? 6.257  45.642 28.068 1.00 19.51  ? 120 GLY A O    1 
ATOM   1847 H H    . GLY A 1 117 ? 6.981  44.809 32.085 0.00 21.08  ? 120 GLY A H    1 
ATOM   1848 H HA2  . GLY A 1 117 ? 6.121  43.908 29.776 0.00 22.36  ? 120 GLY A HA2  1 
ATOM   1849 H HA3  . GLY A 1 117 ? 5.323  44.909 30.701 0.00 22.36  ? 120 GLY A HA3  1 
ATOM   1850 N N    . THR A 1 118 ? 6.881  47.030 29.754 1.00 17.74  ? 121 THR A N    1 
ATOM   1851 C CA   . THR A 1 118 ? 7.175  48.111 28.816 1.00 18.55  ? 121 THR A CA   1 
ATOM   1852 C C    . THR A 1 118 ? 8.434  47.765 27.999 1.00 20.91  ? 121 THR A C    1 
ATOM   1853 O O    . THR A 1 118 ? 8.563  48.188 26.816 1.00 18.06  ? 121 THR A O    1 
ATOM   1854 C CB   . THR A 1 118 ? 7.264  49.476 29.500 1.00 19.35  ? 121 THR A CB   1 
ATOM   1855 O OG1  . THR A 1 118 ? 8.290  49.468 30.498 1.00 19.92  ? 121 THR A OG1  1 
ATOM   1856 C CG2  . THR A 1 118 ? 5.944  49.834 30.076 1.00 21.12  ? 121 THR A CG2  1 
ATOM   1857 H H    . THR A 1 118 ? 7.016  47.215 30.584 0.00 21.29  ? 121 THR A H    1 
ATOM   1858 H HA   . THR A 1 118 ? 6.431  48.212 28.203 0.00 22.26  ? 121 THR A HA   1 
ATOM   1859 H HB   . THR A 1 118 ? 7.499  50.161 28.855 0.00 23.22  ? 121 THR A HB   1 
ATOM   1860 H HG1  . THR A 1 118 ? 8.116  48.892 31.084 0.00 23.90  ? 121 THR A HG1  1 
ATOM   1861 H HG21 . THR A 1 118 ? 5.994  50.702 30.508 0.00 25.34  ? 121 THR A HG21 1 
ATOM   1862 H HG22 . THR A 1 118 ? 5.274  49.870 29.375 0.00 25.34  ? 121 THR A HG22 1 
ATOM   1863 H HG23 . THR A 1 118 ? 5.678  49.171 30.733 0.00 25.34  ? 121 THR A HG23 1 
ATOM   1864 N N    . GLY A 1 119 ? 9.428  47.089 28.560 1.00 19.08  ? 122 GLY A N    1 
ATOM   1865 C CA   . GLY A 1 119 ? 10.583 46.601 27.779 1.00 20.57  ? 122 GLY A CA   1 
ATOM   1866 C C    . GLY A 1 119 ? 10.144 45.724 26.620 1.00 18.09  ? 122 GLY A C    1 
ATOM   1867 O O    . GLY A 1 119 ? 10.674 45.822 25.523 1.00 19.70  ? 122 GLY A O    1 
ATOM   1868 H H    . GLY A 1 119 ? 9.470  46.893 29.397 0.00 22.90  ? 122 GLY A H    1 
ATOM   1869 H HA2  . GLY A 1 119 ? 11.078 47.356 27.425 0.00 24.68  ? 122 GLY A HA2  1 
ATOM   1870 H HA3  . GLY A 1 119 ? 11.168 46.082 28.354 0.00 24.68  ? 122 GLY A HA3  1 
ATOM   1871 N N    . LEU A 1 120 ? 9.202  44.775 26.866 1.00 18.24  ? 123 LEU A N    1 
ATOM   1872 C CA   . LEU A 1 120 ? 8.694  43.918 25.811 1.00 18.27  ? 123 LEU A CA   1 
ATOM   1873 C C    . LEU A 1 120 ? 7.948  44.715 24.750 1.00 17.99  ? 123 LEU A C    1 
ATOM   1874 O O    . LEU A 1 120 ? 8.148  44.443 23.559 1.00 18.24  ? 123 LEU A O    1 
ATOM   1875 C CB   . LEU A 1 120 ? 7.735  42.914 26.488 1.00 18.76  ? 123 LEU A CB   1 
ATOM   1876 C CG   . LEU A 1 120 ? 7.004  42.002 25.570 1.00 20.69  ? 123 LEU A CG   1 
ATOM   1877 C CD1  . LEU A 1 120 ? 7.811  41.142 24.692 1.00 23.58  ? 123 LEU A CD1  1 
ATOM   1878 C CD2  . LEU A 1 120 ? 6.068  41.106 26.509 1.00 28.58  ? 123 LEU A CD2  1 
ATOM   1879 H H    . LEU A 1 120 ? 8.855  44.622 27.638 0.00 21.89  ? 123 LEU A H    1 
ATOM   1880 H HA   . LEU A 1 120 ? 9.420  43.459 25.361 0.00 21.93  ? 123 LEU A HA   1 
ATOM   1881 H HB2  . LEU A 1 120 ? 8.253  42.360 27.093 0.00 22.52  ? 123 LEU A HB2  1 
ATOM   1882 H HB3  . LEU A 1 120 ? 7.071  43.416 26.986 0.00 22.52  ? 123 LEU A HB3  1 
ATOM   1883 H HG   . LEU A 1 120 ? 6.524  42.550 24.930 0.00 24.83  ? 123 LEU A HG   1 
ATOM   1884 H HD11 . LEU A 1 120 ? 7.217  40.605 24.145 0.00 28.30  ? 123 LEU A HD11 1 
ATOM   1885 H HD12 . LEU A 1 120 ? 8.367  41.701 24.127 0.00 28.30  ? 123 LEU A HD12 1 
ATOM   1886 H HD13 . LEU A 1 120 ? 8.368  40.567 25.239 0.00 28.30  ? 123 LEU A HD13 1 
ATOM   1887 H HD21 . LEU A 1 120 ? 5.590  40.465 25.959 0.00 34.30  ? 123 LEU A HD21 1 
ATOM   1888 H HD22 . LEU A 1 120 ? 6.622  40.640 27.154 0.00 34.30  ? 123 LEU A HD22 1 
ATOM   1889 H HD23 . LEU A 1 120 ? 5.438  41.682 26.969 0.00 34.30  ? 123 LEU A HD23 1 
ATOM   1890 N N    . VAL A 1 121 ? 7.099  45.663 25.132 1.00 17.27  ? 124 VAL A N    1 
ATOM   1891 C CA   . VAL A 1 121 ? 6.409  46.516 24.145 1.00 17.58  ? 124 VAL A CA   1 
ATOM   1892 C C    . VAL A 1 121 ? 7.421  47.288 23.331 1.00 18.16  ? 124 VAL A C    1 
ATOM   1893 O O    . VAL A 1 121 ? 7.338  47.245 22.095 1.00 19.50  ? 124 VAL A O    1 
ATOM   1894 C CB   . VAL A 1 121 ? 5.473  47.450 24.821 1.00 18.53  ? 124 VAL A CB   1 
ATOM   1895 C CG1  . VAL A 1 121 ? 4.900  48.492 23.808 1.00 21.37  ? 124 VAL A CG1  1 
ATOM   1896 C CG2  . VAL A 1 121 ? 4.264  46.701 25.459 1.00 22.21  ? 124 VAL A CG2  1 
ATOM   1897 H H    . VAL A 1 121 ? 6.899  45.839 25.949 0.00 20.73  ? 124 VAL A H    1 
ATOM   1898 H HA   . VAL A 1 121 ? 5.896  45.939 23.557 0.00 21.09  ? 124 VAL A HA   1 
ATOM   1899 H HB   . VAL A 1 121 ? 5.981  47.897 25.517 0.00 22.23  ? 124 VAL A HB   1 
ATOM   1900 H HG11 . VAL A 1 121 ? 4.130  48.927 24.205 0.00 25.64  ? 124 VAL A HG11 1 
ATOM   1901 H HG12 . VAL A 1 121 ? 5.585  49.149 23.609 0.00 25.64  ? 124 VAL A HG12 1 
ATOM   1902 H HG13 . VAL A 1 121 ? 4.638  48.031 22.996 0.00 25.64  ? 124 VAL A HG13 1 
ATOM   1903 H HG21 . VAL A 1 121 ? 3.685  47.348 25.891 0.00 26.66  ? 124 VAL A HG21 1 
ATOM   1904 H HG22 . VAL A 1 121 ? 3.777  46.236 24.761 0.00 26.66  ? 124 VAL A HG22 1 
ATOM   1905 H HG23 . VAL A 1 121 ? 4.595  46.065 26.112 0.00 26.66  ? 124 VAL A HG23 1 
ATOM   1906 N N    . GLY A 1 122 ? 8.429  47.792 23.948 1.00 18.48  ? 125 GLY A N    1 
ATOM   1907 C CA   . GLY A 1 122 ? 9.502  48.453 23.196 1.00 19.11  ? 125 GLY A CA   1 
ATOM   1908 C C    . GLY A 1 122 ? 10.226 47.532 22.243 1.00 20.43  ? 125 GLY A C    1 
ATOM   1909 O O    . GLY A 1 122 ? 10.544 47.928 21.100 1.00 21.20  ? 125 GLY A O    1 
ATOM   1910 H H    . GLY A 1 122 ? 8.543  47.780 24.800 0.00 22.18  ? 125 GLY A H    1 
ATOM   1911 H HA2  . GLY A 1 122 ? 9.123  49.182 22.680 0.00 22.93  ? 125 GLY A HA2  1 
ATOM   1912 H HA3  . GLY A 1 122 ? 10.152 48.811 23.820 0.00 22.93  ? 125 GLY A HA3  1 
ATOM   1913 N N    . ALA A 1 123 ? 10.501 46.281 22.626 1.00 18.16  ? 126 ALA A N    1 
ATOM   1914 C CA   . ALA A 1 123 ? 11.213 45.354 21.766 1.00 18.91  ? 126 ALA A CA   1 
ATOM   1915 C C    . ALA A 1 123 ? 10.385 44.950 20.548 1.00 19.77  ? 126 ALA A C    1 
ATOM   1916 O O    . ALA A 1 123 ? 10.948 44.626 19.524 1.00 21.90  ? 126 ALA A O    1 
ATOM   1917 C CB   . ALA A 1 123 ? 11.544 44.052 22.588 1.00 21.21  ? 126 ALA A CB   1 
ATOM   1918 H H    . ALA A 1 123 ? 10.281 45.947 23.387 0.00 21.79  ? 126 ALA A H    1 
ATOM   1919 H HA   . ALA A 1 123 ? 12.029 45.780 21.461 0.00 22.69  ? 126 ALA A HA   1 
ATOM   1920 H HB1  . ALA A 1 123 ? 12.022 43.431 22.017 0.00 25.45  ? 126 ALA A HB1  1 
ATOM   1921 H HB2  . ALA A 1 123 ? 12.094 44.292 23.350 0.00 25.45  ? 126 ALA A HB2  1 
ATOM   1922 H HB3  . ALA A 1 123 ? 10.715 43.651 22.892 0.00 25.45  ? 126 ALA A HB3  1 
ATOM   1923 N N    . LEU A 1 124 ? 9.054  44.984 20.636 1.00 19.56  ? 127 LEU A N    1 
ATOM   1924 C CA   . LEU A 1 124 ? 8.213  44.562 19.539 1.00 20.70  ? 127 LEU A CA   1 
ATOM   1925 C C    . LEU A 1 124 ? 7.545  45.723 18.755 1.00 20.61  ? 127 LEU A C    1 
ATOM   1926 O O    . LEU A 1 124 ? 6.801  45.462 17.798 1.00 23.40  ? 127 LEU A O    1 
ATOM   1927 C CB   . LEU A 1 124 ? 7.043  43.666 20.151 1.00 21.14  ? 127 LEU A CB   1 
ATOM   1928 C CG   . LEU A 1 124 ? 7.582  42.456 20.826 1.00 21.60  ? 127 LEU A CG   1 
ATOM   1929 C CD1  . LEU A 1 124 ? 6.390  41.602 21.416 1.00 30.35  ? 127 LEU A CD1  1 
ATOM   1930 C CD2  . LEU A 1 124 ? 8.308  41.549 19.856 1.00 24.85  ? 127 LEU A CD2  1 
ATOM   1931 H H    . LEU A 1 124 ? 8.622  45.251 21.330 0.00 23.47  ? 127 LEU A H    1 
ATOM   1932 H HA   . LEU A 1 124 ? 8.763  44.069 18.911 0.00 24.84  ? 127 LEU A HA   1 
ATOM   1933 H HB2  . LEU A 1 124 ? 6.550  44.187 20.804 0.00 25.37  ? 127 LEU A HB2  1 
ATOM   1934 H HB3  . LEU A 1 124 ? 6.451  43.382 19.438 0.00 25.37  ? 127 LEU A HB3  1 
ATOM   1935 H HG   . LEU A 1 124 ? 8.191  42.759 21.517 0.00 25.91  ? 127 LEU A HG   1 
ATOM   1936 H HD11 . LEU A 1 124 ? 6.753  40.828 21.874 0.00 36.43  ? 127 LEU A HD11 1 
ATOM   1937 H HD12 . LEU A 1 124 ? 5.888  42.149 22.039 0.00 36.43  ? 127 LEU A HD12 1 
ATOM   1938 H HD13 . LEU A 1 124 ? 5.815  41.317 20.688 0.00 36.43  ? 127 LEU A HD13 1 
ATOM   1939 H HD21 . LEU A 1 124 ? 8.460  40.690 20.280 0.00 29.83  ? 127 LEU A HD21 1 
ATOM   1940 H HD22 . LEU A 1 124 ? 7.763  41.434 19.062 0.00 29.83  ? 127 LEU A HD22 1 
ATOM   1941 H HD23 . LEU A 1 124 ? 9.157  41.955 19.619 0.00 29.83  ? 127 LEU A HD23 1 
ATOM   1942 N N    . THR A 1 125 ? 7.902  46.977 19.076 1.00 19.63  ? 128 THR A N    1 
ATOM   1943 C CA   . THR A 1 125 ? 7.310  48.150 18.411 1.00 19.74  ? 128 THR A CA   1 
ATOM   1944 C C    . THR A 1 125 ? 7.960  48.391 17.031 1.00 22.52  ? 128 THR A C    1 
ATOM   1945 O O    . THR A 1 125 ? 9.188  48.344 16.838 1.00 24.31  ? 128 THR A O    1 
ATOM   1946 C CB   . THR A 1 125 ? 7.537  49.337 19.369 1.00 19.82  ? 128 THR A CB   1 
ATOM   1947 O OG1  . THR A 1 125 ? 6.510  49.277 20.385 1.00 22.34  ? 128 THR A OG1  1 
ATOM   1948 C CG2  . THR A 1 125 ? 7.353  50.696 18.644 1.00 24.38  ? 128 THR A CG2  1 
ATOM   1949 H H    . THR A 1 125 ? 8.486  47.175 19.675 0.00 23.55  ? 128 THR A H    1 
ATOM   1950 H HA   . THR A 1 125 ? 6.364  48.034 18.231 0.00 23.69  ? 128 THR A HA   1 
ATOM   1951 H HB   . THR A 1 125 ? 8.435  49.290 19.732 0.00 23.79  ? 128 THR A HB   1 
ATOM   1952 H HG1  . THR A 1 125 ? 6.600  49.915 20.923 0.00 26.80  ? 128 THR A HG1  1 
ATOM   1953 H HG21 . THR A 1 125 ? 7.273  51.411 19.295 0.00 29.26  ? 128 THR A HG21 1 
ATOM   1954 H HG22 . THR A 1 125 ? 8.118  50.873 18.074 0.00 29.26  ? 128 THR A HG22 1 
ATOM   1955 H HG23 . THR A 1 125 ? 6.552  50.675 18.099 0.00 29.26  ? 128 THR A HG23 1 
ATOM   1956 N N    . LYS A 1 126 ? 7.136  48.572 16.028 1.00 22.37  ? 129 LYS A N    1 
ATOM   1957 C CA   . LYS A 1 126 ? 7.617  48.678 14.653 1.00 22.63  ? 129 LYS A CA   1 
ATOM   1958 C C    . LYS A 1 126 ? 7.963  50.100 14.241 1.00 23.98  ? 129 LYS A C    1 
ATOM   1959 O O    . LYS A 1 126 ? 8.660  50.253 13.217 1.00 31.35  ? 129 LYS A O    1 
ATOM   1960 C CB   . LYS A 1 126 ? 6.470  48.229 13.702 1.00 26.04  ? 129 LYS A CB   1 
ATOM   1961 C CG   . LYS A 1 126 ? 6.157  46.760 13.925 1.00 32.11  ? 129 LYS A CG   1 
ATOM   1962 C CD   . LYS A 1 126 ? 5.035  46.371 12.884 1.00 38.64  ? 129 LYS A CD   1 
ATOM   1963 C CE   . LYS A 1 126 ? 4.436  45.003 13.127 1.00 57.89  ? 129 LYS A CE   1 
ATOM   1964 N NZ   . LYS A 1 126 ? 5.463  43.919 13.119 1.00 70.46  ? 129 LYS A NZ   1 
ATOM   1965 H H    . LYS A 1 126 ? 6.282  48.640 16.108 0.00 26.84  ? 129 LYS A H    1 
ATOM   1966 H HA   . LYS A 1 126 ? 8.404  48.118 14.559 0.00 27.16  ? 129 LYS A HA   1 
ATOM   1967 H HB2  . LYS A 1 126 ? 5.672  48.750 13.886 0.00 31.25  ? 129 LYS A HB2  1 
ATOM   1968 H HB3  . LYS A 1 126 ? 6.743  48.354 12.780 0.00 31.25  ? 129 LYS A HB3  1 
ATOM   1969 H HG2  . LYS A 1 126 ? 6.946  46.218 13.769 0.00 38.54  ? 129 LYS A HG2  1 
ATOM   1970 H HG3  . LYS A 1 126 ? 5.828  46.616 14.826 0.00 38.54  ? 129 LYS A HG3  1 
ATOM   1971 H HD2  . LYS A 1 126 ? 4.319  47.023 12.938 0.00 46.37  ? 129 LYS A HD2  1 
ATOM   1972 H HD3  . LYS A 1 126 ? 5.420  46.373 11.994 0.00 46.37  ? 129 LYS A HD3  1 
ATOM   1973 H HE2  . LYS A 1 126 ? 3.999  44.998 13.993 0.00 69.47  ? 129 LYS A HE2  1 
ATOM   1974 H HE3  . LYS A 1 126 ? 3.790  44.811 12.429 0.00 69.47  ? 129 LYS A HE3  1 
ATOM   1975 H HZ1  . LYS A 1 126 ? 5.075  43.131 13.261 0.00 84.56  ? 129 LYS A HZ1  1 
ATOM   1976 H HZ2  . LYS A 1 126 ? 5.878  43.899 12.332 0.00 84.56  ? 129 LYS A HZ2  1 
ATOM   1977 H HZ3  . LYS A 1 126 ? 6.064  44.065 13.759 0.00 84.56  ? 129 LYS A HZ3  1 
ATOM   1978 N N    . VAL A 1 127 ? 7.586  51.130 15.005 1.00 22.45  ? 130 VAL A N    1 
ATOM   1979 C CA   . VAL A 1 127 ? 7.983  52.515 14.683 1.00 23.36  ? 130 VAL A CA   1 
ATOM   1980 C C    . VAL A 1 127 ? 9.274  52.793 15.472 1.00 24.12  ? 130 VAL A C    1 
ATOM   1981 O O    . VAL A 1 127 ? 9.259  52.789 16.711 1.00 24.46  ? 130 VAL A O    1 
ATOM   1982 C CB   . VAL A 1 127 ? 6.868  53.456 15.093 1.00 23.57  ? 130 VAL A CB   1 
ATOM   1983 C CG1  . VAL A 1 127 ? 7.317  54.933 14.789 1.00 26.92  ? 130 VAL A CG1  1 
ATOM   1984 C CG2  . VAL A 1 127 ? 5.557  53.189 14.358 1.00 28.79  ? 130 VAL A CG2  1 
ATOM   1985 H H    . VAL A 1 127 ? 7.103  51.057 15.712 0.00 26.94  ? 130 VAL A H    1 
ATOM   1986 H HA   . VAL A 1 127 ? 8.171  52.628 13.738 0.00 28.04  ? 130 VAL A HA   1 
ATOM   1987 H HB   . VAL A 1 127 ? 6.700  53.317 16.039 0.00 28.28  ? 130 VAL A HB   1 
ATOM   1988 H HG11 . VAL A 1 127 ? 6.551  55.522 14.882 0.00 32.31  ? 130 VAL A HG11 1 
ATOM   1989 H HG12 . VAL A 1 127 ? 8.009  55.189 15.418 0.00 32.31  ? 130 VAL A HG12 1 
ATOM   1990 H HG13 . VAL A 1 127 ? 7.660  54.978 13.883 0.00 32.31  ? 130 VAL A HG13 1 
ATOM   1991 H HG21 . VAL A 1 127 ? 4.891  53.827 14.658 0.00 34.54  ? 130 VAL A HG21 1 
ATOM   1992 H HG22 . VAL A 1 127 ? 5.704  53.289 13.404 0.00 34.54  ? 130 VAL A HG22 1 
ATOM   1993 H HG23 . VAL A 1 127 ? 5.262  52.286 14.554 0.00 34.54  ? 130 VAL A HG23 1 
ATOM   1994 N N    . TYR A 1 128 ? 10.375 53.007 14.792 1.00 24.48  ? 131 TYR A N    1 
ATOM   1995 C CA   . TYR A 1 128 ? 11.692 53.023 15.413 1.00 24.52  ? 131 TYR A CA   1 
ATOM   1996 C C    . TYR A 1 128 ? 11.770 54.015 16.551 1.00 23.59  ? 131 TYR A C    1 
ATOM   1997 O O    . TYR A 1 128 ? 12.242 53.651 17.626 1.00 22.92  ? 131 TYR A O    1 
ATOM   1998 C CB   . TYR A 1 128 ? 12.749 53.327 14.359 1.00 25.96  ? 131 TYR A CB   1 
ATOM   1999 C CG   . TYR A 1 128 ? 14.152 53.182 14.852 1.00 28.92  ? 131 TYR A CG   1 
ATOM   2000 C CD1  . TYR A 1 128 ? 14.614 51.990 15.321 1.00 31.08  ? 131 TYR A CD1  1 
ATOM   2001 C CD2  . TYR A 1 128 ? 15.014 54.278 14.871 1.00 33.38  ? 131 TYR A CD2  1 
ATOM   2002 C CE1  . TYR A 1 128 ? 15.990 51.856 15.767 1.00 31.96  ? 131 TYR A CE1  1 
ATOM   2003 C CE2  . TYR A 1 128 ? 16.333 54.173 15.303 1.00 34.13  ? 131 TYR A CE2  1 
ATOM   2004 C CZ   . TYR A 1 128 ? 16.796 52.952 15.742 1.00 34.16  ? 131 TYR A CZ   1 
ATOM   2005 O OH   . TYR A 1 128 ? 18.127 52.840 16.152 1.00 40.89  ? 131 TYR A OH   1 
ATOM   2006 H H    . TYR A 1 128 ? 10.397 53.151 13.944 0.00 29.38  ? 131 TYR A H    1 
ATOM   2007 H HA   . TYR A 1 128 ? 11.868 52.145 15.785 0.00 29.42  ? 131 TYR A HA   1 
ATOM   2008 H HB2  . TYR A 1 128 ? 12.632 52.715 13.615 0.00 31.15  ? 131 TYR A HB2  1 
ATOM   2009 H HB3  . TYR A 1 128 ? 12.635 54.241 14.057 0.00 31.15  ? 131 TYR A HB3  1 
ATOM   2010 H HD1  . TYR A 1 128 ? 14.045 51.256 15.356 0.00 37.29  ? 131 TYR A HD1  1 
ATOM   2011 H HD2  . TYR A 1 128 ? 14.697 55.105 14.586 0.00 40.06  ? 131 TYR A HD2  1 
ATOM   2012 H HE1  . TYR A 1 128 ? 16.314 51.036 16.064 0.00 38.35  ? 131 TYR A HE1  1 
ATOM   2013 H HE2  . TYR A 1 128 ? 16.893 54.916 15.295 0.00 40.96  ? 131 TYR A HE2  1 
ATOM   2014 H HH   . TYR A 1 128 ? 18.581 53.469 15.829 0.00 49.07  ? 131 TYR A HH   1 
ATOM   2015 N N    A SER A 1 129 ? 11.348 55.286 16.321 0.49 26.66  ? 132 SER A N    1 
ATOM   2016 N N    B SER A 1 129 ? 11.347 55.283 16.337 0.51 26.70  ? 132 SER A N    1 
ATOM   2017 C CA   A SER A 1 129 ? 11.506 56.291 17.374 0.49 27.19  ? 132 SER A CA   1 
ATOM   2018 C CA   B SER A 1 129 ? 11.524 56.265 17.411 0.51 27.08  ? 132 SER A CA   1 
ATOM   2019 C C    A SER A 1 129 ? 10.727 55.949 18.631 0.49 24.58  ? 132 SER A C    1 
ATOM   2020 C C    B SER A 1 129 ? 10.743 55.905 18.657 0.51 24.61  ? 132 SER A C    1 
ATOM   2021 O O    A SER A 1 129 ? 11.157 56.286 19.754 0.49 25.06  ? 132 SER A O    1 
ATOM   2022 O O    B SER A 1 129 ? 11.185 56.186 19.797 0.51 24.89  ? 132 SER A O    1 
ATOM   2023 C CB   A SER A 1 129 ? 11.074 57.677 16.841 0.49 28.45  ? 132 SER A CB   1 
ATOM   2024 C CB   B SER A 1 129 ? 11.072 57.644 16.908 0.51 28.50  ? 132 SER A CB   1 
ATOM   2025 O OG   A SER A 1 129 ? 9.696  57.704 16.509 0.49 30.67  ? 132 SER A OG   1 
ATOM   2026 O OG   B SER A 1 129 ? 11.926 58.027 15.863 0.51 34.95  ? 132 SER A OG   1 
ATOM   2027 H H    A SER A 1 129 ? 10.985 55.568 15.594 0.49 31.99  ? 132 SER A H    1 
ATOM   2028 H H    B SER A 1 129 ? 10.978 55.575 15.617 0.51 32.04  ? 132 SER A H    1 
ATOM   2029 H HA   A SER A 1 129 ? 12.444 56.328 17.619 0.49 32.63  ? 132 SER A HA   1 
ATOM   2030 H HA   B SER A 1 129 ? 12.464 56.295 17.649 0.51 32.50  ? 132 SER A HA   1 
ATOM   2031 H HB2  A SER A 1 129 ? 11.244 58.342 17.527 0.49 34.14  ? 132 SER A HB2  1 
ATOM   2032 H HB2  B SER A 1 129 ? 10.160 57.590 16.582 0.51 34.20  ? 132 SER A HB2  1 
ATOM   2033 H HB3  A SER A 1 129 ? 11.591 57.881 16.046 0.49 34.14  ? 132 SER A HB3  1 
ATOM   2034 H HB3  B SER A 1 129 ? 11.129 58.289 17.630 0.51 34.20  ? 132 SER A HB3  1 
ATOM   2035 H HG   A SER A 1 129 ? 9.466  58.485 16.304 0.49 36.80  ? 132 SER A HG   1 
ATOM   2036 H HG   B SER A 1 129 ? 11.586 58.663 15.433 0.51 41.95  ? 132 SER A HG   1 
ATOM   2037 N N    . TYR A 1 130 ? 9.601  55.229 18.487 1.00 22.83  ? 133 TYR A N    1 
ATOM   2038 C CA   . TYR A 1 130 ? 8.804  54.912 19.684 1.00 22.20  ? 133 TYR A CA   1 
ATOM   2039 C C    . TYR A 1 130 ? 9.429  53.813 20.523 1.00 21.94  ? 133 TYR A C    1 
ATOM   2040 O O    . TYR A 1 130 ? 9.118  53.726 21.712 1.00 21.10  ? 133 TYR A O    1 
ATOM   2041 C CB   . TYR A 1 130 ? 7.415  54.459 19.245 1.00 21.33  ? 133 TYR A CB   1 
ATOM   2042 C CG   . TYR A 1 130 ? 6.514  55.472 18.609 1.00 25.47  ? 133 TYR A CG   1 
ATOM   2043 C CD1  . TYR A 1 130 ? 6.826  56.793 18.596 1.00 24.74  ? 133 TYR A CD1  1 
ATOM   2044 C CD2  . TYR A 1 130 ? 5.332  55.032 17.995 1.00 28.77  ? 133 TYR A CD2  1 
ATOM   2045 C CE1  . TYR A 1 130 ? 5.940  57.722 17.917 1.00 31.25  ? 133 TYR A CE1  1 
ATOM   2046 C CE2  . TYR A 1 130 ? 4.479  55.869 17.360 1.00 34.45  ? 133 TYR A CE2  1 
ATOM   2047 C CZ   . TYR A 1 130 ? 4.804  57.207 17.323 1.00 30.27  ? 133 TYR A CZ   1 
ATOM   2048 O OH   . TYR A 1 130 ? 3.929  58.136 16.678 1.00 41.92  ? 133 TYR A OH   1 
ATOM   2049 H H    . TYR A 1 130 ? 9.293  54.929 17.742 0.00 27.40  ? 133 TYR A H    1 
ATOM   2050 H HA   . TYR A 1 130 ? 8.732  55.708 20.233 0.00 26.64  ? 133 TYR A HA   1 
ATOM   2051 H HB2  . TYR A 1 130 ? 7.528  53.743 18.600 0.00 25.60  ? 133 TYR A HB2  1 
ATOM   2052 H HB3  . TYR A 1 130 ? 6.951  54.128 20.030 0.00 25.60  ? 133 TYR A HB3  1 
ATOM   2053 H HD1  . TYR A 1 130 ? 7.596  57.100 19.017 0.00 29.69  ? 133 TYR A HD1  1 
ATOM   2054 H HD2  . TYR A 1 130 ? 5.126  54.126 18.027 0.00 34.52  ? 133 TYR A HD2  1 
ATOM   2055 H HE1  . TYR A 1 130 ? 6.132  58.632 17.883 0.00 37.50  ? 133 TYR A HE1  1 
ATOM   2056 H HE2  . TYR A 1 130 ? 3.700  55.551 16.963 0.00 41.35  ? 133 TYR A HE2  1 
ATOM   2057 H HH   . TYR A 1 130 ? 3.295  57.725 16.311 0.00 50.30  ? 133 TYR A HH   1 
ATOM   2058 N N    . ARG A 1 131 ? 10.365 53.021 20.002 1.00 19.48  ? 134 ARG A N    1 
ATOM   2059 C CA   . ARG A 1 131 ? 11.023 52.013 20.821 1.00 18.45  ? 134 ARG A CA   1 
ATOM   2060 C C    . ARG A 1 131 ? 11.689 52.666 21.994 1.00 22.13  ? 134 ARG A C    1 
ATOM   2061 O O    . ARG A 1 131 ? 11.738 52.099 23.102 1.00 20.91  ? 134 ARG A O    1 
ATOM   2062 C CB   . ARG A 1 131 ? 11.994 51.212 19.973 1.00 21.03  ? 134 ARG A CB   1 
ATOM   2063 C CG   . ARG A 1 131 ? 11.293 50.503 18.766 1.00 22.78  ? 134 ARG A CG   1 
ATOM   2064 C CD   . ARG A 1 131 ? 12.329 49.770 17.858 1.00 23.63  ? 134 ARG A CD   1 
ATOM   2065 N NE   . ARG A 1 131 ? 13.055 48.674 18.495 1.00 23.42  ? 134 ARG A NE   1 
ATOM   2066 C CZ   . ARG A 1 131 ? 12.557 47.441 18.613 1.00 22.49  ? 134 ARG A CZ   1 
ATOM   2067 N NH1  . ARG A 1 131 ? 11.366 47.091 18.087 1.00 22.01  ? 134 ARG A NH1  1 
ATOM   2068 N NH2  . ARG A 1 131 ? 13.295 46.530 19.222 1.00 22.92  ? 134 ARG A NH2  1 
ATOM   2069 H H    . ARG A 1 131 ? 10.633 53.048 19.186 0.00 23.38  ? 134 ARG A H    1 
ATOM   2070 H HA   . ARG A 1 131 ? 10.375 51.378 21.166 0.00 22.14  ? 134 ARG A HA   1 
ATOM   2071 H HB2  . ARG A 1 131 ? 12.672 51.809 19.619 0.00 25.24  ? 134 ARG A HB2  1 
ATOM   2072 H HB3  . ARG A 1 131 ? 12.408 50.530 20.524 0.00 25.24  ? 134 ARG A HB3  1 
ATOM   2073 H HG2  . ARG A 1 131 ? 10.662 49.847 19.101 0.00 27.34  ? 134 ARG A HG2  1 
ATOM   2074 H HG3  . ARG A 1 131 ? 10.830 51.165 18.229 0.00 27.34  ? 134 ARG A HG3  1 
ATOM   2075 H HD2  . ARG A 1 131 ? 11.858 49.400 17.095 0.00 28.36  ? 134 ARG A HD2  1 
ATOM   2076 H HD3  . ARG A 1 131 ? 12.987 50.418 17.560 0.00 28.36  ? 134 ARG A HD3  1 
ATOM   2077 H HE   . ARG A 1 131 ? 13.840 48.831 18.809 0.00 28.10  ? 134 ARG A HE   1 
ATOM   2078 H HH11 . ARG A 1 131 ? 10.898 47.671 17.658 0.00 26.41  ? 134 ARG A HH11 1 
ATOM   2079 H HH12 . ARG A 1 131 ? 11.074 46.287 18.181 0.00 26.41  ? 134 ARG A HH12 1 
ATOM   2080 H HH21 . ARG A 1 131 ? 14.070 46.740 19.529 0.00 27.50  ? 134 ARG A HH21 1 
ATOM   2081 H HH22 . ARG A 1 131 ? 12.999 45.728 19.312 0.00 27.50  ? 134 ARG A HH22 1 
ATOM   2082 N N    . PHE A 1 132 ? 12.255 53.876 21.778 1.00 20.30  ? 135 PHE A N    1 
ATOM   2083 C CA   . PHE A 1 132 ? 13.006 54.548 22.815 1.00 21.38  ? 135 PHE A CA   1 
ATOM   2084 C C    . PHE A 1 132 ? 12.123 55.214 23.825 1.00 21.13  ? 135 PHE A C    1 
ATOM   2085 O O    . PHE A 1 132 ? 12.560 55.392 24.971 1.00 20.94  ? 135 PHE A O    1 
ATOM   2086 C CB   . PHE A 1 132 ? 13.988 55.555 22.160 1.00 21.22  ? 135 PHE A CB   1 
ATOM   2087 C CG   . PHE A 1 132 ? 14.957 54.851 21.227 1.00 21.57  ? 135 PHE A CG   1 
ATOM   2088 C CD1  . PHE A 1 132 ? 16.042 54.133 21.745 1.00 23.37  ? 135 PHE A CD1  1 
ATOM   2089 C CD2  . PHE A 1 132 ? 14.686 54.869 19.886 1.00 26.56  ? 135 PHE A CD2  1 
ATOM   2090 C CE1  . PHE A 1 132 ? 16.895 53.493 20.835 1.00 29.45  ? 135 PHE A CE1  1 
ATOM   2091 C CE2  . PHE A 1 132 ? 15.509 54.189 19.005 1.00 28.79  ? 135 PHE A CE2  1 
ATOM   2092 C CZ   . PHE A 1 132 ? 16.629 53.516 19.468 1.00 28.69  ? 135 PHE A CZ   1 
ATOM   2093 H H    . PHE A 1 132 ? 12.209 54.311 21.038 0.00 24.36  ? 135 PHE A H    1 
ATOM   2094 H HA   . PHE A 1 132 ? 13.541 53.907 23.308 0.00 25.66  ? 135 PHE A HA   1 
ATOM   2095 H HB2  . PHE A 1 132 ? 13.485 56.206 21.646 0.00 25.46  ? 135 PHE A HB2  1 
ATOM   2096 H HB3  . PHE A 1 132 ? 14.499 56.002 22.852 0.00 25.46  ? 135 PHE A HB3  1 
ATOM   2097 H HD1  . PHE A 1 132 ? 16.191 54.082 22.661 0.00 28.04  ? 135 PHE A HD1  1 
ATOM   2098 H HD2  . PHE A 1 132 ? 13.949 55.338 19.566 0.00 31.87  ? 135 PHE A HD2  1 
ATOM   2099 H HE1  . PHE A 1 132 ? 17.649 53.046 21.148 0.00 35.34  ? 135 PHE A HE1  1 
ATOM   2100 H HE2  . PHE A 1 132 ? 15.309 54.183 18.097 0.00 34.55  ? 135 PHE A HE2  1 
ATOM   2101 H HZ   . PHE A 1 132 ? 17.197 53.085 18.872 0.00 34.43  ? 135 PHE A HZ   1 
ATOM   2102 N N    . VAL A 1 133 ? 10.869 55.530 23.475 1.00 19.91  ? 136 VAL A N    1 
ATOM   2103 C CA   . VAL A 1 133 ? 9.901  55.982 24.479 1.00 20.37  ? 136 VAL A CA   1 
ATOM   2104 C C    . VAL A 1 133 ? 9.676  54.894 25.490 1.00 20.56  ? 136 VAL A C    1 
ATOM   2105 O O    . VAL A 1 133 ? 9.649  55.142 26.716 1.00 19.19  ? 136 VAL A O    1 
ATOM   2106 C CB   . VAL A 1 133 ? 8.617  56.416 23.737 1.00 21.33  ? 136 VAL A CB   1 
ATOM   2107 C CG1  . VAL A 1 133 ? 7.536  56.783 24.742 1.00 25.53  ? 136 VAL A CG1  1 
ATOM   2108 C CG2  . VAL A 1 133 ? 8.845  57.670 22.893 1.00 25.56  ? 136 VAL A CG2  1 
ATOM   2109 H H    . VAL A 1 133 ? 10.559 55.492 22.674 0.00 23.89  ? 136 VAL A H    1 
ATOM   2110 H HA   . VAL A 1 133 ? 10.234 56.745 24.976 0.00 24.45  ? 136 VAL A HA   1 
ATOM   2111 H HB   . VAL A 1 133 ? 8.354  55.672 23.173 0.00 25.60  ? 136 VAL A HB   1 
ATOM   2112 H HG11 . VAL A 1 133 ? 6.815  57.237 24.279 0.00 30.64  ? 136 VAL A HG11 1 
ATOM   2113 H HG12 . VAL A 1 133 ? 7.203  55.973 25.159 0.00 30.64  ? 136 VAL A HG12 1 
ATOM   2114 H HG13 . VAL A 1 133 ? 7.917  57.369 25.415 0.00 30.64  ? 136 VAL A HG13 1 
ATOM   2115 H HG21 . VAL A 1 133 ? 8.011  57.920 22.466 0.00 30.67  ? 136 VAL A HG21 1 
ATOM   2116 H HG22 . VAL A 1 133 ? 9.149  58.388 23.470 0.00 30.67  ? 136 VAL A HG22 1 
ATOM   2117 H HG23 . VAL A 1 133 ? 9.517  57.480 22.220 0.00 30.67  ? 136 VAL A HG23 1 
ATOM   2118 N N    . TRP A 1 134 ? 9.447  53.668 25.028 1.00 19.05  ? 137 TRP A N    1 
ATOM   2119 C CA   . TRP A 1 134 ? 9.178  52.580 25.982 1.00 17.45  ? 137 TRP A CA   1 
ATOM   2120 C C    . TRP A 1 134 ? 10.443 52.302 26.765 1.00 18.02  ? 137 TRP A C    1 
ATOM   2121 O O    . TRP A 1 134 ? 10.323 52.014 27.995 1.00 18.38  ? 137 TRP A O    1 
ATOM   2122 C CB   . TRP A 1 134 ? 8.758  51.355 25.147 1.00 17.37  ? 137 TRP A CB   1 
ATOM   2123 C CG   . TRP A 1 134 ? 7.407  51.565 24.554 1.00 18.12  ? 137 TRP A CG   1 
ATOM   2124 C CD1  . TRP A 1 134 ? 7.124  51.711 23.215 1.00 17.95  ? 137 TRP A CD1  1 
ATOM   2125 C CD2  . TRP A 1 134 ? 6.150  51.714 25.230 1.00 18.36  ? 137 TRP A CD2  1 
ATOM   2126 N NE1  . TRP A 1 134 ? 5.796  51.928 23.017 1.00 19.42  ? 137 TRP A NE1  1 
ATOM   2127 C CE2  . TRP A 1 134 ? 5.134  51.896 24.244 1.00 19.01  ? 137 TRP A CE2  1 
ATOM   2128 C CE3  . TRP A 1 134 ? 5.791  51.652 26.606 1.00 20.20  ? 137 TRP A CE3  1 
ATOM   2129 C CZ2  . TRP A 1 134 ? 3.758  52.061 24.562 1.00 21.97  ? 137 TRP A CZ2  1 
ATOM   2130 C CZ3  . TRP A 1 134 ? 4.413  51.770 26.889 1.00 22.95  ? 137 TRP A CZ3  1 
ATOM   2131 C CH2  . TRP A 1 134 ? 3.455  52.011 25.905 1.00 23.53  ? 137 TRP A CH2  1 
ATOM   2132 H H    . TRP A 1 134 ? 9.440  53.441 24.198 0.00 22.86  ? 137 TRP A H    1 
ATOM   2133 H HA   . TRP A 1 134 ? 8.470  52.793 26.611 0.00 20.94  ? 137 TRP A HA   1 
ATOM   2134 H HB2  . TRP A 1 134 ? 9.394  51.220 24.427 0.00 20.84  ? 137 TRP A HB2  1 
ATOM   2135 H HB3  . TRP A 1 134 ? 8.728  50.569 25.715 0.00 20.84  ? 137 TRP A HB3  1 
ATOM   2136 H HD1  . TRP A 1 134 ? 7.757  51.666 22.535 0.00 21.54  ? 137 TRP A HD1  1 
ATOM   2137 H HE1  . TRP A 1 134 ? 5.423  52.065 22.254 0.00 23.31  ? 137 TRP A HE1  1 
ATOM   2138 H HE3  . TRP A 1 134 ? 6.426  51.541 27.276 0.00 24.24  ? 137 TRP A HE3  1 
ATOM   2139 H HZ2  . TRP A 1 134 ? 3.108  52.192 23.910 0.00 26.37  ? 137 TRP A HZ2  1 
ATOM   2140 H HZ3  . TRP A 1 134 ? 4.132  51.684 27.772 0.00 27.54  ? 137 TRP A HZ3  1 
ATOM   2141 H HH2  . TRP A 1 134 ? 2.573  52.145 26.167 0.00 28.24  ? 137 TRP A HH2  1 
ATOM   2142 N N    . TRP A 1 135 ? 11.624 52.377 26.151 1.00 18.20  ? 138 TRP A N    1 
ATOM   2143 C CA   . TRP A 1 135 ? 12.868 52.213 26.942 1.00 19.20  ? 138 TRP A CA   1 
ATOM   2144 C C    . TRP A 1 135 ? 12.934 53.220 28.061 1.00 18.50  ? 138 TRP A C    1 
ATOM   2145 O O    . TRP A 1 135 ? 13.330 52.830 29.206 1.00 19.25  ? 138 TRP A O    1 
ATOM   2146 C CB   . TRP A 1 135 ? 14.058 52.330 25.971 1.00 19.73  ? 138 TRP A CB   1 
ATOM   2147 C CG   . TRP A 1 135 ? 15.399 52.265 26.680 1.00 17.55  ? 138 TRP A CG   1 
ATOM   2148 C CD1  . TRP A 1 135 ? 16.170 51.133 26.879 1.00 20.28  ? 138 TRP A CD1  1 
ATOM   2149 C CD2  . TRP A 1 135 ? 16.123 53.329 27.274 1.00 18.72  ? 138 TRP A CD2  1 
ATOM   2150 N NE1  . TRP A 1 135 ? 17.324 51.438 27.533 1.00 22.07  ? 138 TRP A NE1  1 
ATOM   2151 C CE2  . TRP A 1 135 ? 17.309 52.794 27.778 1.00 21.77  ? 138 TRP A CE2  1 
ATOM   2152 C CE3  . TRP A 1 135 ? 15.900 54.722 27.367 1.00 23.12  ? 138 TRP A CE3  1 
ATOM   2153 C CZ2  . TRP A 1 135 ? 18.282 53.530 28.387 1.00 26.92  ? 138 TRP A CZ2  1 
ATOM   2154 C CZ3  . TRP A 1 135 ? 16.919 55.491 28.017 1.00 27.93  ? 138 TRP A CZ3  1 
ATOM   2155 C CH2  . TRP A 1 135 ? 18.034 54.884 28.548 1.00 30.04  ? 138 TRP A CH2  1 
ATOM   2156 H H    . TRP A 1 135 ? 11.741 52.516 25.310 0.00 21.84  ? 138 TRP A H    1 
ATOM   2157 H HA   . TRP A 1 135 ? 12.903 51.341 27.366 0.00 23.04  ? 138 TRP A HA   1 
ATOM   2158 H HB2  . TRP A 1 135 ? 14.019 51.600 25.334 0.00 23.67  ? 138 TRP A HB2  1 
ATOM   2159 H HB3  . TRP A 1 135 ? 14.004 53.179 25.506 0.00 23.67  ? 138 TRP A HB3  1 
ATOM   2160 H HD1  . TRP A 1 135 ? 15.932 50.278 26.603 0.00 24.34  ? 138 TRP A HD1  1 
ATOM   2161 H HE1  . TRP A 1 135 ? 17.947 50.887 27.752 0.00 26.49  ? 138 TRP A HE1  1 
ATOM   2162 H HE3  . TRP A 1 135 ? 15.132 55.119 27.024 0.00 27.74  ? 138 TRP A HE3  1 
ATOM   2163 H HZ2  . TRP A 1 135 ? 19.075 53.142 28.679 0.00 32.31  ? 138 TRP A HZ2  1 
ATOM   2164 H HZ3  . TRP A 1 135 ? 16.826 56.414 28.081 0.00 33.52  ? 138 TRP A HZ3  1 
ATOM   2165 H HH2  . TRP A 1 135 ? 18.640 55.398 29.031 0.00 36.05  ? 138 TRP A HH2  1 
ATOM   2166 N N    . ALA A 1 136 ? 12.518 54.478 27.826 1.00 18.57  ? 139 ALA A N    1 
ATOM   2167 C CA   . ALA A 1 136 ? 12.617 55.496 28.905 1.00 19.57  ? 139 ALA A CA   1 
ATOM   2168 C C    . ALA A 1 136 ? 11.636 55.184 30.032 1.00 20.31  ? 139 ALA A C    1 
ATOM   2169 O O    . ALA A 1 136 ? 11.988 55.390 31.228 1.00 21.58  ? 139 ALA A O    1 
ATOM   2170 C CB   . ALA A 1 136 ? 12.376 56.858 28.318 1.00 20.86  ? 139 ALA A CB   1 
ATOM   2171 H H    . ALA A 1 136 ? 12.188 54.763 27.085 0.00 22.28  ? 139 ALA A H    1 
ATOM   2172 H HA   . ALA A 1 136 ? 13.508 55.493 29.290 0.00 23.48  ? 139 ALA A HA   1 
ATOM   2173 H HB1  . ALA A 1 136 ? 12.444 57.522 29.022 0.00 25.04  ? 139 ALA A HB1  1 
ATOM   2174 H HB2  . ALA A 1 136 ? 13.044 57.030 27.636 0.00 25.04  ? 139 ALA A HB2  1 
ATOM   2175 H HB3  . ALA A 1 136 ? 11.490 56.880 27.926 0.00 25.04  ? 139 ALA A HB3  1 
ATOM   2176 N N    . ILE A 1 137 ? 10.374 54.799 29.718 1.00 18.68  ? 140 ILE A N    1 
ATOM   2177 C CA   . ILE A 1 137 ? 9.433  54.491 30.770 1.00 19.82  ? 140 ILE A CA   1 
ATOM   2178 C C    . ILE A 1 137 ? 9.951  53.281 31.549 1.00 19.88  ? 140 ILE A C    1 
ATOM   2179 O O    . ILE A 1 137 ? 9.882  53.308 32.816 1.00 19.57  ? 140 ILE A O    1 
ATOM   2180 C CB   . ILE A 1 137 ? 8.099  54.174 30.100 1.00 18.77  ? 140 ILE A CB   1 
ATOM   2181 C CG1  . ILE A 1 137 ? 7.583  55.468 29.508 1.00 21.11  ? 140 ILE A CG1  1 
ATOM   2182 C CG2  . ILE A 1 137 ? 7.146  53.581 31.159 1.00 24.22  ? 140 ILE A CG2  1 
ATOM   2183 C CD1  . ILE A 1 137 ? 6.399  55.254 28.495 1.00 26.28  ? 140 ILE A CD1  1 
ATOM   2184 H H    . ILE A 1 137 ? 10.066 54.716 28.919 0.00 22.42  ? 140 ILE A H    1 
ATOM   2185 H HA   . ILE A 1 137 ? 9.328  55.234 31.384 0.00 23.78  ? 140 ILE A HA   1 
ATOM   2186 H HB   . ILE A 1 137 ? 8.183  53.519 29.389 0.00 22.53  ? 140 ILE A HB   1 
ATOM   2187 H HG12 . ILE A 1 137 ? 7.263  56.037 30.226 0.00 25.33  ? 140 ILE A HG12 1 
ATOM   2188 H HG13 . ILE A 1 137 ? 8.306  55.907 29.034 0.00 25.33  ? 140 ILE A HG13 1 
ATOM   2189 H HG21 . ILE A 1 137 ? 6.233  53.664 30.844 0.00 29.07  ? 140 ILE A HG21 1 
ATOM   2190 H HG22 . ILE A 1 137 ? 7.366  52.646 31.294 0.00 29.07  ? 140 ILE A HG22 1 
ATOM   2191 H HG23 . ILE A 1 137 ? 7.255  54.070 31.990 0.00 29.07  ? 140 ILE A HG23 1 
ATOM   2192 H HD11 . ILE A 1 137 ? 6.141  56.112 28.124 0.00 31.53  ? 140 ILE A HD11 1 
ATOM   2193 H HD12 . ILE A 1 137 ? 6.693  54.662 27.786 0.00 31.53  ? 140 ILE A HD12 1 
ATOM   2194 H HD13 . ILE A 1 137 ? 5.648  54.858 28.966 0.00 31.53  ? 140 ILE A HD13 1 
ATOM   2195 N N    . SER A 1 138 ? 10.476 52.258 30.893 1.00 17.26  ? 141 SER A N    1 
ATOM   2196 C CA   . SER A 1 138 ? 10.992 51.087 31.628 1.00 17.72  ? 141 SER A CA   1 
ATOM   2197 C C    . SER A 1 138 ? 12.168 51.454 32.514 1.00 19.17  ? 141 SER A C    1 
ATOM   2198 O O    . SER A 1 138 ? 12.254 50.975 33.680 1.00 19.73  ? 141 SER A O    1 
ATOM   2199 C CB   . SER A 1 138 ? 11.395 50.112 30.550 1.00 18.40  ? 141 SER A CB   1 
ATOM   2200 O OG   . SER A 1 138 ? 11.963 48.902 31.147 1.00 19.23  ? 141 SER A OG   1 
ATOM   2201 H H    . SER A 1 138 ? 10.549 52.206 30.038 0.00 20.71  ? 141 SER A H    1 
ATOM   2202 H HA   . SER A 1 138 ? 10.331 50.702 32.224 0.00 21.26  ? 141 SER A HA   1 
ATOM   2203 H HB2  . SER A 1 138 ? 10.612 49.872 30.029 0.00 22.08  ? 141 SER A HB2  1 
ATOM   2204 H HB3  . SER A 1 138 ? 12.059 50.526 29.978 0.00 22.08  ? 141 SER A HB3  1 
ATOM   2205 H HG   . SER A 1 138 ? 11.400 48.540 31.654 0.00 23.07  ? 141 SER A HG   1 
ATOM   2206 N N    . THR A 1 139 ? 13.032 52.331 32.043 1.00 18.30  ? 142 THR A N    1 
ATOM   2207 C CA   . THR A 1 139 ? 14.190 52.771 32.841 1.00 20.11  ? 142 THR A CA   1 
ATOM   2208 C C    . THR A 1 139 ? 13.698 53.556 34.049 1.00 20.91  ? 142 THR A C    1 
ATOM   2209 O O    . THR A 1 139 ? 14.294 53.415 35.152 1.00 21.89  ? 142 THR A O    1 
ATOM   2210 C CB   . THR A 1 139 ? 15.117 53.600 31.924 1.00 19.54  ? 142 THR A CB   1 
ATOM   2211 O OG1  . THR A 1 139 ? 15.666 52.682 30.947 1.00 21.66  ? 142 THR A OG1  1 
ATOM   2212 C CG2  . THR A 1 139 ? 16.326 54.107 32.699 1.00 25.58  ? 142 THR A CG2  1 
ATOM   2213 H H    . THR A 1 139 ? 12.982 52.695 31.266 0.00 21.96  ? 142 THR A H    1 
ATOM   2214 H HA   . THR A 1 139 ? 14.712 52.025 33.176 0.00 24.13  ? 142 THR A HA   1 
ATOM   2215 H HB   . THR A 1 139 ? 14.623 54.341 31.541 0.00 23.45  ? 142 THR A HB   1 
ATOM   2216 H HG1  . THR A 1 139 ? 15.047 52.343 30.492 0.00 25.99  ? 142 THR A HG1  1 
ATOM   2217 H HG21 . THR A 1 139 ? 16.967 54.504 32.089 0.00 30.70  ? 142 THR A HG21 1 
ATOM   2218 H HG22 . THR A 1 139 ? 16.049 54.775 33.345 0.00 30.70  ? 142 THR A HG22 1 
ATOM   2219 H HG23 . THR A 1 139 ? 16.751 53.372 33.168 0.00 30.70  ? 142 THR A HG23 1 
ATOM   2220 N N    . ALA A 1 140 ? 12.641 54.388 33.891 1.00 20.62  ? 143 ALA A N    1 
ATOM   2221 C CA   . ALA A 1 140 ? 12.132 55.115 35.053 1.00 21.95  ? 143 ALA A CA   1 
ATOM   2222 C C    . ALA A 1 140 ? 11.609 54.114 36.088 1.00 21.69  ? 143 ALA A C    1 
ATOM   2223 O O    . ALA A 1 140 ? 11.863 54.370 37.313 1.00 23.07  ? 143 ALA A O    1 
ATOM   2224 C CB   . ALA A 1 140 ? 11.022 56.083 34.623 1.00 23.87  ? 143 ALA A CB   1 
ATOM   2225 H H    . ALA A 1 140 ? 12.226 54.534 33.152 0.00 24.74  ? 143 ALA A H    1 
ATOM   2226 H HA   . ALA A 1 140 ? 12.840 55.645 35.452 0.00 26.35  ? 143 ALA A HA   1 
ATOM   2227 H HB1  . ALA A 1 140 ? 10.707 56.569 35.401 0.00 28.65  ? 143 ALA A HB1  1 
ATOM   2228 H HB2  . ALA A 1 140 ? 11.380 56.703 33.968 0.00 28.65  ? 143 ALA A HB2  1 
ATOM   2229 H HB3  . ALA A 1 140 ? 10.293 55.575 34.233 0.00 28.65  ? 143 ALA A HB3  1 
ATOM   2230 N N    . ALA A 1 141 ? 10.938 53.044 35.709 1.00 19.70  ? 144 ALA A N    1 
ATOM   2231 C CA   . ALA A 1 141 ? 10.499 52.046 36.676 1.00 19.97  ? 144 ALA A CA   1 
ATOM   2232 C C    . ALA A 1 141 ? 11.715 51.333 37.337 1.00 20.93  ? 144 ALA A C    1 
ATOM   2233 O O    . ALA A 1 141 ? 11.717 51.170 38.568 1.00 22.01  ? 144 ALA A O    1 
ATOM   2234 C CB   . ALA A 1 141 ? 9.683  50.940 35.987 1.00 18.93  ? 144 ALA A CB   1 
ATOM   2235 H H    . ALA A 1 141 ? 10.720 52.866 34.896 0.00 23.64  ? 144 ALA A H    1 
ATOM   2236 H HA   . ALA A 1 141 ? 9.958  52.510 37.334 0.00 23.97  ? 144 ALA A HA   1 
ATOM   2237 H HB1  . ALA A 1 141 ? 9.396  50.297 36.655 0.00 22.72  ? 144 ALA A HB1  1 
ATOM   2238 H HB2  . ALA A 1 141 ? 8.910  51.338 35.558 0.00 22.72  ? 144 ALA A HB2  1 
ATOM   2239 H HB3  . ALA A 1 141 ? 10.240 50.502 35.325 0.00 22.72  ? 144 ALA A HB3  1 
ATOM   2240 N N    . MET A 1 142 ? 12.788 51.039 36.603 1.00 21.39  ? 145 MET A N    1 
ATOM   2241 C CA   . MET A 1 142 ? 13.998 50.492 37.246 1.00 20.13  ? 145 MET A CA   1 
ATOM   2242 C C    . MET A 1 142 ? 14.559 51.457 38.228 1.00 22.35  ? 145 MET A C    1 
ATOM   2243 O O    . MET A 1 142 ? 14.984 51.017 39.317 1.00 23.97  ? 145 MET A O    1 
ATOM   2244 C CB   . MET A 1 142 ? 15.092 50.293 36.153 1.00 21.60  ? 145 MET A CB   1 
ATOM   2245 C CG   . MET A 1 142 ? 16.152 49.245 36.595 1.00 23.48  ? 145 MET A CG   1 
ATOM   2246 S SD   . MET A 1 142 ? 17.664 49.259 35.662 1.00 26.78  ? 145 MET A SD   1 
ATOM   2247 C CE   . MET A 1 142 ? 18.179 50.934 35.741 1.00 29.54  ? 145 MET A CE   1 
ATOM   2248 H H    . MET A 1 142 ? 12.848 51.142 35.751 0.00 25.67  ? 145 MET A H    1 
ATOM   2249 H HA   . MET A 1 142 ? 13.765 49.654 37.675 0.00 24.15  ? 145 MET A HA   1 
ATOM   2250 H HB2  . MET A 1 142 ? 14.675 49.980 35.335 0.00 25.92  ? 145 MET A HB2  1 
ATOM   2251 H HB3  . MET A 1 142 ? 15.544 51.137 35.994 0.00 25.92  ? 145 MET A HB3  1 
ATOM   2252 H HG2  . MET A 1 142 ? 16.383 49.414 37.522 0.00 28.18  ? 145 MET A HG2  1 
ATOM   2253 H HG3  . MET A 1 142 ? 15.765 48.360 36.506 0.00 28.18  ? 145 MET A HG3  1 
ATOM   2254 H HE1  . MET A 1 142 ? 19.040 51.021 35.305 0.00 35.45  ? 145 MET A HE1  1 
ATOM   2255 H HE2  . MET A 1 142 ? 17.522 51.488 35.290 0.00 35.45  ? 145 MET A HE2  1 
ATOM   2256 H HE3  . MET A 1 142 ? 18.251 51.199 36.672 0.00 35.45  ? 145 MET A HE3  1 
ATOM   2257 N N    . LEU A 1 143 ? 14.632 52.794 37.930 1.00 21.81  ? 146 LEU A N    1 
ATOM   2258 C CA   . LEU A 1 143 ? 15.164 53.745 38.920 1.00 23.65  ? 146 LEU A CA   1 
ATOM   2259 C C    . LEU A 1 143 ? 14.324 53.775 40.192 1.00 22.62  ? 146 LEU A C    1 
ATOM   2260 O O    . LEU A 1 143 ? 14.900 53.962 41.288 1.00 25.20  ? 146 LEU A O    1 
ATOM   2261 C CB   . LEU A 1 143 ? 15.268 55.092 38.241 1.00 26.67  ? 146 LEU A CB   1 
ATOM   2262 C CG   . LEU A 1 143 ? 16.314 55.158 37.094 1.00 30.01  ? 146 LEU A CG   1 
ATOM   2263 C CD1  . LEU A 1 143 ? 16.188 56.507 36.429 1.00 34.63  ? 146 LEU A CD1  1 
ATOM   2264 C CD2  . LEU A 1 143 ? 17.729 54.945 37.640 1.00 36.04  ? 146 LEU A CD2  1 
ATOM   2265 H H    . LEU A 1 143 ? 14.386 53.148 37.186 0.00 26.17  ? 146 LEU A H    1 
ATOM   2266 H HA   . LEU A 1 143 ? 16.049 53.482 39.215 0.00 28.38  ? 146 LEU A HA   1 
ATOM   2267 H HB2  . LEU A 1 143 ? 14.403 55.314 37.863 0.00 32.01  ? 146 LEU A HB2  1 
ATOM   2268 H HB3  . LEU A 1 143 ? 15.519 55.752 38.906 0.00 32.01  ? 146 LEU A HB3  1 
ATOM   2269 H HG   . LEU A 1 143 ? 16.156 54.458 36.442 0.00 36.01  ? 146 LEU A HG   1 
ATOM   2270 H HD11 . LEU A 1 143 ? 16.838 56.567 35.711 0.00 41.55  ? 146 LEU A HD11 1 
ATOM   2271 H HD12 . LEU A 1 143 ? 15.291 56.601 36.072 0.00 41.55  ? 146 LEU A HD12 1 
ATOM   2272 H HD13 . LEU A 1 143 ? 16.357 57.200 37.086 0.00 41.55  ? 146 LEU A HD13 1 
ATOM   2273 H HD21 . LEU A 1 143 ? 18.372 55.171 36.950 0.00 43.25  ? 146 LEU A HD21 1 
ATOM   2274 H HD22 . LEU A 1 143 ? 17.859 55.517 38.413 0.00 43.25  ? 146 LEU A HD22 1 
ATOM   2275 H HD23 . LEU A 1 143 ? 17.832 54.015 37.896 0.00 43.25  ? 146 LEU A HD23 1 
ATOM   2276 N N    . TYR A 1 144 ? 12.999 53.624 40.099 1.00 22.34  ? 147 TYR A N    1 
ATOM   2277 C CA   . TYR A 1 144 ? 12.216 53.523 41.316 1.00 22.59  ? 147 TYR A CA   1 
ATOM   2278 C C    . TYR A 1 144 ? 12.637 52.313 42.114 1.00 21.79  ? 147 TYR A C    1 
ATOM   2279 O O    . TYR A 1 144 ? 12.775 52.421 43.347 1.00 23.50  ? 147 TYR A O    1 
ATOM   2280 C CB   . TYR A 1 144 ? 10.690 53.452 40.896 1.00 23.79  ? 147 TYR A CB   1 
ATOM   2281 C CG   . TYR A 1 144 ? 9.801  53.301 42.113 1.00 26.67  ? 147 TYR A CG   1 
ATOM   2282 C CD1  . TYR A 1 144 ? 9.489  54.381 42.859 1.00 30.41  ? 147 TYR A CD1  1 
ATOM   2283 C CD2  . TYR A 1 144 ? 9.405  52.061 42.521 1.00 27.64  ? 147 TYR A CD2  1 
ATOM   2284 C CE1  . TYR A 1 144 ? 8.756  54.225 44.019 1.00 32.40  ? 147 TYR A CE1  1 
ATOM   2285 C CE2  . TYR A 1 144 ? 8.665  51.886 43.702 1.00 33.08  ? 147 TYR A CE2  1 
ATOM   2286 C CZ   . TYR A 1 144 ? 8.351  52.976 44.387 1.00 32.94  ? 147 TYR A CZ   1 
ATOM   2287 O OH   . TYR A 1 144 ? 7.607  52.901 45.590 1.00 39.49  ? 147 TYR A OH   1 
ATOM   2288 H H    . TYR A 1 144 ? 12.551 53.580 39.366 0.00 26.81  ? 147 TYR A H    1 
ATOM   2289 H HA   . TYR A 1 144 ? 12.348 54.297 41.886 0.00 27.11  ? 147 TYR A HA   1 
ATOM   2290 H HB2  . TYR A 1 144 ? 10.444 54.268 40.433 0.00 28.55  ? 147 TYR A HB2  1 
ATOM   2291 H HB3  . TYR A 1 144 ? 10.551 52.687 40.315 0.00 28.55  ? 147 TYR A HB3  1 
ATOM   2292 H HD1  . TYR A 1 144 ? 9.767  55.228 42.593 0.00 36.50  ? 147 TYR A HD1  1 
ATOM   2293 H HD2  . TYR A 1 144 ? 9.629  51.318 42.009 0.00 33.17  ? 147 TYR A HD2  1 
ATOM   2294 H HE1  . TYR A 1 144 ? 8.541  54.962 44.543 0.00 38.88  ? 147 TYR A HE1  1 
ATOM   2295 H HE2  . TYR A 1 144 ? 8.405  51.041 43.990 0.00 39.70  ? 147 TYR A HE2  1 
ATOM   2296 H HH   . TYR A 1 144 ? 7.384  52.106 45.741 0.00 47.39  ? 147 TYR A HH   1 
ATOM   2297 N N    . ILE A 1 145 ? 12.766 51.147 41.475 1.00 21.29  ? 148 ILE A N    1 
ATOM   2298 C CA   . ILE A 1 145 ? 13.168 49.939 42.204 1.00 21.70  ? 148 ILE A CA   1 
ATOM   2299 C C    . ILE A 1 145 ? 14.532 50.152 42.890 1.00 24.81  ? 148 ILE A C    1 
ATOM   2300 O O    . ILE A 1 145 ? 14.711 49.857 44.103 1.00 25.11  ? 148 ILE A O    1 
ATOM   2301 C CB   . ILE A 1 145 ? 13.257 48.779 41.204 1.00 21.72  ? 148 ILE A CB   1 
ATOM   2302 C CG1  . ILE A 1 145 ? 11.827 48.396 40.832 1.00 22.95  ? 148 ILE A CG1  1 
ATOM   2303 C CG2  . ILE A 1 145 ? 13.976 47.568 41.852 1.00 25.38  ? 148 ILE A CG2  1 
ATOM   2304 C CD1  . ILE A 1 145 ? 11.835 47.523 39.553 1.00 28.75  ? 148 ILE A CD1  1 
ATOM   2305 H H    . ILE A 1 145 ? 12.629 51.029 40.635 0.00 25.55  ? 148 ILE A H    1 
ATOM   2306 H HA   . ILE A 1 145 ? 12.510 49.745 42.890 0.00 26.04  ? 148 ILE A HA   1 
ATOM   2307 H HB   . ILE A 1 145 ? 13.762 49.045 40.419 0.00 26.07  ? 148 ILE A HB   1 
ATOM   2308 H HG12 . ILE A 1 145 ? 11.425 47.889 41.555 0.00 27.54  ? 148 ILE A HG12 1 
ATOM   2309 H HG13 . ILE A 1 145 ? 11.308 49.197 40.660 0.00 27.54  ? 148 ILE A HG13 1 
ATOM   2310 H HG21 . ILE A 1 145 ? 13.792 46.774 41.327 0.00 30.45  ? 148 ILE A HG21 1 
ATOM   2311 H HG22 . ILE A 1 145 ? 14.930 47.739 41.870 0.00 30.45  ? 148 ILE A HG22 1 
ATOM   2312 H HG23 . ILE A 1 145 ? 13.644 47.450 42.756 0.00 30.45  ? 148 ILE A HG23 1 
ATOM   2313 H HD11 . ILE A 1 145 ? 10.922 47.400 39.249 0.00 34.50  ? 148 ILE A HD11 1 
ATOM   2314 H HD12 . ILE A 1 145 ? 12.355 47.971 38.868 0.00 34.50  ? 148 ILE A HD12 1 
ATOM   2315 H HD13 . ILE A 1 145 ? 12.233 46.663 39.761 0.00 34.50  ? 148 ILE A HD13 1 
ATOM   2316 N N    . LEU A 1 146 ? 15.486 50.749 42.188 1.00 24.90  ? 149 LEU A N    1 
ATOM   2317 C CA   . LEU A 1 146 ? 16.804 50.937 42.802 1.00 26.51  ? 149 LEU A CA   1 
ATOM   2318 C C    . LEU A 1 146 ? 16.745 51.942 43.959 1.00 27.54  ? 149 LEU A C    1 
ATOM   2319 O O    . LEU A 1 146 ? 17.419 51.758 45.007 1.00 29.90  ? 149 LEU A O    1 
ATOM   2320 C CB   . LEU A 1 146 ? 17.831 51.396 41.752 1.00 30.76  ? 149 LEU A CB   1 
ATOM   2321 C CG   . LEU A 1 146 ? 17.973 50.434 40.570 1.00 36.26  ? 149 LEU A CG   1 
ATOM   2322 C CD1  . LEU A 1 146 ? 19.147 50.965 39.674 1.00 41.16  ? 149 LEU A CD1  1 
ATOM   2323 C CD2  . LEU A 1 146 ? 18.194 49.004 40.979 1.00 38.39  ? 149 LEU A CD2  1 
ATOM   2324 H H    . LEU A 1 146 ? 15.405 51.045 41.384 0.00 29.88  ? 149 LEU A H    1 
ATOM   2325 H HA   . LEU A 1 146 ? 17.097 50.082 43.154 0.00 31.81  ? 149 LEU A HA   1 
ATOM   2326 H HB2  . LEU A 1 146 ? 17.555 52.258 41.403 0.00 36.92  ? 149 LEU A HB2  1 
ATOM   2327 H HB3  . LEU A 1 146 ? 18.698 51.473 42.179 0.00 36.92  ? 149 LEU A HB3  1 
ATOM   2328 H HG   . LEU A 1 146 ? 17.142 50.411 40.070 0.00 43.51  ? 149 LEU A HG   1 
ATOM   2329 H HD11 . LEU A 1 146 ? 19.255 50.374 38.912 0.00 49.39  ? 149 LEU A HD11 1 
ATOM   2330 H HD12 . LEU A 1 146 ? 18.931 51.861 39.370 0.00 49.39  ? 149 LEU A HD12 1 
ATOM   2331 H HD13 . LEU A 1 146 ? 19.962 50.981 40.199 0.00 49.39  ? 149 LEU A HD13 1 
ATOM   2332 H HD21 . LEU A 1 146 ? 18.440 48.486 40.196 0.00 46.07  ? 149 LEU A HD21 1 
ATOM   2333 H HD22 . LEU A 1 146 ? 18.908 48.969 41.635 0.00 46.07  ? 149 LEU A HD22 1 
ATOM   2334 H HD23 . LEU A 1 146 ? 17.375 48.655 41.362 0.00 46.07  ? 149 LEU A HD23 1 
ATOM   2335 N N    . TYR A 1 147 ? 15.904 52.987 43.832 1.00 25.63  ? 150 TYR A N    1 
ATOM   2336 C CA   . TYR A 1 147 ? 15.706 53.934 44.955 1.00 28.26  ? 150 TYR A CA   1 
ATOM   2337 C C    . TYR A 1 147 ? 15.159 53.207 46.202 1.00 28.62  ? 150 TYR A C    1 
ATOM   2338 O O    . TYR A 1 147 ? 15.633 53.398 47.330 1.00 30.71  ? 150 TYR A O    1 
ATOM   2339 C CB   . TYR A 1 147 ? 14.707 54.992 44.499 1.00 30.53  ? 150 TYR A CB   1 
ATOM   2340 C CG   . TYR A 1 147 ? 14.415 55.944 45.596 1.00 37.54  ? 150 TYR A CG   1 
ATOM   2341 C CD1  . TYR A 1 147 ? 15.256 57.005 45.843 1.00 48.34  ? 150 TYR A CD1  1 
ATOM   2342 C CD2  . TYR A 1 147 ? 13.292 55.772 46.389 1.00 46.39  ? 150 TYR A CD2  1 
ATOM   2343 C CE1  . TYR A 1 147 ? 14.989 57.873 46.871 1.00 53.66  ? 150 TYR A CE1  1 
ATOM   2344 C CE2  . TYR A 1 147 ? 13.007 56.645 47.432 1.00 48.44  ? 150 TYR A CE2  1 
ATOM   2345 C CZ   . TYR A 1 147 ? 13.859 57.685 47.662 1.00 50.48  ? 150 TYR A CZ   1 
ATOM   2346 O OH   . TYR A 1 147 ? 13.590 58.566 48.687 1.00 63.04  ? 150 TYR A OH   1 
ATOM   2347 H H    . TYR A 1 147 ? 15.447 53.169 43.126 0.00 30.75  ? 150 TYR A H    1 
ATOM   2348 H HA   . TYR A 1 147 ? 16.550 54.348 45.195 0.00 33.91  ? 150 TYR A HA   1 
ATOM   2349 H HB2  . TYR A 1 147 ? 15.079 55.487 43.751 0.00 36.64  ? 150 TYR A HB2  1 
ATOM   2350 H HB3  . TYR A 1 147 ? 13.879 54.562 44.233 0.00 36.64  ? 150 TYR A HB3  1 
ATOM   2351 H HD1  . TYR A 1 147 ? 16.008 57.135 45.311 0.00 58.00  ? 150 TYR A HD1  1 
ATOM   2352 H HD2  . TYR A 1 147 ? 12.719 55.060 46.220 0.00 55.67  ? 150 TYR A HD2  1 
ATOM   2353 H HE1  . TYR A 1 147 ? 15.562 58.586 47.040 0.00 64.40  ? 150 TYR A HE1  1 
ATOM   2354 H HE2  . TYR A 1 147 ? 12.252 56.523 47.962 0.00 58.13  ? 150 TYR A HE2  1 
ATOM   2355 H HH   . TYR A 1 147 ? 12.883 58.342 49.080 0.00 75.65  ? 150 TYR A HH   1 
ATOM   2356 N N    . VAL A 1 148 ? 14.170 52.345 46.038 1.00 27.06  ? 151 VAL A N    1 
ATOM   2357 C CA   . VAL A 1 148 ? 13.627 51.654 47.208 1.00 28.83  ? 151 VAL A CA   1 
ATOM   2358 C C    . VAL A 1 148 ? 14.692 50.731 47.805 1.00 28.48  ? 151 VAL A C    1 
ATOM   2359 O O    . VAL A 1 148 ? 14.828 50.612 49.033 1.00 32.21  ? 151 VAL A O    1 
ATOM   2360 C CB   . VAL A 1 148 ? 12.369 50.888 46.779 1.00 29.60  ? 151 VAL A CB   1 
ATOM   2361 C CG1  . VAL A 1 148 ? 11.876 49.947 47.896 1.00 31.10  ? 151 VAL A CG1  1 
ATOM   2362 C CG2  . VAL A 1 148 ? 11.272 51.861 46.346 1.00 31.79  ? 151 VAL A CG2  1 
ATOM   2363 H H    . VAL A 1 148 ? 13.802 52.144 45.287 0.00 32.47  ? 151 VAL A H    1 
ATOM   2364 H HA   . VAL A 1 148 ? 13.380 52.293 47.894 0.00 34.60  ? 151 VAL A HA   1 
ATOM   2365 H HB   . VAL A 1 148 ? 12.592 50.331 46.017 0.00 35.52  ? 151 VAL A HB   1 
ATOM   2366 H HG11 . VAL A 1 148 ? 10.966 49.674 47.700 0.00 37.32  ? 151 VAL A HG11 1 
ATOM   2367 H HG12 . VAL A 1 148 ? 12.454 49.169 47.931 0.00 37.32  ? 151 VAL A HG12 1 
ATOM   2368 H HG13 . VAL A 1 148 ? 11.905 50.419 48.742 0.00 37.32  ? 151 VAL A HG13 1 
ATOM   2369 H HG21 . VAL A 1 148 ? 10.483 51.356 46.094 0.00 38.15  ? 151 VAL A HG21 1 
ATOM   2370 H HG22 . VAL A 1 148 ? 11.064 52.452 47.087 0.00 38.15  ? 151 VAL A HG22 1 
ATOM   2371 H HG23 . VAL A 1 148 ? 11.589 52.379 45.590 0.00 38.15  ? 151 VAL A HG23 1 
ATOM   2372 N N    . LEU A 1 149 ? 15.447 50.034 46.973 1.00 27.79  ? 152 LEU A N    1 
ATOM   2373 C CA   . LEU A 1 149 ? 16.430 49.100 47.514 1.00 30.52  ? 152 LEU A CA   1 
ATOM   2374 C C    . LEU A 1 149 ? 17.477 49.853 48.328 1.00 36.45  ? 152 LEU A C    1 
ATOM   2375 O O    . LEU A 1 149 ? 18.006 49.299 49.324 1.00 37.20  ? 152 LEU A O    1 
ATOM   2376 C CB   . LEU A 1 149 ? 17.106 48.319 46.418 1.00 31.69  ? 152 LEU A CB   1 
ATOM   2377 C CG   . LEU A 1 149 ? 16.188 47.372 45.682 1.00 34.50  ? 152 LEU A CG   1 
ATOM   2378 C CD1  . LEU A 1 149 ? 17.048 46.573 44.635 1.00 37.28  ? 152 LEU A CD1  1 
ATOM   2379 C CD2  . LEU A 1 149 ? 15.549 46.387 46.638 1.00 36.58  ? 152 LEU A CD2  1 
ATOM   2380 H H    . LEU A 1 149 ? 15.414 50.078 46.114 0.00 33.34  ? 152 LEU A H    1 
ATOM   2381 H HA   . LEU A 1 149 ? 15.971 48.459 48.079 0.00 36.62  ? 152 LEU A HA   1 
ATOM   2382 H HB2  . LEU A 1 149 ? 17.468 48.944 45.770 0.00 38.03  ? 152 LEU A HB2  1 
ATOM   2383 H HB3  . LEU A 1 149 ? 17.822 47.793 46.808 0.00 38.03  ? 152 LEU A HB3  1 
ATOM   2384 H HG   . LEU A 1 149 ? 15.481 47.873 45.244 0.00 41.40  ? 152 LEU A HG   1 
ATOM   2385 H HD11 . LEU A 1 149 ? 16.470 45.966 44.148 0.00 44.74  ? 152 LEU A HD11 1 
ATOM   2386 H HD12 . LEU A 1 149 ? 17.462 47.201 44.022 0.00 44.74  ? 152 LEU A HD12 1 
ATOM   2387 H HD13 . LEU A 1 149 ? 17.732 46.071 45.106 0.00 44.74  ? 152 LEU A HD13 1 
ATOM   2388 H HD21 . LEU A 1 149 ? 15.135 45.673 46.127 0.00 43.89  ? 152 LEU A HD21 1 
ATOM   2389 H HD22 . LEU A 1 149 ? 16.234 46.022 47.220 0.00 43.89  ? 152 LEU A HD22 1 
ATOM   2390 H HD23 . LEU A 1 149 ? 14.878 46.848 47.165 0.00 43.89  ? 152 LEU A HD23 1 
ATOM   2391 N N    . PHE A 1 150 ? 17.748 51.155 48.034 1.00 34.88  ? 153 PHE A N    1 
ATOM   2392 C CA   . PHE A 1 150 ? 18.732 51.948 48.840 1.00 39.00  ? 153 PHE A CA   1 
ATOM   2393 C C    . PHE A 1 150 ? 18.140 52.852 49.902 1.00 44.52  ? 153 PHE A C    1 
ATOM   2394 O O    . PHE A 1 150 ? 18.818 53.173 50.930 1.00 50.12  ? 153 PHE A O    1 
ATOM   2395 C CB   . PHE A 1 150 ? 19.477 52.863 47.889 1.00 43.91  ? 153 PHE A CB   1 
ATOM   2396 C CG   . PHE A 1 150 ? 20.626 52.228 47.250 1.00 47.25  ? 153 PHE A CG   1 
ATOM   2397 C CD1  . PHE A 1 150 ? 21.782 52.053 47.982 1.00 46.74  ? 153 PHE A CD1  1 
ATOM   2398 C CD2  . PHE A 1 150 ? 20.559 51.778 45.942 1.00 48.92  ? 153 PHE A CD2  1 
ATOM   2399 C CE1  . PHE A 1 150 ? 22.870 51.445 47.428 1.00 56.64  ? 153 PHE A CE1  1 
ATOM   2400 C CE2  . PHE A 1 150 ? 21.671 51.178 45.370 1.00 54.59  ? 153 PHE A CE2  1 
ATOM   2401 C CZ   . PHE A 1 150 ? 22.827 51.009 46.144 1.00 48.91  ? 153 PHE A CZ   1 
ATOM   2402 H H    . PHE A 1 150 ? 17.385 51.593 47.389 0.00 41.86  ? 153 PHE A H    1 
ATOM   2403 H HA   . PHE A 1 150 ? 19.315 51.316 49.289 0.00 46.80  ? 153 PHE A HA   1 
ATOM   2404 H HB2  . PHE A 1 150 ? 18.869 53.150 47.190 0.00 52.69  ? 153 PHE A HB2  1 
ATOM   2405 H HB3  . PHE A 1 150 ? 19.800 53.632 48.384 0.00 52.69  ? 153 PHE A HB3  1 
ATOM   2406 H HD1  . PHE A 1 150 ? 21.820 52.353 48.862 0.00 56.09  ? 153 PHE A HD1  1 
ATOM   2407 H HD2  . PHE A 1 150 ? 19.775 51.877 45.451 0.00 58.70  ? 153 PHE A HD2  1 
ATOM   2408 H HE1  . PHE A 1 150 ? 23.643 51.328 47.931 0.00 67.97  ? 153 PHE A HE1  1 
ATOM   2409 H HE2  . PHE A 1 150 ? 21.651 50.892 44.486 0.00 65.51  ? 153 PHE A HE2  1 
ATOM   2410 H HZ   . PHE A 1 150 ? 23.572 50.594 45.774 0.00 58.70  ? 153 PHE A HZ   1 
ATOM   2411 N N    . PHE A 1 151 ? 16.933 53.328 49.724 1.00 46.77  ? 154 PHE A N    1 
ATOM   2412 C CA   . PHE A 1 151 ? 16.394 54.290 50.674 1.00 47.86  ? 154 PHE A CA   1 
ATOM   2413 C C    . PHE A 1 151 ? 15.166 53.762 51.393 1.00 67.06  ? 154 PHE A C    1 
ATOM   2414 O O    . PHE A 1 151 ? 14.626 54.456 52.264 1.00 72.91  ? 154 PHE A O    1 
ATOM   2415 C CB   . PHE A 1 151 ? 16.133 55.623 49.959 1.00 48.64  ? 154 PHE A CB   1 
ATOM   2416 C CG   . PHE A 1 151 ? 17.389 56.234 49.347 1.00 44.03  ? 154 PHE A CG   1 
ATOM   2417 C CD1  . PHE A 1 151 ? 17.849 55.890 48.106 1.00 58.72  ? 154 PHE A CD1  1 
ATOM   2418 C CD2  . PHE A 1 151 ? 18.136 57.164 50.109 1.00 49.59  ? 154 PHE A CD2  1 
ATOM   2419 C CE1  . PHE A 1 151 ? 18.998 56.451 47.577 1.00 54.31  ? 154 PHE A CE1  1 
ATOM   2420 C CE2  . PHE A 1 151 ? 19.293 57.724 49.580 1.00 59.97  ? 154 PHE A CE2  1 
ATOM   2421 C CZ   . PHE A 1 151 ? 19.728 57.367 48.312 1.00 59.17  ? 154 PHE A CZ   1 
ATOM   2422 H H    . PHE A 1 151 ? 16.409 53.118 49.075 0.00 56.13  ? 154 PHE A H    1 
ATOM   2423 H HA   . PHE A 1 151 ? 17.041 54.489 51.369 0.00 57.44  ? 154 PHE A HA   1 
ATOM   2424 H HB2  . PHE A 1 151 ? 15.494 55.476 49.244 0.00 58.37  ? 154 PHE A HB2  1 
ATOM   2425 H HB3  . PHE A 1 151 ? 15.775 56.258 50.599 0.00 58.37  ? 154 PHE A HB3  1 
ATOM   2426 H HD1  . PHE A 1 151 ? 17.378 55.263 47.606 0.00 70.47  ? 154 PHE A HD1  1 
ATOM   2427 H HD2  . PHE A 1 151 ? 17.853 57.401 50.963 0.00 59.50  ? 154 PHE A HD2  1 
ATOM   2428 H HE1  . PHE A 1 151 ? 19.281 56.211 46.724 0.00 65.17  ? 154 PHE A HE1  1 
ATOM   2429 H HE2  . PHE A 1 151 ? 19.778 58.341 50.079 0.00 71.97  ? 154 PHE A HE2  1 
ATOM   2430 H HZ   . PHE A 1 151 ? 20.504 57.740 47.960 0.00 71.00  ? 154 PHE A HZ   1 
ATOM   2431 N N    . GLY A 1 152 ? 14.730 52.548 51.074 1.00 72.39  ? 155 GLY A N    1 
ATOM   2432 C CA   . GLY A 1 152 ? 13.771 51.829 51.888 1.00 71.27  ? 155 GLY A CA   1 
ATOM   2433 C C    . GLY A 1 152 ? 14.423 50.654 52.599 1.00 69.15  ? 155 GLY A C    1 
ATOM   2434 O O    . GLY A 1 152 ? 14.383 50.543 53.824 1.00 72.31  ? 155 GLY A O    1 
ATOM   2435 H H    . GLY A 1 152 ? 14.983 52.113 50.376 0.00 86.87  ? 155 GLY A H    1 
ATOM   2436 H HA2  . GLY A 1 152 ? 13.397 52.427 52.554 0.00 85.52  ? 155 GLY A HA2  1 
ATOM   2437 H HA3  . GLY A 1 152 ? 13.054 51.494 51.327 0.00 85.52  ? 155 GLY A HA3  1 
ATOM   2438 N N    . PHE A 1 153 ? 15.070 49.782 51.835 1.00 64.25  ? 156 PHE A N    1 
ATOM   2439 C CA   . PHE A 1 153 ? 15.525 48.512 52.397 1.00 61.53  ? 156 PHE A CA   1 
ATOM   2440 C C    . PHE A 1 153 ? 16.771 48.678 53.259 1.00 83.34  ? 156 PHE A C    1 
ATOM   2441 O O    . PHE A 1 153 ? 16.877 48.047 54.319 1.00 72.88  ? 156 PHE A O    1 
ATOM   2442 C CB   . PHE A 1 153 ? 15.841 47.528 51.281 1.00 56.06  ? 156 PHE A CB   1 
ATOM   2443 C CG   . PHE A 1 153 ? 14.655 46.842 50.729 1.00 51.88  ? 156 PHE A CG   1 
ATOM   2444 C CD1  . PHE A 1 153 ? 13.397 47.371 50.889 1.00 58.22  ? 156 PHE A CD1  1 
ATOM   2445 C CD2  . PHE A 1 153 ? 14.806 45.655 50.069 1.00 52.29  ? 156 PHE A CD2  1 
ATOM   2446 C CE1  . PHE A 1 153 ? 12.322 46.737 50.386 1.00 50.21  ? 156 PHE A CE1  1 
ATOM   2447 C CE2  . PHE A 1 153 ? 13.714 44.995 49.572 1.00 55.10  ? 156 PHE A CE2  1 
ATOM   2448 C CZ   . PHE A 1 153 ? 12.464 45.548 49.735 1.00 51.09  ? 156 PHE A CZ   1 
ATOM   2449 H H    . PHE A 1 153 ? 15.257 49.897 51.004 0.00 77.09  ? 156 PHE A H    1 
ATOM   2450 H HA   . PHE A 1 153 ? 14.806 48.161 52.945 0.00 73.83  ? 156 PHE A HA   1 
ATOM   2451 H HB2  . PHE A 1 153 ? 16.268 48.009 50.555 0.00 67.28  ? 156 PHE A HB2  1 
ATOM   2452 H HB3  . PHE A 1 153 ? 16.440 46.848 51.627 0.00 67.28  ? 156 PHE A HB3  1 
ATOM   2453 H HD1  . PHE A 1 153 ? 13.287 48.172 51.349 0.00 69.87  ? 156 PHE A HD1  1 
ATOM   2454 H HD2  . PHE A 1 153 ? 15.655 45.293 49.957 0.00 62.74  ? 156 PHE A HD2  1 
ATOM   2455 H HE1  . PHE A 1 153 ? 11.477 47.112 50.484 0.00 60.25  ? 156 PHE A HE1  1 
ATOM   2456 H HE2  . PHE A 1 153 ? 13.816 44.183 49.130 0.00 66.12  ? 156 PHE A HE2  1 
ATOM   2457 H HZ   . PHE A 1 153 ? 11.715 45.110 49.400 0.00 61.31  ? 156 PHE A HZ   1 
ATOM   2458 N N    . THR A 1 154 ? 17.739 49.490 52.801 1.00 72.77  ? 157 THR A N    1 
ATOM   2459 C CA   . THR A 1 154 ? 19.007 49.608 53.517 1.00 86.04  ? 157 THR A CA   1 
ATOM   2460 C C    . THR A 1 154 ? 18.782 50.053 54.961 1.00 94.75  ? 157 THR A C    1 
ATOM   2461 O O    . THR A 1 154 ? 19.430 49.540 55.880 1.00 82.44  ? 157 THR A O    1 
ATOM   2462 C CB   . THR A 1 154 ? 19.954 50.556 52.759 1.00 78.48  ? 157 THR A CB   1 
ATOM   2463 O OG1  . THR A 1 154 ? 20.341 49.950 51.503 1.00 68.53  ? 157 THR A OG1  1 
ATOM   2464 C CG2  . THR A 1 154 ? 21.197 50.896 53.606 1.00 81.74  ? 157 THR A CG2  1 
ATOM   2465 H H    . THR A 1 154 ? 17.682 49.971 52.090 0.00 87.32  ? 157 THR A H    1 
ATOM   2466 H HA   . THR A 1 154 ? 19.442 48.742 53.552 0.00 103.25 ? 157 THR A HA   1 
ATOM   2467 H HB   . THR A 1 154 ? 19.498 51.393 52.576 0.00 94.18  ? 157 THR A HB   1 
ATOM   2468 H HG1  . THR A 1 154 ? 19.659 49.786 51.041 0.00 82.24  ? 157 THR A HG1  1 
ATOM   2469 H HG21 . THR A 1 154 ? 21.872 51.317 53.051 0.00 98.09  ? 157 THR A HG21 1 
ATOM   2470 H HG22 . THR A 1 154 ? 20.955 51.505 54.322 0.00 98.09  ? 157 THR A HG22 1 
ATOM   2471 H HG23 . THR A 1 154 ? 21.567 50.087 53.993 0.00 98.09  ? 157 THR A HG23 1 
ATOM   2472 N N    . SER A 1 155 ? 17.827 50.963 55.181 1.00 110.84 ? 158 SER A N    1 
ATOM   2473 C CA   . SER A 1 155 ? 17.575 51.495 56.518 1.00 120.92 ? 158 SER A CA   1 
ATOM   2474 C C    . SER A 1 155 ? 16.886 50.490 57.441 1.00 119.86 ? 158 SER A C    1 
ATOM   2475 O O    . SER A 1 155 ? 16.946 50.656 58.664 1.00 122.59 ? 158 SER A O    1 
ATOM   2476 C CB   . SER A 1 155 ? 16.752 52.786 56.420 1.00 127.15 ? 158 SER A CB   1 
ATOM   2477 O OG   . SER A 1 155 ? 15.462 52.543 55.879 1.00 130.69 ? 158 SER A OG   1 
ATOM   2478 H H    . SER A 1 155 ? 17.313 51.288 54.573 0.00 133.00 ? 158 SER A H    1 
ATOM   2479 H HA   . SER A 1 155 ? 18.427 51.714 56.926 0.00 145.10 ? 158 SER A HA   1 
ATOM   2480 N N    . LYS A 1 156 ? 16.231 49.459 56.897 1.00 96.97  ? 159 LYS A N    1 
ATOM   2481 C CA   . LYS A 1 156 ? 15.627 48.443 57.755 1.00 97.40  ? 159 LYS A CA   1 
ATOM   2482 C C    . LYS A 1 156 ? 16.614 47.340 58.115 1.00 93.78  ? 159 LYS A C    1 
ATOM   2483 O O    . LYS A 1 156 ? 16.657 46.904 59.270 1.00 92.74  ? 159 LYS A O    1 
ATOM   2484 C CB   . LYS A 1 156 ? 14.383 47.845 57.093 1.00 88.54  ? 159 LYS A CB   1 
ATOM   2485 C CG   . LYS A 1 156 ? 13.562 46.968 58.031 1.00 89.39  ? 159 LYS A CG   1 
ATOM   2486 C CD   . LYS A 1 156 ? 12.069 47.148 57.803 1.00 78.83  ? 159 LYS A CD   1 
ATOM   2487 C CE   . LYS A 1 156 ? 11.266 46.471 58.896 1.00 85.37  ? 159 LYS A CE   1 
ATOM   2488 N NZ   . LYS A 1 156 ? 11.419 44.994 58.820 1.00 72.32  ? 159 LYS A NZ   1 
ATOM   2489 H H    . LYS A 1 156 ? 16.126 49.330 56.054 0.00 116.37 ? 159 LYS A H    1 
ATOM   2490 H HA   . LYS A 1 156 ? 15.337 48.867 58.578 0.00 116.88 ? 159 LYS A HA   1 
ATOM   2491 H HB2  . LYS A 1 156 ? 13.813 48.568 56.786 0.00 106.24 ? 159 LYS A HB2  1 
ATOM   2492 H HB3  . LYS A 1 156 ? 14.660 47.299 56.341 0.00 106.24 ? 159 LYS A HB3  1 
ATOM   2493 H HG2  . LYS A 1 156 ? 13.783 46.037 57.875 0.00 107.27 ? 159 LYS A HG2  1 
ATOM   2494 H HG3  . LYS A 1 156 ? 13.760 47.208 58.949 0.00 107.27 ? 159 LYS A HG3  1 
ATOM   2495 H HD2  . LYS A 1 156 ? 11.853 48.094 57.806 0.00 94.59  ? 159 LYS A HD2  1 
ATOM   2496 H HD3  . LYS A 1 156 ? 11.822 46.754 56.952 0.00 94.59  ? 159 LYS A HD3  1 
ATOM   2497 H HE2  . LYS A 1 156 ? 11.582 46.770 59.763 0.00 102.44 ? 159 LYS A HE2  1 
ATOM   2498 H HE3  . LYS A 1 156 ? 10.327 46.690 58.791 0.00 102.44 ? 159 LYS A HE3  1 
ATOM   2499 H HZ1  . LYS A 1 156 ? 10.940 44.605 59.461 0.00 86.78  ? 159 LYS A HZ1  1 
ATOM   2500 H HZ2  . LYS A 1 156 ? 11.136 44.698 58.029 0.00 86.78  ? 159 LYS A HZ2  1 
ATOM   2501 H HZ3  . LYS A 1 156 ? 12.274 44.770 58.922 0.00 86.78  ? 159 LYS A HZ3  1 
ATOM   2502 N N    . ALA A 1 157 ? 17.422 46.900 57.144 1.00 90.60  ? 160 ALA A N    1 
ATOM   2503 C CA   . ALA A 1 157 ? 18.406 45.852 57.398 1.00 75.71  ? 160 ALA A CA   1 
ATOM   2504 C C    . ALA A 1 157 ? 19.344 46.232 58.532 1.00 83.03  ? 160 ALA A C    1 
ATOM   2505 O O    . ALA A 1 157 ? 19.752 45.373 59.320 1.00 73.42  ? 160 ALA A O    1 
ATOM   2506 C CB   . ALA A 1 157 ? 19.228 45.608 56.136 1.00 70.17  ? 160 ALA A CB   1 
ATOM   2507 H H    . ALA A 1 157 ? 17.419 47.192 56.335 0.00 108.71 ? 160 ALA A H    1 
ATOM   2508 H HA   . ALA A 1 157 ? 17.935 45.040 57.641 0.00 90.86  ? 160 ALA A HA   1 
ATOM   2509 H HB1  . ALA A 1 157 ? 19.878 44.910 56.312 0.00 84.20  ? 160 ALA A HB1  1 
ATOM   2510 H HB2  . ALA A 1 157 ? 18.633 45.333 55.420 0.00 84.20  ? 160 ALA A HB2  1 
ATOM   2511 H HB3  . ALA A 1 157 ? 19.682 46.429 55.891 0.00 84.20  ? 160 ALA A HB3  1 
ATOM   2512 N N    . GLU A 1 158 ? 19.719 47.514 58.605 1.00 92.11  ? 161 GLU A N    1 
ATOM   2513 C CA   . GLU A 1 158 ? 20.653 48.016 59.608 1.00 91.84  ? 161 GLU A CA   1 
ATOM   2514 C C    . GLU A 1 158 ? 20.083 47.966 61.013 1.00 101.34 ? 161 GLU A C    1 
ATOM   2515 O O    . GLU A 1 158 ? 20.799 48.310 61.961 1.00 97.83  ? 161 GLU A O    1 
ATOM   2516 C CB   . GLU A 1 158 ? 21.051 49.451 59.256 1.00 102.13 ? 161 GLU A CB   1 
ATOM   2517 C CG   . GLU A 1 158 ? 21.846 49.569 57.955 1.00 106.28 ? 161 GLU A CG   1 
ATOM   2518 C CD   . GLU A 1 158 ? 22.741 50.794 57.902 1.00 113.56 ? 161 GLU A CD   1 
ATOM   2519 O OE1  . GLU A 1 158 ? 22.408 51.809 58.552 1.00 114.47 ? 161 GLU A OE1  1 
ATOM   2520 O OE2  . GLU A 1 158 ? 23.765 50.751 57.185 1.00 108.66 ? 161 GLU A OE2  1 
ATOM   2521 H H    . GLU A 1 158 ? 19.437 48.125 58.070 0.00 110.53 ? 161 GLU A H    1 
ATOM   2522 H HA   . GLU A 1 158 ? 21.455 47.470 59.598 0.00 110.21 ? 161 GLU A HA   1 
ATOM   2523 H HB2  . GLU A 1 158 ? 20.245 49.983 59.160 0.00 122.55 ? 161 GLU A HB2  1 
ATOM   2524 H HB3  . GLU A 1 158 ? 21.600 49.807 59.972 0.00 122.55 ? 161 GLU A HB3  1 
ATOM   2525 H HG2  . GLU A 1 158 ? 22.409 48.785 57.861 0.00 127.54 ? 161 GLU A HG2  1 
ATOM   2526 H HG3  . GLU A 1 158 ? 21.225 49.623 57.212 0.00 127.54 ? 161 GLU A HG3  1 
ATOM   2527 N N    . SER A 1 159 ? 18.823 47.561 61.173 1.00 95.30  ? 162 SER A N    1 
ATOM   2528 C CA   . SER A 1 159 ? 18.212 47.385 62.483 1.00 95.55  ? 162 SER A CA   1 
ATOM   2529 C C    . SER A 1 159 ? 17.930 45.922 62.799 1.00 90.71  ? 162 SER A C    1 
ATOM   2530 O O    . SER A 1 159 ? 17.285 45.630 63.811 1.00 91.15  ? 162 SER A O    1 
ATOM   2531 C CB   . SER A 1 159 ? 16.926 48.210 62.587 1.00 101.61 ? 162 SER A CB   1 
ATOM   2532 O OG   . SER A 1 159 ? 16.128 48.076 61.421 1.00 97.90  ? 162 SER A OG   1 
ATOM   2533 H H    . SER A 1 159 ? 18.293 47.379 60.520 0.00 114.37 ? 162 SER A H    1 
ATOM   2534 H HA   . SER A 1 159 ? 18.826 47.718 63.156 0.00 114.66 ? 162 SER A HA   1 
ATOM   2535 H HB2  . SER A 1 159 ? 16.416 47.900 63.353 0.00 121.93 ? 162 SER A HB2  1 
ATOM   2536 H HB3  . SER A 1 159 ? 17.161 49.144 62.701 0.00 121.93 ? 162 SER A HB3  1 
ATOM   2537 H HG   . SER A 1 159 ? 15.486 48.618 61.449 0.00 117.48 ? 162 SER A HG   1 
ATOM   2538 N N    . MET A 1 160 ? 18.411 44.998 61.968 1.00 78.61  ? 163 MET A N    1 
ATOM   2539 C CA   . MET A 1 160 ? 18.172 43.578 62.144 1.00 74.55  ? 163 MET A CA   1 
ATOM   2540 C C    . MET A 1 160 ? 19.470 42.865 62.519 1.00 73.20  ? 163 MET A C    1 
ATOM   2541 O O    . MET A 1 160 ? 20.489 43.501 62.815 1.00 75.94  ? 163 MET A O    1 
ATOM   2542 C CB   . MET A 1 160 ? 17.578 43.023 60.855 1.00 76.30  ? 163 MET A CB   1 
ATOM   2543 C CG   . MET A 1 160 ? 16.563 43.959 60.241 1.00 87.26  ? 163 MET A CG   1 
ATOM   2544 S SD   . MET A 1 160 ? 15.475 43.241 58.990 1.00 79.33  ? 163 MET A SD   1 
ATOM   2545 C CE   . MET A 1 160 ? 15.132 41.593 59.625 1.00 69.00  ? 163 MET A CE   1 
ATOM   2546 H H    . MET A 1 160 ? 18.892 45.181 61.279 0.00 94.33  ? 163 MET A H    1 
ATOM   2547 H HA   . MET A 1 160 ? 17.538 43.451 62.867 0.00 89.46  ? 163 MET A HA   1 
ATOM   2548 H HB2  . MET A 1 160 ? 18.290 42.885 60.211 0.00 91.57  ? 163 MET A HB2  1 
ATOM   2549 H HB3  . MET A 1 160 ? 17.136 42.181 61.046 0.00 91.57  ? 163 MET A HB3  1 
ATOM   2550 H HG2  . MET A 1 160 ? 15.997 44.300 60.951 0.00 104.71 ? 163 MET A HG2  1 
ATOM   2551 H HG3  . MET A 1 160 ? 17.041 44.690 59.818 0.00 104.71 ? 163 MET A HG3  1 
ATOM   2552 H HE1  . MET A 1 160 ? 14.450 41.178 59.075 0.00 82.80  ? 163 MET A HE1  1 
ATOM   2553 H HE2  . MET A 1 160 ? 15.947 41.067 59.594 0.00 82.80  ? 163 MET A HE2  1 
ATOM   2554 H HE3  . MET A 1 160 ? 14.820 41.665 60.541 0.00 82.80  ? 163 MET A HE3  1 
ATOM   2555 N N    . ARG A 1 161 ? 19.424 41.532 62.500 1.00 71.68  ? 164 ARG A N    1 
ATOM   2556 C CA   . ARG A 1 161 ? 20.595 40.722 62.822 1.00 67.21  ? 164 ARG A CA   1 
ATOM   2557 C C    . ARG A 1 161 ? 21.795 41.169 61.981 1.00 65.72  ? 164 ARG A C    1 
ATOM   2558 O O    . ARG A 1 161 ? 21.635 41.529 60.816 1.00 63.42  ? 164 ARG A O    1 
ATOM   2559 C CB   . ARG A 1 161 ? 20.296 39.241 62.533 1.00 62.35  ? 164 ARG A CB   1 
ATOM   2560 C CG   . ARG A 1 161 ? 19.269 38.635 63.465 1.00 64.31  ? 164 ARG A CG   1 
ATOM   2561 C CD   . ARG A 1 161 ? 18.479 37.530 62.787 1.00 66.93  ? 164 ARG A CD   1 
ATOM   2562 N NE   . ARG A 1 161 ? 19.348 36.487 62.265 1.00 68.17  ? 164 ARG A NE   1 
ATOM   2563 C CZ   . ARG A 1 161 ? 18.940 35.494 61.488 1.00 65.67  ? 164 ARG A CZ   1 
ATOM   2564 N NH1  . ARG A 1 161 ? 17.662 35.322 61.204 1.00 59.60  ? 164 ARG A NH1  1 
ATOM   2565 N NH2  . ARG A 1 161 ? 19.843 34.652 60.988 1.00 62.56  ? 164 ARG A NH2  1 
ATOM   2566 H H    . ARG A 1 161 ? 18.725 41.072 62.304 0.00 86.01  ? 164 ARG A H    1 
ATOM   2567 H HA   . ARG A 1 161 ? 20.816 40.829 63.760 0.00 80.65  ? 164 ARG A HA   1 
ATOM   2568 H HB2  . ARG A 1 161 ? 19.959 39.162 61.628 0.00 74.82  ? 164 ARG A HB2  1 
ATOM   2569 H HB3  . ARG A 1 161 ? 21.117 38.733 62.627 0.00 74.82  ? 164 ARG A HB3  1 
ATOM   2570 H HG2  . ARG A 1 161 ? 19.719 38.258 64.237 0.00 77.17  ? 164 ARG A HG2  1 
ATOM   2571 H HG3  . ARG A 1 161 ? 18.647 39.324 63.747 0.00 77.17  ? 164 ARG A HG3  1 
ATOM   2572 H HD2  . ARG A 1 161 ? 17.875 37.128 63.430 0.00 80.32  ? 164 ARG A HD2  1 
ATOM   2573 H HD3  . ARG A 1 161 ? 17.975 37.904 62.047 0.00 80.32  ? 164 ARG A HD3  1 
ATOM   2574 H HE   . ARG A 1 161 ? 20.182 36.517 62.474 0.00 81.80  ? 164 ARG A HE   1 
ATOM   2575 H HH11 . ARG A 1 161 ? 17.074 35.861 61.526 0.00 71.53  ? 164 ARG A HH11 1 
ATOM   2576 H HH12 . ARG A 1 161 ? 17.418 34.671 60.698 0.00 71.53  ? 164 ARG A HH12 1 
ATOM   2577 H HH21 . ARG A 1 161 ? 20.677 34.758 61.171 0.00 75.08  ? 164 ARG A HH21 1 
ATOM   2578 H HH22 . ARG A 1 161 ? 19.592 34.003 60.482 0.00 75.08  ? 164 ARG A HH22 1 
ATOM   2579 N N    . PRO A 1 162 ? 23.004 41.196 62.550 1.00 40.73  ? 165 PRO A N    1 
ATOM   2580 C CA   . PRO A 1 162 ? 24.172 41.629 61.785 1.00 41.41  ? 165 PRO A CA   1 
ATOM   2581 C C    . PRO A 1 162 ? 24.425 40.796 60.555 1.00 40.81  ? 165 PRO A C    1 
ATOM   2582 O O    . PRO A 1 162 ? 24.847 41.335 59.514 1.00 40.70  ? 165 PRO A O    1 
ATOM   2583 C CB   . PRO A 1 162 ? 25.325 41.548 62.796 1.00 41.82  ? 165 PRO A CB   1 
ATOM   2584 C CG   . PRO A 1 162 ? 24.684 41.591 64.119 1.00 44.24  ? 165 PRO A CG   1 
ATOM   2585 C CD   . PRO A 1 162 ? 23.339 40.957 63.952 1.00 42.83  ? 165 PRO A CD   1 
ATOM   2586 H HA   . PRO A 1 162 ? 24.060 42.556 61.522 0.00 49.70  ? 165 PRO A HA   1 
ATOM   2587 H HB2  . PRO A 1 162 ? 25.812 40.719 62.674 0.00 50.18  ? 165 PRO A HB2  1 
ATOM   2588 H HB3  . PRO A 1 162 ? 25.921 42.304 62.676 0.00 50.18  ? 165 PRO A HB3  1 
ATOM   2589 H HG2  . PRO A 1 162 ? 25.220 41.093 64.757 0.00 53.09  ? 165 PRO A HG2  1 
ATOM   2590 H HG3  . PRO A 1 162 ? 24.595 42.512 64.409 0.00 53.09  ? 165 PRO A HG3  1 
ATOM   2591 H HD2  . PRO A 1 162 ? 23.384 40.006 64.135 0.00 51.39  ? 165 PRO A HD2  1 
ATOM   2592 H HD3  . PRO A 1 162 ? 22.688 41.377 64.535 0.00 51.39  ? 165 PRO A HD3  1 
ATOM   2593 N N    . GLU A 1 163 ? 24.175 39.485 60.612 1.00 40.88  ? 166 GLU A N    1 
ATOM   2594 C CA   . GLU A 1 163 ? 24.403 38.690 59.410 1.00 39.74  ? 166 GLU A CA   1 
ATOM   2595 C C    . GLU A 1 163 ? 23.356 38.949 58.344 1.00 42.33  ? 166 GLU A C    1 
ATOM   2596 O O    . GLU A 1 163 ? 23.653 38.818 57.164 1.00 40.71  ? 166 GLU A O    1 
ATOM   2597 C CB   . GLU A 1 163 ? 24.429 37.190 59.765 1.00 51.69  ? 166 GLU A CB   1 
ATOM   2598 C CG   . GLU A 1 163 ? 23.097 36.646 60.226 1.00 49.60  ? 166 GLU A CG   1 
ATOM   2599 C CD   . GLU A 1 163 ? 22.892 36.794 61.702 1.00 59.27  ? 166 GLU A CD   1 
ATOM   2600 O OE1  . GLU A 1 163 ? 23.484 37.719 62.287 1.00 55.16  ? 166 GLU A OE1  1 
ATOM   2601 O OE2  . GLU A 1 163 ? 22.139 35.986 62.306 1.00 70.18  ? 166 GLU A OE2  1 
ATOM   2602 H H    . GLU A 1 163 ? 23.888 39.056 61.299 0.00 49.06  ? 166 GLU A H    1 
ATOM   2603 H HA   . GLU A 1 163 ? 25.267 38.936 59.044 0.00 47.69  ? 166 GLU A HA   1 
ATOM   2604 H HB2  . GLU A 1 163 ? 24.697 36.689 58.979 0.00 62.03  ? 166 GLU A HB2  1 
ATOM   2605 H HB3  . GLU A 1 163 ? 25.069 37.051 60.481 0.00 62.03  ? 166 GLU A HB3  1 
ATOM   2606 H HG2  . GLU A 1 163 ? 22.386 37.126 59.775 0.00 59.52  ? 166 GLU A HG2  1 
ATOM   2607 H HG3  . GLU A 1 163 ? 23.050 35.701 60.010 0.00 59.52  ? 166 GLU A HG3  1 
ATOM   2608 N N    . VAL A 1 164 ? 22.146 39.354 58.734 1.00 38.63  ? 167 VAL A N    1 
ATOM   2609 C CA   . VAL A 1 164 ? 21.165 39.733 57.726 1.00 35.49  ? 167 VAL A CA   1 
ATOM   2610 C C    . VAL A 1 164 ? 21.602 41.052 57.113 1.00 32.69  ? 167 VAL A C    1 
ATOM   2611 O O    . VAL A 1 164 ? 21.581 41.233 55.889 1.00 36.01  ? 167 VAL A O    1 
ATOM   2612 C CB   . VAL A 1 164 ? 19.772 39.829 58.385 1.00 38.40  ? 167 VAL A CB   1 
ATOM   2613 C CG1  . VAL A 1 164 ? 18.777 40.411 57.392 1.00 42.96  ? 167 VAL A CG1  1 
ATOM   2614 C CG2  . VAL A 1 164 ? 19.329 38.445 58.862 1.00 43.64  ? 167 VAL A CG2  1 
ATOM   2615 H H    . VAL A 1 164 ? 21.880 39.416 59.550 0.00 46.36  ? 167 VAL A H    1 
ATOM   2616 H HA   . VAL A 1 164 ? 21.111 39.067 57.023 0.00 42.59  ? 167 VAL A HA   1 
ATOM   2617 H HB   . VAL A 1 164 ? 19.808 40.414 59.158 0.00 46.07  ? 167 VAL A HB   1 
ATOM   2618 H HG11 . VAL A 1 164 ? 17.886 40.361 57.773 0.00 51.55  ? 167 VAL A HG11 1 
ATOM   2619 H HG12 . VAL A 1 164 ? 19.010 41.335 57.216 0.00 51.55  ? 167 VAL A HG12 1 
ATOM   2620 H HG13 . VAL A 1 164 ? 18.814 39.898 56.570 0.00 51.55  ? 167 VAL A HG13 1 
ATOM   2621 H HG21 . VAL A 1 164 ? 18.459 38.520 59.283 0.00 52.37  ? 167 VAL A HG21 1 
ATOM   2622 H HG22 . VAL A 1 164 ? 19.276 37.850 58.098 0.00 52.37  ? 167 VAL A HG22 1 
ATOM   2623 H HG23 . VAL A 1 164 ? 19.977 38.108 59.499 0.00 52.37  ? 167 VAL A HG23 1 
ATOM   2624 N N    . ALA A 1 165 ? 22.087 41.988 57.924 1.00 39.04  ? 168 ALA A N    1 
ATOM   2625 C CA   . ALA A 1 165 ? 22.472 43.274 57.328 1.00 36.39  ? 168 ALA A CA   1 
ATOM   2626 C C    . ALA A 1 165 ? 23.645 43.127 56.368 1.00 39.35  ? 168 ALA A C    1 
ATOM   2627 O O    . ALA A 1 165 ? 23.653 43.753 55.298 1.00 37.62  ? 168 ALA A O    1 
ATOM   2628 C CB   . ALA A 1 165 ? 22.788 44.265 58.436 1.00 42.83  ? 168 ALA A CB   1 
ATOM   2629 H H    . ALA A 1 165 ? 22.200 41.913 58.774 0.00 46.85  ? 168 ALA A H    1 
ATOM   2630 H HA   . ALA A 1 165 ? 21.728 43.620 56.811 0.00 43.67  ? 168 ALA A HA   1 
ATOM   2631 H HB1  . ALA A 1 165 ? 23.031 45.116 58.039 0.00 51.40  ? 168 ALA A HB1  1 
ATOM   2632 H HB2  . ALA A 1 165 ? 22.004 44.373 58.997 0.00 51.40  ? 168 ALA A HB2  1 
ATOM   2633 H HB3  . ALA A 1 165 ? 23.527 43.923 58.964 0.00 51.40  ? 168 ALA A HB3  1 
ATOM   2634 N N    . SER A 1 166 ? 24.678 42.353 56.723 1.00 38.70  ? 169 SER A N    1 
ATOM   2635 C CA   . SER A 1 166 ? 25.854 42.301 55.858 1.00 41.46  ? 169 SER A CA   1 
ATOM   2636 C C    . SER A 1 166 ? 25.536 41.584 54.566 1.00 39.83  ? 169 SER A C    1 
ATOM   2637 O O    . SER A 1 166 ? 25.973 42.010 53.482 1.00 38.79  ? 169 SER A O    1 
ATOM   2638 C CB   . SER A 1 166 ? 27.069 41.655 56.535 1.00 39.89  ? 169 SER A CB   1 
ATOM   2639 O OG   . SER A 1 166 ? 26.698 40.430 57.147 1.00 51.87  ? 169 SER A OG   1 
ATOM   2640 H H    . SER A 1 166 ? 24.719 41.869 57.433 0.00 46.44  ? 169 SER A H    1 
ATOM   2641 H HA   . SER A 1 166 ? 26.108 43.219 55.672 0.00 49.75  ? 169 SER A HA   1 
ATOM   2642 H HB2  . SER A 1 166 ? 27.750 41.483 55.867 0.00 47.87  ? 169 SER A HB2  1 
ATOM   2643 H HB3  . SER A 1 166 ? 27.413 42.258 57.212 0.00 47.87  ? 169 SER A HB3  1 
ATOM   2644 H HG   . SER A 1 166 ? 27.354 40.106 57.561 0.00 62.24  ? 169 SER A HG   1 
ATOM   2645 N N    . THR A 1 167 ? 24.725 40.516 54.644 1.00 34.74  ? 170 THR A N    1 
ATOM   2646 C CA   . THR A 1 167 ? 24.363 39.768 53.454 1.00 33.52  ? 170 THR A CA   1 
ATOM   2647 C C    . THR A 1 167 ? 23.463 40.618 52.557 1.00 31.14  ? 170 THR A C    1 
ATOM   2648 O O    . THR A 1 167 ? 23.622 40.622 51.312 1.00 31.63  ? 170 THR A O    1 
ATOM   2649 C CB   . THR A 1 167 ? 23.730 38.428 53.843 1.00 35.83  ? 170 THR A CB   1 
ATOM   2650 O OG1  . THR A 1 167 ? 24.676 37.613 54.542 1.00 39.02  ? 170 THR A OG1  1 
ATOM   2651 C CG2  . THR A 1 167 ? 23.226 37.702 52.587 1.00 37.92  ? 170 THR A CG2  1 
ATOM   2652 H H    . THR A 1 167 ? 24.379 40.215 55.372 0.00 41.69  ? 170 THR A H    1 
ATOM   2653 H HA   . THR A 1 167 ? 25.154 39.543 52.939 0.00 40.23  ? 170 THR A HA   1 
ATOM   2654 H HB   . THR A 1 167 ? 22.974 38.582 54.432 0.00 43.00  ? 170 THR A HB   1 
ATOM   2655 H HG1  . THR A 1 167 ? 24.357 37.373 55.281 0.00 46.83  ? 170 THR A HG1  1 
ATOM   2656 H HG21 . THR A 1 167 ? 22.909 36.816 52.820 0.00 45.50  ? 170 THR A HG21 1 
ATOM   2657 H HG22 . THR A 1 167 ? 22.498 38.202 52.185 0.00 45.50  ? 170 THR A HG22 1 
ATOM   2658 H HG23 . THR A 1 167 ? 23.945 37.619 51.941 0.00 45.50  ? 170 THR A HG23 1 
ATOM   2659 N N    . PHE A 1 168 ? 22.514 41.345 53.137 1.00 31.77  ? 171 PHE A N    1 
ATOM   2660 C CA   . PHE A 1 168 ? 21.688 42.209 52.290 1.00 31.32  ? 171 PHE A CA   1 
ATOM   2661 C C    . PHE A 1 168 ? 22.558 43.230 51.572 1.00 31.72  ? 171 PHE A C    1 
ATOM   2662 O O    . PHE A 1 168 ? 22.361 43.482 50.376 1.00 30.71  ? 171 PHE A O    1 
ATOM   2663 C CB   . PHE A 1 168 ? 20.630 42.932 53.131 1.00 30.10  ? 171 PHE A CB   1 
ATOM   2664 C CG   . PHE A 1 168 ? 19.894 43.984 52.375 1.00 34.96  ? 171 PHE A CG   1 
ATOM   2665 C CD1  . PHE A 1 168 ? 18.934 43.618 51.481 1.00 32.00  ? 171 PHE A CD1  1 
ATOM   2666 C CD2  . PHE A 1 168 ? 20.204 45.303 52.500 1.00 40.19  ? 171 PHE A CD2  1 
ATOM   2667 C CE1  . PHE A 1 168 ? 18.273 44.545 50.760 1.00 37.96  ? 171 PHE A CE1  1 
ATOM   2668 C CE2  . PHE A 1 168 ? 19.538 46.237 51.764 1.00 37.70  ? 171 PHE A CE2  1 
ATOM   2669 C CZ   . PHE A 1 168 ? 18.572 45.861 50.905 1.00 36.68  ? 171 PHE A CZ   1 
ATOM   2670 H H    . PHE A 1 168 ? 22.333 41.358 53.978 0.00 38.13  ? 171 PHE A H    1 
ATOM   2671 H HA   . PHE A 1 168 ? 21.231 41.658 51.635 0.00 37.59  ? 171 PHE A HA   1 
ATOM   2672 H HB2  . PHE A 1 168 ? 19.981 42.282 53.445 0.00 36.13  ? 171 PHE A HB2  1 
ATOM   2673 H HB3  . PHE A 1 168 ? 21.065 43.357 53.886 0.00 36.13  ? 171 PHE A HB3  1 
ATOM   2674 H HD1  . PHE A 1 168 ? 18.733 42.717 51.366 0.00 38.41  ? 171 PHE A HD1  1 
ATOM   2675 H HD2  . PHE A 1 168 ? 20.873 45.567 53.090 0.00 48.23  ? 171 PHE A HD2  1 
ATOM   2676 H HE1  . PHE A 1 168 ? 17.610 44.283 50.163 0.00 45.55  ? 171 PHE A HE1  1 
ATOM   2677 H HE2  . PHE A 1 168 ? 19.752 47.138 51.855 0.00 45.24  ? 171 PHE A HE2  1 
ATOM   2678 H HZ   . PHE A 1 168 ? 18.111 46.500 50.411 0.00 44.02  ? 171 PHE A HZ   1 
ATOM   2679 N N    . LYS A 1 169 ? 23.479 43.883 52.287 1.00 33.10  ? 172 LYS A N    1 
ATOM   2680 C CA   . LYS A 1 169 ? 24.291 44.938 51.676 1.00 33.84  ? 172 LYS A CA   1 
ATOM   2681 C C    . LYS A 1 169 ? 25.071 44.404 50.481 1.00 33.95  ? 172 LYS A C    1 
ATOM   2682 O O    . LYS A 1 169 ? 25.135 45.055 49.423 1.00 33.67  ? 172 LYS A O    1 
ATOM   2683 C CB   . LYS A 1 169 ? 25.210 45.558 52.733 1.00 36.40  ? 172 LYS A CB   1 
ATOM   2684 C CG   . LYS A 1 169 ? 24.478 46.660 53.482 1.00 43.39  ? 172 LYS A CG   1 
ATOM   2685 C CD   . LYS A 1 169 ? 25.453 47.377 54.469 1.00 56.34  ? 172 LYS A CD   1 
ATOM   2686 C CE   . LYS A 1 169 ? 24.768 47.660 55.801 1.00 72.19  ? 172 LYS A CE   1 
ATOM   2687 N NZ   . LYS A 1 169 ? 25.557 48.580 56.679 1.00 81.91  ? 172 LYS A NZ   1 
ATOM   2688 H H    . LYS A 1 169 ? 23.651 43.736 53.117 0.00 39.73  ? 172 LYS A H    1 
ATOM   2689 H HA   . LYS A 1 169 ? 23.716 45.646 51.346 0.00 40.60  ? 172 LYS A HA   1 
ATOM   2690 N N    . VAL A 1 170 ? 25.674 43.236 50.621 1.00 31.54  ? 173 VAL A N    1 
ATOM   2691 C CA   . VAL A 1 170 ? 26.366 42.645 49.465 1.00 32.77  ? 173 VAL A CA   1 
ATOM   2692 C C    . VAL A 1 170 ? 25.422 42.373 48.319 1.00 32.07  ? 173 VAL A C    1 
ATOM   2693 O O    . VAL A 1 170 ? 25.738 42.676 47.161 1.00 29.79  ? 173 VAL A O    1 
ATOM   2694 C CB   . VAL A 1 170 ? 27.090 41.359 49.884 1.00 29.96  ? 173 VAL A CB   1 
ATOM   2695 C CG1  . VAL A 1 170 ? 27.678 40.632 48.671 1.00 34.65  ? 173 VAL A CG1  1 
ATOM   2696 C CG2  . VAL A 1 170 ? 28.129 41.676 50.944 1.00 37.70  ? 173 VAL A CG2  1 
ATOM   2697 H H    . VAL A 1 170 ? 25.703 42.773 51.346 0.00 37.85  ? 173 VAL A H    1 
ATOM   2698 H HA   . VAL A 1 170 ? 27.015 43.296 49.156 0.00 39.32  ? 173 VAL A HA   1 
ATOM   2699 H HB   . VAL A 1 170 ? 26.455 40.741 50.278 0.00 35.96  ? 173 VAL A HB   1 
ATOM   2700 H HG11 . VAL A 1 170 ? 28.326 39.979 48.978 0.00 41.58  ? 173 VAL A HG11 1 
ATOM   2701 H HG12 . VAL A 1 170 ? 26.961 40.186 48.192 0.00 41.58  ? 173 VAL A HG12 1 
ATOM   2702 H HG13 . VAL A 1 170 ? 28.109 41.280 48.092 0.00 41.58  ? 173 VAL A HG13 1 
ATOM   2703 H HG21 . VAL A 1 170 ? 28.592 40.858 51.187 0.00 45.24  ? 173 VAL A HG21 1 
ATOM   2704 H HG22 . VAL A 1 170 ? 28.760 42.320 50.586 0.00 45.24  ? 173 VAL A HG22 1 
ATOM   2705 H HG23 . VAL A 1 170 ? 27.684 42.046 51.722 0.00 45.24  ? 173 VAL A HG23 1 
ATOM   2706 N N    . LEU A 1 171 ? 24.279 41.702 48.576 1.00 27.77  ? 174 LEU A N    1 
ATOM   2707 C CA   . LEU A 1 171 ? 23.371 41.365 47.461 1.00 26.11  ? 174 LEU A CA   1 
ATOM   2708 C C    . LEU A 1 171 ? 22.727 42.606 46.873 1.00 28.40  ? 174 LEU A C    1 
ATOM   2709 O O    . LEU A 1 171 ? 22.471 42.611 45.656 1.00 27.16  ? 174 LEU A O    1 
ATOM   2710 C CB   . LEU A 1 171 ? 22.308 40.440 48.041 1.00 27.90  ? 174 LEU A CB   1 
ATOM   2711 C CG   . LEU A 1 171 ? 22.789 39.063 48.459 1.00 29.41  ? 174 LEU A CG   1 
ATOM   2712 C CD1  . LEU A 1 171 ? 21.668 38.237 49.034 1.00 34.99  ? 174 LEU A CD1  1 
ATOM   2713 C CD2  . LEU A 1 171 ? 23.353 38.314 47.223 1.00 33.21  ? 174 LEU A CD2  1 
ATOM   2714 H H    . LEU A 1 171 ? 24.019 41.441 49.353 0.00 33.33  ? 174 LEU A H    1 
ATOM   2715 H HA   . LEU A 1 171 ? 23.847 40.926 46.739 0.00 31.34  ? 174 LEU A HA   1 
ATOM   2716 H HB2  . LEU A 1 171 ? 21.932 40.866 48.828 0.00 33.48  ? 174 LEU A HB2  1 
ATOM   2717 H HB3  . LEU A 1 171 ? 21.618 40.314 47.371 0.00 33.48  ? 174 LEU A HB3  1 
ATOM   2718 H HG   . LEU A 1 171 ? 23.474 39.175 49.137 0.00 35.29  ? 174 LEU A HG   1 
ATOM   2719 H HD11 . LEU A 1 171 ? 22.016 37.369 49.293 0.00 41.99  ? 174 LEU A HD11 1 
ATOM   2720 H HD12 . LEU A 1 171 ? 21.306 38.693 49.809 0.00 41.99  ? 174 LEU A HD12 1 
ATOM   2721 H HD13 . LEU A 1 171 ? 20.978 38.129 48.361 0.00 41.99  ? 174 LEU A HD13 1 
ATOM   2722 H HD21 . LEU A 1 171 ? 23.494 37.383 47.455 0.00 39.85  ? 174 LEU A HD21 1 
ATOM   2723 H HD22 . LEU A 1 171 ? 22.714 38.380 46.495 0.00 39.85  ? 174 LEU A HD22 1 
ATOM   2724 H HD23 . LEU A 1 171 ? 24.194 38.721 46.963 0.00 39.85  ? 174 LEU A HD23 1 
ATOM   2725 N N    A ARG A 1 172 ? 22.456 43.635 47.683 0.69 27.66  ? 175 ARG A N    1 
ATOM   2726 N N    B ARG A 1 172 ? 22.483 43.644 47.672 0.31 27.72  ? 175 ARG A N    1 
ATOM   2727 C CA   A ARG A 1 172 ? 21.945 44.901 47.130 0.69 28.75  ? 175 ARG A CA   1 
ATOM   2728 C CA   B ARG A 1 172 ? 21.939 44.885 47.119 0.31 28.85  ? 175 ARG A CA   1 
ATOM   2729 C C    A ARG A 1 172 ? 22.951 45.496 46.157 0.69 29.35  ? 175 ARG A C    1 
ATOM   2730 C C    B ARG A 1 172 ? 22.938 45.549 46.178 0.31 29.35  ? 175 ARG A C    1 
ATOM   2731 O O    A ARG A 1 172 ? 22.594 45.916 45.034 0.69 28.42  ? 175 ARG A O    1 
ATOM   2732 O O    B ARG A 1 172 ? 22.554 46.095 45.129 0.31 28.83  ? 175 ARG A O    1 
ATOM   2733 C CB   A ARG A 1 172 ? 21.628 45.865 48.270 0.69 37.54  ? 175 ARG A CB   1 
ATOM   2734 C CB   B ARG A 1 172 ? 21.554 45.828 48.255 0.31 37.24  ? 175 ARG A CB   1 
ATOM   2735 C CG   A ARG A 1 172 ? 21.379 47.366 47.896 0.69 37.11  ? 175 ARG A CG   1 
ATOM   2736 C CG   B ARG A 1 172 ? 20.902 47.136 47.809 0.31 34.20  ? 175 ARG A CG   1 
ATOM   2737 C CD   A ARG A 1 172 ? 21.791 48.287 49.079 0.69 38.04  ? 175 ARG A CD   1 
ATOM   2738 C CD   B ARG A 1 172 ? 21.832 48.312 48.050 0.31 41.04  ? 175 ARG A CD   1 
ATOM   2739 N NE   A ARG A 1 172 ? 23.234 48.482 49.187 0.69 42.31  ? 175 ARG A NE   1 
ATOM   2740 N NE   B ARG A 1 172 ? 21.939 48.676 49.462 0.31 37.47  ? 175 ARG A NE   1 
ATOM   2741 C CZ   A ARG A 1 172 ? 23.809 49.159 50.175 0.69 40.48  ? 175 ARG A CZ   1 
ATOM   2742 C CZ   B ARG A 1 172 ? 23.053 48.593 50.180 0.31 43.69  ? 175 ARG A CZ   1 
ATOM   2743 N NH1  A ARG A 1 172 ? 23.091 49.703 51.139 0.69 46.27  ? 175 ARG A NH1  1 
ATOM   2744 N NH1  B ARG A 1 172 ? 24.172 48.094 49.676 0.31 38.55  ? 175 ARG A NH1  1 
ATOM   2745 N NH2  A ARG A 1 172 ? 25.130 49.287 50.188 0.69 42.12  ? 175 ARG A NH2  1 
ATOM   2746 N NH2  B ARG A 1 172 ? 23.039 49.008 51.441 0.31 42.13  ? 175 ARG A NH2  1 
ATOM   2747 H H    A ARG A 1 172 ? 22.555 43.630 48.537 0.69 33.19  ? 175 ARG A H    1 
ATOM   2748 H H    B ARG A 1 172 ? 22.619 43.657 48.521 0.31 33.27  ? 175 ARG A H    1 
ATOM   2749 H HA   A ARG A 1 172 ? 21.120 44.744 46.644 0.69 34.50  ? 175 ARG A HA   1 
ATOM   2750 H HA   B ARG A 1 172 ? 21.138 44.686 46.609 0.31 34.63  ? 175 ARG A HA   1 
ATOM   2751 H HB2  A ARG A 1 172 ? 20.824 45.549 48.713 0.69 45.05  ? 175 ARG A HB2  1 
ATOM   2752 H HB2  B ARG A 1 172 ? 20.924 45.370 48.834 0.31 44.69  ? 175 ARG A HB2  1 
ATOM   2753 H HB3  A ARG A 1 172 ? 22.375 45.850 48.889 0.69 45.05  ? 175 ARG A HB3  1 
ATOM   2754 H HB3  B ARG A 1 172 ? 22.356 46.056 48.751 0.31 44.69  ? 175 ARG A HB3  1 
ATOM   2755 H HG2  A ARG A 1 172 ? 21.909 47.601 47.119 0.69 44.54  ? 175 ARG A HG2  1 
ATOM   2756 H HG2  B ARG A 1 172 ? 20.701 47.091 46.861 0.31 41.04  ? 175 ARG A HG2  1 
ATOM   2757 H HG3  A ARG A 1 172 ? 20.437 47.504 47.709 0.69 44.54  ? 175 ARG A HG3  1 
ATOM   2758 H HG3  B ARG A 1 172 ? 20.086 47.280 48.314 0.31 41.04  ? 175 ARG A HG3  1 
ATOM   2759 H HD2  A ARG A 1 172 ? 21.382 49.158 48.956 0.69 45.65  ? 175 ARG A HD2  1 
ATOM   2760 H HD2  B ARG A 1 172 ? 22.719 48.082 47.733 0.31 49.25  ? 175 ARG A HD2  1 
ATOM   2761 H HD3  A ARG A 1 172 ? 21.483 47.889 49.908 0.69 45.65  ? 175 ARG A HD3  1 
ATOM   2762 H HD3  B ARG A 1 172 ? 21.497 49.083 47.567 0.31 49.25  ? 175 ARG A HD3  1 
ATOM   2763 H HE   A ARG A 1 172 ? 23.738 48.141 48.579 0.69 50.77  ? 175 ARG A HE   1 
ATOM   2764 H HE   B ARG A 1 172 ? 21.230 48.965 49.854 0.31 44.96  ? 175 ARG A HE   1 
ATOM   2765 H HH11 A ARG A 1 172 ? 22.235 49.624 51.136 0.69 55.52  ? 175 ARG A HH11 1 
ATOM   2766 H HH11 B ARG A 1 172 ? 24.190 47.814 48.863 0.31 46.26  ? 175 ARG A HH11 1 
ATOM   2767 H HH12 A ARG A 1 172 ? 23.480 50.138 51.772 0.69 55.52  ? 175 ARG A HH12 1 
ATOM   2768 H HH12 B ARG A 1 172 ? 24.880 48.051 50.162 0.31 46.26  ? 175 ARG A HH12 1 
ATOM   2769 H HH21 A ARG A 1 172 ? 25.603 48.935 49.562 0.69 50.54  ? 175 ARG A HH21 1 
ATOM   2770 H HH21 B ARG A 1 172 ? 23.754 48.960 51.918 0.31 50.56  ? 175 ARG A HH21 1 
ATOM   2771 H HH22 A ARG A 1 172 ? 25.513 49.723 50.823 0.69 50.54  ? 175 ARG A HH22 1 
ATOM   2772 H HH22 B ARG A 1 172 ? 22.316 49.326 51.782 0.31 50.56  ? 175 ARG A HH22 1 
ATOM   2773 N N    . ASN A 1 173 ? 24.228 45.507 46.516 1.00 32.64  ? 176 ASN A N    1 
ATOM   2774 C CA   . ASN A 1 173 ? 25.240 46.126 45.658 1.00 32.35  ? 176 ASN A CA   1 
ATOM   2775 C C    . ASN A 1 173 ? 25.438 45.325 44.384 1.00 31.21  ? 176 ASN A C    1 
ATOM   2776 O O    . ASN A 1 173 ? 25.571 45.904 43.272 1.00 30.52  ? 176 ASN A O    1 
ATOM   2777 C CB   . ASN A 1 173 ? 26.569 46.220 46.467 1.00 30.65  ? 176 ASN A CB   1 
ATOM   2778 C CG   . ASN A 1 173 ? 26.529 47.295 47.545 1.00 34.62  ? 176 ASN A CG   1 
ATOM   2779 O OD1  . ASN A 1 173 ? 25.595 48.123 47.585 1.00 42.20  ? 176 ASN A OD1  1 
ATOM   2780 N ND2  . ASN A 1 173 ? 27.538 47.295 48.449 1.00 42.14  ? 176 ASN A ND2  1 
ATOM   2781 H H    . ASN A 1 173 ? 24.533 45.166 47.244 0.00 39.17  ? 176 ASN A H    1 
ATOM   2782 H HA   . ASN A 1 173 ? 24.961 47.018 45.399 0.00 38.82  ? 176 ASN A HA   1 
ATOM   2783 H HB2  . ASN A 1 173 ? 26.737 45.368 46.900 0.00 36.77  ? 176 ASN A HB2  1 
ATOM   2784 H HB3  . ASN A 1 173 ? 27.295 46.432 45.859 0.00 36.77  ? 176 ASN A HB3  1 
ATOM   2785 H HD21 . ASN A 1 173 ? 27.555 47.884 49.074 0.00 50.57  ? 176 ASN A HD21 1 
ATOM   2786 H HD22 . ASN A 1 173 ? 28.162 46.704 48.397 0.00 50.57  ? 176 ASN A HD22 1 
ATOM   2787 N N    . VAL A 1 174 ? 25.422 43.979 44.490 1.00 27.50  ? 177 VAL A N    1 
ATOM   2788 C CA   . VAL A 1 174 ? 25.456 43.137 43.317 1.00 27.24  ? 177 VAL A CA   1 
ATOM   2789 C C    . VAL A 1 174 ? 24.302 43.479 42.389 1.00 26.63  ? 177 VAL A C    1 
ATOM   2790 O O    . VAL A 1 174 ? 24.483 43.615 41.164 1.00 27.67  ? 177 VAL A O    1 
ATOM   2791 C CB   . VAL A 1 174 ? 25.449 41.649 43.701 1.00 29.38  ? 177 VAL A CB   1 
ATOM   2792 C CG1  . VAL A 1 174 ? 25.164 40.781 42.460 1.00 33.76  ? 177 VAL A CG1  1 
ATOM   2793 C CG2  . VAL A 1 174 ? 26.779 41.288 44.318 1.00 32.92  ? 177 VAL A CG2  1 
ATOM   2794 H H    . VAL A 1 174 ? 25.390 43.547 45.233 0.00 33.00  ? 177 VAL A H    1 
ATOM   2795 H HA   . VAL A 1 174 ? 26.287 43.312 42.847 0.00 32.68  ? 177 VAL A HA   1 
ATOM   2796 H HB   . VAL A 1 174 ? 24.748 41.476 44.349 0.00 35.25  ? 177 VAL A HB   1 
ATOM   2797 H HG11 . VAL A 1 174 ? 25.442 39.870 42.641 0.00 40.52  ? 177 VAL A HG11 1 
ATOM   2798 H HG12 . VAL A 1 174 ? 24.213 40.805 42.269 0.00 40.52  ? 177 VAL A HG12 1 
ATOM   2799 H HG13 . VAL A 1 174 ? 25.661 41.135 41.706 0.00 40.52  ? 177 VAL A HG13 1 
ATOM   2800 H HG21 . VAL A 1 174 ? 26.767 40.352 44.570 0.00 39.50  ? 177 VAL A HG21 1 
ATOM   2801 H HG22 . VAL A 1 174 ? 27.482 41.447 43.668 0.00 39.50  ? 177 VAL A HG22 1 
ATOM   2802 H HG23 . VAL A 1 174 ? 26.923 41.840 45.103 0.00 39.50  ? 177 VAL A HG23 1 
ATOM   2803 N N    . THR A 1 175 ? 23.089 43.564 42.957 1.00 26.09  ? 178 THR A N    1 
ATOM   2804 C CA   . THR A 1 175 ? 21.892 43.768 42.155 1.00 25.53  ? 178 THR A CA   1 
ATOM   2805 C C    . THR A 1 175 ? 21.937 45.120 41.468 1.00 24.70  ? 178 THR A C    1 
ATOM   2806 O O    . THR A 1 175 ? 21.624 45.200 40.245 1.00 24.69  ? 178 THR A O    1 
ATOM   2807 C CB   . THR A 1 175 ? 20.675 43.636 43.107 1.00 25.23  ? 178 THR A CB   1 
ATOM   2808 O OG1  . THR A 1 175 ? 20.604 42.298 43.585 1.00 27.68  ? 178 THR A OG1  1 
ATOM   2809 C CG2  . THR A 1 175 ? 19.351 43.931 42.361 1.00 27.08  ? 178 THR A CG2  1 
ATOM   2810 H H    . THR A 1 175 ? 22.940 43.507 43.802 0.00 31.31  ? 178 THR A H    1 
ATOM   2811 H HA   . THR A 1 175 ? 21.814 43.103 41.453 0.00 30.63  ? 178 THR A HA   1 
ATOM   2812 H HB   . THR A 1 175 ? 20.777 44.266 43.837 0.00 30.28  ? 178 THR A HB   1 
ATOM   2813 H HG1  . THR A 1 175 ? 21.315 42.098 43.986 0.00 33.22  ? 178 THR A HG1  1 
ATOM   2814 H HG21 . THR A 1 175 ? 18.595 43.677 42.913 0.00 32.49  ? 178 THR A HG21 1 
ATOM   2815 H HG22 . THR A 1 175 ? 19.289 44.878 42.159 0.00 32.49  ? 178 THR A HG22 1 
ATOM   2816 H HG23 . THR A 1 175 ? 19.319 43.430 41.532 0.00 32.49  ? 178 THR A HG23 1 
ATOM   2817 N N    . VAL A 1 176 ? 22.293 46.226 42.156 1.00 26.19  ? 179 VAL A N    1 
ATOM   2818 C CA   . VAL A 1 176 ? 22.288 47.550 41.541 1.00 25.41  ? 179 VAL A CA   1 
ATOM   2819 C C    . VAL A 1 176 ? 23.258 47.622 40.364 1.00 27.63  ? 179 VAL A C    1 
ATOM   2820 O O    . VAL A 1 176 ? 22.937 48.170 39.282 1.00 29.52  ? 179 VAL A O    1 
ATOM   2821 C CB   . VAL A 1 176 ? 22.509 48.659 42.566 1.00 31.13  ? 179 VAL A CB   1 
ATOM   2822 C CG1  . VAL A 1 176 ? 22.712 50.000 41.831 1.00 35.20  ? 179 VAL A CG1  1 
ATOM   2823 C CG2  . VAL A 1 176 ? 21.341 48.675 43.555 1.00 37.66  ? 179 VAL A CG2  1 
ATOM   2824 H H    . VAL A 1 176 ? 22.541 46.227 42.980 0.00 31.42  ? 179 VAL A H    1 
ATOM   2825 H HA   . VAL A 1 176 ? 21.398 47.692 41.181 0.00 30.49  ? 179 VAL A HA   1 
ATOM   2826 H HB   . VAL A 1 176 ? 23.311 48.506 43.089 0.00 37.35  ? 179 VAL A HB   1 
ATOM   2827 H HG11 . VAL A 1 176 ? 22.594 50.727 42.462 0.00 42.24  ? 179 VAL A HG11 1 
ATOM   2828 H HG12 . VAL A 1 176 ? 23.608 50.025 41.461 0.00 42.24  ? 179 VAL A HG12 1 
ATOM   2829 H HG13 . VAL A 1 176 ? 22.058 50.072 41.118 0.00 42.24  ? 179 VAL A HG13 1 
ATOM   2830 H HG21 . VAL A 1 176 ? 21.692 48.713 44.458 0.00 45.19  ? 179 VAL A HG21 1 
ATOM   2831 H HG22 . VAL A 1 176 ? 20.791 49.455 43.381 0.00 45.19  ? 179 VAL A HG22 1 
ATOM   2832 H HG23 . VAL A 1 176 ? 20.817 47.867 43.438 0.00 45.19  ? 179 VAL A HG23 1 
ATOM   2833 N N    . VAL A 1 177 ? 24.457 47.061 40.510 1.00 25.86  ? 180 VAL A N    1 
ATOM   2834 C CA   . VAL A 1 177 ? 25.410 47.115 39.420 1.00 27.49  ? 180 VAL A CA   1 
ATOM   2835 C C    . VAL A 1 177 ? 24.980 46.276 38.243 1.00 26.22  ? 180 VAL A C    1 
ATOM   2836 O O    . VAL A 1 177 ? 25.009 46.713 37.069 1.00 26.59  ? 180 VAL A O    1 
ATOM   2837 C CB   . VAL A 1 177 ? 26.794 46.672 39.955 1.00 28.70  ? 180 VAL A CB   1 
ATOM   2838 C CG1  . VAL A 1 177 ? 27.762 46.562 38.755 1.00 33.59  ? 180 VAL A CG1  1 
ATOM   2839 C CG2  . VAL A 1 177 ? 27.322 47.627 41.008 1.00 35.90  ? 180 VAL A CG2  1 
ATOM   2840 H H    . VAL A 1 177 ? 24.732 46.654 41.216 0.00 31.03  ? 180 VAL A H    1 
ATOM   2841 H HA   . VAL A 1 177 ? 25.455 48.028 39.096 0.00 32.99  ? 180 VAL A HA   1 
ATOM   2842 H HB   . VAL A 1 177 ? 26.718 45.810 40.393 0.00 34.44  ? 180 VAL A HB   1 
ATOM   2843 H HG11 . VAL A 1 177 ? 28.674 46.561 39.084 0.00 40.31  ? 180 VAL A HG11 1 
ATOM   2844 H HG12 . VAL A 1 177 ? 27.582 45.736 38.278 0.00 40.31  ? 180 VAL A HG12 1 
ATOM   2845 H HG13 . VAL A 1 177 ? 27.623 47.320 38.166 0.00 40.31  ? 180 VAL A HG13 1 
ATOM   2846 H HG21 . VAL A 1 177 ? 28.185 47.311 41.317 0.00 43.08  ? 180 VAL A HG21 1 
ATOM   2847 H HG22 . VAL A 1 177 ? 27.414 48.510 40.616 0.00 43.08  ? 180 VAL A HG22 1 
ATOM   2848 H HG23 . VAL A 1 177 ? 26.697 47.658 41.749 0.00 43.08  ? 180 VAL A HG23 1 
ATOM   2849 N N    . LEU A 1 178 ? 24.594 45.018 38.476 1.00 21.68  ? 181 LEU A N    1 
ATOM   2850 C CA   . LEU A 1 178 ? 24.283 44.164 37.334 1.00 21.14  ? 181 LEU A CA   1 
ATOM   2851 C C    . LEU A 1 178 ? 22.967 44.588 36.662 1.00 22.46  ? 181 LEU A C    1 
ATOM   2852 O O    . LEU A 1 178 ? 22.898 44.612 35.408 1.00 22.63  ? 181 LEU A O    1 
ATOM   2853 C CB   . LEU A 1 178 ? 24.139 42.720 37.796 1.00 22.95  ? 181 LEU A CB   1 
ATOM   2854 C CG   . LEU A 1 178 ? 25.425 42.095 38.294 1.00 26.18  ? 181 LEU A CG   1 
ATOM   2855 C CD1  . LEU A 1 178 ? 25.014 40.677 38.785 1.00 32.95  ? 181 LEU A CD1  1 
ATOM   2856 C CD2  . LEU A 1 178 ? 26.441 42.008 37.182 1.00 32.13  ? 181 LEU A CD2  1 
ATOM   2857 H H    . LEU A 1 178 ? 24.509 44.653 39.250 0.00 26.02  ? 181 LEU A H    1 
ATOM   2858 H HA   . LEU A 1 178 ? 25.009 44.236 36.695 0.00 25.37  ? 181 LEU A HA   1 
ATOM   2859 H HB2  . LEU A 1 178 ? 23.497 42.691 38.522 0.00 27.54  ? 181 LEU A HB2  1 
ATOM   2860 H HB3  . LEU A 1 178 ? 23.822 42.187 37.050 0.00 27.54  ? 181 LEU A HB3  1 
ATOM   2861 H HG   . LEU A 1 178 ? 25.845 42.611 39.000 0.00 31.41  ? 181 LEU A HG   1 
ATOM   2862 H HD11 . LEU A 1 178 ? 25.803 40.213 39.106 0.00 39.54  ? 181 LEU A HD11 1 
ATOM   2863 H HD12 . LEU A 1 178 ? 24.368 40.767 39.503 0.00 39.54  ? 181 LEU A HD12 1 
ATOM   2864 H HD13 . LEU A 1 178 ? 24.620 40.189 38.045 0.00 39.54  ? 181 LEU A HD13 1 
ATOM   2865 H HD21 . LEU A 1 178 ? 27.173 41.439 37.467 0.00 38.56  ? 181 LEU A HD21 1 
ATOM   2866 H HD22 . LEU A 1 178 ? 26.017 41.632 36.395 0.00 38.56  ? 181 LEU A HD22 1 
ATOM   2867 H HD23 . LEU A 1 178 ? 26.772 42.899 36.987 0.00 38.56  ? 181 LEU A HD23 1 
ATOM   2868 N N    . TRP A 1 179 ? 21.933 44.929 37.455 1.00 21.43  ? 182 TRP A N    1 
ATOM   2869 C CA   . TRP A 1 179 ? 20.676 45.276 36.748 1.00 20.72  ? 182 TRP A CA   1 
ATOM   2870 C C    . TRP A 1 179 ? 20.786 46.567 35.943 1.00 22.60  ? 182 TRP A C    1 
ATOM   2871 O O    . TRP A 1 179 ? 20.180 46.656 34.853 1.00 21.77  ? 182 TRP A O    1 
ATOM   2872 C CB   . TRP A 1 179 ? 19.549 45.451 37.755 1.00 21.27  ? 182 TRP A CB   1 
ATOM   2873 C CG   . TRP A 1 179 ? 19.055 44.158 38.368 1.00 19.95  ? 182 TRP A CG   1 
ATOM   2874 C CD1  . TRP A 1 179 ? 19.765 43.086 38.678 1.00 20.76  ? 182 TRP A CD1  1 
ATOM   2875 C CD2  . TRP A 1 179 ? 17.680 43.891 38.737 1.00 20.89  ? 182 TRP A CD2  1 
ATOM   2876 N NE1  . TRP A 1 179 ? 18.898 42.091 39.279 1.00 23.66  ? 182 TRP A NE1  1 
ATOM   2877 C CE2  . TRP A 1 179 ? 17.662 42.577 39.336 1.00 20.50  ? 182 TRP A CE2  1 
ATOM   2878 C CE3  . TRP A 1 179 ? 16.499 44.641 38.638 1.00 21.98  ? 182 TRP A CE3  1 
ATOM   2879 C CZ2  . TRP A 1 179 ? 16.429 42.008 39.812 1.00 23.03  ? 182 TRP A CZ2  1 
ATOM   2880 C CZ3  . TRP A 1 179 ? 15.246 44.006 39.124 1.00 23.57  ? 182 TRP A CZ3  1 
ATOM   2881 C CH2  . TRP A 1 179 ? 15.307 42.760 39.711 1.00 22.06  ? 182 TRP A CH2  1 
ATOM   2882 H H    . TRP A 1 179 ? 21.929 44.964 38.314 0.00 25.72  ? 182 TRP A H    1 
ATOM   2883 H HA   . TRP A 1 179 ? 20.478 44.545 36.142 0.00 24.86  ? 182 TRP A HA   1 
ATOM   2884 H HB2  . TRP A 1 179 ? 19.864 46.016 38.477 0.00 25.52  ? 182 TRP A HB2  1 
ATOM   2885 H HB3  . TRP A 1 179 ? 18.798 45.870 37.308 0.00 25.52  ? 182 TRP A HB3  1 
ATOM   2886 H HD1  . TRP A 1 179 ? 20.678 42.986 38.532 0.00 24.91  ? 182 TRP A HD1  1 
ATOM   2887 H HE1  . TRP A 1 179 ? 19.144 41.314 39.554 0.00 28.39  ? 182 TRP A HE1  1 
ATOM   2888 H HE3  . TRP A 1 179 ? 16.500 45.500 38.283 0.00 26.37  ? 182 TRP A HE3  1 
ATOM   2889 H HZ2  . TRP A 1 179 ? 16.403 41.153 40.177 0.00 27.63  ? 182 TRP A HZ2  1 
ATOM   2890 H HZ3  . TRP A 1 179 ? 14.431 44.445 39.034 0.00 28.29  ? 182 TRP A HZ3  1 
ATOM   2891 H HH2  . TRP A 1 179 ? 14.521 42.410 40.062 0.00 26.47  ? 182 TRP A HH2  1 
ATOM   2892 N N    A SER A 1 180 ? 21.637 47.534 36.391 0.80 22.08  ? 183 SER A N    1 
ATOM   2893 N N    B SER A 1 180 ? 21.631 47.520 36.388 0.20 22.09  ? 183 SER A N    1 
ATOM   2894 C CA   A SER A 1 180 ? 21.808 48.797 35.669 0.80 20.67  ? 183 SER A CA   1 
ATOM   2895 C CA   B SER A 1 180 ? 21.801 48.777 35.660 0.20 20.91  ? 183 SER A CA   1 
ATOM   2896 C C    A SER A 1 180 ? 22.434 48.579 34.315 0.80 23.06  ? 183 SER A C    1 
ATOM   2897 C C    B SER A 1 180 ? 22.410 48.547 34.287 0.20 23.12  ? 183 SER A C    1 
ATOM   2898 O O    A SER A 1 180 ? 22.244 49.411 33.434 0.80 24.54  ? 183 SER A O    1 
ATOM   2899 O O    B SER A 1 180 ? 22.189 49.344 33.373 0.20 24.44  ? 183 SER A O    1 
ATOM   2900 C CB   A SER A 1 180 ? 22.618 49.792 36.471 0.80 25.56  ? 183 SER A CB   1 
ATOM   2901 C CB   B SER A 1 180 ? 22.671 49.752 36.453 0.20 25.65  ? 183 SER A CB   1 
ATOM   2902 O OG   A SER A 1 180 ? 21.935 50.146 37.652 0.80 27.13  ? 183 SER A OG   1 
ATOM   2903 O OG   B SER A 1 180 ? 24.005 49.284 36.582 0.20 26.31  ? 183 SER A OG   1 
ATOM   2904 H H    A SER A 1 180 ? 22.114 47.471 37.103 0.80 26.50  ? 183 SER A H    1 
ATOM   2905 H H    B SER A 1 180 ? 22.108 47.457 37.101 0.20 26.50  ? 183 SER A H    1 
ATOM   2906 H HA   A SER A 1 180 ? 20.933 49.198 35.544 0.80 24.81  ? 183 SER A HA   1 
ATOM   2907 H HA   B SER A 1 180 ? 20.925 49.180 35.550 0.20 25.09  ? 183 SER A HA   1 
ATOM   2908 H HB2  A SER A 1 180 ? 23.470 49.392 36.706 0.80 30.68  ? 183 SER A HB2  1 
ATOM   2909 H HB2  B SER A 1 180 ? 22.683 50.605 35.992 0.20 30.79  ? 183 SER A HB2  1 
ATOM   2910 H HB3  A SER A 1 180 ? 22.762 50.589 35.937 0.80 30.68  ? 183 SER A HB3  1 
ATOM   2911 H HB3  B SER A 1 180 ? 22.291 49.860 37.339 0.20 30.79  ? 183 SER A HB3  1 
ATOM   2912 H HG   A SER A 1 180 ? 22.369 50.731 38.071 0.80 32.55  ? 183 SER A HG   1 
ATOM   2913 H HG   B SER A 1 180 ? 24.402 49.713 37.185 0.20 31.57  ? 183 SER A HG   1 
ATOM   2914 N N    . ALA A 1 181 ? 23.185 47.466 34.111 1.00 21.00  ? 184 ALA A N    1 
ATOM   2915 C CA   . ALA A 1 181 ? 23.759 47.229 32.797 1.00 23.17  ? 184 ALA A CA   1 
ATOM   2916 C C    . ALA A 1 181 ? 22.749 46.807 31.745 1.00 21.01  ? 184 ALA A C    1 
ATOM   2917 O O    . ALA A 1 181 ? 22.993 47.072 30.544 1.00 21.54  ? 184 ALA A O    1 
ATOM   2918 C CB   . ALA A 1 181 ? 24.856 46.113 32.913 1.00 24.53  ? 184 ALA A CB   1 
ATOM   2919 H H    . ALA A 1 181 ? 23.358 46.868 34.705 0.00 25.20  ? 184 ALA A H    1 
ATOM   2920 H HA   . ALA A 1 181 ? 24.146 48.066 32.498 0.00 27.80  ? 184 ALA A HA   1 
ATOM   2921 H HB1  . ALA A 1 181 ? 25.243 45.958 32.037 0.00 29.44  ? 184 ALA A HB1  1 
ATOM   2922 H HB2  . ALA A 1 181 ? 25.543 46.409 33.530 0.00 29.44  ? 184 ALA A HB2  1 
ATOM   2923 H HB3  . ALA A 1 181 ? 24.445 45.298 33.241 0.00 29.44  ? 184 ALA A HB3  1 
ATOM   2924 N N    . TYR A 1 182 ? 21.648 46.145 32.128 1.00 19.12  ? 185 TYR A N    1 
ATOM   2925 C CA   . TYR A 1 182 ? 20.664 45.682 31.115 1.00 18.11  ? 185 TYR A CA   1 
ATOM   2926 C C    . TYR A 1 182 ? 20.117 46.788 30.229 1.00 19.44  ? 185 TYR A C    1 
ATOM   2927 O O    . TYR A 1 182 ? 20.088 46.578 28.995 1.00 19.48  ? 185 TYR A O    1 
ATOM   2928 C CB   . TYR A 1 182 ? 19.523 44.890 31.814 1.00 19.60  ? 185 TYR A CB   1 
ATOM   2929 C CG   . TYR A 1 182 ? 19.913 43.512 32.307 1.00 17.92  ? 185 TYR A CG   1 
ATOM   2930 C CD1  . TYR A 1 182 ? 20.608 43.385 33.503 1.00 19.37  ? 185 TYR A CD1  1 
ATOM   2931 C CD2  . TYR A 1 182 ? 19.536 42.362 31.550 1.00 19.93  ? 185 TYR A CD2  1 
ATOM   2932 C CE1  . TYR A 1 182 ? 20.913 42.072 33.953 1.00 21.18  ? 185 TYR A CE1  1 
ATOM   2933 C CE2  . TYR A 1 182 ? 19.844 41.124 32.017 1.00 19.54  ? 185 TYR A CE2  1 
ATOM   2934 C CZ   . TYR A 1 182 ? 20.476 41.018 33.182 1.00 18.97  ? 185 TYR A CZ   1 
ATOM   2935 O OH   . TYR A 1 182 ? 20.840 39.756 33.730 1.00 20.21  ? 185 TYR A OH   1 
ATOM   2936 H H    . TYR A 1 182 ? 21.446 45.953 32.941 0.00 22.94  ? 185 TYR A H    1 
ATOM   2937 H HA   . TYR A 1 182 ? 21.142 45.076 30.527 0.00 21.73  ? 185 TYR A HA   1 
ATOM   2938 H HB2  . TYR A 1 182 ? 19.221 45.400 32.583 0.00 23.52  ? 185 TYR A HB2  1 
ATOM   2939 H HB3  . TYR A 1 182 ? 18.795 44.779 31.183 0.00 23.52  ? 185 TYR A HB3  1 
ATOM   2940 H HD1  . TYR A 1 182 ? 20.863 44.133 33.992 0.00 23.25  ? 185 TYR A HD1  1 
ATOM   2941 H HD2  . TYR A 1 182 ? 19.083 42.460 30.744 0.00 23.92  ? 185 TYR A HD2  1 
ATOM   2942 H HE1  . TYR A 1 182 ? 21.391 41.929 34.738 0.00 25.41  ? 185 TYR A HE1  1 
ATOM   2943 H HE2  . TYR A 1 182 ? 19.617 40.365 31.530 0.00 23.44  ? 185 TYR A HE2  1 
ATOM   2944 H HH   . TYR A 1 182 ? 20.584 39.137 33.223 0.00 24.25  ? 185 TYR A HH   1 
ATOM   2945 N N    . PRO A 1 183 ? 19.634 47.930 30.723 1.00 19.86  ? 186 PRO A N    1 
ATOM   2946 C CA   . PRO A 1 183 ? 19.163 48.959 29.786 1.00 19.41  ? 186 PRO A CA   1 
ATOM   2947 C C    . PRO A 1 183 ? 20.198 49.495 28.875 1.00 19.94  ? 186 PRO A C    1 
ATOM   2948 O O    . PRO A 1 183 ? 19.880 49.928 27.746 1.00 20.45  ? 186 PRO A O    1 
ATOM   2949 C CB   . PRO A 1 183 ? 18.587 50.064 30.691 1.00 21.75  ? 186 PRO A CB   1 
ATOM   2950 C CG   . PRO A 1 183 ? 19.199 49.787 32.131 1.00 22.90  ? 186 PRO A CG   1 
ATOM   2951 C CD   . PRO A 1 183 ? 19.296 48.246 32.150 1.00 20.41  ? 186 PRO A CD   1 
ATOM   2952 H HA   . PRO A 1 183 ? 18.447 48.575 29.257 0.00 23.29  ? 186 PRO A HA   1 
ATOM   2953 H HB2  . PRO A 1 183 ? 18.859 50.935 30.361 0.00 26.10  ? 186 PRO A HB2  1 
ATOM   2954 H HB3  . PRO A 1 183 ? 17.619 50.003 30.709 0.00 26.10  ? 186 PRO A HB3  1 
ATOM   2955 H HG2  . PRO A 1 183 ? 20.072 50.201 32.217 0.00 27.48  ? 186 PRO A HG2  1 
ATOM   2956 H HG3  . PRO A 1 183 ? 18.606 50.117 32.824 0.00 27.48  ? 186 PRO A HG3  1 
ATOM   2957 H HD2  . PRO A 1 183 ? 19.997 47.948 32.750 0.00 24.49  ? 186 PRO A HD2  1 
ATOM   2958 H HD3  . PRO A 1 183 ? 18.449 47.847 32.405 0.00 24.49  ? 186 PRO A HD3  1 
ATOM   2959 N N    . VAL A 1 184 ? 21.463 49.490 29.302 1.00 21.34  ? 187 VAL A N    1 
ATOM   2960 C CA   . VAL A 1 184 ? 22.555 49.967 28.422 1.00 23.34  ? 187 VAL A CA   1 
ATOM   2961 C C    . VAL A 1 184 ? 22.768 48.963 27.310 1.00 20.61  ? 187 VAL A C    1 
ATOM   2962 O O    . VAL A 1 184 ? 22.888 49.395 26.129 1.00 22.35  ? 187 VAL A O    1 
ATOM   2963 C CB   . VAL A 1 184 ? 23.819 50.147 29.259 1.00 24.89  ? 187 VAL A CB   1 
ATOM   2964 C CG1  . VAL A 1 184 ? 24.918 50.750 28.302 1.00 25.38  ? 187 VAL A CG1  1 
ATOM   2965 C CG2  . VAL A 1 184 ? 23.582 51.231 30.337 1.00 25.26  ? 187 VAL A CG2  1 
ATOM   2966 H H    . VAL A 1 184 ? 21.718 49.223 30.079 0.00 25.61  ? 187 VAL A H    1 
ATOM   2967 H HA   . VAL A 1 184 ? 22.321 50.820 28.025 0.00 28.01  ? 187 VAL A HA   1 
ATOM   2968 H HB   . VAL A 1 184 ? 24.073 49.303 29.664 0.00 29.87  ? 187 VAL A HB   1 
ATOM   2969 H HG11 . VAL A 1 184 ? 25.666 51.060 28.836 0.00 30.45  ? 187 VAL A HG11 1 
ATOM   2970 H HG12 . VAL A 1 184 ? 25.213 50.061 27.687 0.00 30.45  ? 187 VAL A HG12 1 
ATOM   2971 H HG13 . VAL A 1 184 ? 24.534 51.492 27.809 0.00 30.45  ? 187 VAL A HG13 1 
ATOM   2972 H HG21 . VAL A 1 184 ? 24.404 51.369 30.833 0.00 30.31  ? 187 VAL A HG21 1 
ATOM   2973 H HG22 . VAL A 1 184 ? 23.315 52.056 29.902 0.00 30.31  ? 187 VAL A HG22 1 
ATOM   2974 H HG23 . VAL A 1 184 ? 22.881 50.931 30.937 0.00 30.31  ? 187 VAL A HG23 1 
ATOM   2975 N N    . VAL A 1 185 ? 22.812 47.682 27.609 1.00 21.09  ? 188 VAL A N    1 
ATOM   2976 C CA   . VAL A 1 185 ? 22.973 46.659 26.532 1.00 20.67  ? 188 VAL A CA   1 
ATOM   2977 C C    . VAL A 1 185 ? 21.849 46.738 25.530 1.00 22.48  ? 188 VAL A C    1 
ATOM   2978 O O    . VAL A 1 185 ? 22.080 46.652 24.298 1.00 23.68  ? 188 VAL A O    1 
ATOM   2979 C CB   . VAL A 1 185 ? 23.109 45.272 27.157 1.00 21.34  ? 188 VAL A CB   1 
ATOM   2980 C CG1  . VAL A 1 185 ? 23.172 44.237 26.011 1.00 24.38  ? 188 VAL A CG1  1 
ATOM   2981 C CG2  . VAL A 1 185 ? 24.375 45.209 28.034 1.00 23.58  ? 188 VAL A CG2  1 
ATOM   2982 H H    . VAL A 1 185 ? 22.754 47.359 28.404 0.00 25.30  ? 188 VAL A H    1 
ATOM   2983 H HA   . VAL A 1 185 ? 23.789 46.848 26.042 0.00 24.81  ? 188 VAL A HA   1 
ATOM   2984 H HB   . VAL A 1 185 ? 22.352 45.072 27.729 0.00 25.61  ? 188 VAL A HB   1 
ATOM   2985 H HG11 . VAL A 1 185 ? 23.493 43.393 26.364 0.00 29.25  ? 188 VAL A HG11 1 
ATOM   2986 H HG12 . VAL A 1 185 ? 22.283 44.123 25.640 0.00 29.25  ? 188 VAL A HG12 1 
ATOM   2987 H HG13 . VAL A 1 185 ? 23.777 44.561 25.325 0.00 29.25  ? 188 VAL A HG13 1 
ATOM   2988 H HG21 . VAL A 1 185 ? 24.439 44.328 28.433 0.00 28.30  ? 188 VAL A HG21 1 
ATOM   2989 H HG22 . VAL A 1 185 ? 25.153 45.378 27.479 0.00 28.30  ? 188 VAL A HG22 1 
ATOM   2990 H HG23 . VAL A 1 185 ? 24.312 45.883 28.729 0.00 28.30  ? 188 VAL A HG23 1 
ATOM   2991 N N    . TRP A 1 186 ? 20.595 46.902 26.003 1.00 19.48  ? 189 TRP A N    1 
ATOM   2992 C CA   . TRP A 1 186 ? 19.476 46.967 25.096 1.00 21.22  ? 189 TRP A CA   1 
ATOM   2993 C C    . TRP A 1 186 ? 19.597 48.195 24.195 1.00 21.34  ? 189 TRP A C    1 
ATOM   2994 O O    . TRP A 1 186 ? 19.343 48.098 22.959 1.00 22.24  ? 189 TRP A O    1 
ATOM   2995 C CB   . TRP A 1 186 ? 18.234 47.053 26.015 1.00 19.61  ? 189 TRP A CB   1 
ATOM   2996 C CG   . TRP A 1 186 ? 16.892 46.815 25.350 1.00 18.95  ? 189 TRP A CG   1 
ATOM   2997 C CD1  . TRP A 1 186 ? 16.131 45.651 25.520 1.00 20.47  ? 189 TRP A CD1  1 
ATOM   2998 C CD2  . TRP A 1 186 ? 16.076 47.770 24.621 1.00 19.11  ? 189 TRP A CD2  1 
ATOM   2999 N NE1  . TRP A 1 186 ? 14.917 45.876 24.884 1.00 21.29  ? 189 TRP A NE1  1 
ATOM   3000 C CE2  . TRP A 1 186 ? 14.851 47.119 24.350 1.00 21.16  ? 189 TRP A CE2  1 
ATOM   3001 C CE3  . TRP A 1 186 ? 16.274 49.056 24.108 1.00 21.36  ? 189 TRP A CE3  1 
ATOM   3002 C CZ2  . TRP A 1 186 ? 13.784 47.772 23.667 1.00 24.07  ? 189 TRP A CZ2  1 
ATOM   3003 C CZ3  . TRP A 1 186 ? 15.249 49.747 23.427 1.00 25.24  ? 189 TRP A CZ3  1 
ATOM   3004 C CH2  . TRP A 1 186 ? 14.035 49.058 23.134 1.00 24.81  ? 189 TRP A CH2  1 
ATOM   3005 H H    . TRP A 1 186 ? 20.388 46.975 26.834 0.00 23.38  ? 189 TRP A H    1 
ATOM   3006 H HA   . TRP A 1 186 ? 19.414 46.200 24.505 0.00 25.47  ? 189 TRP A HA   1 
ATOM   3007 H HB2  . TRP A 1 186 ? 18.329 46.388 26.714 0.00 23.54  ? 189 TRP A HB2  1 
ATOM   3008 H HB3  . TRP A 1 186 ? 18.207 47.942 26.403 0.00 23.54  ? 189 TRP A HB3  1 
ATOM   3009 H HD1  . TRP A 1 186 ? 16.388 44.880 25.971 0.00 24.57  ? 189 TRP A HD1  1 
ATOM   3010 H HE1  . TRP A 1 186 ? 14.284 45.296 24.836 0.00 25.54  ? 189 TRP A HE1  1 
ATOM   3011 H HE3  . TRP A 1 186 ? 17.101 49.467 24.220 0.00 25.64  ? 189 TRP A HE3  1 
ATOM   3012 H HZ2  . TRP A 1 186 ? 12.952 47.366 23.575 0.00 28.88  ? 189 TRP A HZ2  1 
ATOM   3013 H HZ3  . TRP A 1 186 ? 15.364 50.634 23.173 0.00 30.29  ? 189 TRP A HZ3  1 
ATOM   3014 H HH2  . TRP A 1 186 ? 13.400 49.460 22.587 0.00 29.77  ? 189 TRP A HH2  1 
ATOM   3015 N N    . LEU A 1 187 ? 19.957 49.343 24.781 1.00 21.39  ? 190 LEU A N    1 
ATOM   3016 C CA   . LEU A 1 187 ? 20.016 50.578 24.006 1.00 22.58  ? 190 LEU A CA   1 
ATOM   3017 C C    . LEU A 1 187 ? 21.063 50.522 22.923 1.00 25.59  ? 190 LEU A C    1 
ATOM   3018 O O    . LEU A 1 187 ? 20.786 50.988 21.812 1.00 26.16  ? 190 LEU A O    1 
ATOM   3019 C CB   . LEU A 1 187 ? 20.269 51.737 24.988 1.00 23.55  ? 190 LEU A CB   1 
ATOM   3020 C CG   . LEU A 1 187 ? 20.222 53.113 24.386 1.00 26.74  ? 190 LEU A CG   1 
ATOM   3021 C CD1  . LEU A 1 187 ? 18.823 53.437 24.042 1.00 33.28  ? 190 LEU A CD1  1 
ATOM   3022 C CD2  . LEU A 1 187 ? 20.739 54.055 25.572 1.00 32.56  ? 190 LEU A CD2  1 
ATOM   3023 H H    . LEU A 1 187 ? 20.168 49.429 25.611 0.00 25.67  ? 190 LEU A H    1 
ATOM   3024 H HA   . LEU A 1 187 ? 19.174 50.727 23.549 0.00 27.09  ? 190 LEU A HA   1 
ATOM   3025 H HB2  . LEU A 1 187 ? 19.593 51.702 25.683 0.00 28.27  ? 190 LEU A HB2  1 
ATOM   3026 H HB3  . LEU A 1 187 ? 21.151 51.621 25.377 0.00 28.27  ? 190 LEU A HB3  1 
ATOM   3027 H HG   . LEU A 1 187 ? 20.748 53.216 23.578 0.00 32.09  ? 190 LEU A HG   1 
ATOM   3028 H HD11 . LEU A 1 187 ? 18.780 54.352 23.724 0.00 39.94  ? 190 LEU A HD11 1 
ATOM   3029 H HD12 . LEU A 1 187 ? 18.520 52.831 23.348 0.00 39.94  ? 190 LEU A HD12 1 
ATOM   3030 H HD13 . LEU A 1 187 ? 18.272 53.336 24.833 0.00 39.94  ? 190 LEU A HD13 1 
ATOM   3031 H HD21 . LEU A 1 187 ? 20.696 54.980 25.283 0.00 39.07  ? 190 LEU A HD21 1 
ATOM   3032 H HD22 . LEU A 1 187 ? 20.173 53.925 26.349 0.00 39.07  ? 190 LEU A HD22 1 
ATOM   3033 H HD23 . LEU A 1 187 ? 21.655 53.819 25.787 0.00 39.07  ? 190 LEU A HD23 1 
ATOM   3034 N N    . ILE A 1 188 ? 22.227 49.901 23.177 1.00 24.92  ? 191 ILE A N    1 
ATOM   3035 C CA   . ILE A 1 188 ? 23.333 49.856 22.171 1.00 26.53  ? 191 ILE A CA   1 
ATOM   3036 C C    . ILE A 1 188 ? 23.227 48.654 21.264 1.00 25.71  ? 191 ILE A C    1 
ATOM   3037 O O    . ILE A 1 188 ? 23.908 48.587 20.219 1.00 28.38  ? 191 ILE A O    1 
ATOM   3038 C CB   . ILE A 1 188 ? 24.703 49.949 22.896 1.00 25.47  ? 191 ILE A CB   1 
ATOM   3039 C CG1  . ILE A 1 188 ? 24.967 48.702 23.654 1.00 31.22  ? 191 ILE A CG1  1 
ATOM   3040 C CG2  . ILE A 1 188 ? 24.724 51.265 23.696 1.00 39.90  ? 191 ILE A CG2  1 
ATOM   3041 C CD1  . ILE A 1 188 ? 26.310 48.847 24.510 1.00 46.22  ? 191 ILE A CD1  1 
ATOM   3042 H H    . ILE A 1 188 ? 22.411 49.499 23.914 0.00 29.91  ? 191 ILE A H    1 
ATOM   3043 H HA   . ILE A 1 188 ? 23.283 50.622 21.578 0.00 31.84  ? 191 ILE A HA   1 
ATOM   3044 H HB   . ILE A 1 188 ? 25.452 49.999 22.282 0.00 30.56  ? 191 ILE A HB   1 
ATOM   3045 H HG12 . ILE A 1 188 ? 24.230 48.527 24.260 0.00 37.47  ? 191 ILE A HG12 1 
ATOM   3046 H HG13 . ILE A 1 188 ? 25.071 47.961 23.036 0.00 37.47  ? 191 ILE A HG13 1 
ATOM   3047 H HG21 . ILE A 1 188 ? 25.628 51.434 24.003 0.00 47.88  ? 191 ILE A HG21 1 
ATOM   3048 H HG22 . ILE A 1 188 ? 24.429 51.989 23.121 0.00 47.88  ? 191 ILE A HG22 1 
ATOM   3049 H HG23 . ILE A 1 188 ? 24.127 51.182 24.456 0.00 47.88  ? 191 ILE A HG23 1 
ATOM   3050 H HD11 . ILE A 1 188 ? 26.543 47.982 24.881 0.00 55.46  ? 191 ILE A HD11 1 
ATOM   3051 H HD12 . ILE A 1 188 ? 27.022 49.161 23.930 0.00 55.46  ? 191 ILE A HD12 1 
ATOM   3052 H HD13 . ILE A 1 188 ? 26.161 49.485 25.225 0.00 55.46  ? 191 ILE A HD13 1 
ATOM   3053 N N    . GLY A 1 189 ? 22.420 47.631 21.576 1.00 24.72  ? 192 GLY A N    1 
ATOM   3054 C CA   . GLY A 1 189 ? 22.335 46.384 20.829 1.00 25.32  ? 192 GLY A CA   1 
ATOM   3055 C C    . GLY A 1 189 ? 21.235 46.376 19.783 1.00 25.35  ? 192 GLY A C    1 
ATOM   3056 O O    . GLY A 1 189 ? 20.752 47.431 19.327 1.00 25.19  ? 192 GLY A O    1 
ATOM   3057 H H    . GLY A 1 189 ? 21.887 47.644 22.251 0.00 29.67  ? 192 GLY A H    1 
ATOM   3058 H HA2  . GLY A 1 189 ? 23.179 46.228 20.378 0.00 30.38  ? 192 GLY A HA2  1 
ATOM   3059 H HA3  . GLY A 1 189 ? 22.167 45.656 21.447 0.00 30.38  ? 192 GLY A HA3  1 
ATOM   3060 N N    A SER A 1 190 ? 20.871 45.189 19.384 0.69 26.00  ? 193 SER A N    1 
ATOM   3061 N N    B SER A 1 190 ? 20.845 45.183 19.382 0.31 26.12  ? 193 SER A N    1 
ATOM   3062 C CA   A SER A 1 190 ? 19.967 44.974 18.260 0.69 27.63  ? 193 SER A CA   1 
ATOM   3063 C CA   B SER A 1 190 ? 19.959 44.992 18.239 0.31 27.65  ? 193 SER A CA   1 
ATOM   3064 C C    A SER A 1 190 ? 18.594 45.571 18.477 0.69 28.33  ? 193 SER A C    1 
ATOM   3065 C C    B SER A 1 190 ? 18.522 45.408 18.487 0.31 28.26  ? 193 SER A C    1 
ATOM   3066 O O    A SER A 1 190 ? 17.964 46.002 17.506 0.69 31.48  ? 193 SER A O    1 
ATOM   3067 O O    B SER A 1 190 ? 17.740 45.453 17.536 0.31 25.91  ? 193 SER A O    1 
ATOM   3068 C CB   A SER A 1 190 ? 19.828 43.455 17.985 0.69 30.41  ? 193 SER A CB   1 
ATOM   3069 C CB   B SER A 1 190 ? 19.948 43.513 17.846 0.31 31.02  ? 193 SER A CB   1 
ATOM   3070 O OG   A SER A 1 190 ? 19.266 42.744 19.061 0.69 32.34  ? 193 SER A OG   1 
ATOM   3071 O OG   B SER A 1 190 ? 21.055 43.230 17.033 0.31 33.45  ? 193 SER A OG   1 
ATOM   3072 H H    A SER A 1 190 ? 21.134 44.456 19.750 0.69 31.20  ? 193 SER A H    1 
ATOM   3073 H H    B SER A 1 190 ? 21.082 44.447 19.759 0.31 31.34  ? 193 SER A H    1 
ATOM   3074 H HA   A SER A 1 190 ? 20.354 45.411 17.486 0.69 33.15  ? 193 SER A HA   1 
ATOM   3075 H HA   B SER A 1 190 ? 20.307 45.533 17.513 0.31 33.19  ? 193 SER A HA   1 
ATOM   3076 H HB2  A SER A 1 190 ? 19.258 43.336 17.209 0.69 36.50  ? 193 SER A HB2  1 
ATOM   3077 H HB2  B SER A 1 190 ? 19.992 42.969 18.648 0.31 37.22  ? 193 SER A HB2  1 
ATOM   3078 H HB3  A SER A 1 190 ? 20.711 43.094 17.808 0.69 36.50  ? 193 SER A HB3  1 
ATOM   3079 H HB3  B SER A 1 190 ? 19.133 43.318 17.358 0.31 37.22  ? 193 SER A HB3  1 
ATOM   3080 H HG   A SER A 1 190 ? 19.794 42.747 19.714 0.69 38.81  ? 193 SER A HG   1 
ATOM   3081 H HG   B SER A 1 190 ? 21.090 43.776 16.396 0.31 40.14  ? 193 SER A HG   1 
ATOM   3082 N N    . GLU A 1 191 ? 18.132 45.635 19.724 1.00 24.69  ? 194 GLU A N    1 
ATOM   3083 C CA   . GLU A 1 191 ? 16.802 46.166 19.994 1.00 24.34  ? 194 GLU A CA   1 
ATOM   3084 C C    . GLU A 1 191 ? 16.746 47.644 19.910 1.00 25.13  ? 194 GLU A C    1 
ATOM   3085 O O    . GLU A 1 191 ? 15.664 48.213 19.778 1.00 25.22  ? 194 GLU A O    1 
ATOM   3086 C CB   . GLU A 1 191 ? 16.416 45.806 21.462 1.00 25.50  ? 194 GLU A CB   1 
ATOM   3087 C CG   . GLU A 1 191 ? 16.129 44.340 21.665 1.00 29.99  ? 194 GLU A CG   1 
ATOM   3088 C CD   . GLU A 1 191 ? 17.356 43.554 21.992 1.00 31.02  ? 194 GLU A CD   1 
ATOM   3089 O OE1  . GLU A 1 191 ? 18.453 44.115 22.124 1.00 29.13  ? 194 GLU A OE1  1 
ATOM   3090 O OE2  . GLU A 1 191 ? 17.186 42.316 22.188 1.00 41.72  ? 194 GLU A OE2  1 
ATOM   3091 H H    . GLU A 1 191 ? 18.563 45.379 20.423 0.00 29.63  ? 194 GLU A H    1 
ATOM   3092 H HA   . GLU A 1 191 ? 16.178 45.782 19.358 0.00 29.21  ? 194 GLU A HA   1 
ATOM   3093 H HB2  . GLU A 1 191 ? 17.151 46.048 22.047 0.00 30.60  ? 194 GLU A HB2  1 
ATOM   3094 H HB3  . GLU A 1 191 ? 15.619 46.302 21.706 0.00 30.60  ? 194 GLU A HB3  1 
ATOM   3095 H HG2  . GLU A 1 191 ? 15.503 44.239 22.400 0.00 35.99  ? 194 GLU A HG2  1 
ATOM   3096 H HG3  . GLU A 1 191 ? 15.747 43.976 20.851 0.00 35.99  ? 194 GLU A HG3  1 
ATOM   3097 N N    . GLY A 1 192 ? 17.884 48.287 20.003 1.00 23.40  ? 195 GLY A N    1 
ATOM   3098 C CA   . GLY A 1 192 ? 17.995 49.744 20.087 1.00 26.20  ? 195 GLY A CA   1 
ATOM   3099 C C    . GLY A 1 192 ? 18.693 50.360 18.935 1.00 27.02  ? 195 GLY A C    1 
ATOM   3100 O O    . GLY A 1 192 ? 18.258 50.245 17.770 1.00 30.92  ? 195 GLY A O    1 
ATOM   3101 H H    . GLY A 1 192 ? 18.649 47.895 20.021 0.00 28.08  ? 195 GLY A H    1 
ATOM   3102 H HA2  . GLY A 1 192 ? 17.105 50.126 20.137 0.00 31.44  ? 195 GLY A HA2  1 
ATOM   3103 H HA3  . GLY A 1 192 ? 18.484 49.977 20.892 0.00 31.44  ? 195 GLY A HA3  1 
ATOM   3104 N N    . ALA A 1 193 ? 19.841 51.031 19.225 1.00 24.77  ? 196 ALA A N    1 
ATOM   3105 C CA   . ALA A 1 193 ? 20.570 51.746 18.203 1.00 27.22  ? 196 ALA A CA   1 
ATOM   3106 C C    . ALA A 1 193 ? 21.356 50.849 17.238 1.00 30.94  ? 196 ALA A C    1 
ATOM   3107 O O    . ALA A 1 193 ? 21.815 51.352 16.167 1.00 33.19  ? 196 ALA A O    1 
ATOM   3108 C CB   . ALA A 1 193 ? 21.532 52.726 18.892 1.00 30.71  ? 196 ALA A CB   1 
ATOM   3109 H H    . ALA A 1 193 ? 20.197 51.073 20.007 0.00 29.73  ? 196 ALA A H    1 
ATOM   3110 H HA   . ALA A 1 193 ? 19.931 52.231 17.656 0.00 32.67  ? 196 ALA A HA   1 
ATOM   3111 H HB1  . ALA A 1 193 ? 22.026 53.213 18.215 0.00 36.85  ? 196 ALA A HB1  1 
ATOM   3112 H HB2  . ALA A 1 193 ? 21.018 53.344 19.435 0.00 36.85  ? 196 ALA A HB2  1 
ATOM   3113 H HB3  . ALA A 1 193 ? 22.145 52.225 19.453 0.00 36.85  ? 196 ALA A HB3  1 
ATOM   3114 N N    . GLY A 1 194 ? 21.618 49.577 17.582 1.00 27.18  ? 197 GLY A N    1 
ATOM   3115 C CA   . GLY A 1 194 ? 22.217 48.678 16.594 1.00 28.37  ? 197 GLY A CA   1 
ATOM   3116 C C    . GLY A 1 194 ? 23.709 48.831 16.450 1.00 32.78  ? 197 GLY A C    1 
ATOM   3117 O O    . GLY A 1 194 ? 24.215 48.478 15.387 1.00 35.40  ? 197 GLY A O    1 
ATOM   3118 H H    . GLY A 1 194 ? 21.463 49.228 18.353 0.00 32.62  ? 197 GLY A H    1 
ATOM   3119 H HA2  . GLY A 1 194 ? 22.033 47.761 16.852 0.00 34.05  ? 197 GLY A HA2  1 
ATOM   3120 H HA3  . GLY A 1 194 ? 21.813 48.850 15.729 0.00 34.05  ? 197 GLY A HA3  1 
ATOM   3121 N N    . ILE A 1 195 ? 24.408 49.345 17.454 1.00 27.53  ? 198 ILE A N    1 
ATOM   3122 C CA   . ILE A 1 195 ? 25.875 49.607 17.386 1.00 28.04  ? 198 ILE A CA   1 
ATOM   3123 C C    . ILE A 1 195 ? 26.630 48.309 17.669 1.00 36.26  ? 198 ILE A C    1 
ATOM   3124 O O    . ILE A 1 195 ? 27.635 48.072 17.000 1.00 38.19  ? 198 ILE A O    1 
ATOM   3125 C CB   . ILE A 1 195 ? 26.264 50.715 18.382 1.00 33.69  ? 198 ILE A CB   1 
ATOM   3126 C CG1  . ILE A 1 195 ? 25.454 51.993 18.159 1.00 42.41  ? 198 ILE A CG1  1 
ATOM   3127 C CG2  . ILE A 1 195 ? 27.758 50.976 18.334 1.00 41.88  ? 198 ILE A CG2  1 
ATOM   3128 C CD1  . ILE A 1 195 ? 25.402 52.437 16.723 1.00 54.33  ? 198 ILE A CD1  1 
ATOM   3129 H H    . ILE A 1 195 ? 24.040 49.536 18.266 0.00 33.04  ? 198 ILE A H    1 
ATOM   3130 H HA   . ILE A 1 195 ? 26.096 49.907 16.488 0.00 33.65  ? 198 ILE A HA   1 
ATOM   3131 H HB   . ILE A 1 195 ? 26.048 50.383 19.289 0.00 40.43  ? 198 ILE A HB   1 
ATOM   3132 H HG12 . ILE A 1 195 ? 24.538 51.845 18.476 0.00 50.89  ? 198 ILE A HG12 1 
ATOM   3133 H HG13 . ILE A 1 195 ? 25.848 52.713 18.697 0.00 50.89  ? 198 ILE A HG13 1 
ATOM   3134 H HG21 . ILE A 1 195 ? 27.974 51.734 18.903 0.00 50.26  ? 198 ILE A HG21 1 
ATOM   3135 H HG22 . ILE A 1 195 ? 28.238 50.190 18.647 0.00 50.26  ? 198 ILE A HG22 1 
ATOM   3136 H HG23 . ILE A 1 195 ? 28.023 51.174 17.419 0.00 50.26  ? 198 ILE A HG23 1 
ATOM   3137 H HD11 . ILE A 1 195 ? 24.971 53.307 16.667 0.00 65.20  ? 198 ILE A HD11 1 
ATOM   3138 H HD12 . ILE A 1 195 ? 26.306 52.500 16.370 0.00 65.20  ? 198 ILE A HD12 1 
ATOM   3139 H HD13 . ILE A 1 195 ? 24.896 51.790 16.201 0.00 65.20  ? 198 ILE A HD13 1 
ATOM   3140 N N    . VAL A 1 196 ? 26.175 47.517 18.634 1.00 29.42  ? 199 VAL A N    1 
ATOM   3141 C CA   . VAL A 1 196 ? 26.802 46.239 19.019 1.00 29.82  ? 199 VAL A CA   1 
ATOM   3142 C C    . VAL A 1 196 ? 26.040 45.127 18.301 1.00 29.23  ? 199 VAL A C    1 
ATOM   3143 O O    . VAL A 1 196 ? 24.784 45.103 18.360 1.00 28.61  ? 199 VAL A O    1 
ATOM   3144 C CB   . VAL A 1 196 ? 26.665 46.069 20.562 1.00 33.10  ? 199 VAL A CB   1 
ATOM   3145 C CG1  . VAL A 1 196 ? 27.091 44.665 21.091 1.00 38.50  ? 199 VAL A CG1  1 
ATOM   3146 C CG2  . VAL A 1 196 ? 27.531 47.192 21.224 1.00 36.76  ? 199 VAL A CG2  1 
ATOM   3147 H H    . VAL A 1 196 ? 25.484 47.706 19.109 0.00 35.30  ? 199 VAL A H    1 
ATOM   3148 H HA   . VAL A 1 196 ? 27.734 46.199 18.754 0.00 35.78  ? 199 VAL A HA   1 
ATOM   3149 H HB   . VAL A 1 196 ? 25.728 46.144 20.802 0.00 39.72  ? 199 VAL A HB   1 
ATOM   3150 H HG11 . VAL A 1 196 ? 27.063 44.671 22.060 0.00 46.20  ? 199 VAL A HG11 1 
ATOM   3151 H HG12 . VAL A 1 196 ? 26.477 43.998 20.746 0.00 46.20  ? 199 VAL A HG12 1 
ATOM   3152 H HG13 . VAL A 1 196 ? 27.992 44.473 20.787 0.00 46.20  ? 199 VAL A HG13 1 
ATOM   3153 H HG21 . VAL A 1 196 ? 27.573 47.035 22.180 0.00 44.12  ? 199 VAL A HG21 1 
ATOM   3154 H HG22 . VAL A 1 196 ? 28.423 47.167 20.845 0.00 44.12  ? 199 VAL A HG22 1 
ATOM   3155 H HG23 . VAL A 1 196 ? 27.120 48.053 21.047 0.00 44.12  ? 199 VAL A HG23 1 
ATOM   3156 N N    . PRO A 1 197 ? 26.722 44.194 17.616 1.00 26.69  ? 200 PRO A N    1 
ATOM   3157 C CA   . PRO A 1 197 ? 26.004 43.124 16.910 1.00 26.14  ? 200 PRO A CA   1 
ATOM   3158 C C    . PRO A 1 197 ? 25.304 42.128 17.858 1.00 26.93  ? 200 PRO A C    1 
ATOM   3159 O O    . PRO A 1 197 ? 25.718 41.957 18.980 1.00 27.29  ? 200 PRO A O    1 
ATOM   3160 C CB   . PRO A 1 197 ? 27.118 42.427 16.126 1.00 33.80  ? 200 PRO A CB   1 
ATOM   3161 C CG   . PRO A 1 197 ? 28.340 42.897 16.637 1.00 41.50  ? 200 PRO A CG   1 
ATOM   3162 C CD   . PRO A 1 197 ? 28.162 44.177 17.360 1.00 32.22  ? 200 PRO A CD   1 
ATOM   3163 H HA   . PRO A 1 197 ? 25.341 43.507 16.315 0.00 31.36  ? 200 PRO A HA   1 
ATOM   3164 H HB2  . PRO A 1 197 ? 27.046 41.468 16.248 0.00 40.57  ? 200 PRO A HB2  1 
ATOM   3165 H HB3  . PRO A 1 197 ? 27.037 42.649 15.185 0.00 40.57  ? 200 PRO A HB3  1 
ATOM   3166 H HG2  . PRO A 1 197 ? 28.693 42.228 17.245 0.00 49.80  ? 200 PRO A HG2  1 
ATOM   3167 H HG3  . PRO A 1 197 ? 28.951 43.026 15.895 0.00 49.80  ? 200 PRO A HG3  1 
ATOM   3168 H HD2  . PRO A 1 197 ? 28.664 44.181 18.190 0.00 38.66  ? 200 PRO A HD2  1 
ATOM   3169 H HD3  . PRO A 1 197 ? 28.427 44.929 16.807 0.00 38.66  ? 200 PRO A HD3  1 
ATOM   3170 N N    . LEU A 1 198 ? 24.312 41.437 17.311 1.00 27.63  ? 201 LEU A N    1 
ATOM   3171 C CA   . LEU A 1 198 ? 23.535 40.464 18.125 1.00 24.28  ? 201 LEU A CA   1 
ATOM   3172 C C    . LEU A 1 198 ? 24.398 39.406 18.774 1.00 26.80  ? 201 LEU A C    1 
ATOM   3173 O O    . LEU A 1 198 ? 24.117 39.012 19.898 1.00 25.65  ? 201 LEU A O    1 
ATOM   3174 C CB   . LEU A 1 198 ? 22.426 39.808 17.220 1.00 25.76  ? 201 LEU A CB   1 
ATOM   3175 C CG   . LEU A 1 198 ? 21.487 38.836 17.873 1.00 25.98  ? 201 LEU A CG   1 
ATOM   3176 C CD1  . LEU A 1 198 ? 20.744 39.438 19.070 1.00 26.11  ? 201 LEU A CD1  1 
ATOM   3177 C CD2  . LEU A 1 198 ? 20.458 38.398 16.838 1.00 32.28  ? 201 LEU A CD2  1 
ATOM   3178 H H    . LEU A 1 198 ? 24.061 41.500 16.491 0.00 33.16  ? 201 LEU A H    1 
ATOM   3179 H HA   . LEU A 1 198 ? 23.112 40.947 18.852 0.00 29.14  ? 201 LEU A HA   1 
ATOM   3180 H HB2  . LEU A 1 198 ? 21.882 40.521 16.853 0.00 30.91  ? 201 LEU A HB2  1 
ATOM   3181 H HB3  . LEU A 1 198 ? 22.872 39.329 16.504 0.00 30.91  ? 201 LEU A HB3  1 
ATOM   3182 H HG   . LEU A 1 198 ? 22.007 38.088 18.206 0.00 31.18  ? 201 LEU A HG   1 
ATOM   3183 H HD11 . LEU A 1 198 ? 20.137 38.773 19.431 0.00 31.34  ? 201 LEU A HD11 1 
ATOM   3184 H HD12 . LEU A 1 198 ? 21.390 39.697 19.745 0.00 31.34  ? 201 LEU A HD12 1 
ATOM   3185 H HD13 . LEU A 1 198 ? 20.246 40.215 18.773 0.00 31.34  ? 201 LEU A HD13 1 
ATOM   3186 H HD21 . LEU A 1 198 ? 19.940 37.662 17.199 0.00 38.74  ? 201 LEU A HD21 1 
ATOM   3187 H HD22 . LEU A 1 198 ? 19.874 39.146 16.637 0.00 38.74  ? 201 LEU A HD22 1 
ATOM   3188 H HD23 . LEU A 1 198 ? 20.920 38.114 16.034 0.00 38.74  ? 201 LEU A HD23 1 
ATOM   3189 N N    A ASN A 1 199 ? 25.474 38.924 18.135 0.71 26.55  ? 202 ASN A N    1 
ATOM   3190 N N    B ASN A 1 199 ? 25.441 38.960 18.075 0.29 26.81  ? 202 ASN A N    1 
ATOM   3191 C CA   A ASN A 1 199 ? 26.287 37.883 18.753 0.71 26.59  ? 202 ASN A CA   1 
ATOM   3192 C CA   B ASN A 1 199 ? 26.348 37.924 18.631 0.29 26.71  ? 202 ASN A CA   1 
ATOM   3193 C C    A ASN A 1 199 ? 26.994 38.373 20.007 0.71 29.54  ? 202 ASN A C    1 
ATOM   3194 C C    B ASN A 1 199 ? 26.924 38.416 19.963 0.29 29.41  ? 202 ASN A C    1 
ATOM   3195 O O    A ASN A 1 199 ? 27.048 37.634 21.017 0.71 28.12  ? 202 ASN A O    1 
ATOM   3196 O O    B ASN A 1 199 ? 26.909 37.631 20.926 0.29 27.08  ? 202 ASN A O    1 
ATOM   3197 C CB   A ASN A 1 199 ? 27.218 37.194 17.754 0.71 30.97  ? 202 ASN A CB   1 
ATOM   3198 C CB   B ASN A 1 199 ? 27.455 37.558 17.640 0.29 29.88  ? 202 ASN A CB   1 
ATOM   3199 C CG   A ASN A 1 199 ? 28.324 38.063 17.324 0.71 33.29  ? 202 ASN A CG   1 
ATOM   3200 C CG   B ASN A 1 199 ? 28.134 36.248 17.971 0.29 29.35  ? 202 ASN A CG   1 
ATOM   3201 O OD1  A ASN A 1 199 ? 28.103 39.177 16.926 0.71 35.55  ? 202 ASN A OD1  1 
ATOM   3202 O OD1  B ASN A 1 199 ? 27.785 35.590 18.948 0.29 34.24  ? 202 ASN A OD1  1 
ATOM   3203 N ND2  A ASN A 1 199 ? 29.557 37.546 17.398 0.71 41.88  ? 202 ASN A ND2  1 
ATOM   3204 N ND2  B ASN A 1 199 ? 29.099 35.857 17.156 0.29 44.59  ? 202 ASN A ND2  1 
ATOM   3205 H H    A ASN A 1 199 ? 25.744 39.180 17.360 0.71 31.86  ? 202 ASN A H    1 
ATOM   3206 H H    B ASN A 1 199 ? 25.337 38.820 17.182 0.29 32.17  ? 202 ASN A H    1 
ATOM   3207 H HA   A ASN A 1 199 ? 25.687 37.178 19.042 0.71 31.91  ? 202 ASN A HA   1 
ATOM   3208 H HA   B ASN A 1 199 ? 25.817 37.111 18.801 0.29 32.05  ? 202 ASN A HA   1 
ATOM   3209 H HB2  A ASN A 1 199 ? 27.599 36.405 18.169 0.71 37.17  ? 202 ASN A HB2  1 
ATOM   3210 H HB2  B ASN A 1 199 ? 27.068 37.499 16.743 0.29 35.86  ? 202 ASN A HB2  1 
ATOM   3211 H HB3  A ASN A 1 199 ? 26.709 36.943 16.968 0.71 37.17  ? 202 ASN A HB3  1 
ATOM   3212 H HB3  B ASN A 1 199 ? 28.123 38.273 17.636 0.29 35.86  ? 202 ASN A HB3  1 
ATOM   3213 H HD21 A ASN A 1 199 ? 29.670 36.744 17.687 0.71 50.25  ? 202 ASN A HD21 1 
ATOM   3214 H HD21 B ASN A 1 199 ? 29.311 36.351 16.455 0.29 53.50  ? 202 ASN A HD21 1 
ATOM   3215 H HD22 A ASN A 1 199 ? 30.236 38.016 17.158 0.71 50.25  ? 202 ASN A HD22 1 
ATOM   3216 H HD22 B ASN A 1 199 ? 29.527 35.100 17.310 0.29 53.50  ? 202 ASN A HD22 1 
ATOM   3217 N N    . ILE A 1 200 ? 27.481 39.631 20.000 1.00 28.47  ? 203 ILE A N    1 
ATOM   3218 C CA   . ILE A 1 200 ? 28.105 40.151 21.212 1.00 27.73  ? 203 ILE A CA   1 
ATOM   3219 C C    . ILE A 1 200 ? 27.039 40.527 22.225 1.00 25.56  ? 203 ILE A C    1 
ATOM   3220 O O    . ILE A 1 200 ? 27.232 40.304 23.419 1.00 26.10  ? 203 ILE A O    1 
ATOM   3221 C CB   . ILE A 1 200 ? 28.968 41.363 20.802 1.00 27.42  ? 203 ILE A CB   1 
ATOM   3222 C CG1  . ILE A 1 200 ? 30.022 40.856 19.818 1.00 32.13  ? 203 ILE A CG1  1 
ATOM   3223 C CG2  . ILE A 1 200 ? 29.621 41.972 22.031 1.00 33.01  ? 203 ILE A CG2  1 
ATOM   3224 C CD1  . ILE A 1 200 ? 30.807 39.729 20.273 1.00 35.52  ? 203 ILE A CD1  1 
ATOM   3225 H H    . ILE A 1 200 ? 27.458 40.169 19.330 0.00 34.17  ? 203 ILE A H    1 
ATOM   3226 H HA   . ILE A 1 200 ? 28.669 39.481 21.628 0.00 33.28  ? 203 ILE A HA   1 
ATOM   3227 H HB   . ILE A 1 200 ? 28.426 42.052 20.387 0.00 32.90  ? 203 ILE A HB   1 
ATOM   3228 H HG12 . ILE A 1 200 ? 29.572 40.585 19.002 0.00 38.56  ? 203 ILE A HG12 1 
ATOM   3229 H HG13 . ILE A 1 200 ? 30.638 41.581 19.630 0.00 38.56  ? 203 ILE A HG13 1 
ATOM   3230 H HG21 . ILE A 1 200 ? 30.339 42.560 21.748 0.00 39.62  ? 203 ILE A HG21 1 
ATOM   3231 H HG22 . ILE A 1 200 ? 28.956 42.476 22.525 0.00 39.62  ? 203 ILE A HG22 1 
ATOM   3232 H HG23 . ILE A 1 200 ? 29.977 41.260 22.585 0.00 39.62  ? 203 ILE A HG23 1 
ATOM   3233 H HD11 . ILE A 1 200 ? 31.595 39.646 19.713 0.00 42.62  ? 203 ILE A HD11 1 
ATOM   3234 H HD12 . ILE A 1 200 ? 31.071 39.879 21.194 0.00 42.62  ? 203 ILE A HD12 1 
ATOM   3235 H HD13 . ILE A 1 200 ? 30.270 38.924 20.210 0.00 42.62  ? 203 ILE A HD13 1 
ATOM   3236 N N    . GLU A 1 201 ? 25.904 41.077 21.795 1.00 23.03  ? 204 GLU A N    1 
ATOM   3237 C CA   . GLU A 1 201 ? 24.823 41.377 22.723 1.00 22.59  ? 204 GLU A CA   1 
ATOM   3238 C C    . GLU A 1 201 ? 24.419 40.093 23.464 1.00 24.53  ? 204 GLU A C    1 
ATOM   3239 O O    . GLU A 1 201 ? 24.175 40.136 24.705 1.00 22.41  ? 204 GLU A O    1 
ATOM   3240 C CB   . GLU A 1 201 ? 23.652 41.946 21.941 1.00 26.39  ? 204 GLU A CB   1 
ATOM   3241 C CG   . GLU A 1 201 ? 22.382 42.156 22.817 1.00 25.77  ? 204 GLU A CG   1 
ATOM   3242 C CD   . GLU A 1 201 ? 21.207 42.587 22.033 1.00 32.11  ? 204 GLU A CD   1 
ATOM   3243 O OE1  . GLU A 1 201 ? 21.349 42.848 20.883 1.00 28.63  ? 204 GLU A OE1  1 
ATOM   3244 O OE2  . GLU A 1 201 ? 20.052 42.491 22.515 1.00 39.68  ? 204 GLU A OE2  1 
ATOM   3245 H H    . GLU A 1 201 ? 25.738 41.285 20.977 0.00 27.64  ? 204 GLU A H    1 
ATOM   3246 H HA   . GLU A 1 201 ? 25.096 42.039 23.377 0.00 27.11  ? 204 GLU A HA   1 
ATOM   3247 H HB2  . GLU A 1 201 ? 23.908 42.806 21.573 0.00 31.67  ? 204 GLU A HB2  1 
ATOM   3248 H HB3  . GLU A 1 201 ? 23.424 41.333 21.224 0.00 31.67  ? 204 GLU A HB3  1 
ATOM   3249 H HG2  . GLU A 1 201 ? 22.159 41.319 23.255 0.00 30.93  ? 204 GLU A HG2  1 
ATOM   3250 H HG3  . GLU A 1 201 ? 22.565 42.839 23.481 0.00 30.93  ? 204 GLU A HG3  1 
ATOM   3251 N N    . THR A 1 202 ? 24.339 38.986 22.745 1.00 22.75  ? 205 THR A N    1 
ATOM   3252 C CA   . THR A 1 202 ? 23.900 37.728 23.395 1.00 22.94  ? 205 THR A CA   1 
ATOM   3253 C C    . THR A 1 202 ? 24.923 37.292 24.424 1.00 23.34  ? 205 THR A C    1 
ATOM   3254 O O    . THR A 1 202 ? 24.545 36.812 25.511 1.00 21.66  ? 205 THR A O    1 
ATOM   3255 C CB   . THR A 1 202 ? 23.719 36.652 22.325 1.00 21.66  ? 205 THR A CB   1 
ATOM   3256 O OG1  . THR A 1 202 ? 22.653 37.118 21.426 1.00 22.94  ? 205 THR A OG1  1 
ATOM   3257 C CG2  . THR A 1 202 ? 23.165 35.348 22.910 1.00 20.55  ? 205 THR A CG2  1 
ATOM   3258 H H    . THR A 1 202 ? 24.523 38.922 21.907 0.00 27.30  ? 205 THR A H    1 
ATOM   3259 H HA   . THR A 1 202 ? 23.049 37.858 23.843 0.00 27.53  ? 205 THR A HA   1 
ATOM   3260 H HB   . THR A 1 202 ? 24.575 36.491 21.899 0.00 25.99  ? 205 THR A HB   1 
ATOM   3261 H HG1  . THR A 1 202 ? 22.873 37.848 21.073 0.00 27.53  ? 205 THR A HG1  1 
ATOM   3262 H HG21 . THR A 1 202 ? 23.026 34.700 22.203 0.00 24.66  ? 205 THR A HG21 1 
ATOM   3263 H HG22 . THR A 1 202 ? 23.791 34.982 23.555 0.00 24.66  ? 205 THR A HG22 1 
ATOM   3264 H HG23 . THR A 1 202 ? 22.319 35.517 23.354 0.00 24.66  ? 205 THR A HG23 1 
ATOM   3265 N N    . LEU A 1 203 ? 26.211 37.373 24.102 1.00 21.59  ? 206 LEU A N    1 
ATOM   3266 C CA   . LEU A 1 203 ? 27.262 37.138 25.106 1.00 24.15  ? 206 LEU A CA   1 
ATOM   3267 C C    . LEU A 1 203 ? 27.112 38.026 26.347 1.00 23.94  ? 206 LEU A C    1 
ATOM   3268 O O    . LEU A 1 203 ? 27.164 37.525 27.480 1.00 22.30  ? 206 LEU A O    1 
ATOM   3269 C CB   . LEU A 1 203 ? 28.643 37.391 24.407 1.00 24.27  ? 206 LEU A CB   1 
ATOM   3270 C CG   . LEU A 1 203 ? 29.835 37.435 25.329 1.00 25.02  ? 206 LEU A CG   1 
ATOM   3271 C CD1  . LEU A 1 203 ? 29.971 36.152 26.034 1.00 28.84  ? 206 LEU A CD1  1 
ATOM   3272 C CD2  . LEU A 1 203 ? 31.033 37.726 24.347 1.00 29.54  ? 206 LEU A CD2  1 
ATOM   3273 H H    . LEU A 1 203 ? 26.508 37.561 23.317 0.00 25.91  ? 206 LEU A H    1 
ATOM   3274 H HA   . LEU A 1 203 ? 27.204 36.223 25.423 0.00 28.98  ? 206 LEU A HA   1 
ATOM   3275 H HB2  . LEU A 1 203 ? 28.797 36.678 23.768 0.00 29.12  ? 206 LEU A HB2  1 
ATOM   3276 H HB3  . LEU A 1 203 ? 28.601 38.245 23.948 0.00 29.12  ? 206 LEU A HB3  1 
ATOM   3277 H HG   . LEU A 1 203 ? 29.785 38.100 26.034 0.00 30.03  ? 206 LEU A HG   1 
ATOM   3278 H HD11 . LEU A 1 203 ? 30.773 36.175 26.579 0.00 34.61  ? 206 LEU A HD11 1 
ATOM   3279 H HD12 . LEU A 1 203 ? 29.192 36.017 26.597 0.00 34.61  ? 206 LEU A HD12 1 
ATOM   3280 H HD13 . LEU A 1 203 ? 30.035 35.438 25.381 0.00 34.61  ? 206 LEU A HD13 1 
ATOM   3281 H HD21 . LEU A 1 203 ? 31.844 37.845 24.865 0.00 35.44  ? 206 LEU A HD21 1 
ATOM   3282 H HD22 . LEU A 1 203 ? 31.134 36.974 23.742 0.00 35.44  ? 206 LEU A HD22 1 
ATOM   3283 H HD23 . LEU A 1 203 ? 30.840 38.532 23.844 0.00 35.44  ? 206 LEU A HD23 1 
ATOM   3284 N N    . LEU A 1 204 ? 26.872 39.297 26.158 1.00 22.52  ? 207 LEU A N    1 
ATOM   3285 C CA   . LEU A 1 204 ? 26.732 40.238 27.303 1.00 24.58  ? 207 LEU A CA   1 
ATOM   3286 C C    . LEU A 1 204 ? 25.528 39.845 28.171 1.00 20.99  ? 207 LEU A C    1 
ATOM   3287 O O    . LEU A 1 204 ? 25.688 39.775 29.407 1.00 21.85  ? 207 LEU A O    1 
ATOM   3288 C CB   . LEU A 1 204 ? 26.605 41.672 26.787 1.00 22.99  ? 207 LEU A CB   1 
ATOM   3289 C CG   . LEU A 1 204 ? 27.895 42.183 26.113 1.00 24.80  ? 207 LEU A CG   1 
ATOM   3290 C CD1  . LEU A 1 204 ? 27.598 43.581 25.611 1.00 29.09  ? 207 LEU A CD1  1 
ATOM   3291 C CD2  . LEU A 1 204 ? 29.015 42.329 27.073 1.00 31.79  ? 207 LEU A CD2  1 
ATOM   3292 H H    . LEU A 1 204 ? 26.781 39.667 25.387 0.00 27.03  ? 207 LEU A H    1 
ATOM   3293 H HA   . LEU A 1 204 ? 27.527 40.199 27.857 0.00 29.49  ? 207 LEU A HA   1 
ATOM   3294 H HB2  . LEU A 1 204 ? 25.889 41.708 26.133 0.00 27.59  ? 207 LEU A HB2  1 
ATOM   3295 H HB3  . LEU A 1 204 ? 26.403 42.258 27.533 0.00 27.59  ? 207 LEU A HB3  1 
ATOM   3296 H HG   . LEU A 1 204 ? 28.157 41.557 25.420 0.00 29.76  ? 207 LEU A HG   1 
ATOM   3297 H HD11 . LEU A 1 204 ? 28.379 43.923 25.148 0.00 34.90  ? 207 LEU A HD11 1 
ATOM   3298 H HD12 . LEU A 1 204 ? 26.843 43.544 25.004 0.00 34.90  ? 207 LEU A HD12 1 
ATOM   3299 H HD13 . LEU A 1 204 ? 27.387 44.150 26.368 0.00 34.90  ? 207 LEU A HD13 1 
ATOM   3300 H HD21 . LEU A 1 204 ? 29.731 42.827 26.650 0.00 38.15  ? 207 LEU A HD21 1 
ATOM   3301 H HD22 . LEU A 1 204 ? 28.699 42.805 27.857 0.00 38.15  ? 207 LEU A HD22 1 
ATOM   3302 H HD23 . LEU A 1 204 ? 29.330 41.447 27.327 0.00 38.15  ? 207 LEU A HD23 1 
ATOM   3303 N N    . PHE A 1 205 ? 24.394 39.569 27.579 1.00 20.49  ? 208 PHE A N    1 
ATOM   3304 C CA   . PHE A 1 205 ? 23.263 39.196 28.431 1.00 21.67  ? 208 PHE A CA   1 
ATOM   3305 C C    . PHE A 1 205 ? 23.524 37.850 29.098 1.00 21.79  ? 208 PHE A C    1 
ATOM   3306 O O    . PHE A 1 205 ? 23.002 37.628 30.209 1.00 20.53  ? 208 PHE A O    1 
ATOM   3307 C CB   . PHE A 1 205 ? 21.946 39.108 27.597 1.00 19.94  ? 208 PHE A CB   1 
ATOM   3308 C CG   . PHE A 1 205 ? 21.284 40.437 27.312 1.00 18.95  ? 208 PHE A CG   1 
ATOM   3309 C CD1  . PHE A 1 205 ? 21.052 41.384 28.330 1.00 22.18  ? 208 PHE A CD1  1 
ATOM   3310 C CD2  . PHE A 1 205 ? 20.756 40.683 26.053 1.00 21.96  ? 208 PHE A CD2  1 
ATOM   3311 C CE1  . PHE A 1 205 ? 20.369 42.575 28.026 1.00 24.60  ? 208 PHE A CE1  1 
ATOM   3312 C CE2  . PHE A 1 205 ? 20.001 41.836 25.763 1.00 24.14  ? 208 PHE A CE2  1 
ATOM   3313 C CZ   . PHE A 1 205 ? 19.904 42.800 26.748 1.00 25.23  ? 208 PHE A CZ   1 
ATOM   3314 H H    . PHE A 1 205 ? 24.247 39.585 26.732 0.00 24.59  ? 208 PHE A H    1 
ATOM   3315 H HA   . PHE A 1 205 ? 23.143 39.882 29.106 0.00 26.00  ? 208 PHE A HA   1 
ATOM   3316 H HB2  . PHE A 1 205 ? 22.149 38.694 26.744 0.00 23.92  ? 208 PHE A HB2  1 
ATOM   3317 H HB3  . PHE A 1 205 ? 21.308 38.564 28.086 0.00 23.92  ? 208 PHE A HB3  1 
ATOM   3318 H HD1  . PHE A 1 205 ? 21.349 41.222 29.196 0.00 26.62  ? 208 PHE A HD1  1 
ATOM   3319 H HD2  . PHE A 1 205 ? 20.906 40.064 25.376 0.00 26.36  ? 208 PHE A HD2  1 
ATOM   3320 H HE1  . PHE A 1 205 ? 20.230 43.212 28.689 0.00 29.52  ? 208 PHE A HE1  1 
ATOM   3321 H HE2  . PHE A 1 205 ? 19.584 41.945 24.939 0.00 28.97  ? 208 PHE A HE2  1 
ATOM   3322 H HZ   . PHE A 1 205 ? 19.516 43.620 26.544 0.00 30.28  ? 208 PHE A HZ   1 
ATOM   3323 N N    . MET A 1 206 ? 24.259 36.901 28.487 1.00 21.14  ? 209 MET A N    1 
ATOM   3324 C CA   . MET A 1 206 ? 24.535 35.635 29.140 1.00 21.16  ? 209 MET A CA   1 
ATOM   3325 C C    . MET A 1 206 ? 25.376 35.854 30.393 1.00 22.26  ? 209 MET A C    1 
ATOM   3326 O O    . MET A 1 206 ? 25.083 35.244 31.449 1.00 22.99  ? 209 MET A O    1 
ATOM   3327 C CB   . MET A 1 206 ? 25.197 34.639 28.154 1.00 25.06  ? 209 MET A CB   1 
ATOM   3328 C CG   . MET A 1 206 ? 25.363 33.345 28.905 1.00 25.36  ? 209 MET A CG   1 
ATOM   3329 S SD   . MET A 1 206 ? 26.894 32.994 29.494 1.00 37.66  ? 209 MET A SD   1 
ATOM   3330 C CE   . MET A 1 206 ? 27.145 32.578 27.851 1.00 22.11  ? 209 MET A CE   1 
ATOM   3331 H H    . MET A 1 206 ? 24.601 36.977 27.702 0.00 25.37  ? 209 MET A H    1 
ATOM   3332 H HA   . MET A 1 206 ? 23.695 35.226 29.404 0.00 25.39  ? 209 MET A HA   1 
ATOM   3333 H HB2  . MET A 1 206 ? 24.629 34.498 27.381 0.00 30.07  ? 209 MET A HB2  1 
ATOM   3334 H HB3  . MET A 1 206 ? 26.065 34.967 27.872 0.00 30.07  ? 209 MET A HB3  1 
ATOM   3335 H HG2  . MET A 1 206 ? 24.765 33.363 29.668 0.00 30.44  ? 209 MET A HG2  1 
ATOM   3336 H HG3  . MET A 1 206 ? 25.118 32.620 28.309 0.00 30.44  ? 209 MET A HG3  1 
ATOM   3337 H HE1  . MET A 1 206 ? 28.049 32.243 27.745 0.00 26.54  ? 209 MET A HE1  1 
ATOM   3338 H HE2  . MET A 1 206 ? 26.506 31.893 27.598 0.00 26.54  ? 209 MET A HE2  1 
ATOM   3339 H HE3  . MET A 1 206 ? 27.018 33.368 27.303 0.00 26.54  ? 209 MET A HE3  1 
ATOM   3340 N N    . VAL A 1 207 ? 26.445 36.675 30.288 1.00 20.71  ? 210 VAL A N    1 
ATOM   3341 C CA   . VAL A 1 207 ? 27.272 36.927 31.456 1.00 21.39  ? 210 VAL A CA   1 
ATOM   3342 C C    . VAL A 1 207 ? 26.447 37.631 32.527 1.00 21.76  ? 210 VAL A C    1 
ATOM   3343 O O    . VAL A 1 207 ? 26.539 37.275 33.730 1.00 22.79  ? 210 VAL A O    1 
ATOM   3344 C CB   . VAL A 1 207 ? 28.461 37.798 31.034 1.00 24.64  ? 210 VAL A CB   1 
ATOM   3345 C CG1  . VAL A 1 207 ? 29.265 38.192 32.222 1.00 30.37  ? 210 VAL A CG1  1 
ATOM   3346 C CG2  . VAL A 1 207 ? 29.353 36.888 30.165 1.00 26.13  ? 210 VAL A CG2  1 
ATOM   3347 H H    . VAL A 1 207 ? 26.692 37.079 29.570 0.00 24.85  ? 210 VAL A H    1 
ATOM   3348 H HA   . VAL A 1 207 ? 27.597 36.087 31.816 0.00 25.67  ? 210 VAL A HA   1 
ATOM   3349 H HB   . VAL A 1 207 ? 28.160 38.599 30.578 0.00 29.57  ? 210 VAL A HB   1 
ATOM   3350 H HG11 . VAL A 1 207 ? 30.127 38.520 31.924 0.00 36.44  ? 210 VAL A HG11 1 
ATOM   3351 H HG12 . VAL A 1 207 ? 28.794 38.889 32.705 0.00 36.44  ? 210 VAL A HG12 1 
ATOM   3352 H HG13 . VAL A 1 207 ? 29.385 37.417 32.792 0.00 36.44  ? 210 VAL A HG13 1 
ATOM   3353 H HG21 . VAL A 1 207 ? 30.130 37.390 29.876 0.00 31.36  ? 210 VAL A HG21 1 
ATOM   3354 H HG22 . VAL A 1 207 ? 29.631 36.122 30.692 0.00 31.36  ? 210 VAL A HG22 1 
ATOM   3355 H HG23 . VAL A 1 207 ? 28.845 36.592 29.394 0.00 31.36  ? 210 VAL A HG23 1 
ATOM   3356 N N    . LEU A 1 208 ? 25.626 38.608 32.144 1.00 21.03  ? 211 LEU A N    1 
ATOM   3357 C CA   . LEU A 1 208 ? 24.817 39.275 33.166 1.00 20.40  ? 211 LEU A CA   1 
ATOM   3358 C C    . LEU A 1 208 ? 23.833 38.329 33.812 1.00 19.90  ? 211 LEU A C    1 
ATOM   3359 O O    . LEU A 1 208 ? 23.706 38.305 35.038 1.00 20.55  ? 211 LEU A O    1 
ATOM   3360 C CB   . LEU A 1 208 ? 24.033 40.490 32.567 1.00 20.20  ? 211 LEU A CB   1 
ATOM   3361 C CG   . LEU A 1 208 ? 24.971 41.625 32.149 1.00 20.11  ? 211 LEU A CG   1 
ATOM   3362 C CD1  . LEU A 1 208 ? 24.089 42.607 31.330 1.00 25.54  ? 211 LEU A CD1  1 
ATOM   3363 C CD2  . LEU A 1 208 ? 25.550 42.368 33.391 1.00 27.27  ? 211 LEU A CD2  1 
ATOM   3364 H H    . LEU A 1 208 ? 25.522 38.892 31.339 0.00 25.24  ? 211 LEU A H    1 
ATOM   3365 H HA   . LEU A 1 208 ? 25.431 39.604 33.840 0.00 24.48  ? 211 LEU A HA   1 
ATOM   3366 H HB2  . LEU A 1 208 ? 23.541 40.197 31.784 0.00 24.24  ? 211 LEU A HB2  1 
ATOM   3367 H HB3  . LEU A 1 208 ? 23.419 40.833 33.236 0.00 24.24  ? 211 LEU A HB3  1 
ATOM   3368 H HG   . LEU A 1 208 ? 25.727 41.291 31.641 0.00 24.13  ? 211 LEU A HG   1 
ATOM   3369 H HD11 . LEU A 1 208 ? 24.636 43.352 31.036 0.00 30.65  ? 211 LEU A HD11 1 
ATOM   3370 H HD12 . LEU A 1 208 ? 23.726 42.140 30.562 0.00 30.65  ? 211 LEU A HD12 1 
ATOM   3371 H HD13 . LEU A 1 208 ? 23.368 42.929 31.894 0.00 30.65  ? 211 LEU A HD13 1 
ATOM   3372 H HD21 . LEU A 1 208 ? 26.047 43.145 33.091 0.00 32.72  ? 211 LEU A HD21 1 
ATOM   3373 H HD22 . LEU A 1 208 ? 24.817 42.646 33.963 0.00 32.72  ? 211 LEU A HD22 1 
ATOM   3374 H HD23 . LEU A 1 208 ? 26.136 41.766 33.874 0.00 32.72  ? 211 LEU A HD23 1 
ATOM   3375 N N    . ASP A 1 209 ? 23.162 37.509 33.039 1.00 18.99  ? 212 ASP A N    1 
ATOM   3376 C CA   . ASP A 1 209 ? 22.084 36.625 33.564 1.00 18.63  ? 212 ASP A CA   1 
ATOM   3377 C C    . ASP A 1 209 ? 22.671 35.588 34.476 1.00 19.82  ? 212 ASP A C    1 
ATOM   3378 O O    . ASP A 1 209 ? 22.141 35.324 35.580 1.00 20.25  ? 212 ASP A O    1 
ATOM   3379 C CB   . ASP A 1 209 ? 21.422 35.905 32.379 1.00 18.91  ? 212 ASP A CB   1 
ATOM   3380 C CG   . ASP A 1 209 ? 20.420 36.706 31.602 1.00 19.66  ? 212 ASP A CG   1 
ATOM   3381 O OD1  . ASP A 1 209 ? 19.955 37.754 32.085 1.00 22.26  ? 212 ASP A OD1  1 
ATOM   3382 O OD2  . ASP A 1 209 ? 19.922 36.209 30.567 1.00 19.32  ? 212 ASP A OD2  1 
ATOM   3383 H H    . ASP A 1 209 ? 23.293 37.424 32.193 0.00 22.78  ? 212 ASP A H    1 
ATOM   3384 H HA   . ASP A 1 209 ? 21.427 37.154 34.044 0.00 22.35  ? 212 ASP A HA   1 
ATOM   3385 H HB2  . ASP A 1 209 ? 22.118 35.638 31.758 0.00 22.69  ? 212 ASP A HB2  1 
ATOM   3386 H HB3  . ASP A 1 209 ? 20.961 35.122 32.718 0.00 22.69  ? 212 ASP A HB3  1 
ATOM   3387 N N    . VAL A 1 210 ? 23.831 35.007 34.131 1.00 20.86  ? 213 VAL A N    1 
ATOM   3388 C CA   . VAL A 1 210 ? 24.366 33.961 35.024 1.00 22.22  ? 213 VAL A CA   1 
ATOM   3389 C C    . VAL A 1 210 ? 24.858 34.616 36.282 1.00 22.53  ? 213 VAL A C    1 
ATOM   3390 O O    . VAL A 1 210 ? 24.687 34.049 37.382 1.00 22.68  ? 213 VAL A O    1 
ATOM   3391 C CB   . VAL A 1 210 ? 25.482 33.225 34.233 1.00 21.45  ? 213 VAL A CB   1 
ATOM   3392 C CG1  . VAL A 1 210 ? 26.263 32.276 35.170 1.00 26.66  ? 213 VAL A CG1  1 
ATOM   3393 C CG2  . VAL A 1 210 ? 24.938 32.435 33.121 1.00 24.61  ? 213 VAL A CG2  1 
ATOM   3394 H H    . VAL A 1 210 ? 24.299 35.187 33.432 0.00 25.03  ? 213 VAL A H    1 
ATOM   3395 H HA   . VAL A 1 210 ? 23.697 33.310 35.288 0.00 26.67  ? 213 VAL A HA   1 
ATOM   3396 H HB   . VAL A 1 210 ? 26.073 33.902 33.869 0.00 25.74  ? 213 VAL A HB   1 
ATOM   3397 H HG11 . VAL A 1 210 ? 26.808 31.680 34.633 0.00 31.99  ? 213 VAL A HG11 1 
ATOM   3398 H HG12 . VAL A 1 210 ? 26.828 32.804 35.755 0.00 31.99  ? 213 VAL A HG12 1 
ATOM   3399 H HG13 . VAL A 1 210 ? 25.631 31.762 35.697 0.00 31.99  ? 213 VAL A HG13 1 
ATOM   3400 H HG21 . VAL A 1 210 ? 25.671 32.024 32.637 0.00 29.54  ? 213 VAL A HG21 1 
ATOM   3401 H HG22 . VAL A 1 210 ? 24.352 31.748 33.478 0.00 29.54  ? 213 VAL A HG22 1 
ATOM   3402 H HG23 . VAL A 1 210 ? 24.439 33.021 32.532 0.00 29.54  ? 213 VAL A HG23 1 
ATOM   3403 N N    . SER A 1 211 ? 25.470 35.804 36.173 1.00 20.76  ? 214 SER A N    1 
ATOM   3404 C CA   . SER A 1 211 ? 25.948 36.500 37.395 1.00 21.71  ? 214 SER A CA   1 
ATOM   3405 C C    . SER A 1 211 ? 24.766 36.873 38.298 1.00 20.60  ? 214 SER A C    1 
ATOM   3406 O O    . SER A 1 211 ? 24.863 36.731 39.522 1.00 23.01  ? 214 SER A O    1 
ATOM   3407 C CB   . SER A 1 211 ? 26.701 37.751 36.978 1.00 24.38  ? 214 SER A CB   1 
ATOM   3408 O OG   . SER A 1 211 ? 27.880 37.317 36.265 1.00 26.29  ? 214 SER A OG   1 
ATOM   3409 H H    . SER A 1 211 ? 25.619 36.220 35.434 0.00 24.92  ? 214 SER A H    1 
ATOM   3410 H HA   . SER A 1 211 ? 26.545 35.923 37.897 0.00 26.05  ? 214 SER A HA   1 
ATOM   3411 H HB2  . SER A 1 211 ? 26.145 38.293 36.397 0.00 29.26  ? 214 SER A HB2  1 
ATOM   3412 H HB3  . SER A 1 211 ? 26.958 38.260 37.762 0.00 29.26  ? 214 SER A HB3  1 
ATOM   3413 H HG   . SER A 1 211 ? 27.658 36.904 35.568 0.00 31.54  ? 214 SER A HG   1 
ATOM   3414 N N    . ALA A 1 212 ? 23.660 37.394 37.726 1.00 20.87  ? 215 ALA A N    1 
ATOM   3415 C CA   . ALA A 1 212 ? 22.557 37.934 38.529 1.00 20.50  ? 215 ALA A CA   1 
ATOM   3416 C C    . ALA A 1 212 ? 21.687 36.894 39.063 1.00 22.56  ? 215 ALA A C    1 
ATOM   3417 O O    . ALA A 1 212 ? 20.892 37.158 39.949 1.00 24.16  ? 215 ALA A O    1 
ATOM   3418 C CB   . ALA A 1 212 ? 21.677 38.870 37.617 1.00 21.93  ? 215 ALA A CB   1 
ATOM   3419 H H    . ALA A 1 212 ? 23.531 37.443 36.877 0.00 25.04  ? 215 ALA A H    1 
ATOM   3420 H HA   . ALA A 1 212 ? 22.942 38.421 39.275 0.00 24.60  ? 215 ALA A HA   1 
ATOM   3421 H HB1  . ALA A 1 212 ? 20.944 39.226 38.144 0.00 26.31  ? 215 ALA A HB1  1 
ATOM   3422 H HB2  . ALA A 1 212 ? 22.227 39.596 37.284 0.00 26.31  ? 215 ALA A HB2  1 
ATOM   3423 H HB3  . ALA A 1 212 ? 21.329 38.351 36.875 0.00 26.31  ? 215 ALA A HB3  1 
ATOM   3424 N N    . LYS A 1 213 ? 21.844 35.628 38.579 1.00 20.53  ? 216 LYS A N    1 
ATOM   3425 C CA   . LYS A 1 213 ? 20.967 34.529 39.029 1.00 21.24  ? 216 LYS A CA   1 
ATOM   3426 C C    . LYS A 1 213 ? 21.812 33.486 39.766 1.00 23.89  ? 216 LYS A C    1 
ATOM   3427 O O    . LYS A 1 213 ? 21.592 33.274 40.979 1.00 23.74  ? 216 LYS A O    1 
ATOM   3428 C CB   . LYS A 1 213 ? 20.218 33.861 37.841 1.00 19.57  ? 216 LYS A CB   1 
ATOM   3429 C CG   . LYS A 1 213 ? 19.221 34.790 37.104 1.00 18.87  ? 216 LYS A CG   1 
ATOM   3430 C CD   . LYS A 1 213 ? 18.441 34.171 36.072 1.00 19.85  ? 216 LYS A CD   1 
ATOM   3431 C CE   . LYS A 1 213 ? 17.222 35.008 35.699 1.00 20.67  ? 216 LYS A CE   1 
ATOM   3432 N NZ   . LYS A 1 213 ? 17.582 36.198 34.920 1.00 19.31  ? 216 LYS A NZ   1 
ATOM   3433 H HA   . LYS A 1 213 ? 20.333 34.945 39.648 1.00 25.49  ? 216 LYS A HA   1 
ATOM   3434 H HB2  . LYS A 1 213 ? 20.883 33.521 37.208 1.00 23.49  ? 216 LYS A HB2  1 
ATOM   3435 H HB3  . LYS A 1 213 ? 19.748 33.071 38.177 1.00 23.49  ? 216 LYS A HB3  1 
ATOM   3436 H HG2  . LYS A 1 213 ? 18.595 35.187 37.743 1.00 22.64  ? 216 LYS A HG2  1 
ATOM   3437 H HG3  . LYS A 1 213 ? 19.698 35.542 36.697 1.00 22.64  ? 216 LYS A HG3  1 
ATOM   3438 H HD2  . LYS A 1 213 ? 19.001 34.030 35.281 1.00 23.83  ? 216 LYS A HD2  1 
ATOM   3439 H HD3  . LYS A 1 213 ? 18.156 33.283 36.367 1.00 23.83  ? 216 LYS A HD3  1 
ATOM   3440 H HE2  . LYS A 1 213 ? 16.612 34.484 35.139 1.00 24.80  ? 216 LYS A HE2  1 
ATOM   3441 H HE3  . LYS A 1 213 ? 16.774 35.330 36.507 1.00 24.80  ? 216 LYS A HE3  1 
ATOM   3442 H HZ2  . LYS A 1 213 ? 17.742 36.100 34.058 1.00 23.17  ? 216 LYS A HZ2  1 
ATOM   3443 N N    . VAL A 1 214 ? 22.791 32.858 39.111 1.00 21.40  ? 217 VAL A N    1 
ATOM   3444 C CA   . VAL A 1 214 ? 23.553 31.819 39.793 1.00 25.29  ? 217 VAL A CA   1 
ATOM   3445 C C    . VAL A 1 214 ? 24.554 32.453 40.740 1.00 24.31  ? 217 VAL A C    1 
ATOM   3446 O O    . VAL A 1 214 ? 24.752 31.985 41.867 1.00 24.40  ? 217 VAL A O    1 
ATOM   3447 C CB   . VAL A 1 214 ? 24.208 30.890 38.700 1.00 22.40  ? 217 VAL A CB   1 
ATOM   3448 C CG1  . VAL A 1 214 ? 25.086 29.824 39.409 1.00 25.38  ? 217 VAL A CG1  1 
ATOM   3449 C CG2  . VAL A 1 214 ? 23.193 30.260 37.815 1.00 27.90  ? 217 VAL A CG2  1 
ATOM   3450 H H    . VAL A 1 214 ? 23.024 33.014 38.298 0.00 25.68  ? 217 VAL A H    1 
ATOM   3451 H HA   . VAL A 1 214 ? 22.990 31.260 40.352 0.00 30.35  ? 217 VAL A HA   1 
ATOM   3452 H HB   . VAL A 1 214 ? 24.767 31.429 38.118 0.00 26.88  ? 217 VAL A HB   1 
ATOM   3453 H HG11 . VAL A 1 214 ? 25.366 29.162 38.757 0.00 30.45  ? 217 VAL A HG11 1 
ATOM   3454 H HG12 . VAL A 1 214 ? 25.863 30.259 39.793 0.00 30.45  ? 217 VAL A HG12 1 
ATOM   3455 H HG13 . VAL A 1 214 ? 24.564 29.400 40.108 0.00 30.45  ? 217 VAL A HG13 1 
ATOM   3456 H HG21 . VAL A 1 214 ? 23.629 29.597 37.257 0.00 33.48  ? 217 VAL A HG21 1 
ATOM   3457 H HG22 . VAL A 1 214 ? 22.514 29.838 38.363 0.00 33.48  ? 217 VAL A HG22 1 
ATOM   3458 H HG23 . VAL A 1 214 ? 22.790 30.946 37.259 0.00 33.48  ? 217 VAL A HG23 1 
ATOM   3459 N N    . GLY A 1 215 ? 25.231 33.536 40.322 1.00 23.39  ? 218 GLY A N    1 
ATOM   3460 C CA   . GLY A 1 215 ? 26.179 34.234 41.244 1.00 25.17  ? 218 GLY A CA   1 
ATOM   3461 C C    . GLY A 1 215 ? 25.465 34.783 42.489 1.00 24.96  ? 218 GLY A C    1 
ATOM   3462 O O    . GLY A 1 215 ? 25.871 34.500 43.626 1.00 25.45  ? 218 GLY A O    1 
ATOM   3463 H H    . GLY A 1 215 ? 25.170 33.884 39.538 0.00 28.07  ? 218 GLY A H    1 
ATOM   3464 H HA2  . GLY A 1 215 ? 26.866 33.613 41.531 0.00 30.21  ? 218 GLY A HA2  1 
ATOM   3465 H HA3  . GLY A 1 215 ? 26.597 34.974 40.777 0.00 30.21  ? 218 GLY A HA3  1 
ATOM   3466 N N    . PHE A 1 216 ? 24.345 35.481 42.287 1.00 24.15  ? 219 PHE A N    1 
ATOM   3467 C CA   . PHE A 1 216 ? 23.559 35.954 43.395 1.00 23.73  ? 219 PHE A CA   1 
ATOM   3468 C C    . PHE A 1 216 ? 23.123 34.819 44.278 1.00 24.08  ? 219 PHE A C    1 
ATOM   3469 O O    . PHE A 1 216 ? 23.272 34.890 45.505 1.00 24.16  ? 219 PHE A O    1 
ATOM   3470 C CB   . PHE A 1 216 ? 22.359 36.650 42.757 1.00 23.13  ? 219 PHE A CB   1 
ATOM   3471 C CG   . PHE A 1 216 ? 21.305 37.179 43.709 1.00 23.70  ? 219 PHE A CG   1 
ATOM   3472 C CD1  . PHE A 1 216 ? 20.386 36.346 44.249 1.00 25.91  ? 219 PHE A CD1  1 
ATOM   3473 C CD2  . PHE A 1 216 ? 21.209 38.557 43.972 1.00 26.06  ? 219 PHE A CD2  1 
ATOM   3474 C CE1  . PHE A 1 216 ? 19.363 36.832 45.107 1.00 26.33  ? 219 PHE A CE1  1 
ATOM   3475 C CE2  . PHE A 1 216 ? 20.108 39.030 44.742 1.00 28.22  ? 219 PHE A CE2  1 
ATOM   3476 C CZ   . PHE A 1 216 ? 19.250 38.173 45.295 1.00 25.58  ? 219 PHE A CZ   1 
ATOM   3477 H H    . PHE A 1 216 ? 24.029 35.686 41.514 0.00 28.98  ? 219 PHE A H    1 
ATOM   3478 H HA   . PHE A 1 216 ? 24.056 36.562 43.964 0.00 28.47  ? 219 PHE A HA   1 
ATOM   3479 H HB2  . PHE A 1 216 ? 22.685 37.407 42.245 0.00 27.76  ? 219 PHE A HB2  1 
ATOM   3480 H HB3  . PHE A 1 216 ? 21.920 36.017 42.168 0.00 27.76  ? 219 PHE A HB3  1 
ATOM   3481 H HD1  . PHE A 1 216 ? 20.424 35.438 44.055 0.00 31.09  ? 219 PHE A HD1  1 
ATOM   3482 H HD2  . PHE A 1 216 ? 21.851 39.148 43.649 0.00 31.27  ? 219 PHE A HD2  1 
ATOM   3483 H HE1  . PHE A 1 216 ? 18.781 36.243 45.532 0.00 31.60  ? 219 PHE A HE1  1 
ATOM   3484 H HE2  . PHE A 1 216 ? 19.988 39.945 44.861 0.00 33.86  ? 219 PHE A HE2  1 
ATOM   3485 H HZ   . PHE A 1 216 ? 18.557 38.501 45.822 0.00 30.69  ? 219 PHE A HZ   1 
ATOM   3486 N N    . GLY A 1 217 ? 22.651 33.723 43.723 1.00 22.31  ? 220 GLY A N    1 
ATOM   3487 C CA   . GLY A 1 217 ? 22.196 32.615 44.556 1.00 24.18  ? 220 GLY A CA   1 
ATOM   3488 C C    . GLY A 1 217 ? 23.310 31.924 45.350 1.00 26.13  ? 220 GLY A C    1 
ATOM   3489 O O    . GLY A 1 217 ? 23.085 31.481 46.487 1.00 29.37  ? 220 GLY A O    1 
ATOM   3490 H H    . GLY A 1 217 ? 22.581 33.589 42.877 0.00 26.77  ? 220 GLY A H    1 
ATOM   3491 H HA2  . GLY A 1 217 ? 21.541 32.948 45.189 0.00 29.02  ? 220 GLY A HA2  1 
ATOM   3492 H HA3  . GLY A 1 217 ? 21.777 31.949 43.989 0.00 29.02  ? 220 GLY A HA3  1 
ATOM   3493 N N    . LEU A 1 218 ? 24.524 31.804 44.764 1.00 23.14  ? 221 LEU A N    1 
ATOM   3494 C CA   . LEU A 1 218 ? 25.612 31.248 45.525 1.00 25.75  ? 221 LEU A CA   1 
ATOM   3495 C C    . LEU A 1 218 ? 25.921 32.098 46.739 1.00 28.37  ? 221 LEU A C    1 
ATOM   3496 O O    . LEU A 1 218 ? 26.194 31.550 47.820 1.00 31.65  ? 221 LEU A O    1 
ATOM   3497 C CB   . LEU A 1 218 ? 26.836 31.190 44.607 1.00 27.52  ? 221 LEU A CB   1 
ATOM   3498 C CG   . LEU A 1 218 ? 26.774 30.010 43.621 1.00 30.20  ? 221 LEU A CG   1 
ATOM   3499 C CD1  . LEU A 1 218 ? 27.875 30.212 42.562 1.00 35.88  ? 221 LEU A CD1  1 
ATOM   3500 C CD2  . LEU A 1 218 ? 26.891 28.641 44.329 1.00 31.32  ? 221 LEU A CD2  1 
ATOM   3501 H H    . LEU A 1 218 ? 24.715 32.033 43.958 0.00 27.77  ? 221 LEU A H    1 
ATOM   3502 H HA   . LEU A 1 218 ? 25.383 30.358 45.837 0.00 30.91  ? 221 LEU A HA   1 
ATOM   3503 H HB2  . LEU A 1 218 ? 26.885 32.011 44.093 0.00 33.02  ? 221 LEU A HB2  1 
ATOM   3504 H HB3  . LEU A 1 218 ? 27.634 31.090 45.149 0.00 33.02  ? 221 LEU A HB3  1 
ATOM   3505 H HG   . LEU A 1 218 ? 25.908 29.988 43.184 0.00 36.24  ? 221 LEU A HG   1 
ATOM   3506 H HD11 . LEU A 1 218 ? 27.816 29.501 41.905 0.00 43.05  ? 221 LEU A HD11 1 
ATOM   3507 H HD12 . LEU A 1 218 ? 27.745 31.072 42.132 0.00 43.05  ? 221 LEU A HD12 1 
ATOM   3508 H HD13 . LEU A 1 218 ? 28.741 30.189 42.999 0.00 43.05  ? 221 LEU A HD13 1 
ATOM   3509 H HD21 . LEU A 1 218 ? 27.020 27.950 43.661 0.00 37.59  ? 221 LEU A HD21 1 
ATOM   3510 H HD22 . LEU A 1 218 ? 27.648 28.663 44.935 0.00 37.59  ? 221 LEU A HD22 1 
ATOM   3511 H HD23 . LEU A 1 218 ? 26.075 28.472 44.826 0.00 37.59  ? 221 LEU A HD23 1 
ATOM   3512 N N    . ILE A 1 219 ? 25.886 33.406 46.612 1.00 25.07  ? 222 ILE A N    1 
ATOM   3513 C CA   . ILE A 1 219 ? 26.132 34.277 47.769 1.00 29.16  ? 222 ILE A CA   1 
ATOM   3514 C C    . ILE A 1 219 ? 25.049 34.096 48.823 1.00 29.31  ? 222 ILE A C    1 
ATOM   3515 O O    . ILE A 1 219 ? 25.345 33.934 50.032 1.00 30.33  ? 222 ILE A O    1 
ATOM   3516 C CB   . ILE A 1 219 ? 26.243 35.724 47.288 1.00 29.06  ? 222 ILE A CB   1 
ATOM   3517 C CG1  . ILE A 1 219 ? 27.468 35.884 46.362 1.00 31.40  ? 222 ILE A CG1  1 
ATOM   3518 C CG2  . ILE A 1 219 ? 26.427 36.649 48.497 1.00 35.62  ? 222 ILE A CG2  1 
ATOM   3519 C CD1  . ILE A 1 219 ? 27.409 37.203 45.490 1.00 33.92  ? 222 ILE A CD1  1 
ATOM   3520 H H    . ILE A 1 219 ? 25.724 33.824 45.879 0.00 30.08  ? 222 ILE A H    1 
ATOM   3521 H HA   . ILE A 1 219 ? 26.969 34.027 48.191 0.00 35.00  ? 222 ILE A HA   1 
ATOM   3522 H HB   . ILE A 1 219 ? 25.433 35.951 46.804 0.00 34.87  ? 222 ILE A HB   1 
ATOM   3523 H HG12 . ILE A 1 219 ? 28.272 35.919 46.904 0.00 37.68  ? 222 ILE A HG12 1 
ATOM   3524 H HG13 . ILE A 1 219 ? 27.508 35.127 45.757 0.00 37.68  ? 222 ILE A HG13 1 
ATOM   3525 H HG21 . ILE A 1 219 ? 26.906 37.444 48.216 0.00 42.75  ? 222 ILE A HG21 1 
ATOM   3526 H HG22 . ILE A 1 219 ? 25.555 36.894 48.844 0.00 42.75  ? 222 ILE A HG22 1 
ATOM   3527 H HG23 . ILE A 1 219 ? 26.934 36.181 49.179 0.00 42.75  ? 222 ILE A HG23 1 
ATOM   3528 H HD11 . ILE A 1 219 ? 28.168 37.217 44.887 0.00 40.71  ? 222 ILE A HD11 1 
ATOM   3529 H HD12 . ILE A 1 219 ? 26.583 37.209 44.982 0.00 40.71  ? 222 ILE A HD12 1 
ATOM   3530 H HD13 . ILE A 1 219 ? 27.440 37.972 46.080 0.00 40.71  ? 222 ILE A HD13 1 
ATOM   3531 N N    . LEU A 1 220 ? 23.791 34.108 48.429 1.00 27.22  ? 223 LEU A N    1 
ATOM   3532 C CA   . LEU A 1 220 ? 22.692 34.063 49.404 1.00 26.31  ? 223 LEU A CA   1 
ATOM   3533 C C    . LEU A 1 220 ? 22.637 32.723 50.101 1.00 29.31  ? 223 LEU A C    1 
ATOM   3534 O O    . LEU A 1 220 ? 22.489 32.650 51.349 1.00 29.37  ? 223 LEU A O    1 
ATOM   3535 C CB   . LEU A 1 220 ? 21.365 34.289 48.638 1.00 24.74  ? 223 LEU A CB   1 
ATOM   3536 C CG   . LEU A 1 220 ? 20.115 34.166 49.491 1.00 24.98  ? 223 LEU A CG   1 
ATOM   3537 C CD1  . LEU A 1 220 ? 20.047 35.232 50.590 1.00 33.07  ? 223 LEU A CD1  1 
ATOM   3538 C CD2  . LEU A 1 220 ? 18.827 34.225 48.667 1.00 26.52  ? 223 LEU A CD2  1 
ATOM   3539 H H    . LEU A 1 220 ? 23.535 34.142 47.609 0.00 32.67  ? 223 LEU A H    1 
ATOM   3540 H HA   . LEU A 1 220 ? 22.821 34.753 50.073 0.00 31.57  ? 223 LEU A HA   1 
ATOM   3541 H HB2  . LEU A 1 220 ? 21.376 35.182 48.260 0.00 29.69  ? 223 LEU A HB2  1 
ATOM   3542 H HB3  . LEU A 1 220 ? 21.303 33.629 47.930 0.00 29.69  ? 223 LEU A HB3  1 
ATOM   3543 H HG   . LEU A 1 220 ? 20.173 33.292 49.908 0.00 29.97  ? 223 LEU A HG   1 
ATOM   3544 H HD11 . LEU A 1 220 ? 19.225 35.115 51.093 0.00 39.69  ? 223 LEU A HD11 1 
ATOM   3545 H HD12 . LEU A 1 220 ? 20.812 35.129 51.177 0.00 39.69  ? 223 LEU A HD12 1 
ATOM   3546 H HD13 . LEU A 1 220 ? 20.061 36.110 50.179 0.00 39.69  ? 223 LEU A HD13 1 
ATOM   3547 H HD21 . LEU A 1 220 ? 18.066 34.151 49.264 0.00 31.83  ? 223 LEU A HD21 1 
ATOM   3548 H HD22 . LEU A 1 220 ? 18.794 35.070 48.192 0.00 31.83  ? 223 LEU A HD22 1 
ATOM   3549 H HD23 . LEU A 1 220 ? 18.823 33.490 48.033 0.00 31.83  ? 223 LEU A HD23 1 
ATOM   3550 N N    . LEU A 1 221 ? 22.768 31.628 49.351 1.00 29.67  ? 224 LEU A N    1 
ATOM   3551 C CA   . LEU A 1 221 ? 22.478 30.324 49.954 1.00 27.91  ? 224 LEU A CA   1 
ATOM   3552 C C    . LEU A 1 221 ? 23.649 29.792 50.745 1.00 34.07  ? 224 LEU A C    1 
ATOM   3553 O O    . LEU A 1 221 ? 23.492 28.747 51.391 1.00 37.09  ? 224 LEU A O    1 
ATOM   3554 C CB   . LEU A 1 221 ? 22.049 29.352 48.852 1.00 27.81  ? 224 LEU A CB   1 
ATOM   3555 C CG   . LEU A 1 221 ? 20.769 29.722 48.135 1.00 30.11  ? 224 LEU A CG   1 
ATOM   3556 C CD1  . LEU A 1 221 ? 20.553 28.671 47.019 1.00 30.75  ? 224 LEU A CD1  1 
ATOM   3557 C CD2  . LEU A 1 221 ? 19.591 29.674 49.111 1.00 30.56  ? 224 LEU A CD2  1 
ATOM   3558 H H    . LEU A 1 221 ? 23.012 31.613 48.526 0.00 35.60  ? 224 LEU A H    1 
ATOM   3559 H HA   . LEU A 1 221 ? 21.736 30.389 50.574 0.00 33.49  ? 224 LEU A HA   1 
ATOM   3560 H HB2  . LEU A 1 221 ? 22.754 29.312 48.187 0.00 33.37  ? 224 LEU A HB2  1 
ATOM   3561 H HB3  . LEU A 1 221 ? 21.917 28.477 49.249 0.00 33.37  ? 224 LEU A HB3  1 
ATOM   3562 H HG   . LEU A 1 221 ? 20.820 30.617 47.764 0.00 36.13  ? 224 LEU A HG   1 
ATOM   3563 H HD11 . LEU A 1 221 ? 19.742 28.888 46.534 0.00 36.90  ? 224 LEU A HD11 1 
ATOM   3564 H HD12 . LEU A 1 221 ? 21.314 28.689 46.418 0.00 36.90  ? 224 LEU A HD12 1 
ATOM   3565 H HD13 . LEU A 1 221 ? 20.472 27.793 47.424 0.00 36.90  ? 224 LEU A HD13 1 
ATOM   3566 H HD21 . LEU A 1 221 ? 18.762 29.710 48.609 0.00 36.68  ? 224 LEU A HD21 1 
ATOM   3567 H HD22 . LEU A 1 221 ? 19.635 28.848 49.619 0.00 36.68  ? 224 LEU A HD22 1 
ATOM   3568 H HD23 . LEU A 1 221 ? 19.647 30.434 49.711 0.00 36.68  ? 224 LEU A HD23 1 
ATOM   3569 N N    A ARG A 1 222 ? 24.807 30.449 50.697 0.44 38.62  ? 225 ARG A N    1 
ATOM   3570 N N    B ARG A 1 222 ? 24.795 30.455 50.692 0.56 38.59  ? 225 ARG A N    1 
ATOM   3571 C CA   A ARG A 1 222 ? 25.889 30.112 51.622 0.44 41.69  ? 225 ARG A CA   1 
ATOM   3572 C CA   B ARG A 1 222 ? 25.905 30.131 51.586 0.56 41.71  ? 225 ARG A CA   1 
ATOM   3573 C C    A ARG A 1 222 ? 25.787 30.886 52.923 0.44 42.76  ? 225 ARG A C    1 
ATOM   3574 C C    B ARG A 1 222 ? 25.863 30.966 52.856 0.56 42.91  ? 225 ARG A C    1 
ATOM   3575 O O    A ARG A 1 222 ? 26.537 30.586 53.863 0.44 46.01  ? 225 ARG A O    1 
ATOM   3576 O O    B ARG A 1 222 ? 26.721 30.766 53.730 0.56 46.40  ? 225 ARG A O    1 
ATOM   3577 C CB   A ARG A 1 222 ? 27.266 30.364 50.997 0.44 45.02  ? 225 ARG A CB   1 
ATOM   3578 C CB   B ARG A 1 222 ? 27.235 30.310 50.852 0.56 44.81  ? 225 ARG A CB   1 
ATOM   3579 C CG   A ARG A 1 222 ? 27.536 31.749 50.472 0.44 46.30  ? 225 ARG A CG   1 
ATOM   3580 C CG   B ARG A 1 222 ? 27.423 29.321 49.665 0.56 44.48  ? 225 ARG A CG   1 
ATOM   3581 C CD   A ARG A 1 222 ? 27.627 32.817 51.544 0.44 48.10  ? 225 ARG A CD   1 
ATOM   3582 C CD   B ARG A 1 222 ? 28.668 29.646 48.850 0.56 47.56  ? 225 ARG A CD   1 
ATOM   3583 N NE   A ARG A 1 222 ? 28.192 34.045 51.011 0.44 51.01  ? 225 ARG A NE   1 
ATOM   3584 N NE   B ARG A 1 222 ? 29.878 29.269 49.571 0.56 53.64  ? 225 ARG A NE   1 
ATOM   3585 C CZ   A ARG A 1 222 ? 27.889 35.262 51.431 0.44 51.90  ? 225 ARG A CZ   1 
ATOM   3586 C CZ   B ARG A 1 222 ? 30.208 28.017 49.858 0.56 52.60  ? 225 ARG A CZ   1 
ATOM   3587 N NH1  A ARG A 1 222 ? 26.902 35.473 52.268 0.44 49.33  ? 225 ARG A NH1  1 
ATOM   3588 N NH1  B ARG A 1 222 ? 29.549 26.994 49.345 0.56 50.41  ? 225 ARG A NH1  1 
ATOM   3589 N NH2  A ARG A 1 222 ? 28.637 36.293 51.027 0.44 56.63  ? 225 ARG A NH2  1 
ATOM   3590 N NH2  B ARG A 1 222 ? 31.216 27.789 50.685 0.56 57.24  ? 225 ARG A NH2  1 
ATOM   3591 H H    A ARG A 1 222 ? 24.987 31.085 50.147 0.44 46.34  ? 225 ARG A H    1 
ATOM   3592 H H    B ARG A 1 222 ? 24.958 31.099 50.145 0.56 46.31  ? 225 ARG A H    1 
ATOM   3593 H HA   A ARG A 1 222 ? 25.840 29.162 51.811 0.44 50.03  ? 225 ARG A HA   1 
ATOM   3594 H HA   B ARG A 1 222 ? 25.860 29.199 51.849 0.56 50.05  ? 225 ARG A HA   1 
ATOM   3595 H HB2  A ARG A 1 222 ? 27.938 30.182 51.672 0.44 54.02  ? 225 ARG A HB2  1 
ATOM   3596 H HB2  B ARG A 1 222 ? 27.278 31.212 50.497 0.56 53.77  ? 225 ARG A HB2  1 
ATOM   3597 H HB3  A ARG A 1 222 ? 27.371 29.754 50.251 0.44 54.02  ? 225 ARG A HB3  1 
ATOM   3598 H HB3  B ARG A 1 222 ? 27.961 30.165 51.478 0.56 53.77  ? 225 ARG A HB3  1 
ATOM   3599 H HG2  A ARG A 1 222 ? 28.381 31.741 49.995 0.44 55.55  ? 225 ARG A HG2  1 
ATOM   3600 H HG2  B ARG A 1 222 ? 27.513 28.420 50.011 0.56 53.38  ? 225 ARG A HG2  1 
ATOM   3601 H HG3  A ARG A 1 222 ? 26.818 31.999 49.870 0.44 55.55  ? 225 ARG A HG3  1 
ATOM   3602 H HG3  B ARG A 1 222 ? 26.653 29.376 49.078 0.56 53.38  ? 225 ARG A HG3  1 
ATOM   3603 H HD2  A ARG A 1 222 ? 26.739 33.010 51.883 0.44 57.72  ? 225 ARG A HD2  1 
ATOM   3604 H HD2  B ARG A 1 222 ? 28.644 29.155 48.013 0.56 57.07  ? 225 ARG A HD2  1 
ATOM   3605 H HD3  A ARG A 1 222 ? 28.196 32.504 52.264 0.44 57.72  ? 225 ARG A HD3  1 
ATOM   3606 H HD3  B ARG A 1 222 ? 28.700 30.599 48.674 0.56 57.07  ? 225 ARG A HD3  1 
ATOM   3607 H HE   A ARG A 1 222 ? 28.766 33.975 50.374 0.44 61.21  ? 225 ARG A HE   1 
ATOM   3608 H HE   B ARG A 1 222 ? 30.409 29.896 49.825 0.56 64.37  ? 225 ARG A HE   1 
ATOM   3609 H HH11 A ARG A 1 222 ? 26.434 34.812 52.556 0.44 59.19  ? 225 ARG A HH11 1 
ATOM   3610 H HH11 B ARG A 1 222 ? 28.889 27.131 48.811 0.56 60.49  ? 225 ARG A HH11 1 
ATOM   3611 H HH12 A ARG A 1 222 ? 26.723 36.273 52.528 0.44 59.19  ? 225 ARG A HH12 1 
ATOM   3612 H HH12 B ARG A 1 222 ? 29.781 26.190 49.545 0.56 60.49  ? 225 ARG A HH12 1 
ATOM   3613 H HH21 A ARG A 1 222 ? 29.304 36.160 50.501 0.44 67.96  ? 225 ARG A HH21 1 
ATOM   3614 H HH21 B ARG A 1 222 ? 31.647 28.449 51.029 0.56 68.69  ? 225 ARG A HH21 1 
ATOM   3615 H HH22 A ARG A 1 222 ? 28.451 37.090 51.293 0.44 67.96  ? 225 ARG A HH22 1 
ATOM   3616 H HH22 B ARG A 1 222 ? 31.439 26.982 50.879 0.56 68.69  ? 225 ARG A HH22 1 
ATOM   3617 N N    . SER A 1 223 ? 24.868 31.833 53.026 1.00 40.67  ? 226 SER A N    1 
ATOM   3618 C CA   . SER A 1 223 ? 24.837 32.776 54.143 1.00 42.09  ? 226 SER A CA   1 
ATOM   3619 C C    . SER A 1 223 ? 24.083 32.200 55.327 1.00 41.34  ? 226 SER A C    1 
ATOM   3620 O O    . SER A 1 223 ? 23.121 31.447 55.153 1.00 43.18  ? 226 SER A O    1 
ATOM   3621 C CB   . SER A 1 223 ? 24.075 34.061 53.750 1.00 44.59  ? 226 SER A CB   1 
ATOM   3622 O OG   . SER A 1 223 ? 24.101 34.944 54.918 1.00 48.52  ? 226 SER A OG   1 
ATOM   3623 H H    . SER A 1 223 ? 24.189 31.897 52.501 0.00 48.80  ? 226 SER A H    1 
ATOM   3624 H HA   . SER A 1 223 ? 25.756 32.973 54.386 0.00 50.50  ? 226 SER A HA   1 
ATOM   3625 H HB2  . SER A 1 223 ? 24.515 34.491 52.999 0.00 53.51  ? 226 SER A HB2  1 
ATOM   3626 H HB3  . SER A 1 223 ? 23.159 33.845 53.517 0.00 53.51  ? 226 SER A HB3  1 
ATOM   3627 H HG   . SER A 1 223 ? 23.710 35.667 54.741 0.00 58.23  ? 226 SER A HG   1 
ATOM   3628 N N    . ARG A 1 224 ? 24.495 32.592 56.553 1.00 44.50  ? 227 ARG A N    1 
ATOM   3629 C CA   . ARG A 1 224 ? 23.730 32.218 57.735 1.00 44.51  ? 227 ARG A CA   1 
ATOM   3630 C C    . ARG A 1 224 ? 22.429 33.002 57.856 1.00 43.86  ? 227 ARG A C    1 
ATOM   3631 O O    . ARG A 1 224 ? 21.571 32.636 58.651 1.00 45.72  ? 227 ARG A O    1 
ATOM   3632 C CB   . ARG A 1 224 ? 24.595 32.376 59.008 1.00 56.22  ? 227 ARG A CB   1 
ATOM   3633 C CG   . ARG A 1 224 ? 26.102 32.393 58.724 1.00 68.57  ? 227 ARG A CG   1 
ATOM   3634 C CD   . ARG A 1 224 ? 26.597 31.151 57.928 1.00 81.63  ? 227 ARG A CD   1 
ATOM   3635 N NE   . ARG A 1 224 ? 27.688 31.485 57.010 1.00 85.82  ? 227 ARG A NE   1 
ATOM   3636 C CZ   . ARG A 1 224 ? 28.173 30.683 56.064 1.00 79.93  ? 227 ARG A CZ   1 
ATOM   3637 N NH1  . ARG A 1 224 ? 27.711 29.452 55.885 1.00 67.91  ? 227 ARG A NH1  1 
ATOM   3638 N NH2  . ARG A 1 224 ? 29.127 31.142 55.253 1.00 86.59  ? 227 ARG A NH2  1 
ATOM   3639 H H    . ARG A 1 224 ? 25.196 33.064 56.710 0.00 53.39  ? 227 ARG A H    1 
ATOM   3640 H HA   . ARG A 1 224 ? 23.495 31.278 57.677 0.00 53.41  ? 227 ARG A HA   1 
ATOM   3641 H HB2  . ARG A 1 224 ? 24.365 33.214 59.441 0.00 67.47  ? 227 ARG A HB2  1 
ATOM   3642 H HB3  . ARG A 1 224 ? 24.413 31.634 59.605 0.00 67.47  ? 227 ARG A HB3  1 
ATOM   3643 H HG2  . ARG A 1 224 ? 26.315 33.183 58.203 0.00 82.29  ? 227 ARG A HG2  1 
ATOM   3644 H HG3  . ARG A 1 224 ? 26.580 32.413 59.568 0.00 82.29  ? 227 ARG A HG3  1 
ATOM   3645 H HD2  . ARG A 1 224 ? 26.920 30.480 58.551 0.00 97.96  ? 227 ARG A HD2  1 
ATOM   3646 H HD3  . ARG A 1 224 ? 25.862 30.792 57.407 0.00 97.96  ? 227 ARG A HD3  1 
ATOM   3647 H HE   . ARG A 1 224 ? 28.045 32.263 57.088 0.00 102.98 ? 227 ARG A HE   1 
ATOM   3648 H HH11 . ARG A 1 224 ? 27.082 29.151 56.388 0.00 81.49  ? 227 ARG A HH11 1 
ATOM   3649 H HH12 . ARG A 1 224 ? 28.042 28.954 55.267 0.00 81.49  ? 227 ARG A HH12 1 
ATOM   3650 H HH21 . ARG A 1 224 ? 29.420 31.945 55.345 0.00 103.91 ? 227 ARG A HH21 1 
ATOM   3651 H HH22 . ARG A 1 224 ? 29.449 30.634 54.638 0.00 103.91 ? 227 ARG A HH22 1 
ATOM   3652 N N    . ALA A 1 225 ? 22.247 34.043 57.049 1.00 39.43  ? 228 ALA A N    1 
ATOM   3653 C CA   . ALA A 1 225 ? 21.111 34.934 57.203 1.00 39.49  ? 228 ALA A CA   1 
ATOM   3654 C C    . ALA A 1 225 ? 19.819 34.253 56.776 1.00 42.28  ? 228 ALA A C    1 
ATOM   3655 O O    . ALA A 1 225 ? 18.741 34.736 57.100 1.00 44.21  ? 228 ALA A O    1 
ATOM   3656 C CB   . ALA A 1 225 ? 21.237 36.121 56.235 1.00 39.03  ? 228 ALA A CB   1 
ATOM   3657 H H    . ALA A 1 225 ? 22.772 34.254 56.401 0.00 47.31  ? 228 ALA A H    1 
ATOM   3658 H HA   . ALA A 1 225 ? 21.092 35.226 58.128 0.00 47.39  ? 228 ALA A HA   1 
ATOM   3659 H HB1  . ALA A 1 225 ? 20.469 36.704 56.349 0.00 46.84  ? 228 ALA A HB1  1 
ATOM   3660 H HB2  . ALA A 1 225 ? 22.053 36.606 56.434 0.00 46.84  ? 228 ALA A HB2  1 
ATOM   3661 H HB3  . ALA A 1 225 ? 21.265 35.785 55.326 0.00 46.84  ? 228 ALA A HB3  1 
ATOM   3662 N N    . ILE A 1 226 ? 19.905 33.151 56.045 1.00 35.94  ? 229 ILE A N    1 
ATOM   3663 C CA   . ILE A 1 226 ? 18.641 32.583 55.549 1.00 35.94  ? 229 ILE A CA   1 
ATOM   3664 C C    . ILE A 1 226 ? 18.023 31.659 56.581 1.00 39.84  ? 229 ILE A C    1 
ATOM   3665 O O    . ILE A 1 226 ? 16.916 31.145 56.385 1.00 38.27  ? 229 ILE A O    1 
ATOM   3666 C CB   . ILE A 1 226 ? 18.881 31.880 54.198 1.00 31.62  ? 229 ILE A CB   1 
ATOM   3667 C CG1  . ILE A 1 226 ? 19.844 30.684 54.381 1.00 37.10  ? 229 ILE A CG1  1 
ATOM   3668 C CG2  . ILE A 1 226 ? 19.298 32.877 53.101 1.00 32.60  ? 229 ILE A CG2  1 
ATOM   3669 C CD1  . ILE A 1 226 ? 19.914 29.777 53.078 1.00 38.83  ? 229 ILE A CD1  1 
ATOM   3670 H H    . ILE A 1 226 ? 20.628 32.737 55.833 0.00 43.13  ? 229 ILE A H    1 
ATOM   3671 H HA   . ILE A 1 226 ? 17.989 33.281 55.380 0.00 43.13  ? 229 ILE A HA   1 
ATOM   3672 H HB   . ILE A 1 226 ? 18.044 31.506 53.881 0.00 37.94  ? 229 ILE A HB   1 
ATOM   3673 H HG12 . ILE A 1 226 ? 20.735 31.017 54.568 0.00 44.52  ? 229 ILE A HG12 1 
ATOM   3674 H HG13 . ILE A 1 226 ? 19.533 30.134 55.118 0.00 44.52  ? 229 ILE A HG13 1 
ATOM   3675 H HG21 . ILE A 1 226 ? 19.352 32.409 52.253 0.00 39.12  ? 229 ILE A HG21 1 
ATOM   3676 H HG22 . ILE A 1 226 ? 18.635 33.583 53.048 0.00 39.12  ? 229 ILE A HG22 1 
ATOM   3677 H HG23 . ILE A 1 226 ? 20.163 33.252 53.327 0.00 39.12  ? 229 ILE A HG23 1 
ATOM   3678 H HD11 . ILE A 1 226 ? 20.514 29.033 53.243 0.00 46.60  ? 229 ILE A HD11 1 
ATOM   3679 H HD12 . ILE A 1 226 ? 19.025 29.446 52.875 0.00 46.60  ? 229 ILE A HD12 1 
ATOM   3680 H HD13 . ILE A 1 226 ? 20.244 30.311 52.339 0.00 46.60  ? 229 ILE A HD13 1 
ATOM   3681 N N    . PHE A 1 227 ? 18.722 31.380 57.703 1.00 36.08  ? 230 PHE A N    1 
ATOM   3682 C CA   . PHE A 1 227 ? 18.140 30.545 58.740 1.00 37.42  ? 230 PHE A CA   1 
ATOM   3683 C C    . PHE A 1 227 ? 17.609 31.381 59.886 1.00 43.20  ? 230 PHE A C    1 
ATOM   3684 O O    . PHE A 1 227 ? 18.165 32.430 60.254 1.00 43.32  ? 230 PHE A O    1 
ATOM   3685 C CB   . PHE A 1 227 ? 19.205 29.619 59.332 1.00 38.49  ? 230 PHE A CB   1 
ATOM   3686 C CG   . PHE A 1 227 ? 19.633 28.569 58.401 1.00 39.59  ? 230 PHE A CG   1 
ATOM   3687 C CD1  . PHE A 1 227 ? 20.627 28.806 57.459 1.00 49.37  ? 230 PHE A CD1  1 
ATOM   3688 C CD2  . PHE A 1 227 ? 18.954 27.366 58.352 1.00 41.93  ? 230 PHE A CD2  1 
ATOM   3689 C CE1  . PHE A 1 227 ? 20.996 27.844 56.578 1.00 53.90  ? 230 PHE A CE1  1 
ATOM   3690 C CE2  . PHE A 1 227 ? 19.333 26.396 57.483 1.00 51.14  ? 230 PHE A CE2  1 
ATOM   3691 C CZ   . PHE A 1 227 ? 20.350 26.638 56.576 1.00 54.85  ? 230 PHE A CZ   1 
ATOM   3692 H H    . PHE A 1 227 ? 19.517 31.663 57.869 0.00 43.29  ? 230 PHE A H    1 
ATOM   3693 H HA   . PHE A 1 227 ? 17.415 30.037 58.345 0.00 44.91  ? 230 PHE A HA   1 
ATOM   3694 H HB2  . PHE A 1 227 ? 19.984 30.146 59.567 0.00 46.19  ? 230 PHE A HB2  1 
ATOM   3695 H HB3  . PHE A 1 227 ? 18.843 29.190 60.123 0.00 46.19  ? 230 PHE A HB3  1 
ATOM   3696 H HD1  . PHE A 1 227 ? 21.045 29.637 57.433 0.00 59.25  ? 230 PHE A HD1  1 
ATOM   3697 H HD2  . PHE A 1 227 ? 18.232 27.221 58.920 0.00 50.32  ? 230 PHE A HD2  1 
ATOM   3698 H HE1  . PHE A 1 227 ? 21.687 28.004 55.976 0.00 64.69  ? 230 PHE A HE1  1 
ATOM   3699 H HE2  . PHE A 1 227 ? 18.910 25.568 57.496 0.00 61.37  ? 230 PHE A HE2  1 
ATOM   3700 H HZ   . PHE A 1 227 ? 20.594 25.981 55.964 0.00 65.82  ? 230 PHE A HZ   1 
ATOM   3701 N N    . GLY A 1 228 ? 16.528 30.901 60.472 1.00 41.82  ? 231 GLY A N    1 
ATOM   3702 C CA   . GLY A 1 228 ? 16.054 31.527 61.683 1.00 41.24  ? 231 GLY A CA   1 
ATOM   3703 C C    . GLY A 1 228 ? 17.097 31.419 62.782 1.00 51.18  ? 231 GLY A C    1 
ATOM   3704 O O    . GLY A 1 228 ? 17.915 30.502 62.791 1.00 46.41  ? 231 GLY A O    1 
ATOM   3705 H H    . GLY A 1 228 ? 16.065 30.232 60.195 0.00 50.19  ? 231 GLY A H    1 
ATOM   3706 H HA2  . GLY A 1 228 ? 15.869 32.464 61.517 0.00 49.49  ? 231 GLY A HA2  1 
ATOM   3707 H HA3  . GLY A 1 228 ? 15.239 31.092 61.980 0.00 49.49  ? 231 GLY A HA3  1 
ATOM   3708 N N    . GLU A 1 229 ? 17.092 32.387 63.685 1.00 51.18  ? 232 GLU A N    1 
ATOM   3709 C CA   . GLU A 1 229 ? 17.954 32.290 64.869 1.00 45.49  ? 232 GLU A CA   1 
ATOM   3710 C C    . GLU A 1 229 ? 17.443 31.180 65.776 1.00 58.98  ? 232 GLU A C    1 
ATOM   3711 O O    . GLU A 1 229 ? 16.301 31.227 66.245 1.00 57.01  ? 232 GLU A O    1 
ATOM   3712 C CB   . GLU A 1 229 ? 17.977 33.628 65.623 1.00 66.53  ? 232 GLU A CB   1 
ATOM   3713 C CG   . GLU A 1 229 ? 19.363 34.333 65.640 1.00 64.60  ? 232 GLU A CG   1 
ATOM   3714 C CD   . GLU A 1 229 ? 19.521 35.325 66.770 1.00 66.66  ? 232 GLU A CD   1 
ATOM   3715 O OE1  . GLU A 1 229 ? 18.540 36.065 67.003 1.00 67.00  ? 232 GLU A OE1  1 
ATOM   3716 O OE2  . GLU A 1 229 ? 20.636 35.413 67.374 1.00 47.39  ? 232 GLU A OE2  1 
ATOM   3717 H H    . GLU A 1 229 ? 16.612 33.099 63.643 0.00 61.42  ? 232 GLU A H    1 
ATOM   3718 H HA   . GLU A 1 229 ? 18.861 32.083 64.594 0.00 54.59  ? 232 GLU A HA   1 
ATOM   3719 H HB2  . GLU A 1 229 ? 17.346 34.231 65.201 0.00 79.84  ? 232 GLU A HB2  1 
ATOM   3720 H HB3  . GLU A 1 229 ? 17.717 33.468 66.544 0.00 79.84  ? 232 GLU A HB3  1 
ATOM   3721 H HG2  . GLU A 1 229 ? 20.055 33.661 65.737 0.00 77.53  ? 232 GLU A HG2  1 
ATOM   3722 H HG3  . GLU A 1 229 ? 19.480 34.813 64.806 0.00 77.53  ? 232 GLU A HG3  1 
ATOM   3723 N N    . ALA A 1 230 ? 18.269 30.173 66.029 1.00 46.70  ? 233 ALA A N    1 
ATOM   3724 C CA   . ALA A 1 230 ? 17.841 29.101 66.914 1.00 49.15  ? 233 ALA A CA   1 
ATOM   3725 C C    . ALA A 1 230 ? 19.052 28.523 67.607 1.00 51.94  ? 233 ALA A C    1 
ATOM   3726 O O    . ALA A 1 230 ? 20.183 28.670 67.144 1.00 61.55  ? 233 ALA A O    1 
ATOM   3727 C CB   . ALA A 1 230 ? 17.125 27.986 66.158 1.00 58.01  ? 233 ALA A CB   1 
ATOM   3728 H H    . ALA A 1 230 ? 19.063 30.091 65.708 0.00 56.05  ? 233 ALA A H    1 
ATOM   3729 H HA   . ALA A 1 230 ? 17.236 29.472 67.575 0.00 58.98  ? 233 ALA A HA   1 
ATOM   3730 H HB1  . ALA A 1 230 ? 16.875 27.289 66.785 0.00 69.61  ? 233 ALA A HB1  1 
ATOM   3731 H HB2  . ALA A 1 230 ? 16.331 28.350 65.735 0.00 69.61  ? 233 ALA A HB2  1 
ATOM   3732 H HB3  . ALA A 1 230 ? 17.723 27.626 65.484 0.00 69.61  ? 233 ALA A HB3  1 
ATOM   3733 N N    . GLU A 1 231 ? 18.800 27.892 68.761 1.00 50.50  ? 234 GLU A N    1 
ATOM   3734 C CA   . GLU A 1 231 ? 19.845 27.237 69.522 1.00 55.32  ? 234 GLU A CA   1 
ATOM   3735 C C    . GLU A 1 231 ? 20.176 25.863 68.931 1.00 71.77  ? 234 GLU A C    1 
ATOM   3736 O O    . GLU A 1 231 ? 19.462 24.886 69.182 1.00 79.39  ? 234 GLU A O    1 
ATOM   3737 C CB   . GLU A 1 231 ? 19.408 27.076 70.977 1.00 53.21  ? 234 GLU A CB   1 
ATOM   3738 C CG   . GLU A 1 231 ? 20.514 26.847 71.873 1.00 52.24  ? 234 GLU A CG   1 
ATOM   3739 C CD   . GLU A 1 231 ? 21.451 28.065 71.923 1.00 50.58  ? 234 GLU A CD   1 
ATOM   3740 O OE1  . GLU A 1 231 ? 20.943 29.192 71.891 1.00 49.52  ? 234 GLU A OE1  1 
ATOM   3741 O OE2  . GLU A 1 231 ? 22.654 27.874 72.091 1.00 51.21  ? 234 GLU A OE2  1 
ATOM   3742 H H    . GLU A 1 231 ? 18.021 27.834 69.120 0.00 60.61  ? 234 GLU A H    1 
ATOM   3743 H HA   . GLU A 1 231 ? 20.647 27.782 69.494 0.00 66.38  ? 234 GLU A HA   1 
ATOM   3744 H HB2  . GLU A 1 231 ? 18.954 27.884 71.261 0.00 63.86  ? 234 GLU A HB2  1 
ATOM   3745 H HB3  . GLU A 1 231 ? 18.807 26.317 71.043 0.00 63.86  ? 234 GLU A HB3  1 
ATOM   3746 H HG2  . GLU A 1 231 ? 20.175 26.684 72.767 0.00 62.69  ? 234 GLU A HG2  1 
ATOM   3747 H HG3  . GLU A 1 231 ? 21.023 26.081 71.566 0.00 62.69  ? 234 GLU A HG3  1 
HETATM 3748 C C52  . LI1 B 2 .   ? 13.210 59.652 25.049 1.00 49.82  ? 301 LI1 A C52  1 
HETATM 3749 C C53  . LI1 B 2 .   ? 13.026 59.534 23.534 1.00 47.90  ? 301 LI1 A C53  1 
HETATM 3750 C C55  . LI1 B 2 .   ? 14.321 59.493 22.730 1.00 54.91  ? 301 LI1 A C55  1 
HETATM 3751 C C56  . LI1 B 2 .   ? 14.084 59.323 21.226 1.00 47.64  ? 301 LI1 A C56  1 
HETATM 3752 C C57  . LI1 B 2 .   ? 15.258 59.662 20.308 1.00 57.20  ? 301 LI1 A C57  1 
HETATM 3753 C C58  . LI1 B 2 .   ? 15.012 59.336 18.844 1.00 44.13  ? 301 LI1 A C58  1 
HETATM 3754 C C46  . LI1 C 2 .   ? 4.646  60.958 20.091 1.00 63.23  ? 302 LI1 A C46  1 
HETATM 3755 C C47  . LI1 C 2 .   ? 4.013  61.089 21.474 1.00 60.86  ? 302 LI1 A C47  1 
HETATM 3756 C C48  . LI1 C 2 .   ? 4.958  60.867 22.649 1.00 62.52  ? 302 LI1 A C48  1 
HETATM 3757 C C49  . LI1 C 2 .   ? 5.772  59.623 22.359 1.00 64.68  ? 302 LI1 A C49  1 
HETATM 3758 C C50  . LI1 C 2 .   ? 4.068  60.589 23.856 1.00 57.32  ? 302 LI1 A C50  1 
HETATM 3759 C C51  . LI1 C 2 .   ? 4.792  60.485 25.193 1.00 57.54  ? 302 LI1 A C51  1 
HETATM 3760 C C52  . LI1 C 2 .   ? 3.955  60.978 26.363 1.00 68.85  ? 302 LI1 A C52  1 
HETATM 3761 C C53  . LI1 C 2 .   ? 4.708  61.044 27.681 1.00 63.56  ? 302 LI1 A C53  1 
HETATM 3762 C C55  . LI1 C 2 .   ? 5.906  60.117 27.731 1.00 63.95  ? 302 LI1 A C55  1 
HETATM 3763 C C56  . LI1 C 2 .   ? 6.726  60.267 28.996 1.00 71.18  ? 302 LI1 A C56  1 
HETATM 3764 C C57  . LI1 C 2 .   ? 8.095  59.593 28.935 1.00 69.13  ? 302 LI1 A C57  1 
HETATM 3765 C C58  . LI1 C 2 .   ? 9.012  59.859 30.126 1.00 73.64  ? 302 LI1 A C58  1 
HETATM 3766 C C59  . LI1 C 2 .   ? 8.666  61.162 30.826 1.00 79.96  ? 302 LI1 A C59  1 
HETATM 3767 C C60  . LI1 C 2 .   ? 9.022  58.728 31.125 1.00 57.46  ? 302 LI1 A C60  1 
HETATM 3768 H H461 . LI1 C 2 .   ? 5.507  61.401 20.074 1.00 75.88  ? 302 LI1 A H461 1 
HETATM 3769 H H462 . LI1 C 2 .   ? 4.790  60.019 19.895 1.00 75.88  ? 302 LI1 A H462 1 
HETATM 3770 H H471 . LI1 C 2 .   ? 3.622  61.974 21.540 1.00 73.04  ? 302 LI1 A H471 1 
HETATM 3771 H H472 . LI1 C 2 .   ? 3.281  60.454 21.527 1.00 73.04  ? 302 LI1 A H472 1 
HETATM 3772 H H48  . LI1 C 2 .   ? 5.541  61.628 22.800 1.00 75.03  ? 302 LI1 A H48  1 
HETATM 3773 C C50  . LI1 D 2 .   ? 24.019 22.000 24.591 1.00 54.14  ? 303 LI1 A C50  1 
HETATM 3774 C C51  . LI1 D 2 .   ? 22.956 22.559 25.527 1.00 47.40  ? 303 LI1 A C51  1 
HETATM 3775 C C52  . LI1 D 2 .   ? 23.232 22.348 26.999 1.00 55.45  ? 303 LI1 A C52  1 
HETATM 3776 C C53  . LI1 D 2 .   ? 22.611 21.093 27.571 1.00 52.63  ? 303 LI1 A C53  1 
HETATM 3777 C C55  . LI1 D 2 .   ? 22.270 21.172 29.058 1.00 56.73  ? 303 LI1 A C55  1 
HETATM 3778 C C56  . LI1 D 2 .   ? 22.912 20.086 29.921 1.00 60.14  ? 303 LI1 A C56  1 
HETATM 3779 C C57  . LI1 D 2 .   ? 24.113 20.560 30.750 1.00 54.23  ? 303 LI1 A C57  1 
HETATM 3780 C C58  . LI1 D 2 .   ? 23.867 20.687 32.255 1.00 51.58  ? 303 LI1 A C58  1 
HETATM 3781 C C45  . LI1 E 2 .   ? -1.397 30.375 19.229 1.00 44.40  ? 304 LI1 A C45  1 
HETATM 3782 C C46  . LI1 E 2 .   ? -2.152 30.832 20.476 1.00 58.00  ? 304 LI1 A C46  1 
HETATM 3783 C C47  . LI1 E 2 .   ? -1.370 30.650 21.774 1.00 44.01  ? 304 LI1 A C47  1 
HETATM 3784 C C48  . LI1 E 2 .   ? -1.989 31.321 23.004 1.00 53.75  ? 304 LI1 A C48  1 
HETATM 3785 C C50  . LI1 E 2 .   ? -1.249 30.987 24.296 1.00 57.21  ? 304 LI1 A C50  1 
HETATM 3786 C C51  . LI1 E 2 .   ? -2.112 30.343 25.354 1.00 45.58  ? 304 LI1 A C51  1 
HETATM 3787 C C52  . LI1 E 2 .   ? -1.680 30.548 26.791 1.00 53.13  ? 304 LI1 A C52  1 
HETATM 3788 C C53  . LI1 E 2 .   ? -2.477 31.615 27.537 1.00 63.40  ? 304 LI1 A C53  1 
HETATM 3789 C C55  . LI1 E 2 .   ? -2.325 31.534 29.048 1.00 50.30  ? 304 LI1 A C55  1 
HETATM 3790 C C56  . LI1 E 2 .   ? -2.212 32.892 29.764 1.00 60.93  ? 304 LI1 A C56  1 
HETATM 3791 C C57  . LI1 E 2 .   ? -3.315 33.893 29.411 1.00 66.12  ? 304 LI1 A C57  1 
HETATM 3792 C C58  . LI1 E 2 .   ? -3.654 34.928 30.472 1.00 60.71  ? 304 LI1 A C58  1 
HETATM 3793 H H451 . LI1 E 2 .   ? -1.486 31.060 18.546 1.00 53.28  ? 304 LI1 A H451 1 
HETATM 3794 H H452 . LI1 E 2 .   ? -0.455 30.325 19.446 1.00 53.28  ? 304 LI1 A H452 1 
HETATM 3795 H H461 . LI1 E 2 .   ? -2.981 30.332 20.527 1.00 69.60  ? 304 LI1 A H461 1 
HETATM 3796 H H462 . LI1 E 2 .   ? -2.377 31.769 20.366 1.00 69.60  ? 304 LI1 A H462 1 
HETATM 3797 C C45  . LI1 F 2 .   ? 26.296 59.448 53.568 1.00 67.81  ? 305 LI1 A C45  1 
HETATM 3798 C C46  . LI1 F 2 .   ? 25.161 59.723 52.585 1.00 59.93  ? 305 LI1 A C46  1 
HETATM 3799 C C47  . LI1 F 2 .   ? 24.550 58.466 51.963 1.00 65.96  ? 305 LI1 A C47  1 
HETATM 3800 C C48  . LI1 F 2 .   ? 23.591 58.721 50.787 1.00 62.26  ? 305 LI1 A C48  1 
HETATM 3801 C C50  . LI1 F 2 .   ? 24.346 58.992 49.487 1.00 61.82  ? 305 LI1 A C50  1 
HETATM 3802 C C51  . LI1 F 2 .   ? 23.515 59.646 48.387 1.00 56.99  ? 305 LI1 A C51  1 
HETATM 3803 C C52  . LI1 F 2 .   ? 23.503 58.868 47.077 1.00 64.92  ? 305 LI1 A C52  1 
HETATM 3804 C C53  . LI1 F 2 .   ? 22.701 59.542 45.968 1.00 62.76  ? 305 LI1 A C53  1 
HETATM 3805 C C55  . LI1 F 2 .   ? 23.484 59.785 44.689 1.00 55.84  ? 305 LI1 A C55  1 
HETATM 3806 C C56  . LI1 F 2 .   ? 22.611 60.119 43.494 1.00 57.78  ? 305 LI1 A C56  1 
HETATM 3807 C C57  . LI1 F 2 .   ? 23.195 59.682 42.154 1.00 57.85  ? 305 LI1 A C57  1 
HETATM 3808 C C58  . LI1 F 2 .   ? 22.494 60.208 40.906 1.00 59.15  ? 305 LI1 A C58  1 
HETATM 3809 C C59  . LI1 F 2 .   ? 22.753 59.302 39.695 1.00 58.65  ? 305 LI1 A C59  1 
HETATM 3810 H H451 . LI1 F 2 .   ? 26.007 58.802 54.231 1.00 81.38  ? 305 LI1 A H451 1 
HETATM 3811 H H452 . LI1 F 2 .   ? 27.029 59.039 53.079 1.00 81.38  ? 305 LI1 A H452 1 
HETATM 3812 H H461 . LI1 F 2 .   ? 24.469 60.216 53.055 1.00 71.92  ? 305 LI1 A H461 1 
HETATM 3813 H H462 . LI1 F 2 .   ? 25.505 60.294 51.881 1.00 71.92  ? 305 LI1 A H462 1 
HETATM 3814 H H471 . LI1 F 2 .   ? 24.081 57.984 52.663 1.00 79.15  ? 305 LI1 A H471 1 
HETATM 3815 H H472 . LI1 F 2 .   ? 25.277 57.896 51.668 1.00 79.15  ? 305 LI1 A H472 1 
HETATM 3816 C C46  . LI1 G 2 .   ? 27.496 50.483 44.985 1.00 69.32  ? 306 LI1 A C46  1 
HETATM 3817 C C47  . LI1 G 2 .   ? 26.791 51.686 44.381 1.00 85.25  ? 306 LI1 A C47  1 
HETATM 3818 C C48  . LI1 G 2 .   ? 26.226 51.472 42.974 1.00 85.72  ? 306 LI1 A C48  1 
HETATM 3819 C C50  . LI1 G 2 .   ? 27.283 51.820 41.926 1.00 82.81  ? 306 LI1 A C50  1 
HETATM 3820 C C51  . LI1 G 2 .   ? 26.773 51.949 40.500 1.00 72.57  ? 306 LI1 A C51  1 
HETATM 3821 C C52  . LI1 G 2 .   ? 27.873 51.777 39.465 1.00 80.49  ? 306 LI1 A C52  1 
HETATM 3822 C C53  . LI1 G 2 .   ? 27.513 52.344 38.107 1.00 78.25  ? 306 LI1 A C53  1 
HETATM 3823 C C55  . LI1 G 2 .   ? 26.085 52.052 37.694 1.00 68.66  ? 306 LI1 A C55  1 
HETATM 3824 C C56  . LI1 G 2 .   ? 25.983 51.502 36.279 1.00 61.86  ? 306 LI1 A C56  1 
HETATM 3825 C C57  . LI1 G 2 .   ? 27.065 50.492 35.958 1.00 59.84  ? 306 LI1 A C57  1 
HETATM 3826 C C58  . LI1 G 2 .   ? 27.227 50.236 34.471 1.00 64.26  ? 306 LI1 A C58  1 
HETATM 3827 C C59  . LI1 G 2 .   ? 26.254 51.110 33.694 1.00 55.32  ? 306 LI1 A C59  1 
HETATM 3828 C C60  . LI1 G 2 .   ? 27.010 48.781 34.150 1.00 60.22  ? 306 LI1 A C60  1 
HETATM 3829 H H461 . LI1 G 2 .   ? 28.152 50.137 44.363 1.00 83.19  ? 306 LI1 A H461 1 
HETATM 3830 H H462 . LI1 G 2 .   ? 27.966 50.776 45.783 1.00 83.19  ? 306 LI1 A H462 1 
HETATM 3831 H H471 . LI1 G 2 .   ? 27.420 52.424 44.365 1.00 102.31 ? 306 LI1 A H471 1 
HETATM 3832 H H472 . LI1 G 2 .   ? 26.073 51.943 44.980 1.00 102.31 ? 306 LI1 A H472 1 
HETATM 3833 C C18  . OLC H 3 .   ? 20.277 19.460 32.642 1.00 58.51  ? 307 OLC A C18  1 
HETATM 3834 C C10  . OLC H 3 .   ? 12.601 20.964 35.668 1.00 41.72  ? 307 OLC A C10  1 
HETATM 3835 C C9   . OLC H 3 .   ? 12.066 21.068 36.883 1.00 50.39  ? 307 OLC A C9   1 
HETATM 3836 C C17  . OLC H 3 .   ? 19.351 19.659 33.859 1.00 58.71  ? 307 OLC A C17  1 
HETATM 3837 C C11  . OLC H 3 .   ? 13.033 22.144 34.755 1.00 49.17  ? 307 OLC A C11  1 
HETATM 3838 C C8   . OLC H 3 .   ? 11.483 21.847 38.093 1.00 55.85  ? 307 OLC A C8   1 
HETATM 3839 C C24  . OLC H 3 .   ? 11.060 22.962 49.186 1.00 54.03  ? 307 OLC A C24  1 
HETATM 3840 C C16  . OLC H 3 .   ? 18.188 20.577 33.455 1.00 51.83  ? 307 OLC A C16  1 
HETATM 3841 C C12  . OLC H 3 .   ? 14.511 22.450 35.098 1.00 50.05  ? 307 OLC A C12  1 
HETATM 3842 C C7   . OLC H 3 .   ? 12.131 21.198 39.329 1.00 50.40  ? 307 OLC A C7   1 
HETATM 3843 C C15  . OLC H 3 .   ? 17.857 21.623 34.547 1.00 49.83  ? 307 OLC A C15  1 
HETATM 3844 C C13  . OLC H 3 .   ? 15.404 21.319 34.525 1.00 57.48  ? 307 OLC A C13  1 
HETATM 3845 C C6   . OLC H 3 .   ? 11.850 21.946 40.656 1.00 49.37  ? 307 OLC A C6   1 
HETATM 3846 C C14  . OLC H 3 .   ? 16.663 21.139 35.391 1.00 54.21  ? 307 OLC A C14  1 
HETATM 3847 C C5   . OLC H 3 .   ? 12.064 23.477 40.638 1.00 47.79  ? 307 OLC A C5   1 
HETATM 3848 C C4   . OLC H 3 .   ? 11.575 23.948 42.039 1.00 44.62  ? 307 OLC A C4   1 
HETATM 3849 C C3   . OLC H 3 .   ? 12.597 23.524 43.128 1.00 48.93  ? 307 OLC A C3   1 
HETATM 3850 C C2   . OLC H 3 .   ? 12.196 24.307 44.387 1.00 37.55  ? 307 OLC A C2   1 
HETATM 3851 C C21  . OLC H 3 .   ? 13.126 23.679 48.008 1.00 49.93  ? 307 OLC A C21  1 
HETATM 3852 C C1   . OLC H 3 .   ? 13.020 23.954 45.640 1.00 40.25  ? 307 OLC A C1   1 
HETATM 3853 C C22  . OLC H 3 .   ? 12.243 23.938 49.244 1.00 52.56  ? 307 OLC A C22  1 
HETATM 3854 O O19  . OLC H 3 .   ? 14.157 23.690 45.584 1.00 52.71  ? 307 OLC A O19  1 
HETATM 3855 O O25  . OLC H 3 .   ? 10.324 22.903 50.394 1.00 52.58  ? 307 OLC A O25  1 
HETATM 3856 O O23  . OLC H 3 .   ? 13.027 23.690 50.381 1.00 67.48  ? 307 OLC A O23  1 
HETATM 3857 O O20  . OLC H 3 .   ? 12.358 24.022 46.883 1.00 40.97  ? 307 OLC A O20  1 
HETATM 3858 H H18  . OLC H 3 .   ? 20.688 20.421 32.337 0.00 70.22  ? 307 OLC A H18  1 
HETATM 3859 H H18A . OLC H 3 .   ? 21.089 18.788 32.910 0.00 70.22  ? 307 OLC A H18A 1 
HETATM 3860 H H18B . OLC H 3 .   ? 19.708 19.032 31.819 0.00 70.22  ? 307 OLC A H18B 1 
HETATM 3861 H H10  . OLC H 3 .   ? 13.656 20.717 35.749 0.00 50.07  ? 307 OLC A H10  1 
HETATM 3862 H H9   . OLC H 3 .   ? 12.374 22.110 36.871 0.00 60.47  ? 307 OLC A H9   1 
HETATM 3863 H H17  . OLC H 3 .   ? 19.911 20.116 34.673 0.00 70.46  ? 307 OLC A H17  1 
HETATM 3864 H H17A . OLC H 3 .   ? 18.961 18.696 34.182 0.00 70.46  ? 307 OLC A H17A 1 
HETATM 3865 H H11  . OLC H 3 .   ? 12.941 21.861 33.705 0.00 59.01  ? 307 OLC A H11  1 
HETATM 3866 H H11A . OLC H 3 .   ? 12.412 23.019 34.951 0.00 59.01  ? 307 OLC A H11A 1 
HETATM 3867 H H8   . OLC H 3 .   ? 10.399 21.744 38.129 0.00 67.02  ? 307 OLC A H8   1 
HETATM 3868 H H8A  . OLC H 3 .   ? 11.746 22.903 38.031 0.00 67.02  ? 307 OLC A H8A  1 
HETATM 3869 H H24  . OLC H 3 .   ? 11.443 21.967 48.966 0.00 64.84  ? 307 OLC A H24  1 
HETATM 3870 H H24A . OLC H 3 .   ? 10.389 23.278 48.388 0.00 64.84  ? 307 OLC A H24A 1 
HETATM 3871 H H16  . OLC H 3 .   ? 18.458 21.101 32.538 0.00 62.20  ? 307 OLC A H16  1 
HETATM 3872 H H16A . OLC H 3 .   ? 17.304 19.964 33.277 0.00 62.20  ? 307 OLC A H16A 1 
HETATM 3873 H H12  . OLC H 3 .   ? 14.799 23.403 34.656 0.00 60.06  ? 307 OLC A H12  1 
HETATM 3874 H H12A . OLC H 3 .   ? 14.633 22.500 36.179 0.00 60.06  ? 307 OLC A H12A 1 
HETATM 3875 H H7   . OLC H 3 .   ? 11.750 20.181 39.421 0.00 60.48  ? 307 OLC A H7   1 
HETATM 3876 H H7A  . OLC H 3 .   ? 13.210 21.169 39.174 0.00 60.48  ? 307 OLC A H7A  1 
HETATM 3877 H H15  . OLC H 3 .   ? 17.604 22.571 34.075 0.00 59.80  ? 307 OLC A H15  1 
HETATM 3878 H H15A . OLC H 3 .   ? 18.724 21.759 35.192 0.00 59.80  ? 307 OLC A H15A 1 
HETATM 3879 H H13  . OLC H 3 .   ? 15.701 21.576 33.509 0.00 68.97  ? 307 OLC A H13  1 
HETATM 3880 H H13A . OLC H 3 .   ? 14.840 20.388 34.514 0.00 68.97  ? 307 OLC A H13A 1 
HETATM 3881 H H6   . OLC H 3 .   ? 10.812 21.759 40.929 0.00 59.24  ? 307 OLC A H6   1 
HETATM 3882 H H6A  . OLC H 3 .   ? 12.507 21.528 41.419 0.00 59.24  ? 307 OLC A H6A  1 
HETATM 3883 H H14  . OLC H 3 .   ? 16.581 21.734 36.301 0.00 65.06  ? 307 OLC A H14  1 
HETATM 3884 H H14A . OLC H 3 .   ? 16.791 20.089 35.654 0.00 65.06  ? 307 OLC A H14A 1 
HETATM 3885 H H5   . OLC H 3 .   ? 11.474 23.940 39.847 0.00 57.34  ? 307 OLC A H5   1 
HETATM 3886 H H5A  . OLC H 3 .   ? 13.117 23.718 40.494 0.00 57.34  ? 307 OLC A H5A  1 
HETATM 3887 H H4   . OLC H 3 .   ? 11.476 25.034 42.041 0.00 53.54  ? 307 OLC A H4   1 
HETATM 3888 H H4A  . OLC H 3 .   ? 10.608 23.495 42.255 0.00 53.54  ? 307 OLC A H4A  1 
HETATM 3889 H H3   . OLC H 3 .   ? 12.537 22.451 43.310 0.00 58.72  ? 307 OLC A H3   1 
HETATM 3890 H H3A  . OLC H 3 .   ? 13.610 23.785 42.823 0.00 58.72  ? 307 OLC A H3A  1 
HETATM 3891 H H2   . OLC H 3 .   ? 12.322 25.369 44.184 0.00 45.06  ? 307 OLC A H2   1 
HETATM 3892 H H2A  . OLC H 3 .   ? 11.148 24.100 44.599 0.00 45.06  ? 307 OLC A H2A  1 
HETATM 3893 H H21  . OLC H 3 .   ? 14.024 24.295 48.052 0.00 59.91  ? 307 OLC A H21  1 
HETATM 3894 H H21A . OLC H 3 .   ? 13.409 22.627 47.963 0.00 59.91  ? 307 OLC A H21A 1 
HETATM 3895 H H22  . OLC H 3 .   ? 11.868 24.961 49.275 0.00 63.07  ? 307 OLC A H22  1 
HETATM 3896 H HO25 . OLC H 3 .   ? 10.043 22.017 50.554 0.00 63.10  ? 307 OLC A HO25 1 
HETATM 3897 H HO23 . OLC H 3 .   ? 12.981 24.437 50.965 0.00 80.98  ? 307 OLC A HO23 1 
HETATM 3898 C C18  . OLC I 3 .   ? 6.220  32.057 41.803 1.00 56.71  ? 308 OLC A C18  1 
HETATM 3899 C C10  . OLC I 3 .   ? 7.780  28.691 32.559 1.00 54.12  ? 308 OLC A C10  1 
HETATM 3900 C C9   . OLC I 3 .   ? 7.805  28.515 31.217 1.00 56.20  ? 308 OLC A C9   1 
HETATM 3901 C C17  . OLC I 3 .   ? 5.676  32.096 40.364 1.00 50.79  ? 308 OLC A C17  1 
HETATM 3902 C C11  . OLC I 3 .   ? 6.783  29.548 33.343 1.00 53.86  ? 308 OLC A C11  1 
HETATM 3903 C C8   . OLC I 3 .   ? 7.321  28.709 29.761 1.00 50.39  ? 308 OLC A C8   1 
HETATM 3904 C C24  . OLC I 3 .   ? 4.959  32.782 19.375 1.00 67.74  ? 308 OLC A C24  1 
HETATM 3905 C C16  . OLC I 3 .   ? 6.262  30.931 39.539 1.00 53.41  ? 308 OLC A C16  1 
HETATM 3906 C C12  . OLC I 3 .   ? 7.217  29.622 34.821 1.00 48.33  ? 308 OLC A C12  1 
HETATM 3907 C C7   . OLC I 3 .   ? 6.877  30.150 29.392 1.00 52.42  ? 308 OLC A C7   1 
HETATM 3908 C C15  . OLC I 3 .   ? 5.878  31.131 38.052 1.00 47.64  ? 308 OLC A C15  1 
HETATM 3909 C C13  . OLC I 3 .   ? 6.105  30.272 35.683 1.00 49.60  ? 308 OLC A C13  1 
HETATM 3910 C C6   . OLC I 3 .   ? 6.416  30.079 27.905 1.00 56.70  ? 308 OLC A C6   1 
HETATM 3911 C C14  . OLC I 3 .   ? 6.387  29.966 37.177 1.00 51.18  ? 308 OLC A C14  1 
HETATM 3912 C C5   . OLC I 3 .   ? 5.735  31.383 27.404 1.00 56.12  ? 308 OLC A C5   1 
HETATM 3913 C C4   . OLC I 3 .   ? 4.538  30.980 26.490 1.00 59.04  ? 308 OLC A C4   1 
HETATM 3914 C C3   . OLC I 3 .   ? 4.436  31.870 25.222 1.00 57.47  ? 308 OLC A C3   1 
HETATM 3915 C C2   . OLC I 3 .   ? 3.768  31.020 24.106 1.00 61.92  ? 308 OLC A C2   1 
HETATM 3916 C C21  . OLC I 3 .   ? 2.868  32.765 20.840 1.00 63.03  ? 308 OLC A C21  1 
HETATM 3917 C C1   . OLC I 3 .   ? 3.099  31.912 23.043 1.00 57.80  ? 308 OLC A C1   1 
HETATM 3918 C C22  . OLC I 3 .   ? 3.422  32.689 19.401 1.00 67.78  ? 308 OLC A C22  1 
HETATM 3919 O O19  . OLC I 3 .   ? 2.089  32.477 23.297 1.00 72.75  ? 308 OLC A O19  1 
HETATM 3920 O O25  . OLC I 3 .   ? 5.367  34.129 19.208 1.00 72.13  ? 308 OLC A O25  1 
HETATM 3921 O O23  . OLC I 3 .   ? 3.045  31.480 18.808 1.00 70.36  ? 308 OLC A O23  1 
HETATM 3922 O O20  . OLC I 3 .   ? 3.679  32.043 21.762 1.00 54.79  ? 308 OLC A O20  1 
HETATM 3923 H H18  . OLC I 3 .   ? 5.913  32.957 42.332 0.00 68.05  ? 308 OLC A H18  1 
HETATM 3924 H H18A . OLC I 3 .   ? 5.826  31.182 42.316 0.00 68.05  ? 308 OLC A H18A 1 
HETATM 3925 H H18B . OLC I 3 .   ? 7.307  32.004 41.779 0.00 68.05  ? 308 OLC A H18B 1 
HETATM 3926 H H10  . OLC I 3 .   ? 7.320  27.828 33.034 0.00 64.94  ? 308 OLC A H10  1 
HETATM 3927 H H9   . OLC I 3 .   ? 6.766  28.833 31.187 0.00 67.44  ? 308 OLC A H9   1 
HETATM 3928 H H17  . OLC I 3 .   ? 4.591  32.010 40.387 0.00 60.95  ? 308 OLC A H17  1 
HETATM 3929 H H17A . OLC I 3 .   ? 5.955  33.041 39.900 0.00 60.95  ? 308 OLC A H17A 1 
HETATM 3930 H H11  . OLC I 3 .   ? 6.757  30.554 32.921 0.00 64.63  ? 308 OLC A H11  1 
HETATM 3931 H H11A . OLC I 3 .   ? 5.789  29.101 33.278 0.00 64.63  ? 308 OLC A H11A 1 
HETATM 3932 H H8   . OLC I 3 .   ? 6.472  28.045 29.598 0.00 60.46  ? 308 OLC A H8   1 
HETATM 3933 H H8A  . OLC I 3 .   ? 8.136  28.428 29.095 0.00 60.46  ? 308 OLC A H8A  1 
HETATM 3934 H H24  . OLC I 3 .   ? 5.340  32.186 18.547 0.00 81.29  ? 308 OLC A H24  1 
HETATM 3935 H H24A . OLC I 3 .   ? 5.358  32.399 20.313 0.00 81.29  ? 308 OLC A H24A 1 
HETATM 3936 H H16  . OLC I 3 .   ? 7.348  30.920 39.639 0.00 64.09  ? 308 OLC A H16  1 
HETATM 3937 H H16A . OLC I 3 .   ? 5.855  29.986 39.899 0.00 64.09  ? 308 OLC A H16A 1 
HETATM 3938 H H12  . OLC I 3 .   ? 7.412  28.615 35.187 0.00 58.00  ? 308 OLC A H12  1 
HETATM 3939 H H12A . OLC I 3 .   ? 8.125  30.218 34.898 0.00 58.00  ? 308 OLC A H12A 1 
HETATM 3940 H H7   . OLC I 3 .   ? 6.054  30.470 30.031 0.00 62.91  ? 308 OLC A H7   1 
HETATM 3941 H H7A  . OLC I 3 .   ? 7.711  30.844 29.499 0.00 62.91  ? 308 OLC A H7A  1 
HETATM 3942 H H15  . OLC I 3 .   ? 6.318  32.061 37.694 0.00 57.16  ? 308 OLC A H15  1 
HETATM 3943 H H15A . OLC I 3 .   ? 4.794  31.187 37.970 0.00 57.16  ? 308 OLC A H15A 1 
HETATM 3944 H H13  . OLC I 3 .   ? 5.136  29.861 35.402 0.00 59.52  ? 308 OLC A H13  1 
HETATM 3945 H H13A . OLC I 3 .   ? 6.101  31.349 35.525 0.00 59.52  ? 308 OLC A H13A 1 
HETATM 3946 H H6   . OLC I 3 .   ? 7.289  29.884 27.282 0.00 68.04  ? 308 OLC A H6   1 
HETATM 3947 H H6A  . OLC I 3 .   ? 5.707  29.258 27.802 0.00 68.04  ? 308 OLC A H6A  1 
HETATM 3948 H H14  . OLC I 3 .   ? 5.874  29.048 37.462 0.00 61.42  ? 308 OLC A H14  1 
HETATM 3949 H H14A . OLC I 3 .   ? 7.460  29.844 37.326 0.00 61.42  ? 308 OLC A H14A 1 
HETATM 3950 H H5   . OLC I 3 .   ? 5.373  31.961 28.255 0.00 67.34  ? 308 OLC A H5   1 
HETATM 3951 H H5A  . OLC I 3 .   ? 6.450  31.980 26.837 0.00 67.34  ? 308 OLC A H5A  1 
HETATM 3952 H H4   . OLC I 3 .   ? 4.668  29.943 26.180 0.00 70.85  ? 308 OLC A H4   1 
HETATM 3953 H H4A  . OLC I 3 .   ? 3.614  31.076 27.060 0.00 70.85  ? 308 OLC A H4A  1 
HETATM 3954 H H3   . OLC I 3 .   ? 3.829  32.751 25.433 0.00 68.96  ? 308 OLC A H3   1 
HETATM 3955 H H3A  . OLC I 3 .   ? 5.432  32.183 24.906 0.00 68.96  ? 308 OLC A H3A  1 
HETATM 3956 H H2   . OLC I 3 .   ? 4.528  30.406 23.626 0.00 74.31  ? 308 OLC A H2   1 
HETATM 3957 H H2A  . OLC I 3 .   ? 3.013  30.377 24.555 0.00 74.31  ? 308 OLC A H2A  1 
HETATM 3958 H H21  . OLC I 3 .   ? 2.830  33.810 21.148 0.00 75.64  ? 308 OLC A H21  1 
HETATM 3959 H H21A . OLC I 3 .   ? 1.862  32.346 20.853 0.00 75.64  ? 308 OLC A H21A 1 
HETATM 3960 H H22  . OLC I 3 .   ? 3.008  33.535 18.851 0.00 81.33  ? 308 OLC A H22  1 
HETATM 3961 H HO25 . OLC I 3 .   ? 5.879  34.204 18.417 0.00 86.55  ? 308 OLC A HO25 1 
HETATM 3962 H HO23 . OLC I 3 .   ? 2.519  30.978 19.421 0.00 84.44  ? 308 OLC A HO23 1 
HETATM 3963 C C18  . OLC J 3 .   ? 34.276 35.811 35.643 1.00 57.68  ? 309 OLC A C18  1 
HETATM 3964 C C10  . OLC J 3 .   ? 32.506 39.852 28.103 1.00 66.43  ? 309 OLC A C10  1 
HETATM 3965 C C9   . OLC J 3 .   ? 32.855 40.929 27.394 1.00 65.89  ? 309 OLC A C9   1 
HETATM 3966 C C17  . OLC J 3 .   ? 35.537 35.459 34.817 1.00 67.00  ? 309 OLC A C17  1 
HETATM 3967 C C11  . OLC J 3 .   ? 32.638 39.613 29.628 1.00 64.38  ? 309 OLC A C11  1 
HETATM 3968 C C8   . OLC J 3 .   ? 33.018 41.736 26.065 1.00 55.40  ? 309 OLC A C8   1 
HETATM 3969 C C24  . OLC J 3 .   ? 35.494 45.477 14.847 1.00 76.29  ? 309 OLC A C24  1 
HETATM 3970 C C16  . OLC J 3 .   ? 35.255 35.597 33.298 1.00 63.65  ? 309 OLC A C16  1 
HETATM 3971 C C12  . OLC J 3 .   ? 34.059 39.002 29.832 1.00 64.58  ? 309 OLC A C12  1 
HETATM 3972 C C7   . OLC J 3 .   ? 34.088 41.028 25.139 1.00 57.38  ? 309 OLC A C7   1 
HETATM 3973 C C15  . OLC J 3 .   ? 35.656 37.011 32.794 1.00 50.33  ? 309 OLC A C15  1 
HETATM 3974 C C13  . OLC J 3 .   ? 34.315 38.627 31.326 1.00 69.98  ? 309 OLC A C13  1 
HETATM 3975 C C6   . OLC J 3 .   ? 33.370 40.699 23.820 1.00 62.65  ? 309 OLC A C6   1 
HETATM 3976 C C14  . OLC J 3 .   ? 34.996 37.220 31.396 1.00 60.41  ? 309 OLC A C14  1 
HETATM 3977 C C5   . OLC J 3 .   ? 34.425 40.284 22.776 1.00 50.12  ? 309 OLC A C5   1 
HETATM 3978 C C4   . OLC J 3 .   ? 34.818 41.549 21.961 1.00 50.78  ? 309 OLC A C4   1 
HETATM 3979 C C3   . OLC J 3 .   ? 34.472 41.377 20.456 1.00 49.83  ? 309 OLC A C3   1 
HETATM 3980 C C2   . OLC J 3 .   ? 34.197 42.772 19.828 1.00 70.60  ? 309 OLC A C2   1 
HETATM 3981 C C21  . OLC J 3 .   ? 35.499 43.539 16.378 1.00 66.58  ? 309 OLC A C21  1 
HETATM 3982 C C1   . OLC J 3 .   ? 35.010 42.897 18.520 1.00 71.08  ? 309 OLC A C1   1 
HETATM 3983 C C22  . OLC J 3 .   ? 34.999 44.035 15.025 1.00 81.15  ? 309 OLC A C22  1 
HETATM 3984 O O19  . OLC J 3 .   ? 36.175 42.648 18.542 1.00 74.72  ? 309 OLC A O19  1 
HETATM 3985 O O25  . OLC J 3 .   ? 35.040 46.248 15.939 1.00 71.27  ? 309 OLC A O25  1 
HETATM 3986 O O23  . OLC J 3 .   ? 35.528 43.198 14.037 1.00 82.22  ? 309 OLC A O23  1 
HETATM 3987 O O20  . OLC J 3 .   ? 34.446 43.334 17.301 1.00 74.67  ? 309 OLC A O20  1 
HETATM 3988 H H18  . OLC J 3 .   ? 34.473 35.632 36.698 0.00 69.21  ? 309 OLC A H18  1 
HETATM 3989 H H18A . OLC J 3 .   ? 34.025 36.859 35.494 0.00 69.21  ? 309 OLC A H18A 1 
HETATM 3990 H H18B . OLC J 3 .   ? 33.445 35.189 35.318 0.00 69.21  ? 309 OLC A H18B 1 
HETATM 3991 H H10  . OLC J 3 .   ? 33.270 39.086 27.995 0.00 79.71  ? 309 OLC A H10  1 
HETATM 3992 H H9   . OLC J 3 .   ? 32.227 40.529 26.602 0.00 79.07  ? 309 OLC A H9   1 
HETATM 3993 H H17  . OLC J 3 .   ? 36.345 36.135 35.094 0.00 80.40  ? 309 OLC A H17  1 
HETATM 3994 H H17A . OLC J 3 .   ? 35.832 34.434 35.034 0.00 80.40  ? 309 OLC A H17A 1 
HETATM 3995 H H11  . OLC J 3 .   ? 32.546 40.555 30.171 0.00 77.25  ? 309 OLC A H11  1 
HETATM 3996 H H11A . OLC J 3 .   ? 31.871 38.918 29.973 0.00 77.25  ? 309 OLC A H11A 1 
HETATM 3997 H H8   . OLC J 3 .   ? 33.351 42.748 26.294 0.00 66.48  ? 309 OLC A H8   1 
HETATM 3998 H H8A  . OLC J 3 .   ? 32.061 41.777 25.546 0.00 66.48  ? 309 OLC A H8A  1 
HETATM 3999 H H24  . OLC J 3 .   ? 35.099 45.888 13.919 0.00 91.55  ? 309 OLC A H24  1 
HETATM 4000 H H24A . OLC J 3 .   ? 36.582 45.490 14.815 0.00 91.55  ? 309 OLC A H24A 1 
HETATM 4001 H H16  . OLC J 3 .   ? 35.832 34.847 32.757 0.00 76.39  ? 309 OLC A H16  1 
HETATM 4002 H H16A . OLC J 3 .   ? 34.192 35.440 33.115 0.00 76.39  ? 309 OLC A H16A 1 
HETATM 4003 H H12  . OLC J 3 .   ? 34.148 38.105 29.222 0.00 77.50  ? 309 OLC A H12  1 
HETATM 4004 H H12A . OLC J 3 .   ? 34.805 39.731 29.518 0.00 77.50  ? 309 OLC A H12A 1 
HETATM 4005 H H7   . OLC J 3 .   ? 34.928 41.698 24.955 0.00 68.86  ? 309 OLC A H7   1 
HETATM 4006 H H7A  . OLC J 3 .   ? 34.448 40.114 25.611 0.00 68.86  ? 309 OLC A H7A  1 
HETATM 4007 H H15  . OLC J 3 .   ? 36.739 37.080 32.706 0.00 60.39  ? 309 OLC A H15  1 
HETATM 4008 H H15A . OLC J 3 .   ? 35.299 37.768 33.490 0.00 60.39  ? 309 OLC A H15A 1 
HETATM 4009 H H13  . OLC J 3 .   ? 33.368 38.600 31.862 0.00 83.98  ? 309 OLC A H13  1 
HETATM 4010 H H13A . OLC J 3 .   ? 34.969 39.370 31.781 0.00 83.98  ? 309 OLC A H13A 1 
HETATM 4011 H H6   . OLC J 3 .   ? 32.668 39.880 23.978 0.00 75.18  ? 309 OLC A H6   1 
HETATM 4012 H H6A  . OLC J 3 .   ? 32.830 41.577 23.466 0.00 75.18  ? 309 OLC A H6A  1 
HETATM 4013 H H14  . OLC J 3 .   ? 34.244 36.448 31.234 0.00 72.49  ? 309 OLC A H14  1 
HETATM 4014 H H14A . OLC J 3 .   ? 35.760 37.150 30.622 0.00 72.49  ? 309 OLC A H14A 1 
HETATM 4015 H H5   . OLC J 3 .   ? 34.008 39.529 22.109 0.00 60.15  ? 309 OLC A H5   1 
HETATM 4016 H H5A  . OLC J 3 .   ? 35.303 39.879 23.279 0.00 60.15  ? 309 OLC A H5A  1 
HETATM 4017 H H4   . OLC J 3 .   ? 34.276 42.408 22.355 0.00 60.94  ? 309 OLC A H4   1 
HETATM 4018 H H4A  . OLC J 3 .   ? 35.890 41.718 22.062 0.00 60.94  ? 309 OLC A H4A  1 
HETATM 4019 H H3   . OLC J 3 .   ? 35.309 40.905 19.942 0.00 59.80  ? 309 OLC A H3   1 
HETATM 4020 H H3A  . OLC J 3 .   ? 33.584 40.752 20.356 0.00 59.80  ? 309 OLC A H3A  1 
HETATM 4021 H H2   . OLC J 3 .   ? 33.135 42.873 19.610 0.00 84.72  ? 309 OLC A H2   1 
HETATM 4022 H H2A  . OLC J 3 .   ? 34.501 43.553 20.523 0.00 84.72  ? 309 OLC A H2A  1 
HETATM 4023 H H21  . OLC J 3 .   ? 36.025 42.595 16.232 0.00 79.89  ? 309 OLC A H21  1 
HETATM 4024 H H21A . OLC J 3 .   ? 36.186 44.277 16.789 0.00 79.89  ? 309 OLC A H21A 1 
HETATM 4025 H H22  . OLC J 3 .   ? 33.912 44.019 14.957 0.00 97.38  ? 309 OLC A H22  1 
HETATM 4026 H HO25 . OLC J 3 .   ? 34.157 45.993 16.158 0.00 85.52  ? 309 OLC A HO25 1 
HETATM 4027 H HO23 . OLC J 3 .   ? 36.470 43.297 14.007 0.00 98.67  ? 309 OLC A HO23 1 
HETATM 4028 C C18  . OLC K 3 .   ? 3.575  38.525 36.418 1.00 57.69  ? 310 OLC A C18  1 
HETATM 4029 C C10  . OLC K 3 .   ? 4.819  37.764 43.333 1.00 78.71  ? 310 OLC A C10  1 
HETATM 4030 C C9   . OLC K 3 .   ? 4.462  38.663 44.282 1.00 81.50  ? 310 OLC A C9   1 
HETATM 4031 C C17  . OLC K 3 .   ? 4.271  39.435 37.438 1.00 63.00  ? 310 OLC A C17  1 
HETATM 4032 C C11  . OLC K 3 .   ? 6.133  36.993 43.095 1.00 61.83  ? 310 OLC A C11  1 
HETATM 4033 C C8   . OLC K 3 .   ? 4.591  39.571 45.530 1.00 73.03  ? 310 OLC A C8   1 
HETATM 4034 C C24  . OLC K 3 .   ? 4.520  36.164 56.275 1.00 93.51  ? 310 OLC A C24  1 
HETATM 4035 C C16  . OLC K 3 .   ? 3.711  39.146 38.852 1.00 63.05  ? 310 OLC A C16  1 
HETATM 4036 C C12  . OLC K 3 .   ? 6.467  37.008 41.569 1.00 59.77  ? 310 OLC A C12  1 
HETATM 4037 C C7   . OLC K 3 .   ? 3.190  39.733 46.179 1.00 64.57  ? 310 OLC A C7   1 
HETATM 4038 C C15  . OLC K 3 .   ? 3.789  37.637 39.256 1.00 71.91  ? 310 OLC A C15  1 
HETATM 4039 C C13  . OLC K 3 .   ? 5.495  36.251 40.611 1.00 56.36  ? 310 OLC A C13  1 
HETATM 4040 C C6   . OLC K 3 .   ? 3.286  39.990 47.717 1.00 64.11  ? 310 OLC A C6   1 
HETATM 4041 C C14  . OLC K 3 .   ? 5.247  37.085 39.311 1.00 56.63  ? 310 OLC A C14  1 
HETATM 4042 C C5   . OLC K 3 .   ? 3.892  38.782 48.487 1.00 68.74  ? 310 OLC A C5   1 
HETATM 4043 C C4   . OLC K 3 .   ? 4.758  39.300 49.676 1.00 70.05  ? 310 OLC A C4   1 
HETATM 4044 C C3   . OLC K 3 .   ? 4.429  38.526 50.990 1.00 79.49  ? 310 OLC A C3   1 
HETATM 4045 C C2   . OLC K 3 .   ? 5.704  38.391 51.877 1.00 83.70  ? 310 OLC A C2   1 
HETATM 4046 C C21  . OLC K 3 .   ? 3.814  37.406 54.200 1.00 99.13  ? 310 OLC A C21  1 
HETATM 4047 C C1   . OLC K 3 .   ? 5.447  38.864 53.333 1.00 86.46  ? 310 OLC A C1   1 
HETATM 4048 C C22  . OLC K 3 .   ? 3.706  36.081 54.969 1.00 102.11 ? 310 OLC A C22  1 
HETATM 4049 O O19  . OLC K 3 .   ? 5.524  40.009 53.643 1.00 83.99  ? 310 OLC A O19  1 
HETATM 4050 O O25  . OLC K 3 .   ? 4.722  34.868 56.797 1.00 90.65  ? 310 OLC A O25  1 
HETATM 4051 O O23  . OLC K 3 .   ? 2.350  35.823 55.226 1.00 107.12 ? 310 OLC A O23  1 
HETATM 4052 O O20  . OLC K 3 .   ? 5.128  37.919 54.325 1.00 98.14  ? 310 OLC A O20  1 
HETATM 4053 H H18  . OLC K 3 .   ? 3.936  37.506 36.536 0.00 69.23  ? 310 OLC A H18  1 
HETATM 4054 H H18A . OLC K 3 .   ? 2.500  38.551 36.584 0.00 69.23  ? 310 OLC A H18A 1 
HETATM 4055 H H18B . OLC K 3 .   ? 3.795  38.874 35.411 0.00 69.23  ? 310 OLC A H18B 1 
HETATM 4056 H H10  . OLC K 3 .   ? 5.083  38.298 42.424 0.00 94.45  ? 310 OLC A H10  1 
HETATM 4057 H H9   . OLC K 3 .   ? 5.504  38.895 44.487 0.00 97.80  ? 310 OLC A H9   1 
HETATM 4058 H H17  . OLC K 3 .   ? 4.088  40.477 37.181 0.00 75.60  ? 310 OLC A H17  1 
HETATM 4059 H H17A . OLC K 3 .   ? 5.343  39.242 37.425 0.00 75.60  ? 310 OLC A H17A 1 
HETATM 4060 H H11  . OLC K 3 .   ? 6.942  37.469 43.651 0.00 74.20  ? 310 OLC A H11  1 
HETATM 4061 H H11A . OLC K 3 .   ? 6.017  35.962 43.433 0.00 74.20  ? 310 OLC A H11A 1 
HETATM 4062 H H8   . OLC K 3 .   ? 4.973  40.548 45.233 0.00 87.64  ? 310 OLC A H8   1 
HETATM 4063 H H8A  . OLC K 3 .   ? 5.276  39.116 46.245 0.00 87.64  ? 310 OLC A H8A  1 
HETATM 4064 H H24  . OLC K 3 .   ? 3.977  36.766 57.002 0.00 112.22 ? 310 OLC A H24  1 
HETATM 4065 H H24A . OLC K 3 .   ? 5.485  36.625 56.071 0.00 112.22 ? 310 OLC A H24A 1 
HETATM 4066 H H16  . OLC K 3 .   ? 4.282  39.727 39.576 0.00 75.66  ? 310 OLC A H16  1 
HETATM 4067 H H16A . OLC K 3 .   ? 2.667  39.457 38.880 0.00 75.66  ? 310 OLC A H16A 1 
HETATM 4068 H H12  . OLC K 3 .   ? 6.494  38.050 41.252 0.00 71.73  ? 310 OLC A H12  1 
HETATM 4069 H H12A . OLC K 3 .   ? 7.456  36.567 41.448 0.00 71.73  ? 310 OLC A H12A 1 
HETATM 4070 H H7   . OLC K 3 .   ? 2.681  40.577 45.712 0.00 77.49  ? 310 OLC A H7   1 
HETATM 4071 H H7A  . OLC K 3 .   ? 2.616  38.823 46.009 0.00 77.49  ? 310 OLC A H7A  1 
HETATM 4072 H H15  . OLC K 3 .   ? 3.227  37.055 38.527 0.00 86.29  ? 310 OLC A H15  1 
HETATM 4073 H H15A . OLC K 3 .   ? 3.338  37.519 40.240 0.00 86.29  ? 310 OLC A H15A 1 
HETATM 4074 H H13  . OLC K 3 .   ? 4.546  36.088 41.118 0.00 67.63  ? 310 OLC A H13  1 
HETATM 4075 H H13A . OLC K 3 .   ? 5.932  35.290 40.342 0.00 67.63  ? 310 OLC A H13A 1 
HETATM 4076 H H6   . OLC K 3 .   ? 3.915  40.864 47.887 0.00 76.93  ? 310 OLC A H6   1 
HETATM 4077 H H6A  . OLC K 3 .   ? 2.285  40.183 48.102 0.00 76.93  ? 310 OLC A H6A  1 
HETATM 4078 H H14  . OLC K 3 .   ? 5.944  37.922 39.289 0.00 67.96  ? 310 OLC A H14  1 
HETATM 4079 H H14A . OLC K 3 .   ? 5.418  36.448 38.443 0.00 67.96  ? 310 OLC A H14A 1 
HETATM 4080 H H5   . OLC K 3 .   ? 3.087  38.156 48.870 0.00 82.49  ? 310 OLC A H5   1 
HETATM 4081 H H5A  . OLC K 3 .   ? 4.516  38.198 47.811 0.00 82.49  ? 310 OLC A H5A  1 
HETATM 4082 H H4   . OLC K 3 .   ? 5.812  39.161 49.436 0.00 84.07  ? 310 OLC A H4   1 
HETATM 4083 H H4A  . OLC K 3 .   ? 4.557  40.361 49.828 0.00 84.07  ? 310 OLC A H4A  1 
HETATM 4084 H H3   . OLC K 3 .   ? 3.662  39.069 51.544 0.00 95.39  ? 310 OLC A H3   1 
HETATM 4085 H H3A  . OLC K 3 .   ? 4.059  37.532 50.738 0.00 95.39  ? 310 OLC A H3A  1 
HETATM 4086 H H2   . OLC K 3 .   ? 6.012  37.347 51.895 0.00 100.44 ? 310 OLC A H2   1 
HETATM 4087 H H2A  . OLC K 3 .   ? 6.500  38.996 51.445 0.00 100.44 ? 310 OLC A H2A  1 
HETATM 4088 H H21  . OLC K 3 .   ? 3.590  37.233 53.147 0.00 118.96 ? 310 OLC A H21  1 
HETATM 4089 H H21A . OLC K 3 .   ? 3.103  38.123 54.610 0.00 118.96 ? 310 OLC A H21A 1 
HETATM 4090 H H22  . OLC K 3 .   ? 4.117  35.263 54.379 0.00 122.54 ? 310 OLC A H22  1 
HETATM 4091 H HO25 . OLC K 3 .   ? 3.904  34.394 56.785 0.00 108.79 ? 310 OLC A HO25 1 
HETATM 4092 H HO23 . OLC K 3 .   ? 2.167  36.007 56.139 0.00 128.55 ? 310 OLC A HO23 1 
HETATM 4093 C C18  . OLC L 3 .   ? 21.871 54.812 37.381 1.00 59.07  ? 311 OLC A C18  1 
HETATM 4094 C C10  . OLC L 3 .   ? 23.024 56.648 29.391 1.00 64.00  ? 311 OLC A C10  1 
HETATM 4095 C C9   . OLC L 3 .   ? 23.252 57.137 28.167 1.00 70.66  ? 311 OLC A C9   1 
HETATM 4096 C C17  . OLC L 3 .   ? 22.366 53.547 36.639 1.00 55.44  ? 311 OLC A C17  1 
HETATM 4097 C C11  . OLC L 3 .   ? 21.810 55.832 29.847 1.00 56.83  ? 311 OLC A C11  1 
HETATM 4098 C C8   . OLC L 3 .   ? 22.901 57.378 26.691 1.00 74.78  ? 311 OLC A C8   1 
HETATM 4099 C C24  . OLC L 3 .   ? 28.320 55.813 15.680 1.00 88.05  ? 311 OLC A C24  1 
HETATM 4100 C C16  . OLC L 3 .   ? 21.457 53.197 35.424 1.00 53.12  ? 311 OLC A C16  1 
HETATM 4101 C C12  . OLC L 3 .   ? 22.077 55.325 31.300 1.00 62.92  ? 311 OLC A C12  1 
HETATM 4102 C C7   . OLC L 3 .   ? 24.160 57.583 25.794 1.00 73.77  ? 311 OLC A C7   1 
HETATM 4103 C C15  . OLC L 3 .   ? 21.528 54.269 34.311 1.00 61.44  ? 311 OLC A C15  1 
HETATM 4104 C C13  . OLC L 3 .   ? 20.784 54.741 31.935 1.00 60.87  ? 311 OLC A C13  1 
HETATM 4105 C C6   . OLC L 3 .   ? 23.593 57.733 24.348 1.00 75.59  ? 311 OLC A C6   1 
HETATM 4106 C C14  . OLC L 3 .   ? 21.139 53.616 32.951 1.00 52.32  ? 311 OLC A C14  1 
HETATM 4107 C C5   . OLC L 3 .   ? 24.575 57.254 23.246 1.00 79.53  ? 311 OLC A C5   1 
HETATM 4108 C C4   . OLC L 3 .   ? 23.748 56.701 22.033 1.00 70.55  ? 311 OLC A C4   1 
HETATM 4109 C C3   . OLC L 3 .   ? 24.180 57.387 20.701 1.00 83.36  ? 311 OLC A C3   1 
HETATM 4110 C C2   . OLC L 3 .   ? 24.072 56.350 19.555 1.00 82.34  ? 311 OLC A C2   1 
HETATM 4111 C C21  . OLC L 3 .   ? 26.027 56.289 16.631 1.00 93.89  ? 311 OLC A C21  1 
HETATM 4112 C C1   . OLC L 3 .   ? 24.360 56.972 18.168 1.00 78.43  ? 311 OLC A C1   1 
HETATM 4113 C C22  . OLC L 3 .   ? 27.357 55.534 16.843 1.00 89.00  ? 311 OLC A C22  1 
HETATM 4114 O O19  . OLC L 3 .   ? 23.485 57.316 17.435 1.00 77.17  ? 311 OLC A O19  1 
HETATM 4115 O O25  . OLC L 3 .   ? 29.342 54.839 15.668 1.00 95.10  ? 311 OLC A O25  1 
HETATM 4116 O O23  . OLC L 3 .   ? 27.947 55.923 18.054 1.00 86.24  ? 311 OLC A O23  1 
HETATM 4117 O O20  . OLC L 3 .   ? 25.709 57.077 17.769 1.00 84.03  ? 311 OLC A O20  1 
HETATM 4118 H H18  . OLC L 3 .   ? 22.483 54.977 38.265 0.00 70.89  ? 311 OLC A H18  1 
HETATM 4119 H H18A . OLC L 3 .   ? 21.948 55.674 36.720 0.00 70.89  ? 311 OLC A H18A 1 
HETATM 4120 H H18B . OLC L 3 .   ? 20.833 54.676 37.678 0.00 70.89  ? 311 OLC A H18B 1 
HETATM 4121 H H10  . OLC L 3 .   ? 23.606 55.741 29.536 0.00 76.80  ? 311 OLC A H10  1 
HETATM 4122 H H9   . OLC L 3 .   ? 22.514 56.423 27.810 0.00 84.80  ? 311 OLC A H9   1 
HETATM 4123 H H17  . OLC L 3 .   ? 22.365 52.708 37.333 0.00 66.53  ? 311 OLC A H17  1 
HETATM 4124 H H17A . OLC L 3 .   ? 23.380 53.721 36.282 0.00 66.53  ? 311 OLC A H17A 1 
HETATM 4125 H H11  . OLC L 3 .   ? 21.666 54.980 29.180 0.00 68.19  ? 311 OLC A H11  1 
HETATM 4126 H H11A . OLC L 3 .   ? 20.918 56.459 29.833 0.00 68.19  ? 311 OLC A H11A 1 
HETATM 4127 H H8   . OLC L 3 .   ? 22.276 58.269 26.623 0.00 89.73  ? 311 OLC A H8   1 
HETATM 4128 H H8A  . OLC L 3 .   ? 22.346 56.516 26.320 0.00 89.73  ? 311 OLC A H8A  1 
HETATM 4129 H H24  . OLC L 3 .   ? 28.762 56.801 15.804 0.00 105.67 ? 311 OLC A H24  1 
HETATM 4130 H H24A . OLC L 3 .   ? 27.773 55.776 14.739 0.00 105.67 ? 311 OLC A H24A 1 
HETATM 4131 H H16  . OLC L 3 .   ? 20.427 53.118 35.770 0.00 63.75  ? 311 OLC A H16  1 
HETATM 4132 H H16A . OLC L 3 .   ? 21.777 52.241 35.011 0.00 63.75  ? 311 OLC A H16A 1 
HETATM 4133 H H12  . OLC L 3 .   ? 22.841 54.550 31.272 0.00 75.50  ? 311 OLC A H12  1 
HETATM 4134 H H12A . OLC L 3 .   ? 22.427 56.158 31.908 0.00 75.50  ? 311 OLC A H12A 1 
HETATM 4135 H H7   . OLC L 3 .   ? 24.701 58.482 26.090 0.00 88.52  ? 311 OLC A H7   1 
HETATM 4136 H H7A  . OLC L 3 .   ? 24.823 56.721 25.860 0.00 88.52  ? 311 OLC A H7A  1 
HETATM 4137 H H15  . OLC L 3 .   ? 22.540 54.665 34.249 0.00 73.73  ? 311 OLC A H15  1 
HETATM 4138 H H15A . OLC L 3 .   ? 20.835 55.077 34.539 0.00 73.73  ? 311 OLC A H15A 1 
HETATM 4139 H H13  . OLC L 3 .   ? 20.153 54.328 31.149 0.00 73.05  ? 311 OLC A H13  1 
HETATM 4140 H H13A . OLC L 3 .   ? 20.247 55.535 32.452 0.00 73.05  ? 311 OLC A H13A 1 
HETATM 4141 H H6   . OLC L 3 .   ? 22.678 57.146 24.274 0.00 90.71  ? 311 OLC A H6   1 
HETATM 4142 H H6A  . OLC L 3 .   ? 23.365 58.784 24.174 0.00 90.71  ? 311 OLC A H6A  1 
HETATM 4143 H H14  . OLC L 3 .   ? 20.277 52.964 33.091 0.00 62.78  ? 311 OLC A H14  1 
HETATM 4144 H H14A . OLC L 3 .   ? 21.978 53.032 32.572 0.00 62.78  ? 311 OLC A H14A 1 
HETATM 4145 H H5   . OLC L 3 .   ? 25.214 56.465 23.643 0.00 95.44  ? 311 OLC A H5   1 
HETATM 4146 H H5A  . OLC L 3 .   ? 25.192 58.090 22.917 0.00 95.44  ? 311 OLC A H5A  1 
HETATM 4147 H H4   . OLC L 3 .   ? 23.912 55.626 21.950 0.00 84.66  ? 311 OLC A H4   1 
HETATM 4148 H H4A  . OLC L 3 .   ? 22.689 56.893 22.207 0.00 84.66  ? 311 OLC A H4A  1 
HETATM 4149 H H3   . OLC L 3 .   ? 23.524 58.233 20.494 0.00 100.04 ? 311 OLC A H3   1 
HETATM 4150 H H3A  . OLC L 3 .   ? 25.208 57.738 20.785 0.00 100.04 ? 311 OLC A H3A  1 
HETATM 4151 H H2   . OLC L 3 .   ? 24.791 55.552 19.737 0.00 98.80  ? 311 OLC A H2   1 
HETATM 4152 H H2A  . OLC L 3 .   ? 23.065 55.936 19.551 0.00 98.80  ? 311 OLC A H2A  1 
HETATM 4153 H H21  . OLC L 3 .   ? 26.119 56.938 15.760 0.00 112.67 ? 311 OLC A H21  1 
HETATM 4154 H H21A . OLC L 3 .   ? 25.229 55.566 16.462 0.00 112.67 ? 311 OLC A H21A 1 
HETATM 4155 H H22  . OLC L 3 .   ? 27.148 54.465 16.878 0.00 106.80 ? 311 OLC A H22  1 
HETATM 4156 H HO25 . OLC L 3 .   ? 29.072 54.086 16.171 0.00 114.12 ? 311 OLC A HO25 1 
HETATM 4157 H HO23 . OLC L 3 .   ? 27.457 56.646 18.425 0.00 103.48 ? 311 OLC A HO23 1 
HETATM 4158 C C45  . LI1 M 2 .   ? 30.902 33.635 46.485 1.00 80.39  ? 312 LI1 A C45  1 
HETATM 4159 C C46  . LI1 M 2 .   ? 30.359 33.513 45.064 1.00 64.29  ? 312 LI1 A C46  1 
HETATM 4160 C C47  . LI1 M 2 .   ? 31.457 33.373 44.017 1.00 76.12  ? 312 LI1 A C47  1 
HETATM 4161 C C48  . LI1 M 2 .   ? 31.717 34.616 43.168 1.00 70.43  ? 312 LI1 A C48  1 
HETATM 4162 C C50  . LI1 M 2 .   ? 30.786 34.632 41.953 1.00 67.68  ? 312 LI1 A C50  1 
HETATM 4163 C C51  . LI1 M 2 .   ? 29.522 35.472 42.127 1.00 57.86  ? 312 LI1 A C51  1 
HETATM 4164 C C52  . LI1 M 2 .   ? 29.727 36.964 41.884 1.00 61.52  ? 312 LI1 A C52  1 
HETATM 4165 C C53  . LI1 M 2 .   ? 28.602 37.632 41.108 1.00 47.95  ? 312 LI1 A C53  1 
HETATM 4166 C C55  . LI1 M 2 .   ? 29.038 38.218 39.776 1.00 58.85  ? 312 LI1 A C55  1 
HETATM 4167 C C56  . LI1 M 2 .   ? 30.122 39.273 39.882 1.00 65.19  ? 312 LI1 A C56  1 
HETATM 4168 H H451 . LI1 M 2 .   ? 30.173 33.819 47.100 1.00 96.47  ? 312 LI1 A H451 1 
HETATM 4169 H H452 . LI1 M 2 .   ? 31.495 34.402 46.523 1.00 96.47  ? 312 LI1 A H452 1 
HETATM 4170 H H461 . LI1 M 2 .   ? 29.773 32.741 45.025 1.00 77.15  ? 312 LI1 A H461 1 
HETATM 4171 H H462 . LI1 M 2 .   ? 29.826 34.300 44.871 1.00 77.15  ? 312 LI1 A H462 1 
HETATM 4172 H H471 . LI1 M 2 .   ? 31.221 32.632 43.436 1.00 91.35  ? 312 LI1 A H471 1 
HETATM 4173 H H472 . LI1 M 2 .   ? 32.274 33.120 44.475 1.00 91.35  ? 312 LI1 A H472 1 
HETATM 4174 C C45  . LI1 N 2 .   ? 30.739 27.451 46.240 1.00 77.53  ? 313 LI1 A C45  1 
HETATM 4175 C C46  . LI1 N 2 .   ? 30.613 26.121 45.491 1.00 72.64  ? 313 LI1 A C46  1 
HETATM 4176 C C47  . LI1 N 2 .   ? 30.818 26.241 43.979 1.00 71.92  ? 313 LI1 A C47  1 
HETATM 4177 C C48  . LI1 N 2 .   ? 29.721 25.600 43.115 1.00 64.15  ? 313 LI1 A C48  1 
HETATM 4178 C C50  . LI1 N 2 .   ? 29.687 26.204 41.710 1.00 67.36  ? 313 LI1 A C50  1 
HETATM 4179 C C51  . LI1 N 2 .   ? 28.301 26.267 41.068 1.00 64.80  ? 313 LI1 A C51  1 
HETATM 4180 C C52  . LI1 N 2 .   ? 28.272 25.938 39.579 1.00 69.61  ? 313 LI1 A C52  1 
HETATM 4181 C C53  . LI1 N 2 .   ? 27.971 27.133 38.677 1.00 73.55  ? 313 LI1 A C53  1 
HETATM 4182 C C55  . LI1 N 2 .   ? 28.350 28.485 39.280 1.00 66.31  ? 313 LI1 A C55  1 
HETATM 4183 C C56  . LI1 N 2 .   ? 28.641 29.598 38.262 1.00 62.14  ? 313 LI1 A C56  1 
HETATM 4184 C C57  . LI1 N 2 .   ? 29.048 30.938 38.914 1.00 49.34  ? 313 LI1 A C57  1 
HETATM 4185 C C58  . LI1 N 2 .   ? 29.091 32.153 37.999 1.00 56.19  ? 313 LI1 A C58  1 
HETATM 4186 C C59  . LI1 N 2 .   ? 29.642 33.377 38.714 1.00 58.72  ? 313 LI1 A C59  1 
HETATM 4187 H H451 . LI1 N 2 .   ? 30.001 28.033 45.996 1.00 93.03  ? 313 LI1 A H451 1 
HETATM 4188 H H452 . LI1 N 2 .   ? 31.551 27.898 45.951 1.00 93.03  ? 313 LI1 A H452 1 
HETATM 4189 H H461 . LI1 N 2 .   ? 29.732 25.756 45.668 1.00 87.16  ? 313 LI1 A H461 1 
HETATM 4190 H H462 . LI1 N 2 .   ? 31.268 25.505 45.856 1.00 87.16  ? 313 LI1 A H462 1 
HETATM 4191 H H471 . LI1 N 2 .   ? 31.674 25.840 43.761 1.00 86.31  ? 313 LI1 A H471 1 
HETATM 4192 H H472 . LI1 N 2 .   ? 30.888 27.184 43.762 1.00 86.31  ? 313 LI1 A H472 1 
HETATM 4193 C C50  . LI1 O 2 .   ? 29.082 24.943 24.495 1.00 57.86  ? 314 LI1 A C50  1 
HETATM 4194 C C51  . LI1 O 2 .   ? 28.148 23.758 24.670 1.00 55.79  ? 314 LI1 A C51  1 
HETATM 4195 C C52  . LI1 O 2 .   ? 27.892 23.417 26.126 1.00 51.47  ? 314 LI1 A C52  1 
HETATM 4196 C C53  . LI1 O 2 .   ? 29.133 22.919 26.852 1.00 62.13  ? 314 LI1 A C53  1 
HETATM 4197 C C55  . LI1 O 2 .   ? 29.115 23.195 28.353 1.00 73.32  ? 314 LI1 A C55  1 
HETATM 4198 C C56  . LI1 O 2 .   ? 30.450 23.660 28.932 1.00 72.28  ? 314 LI1 A C56  1 
HETATM 4199 C C57  . LI1 O 2 .   ? 30.404 23.933 30.434 1.00 66.18  ? 314 LI1 A C57  1 
HETATM 4200 C C58  . LI1 O 2 .   ? 31.639 24.608 31.006 1.00 65.03  ? 314 LI1 A C58  1 
HETATM 4201 C C46  . LI1 P 2 .   ? 30.378 32.985 33.718 1.00 61.10  ? 315 LI1 A C46  1 
HETATM 4202 C C47  . LI1 P 2 .   ? 30.228 33.553 32.305 1.00 54.45  ? 315 LI1 A C47  1 
HETATM 4203 C C48  . LI1 P 2 .   ? 31.351 33.194 31.321 1.00 68.56  ? 315 LI1 A C48  1 
HETATM 4204 C C50  . LI1 P 2 .   ? 31.332 31.714 30.927 1.00 72.20  ? 315 LI1 A C50  1 
HETATM 4205 C C51  . LI1 P 2 .   ? 32.624 30.947 31.216 1.00 83.04  ? 315 LI1 A C51  1 
HETATM 4206 C C52  . LI1 P 2 .   ? 32.753 29.621 30.472 1.00 81.32  ? 315 LI1 A C52  1 
HETATM 4207 C C53  . LI1 P 2 .   ? 33.879 28.723 30.977 1.00 73.41  ? 315 LI1 A C53  1 
HETATM 4208 C C55  . LI1 P 2 .   ? 33.814 27.297 30.452 1.00 72.45  ? 315 LI1 A C55  1 
HETATM 4209 C C56  . LI1 P 2 .   ? 33.921 27.182 28.933 1.00 70.48  ? 315 LI1 A C56  1 
HETATM 4210 C C57  . LI1 P 2 .   ? 33.477 25.824 28.387 1.00 70.84  ? 315 LI1 A C57  1 
HETATM 4211 C C58  . LI1 P 2 .   ? 34.165 25.356 27.113 1.00 66.88  ? 315 LI1 A C58  1 
HETATM 4212 C C59  . LI1 P 2 .   ? 34.467 26.509 26.180 1.00 65.22  ? 315 LI1 A C59  1 
HETATM 4213 C C60  . LI1 P 2 .   ? 33.362 24.288 26.393 1.00 69.67  ? 315 LI1 A C60  1 
HETATM 4214 C C45  . LI1 Q 2 .   ? 9.260  58.891 46.429 1.00 63.01  ? 316 LI1 A C45  1 
HETATM 4215 C C46  . LI1 Q 2 .   ? 9.832  58.195 45.208 1.00 70.08  ? 316 LI1 A C46  1 
HETATM 4216 C C47  . LI1 Q 2 .   ? 11.201 58.734 44.815 1.00 69.46  ? 316 LI1 A C47  1 
HETATM 4217 C C48  . LI1 Q 2 .   ? 11.294 59.321 43.407 1.00 70.76  ? 316 LI1 A C48  1 
HETATM 4218 C C50  . LI1 Q 2 .   ? 12.726 59.252 42.874 1.00 65.70  ? 316 LI1 A C50  1 
HETATM 4219 C C51  . LI1 Q 2 .   ? 13.047 58.029 42.013 1.00 59.80  ? 316 LI1 A C51  1 
HETATM 4220 C C52  . LI1 Q 2 .   ? 14.407 58.105 41.325 1.00 59.01  ? 316 LI1 A C52  1 
HETATM 4221 C C53  . LI1 Q 2 .   ? 15.595 57.799 42.243 1.00 68.89  ? 316 LI1 A C53  1 
HETATM 4222 C C55  . LI1 Q 2 .   ? 16.948 57.736 41.530 1.00 63.73  ? 316 LI1 A C55  1 
HETATM 4223 C C56  . LI1 Q 2 .   ? 17.663 56.398 41.672 1.00 58.85  ? 316 LI1 A C56  1 
HETATM 4224 C C57  . LI1 Q 2 .   ? 18.525 56.276 42.929 1.00 58.42  ? 316 LI1 A C57  1 
HETATM 4225 C C58  . LI1 Q 2 .   ? 19.599 55.197 42.886 1.00 55.98  ? 316 LI1 A C58  1 
HETATM 4226 C C59  . LI1 Q 2 .   ? 20.285 55.094 44.238 1.00 55.33  ? 316 LI1 A C59  1 
HETATM 4227 H H451 . LI1 Q 2 .   ? 9.909  58.880 47.148 1.00 75.62  ? 316 LI1 A H451 1 
HETATM 4228 H H452 . LI1 Q 2 .   ? 9.128  59.817 46.184 1.00 75.62  ? 316 LI1 A H452 1 
HETATM 4229 H H461 . LI1 Q 2 .   ? 9.213  58.309 44.470 1.00 84.10  ? 316 LI1 A H461 1 
HETATM 4230 H H462 . LI1 Q 2 .   ? 9.897  57.246 45.396 1.00 84.10  ? 316 LI1 A H462 1 
HETATM 4231 H H471 . LI1 Q 2 .   ? 11.842 58.011 44.904 1.00 83.35  ? 316 LI1 A H471 1 
HETATM 4232 H H472 . LI1 Q 2 .   ? 11.451 59.411 45.463 1.00 83.35  ? 316 LI1 A H472 1 
HETATM 4233 C C52  . LI1 R 2 .   ? 26.592 18.356 43.622 1.00 64.82  ? 317 LI1 A C52  1 
HETATM 4234 C C53  . LI1 R 2 .   ? 26.081 17.582 42.409 1.00 60.74  ? 317 LI1 A C53  1 
HETATM 4235 C C55  . LI1 R 2 .   ? 24.945 18.295 41.700 1.00 50.77  ? 317 LI1 A C55  1 
HETATM 4236 C C56  . LI1 R 2 .   ? 25.368 19.405 40.735 1.00 50.43  ? 317 LI1 A C56  1 
HETATM 4237 C C57  . LI1 R 2 .   ? 25.285 18.892 39.301 1.00 58.24  ? 317 LI1 A C57  1 
HETATM 4238 C C58  . LI1 R 2 .   ? 25.532 17.401 39.147 1.00 63.47  ? 317 LI1 A C58  1 
HETATM 4239 C C1   . RET S 4 .   ? 15.118 46.238 29.703 1.00 18.95  ? 318 RET A C1   1 
HETATM 4240 C C2   . RET S 4 .   ? 14.938 47.166 28.479 1.00 30.04  ? 318 RET A C2   1 
HETATM 4241 C C3   . RET S 4 .   ? 14.878 48.640 28.572 1.00 36.61  ? 318 RET A C3   1 
HETATM 4242 C C4   . RET S 4 .   ? 14.883 49.250 29.949 1.00 19.37  ? 318 RET A C4   1 
HETATM 4243 C C5   . RET S 4 .   ? 15.259 48.347 31.074 1.00 18.84  ? 318 RET A C5   1 
HETATM 4244 C C6   . RET S 4 .   ? 15.355 47.023 31.000 1.00 19.00  ? 318 RET A C6   1 
HETATM 4245 C C7   . RET S 4 .   ? 15.842 46.290 32.184 1.00 17.74  ? 318 RET A C7   1 
HETATM 4246 C C8   . RET S 4 .   ? 15.967 44.913 32.431 1.00 18.15  ? 318 RET A C8   1 
HETATM 4247 C C9   . RET S 4 .   ? 16.413 44.303 33.631 1.00 18.73  ? 318 RET A C9   1 
HETATM 4248 C C10  . RET S 4 .   ? 16.659 42.942 33.549 1.00 19.20  ? 318 RET A C10  1 
HETATM 4249 C C11  . RET S 4 .   ? 17.168 42.151 34.489 1.00 19.15  ? 318 RET A C11  1 
HETATM 4250 C C12  . RET S 4 .   ? 17.337 40.799 34.244 1.00 20.37  ? 318 RET A C12  1 
HETATM 4251 C C13  . RET S 4 .   ? 17.727 39.818 35.209 1.00 19.57  ? 318 RET A C13  1 
HETATM 4252 C C14  . RET S 4 .   ? 17.747 38.512 34.713 1.00 21.59  ? 318 RET A C14  1 
HETATM 4253 C C15  . RET S 4 .   ? 17.675 37.425 35.475 1.00 21.97  ? 318 RET A C15  1 
HETATM 4254 C C16  . RET S 4 .   ? 16.376 45.476 29.245 1.00 20.00  ? 318 RET A C16  1 
HETATM 4255 C C17  . RET S 4 .   ? 13.912 45.280 29.849 1.00 23.28  ? 318 RET A C17  1 
HETATM 4256 C C18  . RET S 4 .   ? 15.318 49.129 32.375 1.00 21.54  ? 318 RET A C18  1 
HETATM 4257 C C19  . RET S 4 .   ? 16.826 45.144 34.831 1.00 20.74  ? 318 RET A C19  1 
HETATM 4258 C C20  . RET S 4 .   ? 18.099 40.219 36.609 1.00 21.24  ? 318 RET A C20  1 
HETATM 4259 H H21  . RET S 4 .   ? 15.665 46.974 27.852 1.00 36.05  ? 318 RET A H21  1 
HETATM 4260 H H22  . RET S 4 .   ? 14.111 46.900 28.026 1.00 36.05  ? 318 RET A H22  1 
HETATM 4261 H H31  . RET S 4 .   ? 14.070 48.947 28.112 1.00 43.93  ? 318 RET A H31  1 
HETATM 4262 H H32  . RET S 4 .   ? 15.637 49.012 28.078 1.00 43.93  ? 318 RET A H32  1 
HETATM 4263 H H41  . RET S 4 .   ? 13.991 49.607 30.139 1.00 23.24  ? 318 RET A H41  1 
HETATM 4264 H H42  . RET S 4 .   ? 15.501 50.009 29.956 1.00 23.24  ? 318 RET A H42  1 
HETATM 4265 H H7   . RET S 4 .   ? 15.781 46.853 32.982 1.00 21.29  ? 318 RET A H7   1 
HETATM 4266 H H8   . RET S 4 .   ? 16.103 44.362 31.633 1.00 21.78  ? 318 RET A H8   1 
HETATM 4267 H H10  . RET S 4 .   ? 16.438 42.496 32.706 1.00 23.05  ? 318 RET A H10  1 
HETATM 4268 H H11  . RET S 4 .   ? 17.094 42.437 35.423 1.00 22.98  ? 318 RET A H11  1 
HETATM 4269 H H12  . RET S 4 .   ? 17.179 40.479 33.332 1.00 24.45  ? 318 RET A H12  1 
HETATM 4270 H H14  . RET S 4 .   ? 17.818 38.337 33.753 1.00 25.91  ? 318 RET A H14  1 
HETATM 4271 H H15  . RET S 4 .   ? 17.691 37.534 36.448 1.00 26.36  ? 318 RET A H15  1 
HETATM 4272 H H161 . RET S 4 .   ? 16.239 45.027 28.386 1.00 24.00  ? 318 RET A H161 1 
HETATM 4273 H H162 . RET S 4 .   ? 17.145 46.072 29.136 1.00 24.00  ? 318 RET A H162 1 
HETATM 4274 H H163 . RET S 4 .   ? 16.639 44.786 29.888 1.00 24.00  ? 318 RET A H163 1 
HETATM 4275 H H171 . RET S 4 .   ? 14.090 44.595 30.525 1.00 27.94  ? 318 RET A H171 1 
HETATM 4276 H H172 . RET S 4 .   ? 13.720 44.828 29.002 1.00 27.94  ? 318 RET A H172 1 
HETATM 4277 H H173 . RET S 4 .   ? 13.108 45.770 30.119 1.00 27.94  ? 318 RET A H173 1 
HETATM 4278 H H181 . RET S 4 .   ? 15.424 50.094 32.250 1.00 25.85  ? 318 RET A H181 1 
HETATM 4279 H H182 . RET S 4 .   ? 16.059 48.869 32.959 1.00 25.85  ? 318 RET A H182 1 
HETATM 4280 H H183 . RET S 4 .   ? 14.517 49.035 32.929 1.00 25.85  ? 318 RET A H183 1 
HETATM 4281 H H191 . RET S 4 .   ? 17.302 44.592 35.485 1.00 24.89  ? 318 RET A H191 1 
HETATM 4282 H H192 . RET S 4 .   ? 17.417 45.872 34.548 1.00 24.89  ? 318 RET A H192 1 
HETATM 4283 H H193 . RET S 4 .   ? 16.038 45.531 35.263 1.00 24.89  ? 318 RET A H193 1 
HETATM 4284 H H201 . RET S 4 .   ? 17.309 40.479 37.126 1.00 25.49  ? 318 RET A H201 1 
HETATM 4285 H H202 . RET S 4 .   ? 18.536 39.484 37.085 1.00 25.49  ? 318 RET A H202 1 
HETATM 4286 H H203 . RET S 4 .   ? 18.715 40.980 36.609 1.00 25.49  ? 318 RET A H203 1 
HETATM 4287 O O    . HOH T 5 .   ? 3.951  29.493 18.525 1.00 52.89  ? 401 HOH A O    1 
HETATM 4288 O O    . HOH T 5 .   ? 22.812 34.995 67.304 1.00 44.34  ? 402 HOH A O    1 
HETATM 4289 O O    . HOH T 5 .   ? 9.557  47.948 54.317 1.00 48.34  ? 403 HOH A O    1 
HETATM 4290 O O    . HOH T 5 .   ? 19.110 29.064 73.623 1.00 36.59  ? 404 HOH A O    1 
HETATM 4291 O O    . HOH T 5 .   ? 15.307 41.052 23.319 1.00 36.80  ? 405 HOH A O    1 
HETATM 4292 O O    . HOH T 5 .   ? 20.871 26.703 12.364 1.00 78.30  ? 406 HOH A O    1 
HETATM 4293 O O    . HOH T 5 .   ? 21.296 30.580 65.698 1.00 63.07  ? 407 HOH A O    1 
HETATM 4294 O O    . HOH T 5 .   ? 17.890 35.168 32.425 1.00 23.53  ? 408 HOH A O    1 
HETATM 4295 O O    . HOH T 5 .   ? 5.316  43.624 16.609 1.00 47.26  ? 409 HOH A O    1 
HETATM 4296 O O    . HOH T 5 .   ? 22.725 45.207 16.444 1.00 41.89  ? 410 HOH A O    1 
HETATM 4297 O O    . HOH T 5 .   ? 16.414 34.300 29.088 1.00 24.76  ? 411 HOH A O    1 
HETATM 4298 O O    . HOH T 5 .   ? 17.979 36.661 28.809 1.00 25.05  ? 412 HOH A O    1 
HETATM 4299 O O    . HOH T 5 .   ? 22.108 25.927 53.596 1.00 47.29  ? 413 HOH A O    1 
HETATM 4300 O O    . HOH T 5 .   ? 18.840 37.502 69.240 1.00 33.70  ? 414 HOH A O    1 
HETATM 4301 O O    . HOH T 5 .   ? 18.703 48.068 15.945 1.00 43.88  ? 415 HOH A O    1 
HETATM 4302 O O    . HOH T 5 .   ? 30.356 39.768 15.536 1.00 54.85  ? 416 HOH A O    1 
HETATM 4303 O O    . HOH T 5 .   ? 8.651  27.979 54.489 1.00 35.79  ? 417 HOH A O    1 
HETATM 4304 O O    . HOH T 5 .   ? 7.761  30.748 18.257 1.00 46.31  ? 418 HOH A O    1 
HETATM 4305 O O    . HOH T 5 .   ? 23.512 28.548 54.164 1.00 45.99  ? 419 HOH A O    1 
HETATM 4306 O O    . HOH T 5 .   ? 16.719 23.739 46.696 1.00 33.75  ? 420 HOH A O    1 
HETATM 4307 O O    . HOH T 5 .   ? 23.346 36.950 14.509 1.00 44.92  ? 421 HOH A O    1 
HETATM 4308 O O    . HOH T 5 .   ? 15.846 21.086 47.129 1.00 39.39  ? 422 HOH A O    1 
HETATM 4309 O O    . HOH T 5 .   ? 15.122 25.332 14.957 1.00 54.48  ? 423 HOH A O    1 
HETATM 4310 O O    . HOH T 5 .   ? 28.516 39.394 14.128 1.00 53.75  ? 424 HOH A O    1 
HETATM 4311 O O    . HOH T 5 .   ? 23.635 41.937 14.594 1.00 43.67  ? 425 HOH A O    1 
HETATM 4312 O O    . HOH T 5 .   ? 25.522 38.922 15.228 1.00 37.09  ? 426 HOH A O    1 
HETATM 4313 O O    . HOH T 5 .   ? 17.276 22.943 58.490 1.00 53.55  ? 427 HOH A O    1 
HETATM 4314 O O    . HOH T 5 .   ? 10.636 49.158 8.863  1.00 56.36  ? 428 HOH A O    1 
HETATM 4315 O O    . HOH T 5 .   ? 10.139 31.202 16.021 1.00 59.19  ? 429 HOH A O    1 
HETATM 4316 O O    . HOH T 5 .   ? 4.456  51.358 20.512 1.00 24.85  ? 430 HOH A O    1 
HETATM 4317 O O    . HOH T 5 .   ? 22.002 35.597 26.235 1.00 23.17  ? 431 HOH A O    1 
HETATM 4318 O O    . HOH T 5 .   ? 20.219 39.910 40.778 1.00 28.00  ? 432 HOH A O    1 
HETATM 4319 O O    . HOH T 5 .   ? 18.817 32.602 41.737 1.00 41.68  ? 433 HOH A O    1 
HETATM 4320 O O    . HOH T 5 .   ? 14.714 34.383 60.230 1.00 65.10  ? 434 HOH A O    1 
HETATM 4321 O O    . HOH T 5 .   ? 26.810 43.552 59.529 1.00 54.52  ? 435 HOH A O    1 
HETATM 4322 O O    . HOH T 5 .   ? 29.715 31.221 16.369 1.00 61.83  ? 436 HOH A O    1 
HETATM 4323 O O    . HOH T 5 .   ? 18.774 39.768 22.434 1.00 33.17  ? 437 HOH A O    1 
HETATM 4324 O O    . HOH T 5 .   ? 8.409  49.016 10.499 1.00 46.49  ? 438 HOH A O    1 
HETATM 4325 O O    . HOH T 5 .   ? 8.162  33.339 17.791 1.00 40.09  ? 439 HOH A O    1 
HETATM 4326 O O    . HOH T 5 .   ? 17.208 40.185 20.067 1.00 29.59  ? 440 HOH A O    1 
HETATM 4327 O O    . HOH T 5 .   ? 19.913 35.676 14.226 1.00 50.76  ? 441 HOH A O    1 
HETATM 4328 O O    . HOH T 5 .   ? 16.665 42.097 7.065  1.00 59.11  ? 442 HOH A O    1 
HETATM 4329 O O    . HOH T 5 .   ? 8.591  39.981 54.311 1.00 54.16  ? 443 HOH A O    1 
HETATM 4330 O O    . HOH T 5 .   ? 3.925  57.750 13.399 1.00 70.41  ? 444 HOH A O    1 
HETATM 4331 O O    . HOH T 5 .   ? 20.949 45.857 14.673 1.00 52.39  ? 445 HOH A O    1 
HETATM 4332 O O    . HOH T 5 .   ? 18.347 34.844 12.737 1.00 53.78  ? 446 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   . ILE A 1   ? 1.6029 1.1363 0.9521 -0.2669 -0.0027 -0.0524 4   ILE A N   
2    C CA  . ILE A 1   ? 1.5293 1.1536 0.9797 -0.2349 -0.0116 -0.0510 4   ILE A CA  
3    C C   . ILE A 1   ? 1.3644 1.0009 0.8556 -0.1839 0.0326  -0.0567 4   ILE A C   
4    O O   . ILE A 1   ? 1.1611 0.8856 0.7471 -0.1620 0.0230  -0.0406 4   ILE A O   
5    C CB  . ILE A 1   ? 1.4824 1.1271 0.9931 -0.2155 -0.0121 -0.0554 4   ILE A CB  
6    C CG1 . ILE A 1   ? 1.5491 1.1054 1.0101 -0.1877 0.0404  -0.0810 4   ILE A CG1 
7    C CG2 . ILE A 1   ? 1.2565 0.9169 0.7645 -0.2567 -0.0545 -0.0358 4   ILE A CG2 
8    C CD1 . ILE A 1   ? 1.4717 1.0399 0.9786 -0.1739 0.0387  -0.0837 4   ILE A CD1 
9    N N   . THR A 2   ? 1.2827 0.8256 0.7001 -0.1662 0.0846  -0.0762 5   THR A N   
10   C CA  . THR A 2   ? 1.0338 0.5876 0.4948 -0.1174 0.1307  -0.0744 5   THR A CA  
11   C C   . THR A 2   ? 1.0959 0.6593 0.5327 -0.1278 0.1281  -0.0653 5   THR A C   
12   O O   . THR A 2   ? 1.1461 0.7205 0.6194 -0.0902 0.1656  -0.0602 5   THR A O   
13   C CB  . THR A 2   ? 1.2814 0.7353 0.6832 -0.0929 0.1907  -0.0855 5   THR A CB  
14   O OG1 . THR A 2   ? 1.4152 0.7790 0.7111 -0.1339 0.1858  -0.0884 5   THR A OG1 
15   C CG2 . THR A 2   ? 1.1663 0.6322 0.6215 -0.0691 0.1993  -0.0878 5   THR A CG2 
22   N N   . GLY A 3   ? 1.2385 0.8011 0.6180 -0.1788 0.0847  -0.0582 6   GLY A N   
23   C CA  . GLY A 3   ? 1.1134 0.6898 0.4717 -0.1896 0.0800  -0.0456 6   GLY A CA  
24   C C   . GLY A 3   ? 0.8740 0.5724 0.3694 -0.1617 0.0640  -0.0235 6   GLY A C   
25   O O   . GLY A 3   ? 1.0563 0.7698 0.5533 -0.1560 0.0729  -0.0133 6   GLY A O   
29   N N   . ARG A 4   ? 0.7760 0.5518 0.3769 -0.1460 0.0431  -0.0162 7   ARG A N   
30   C CA  . ARG A 4   ? 0.6127 0.4878 0.3308 -0.1231 0.0313  0.0028  7   ARG A CA  
31   C C   . ARG A 4   ? 0.5103 0.4023 0.2984 -0.0761 0.0656  -0.0059 7   ARG A C   
32   O O   . ARG A 4   ? 0.5893 0.4719 0.3952 -0.0633 0.0714  -0.0162 7   ARG A O   
33   C CB  . ARG A 4   ? 0.5268 0.4634 0.3057 -0.1374 -0.0088 0.0188  7   ARG A CB  
34   C CG  . ARG A 4   ? 0.5727 0.5245 0.3163 -0.1861 -0.0517 0.0450  7   ARG A CG  
35   C CD  . ARG A 4   ? 0.6554 0.6587 0.4598 -0.1962 -0.0824 0.0646  7   ARG A CD  
36   N NE  . ARG A 4   ? 0.7096 0.6581 0.4562 -0.2172 -0.0906 0.0481  7   ARG A NE  
37   C CZ  . ARG A 4   ? 0.6759 0.6445 0.4724 -0.2061 -0.0957 0.0473  7   ARG A CZ  
38   N NH1 . ARG A 4   ? 0.4508 0.4822 0.3472 -0.1718 -0.0891 0.0574  7   ARG A NH1 
39   N NH2 . ARG A 4   ? 0.7393 0.6519 0.4745 -0.2292 -0.1027 0.0335  7   ARG A NH2 
53   N N   . PRO A 5   ? 0.4835 0.4127 0.3243 -0.0533 0.0817  0.0033  8   PRO A N   
54   C CA  . PRO A 5   ? 0.4597 0.4077 0.3667 -0.0160 0.1097  0.0023  8   PRO A CA  
55   C C   . PRO A 5   ? 0.4275 0.4224 0.4074 -0.0072 0.0914  0.0026  8   PRO A C   
56   O O   . PRO A 5   ? 0.4311 0.4248 0.4414 0.0144  0.1088  0.0014  8   PRO A O   
57   C CB  . PRO A 5   ? 0.4956 0.4801 0.4451 -0.0035 0.1213  0.0164  8   PRO A CB  
58   C CG  . PRO A 5   ? 0.6424 0.6424 0.5665 -0.0307 0.0952  0.0259  8   PRO A CG  
59   C CD  . PRO A 5   ? 0.5195 0.4699 0.3552 -0.0633 0.0765  0.0185  8   PRO A CD  
67   N N   . GLU A 6   ? 0.3371 0.3699 0.3429 -0.0237 0.0585  0.0080  9   GLU A N   
68   C CA  . GLU A 6   ? 0.2865 0.3526 0.3497 -0.0161 0.0448  0.0075  9   GLU A CA  
69   C C   . GLU A 6   ? 0.2771 0.3148 0.3149 -0.0192 0.0395  -0.0034 9   GLU A C   
70   O O   . GLU A 6   ? 0.2602 0.3179 0.3354 -0.0133 0.0294  -0.0044 9   GLU A O   
71   C CB  . GLU A 6   ? 0.2792 0.3838 0.3738 -0.0281 0.0228  0.0214  9   GLU A CB  
72   C CG  . GLU A 6   ? 0.2826 0.3836 0.3447 -0.0527 0.0012  0.0318  9   GLU A CG  
73   C CD  . GLU A 6   ? 0.2902 0.3909 0.3162 -0.0727 -0.0055 0.0467  9   GLU A CD  
74   O OE1 . GLU A 6   ? 0.3254 0.4106 0.3319 -0.0646 0.0139  0.0413  9   GLU A OE1 
75   O OE2 . GLU A 6   ? 0.3332 0.4487 0.3492 -0.0966 -0.0288 0.0668  9   GLU A OE2 
82   N N   . TRP A 7   ? 0.3335 0.3137 0.2988 -0.0291 0.0499  -0.0130 10  TRP A N   
83   C CA  . TRP A 7   ? 0.3594 0.3057 0.2949 -0.0351 0.0459  -0.0231 10  TRP A CA  
84   C C   . TRP A 7   ? 0.3269 0.2849 0.3107 -0.0071 0.0605  -0.0248 10  TRP A C   
85   O O   . TRP A 7   ? 0.3269 0.2871 0.3213 -0.0079 0.0489  -0.0279 10  TRP A O   
86   C CB  . TRP A 7   ? 0.5001 0.3629 0.3321 -0.0535 0.0617  -0.0349 10  TRP A CB  
87   C CG  . TRP A 7   ? 0.5601 0.3689 0.3657 -0.0257 0.1105  -0.0417 10  TRP A CG  
88   C CD1 . TRP A 7   ? 0.6446 0.4319 0.4300 -0.0131 0.1413  -0.0381 10  TRP A CD1 
89   C CD2 . TRP A 7   ? 0.5731 0.3480 0.3796 -0.0036 0.1379  -0.0462 10  TRP A CD2 
90   N NE1 . TRP A 7   ? 0.7124 0.4487 0.4836 0.0173  0.1916  -0.0379 10  TRP A NE1 
91   C CE2 . TRP A 7   ? 0.6370 0.3697 0.4265 0.0245  0.1897  -0.0411 10  TRP A CE2 
92   C CE3 . TRP A 7   ? 0.6329 0.4096 0.4563 -0.0022 0.1274  -0.0499 10  TRP A CE3 
93   C CZ2 . TRP A 7   ? 0.7963 0.4891 0.5881 0.0546  0.2330  -0.0360 10  TRP A CZ2 
94   C CZ3 . TRP A 7   ? 0.7581 0.4965 0.5807 0.0253  0.1659  -0.0483 10  TRP A CZ3 
95   C CH2 . TRP A 7   ? 0.7403 0.4405 0.5519 0.0543  0.2184  -0.0392 10  TRP A CH2 
106  N N   . ILE A 8   ? 0.3346 0.3018 0.3500 0.0178  0.0873  -0.0176 11  ILE A N   
107  C CA  . ILE A 8   ? 0.3176 0.3002 0.3804 0.0409  0.0988  -0.0099 11  ILE A CA  
108  C C   . ILE A 8   ? 0.2498 0.2861 0.3684 0.0358  0.0664  -0.0062 11  ILE A C   
109  O O   . ILE A 8   ? 0.2498 0.2917 0.3871 0.0427  0.0617  -0.0039 11  ILE A O   
110  C CB  . ILE A 8   ? 0.3614 0.3565 0.4617 0.0662  0.1313  0.0087  11  ILE A CB  
111  C CG1 . ILE A 8   ? 0.3955 0.4193 0.5566 0.0877  0.1392  0.0283  11  ILE A CG1 
112  C CG2 . ILE A 8   ? 0.3566 0.3990 0.4959 0.0597  0.1172  0.0164  11  ILE A CG2 
113  C CD1 . ILE A 8   ? 0.5673 0.5374 0.6891 0.0983  0.1614  0.0230  11  ILE A CD1 
125  N N   . TRP A 9   ? 0.2133 0.2820 0.3533 0.0243  0.0477  -0.0042 12  TRP A N   
126  C CA  . TRP A 9   ? 0.1971 0.2959 0.3718 0.0187  0.0255  -0.0022 12  TRP A CA  
127  C C   . TRP A 9   ? 0.2155 0.2999 0.3671 0.0085  0.0109  -0.0097 12  TRP A C   
128  O O   . TRP A 9   ? 0.2060 0.2965 0.3715 0.0092  0.0007  -0.0098 12  TRP A O   
129  C CB  . TRP A 9   ? 0.1791 0.3032 0.3777 0.0111  0.0192  0.0033  12  TRP A CB  
130  C CG  . TRP A 9   ? 0.1860 0.3265 0.4098 0.0192  0.0340  0.0139  12  TRP A CG  
131  C CD1 . TRP A 9   ? 0.2369 0.3788 0.4546 0.0179  0.0443  0.0169  12  TRP A CD1 
132  C CD2 . TRP A 9   ? 0.2032 0.3642 0.4658 0.0301  0.0412  0.0289  12  TRP A CD2 
133  N NE1 . TRP A 9   ? 0.2487 0.4076 0.4990 0.0290  0.0598  0.0305  12  TRP A NE1 
134  C CE2 . TRP A 9   ? 0.2164 0.3890 0.4960 0.0358  0.0570  0.0404  12  TRP A CE2 
135  C CE3 . TRP A 9   ? 0.1999 0.3740 0.4865 0.0346  0.0342  0.0390  12  TRP A CE3 
136  C CZ2 . TRP A 9   ? 0.2441 0.4292 0.5483 0.0442  0.0635  0.0608  12  TRP A CZ2 
137  C CZ3 . TRP A 9   ? 0.2518 0.4421 0.5630 0.0413  0.0395  0.0608  12  TRP A CZ3 
138  C CH2 . TRP A 9   ? 0.2268 0.4224 0.5486 0.0459  0.0541  0.0721  12  TRP A CH2 
149  N N   . LEU A 10  ? 0.1979 0.2633 0.3131 -0.0038 0.0087  -0.0122 13  LEU A N   
150  C CA  . LEU A 10  ? 0.2098 0.2659 0.3100 -0.0153 -0.0057 -0.0121 13  LEU A CA  
151  C C   . LEU A 10  ? 0.2432 0.2716 0.3257 -0.0090 -0.0004 -0.0209 13  LEU A C   
152  O O   . LEU A 10  ? 0.2268 0.2582 0.3198 -0.0089 -0.0101 -0.0199 13  LEU A O   
153  C CB  . LEU A 10  ? 0.2210 0.2690 0.2877 -0.0377 -0.0154 -0.0051 13  LEU A CB  
154  C CG  . LEU A 10  ? 0.2015 0.2837 0.2934 -0.0425 -0.0196 0.0114  13  LEU A CG  
155  C CD1 . LEU A 10  ? 0.2561 0.3348 0.3132 -0.0697 -0.0351 0.0251  13  LEU A CD1 
156  C CD2 . LEU A 10  ? 0.2392 0.3486 0.3771 -0.0356 -0.0230 0.0249  13  LEU A CD2 
168  N N   . ALA A 11  ? 0.2568 0.2541 0.3138 -0.0002 0.0203  -0.0269 14  ALA A N   
169  C CA  . ALA A 11  ? 0.2620 0.2276 0.3033 0.0092  0.0324  -0.0317 14  ALA A CA  
170  C C   . ALA A 11  ? 0.2639 0.2662 0.3606 0.0275  0.0290  -0.0227 14  ALA A C   
171  O O   . ALA A 11  ? 0.2526 0.2491 0.3517 0.0307  0.0242  -0.0230 14  ALA A O   
172  C CB  . ALA A 11  ? 0.3565 0.2732 0.3580 0.0198  0.0671  -0.0350 14  ALA A CB  
178  N N   A LEU A 12  ? 0.2423 0.2807 0.3806 0.0368  0.0307  -0.0119 15  LEU A N   
179  N N   B LEU A 12  ? 0.2419 0.2806 0.3805 0.0368  0.0305  -0.0118 15  LEU A N   
180  C CA  A LEU A 12  ? 0.2353 0.3075 0.4175 0.0441  0.0203  0.0010  15  LEU A CA  
181  C CA  B LEU A 12  ? 0.2336 0.3060 0.4158 0.0438  0.0196  0.0009  15  LEU A CA  
182  C C   A LEU A 12  ? 0.2140 0.2933 0.3931 0.0305  -0.0040 -0.0049 15  LEU A C   
183  C C   B LEU A 12  ? 0.2147 0.2932 0.3928 0.0303  -0.0042 -0.0053 15  LEU A C   
184  O O   A LEU A 12  ? 0.2037 0.2858 0.3891 0.0330  -0.0123 -0.0007 15  LEU A O   
185  O O   B LEU A 12  ? 0.2045 0.2854 0.3885 0.0326  -0.0127 -0.0013 15  LEU A O   
186  C CB  A LEU A 12  ? 0.2237 0.3335 0.4489 0.0478  0.0220  0.0178  15  LEU A CB  
187  C CB  B LEU A 12  ? 0.2230 0.3341 0.4484 0.0463  0.0192  0.0173  15  LEU A CB  
188  C CG  A LEU A 12  ? 0.2119 0.3619 0.4830 0.0473  0.0063  0.0397  15  LEU A CG  
189  C CG  B LEU A 12  ? 0.1932 0.3025 0.4372 0.0680  0.0503  0.0341  15  LEU A CG  
190  C CD1 A LEU A 12  ? 0.2644 0.4171 0.5549 0.0656  0.0182  0.0573  15  LEU A CD1 
191  C CD1 B LEU A 12  ? 0.2760 0.4245 0.5629 0.0671  0.0502  0.0517  15  LEU A CD1 
192  C CD2 A LEU A 12  ? 0.2167 0.3979 0.5198 0.0436  0.0064  0.0575  15  LEU A CD2 
193  C CD2 B LEU A 12  ? 0.2824 0.4035 0.5588 0.0857  0.0596  0.0563  15  LEU A CD2 
216  N N   . GLY A 13  ? 0.1853 0.2630 0.3523 0.0180  -0.0110 -0.0115 16  GLY A N   
217  C CA  . GLY A 13  ? 0.1886 0.2615 0.3490 0.0103  -0.0220 -0.0132 16  GLY A CA  
218  C C   . GLY A 13  ? 0.2118 0.2661 0.3566 0.0120  -0.0234 -0.0155 16  GLY A C   
219  O O   . GLY A 13  ? 0.1952 0.2436 0.3381 0.0133  -0.0285 -0.0142 16  GLY A O   
223  N N   . THR A 14  ? 0.1930 0.2320 0.3194 0.0085  -0.0191 -0.0186 17  THR A N   
224  C CA  . THR A 14  ? 0.2203 0.2386 0.3300 0.0052  -0.0215 -0.0196 17  THR A CA  
225  C C   . THR A 14  ? 0.2598 0.2713 0.3749 0.0193  -0.0167 -0.0206 17  THR A C   
226  O O   . THR A 14  ? 0.2388 0.2461 0.3552 0.0209  -0.0220 -0.0180 17  THR A O   
227  C CB  . THR A 14  ? 0.2327 0.2235 0.3059 -0.0091 -0.0187 -0.0241 17  THR A CB  
228  O OG1 . THR A 14  ? 0.2347 0.2414 0.3065 -0.0268 -0.0294 -0.0154 17  THR A OG1 
229  C CG2 . THR A 14  ? 0.2785 0.2456 0.3331 -0.0195 -0.0250 -0.0231 17  THR A CG2 
237  N N   . ALA A 15  ? 0.2280 0.2395 0.3500 0.0316  -0.0035 -0.0191 18  ALA A N   
238  C CA  . ALA A 15  ? 0.2302 0.2429 0.3677 0.0474  0.0031  -0.0104 18  ALA A CA  
239  C C   . ALA A 15  ? 0.2478 0.2887 0.4063 0.0455  -0.0161 -0.0019 18  ALA A C   
240  O O   . ALA A 15  ? 0.2539 0.2910 0.4128 0.0508  -0.0195 0.0034  18  ALA A O   
241  C CB  . ALA A 15  ? 0.2606 0.2784 0.4165 0.0636  0.0248  0.0009  18  ALA A CB  
247  N N   . LEU A 16  ? 0.1938 0.2572 0.3637 0.0364  -0.0277 0.0009  19  LEU A N   
248  C CA  . LEU A 16  ? 0.2134 0.2884 0.3844 0.0272  -0.0461 0.0085  19  LEU A CA  
249  C C   . LEU A 16  ? 0.2128 0.2583 0.3514 0.0216  -0.0487 -0.0010 19  LEU A C   
250  O O   . LEU A 16  ? 0.2484 0.2861 0.3726 0.0185  -0.0580 0.0041  19  LEU A O   
251  C CB  . LEU A 16  ? 0.2261 0.3204 0.4075 0.0134  -0.0557 0.0129  19  LEU A CB  
252  C CG  . LEU A 16  ? 0.1871 0.3192 0.4131 0.0206  -0.0523 0.0325  19  LEU A CG  
253  C CD1 . LEU A 16  ? 0.3063 0.4544 0.5418 0.0044  -0.0609 0.0352  19  LEU A CD1 
254  C CD2 . LEU A 16  ? 0.2986 0.4582 0.5507 0.0222  -0.0651 0.0585  19  LEU A CD2 
266  N N   . MET A 17  ? 0.2024 0.2337 0.3316 0.0201  -0.0398 -0.0092 20  MET A N   
267  C CA  . MET A 17  ? 0.2306 0.2377 0.3411 0.0200  -0.0352 -0.0090 20  MET A CA  
268  C C   . MET A 17  ? 0.2612 0.2600 0.3712 0.0283  -0.0337 -0.0067 20  MET A C   
269  O O   . MET A 17  ? 0.2533 0.2340 0.3476 0.0310  -0.0322 -0.0033 20  MET A O   
270  C CB  . MET A 17  ? 0.2029 0.2089 0.3197 0.0175  -0.0255 -0.0056 20  MET A CB  
271  C CG  . MET A 17  ? 0.2085 0.2163 0.3244 0.0115  -0.0215 -0.0062 20  MET A CG  
272  S SD  . MET A 17  ? 0.2572 0.2214 0.3312 0.0057  -0.0144 -0.0085 20  MET A SD  
273  C CE  . MET A 17  ? 0.2802 0.2470 0.3609 -0.0016 -0.0049 -0.0082 20  MET A CE  
283  N N   . GLY A 18  ? 0.2424 0.2456 0.3618 0.0319  -0.0310 -0.0088 21  GLY A N   
284  C CA  . GLY A 18  ? 0.2632 0.2507 0.3785 0.0387  -0.0266 -0.0071 21  GLY A CA  
285  C C   . GLY A 18  ? 0.2756 0.2684 0.3950 0.0488  -0.0299 0.0004  21  GLY A C   
286  O O   . GLY A 18  ? 0.2825 0.2624 0.3937 0.0531  -0.0296 0.0044  21  GLY A O   
290  N N   . LEU A 19  ? 0.2629 0.2788 0.3996 0.0523  -0.0333 0.0078  22  LEU A N   
291  C CA  . LEU A 19  ? 0.2466 0.2805 0.3957 0.0575  -0.0422 0.0254  22  LEU A CA  
292  C C   . LEU A 19  ? 0.2945 0.3192 0.4140 0.0435  -0.0592 0.0257  22  LEU A C   
293  O O   . LEU A 19  ? 0.3122 0.3323 0.4212 0.0455  -0.0655 0.0358  22  LEU A O   
294  C CB  . LEU A 19  ? 0.2790 0.3496 0.4637 0.0602  -0.0443 0.0425  22  LEU A CB  
295  C CG  . LEU A 19  ? 0.3106 0.3781 0.5180 0.0805  -0.0171 0.0489  22  LEU A CG  
296  C CD1 . LEU A 19  ? 0.3927 0.5005 0.6424 0.0845  -0.0158 0.0715  22  LEU A CD1 
297  C CD2 . LEU A 19  ? 0.4091 0.4696 0.6286 0.0996  -0.0030 0.0652  22  LEU A CD2 
309  N N   . GLY A 20  ? 0.2794 0.2932 0.3773 0.0284  -0.0640 0.0159  23  GLY A N   
310  C CA  . GLY A 20  ? 0.2782 0.2590 0.3274 0.0140  -0.0707 0.0134  23  GLY A CA  
311  C C   . GLY A 20  ? 0.2978 0.2444 0.3251 0.0248  -0.0551 0.0101  23  GLY A C   
312  O O   . GLY A 20  ? 0.3378 0.2596 0.3285 0.0209  -0.0591 0.0149  23  GLY A O   
316  N N   . THR A 21  ? 0.2954 0.2418 0.3449 0.0363  -0.0388 0.0060  24  THR A N   
317  C CA  . THR A 21  ? 0.3288 0.2521 0.3719 0.0465  -0.0242 0.0106  24  THR A CA  
318  C C   . THR A 21  ? 0.3223 0.2472 0.3667 0.0549  -0.0289 0.0172  24  THR A C   
319  O O   . THR A 21  ? 0.3379 0.2356 0.3537 0.0583  -0.0231 0.0224  24  THR A O   
320  C CB  . THR A 21  ? 0.2803 0.2169 0.3562 0.0490  -0.0162 0.0124  24  THR A CB  
321  O OG1 . THR A 21  ? 0.2775 0.2160 0.3562 0.0432  -0.0102 0.0128  24  THR A OG1 
322  C CG2 . THR A 21  ? 0.3136 0.2342 0.3945 0.0567  -0.0025 0.0257  24  THR A CG2 
330  N N   . LEU A 22  ? 0.3000 0.2504 0.3734 0.0602  -0.0343 0.0192  25  LEU A N   
331  C CA  . LEU A 22  ? 0.2739 0.2253 0.3553 0.0720  -0.0328 0.0296  25  LEU A CA  
332  C C   . LEU A 22  ? 0.3112 0.2684 0.3727 0.0670  -0.0486 0.0422  25  LEU A C   
333  O O   . LEU A 22  ? 0.3586 0.3018 0.4053 0.0732  -0.0469 0.0509  25  LEU A O   
334  C CB  . LEU A 22  ? 0.3324 0.2996 0.4446 0.0810  -0.0257 0.0321  25  LEU A CB  
335  C CG  . LEU A 22  ? 0.4360 0.3823 0.5472 0.0776  -0.0132 0.0193  25  LEU A CG  
336  C CD1 . LEU A 22  ? 0.4364 0.3792 0.5578 0.0849  0.0005  0.0188  25  LEU A CD1 
337  C CD2 . LEU A 22  ? 0.5771 0.4984 0.6815 0.0785  -0.0058 0.0208  25  LEU A CD2 
349  N N   . TYR A 23  ? 0.2898 0.2650 0.3461 0.0519  -0.0661 0.0458  26  TYR A N   
350  C CA  . TYR A 23  ? 0.3440 0.3233 0.3724 0.0365  -0.0892 0.0622  26  TYR A CA  
351  C C   . TYR A 23  ? 0.3567 0.2796 0.3158 0.0274  -0.0846 0.0533  26  TYR A C   
352  O O   . TYR A 23  ? 0.3910 0.3025 0.3226 0.0250  -0.0924 0.0656  26  TYR A O   
353  C CB  . TYR A 23  ? 0.3389 0.3474 0.3735 0.0141  -0.1128 0.0706  26  TYR A CB  
354  C CG  . TYR A 23  ? 0.3634 0.3746 0.3608 -0.0138 -0.1446 0.0905  26  TYR A CG  
355  C CD1 . TYR A 23  ? 0.4200 0.4774 0.4529 -0.0108 -0.1620 0.1257  26  TYR A CD1 
356  C CD2 . TYR A 23  ? 0.4571 0.4243 0.3821 -0.0466 -0.1585 0.0793  26  TYR A CD2 
357  C CE1 . TYR A 23  ? 0.4987 0.5628 0.4936 -0.0441 -0.1989 0.1501  26  TYR A CE1 
358  C CE2 . TYR A 23  ? 0.5484 0.5080 0.4219 -0.0827 -0.1931 0.0975  26  TYR A CE2 
359  C CZ  . TYR A 23  ? 0.5229 0.5376 0.4343 -0.0841 -0.2179 0.1351  26  TYR A CZ  
360  O OH  . TYR A 23  ? 0.6791 0.6911 0.5463 -0.1227 -0.2478 0.1542  26  TYR A OH  
370  N N   . PHE A 24  ? 0.3862 0.2696 0.3148 0.0234  -0.0677 0.0348  27  PHE A N   
371  C CA  . PHE A 24  ? 0.4364 0.2527 0.2916 0.0178  -0.0527 0.0297  27  PHE A CA  
372  C C   . PHE A 24  ? 0.4435 0.2464 0.3089 0.0416  -0.0311 0.0355  27  PHE A C   
373  O O   . PHE A 24  ? 0.5005 0.2571 0.3092 0.0404  -0.0229 0.0397  27  PHE A O   
374  C CB  . PHE A 24  ? 0.4273 0.2069 0.2630 0.0165  -0.0286 0.0161  27  PHE A CB  
375  C CG  . PHE A 24  ? 0.4500 0.2250 0.2597 -0.0099 -0.0452 0.0087  27  PHE A CG  
376  C CD1 . PHE A 24  ? 0.5276 0.3096 0.3050 -0.0398 -0.0804 0.0152  27  PHE A CD1 
377  C CD2 . PHE A 24  ? 0.4596 0.2215 0.2756 -0.0080 -0.0259 -0.0004 27  PHE A CD2 
378  C CE1 . PHE A 24  ? 0.5916 0.3706 0.3498 -0.0679 -0.0965 0.0105  27  PHE A CE1 
379  C CE2 . PHE A 24  ? 0.4889 0.2446 0.2838 -0.0322 -0.0385 -0.0075 27  PHE A CE2 
380  C CZ  . PHE A 24  ? 0.5418 0.3007 0.3029 -0.0638 -0.0734 -0.0035 27  PHE A CZ  
390  N N   . LEU A 25  ? 0.3955 0.2332 0.3263 0.0598  -0.0220 0.0367  28  LEU A N   
391  C CA  . LEU A 25  ? 0.4501 0.2791 0.3962 0.0781  -0.0053 0.0454  28  LEU A CA  
392  C C   . LEU A 25  ? 0.4835 0.3199 0.4216 0.0816  -0.0178 0.0574  28  LEU A C   
393  O O   . LEU A 25  ? 0.5350 0.3390 0.4416 0.0889  -0.0061 0.0651  28  LEU A O   
394  C CB  . LEU A 25  ? 0.5129 0.3742 0.5206 0.0860  -0.0010 0.0443  28  LEU A CB  
395  C CG  . LEU A 25  ? 0.6453 0.5002 0.6714 0.0942  0.0149  0.0525  28  LEU A CG  
396  C CD1 . LEU A 25  ? 0.5957 0.4396 0.6143 0.0904  0.0325  0.0561  28  LEU A CD1 
397  C CD2 . LEU A 25  ? 0.7638 0.6446 0.8264 0.0884  0.0093  0.0478  28  LEU A CD2 
409  N N   . VAL A 26  ? 0.4262 0.3048 0.3932 0.0781  -0.0388 0.0645  29  VAL A N   
410  C CA  . VAL A 26  ? 0.4346 0.3288 0.4044 0.0831  -0.0499 0.0850  29  VAL A CA  
411  C C   . VAL A 26  ? 0.4711 0.3359 0.3687 0.0628  -0.0667 0.0925  29  VAL A C   
412  O O   . VAL A 26  ? 0.5593 0.4056 0.4295 0.0680  -0.0647 0.1051  29  VAL A O   
413  C CB  . VAL A 26  ? 0.4273 0.3767 0.4538 0.0871  -0.0625 0.1007  29  VAL A CB  
414  C CG1 . VAL A 26  ? 0.4960 0.4696 0.5308 0.0912  -0.0754 0.1319  29  VAL A CG1 
415  C CG2 . VAL A 26  ? 0.5324 0.4846 0.6050 0.1059  -0.0385 0.0910  29  VAL A CG2 
425  N N   . LYS A 27  ? 0.4734 0.3267 0.3302 0.0359  -0.0840 0.0851  30  LYS A N   
426  C CA  . LYS A 27  ? 0.5543 0.3648 0.3216 0.0054  -0.1033 0.0899  30  LYS A CA  
427  C C   . LYS A 27  ? 0.6047 0.3342 0.2965 0.0122  -0.0730 0.0793  30  LYS A C   
428  O O   . LYS A 27  ? 0.7223 0.4118 0.3383 -0.0043 -0.0833 0.0893  30  LYS A O   
429  C CB  . LYS A 27  ? 0.5912 0.3917 0.3252 -0.0266 -0.1216 0.0799  30  LYS A CB  
430  C CG  . LYS A 27  ? 0.7488 0.5147 0.3895 -0.0740 -0.1571 0.0897  30  LYS A CG  
431  C CD  . LYS A 27  ? 0.7940 0.5690 0.4252 -0.1091 -0.1817 0.0849  30  LYS A CD  
432  C CE  . LYS A 27  ? 0.9896 0.7313 0.5328 -0.1655 -0.2188 0.0953  30  LYS A CE  
433  N NZ  . LYS A 27  ? 1.1271 0.7552 0.5470 -0.1811 -0.1950 0.0747  30  LYS A NZ  
447  N N   . GLY A 28  ? 0.5988 0.3695 0.3719 0.0715  -0.1027 0.0662  31  GLY A N   
448  C CA  . GLY A 28  ? 0.6334 0.4045 0.3814 0.0587  -0.0892 0.0734  31  GLY A CA  
449  C C   . GLY A 28  ? 0.7871 0.5182 0.4918 0.0491  -0.0822 0.0904  31  GLY A C   
450  O O   . GLY A 28  ? 0.7092 0.4387 0.3890 0.0376  -0.0697 0.0969  31  GLY A O   
454  N N   . MET A 29  ? 0.7689 0.4669 0.4638 0.0535  -0.0896 0.0970  32  MET A N   
455  C CA  . MET A 29  ? 0.8074 0.4582 0.4554 0.0465  -0.0855 0.1141  32  MET A CA  
456  C C   . MET A 29  ? 0.8615 0.4970 0.4677 0.0552  -0.0912 0.1203  32  MET A C   
457  O O   . MET A 29  ? 0.9865 0.6279 0.5949 0.0751  -0.1083 0.1128  32  MET A O   
458  C CB  . MET A 29  ? 0.8570 0.4830 0.5110 0.0548  -0.0951 0.1143  32  MET A CB  
459  C CG  . MET A 29  ? 0.9391 0.5713 0.6259 0.0466  -0.0902 0.1099  32  MET A CG  
460  S SD  . MET A 29  ? 1.2057 0.8033 0.8875 0.0409  -0.0873 0.1146  32  MET A SD  
461  C CE  . MET A 29  ? 0.9777 0.5398 0.6094 0.0273  -0.0757 0.1312  32  MET A CE  
471  N N   . GLY A 30  ? 1.0010 0.6217 0.5743 0.0387  -0.0753 0.1318  33  GLY A N   
472  C CA  . GLY A 30  ? 1.0135 0.6203 0.5486 0.0441  -0.0775 0.1377  33  GLY A CA  
473  C C   . GLY A 30  ? 1.0498 0.6829 0.5762 0.0490  -0.0783 0.1319  33  GLY A C   
474  O O   . GLY A 30  ? 1.1132 0.7369 0.6041 0.0487  -0.0752 0.1377  33  GLY A O   
478  N N   . VAL A 31  ? 0.8448 0.5148 0.4072 0.0528  -0.0813 0.1185  34  VAL A N   
479  C CA  . VAL A 31  ? 0.8739 0.5756 0.4361 0.0547  -0.0785 0.1094  34  VAL A CA  
480  C C   . VAL A 31  ? 0.8697 0.5696 0.4058 0.0332  -0.0549 0.1181  34  VAL A C   
481  O O   . VAL A 31  ? 0.9602 0.6678 0.5155 0.0138  -0.0373 0.1200  34  VAL A O   
482  C CB  . VAL A 31  ? 0.8677 0.6177 0.4888 0.0572  -0.0796 0.0903  34  VAL A CB  
483  C CG1 . VAL A 31  ? 0.7843 0.5650 0.4048 0.0569  -0.0742 0.0805  34  VAL A CG1 
484  C CG2 . VAL A 31  ? 0.8967 0.6489 0.5408 0.0774  -0.1017 0.0811  34  VAL A CG2 
494  N N   . SER A 32  ? 0.8821 0.5742 0.3749 0.0362  -0.0540 0.1223  35  SER A N   
495  C CA  . SER A 32  ? 0.9614 0.6540 0.4282 0.0153  -0.0300 0.1295  35  SER A CA  
496  C C   . SER A 32  ? 1.0173 0.7517 0.4943 0.0148  -0.0224 0.1157  35  SER A C   
497  O O   . SER A 32  ? 0.9711 0.7176 0.4400 -0.0038 -0.0001 0.1173  35  SER A O   
498  C CB  . SER A 32  ? 1.0737 0.7293 0.4944 0.0121  -0.0268 0.1449  35  SER A CB  
499  O OG  . SER A 32  ? 1.0936 0.7456 0.4926 0.0319  -0.0439 0.1423  35  SER A OG  
505  N N   . ASP A 33  ? 0.7514 0.5103 0.2496 0.0340  -0.0397 0.1005  36  ASP A N   
506  C CA  . ASP A 33  ? 0.7792 0.5750 0.2850 0.0348  -0.0335 0.0861  36  ASP A CA  
507  C C   . ASP A 33  ? 0.6791 0.5134 0.2359 0.0205  -0.0166 0.0757  36  ASP A C   
508  O O   . ASP A 33  ? 0.6651 0.5123 0.2666 0.0229  -0.0223 0.0693  36  ASP A O   
509  C CB  . ASP A 33  ? 0.7532 0.5649 0.2771 0.0574  -0.0568 0.0709  36  ASP A CB  
510  C CG  . ASP A 33  ? 0.7719 0.6205 0.3081 0.0596  -0.0524 0.0538  36  ASP A CG  
511  O OD1 . ASP A 33  ? 0.8820 0.7246 0.3746 0.0614  -0.0498 0.0556  36  ASP A OD1 
512  O OD2 . ASP A 33  ? 0.7290 0.6094 0.3148 0.0601  -0.0521 0.0390  36  ASP A OD2 
517  N N   . PRO A 34  ? 0.6888 0.5434 0.2392 0.0071  0.0036  0.0726  37  PRO A N   
518  C CA  . PRO A 34  ? 0.6821 0.5723 0.2804 -0.0053 0.0185  0.0628  37  PRO A CA  
519  C C   . PRO A 34  ? 0.6201 0.5420 0.2685 0.0075  0.0072  0.0450  37  PRO A C   
520  O O   . PRO A 34  ? 0.5816 0.5201 0.2721 0.0027  0.0104  0.0405  37  PRO A O   
521  C CB  . PRO A 34  ? 0.7278 0.6360 0.3060 -0.0184 0.0403  0.0603  37  PRO A CB  
522  C CG  . PRO A 34  ? 0.8925 0.7678 0.4090 -0.0178 0.0403  0.0730  37  PRO A CG  
523  C CD  . PRO A 34  ? 0.7920 0.6351 0.2891 0.0006  0.0155  0.0796  37  PRO A CD  
531  N N   . ASP A 35  ? 0.6144 0.5442 0.2588 0.0236  -0.0062 0.0344  38  ASP A N   
532  C CA  . ASP A 35  ? 0.5369 0.4930 0.2279 0.0339  -0.0158 0.0177  38  ASP A CA  
533  C C   . ASP A 35  ? 0.5155 0.4598 0.2324 0.0401  -0.0301 0.0203  38  ASP A C   
534  O O   . ASP A 35  ? 0.4989 0.4596 0.2585 0.0382  -0.0289 0.0142  38  ASP A O   
535  C CB  . ASP A 35  ? 0.6175 0.5823 0.2980 0.0489  -0.0280 0.0046  38  ASP A CB  
536  C CG  . ASP A 35  ? 0.7833 0.7695 0.4509 0.0447  -0.0138 -0.0042 38  ASP A CG  
537  O OD1 . ASP A 35  ? 0.8772 0.8841 0.5671 0.0336  0.0028  -0.0073 38  ASP A OD1 
538  O OD2 . ASP A 35  ? 0.8227 0.8066 0.4592 0.0533  -0.0197 -0.0092 38  ASP A OD2 
543  N N   . ALA A 36  ? 0.5505 0.4649 0.2403 0.0478  -0.0436 0.0299  39  ALA A N   
544  C CA  . ALA A 36  ? 0.5156 0.4195 0.2296 0.0540  -0.0566 0.0314  39  ALA A CA  
545  C C   . ALA A 36  ? 0.4954 0.3965 0.2294 0.0400  -0.0447 0.0393  39  ALA A C   
546  O O   . ALA A 36  ? 0.4586 0.3681 0.2298 0.0420  -0.0494 0.0345  39  ALA A O   
547  C CB  . ALA A 36  ? 0.5620 0.4341 0.2419 0.0665  -0.0736 0.0396  39  ALA A CB  
553  N N   . LYS A 37  ? 0.5222 0.4106 0.2308 0.0251  -0.0292 0.0512  40  LYS A N   
554  C CA  . LYS A 37  ? 0.5036 0.3918 0.2331 0.0106  -0.0180 0.0567  40  LYS A CA  
555  C C   . LYS A 37  ? 0.4697 0.3938 0.2465 0.0075  -0.0120 0.0442  40  LYS A C   
556  O O   . LYS A 37  ? 0.4625 0.3889 0.2669 0.0033  -0.0116 0.0446  40  LYS A O   
557  C CB  . LYS A 37  ? 0.5550 0.4302 0.2525 -0.0078 0.0006  0.0683  40  LYS A CB  
558  C CG  . LYS A 37  ? 0.6679 0.4977 0.3204 -0.0086 -0.0034 0.0849  40  LYS A CG  
559  C CD  . LYS A 37  ? 0.8760 0.6916 0.4867 -0.0248 0.0146  0.0955  40  LYS A CD  
560  C CE  . LYS A 37  ? 0.9135 0.7049 0.5176 -0.0434 0.0264  0.1076  40  LYS A CE  
561  N NZ  . LYS A 37  ? 0.8741 0.6595 0.4451 -0.0637 0.0486  0.1156  40  LYS A NZ  
575  N N   . LYS A 38  ? 0.4420 0.3933 0.2273 0.0088  -0.0062 0.0333  41  LYS A N   
576  C CA  . LYS A 38  ? 0.4291 0.4112 0.2569 0.0084  -0.0022 0.0217  41  LYS A CA  
577  C C   . LYS A 38  ? 0.3772 0.3596 0.2333 0.0198  -0.0167 0.0159  41  LYS A C   
578  O O   . LYS A 38  ? 0.3451 0.3361 0.2308 0.0172  -0.0154 0.0142  41  LYS A O   
579  C CB  . LYS A 38  ? 0.4905 0.4975 0.3190 0.0121  0.0031  0.0095  41  LYS A CB  
580  C CG  . LYS A 38  ? 0.6451 0.6642 0.4574 -0.0013 0.0220  0.0108  41  LYS A CG  
581  C CD  . LYS A 38  ? 0.7785 0.8272 0.6005 0.0041  0.0271  -0.0045 41  LYS A CD  
582  C CE  . LYS A 38  ? 0.7751 0.8198 0.5868 0.0195  0.0135  -0.0125 41  LYS A CE  
583  N NZ  . LYS A 38  ? 0.9196 0.9785 0.7087 0.0199  0.0224  -0.0206 41  LYS A NZ  
597  N N   . PHE A 39  ? 0.3758 0.3504 0.2246 0.0328  -0.0309 0.0117  42  PHE A N   
598  C CA  . PHE A 39  ? 0.3476 0.3252 0.2263 0.0417  -0.0427 0.0048  42  PHE A CA  
599  C C   . PHE A 39  ? 0.3515 0.3118 0.2360 0.0397  -0.0467 0.0134  42  PHE A C   
600  O O   . PHE A 39  ? 0.3304 0.2980 0.2454 0.0405  -0.0487 0.0094  42  PHE A O   
601  C CB  . PHE A 39  ? 0.3807 0.3551 0.2496 0.0553  -0.0576 -0.0029 42  PHE A CB  
602  C CG  . PHE A 39  ? 0.3740 0.3674 0.2456 0.0588  -0.0555 -0.0153 42  PHE A CG  
603  C CD1 . PHE A 39  ? 0.3663 0.3783 0.2733 0.0598  -0.0537 -0.0266 42  PHE A CD1 
604  C CD2 . PHE A 39  ? 0.4212 0.4128 0.2603 0.0615  -0.0553 -0.0162 42  PHE A CD2 
605  C CE1 . PHE A 39  ? 0.3873 0.4145 0.2975 0.0640  -0.0526 -0.0394 42  PHE A CE1 
606  C CE2 . PHE A 39  ? 0.4385 0.4481 0.2805 0.0660  -0.0543 -0.0300 42  PHE A CE2 
607  C CZ  . PHE A 39  ? 0.4629 0.4906 0.3420 0.0671  -0.0527 -0.0420 42  PHE A CZ  
617  N N   . TYR A 40  ? 0.3742 0.3094 0.2290 0.0379  -0.0486 0.0249  43  TYR A N   
618  C CA  . TYR A 40  ? 0.3818 0.2993 0.2422 0.0359  -0.0516 0.0321  43  TYR A CA  
619  C C   . TYR A 40  ? 0.3732 0.3007 0.2538 0.0227  -0.0389 0.0341  43  TYR A C   
620  O O   . TYR A 40  ? 0.3625 0.2898 0.2651 0.0229  -0.0416 0.0331  43  TYR A O   
621  C CB  . TYR A 40  ? 0.4233 0.3076 0.2450 0.0367  -0.0558 0.0445  43  TYR A CB  
622  C CG  . TYR A 40  ? 0.4317 0.3022 0.2440 0.0536  -0.0744 0.0422  43  TYR A CG  
623  C CD1 . TYR A 40  ? 0.4868 0.3514 0.3194 0.0606  -0.0841 0.0398  43  TYR A CD1 
624  C CD2 . TYR A 40  ? 0.4838 0.3520 0.2708 0.0621  -0.0813 0.0404  43  TYR A CD2 
625  C CE1 . TYR A 40  ? 0.5003 0.3561 0.3278 0.0771  -0.1019 0.0356  43  TYR A CE1 
626  C CE2 . TYR A 40  ? 0.5341 0.3914 0.3122 0.0796  -0.1008 0.0369  43  TYR A CE2 
627  C CZ  . TYR A 40  ? 0.5244 0.3780 0.3273 0.0863  -0.1103 0.0338  43  TYR A CZ  
628  O OH  . TYR A 40  ? 0.6118 0.4589 0.4084 0.1051  -0.1307 0.0279  43  TYR A OH  
638  N N   . ALA A 41  ? 0.3564 0.2935 0.2289 0.0108  -0.0248 0.0365  44  ALA A N   
639  C CA  . ALA A 41  ? 0.3354 0.2854 0.2298 -0.0012 -0.0141 0.0365  44  ALA A CA  
640  C C   . ALA A 41  ? 0.3402 0.3132 0.2702 0.0043  -0.0166 0.0265  44  ALA A C   
641  O O   . ALA A 41  ? 0.3230 0.2971 0.2724 0.0022  -0.0172 0.0266  44  ALA A O   
642  C CB  . ALA A 41  ? 0.3526 0.3146 0.2357 -0.0138 0.0011  0.0376  44  ALA A CB  
648  N N   . ILE A 42  ? 0.2974 0.2877 0.2359 0.0117  -0.0180 0.0175  45  ILE A N   
649  C CA  . ILE A 42  ? 0.2956 0.3041 0.2656 0.0167  -0.0196 0.0087  45  ILE A CA  
650  C C   . ILE A 42  ? 0.2809 0.2787 0.2640 0.0230  -0.0294 0.0084  45  ILE A C   
651  O O   . ILE A 42  ? 0.2884 0.2912 0.2921 0.0219  -0.0287 0.0073  45  ILE A O   
652  C CB  . ILE A 42  ? 0.2751 0.2979 0.2477 0.0242  -0.0205 -0.0013 45  ILE A CB  
653  C CG1 . ILE A 42  ? 0.3025 0.3415 0.2672 0.0186  -0.0093 -0.0037 45  ILE A CG1 
654  C CG2 . ILE A 42  ? 0.2928 0.3251 0.2955 0.0307  -0.0244 -0.0092 45  ILE A CG2 
655  C CD1 . ILE A 42  ? 0.3831 0.4327 0.3433 0.0267  -0.0106 -0.0139 45  ILE A CD1 
667  N N   . THR A 43  ? 0.2756 0.2597 0.2468 0.0302  -0.0390 0.0085  46  THR A N   
668  C CA  . THR A 43  ? 0.2848 0.2643 0.2719 0.0375  -0.0486 0.0045  46  THR A CA  
669  C C   . THR A 43  ? 0.3597 0.3264 0.3487 0.0340  -0.0491 0.0109  46  THR A C   
670  O O   . THR A 43  ? 0.3478 0.3173 0.3573 0.0365  -0.0518 0.0070  46  THR A O   
671  C CB  . THR A 43  ? 0.3125 0.2867 0.2892 0.0474  -0.0596 -0.0003 46  THR A CB  
672  O OG1 . THR A 43  ? 0.3105 0.2974 0.2850 0.0497  -0.0582 -0.0074 46  THR A OG1 
673  C CG2 . THR A 43  ? 0.3908 0.3679 0.3916 0.0540  -0.0681 -0.0082 46  THR A CG2 
681  N N   . THR A 44  ? 0.3039 0.2559 0.2719 0.0272  -0.0453 0.0203  47  THR A N   
682  C CA  . THR A 44  ? 0.3037 0.2413 0.2728 0.0237  -0.0457 0.0254  47  THR A CA  
683  C C   . THR A 44  ? 0.3020 0.2529 0.2897 0.0148  -0.0370 0.0248  47  THR A C   
684  O O   . THR A 44  ? 0.2917 0.2400 0.2922 0.0146  -0.0383 0.0239  47  THR A O   
685  C CB  . THR A 44  ? 0.3097 0.2230 0.2483 0.0186  -0.0445 0.0356  47  THR A CB  
686  O OG1 . THR A 44  ? 0.3610 0.2609 0.2796 0.0297  -0.0551 0.0362  47  THR A OG1 
687  C CG2 . THR A 44  ? 0.3567 0.2513 0.2961 0.0156  -0.0460 0.0398  47  THR A CG2 
695  N N   A LEU A 45  ? 0.2628 0.2296 0.2525 0.0084  -0.0284 0.0240  48  LEU A N   
696  N N   B LEU A 45  ? 0.2631 0.2302 0.2532 0.0086  -0.0286 0.0238  48  LEU A N   
697  C CA  A LEU A 45  ? 0.2609 0.2433 0.2683 0.0021  -0.0221 0.0220  48  LEU A CA  
698  C CA  B LEU A 45  ? 0.2629 0.2449 0.2701 0.0021  -0.0221 0.0221  48  LEU A CA  
699  C C   A LEU A 45  ? 0.2497 0.2403 0.2784 0.0090  -0.0259 0.0166  48  LEU A C   
700  C C   B LEU A 45  ? 0.2531 0.2456 0.2826 0.0091  -0.0254 0.0162  48  LEU A C   
701  O O   A LEU A 45  ? 0.2460 0.2399 0.2853 0.0059  -0.0242 0.0166  48  LEU A O   
702  O O   B LEU A 45  ? 0.2506 0.2493 0.2922 0.0061  -0.0232 0.0156  48  LEU A O   
703  C CB  A LEU A 45  ? 0.2627 0.2641 0.2704 -0.0031 -0.0137 0.0197  48  LEU A CB  
704  C CB  B LEU A 45  ? 0.2504 0.2489 0.2545 -0.0045 -0.0133 0.0209  48  LEU A CB  
705  C CG  A LEU A 45  ? 0.2769 0.2747 0.2685 -0.0155 -0.0053 0.0248  48  LEU A CG  
706  C CG  B LEU A 45  ? 0.2718 0.2906 0.2929 -0.0104 -0.0071 0.0176  48  LEU A CG  
707  C CD1 A LEU A 45  ? 0.3399 0.3611 0.3341 -0.0189 0.0032  0.0199  48  LEU A CD1 
708  C CD1 B LEU A 45  ? 0.2511 0.2610 0.2703 -0.0208 -0.0046 0.0216  48  LEU A CD1 
709  C CD2 A LEU A 45  ? 0.3089 0.3063 0.3088 -0.0255 -0.0019 0.0264  48  LEU A CD2 
710  C CD2 B LEU A 45  ? 0.2372 0.2761 0.2580 -0.0145 0.0010  0.0137  48  LEU A CD2 
733  N N   . VAL A 46  ? 0.2303 0.2242 0.2652 0.0177  -0.0305 0.0114  49  VAL A N   
734  C CA  . VAL A 46  ? 0.2317 0.2323 0.2860 0.0221  -0.0318 0.0065  49  VAL A CA  
735  C C   . VAL A 46  ? 0.2224 0.2140 0.2830 0.0221  -0.0342 0.0075  49  VAL A C   
736  O O   . VAL A 46  ? 0.2175 0.2139 0.2875 0.0197  -0.0308 0.0078  49  VAL A O   
737  C CB  . VAL A 46  ? 0.2203 0.2239 0.2784 0.0292  -0.0357 0.0000  49  VAL A CB  
738  C CG1 . VAL A 46  ? 0.2455 0.2500 0.3225 0.0323  -0.0369 -0.0048 49  VAL A CG1 
739  C CG2 . VAL A 46  ? 0.2534 0.2687 0.3090 0.0301  -0.0322 -0.0032 49  VAL A CG2 
749  N N   . PRO A 47  ? 0.2140 0.1942 0.2705 0.0251  -0.0396 0.0075  50  PRO A N   
750  C CA  . PRO A 47  ? 0.2378 0.2123 0.3023 0.0252  -0.0406 0.0067  50  PRO A CA  
751  C C   . PRO A 47  ? 0.2543 0.2224 0.3115 0.0183  -0.0373 0.0118  50  PRO A C   
752  O O   . PRO A 47  ? 0.2374 0.2052 0.3023 0.0171  -0.0360 0.0104  50  PRO A O   
753  C CB  . PRO A 47  ? 0.2526 0.2181 0.3150 0.0327  -0.0491 0.0034  50  PRO A CB  
754  C CG  . PRO A 47  ? 0.2986 0.2579 0.3410 0.0341  -0.0523 0.0071  50  PRO A CG  
755  C CD  . PRO A 47  ? 0.2375 0.2107 0.2824 0.0307  -0.0463 0.0064  50  PRO A CD  
763  N N   . ALA A 48  ? 0.2140 0.1781 0.2569 0.0125  -0.0349 0.0168  51  ALA A N   
764  C CA  . ALA A 48  ? 0.2339 0.1928 0.2722 0.0039  -0.0312 0.0201  51  ALA A CA  
765  C C   . ALA A 48  ? 0.2164 0.1925 0.2676 0.0004  -0.0266 0.0176  51  ALA A C   
766  O O   . ALA A 48  ? 0.2281 0.2027 0.2832 -0.0026 -0.0260 0.0166  51  ALA A O   
767  C CB  . ALA A 48  ? 0.2536 0.2064 0.2745 -0.0040 -0.0274 0.0254  51  ALA A CB  
773  N N   . ILE A 49  ? 0.2143 0.2063 0.2716 0.0021  -0.0243 0.0159  52  ILE A N   
774  C CA  . ILE A 49  ? 0.1839 0.1909 0.2519 0.0017  -0.0220 0.0137  52  ILE A CA  
775  C C   . ILE A 49  ? 0.2083 0.2113 0.2836 0.0072  -0.0240 0.0122  52  ILE A C   
776  O O   . ILE A 49  ? 0.2118 0.2175 0.2896 0.0059  -0.0233 0.0117  52  ILE A O   
777  C CB  . ILE A 49  ? 0.1899 0.2112 0.2618 0.0051  -0.0204 0.0116  52  ILE A CB  
778  C CG1 . ILE A 49  ? 0.1963 0.2254 0.2620 -0.0022 -0.0161 0.0120  52  ILE A CG1 
779  C CG2 . ILE A 49  ? 0.2284 0.2625 0.3104 0.0087  -0.0204 0.0092  52  ILE A CG2 
780  C CD1 . ILE A 49  ? 0.2406 0.2841 0.3086 0.0022  -0.0140 0.0083  52  ILE A CD1 
792  N N   . ALA A 50  ? 0.2060 0.2036 0.2844 0.0126  -0.0260 0.0106  53  ALA A N   
793  C CA  . ALA A 50  ? 0.1986 0.1933 0.2847 0.0155  -0.0254 0.0085  53  ALA A CA  
794  C C   . ALA A 50  ? 0.2213 0.2089 0.3059 0.0133  -0.0256 0.0080  53  ALA A C   
795  O O   . ALA A 50  ? 0.2148 0.2037 0.3020 0.0130  -0.0229 0.0073  53  ALA A O   
796  C CB  . ALA A 50  ? 0.2185 0.2115 0.3117 0.0203  -0.0270 0.0048  53  ALA A CB  
802  N N   . PHE A 51  ? 0.2085 0.1870 0.2870 0.0121  -0.0285 0.0084  54  PHE A N   
803  C CA  . PHE A 51  ? 0.2049 0.1750 0.2815 0.0105  -0.0291 0.0069  54  PHE A CA  
804  C C   . PHE A 51  ? 0.2247 0.1999 0.2990 0.0049  -0.0262 0.0076  54  PHE A C   
805  O O   . PHE A 51  ? 0.2219 0.1969 0.2983 0.0052  -0.0247 0.0046  54  PHE A O   
806  C CB  . PHE A 51  ? 0.2340 0.1886 0.3000 0.0100  -0.0334 0.0088  54  PHE A CB  
807  C CG  . PHE A 51  ? 0.2474 0.1904 0.3093 0.0073  -0.0340 0.0073  54  PHE A CG  
808  C CD1 . PHE A 51  ? 0.3176 0.2554 0.3853 0.0128  -0.0360 0.0018  54  PHE A CD1 
809  C CD2 . PHE A 51  ? 0.2819 0.2205 0.3355 -0.0014 -0.0320 0.0101  54  PHE A CD2 
810  C CE1 . PHE A 51  ? 0.3245 0.2505 0.3878 0.0108  -0.0368 -0.0007 54  PHE A CE1 
811  C CE2 . PHE A 51  ? 0.3336 0.2596 0.3832 -0.0049 -0.0327 0.0076  54  PHE A CE2 
812  C CZ  . PHE A 51  ? 0.3252 0.2448 0.3794 0.0020  -0.0353 0.0022  54  PHE A CZ  
822  N N   . THR A 52  ? 0.2097 0.1913 0.2802 -0.0002 -0.0252 0.0101  55  THR A N   
823  C CA  . THR A 52  ? 0.2072 0.1968 0.2774 -0.0053 -0.0240 0.0086  55  THR A CA  
824  C C   . THR A 52  ? 0.2055 0.2041 0.2793 -0.0005 -0.0233 0.0077  55  THR A C   
825  O O   . THR A 52  ? 0.2071 0.2077 0.2786 -0.0018 -0.0234 0.0054  55  THR A O   
826  C CB  . THR A 52  ? 0.2293 0.2289 0.2986 -0.0121 -0.0227 0.0094  55  THR A CB  
827  O OG1 . THR A 52  ? 0.2519 0.2648 0.3259 -0.0078 -0.0220 0.0101  55  THR A OG1 
828  C CG2 . THR A 52  ? 0.2683 0.2531 0.3289 -0.0181 -0.0220 0.0120  55  THR A CG2 
836  N N   . MET A 53  ? 0.1835 0.1864 0.2609 0.0050  -0.0226 0.0095  56  MET A N   
837  C CA  . MET A 53  ? 0.1812 0.1875 0.2580 0.0093  -0.0216 0.0102  56  MET A CA  
838  C C   . MET A 53  ? 0.2010 0.1984 0.2769 0.0104  -0.0186 0.0094  56  MET A C   
839  O O   . MET A 53  ? 0.2015 0.1989 0.2711 0.0115  -0.0171 0.0100  56  MET A O   
840  C CB  . MET A 53  ? 0.2029 0.2141 0.2833 0.0143  -0.0219 0.0120  56  MET A CB  
841  C CG  . MET A 53  ? 0.2858 0.3115 0.3682 0.0141  -0.0241 0.0111  56  MET A CG  
842  S SD  . MET A 53  ? 0.2835 0.3221 0.3636 0.0138  -0.0274 0.0090  56  MET A SD  
843  C CE  . MET A 53  ? 0.3000 0.3376 0.3793 0.0023  -0.0266 0.0059  56  MET A CE  
853  N N   . TYR A 54  ? 0.2022 0.1932 0.2838 0.0108  -0.0175 0.0074  57  TYR A N   
854  C CA  . TYR A 54  ? 0.2044 0.1908 0.2880 0.0109  -0.0137 0.0041  57  TYR A CA  
855  C C   . TYR A 54  ? 0.2098 0.1949 0.2875 0.0085  -0.0140 0.0014  57  TYR A C   
856  O O   . TYR A 54  ? 0.2085 0.1934 0.2819 0.0083  -0.0097 -0.0001 57  TYR A O   
857  C CB  . TYR A 54  ? 0.1903 0.1740 0.2841 0.0129  -0.0146 -0.0001 57  TYR A CB  
858  C CG  . TYR A 54  ? 0.1939 0.1793 0.2957 0.0141  -0.0113 -0.0007 57  TYR A CG  
859  C CD1 . TYR A 54  ? 0.1999 0.1866 0.3042 0.0159  -0.0136 0.0011  57  TYR A CD1 
860  C CD2 . TYR A 54  ? 0.2259 0.2116 0.3333 0.0125  -0.0045 -0.0042 57  TYR A CD2 
861  C CE1 . TYR A 54  ? 0.2115 0.1976 0.3233 0.0160  -0.0101 -0.0005 57  TYR A CE1 
862  C CE2 . TYR A 54  ? 0.2180 0.2035 0.3332 0.0111  0.0002  -0.0052 57  TYR A CE2 
863  C CZ  . TYR A 54  ? 0.1911 0.1756 0.3085 0.0128  -0.0029 -0.0035 57  TYR A CZ  
864  O OH  . TYR A 54  ? 0.2196 0.2013 0.3442 0.0109  0.0014  -0.0050 57  TYR A OH  
874  N N   . LEU A 55  ? 0.2090 0.1917 0.2847 0.0060  -0.0181 0.0004  58  LEU A N   
875  C CA  . LEU A 55  ? 0.1959 0.1756 0.2665 0.0032  -0.0185 -0.0038 58  LEU A CA  
876  C C   . LEU A 55  ? 0.2143 0.2023 0.2772 0.0020  -0.0181 -0.0030 58  LEU A C   
877  O O   . LEU A 55  ? 0.2245 0.2118 0.2813 0.0018  -0.0163 -0.0070 58  LEU A O   
878  C CB  . LEU A 55  ? 0.2229 0.1947 0.2917 -0.0008 -0.0226 -0.0044 58  LEU A CB  
879  C CG  . LEU A 55  ? 0.2261 0.1924 0.2900 -0.0047 -0.0236 -0.0097 58  LEU A CG  
880  C CD1 . LEU A 55  ? 0.2957 0.2544 0.3619 0.0001  -0.0223 -0.0160 58  LEU A CD1 
881  C CD2 . LEU A 55  ? 0.2685 0.2237 0.3293 -0.0104 -0.0265 -0.0087 58  LEU A CD2 
893  N N   . SER A 56  ? 0.1872 0.1837 0.2494 0.0023  -0.0203 0.0009  59  SER A N   
894  C CA  . SER A 56  ? 0.1949 0.1997 0.2494 0.0036  -0.0221 0.0010  59  SER A CA  
895  C C   . SER A 56  ? 0.2370 0.2376 0.2828 0.0082  -0.0182 0.0035  59  SER A C   
896  O O   . SER A 56  ? 0.2408 0.2433 0.2753 0.0092  -0.0190 0.0022  59  SER A O   
897  C CB  . SER A 56  ? 0.2349 0.2512 0.2932 0.0051  -0.0258 0.0035  59  SER A CB  
898  O OG  . SER A 56  ? 0.2806 0.2953 0.3385 0.0114  -0.0245 0.0084  59  SER A OG  
904  N N   . MET A 57  ? 0.2135 0.2074 0.2632 0.0100  -0.0133 0.0066  60  MET A N   
905  C CA  . MET A 57  ? 0.2236 0.2108 0.2639 0.0117  -0.0069 0.0092  60  MET A CA  
906  C C   . MET A 57  ? 0.2240 0.2088 0.2626 0.0087  -0.0016 0.0033  60  MET A C   
907  O O   . MET A 57  ? 0.2602 0.2427 0.2835 0.0091  0.0021  0.0040  60  MET A O   
908  C CB  . MET A 57  ? 0.2327 0.2142 0.2811 0.0124  -0.0027 0.0124  60  MET A CB  
909  C CG  . MET A 57  ? 0.2186 0.2016 0.2672 0.0167  -0.0077 0.0172  60  MET A CG  
910  S SD  . MET A 57  ? 0.2799 0.2521 0.3339 0.0176  -0.0021 0.0205  60  MET A SD  
911  C CE  . MET A 57  ? 0.2830 0.2615 0.3556 0.0157  -0.0041 0.0149  60  MET A CE  
921  N N   . LEU A 58  ? 0.2293 0.2143 0.2801 0.0070  -0.0017 -0.0026 61  LEU A N   
922  C CA  . LEU A 58  ? 0.2293 0.2134 0.2806 0.0058  0.0026  -0.0104 61  LEU A CA  
923  C C   . LEU A 58  ? 0.2646 0.2502 0.3024 0.0050  0.0002  -0.0134 61  LEU A C   
924  O O   . LEU A 58  ? 0.2895 0.2750 0.3182 0.0047  0.0060  -0.0174 61  LEU A O   
925  C CB  . LEU A 58  ? 0.2541 0.2361 0.3205 0.0067  -0.0012 -0.0156 61  LEU A CB  
926  C CG  . LEU A 58  ? 0.2521 0.2332 0.3213 0.0076  0.0017  -0.0254 61  LEU A CG  
927  C CD1 . LEU A 58  ? 0.3370 0.3237 0.4116 0.0075  0.0121  -0.0286 61  LEU A CD1 
928  C CD2 . LEU A 58  ? 0.3171 0.2921 0.3970 0.0106  -0.0046 -0.0298 61  LEU A CD2 
940  N N   . LEU A 59  ? 0.2394 0.2275 0.2760 0.0039  -0.0080 -0.0131 62  LEU A N   
941  C CA  . LEU A 59  ? 0.2432 0.2344 0.2694 0.0023  -0.0114 -0.0189 62  LEU A CA  
942  C C   . LEU A 59  ? 0.2793 0.2758 0.2891 0.0051  -0.0128 -0.0149 62  LEU A C   
943  O O   . LEU A 59  ? 0.3507 0.3517 0.3504 0.0046  -0.0168 -0.0205 62  LEU A O   
944  C CB  . LEU A 59  ? 0.2659 0.2583 0.2994 -0.0022 -0.0188 -0.0217 62  LEU A CB  
945  C CG  . LEU A 59  ? 0.2617 0.2437 0.3057 -0.0041 -0.0189 -0.0242 62  LEU A CG  
946  C CD1 . LEU A 59  ? 0.3300 0.3097 0.3771 -0.0109 -0.0244 -0.0257 62  LEU A CD1 
947  C CD2 . LEU A 59  ? 0.3332 0.3077 0.3763 -0.0025 -0.0159 -0.0331 62  LEU A CD2 
959  N N   . GLY A 60  ? 0.3122 0.2728 0.2646 0.0042  0.0186  -0.0649 63  GLY A N   
960  C CA  . GLY A 60  ? 0.3416 0.3162 0.2821 0.0011  0.0177  -0.0618 63  GLY A CA  
961  C C   . GLY A 60  ? 0.3320 0.3118 0.2747 -0.0074 0.0074  -0.0582 63  GLY A C   
962  O O   . GLY A 60  ? 0.3786 0.3704 0.3115 -0.0075 0.0041  -0.0544 63  GLY A O   
966  N N   . TYR A 61  ? 0.2981 0.2707 0.2523 -0.0142 0.0022  -0.0588 64  TYR A N   
967  C CA  . TYR A 61  ? 0.2966 0.2813 0.2560 -0.0227 -0.0064 -0.0571 64  TYR A CA  
968  C C   . TYR A 61  ? 0.2855 0.2858 0.2559 -0.0191 -0.0067 -0.0452 64  TYR A C   
969  O O   . TYR A 61  ? 0.3086 0.3242 0.2776 -0.0195 -0.0134 -0.0437 64  TYR A O   
970  C CB  . TYR A 61  ? 0.3043 0.2760 0.2716 -0.0337 -0.0093 -0.0610 64  TYR A CB  
971  C CG  . TYR A 61  ? 0.2872 0.2775 0.2631 -0.0449 -0.0167 -0.0618 64  TYR A CG  
972  C CD1 . TYR A 61  ? 0.3676 0.3628 0.3353 -0.0537 -0.0232 -0.0730 64  TYR A CD1 
973  C CD2 . TYR A 61  ? 0.2934 0.2973 0.2848 -0.0455 -0.0167 -0.0533 64  TYR A CD2 
974  C CE1 . TYR A 61  ? 0.4123 0.4333 0.3916 -0.0643 -0.0305 -0.0760 64  TYR A CE1 
975  C CE2 . TYR A 61  ? 0.3092 0.3365 0.3106 -0.0545 -0.0228 -0.0560 64  TYR A CE2 
976  C CZ  . TYR A 61  ? 0.3827 0.4201 0.3796 -0.0630 -0.0292 -0.0666 64  TYR A CZ  
977  O OH  . TYR A 61  ? 0.4519 0.5201 0.4628 -0.0721 -0.0355 -0.0711 64  TYR A OH  
987  N N   . GLY A 62  ? 0.2660 0.2624 0.2459 -0.0146 -0.0008 -0.0379 65  GLY A N   
988  C CA  . GLY A 62  ? 0.2772 0.2830 0.2683 -0.0122 -0.0014 -0.0274 65  GLY A CA  
989  C C   . GLY A 62  ? 0.2711 0.2802 0.2523 -0.0064 0.0019  -0.0208 65  GLY A C   
990  O O   . GLY A 62  ? 0.2724 0.2818 0.2612 -0.0045 0.0038  -0.0126 65  GLY A O   
994  N N   . LEU A 63  ? 0.3189 0.3277 0.2809 -0.0046 0.0029  -0.0243 66  LEU A N   
995  C CA  . LEU A 63  ? 0.3076 0.3154 0.2536 -0.0007 0.0073  -0.0167 66  LEU A CA  
996  C C   . LEU A 63  ? 0.3705 0.3827 0.2982 0.0024  -0.0021 -0.0167 66  LEU A C   
997  O O   . LEU A 63  ? 0.3924 0.4102 0.3149 0.0007  -0.0088 -0.0268 66  LEU A O   
998  C CB  . LEU A 63  ? 0.3652 0.3701 0.3019 0.0000  0.0181  -0.0213 66  LEU A CB  
999  C CG  . LEU A 63  ? 0.3458 0.3494 0.2619 0.0011  0.0263  -0.0147 66  LEU A CG  
1000 C CD1 . LEU A 63  ? 0.4222 0.4237 0.3471 -0.0017 0.0327  -0.0030 66  LEU A CD1 
1001 C CD2 . LEU A 63  ? 0.4745 0.4810 0.3851 0.0022  0.0371  -0.0235 66  LEU A CD2 
1013 N N   . THR A 64  ? 0.3265 0.3350 0.2422 0.0074  -0.0043 -0.0062 67  THR A N   
1014 C CA  . THR A 64  ? 0.3351 0.3455 0.2270 0.0139  -0.0137 -0.0051 67  THR A CA  
1015 C C   . THR A 64  ? 0.3669 0.3611 0.2320 0.0170  -0.0070 0.0069  67  THR A C   
1016 O O   . THR A 64  ? 0.4153 0.3998 0.2862 0.0124  0.0041  0.0142  67  THR A O   
1017 C CB  . THR A 64  ? 0.3603 0.3821 0.2633 0.0197  -0.0272 -0.0046 67  THR A CB  
1018 O OG1 . THR A 64  ? 0.4329 0.4639 0.3173 0.0265  -0.0391 -0.0085 67  THR A OG1 
1019 C CG2 . THR A 64  ? 0.3723 0.3820 0.2787 0.0249  -0.0261 0.0076  67  THR A CG2 
1027 N N   . MET A 65  ? 0.4144 0.4047 0.2490 0.0238  -0.0136 0.0094  68  MET A N   
1028 C CA  . MET A 65  ? 0.4637 0.4332 0.2663 0.0259  -0.0071 0.0230  68  MET A CA  
1029 C C   . MET A 65  ? 0.5372 0.4954 0.3265 0.0374  -0.0203 0.0327  68  MET A C   
1030 O O   . MET A 65  ? 0.5419 0.5137 0.3297 0.0473  -0.0363 0.0267  68  MET A O   
1031 C CB  . MET A 65  ? 0.5187 0.4877 0.2881 0.0276  -0.0056 0.0197  68  MET A CB  
1032 C CG  . MET A 65  ? 0.6232 0.6011 0.3987 0.0195  0.0079  0.0087  68  MET A CG  
1033 S SD  . MET A 65  ? 0.6714 0.6438 0.4607 0.0090  0.0303  0.0161  68  MET A SD  
1034 C CE  . MET A 65  ? 0.8389 0.8284 0.6480 0.0059  0.0399  -0.0018 68  MET A CE  
1044 N N   . VAL A 66  ? 0.4844 0.4184 0.2647 0.0364  -0.0144 0.0465  69  VAL A N   
1045 C CA  . VAL A 66  ? 0.4651 0.3810 0.2301 0.0494  -0.0268 0.0560  69  VAL A CA  
1046 C C   . VAL A 66  ? 0.5454 0.4276 0.2646 0.0498  -0.0212 0.0714  69  VAL A C   
1047 O O   . VAL A 66  ? 0.5691 0.4363 0.2835 0.0355  -0.0042 0.0787  69  VAL A O   
1048 C CB  . VAL A 66  ? 0.4670 0.3765 0.2587 0.0478  -0.0259 0.0583  69  VAL A CB  
1049 C CG1 . VAL A 66  ? 0.5868 0.4734 0.3573 0.0648  -0.0397 0.0672  69  VAL A CG1 
1050 C CG2 . VAL A 66  ? 0.4539 0.3952 0.2880 0.0458  -0.0294 0.0444  69  VAL A CG2 
1060 N N   . PRO A 67  ? 0.5835 0.4526 0.2669 0.0654  -0.0350 0.0773  70  PRO A N   
1061 C CA  . PRO A 67  ? 0.6148 0.4453 0.2478 0.0659  -0.0299 0.0942  70  PRO A CA  
1062 C C   . PRO A 67  ? 0.8064 0.5987 0.4302 0.0686  -0.0309 0.1079  70  PRO A C   
1063 O O   . PRO A 67  ? 0.8173 0.6084 0.4498 0.0851  -0.0469 0.1060  70  PRO A O   
1064 C CB  . PRO A 67  ? 0.6942 0.5282 0.2948 0.0851  -0.0484 0.0931  70  PRO A CB  
1065 C CG  . PRO A 67  ? 0.6768 0.5435 0.3145 0.0985  -0.0669 0.0790  70  PRO A CG  
1066 C CD  . PRO A 67  ? 0.5831 0.4772 0.2719 0.0824  -0.0559 0.0668  70  PRO A CD  
1074 N N   . PHE A 68  ? 0.6992 0.4633 0.3096 0.0510  -0.0128 0.1197  71  PHE A N   
1075 C CA  . PHE A 68  ? 0.7292 0.4451 0.3167 0.0514  -0.0131 0.1350  71  PHE A CA  
1076 C C   . PHE A 68  ? 0.8040 0.4909 0.3600 0.0296  0.0082  0.1493  71  PHE A C   
1077 O O   . PHE A 68  ? 0.8671 0.5799 0.4358 0.0129  0.0252  0.1441  71  PHE A O   
1078 C CB  . PHE A 68  ? 0.7902 0.5086 0.4174 0.0504  -0.0159 0.1290  71  PHE A CB  
1079 C CG  . PHE A 68  ? 0.7022 0.4483 0.3736 0.0289  0.0002  0.1200  71  PHE A CG  
1080 C CD1 . PHE A 68  ? 0.7439 0.4698 0.4109 0.0061  0.0186  0.1284  71  PHE A CD1 
1081 C CD2 . PHE A 68  ? 0.5682 0.3579 0.2823 0.0311  -0.0033 0.1039  71  PHE A CD2 
1082 C CE1 . PHE A 68  ? 0.6801 0.4352 0.3898 -0.0107 0.0309  0.1188  71  PHE A CE1 
1083 C CE2 . PHE A 68  ? 0.5928 0.4060 0.3451 0.0145  0.0095  0.0958  71  PHE A CE2 
1084 C CZ  . PHE A 68  ? 0.6386 0.4350 0.3884 -0.0055 0.0262  0.1033  71  PHE A CZ  
1094 N N   . GLY A 69  ? 1.0136 0.6513 0.5337 0.0297  0.0074  0.1650  72  GLY A N   
1095 C CA  . GLY A 69  ? 0.9514 0.5716 0.4527 0.0064  0.0277  0.1756  72  GLY A CA  
1096 C C   . GLY A 69  ? 1.0932 0.7297 0.5689 0.0039  0.0359  0.1768  72  GLY A C   
1097 O O   . GLY A 69  ? 1.0366 0.6792 0.5095 -0.0184 0.0577  0.1803  72  GLY A O   
1101 N N   . GLY A 70  ? 0.9537 0.6021 0.4133 0.0262  0.0187  0.1722  73  GLY A N   
1102 C CA  . GLY A 70  ? 0.9306 0.5913 0.3623 0.0251  0.0245  0.1727  73  GLY A CA  
1103 C C   . GLY A 70  ? 1.0368 0.7363 0.4842 0.0145  0.0390  0.1606  73  GLY A C   
1104 O O   . GLY A 70  ? 1.1409 0.8519 0.5660 0.0109  0.0475  0.1597  73  GLY A O   
1108 N N   . GLU A 71  ? 0.8918 0.6173 0.3851 0.0103  0.0410  0.1482  74  GLU A N   
1109 C CA  . GLU A 71  ? 0.8638 0.6362 0.3934 0.0013  0.0528  0.1308  74  GLU A CA  
1110 C C   . GLU A 71  ? 0.7480 0.5540 0.3190 0.0156  0.0344  0.1126  74  GLU A C   
1111 O O   . GLU A 71  ? 0.8118 0.6105 0.3940 0.0282  0.0170  0.1129  74  GLU A O   
1112 C CB  . GLU A 71  ? 0.8620 0.6450 0.4276 -0.0212 0.0736  0.1295  74  GLU A CB  
1113 C CG  . GLU A 71  ? 1.0228 0.7707 0.5543 -0.0405 0.0924  0.1484  74  GLU A CG  
1114 C CD  . GLU A 71  ? 1.2762 1.0497 0.8424 -0.0646 0.1163  0.1432  74  GLU A CD  
1115 O OE1 . GLU A 71  ? 1.2799 1.0947 0.8968 -0.0632 0.1160  0.1256  74  GLU A OE1 
1116 O OE2 . GLU A 71  ? 1.3594 1.1165 0.9096 -0.0837 0.1329  0.1551  74  GLU A OE2 
1119 N N   . GLN A 72  ? 0.6819 0.5243 0.2753 0.0132  0.0392  0.0959  75  GLN A N   
1120 C CA  . GLN A 72  ? 0.6054 0.4790 0.2458 0.0193  0.0274  0.0785  75  GLN A CA  
1121 C C   . GLN A 72  ? 0.6219 0.5104 0.3075 0.0056  0.0408  0.0731  75  GLN A C   
1122 O O   . GLN A 72  ? 0.7262 0.6288 0.4196 -0.0054 0.0583  0.0683  75  GLN A O   
1123 C CB  . GLN A 72  ? 0.7817 0.6804 0.4186 0.0249  0.0224  0.0628  75  GLN A CB  
1124 C CG  . GLN A 72  ? 1.0209 0.9062 0.6068 0.0365  0.0119  0.0681  75  GLN A CG  
1125 C CD  . GLN A 72  ? 0.9463 0.8322 0.5320 0.0539  -0.0138 0.0671  75  GLN A CD  
1126 O OE1 . GLN A 72  ? 0.9426 0.8491 0.5698 0.0563  -0.0236 0.0568  75  GLN A OE1 
1127 N NE2 . GLN A 72  ? 1.0996 0.9632 0.6375 0.0667  -0.0247 0.0784  75  GLN A NE2 
1136 N N   . ASN A 73  ? 0.5234 0.4105 0.2383 0.0075  0.0325  0.0731  76  ASN A N   
1137 C CA  . ASN A 73  ? 0.4957 0.3931 0.2476 -0.0051 0.0444  0.0700  76  ASN A CA  
1138 C C   . ASN A 73  ? 0.4624 0.3883 0.2554 -0.0016 0.0377  0.0540  76  ASN A C   
1139 O O   . ASN A 73  ? 0.4361 0.3666 0.2395 0.0082  0.0221  0.0495  76  ASN A O   
1140 C CB  . ASN A 73  ? 0.5461 0.4183 0.3012 -0.0074 0.0410  0.0811  76  ASN A CB  
1141 C CG  . ASN A 73  ? 0.6004 0.4355 0.3127 -0.0126 0.0473  0.0985  76  ASN A CG  
1142 O OD1 . ASN A 73  ? 0.7134 0.5435 0.4223 -0.0302 0.0656  0.1042  76  ASN A OD1 
1143 N ND2 . ASN A 73  ? 0.6359 0.4462 0.3121 0.0022  0.0332  0.1068  76  ASN A ND2 
1150 N N   . PRO A 74  ? 0.4375 0.3828 0.2579 -0.0097 0.0494  0.0453  77  PRO A N   
1151 C CA  . PRO A 74  ? 0.4001 0.3655 0.2539 -0.0065 0.0434  0.0317  77  PRO A CA  
1152 C C   . PRO A 74  ? 0.4342 0.3978 0.3154 -0.0073 0.0376  0.0337  77  PRO A C   
1153 O O   . PRO A 74  ? 0.4837 0.4429 0.3756 -0.0155 0.0457  0.0391  77  PRO A O   
1154 C CB  . PRO A 74  ? 0.4559 0.4381 0.3224 -0.0123 0.0585  0.0233  77  PRO A CB  
1155 C CG  . PRO A 74  ? 0.5902 0.5665 0.4413 -0.0223 0.0744  0.0333  77  PRO A CG  
1156 C CD  . PRO A 74  ? 0.5255 0.4759 0.3389 -0.0209 0.0694  0.0471  77  PRO A CD  
1164 N N   . ILE A 75  ? 0.3338 0.3012 0.2248 0.0004  0.0233  0.0294  78  ILE A N   
1165 C CA  . ILE A 75  ? 0.3151 0.2822 0.2296 0.0006  0.0181  0.0302  78  ILE A CA  
1166 C C   . ILE A 75  ? 0.3164 0.3007 0.2559 0.0012  0.0142  0.0189  78  ILE A C   
1167 O O   . ILE A 75  ? 0.3135 0.3063 0.2509 0.0051  0.0060  0.0121  78  ILE A O   
1168 C CB  . ILE A 75  ? 0.3318 0.2866 0.2324 0.0103  0.0054  0.0365  78  ILE A CB  
1169 C CG1 . ILE A 75  ? 0.3994 0.3271 0.2681 0.0104  0.0085  0.0498  78  ILE A CG1 
1170 C CG2 . ILE A 75  ? 0.3515 0.3102 0.2779 0.0120  -0.0002 0.0342  78  ILE A CG2 
1171 C CD1 . ILE A 75  ? 0.4512 0.3616 0.3259 -0.0006 0.0182  0.0574  78  ILE A CD1 
1183 N N   . TYR A 76  ? 0.2634 0.2521 0.2255 -0.0035 0.0195  0.0167  79  TYR A N   
1184 C CA  . TYR A 76  ? 0.2464 0.2450 0.2289 -0.0031 0.0159  0.0082  79  TYR A CA  
1185 C C   . TYR A 76  ? 0.2593 0.2588 0.2514 -0.0004 0.0066  0.0094  79  TYR A C   
1186 O O   . TYR A 76  ? 0.2869 0.2836 0.2912 -0.0012 0.0068  0.0124  79  TYR A O   
1187 C CB  . TYR A 76  ? 0.2843 0.2875 0.2846 -0.0064 0.0240  0.0056  79  TYR A CB  
1188 C CG  . TYR A 76  ? 0.2539 0.2630 0.2499 -0.0063 0.0326  -0.0005 79  TYR A CG  
1189 C CD1 . TYR A 76  ? 0.2713 0.2810 0.2659 -0.0029 0.0303  -0.0100 79  TYR A CD1 
1190 C CD2 . TYR A 76  ? 0.3257 0.3392 0.3180 -0.0101 0.0437  0.0023  79  TYR A CD2 
1191 C CE1 . TYR A 76  ? 0.2524 0.2661 0.2418 -0.0003 0.0382  -0.0175 79  TYR A CE1 
1192 C CE2 . TYR A 76  ? 0.3262 0.3491 0.3147 -0.0083 0.0529  -0.0051 79  TYR A CE2 
1193 C CZ  . TYR A 76  ? 0.2645 0.2866 0.2516 -0.0019 0.0492  -0.0154 79  TYR A CZ  
1194 O OH  . TYR A 76  ? 0.3057 0.3356 0.2877 0.0020  0.0581  -0.0242 79  TYR A OH  
1204 N N   . TRP A 77  ? 0.2454 0.2516 0.2330 0.0028  -0.0017 0.0057  80  TRP A N   
1205 C CA  . TRP A 77  ? 0.2344 0.2470 0.2316 0.0062  -0.0093 0.0058  80  TRP A CA  
1206 C C   . TRP A 77  ? 0.2235 0.2420 0.2388 0.0015  -0.0084 0.0013  80  TRP A C   
1207 O O   . TRP A 77  ? 0.2194 0.2428 0.2438 0.0034  -0.0117 0.0020  80  TRP A O   
1208 C CB  . TRP A 77  ? 0.2716 0.2969 0.2610 0.0112  -0.0188 0.0020  80  TRP A CB  
1209 C CG  . TRP A 77  ? 0.2544 0.2898 0.2452 0.0043  -0.0196 -0.0077 80  TRP A CG  
1210 C CD1 . TRP A 77  ? 0.3253 0.3580 0.3001 0.0034  -0.0190 -0.0112 80  TRP A CD1 
1211 C CD2 . TRP A 77  ? 0.2344 0.2802 0.2402 -0.0036 -0.0208 -0.0151 80  TRP A CD2 
1212 N NE1 . TRP A 77  ? 0.3354 0.3752 0.3152 -0.0043 -0.0210 -0.0217 80  TRP A NE1 
1213 C CE2 . TRP A 77  ? 0.2963 0.3428 0.2948 -0.0095 -0.0218 -0.0233 80  TRP A CE2 
1214 C CE3 . TRP A 77  ? 0.2810 0.3332 0.3031 -0.0071 -0.0204 -0.0153 80  TRP A CE3 
1215 C CZ2 . TRP A 77  ? 0.3589 0.4089 0.3657 -0.0204 -0.0224 -0.0312 80  TRP A CZ2 
1216 C CZ3 . TRP A 77  ? 0.3287 0.3870 0.3584 -0.0182 -0.0202 -0.0223 80  TRP A CZ3 
1217 C CH2 . TRP A 77  ? 0.3203 0.3756 0.3422 -0.0252 -0.0213 -0.0298 80  TRP A CH2 
1228 N N   . ALA A 78  ? 0.2099 0.2257 0.2282 -0.0038 -0.0038 -0.0034 81  ALA A N   
1229 C CA  . ALA A 78  ? 0.2133 0.2290 0.2435 -0.0077 -0.0038 -0.0061 81  ALA A CA  
1230 C C   . ALA A 78  ? 0.2008 0.2126 0.2403 -0.0058 -0.0021 -0.0016 81  ALA A C   
1231 O O   . ALA A 78  ? 0.2407 0.2533 0.2868 -0.0078 -0.0035 -0.0021 81  ALA A O   
1232 C CB  . ALA A 78  ? 0.2868 0.2937 0.3137 -0.0111 -0.0006 -0.0120 81  ALA A CB  
1238 N N   . ARG A 79  ? 0.2136 0.2215 0.2528 -0.0034 0.0008  0.0027  82  ARG A N   
1239 C CA  . ARG A 79  ? 0.2166 0.2219 0.2651 -0.0028 0.0010  0.0055  82  ARG A CA  
1240 C C   . ARG A 79  ? 0.2175 0.2254 0.2674 -0.0002 -0.0044 0.0065  82  ARG A C   
1241 O O   . ARG A 79  ? 0.2104 0.2182 0.2670 -0.0002 -0.0054 0.0059  82  ARG A O   
1242 C CB  . ARG A 79  ? 0.2313 0.2317 0.2777 -0.0040 0.0050  0.0097  82  ARG A CB  
1243 C CG  . ARG A 79  ? 0.2457 0.2497 0.2939 -0.0067 0.0124  0.0079  82  ARG A CG  
1244 C CD  . ARG A 79  ? 0.2510 0.2533 0.3017 -0.0119 0.0176  0.0118  82  ARG A CD  
1245 N NE  . ARG A 79  ? 0.2679 0.2788 0.3200 -0.0152 0.0269  0.0099  82  ARG A NE  
1246 C CZ  . ARG A 79  ? 0.2759 0.3000 0.3420 -0.0129 0.0298  0.0033  82  ARG A CZ  
1247 N NH1 . ARG A 79  ? 0.3138 0.3402 0.3919 -0.0081 0.0236  -0.0003 82  ARG A NH1 
1248 N NH2 . ARG A 79  ? 0.3670 0.4018 0.4332 -0.0142 0.0391  0.0003  82  ARG A NH2 
1262 N N   . TYR A 80  ? 0.2173 0.2287 0.2599 0.0035  -0.0080 0.0071  83  TYR A N   
1263 C CA  . TYR A 80  ? 0.2146 0.2316 0.2598 0.0088  -0.0127 0.0065  83  TYR A CA  
1264 C C   . TYR A 80  ? 0.1859 0.2175 0.2385 0.0054  -0.0131 0.0019  83  TYR A C   
1265 O O   . TYR A 80  ? 0.2189 0.2566 0.2762 0.0080  -0.0141 0.0007  83  TYR A O   
1266 C CB  . TYR A 80  ? 0.2304 0.2477 0.2652 0.0174  -0.0179 0.0080  83  TYR A CB  
1267 C CG  . TYR A 80  ? 0.2322 0.2287 0.2544 0.0179  -0.0160 0.0145  83  TYR A CG  
1268 C CD1 . TYR A 80  ? 0.2559 0.2359 0.2752 0.0202  -0.0166 0.0177  83  TYR A CD1 
1269 C CD2 . TYR A 80  ? 0.2567 0.2490 0.2683 0.0145  -0.0126 0.0170  83  TYR A CD2 
1270 C CE1 . TYR A 80  ? 0.2967 0.2561 0.3042 0.0158  -0.0128 0.0241  83  TYR A CE1 
1271 C CE2 . TYR A 80  ? 0.2940 0.2683 0.2934 0.0114  -0.0078 0.0235  83  TYR A CE2 
1272 C CZ  . TYR A 80  ? 0.3051 0.2631 0.3029 0.0112  -0.0079 0.0274  83  TYR A CZ  
1273 O OH  . TYR A 80  ? 0.3319 0.2726 0.3178 0.0040  -0.0014 0.0340  83  TYR A OH  
1283 N N   . ALA A 81  ? 0.1855 0.2225 0.2378 -0.0012 -0.0118 -0.0012 84  ALA A N   
1284 C CA  . ALA A 81  ? 0.1727 0.2199 0.2304 -0.0085 -0.0108 -0.0048 84  ALA A CA  
1285 C C   . ALA A 81  ? 0.1870 0.2211 0.2451 -0.0116 -0.0073 -0.0023 84  ALA A C   
1286 O O   . ALA A 81  ? 0.2392 0.2800 0.2993 -0.0146 -0.0061 -0.0026 84  ALA A O   
1287 C CB  . ALA A 81  ? 0.2314 0.2808 0.2857 -0.0162 -0.0109 -0.0093 84  ALA A CB  
1293 N N   . ASP A 82  ? 0.1841 0.2033 0.2403 -0.0098 -0.0061 -0.0001 85  ASP A N   
1294 C CA  . ASP A 82  ? 0.1963 0.2054 0.2528 -0.0092 -0.0054 0.0019  85  ASP A CA  
1295 C C   . ASP A 82  ? 0.1780 0.1913 0.2375 -0.0046 -0.0073 0.0033  85  ASP A C   
1296 O O   . ASP A 82  ? 0.1929 0.2076 0.2498 -0.0060 -0.0070 0.0036  85  ASP A O   
1297 C CB  . ASP A 82  ? 0.2036 0.2042 0.2618 -0.0059 -0.0045 0.0020  85  ASP A CB  
1298 C CG  . ASP A 82  ? 0.2194 0.2138 0.2808 -0.0020 -0.0060 0.0029  85  ASP A CG  
1299 O OD1 . ASP A 82  ? 0.2266 0.2209 0.2872 -0.0009 -0.0084 0.0044  85  ASP A OD1 
1300 O OD2 . ASP A 82  ? 0.2179 0.2093 0.2823 0.0012  -0.0050 0.0012  85  ASP A OD2 
1305 N N   . TRP A 83  ? 0.1831 0.1969 0.2448 0.0001  -0.0089 0.0038  86  TRP A N   
1306 C CA  . TRP A 83  ? 0.1962 0.2080 0.2589 0.0043  -0.0114 0.0038  86  TRP A CA  
1307 C C   . TRP A 83  ? 0.1976 0.2199 0.2584 0.0076  -0.0122 0.0015  86  TRP A C   
1308 O O   . TRP A 83  ? 0.2052 0.2271 0.2643 0.0106  -0.0134 0.0000  86  TRP A O   
1309 C CB  . TRP A 83  ? 0.2067 0.2108 0.2692 0.0067  -0.0125 0.0051  86  TRP A CB  
1310 C CG  . TRP A 83  ? 0.1783 0.1779 0.2447 0.0025  -0.0098 0.0064  86  TRP A CG  
1311 C CD1 . TRP A 83  ? 0.2156 0.2176 0.2877 0.0009  -0.0086 0.0052  86  TRP A CD1 
1312 C CD2 . TRP A 83  ? 0.1910 0.1840 0.2555 0.0001  -0.0075 0.0089  86  TRP A CD2 
1313 N NE1 . TRP A 83  ? 0.2122 0.2155 0.2904 -0.0019 -0.0052 0.0051  86  TRP A NE1 
1314 C CE2 . TRP A 83  ? 0.2042 0.2018 0.2766 -0.0041 -0.0035 0.0080  86  TRP A CE2 
1315 C CE3 . TRP A 83  ? 0.2359 0.2188 0.2903 0.0018  -0.0082 0.0120  86  TRP A CE3 
1316 C CZ2 . TRP A 83  ? 0.2175 0.2132 0.2904 -0.0098 0.0018  0.0100  86  TRP A CZ2 
1317 C CZ3 . TRP A 83  ? 0.2423 0.2159 0.2920 -0.0038 -0.0038 0.0159  86  TRP A CZ3 
1318 C CH2 . TRP A 83  ? 0.2509 0.2330 0.3106 -0.0110 0.0022  0.0148  86  TRP A CH2 
1329 N N   . LEU A 84  ? 0.1660 0.2018 0.2278 0.0077  -0.0118 -0.0003 87  LEU A N   
1330 C CA  . LEU A 84  ? 0.1790 0.2330 0.2430 0.0109  -0.0116 -0.0042 87  LEU A CA  
1331 C C   . LEU A 84  ? 0.1856 0.2431 0.2477 0.0045  -0.0073 -0.0043 87  LEU A C   
1332 O O   . LEU A 84  ? 0.1984 0.2662 0.2598 0.0089  -0.0062 -0.0073 87  LEU A O   
1333 C CB  . LEU A 84  ? 0.2023 0.2756 0.2710 0.0093  -0.0123 -0.0072 87  LEU A CB  
1334 C CG  . LEU A 84  ? 0.2594 0.3593 0.3348 0.0130  -0.0118 -0.0129 87  LEU A CG  
1335 C CD1 . LEU A 84  ? 0.3795 0.4783 0.4529 0.0292  -0.0166 -0.0151 87  LEU A CD1 
1336 C CD2 . LEU A 84  ? 0.3340 0.4560 0.4163 0.0090  -0.0138 -0.0169 87  LEU A CD2 
1348 N N   . PHE A 85  ? 0.1931 0.2411 0.2516 -0.0051 -0.0045 -0.0012 88  PHE A N   
1349 C CA  . PHE A 85  ? 0.2131 0.2582 0.2638 -0.0111 -0.0006 0.0008  88  PHE A CA  
1350 C C   . PHE A 85  ? 0.2173 0.2432 0.2601 -0.0073 -0.0034 0.0041  88  PHE A C   
1351 O O   . PHE A 85  ? 0.2554 0.2805 0.2890 -0.0067 -0.0021 0.0048  88  PHE A O   
1352 C CB  . PHE A 85  ? 0.2677 0.3078 0.3145 -0.0240 0.0033  0.0025  88  PHE A CB  
1353 C CG  . PHE A 85  ? 0.2742 0.3390 0.3301 -0.0312 0.0059  -0.0024 88  PHE A CG  
1354 C CD1 . PHE A 85  ? 0.3242 0.4133 0.3840 -0.0349 0.0107  -0.0056 88  PHE A CD1 
1355 C CD2 . PHE A 85  ? 0.2638 0.3286 0.3242 -0.0324 0.0029  -0.0046 88  PHE A CD2 
1356 C CE1 . PHE A 85  ? 0.3493 0.4681 0.4216 -0.0409 0.0121  -0.0119 88  PHE A CE1 
1357 C CE2 . PHE A 85  ? 0.3672 0.4578 0.4368 -0.0384 0.0031  -0.0106 88  PHE A CE2 
1358 C CZ  . PHE A 85  ? 0.3441 0.4632 0.4215 -0.0418 0.0071  -0.0144 88  PHE A CZ  
1368 N N   . THR A 86  ? 0.2050 0.2195 0.2515 -0.0034 -0.0074 0.0049  89  THR A N   
1369 C CA  . THR A 86  ? 0.2051 0.2065 0.2466 0.0004  -0.0114 0.0067  89  THR A CA  
1370 C C   . THR A 86  ? 0.2254 0.2298 0.2688 0.0068  -0.0155 0.0036  89  THR A C   
1371 O O   . THR A 86  ? 0.2208 0.2199 0.2568 0.0098  -0.0192 0.0035  89  THR A O   
1372 C CB  . THR A 86  ? 0.1967 0.1889 0.2433 0.0019  -0.0135 0.0074  89  THR A CB  
1373 O OG1 . THR A 86  ? 0.2054 0.2038 0.2628 0.0031  -0.0136 0.0053  89  THR A OG1 
1374 C CG2 . THR A 86  ? 0.2327 0.2149 0.2725 -0.0035 -0.0104 0.0095  89  THR A CG2 
1382 N N   . THR A 87  ? 0.2134 0.2230 0.2635 0.0097  -0.0162 0.0006  90  THR A N   
1383 C CA  . THR A 87  ? 0.2170 0.2230 0.2665 0.0150  -0.0208 -0.0034 90  THR A CA  
1384 C C   . THR A 87  ? 0.2161 0.2279 0.2556 0.0188  -0.0199 -0.0065 90  THR A C   
1385 O O   . THR A 87  ? 0.2325 0.2387 0.2660 0.0217  -0.0243 -0.0095 90  THR A O   
1386 C CB  . THR A 87  ? 0.2190 0.2202 0.2737 0.0168  -0.0221 -0.0047 90  THR A CB  
1387 O OG1 . THR A 87  ? 0.2191 0.2279 0.2732 0.0197  -0.0196 -0.0046 90  THR A OG1 
1388 C CG2 . THR A 87  ? 0.2404 0.2367 0.3028 0.0116  -0.0217 -0.0020 90  THR A CG2 
1396 N N   . PRO A 88  ? 0.2077 0.2332 0.2454 0.0184  -0.0143 -0.0071 91  PRO A N   
1397 C CA  . PRO A 88  ? 0.2166 0.2503 0.2443 0.0216  -0.0118 -0.0106 91  PRO A CA  
1398 C C   . PRO A 88  ? 0.2530 0.2797 0.2673 0.0164  -0.0105 -0.0060 91  PRO A C   
1399 O O   . PRO A 88  ? 0.2679 0.2941 0.2696 0.0206  -0.0114 -0.0089 91  PRO A O   
1400 C CB  . PRO A 88  ? 0.2679 0.3248 0.3008 0.0210  -0.0049 -0.0130 91  PRO A CB  
1401 C CG  . PRO A 88  ? 0.3587 0.4157 0.4018 0.0149  -0.0048 -0.0092 91  PRO A CG  
1402 C CD  . PRO A 88  ? 0.2169 0.2538 0.2627 0.0157  -0.0108 -0.0062 91  PRO A CD  
1410 N N   . LEU A 89  ? 0.2465 0.2648 0.2597 0.0091  -0.0093 0.0006  92  LEU A N   
1411 C CA  . LEU A 89  ? 0.2443 0.2490 0.2398 0.0068  -0.0099 0.0061  92  LEU A CA  
1412 C C   . LEU A 89  ? 0.2722 0.2672 0.2646 0.0149  -0.0199 0.0039  92  LEU A C   
1413 O O   . LEU A 89  ? 0.2844 0.2740 0.2590 0.0181  -0.0225 0.0046  92  LEU A O   
1414 C CB  . LEU A 89  ? 0.2678 0.2593 0.2611 -0.0004 -0.0081 0.0128  92  LEU A CB  
1415 C CG  . LEU A 89  ? 0.2730 0.2727 0.2638 -0.0127 0.0021  0.0149  92  LEU A CG  
1416 C CD1 . LEU A 89  ? 0.3028 0.2855 0.2925 -0.0192 0.0022  0.0191  92  LEU A CD1 
1417 C CD2 . LEU A 89  ? 0.3604 0.3608 0.3314 -0.0186 0.0090  0.0182  92  LEU A CD2 
1429 N N   . LEU A 90  ? 0.2574 0.2520 0.2659 0.0178  -0.0257 0.0007  93  LEU A N   
1430 C CA  . LEU A 90  ? 0.2478 0.2385 0.2573 0.0232  -0.0355 -0.0032 93  LEU A CA  
1431 C C   . LEU A 90  ? 0.2403 0.2338 0.2417 0.0273  -0.0380 -0.0102 93  LEU A C   
1432 O O   . LEU A 90  ? 0.2684 0.2583 0.2581 0.0317  -0.0456 -0.0130 93  LEU A O   
1433 C CB  . LEU A 90  ? 0.2534 0.2465 0.2837 0.0219  -0.0385 -0.0056 93  LEU A CB  
1434 C CG  . LEU A 90  ? 0.2458 0.2364 0.2821 0.0209  -0.0375 -0.0008 93  LEU A CG  
1435 C CD1 . LEU A 90  ? 0.2838 0.2806 0.3400 0.0176  -0.0360 -0.0032 93  LEU A CD1 
1436 C CD2 . LEU A 90  ? 0.2780 0.2645 0.3086 0.0277  -0.0462 -0.0003 93  LEU A CD2 
1448 N N   . LEU A 91  ? 0.2508 0.2496 0.2562 0.0280  -0.0335 -0.0142 94  LEU A N   
1449 C CA  . LEU A 91  ? 0.2734 0.2728 0.2691 0.0339  -0.0354 -0.0223 94  LEU A CA  
1450 C C   . LEU A 91  ? 0.2852 0.2895 0.2597 0.0358  -0.0310 -0.0213 94  LEU A C   
1451 O O   . LEU A 91  ? 0.3178 0.3187 0.2781 0.0411  -0.0361 -0.0275 94  LEU A O   
1452 C CB  . LEU A 91  ? 0.2877 0.2910 0.2905 0.0378  -0.0315 -0.0270 94  LEU A CB  
1453 C CG  . LEU A 91  ? 0.2826 0.2750 0.2988 0.0361  -0.0360 -0.0279 94  LEU A CG  
1454 C CD1 . LEU A 91  ? 0.3416 0.3334 0.3592 0.0432  -0.0334 -0.0313 94  LEU A CD1 
1455 C CD2 . LEU A 91  ? 0.3446 0.3239 0.3600 0.0349  -0.0452 -0.0340 94  LEU A CD2 
1467 N N   . LEU A 92  ? 0.2893 0.2992 0.2589 0.0301  -0.0222 -0.0138 95  LEU A N   
1468 C CA  . LEU A 92  ? 0.2999 0.3127 0.2465 0.0287  -0.0160 -0.0110 95  LEU A CA  
1469 C C   . LEU A 92  ? 0.3292 0.3257 0.2570 0.0308  -0.0243 -0.0069 95  LEU A C   
1470 O O   . LEU A 92  ? 0.3451 0.3403 0.2498 0.0348  -0.0249 -0.0090 95  LEU A O   
1471 C CB  . LEU A 92  ? 0.3026 0.3231 0.2487 0.0180  -0.0040 -0.0034 95  LEU A CB  
1472 C CG  . LEU A 92  ? 0.4123 0.4384 0.3368 0.0117  0.0067  0.0004  95  LEU A CG  
1473 C CD1 . LEU A 92  ? 0.4929 0.5425 0.4173 0.0187  0.0125  -0.0105 95  LEU A CD1 
1474 C CD2 . LEU A 92  ? 0.4641 0.4949 0.3933 -0.0026 0.0169  0.0074  95  LEU A CD2 
1486 N N   . ASP A 93  ? 0.3194 0.3047 0.2543 0.0304  -0.0317 -0.0021 96  ASP A N   
1487 C CA  . ASP A 93  ? 0.3199 0.2927 0.2383 0.0365  -0.0428 -0.0001 96  ASP A CA  
1488 C C   . ASP A 93  ? 0.3741 0.3514 0.2900 0.0437  -0.0527 -0.0111 96  ASP A C   
1489 O O   . ASP A 93  ? 0.4038 0.3757 0.2948 0.0491  -0.0583 -0.0117 96  ASP A O   
1490 C CB  . ASP A 93  ? 0.3317 0.2990 0.2672 0.0382  -0.0507 0.0024  96  ASP A CB  
1491 C CG  . ASP A 93  ? 0.3336 0.2841 0.2557 0.0369  -0.0486 0.0136  96  ASP A CG  
1492 O OD1 . ASP A 93  ? 0.3628 0.3003 0.2580 0.0343  -0.0435 0.0213  96  ASP A OD1 
1493 O OD2 . ASP A 93  ? 0.3588 0.3076 0.2983 0.0385  -0.0523 0.0142  96  ASP A OD2 
1498 N N   . LEU A 94  ? 0.3288 0.3129 0.2673 0.0436  -0.0560 -0.0203 97  LEU A N   
1499 C CA  . LEU A 94  ? 0.3529 0.3373 0.2877 0.0483  -0.0652 -0.0321 97  LEU A CA  
1500 C C   . LEU A 94  ? 0.3256 0.3114 0.2373 0.0527  -0.0599 -0.0375 97  LEU A C   
1501 O O   . LEU A 94  ? 0.3774 0.3603 0.2692 0.0583  -0.0677 -0.0441 97  LEU A O   
1502 C CB  . LEU A 94  ? 0.3577 0.3428 0.3178 0.0449  -0.0680 -0.0400 97  LEU A CB  
1503 C CG  . LEU A 94  ? 0.3453 0.3331 0.3288 0.0400  -0.0735 -0.0376 97  LEU A CG  
1504 C CD1 . LEU A 94  ? 0.4781 0.4633 0.4816 0.0338  -0.0717 -0.0424 97  LEU A CD1 
1505 C CD2 . LEU A 94  ? 0.4172 0.4093 0.3997 0.0429  -0.0879 -0.0427 97  LEU A CD2 
1517 N N   . ALA A 95  ? 0.3474 0.3408 0.2613 0.0515  -0.0469 -0.0367 98  ALA A N   
1518 C CA  . ALA A 95  ? 0.3543 0.3547 0.2496 0.0569  -0.0402 -0.0434 98  ALA A CA  
1519 C C   . ALA A 95  ? 0.4096 0.4094 0.2732 0.0566  -0.0362 -0.0371 98  ALA A C   
1520 O O   . ALA A 95  ? 0.4502 0.4515 0.2906 0.0629  -0.0364 -0.0446 98  ALA A O   
1521 C CB  . ALA A 95  ? 0.3976 0.4128 0.3071 0.0560  -0.0272 -0.0436 98  ALA A CB  
1527 N N   . LEU A 96  ? 0.3884 0.3829 0.2473 0.0495  -0.0325 -0.0232 99  LEU A N   
1528 C CA  . LEU A 96  ? 0.4399 0.4274 0.2633 0.0483  -0.0282 -0.0152 99  LEU A CA  
1529 C C   . LEU A 96  ? 0.4692 0.4436 0.2717 0.0569  -0.0442 -0.0175 99  LEU A C   
1530 O O   . LEU A 96  ? 0.5166 0.4861 0.2842 0.0601  -0.0430 -0.0159 99  LEU A O   
1531 C CB  . LEU A 96  ? 0.4938 0.4711 0.3142 0.0381  -0.0213 0.0005  99  LEU A CB  
1532 C CG  . LEU A 96  ? 0.4911 0.4854 0.3274 0.0277  -0.0047 0.0021  99  LEU A CG  
1533 C CD1 . LEU A 96  ? 0.5845 0.5626 0.4139 0.0159  0.0006  0.0169  99  LEU A CD1 
1534 C CD2 . LEU A 96  ? 0.6982 0.7133 0.5204 0.0255  0.0103  -0.0026 99  LEU A CD2 
1546 N N   . LEU A 97  ? 0.4648 0.4352 0.2874 0.0602  -0.0588 -0.0211 100 LEU A N   
1547 C CA  . LEU A 97  ? 0.5214 0.4850 0.3302 0.0686  -0.0764 -0.0251 100 LEU A CA  
1548 C C   . LEU A 97  ? 0.4748 0.4430 0.2686 0.0744  -0.0811 -0.0397 100 LEU A C   
1549 O O   . LEU A 97  ? 0.5473 0.5096 0.3092 0.0813  -0.0893 -0.0408 100 LEU A O   
1550 C CB  . LEU A 97  ? 0.5206 0.4878 0.3642 0.0683  -0.0882 -0.0286 100 LEU A CB  
1551 C CG  . LEU A 97  ? 0.6419 0.6094 0.4857 0.0756  -0.1074 -0.0322 100 LEU A CG  
1552 C CD1 . LEU A 97  ? 0.6069 0.5599 0.4226 0.0822  -0.1106 -0.0182 100 LEU A CD1 
1553 C CD2 . LEU A 97  ? 0.5700 0.5486 0.4551 0.0716  -0.1132 -0.0371 100 LEU A CD2 
1565 N N   . VAL A 98  ? 0.4477 0.5387 0.2551 0.0209  -0.1101 0.0193  101 VAL A N   
1566 C CA  . VAL A 98  ? 0.5078 0.5935 0.2856 0.0063  -0.1099 0.0055  101 VAL A CA  
1567 C C   . VAL A 98  ? 0.5035 0.5628 0.2553 0.0090  -0.0944 0.0054  101 VAL A C   
1568 O O   . VAL A 98  ? 0.6046 0.6498 0.3247 0.0014  -0.0899 -0.0071 101 VAL A O   
1569 C CB  . VAL A 98  ? 0.5120 0.5943 0.2978 -0.0079 -0.1094 -0.0116 101 VAL A CB  
1570 C CG1 . VAL A 98  ? 0.6191 0.7361 0.4361 -0.0102 -0.1227 -0.0079 101 VAL A CG1 
1571 C CG2 . VAL A 98  ? 0.5223 0.5794 0.3220 -0.0041 -0.0924 -0.0170 101 VAL A CG2 
1581 N N   . ASP A 99  ? 0.5035 0.5554 0.2638 0.0192  -0.0862 0.0198  102 ASP A N   
1582 C CA  . ASP A 99  ? 0.4931 0.5309 0.2352 0.0217  -0.0706 0.0247  102 ASP A CA  
1583 C C   . ASP A 99  ? 0.5229 0.5462 0.2620 0.0193  -0.0554 0.0102  102 ASP A C   
1584 O O   . ASP A 99  ? 0.5586 0.5719 0.2663 0.0210  -0.0447 0.0044  102 ASP A O   
1585 C CB  . ASP A 99  ? 0.5821 0.6239 0.2868 0.0222  -0.0733 0.0296  102 ASP A CB  
1586 C CG  . ASP A 99  ? 0.7407 0.7776 0.4338 0.0274  -0.0586 0.0442  102 ASP A CG  
1587 O OD1 . ASP A 99  ? 0.7510 0.7853 0.4679 0.0286  -0.0525 0.0566  102 ASP A OD1 
1588 O OD2 . ASP A 99  ? 0.7926 0.8293 0.4508 0.0287  -0.0535 0.0439  102 ASP A OD2 
1593 N N   . ALA A 100 ? 0.4683 0.4886 0.2366 0.0181  -0.0534 0.0052  103 ALA A N   
1594 C CA  . ALA A 100 ? 0.4936 0.4990 0.2609 0.0179  -0.0398 -0.0072 103 ALA A CA  
1595 C C   . ALA A 100 ? 0.5454 0.5498 0.3078 0.0267  -0.0213 0.0029  103 ALA A C   
1596 O O   . ALA A 100 ? 0.5058 0.5218 0.2811 0.0282  -0.0201 0.0206  103 ALA A O   
1597 C CB  . ALA A 100 ? 0.4712 0.4773 0.2738 0.0154  -0.0420 -0.0108 103 ALA A CB  
1603 N N   . ASP A 101 ? 0.5188 0.5086 0.2588 0.0327  -0.0066 -0.0072 104 ASP A N   
1604 C CA  . ASP A 101 ? 0.5619 0.5599 0.3013 0.0447  0.0134  0.0046  104 ASP A CA  
1605 C C   . ASP A 101 ? 0.4499 0.4619 0.2315 0.0445  0.0179  0.0152  104 ASP A C   
1606 O O   . ASP A 101 ? 0.4243 0.4303 0.2293 0.0385  0.0100  0.0082  104 ASP A O   
1607 C CB  . ASP A 101 ? 0.5854 0.5601 0.2871 0.0566  0.0297  -0.0091 104 ASP A CB  
1608 C CG  . ASP A 101 ? 0.7092 0.6617 0.4180 0.0565  0.0319  -0.0237 104 ASP A CG  
1609 O OD1 . ASP A 101 ? 0.8515 0.7817 0.5453 0.0446  0.0190  -0.0404 104 ASP A OD1 
1610 O OD2 . ASP A 101 ? 0.7273 0.6874 0.4574 0.0667  0.0455  -0.0167 104 ASP A OD2 
1615 N N   . GLN A 102 ? 0.4800 0.5146 0.2710 0.0499  0.0307  0.0342  105 GLN A N   
1616 C CA  . GLN A 102 ? 0.4556 0.5076 0.2848 0.0446  0.0312  0.0475  105 GLN A CA  
1617 C C   . GLN A 102 ? 0.4352 0.4811 0.2769 0.0520  0.0397  0.0377  105 GLN A C   
1618 O O   . GLN A 102 ? 0.4027 0.4516 0.2740 0.0444  0.0329  0.0397  105 GLN A O   
1619 C CB  . GLN A 102 ? 0.5165 0.6013 0.3517 0.0458  0.0431  0.0725  105 GLN A CB  
1620 C CG  . GLN A 102 ? 0.7039 0.7938 0.5244 0.0380  0.0364  0.0854  105 GLN A CG  
1621 C CD  . GLN A 102 ? 0.8906 1.0154 0.7257 0.0310  0.0442  0.1137  105 GLN A CD  
1622 O OE1 . GLN A 102 ? 0.8622 1.0147 0.7181 0.0344  0.0562  0.1240  105 GLN A OE1 
1623 N NE2 . GLN A 102 ? 1.1248 1.2510 0.9489 0.0202  0.0370  0.1285  105 GLN A NE2 
1632 N N   . GLY A 103 ? 0.4433 0.4756 0.2593 0.0676  0.0546  0.0270  106 GLY A N   
1633 C CA  . GLY A 103 ? 0.4319 0.4518 0.2557 0.0762  0.0627  0.0184  106 GLY A CA  
1634 C C   . GLY A 103 ? 0.4288 0.4239 0.2607 0.0634  0.0471  0.0014  106 GLY A C   
1635 O O   . GLY A 103 ? 0.4066 0.4032 0.2634 0.0618  0.0463  0.0016  106 GLY A O   
1639 N N   . THR A 104 ? 0.4464 0.4239 0.2587 0.0535  0.0338  -0.0113 107 THR A N   
1640 C CA  . THR A 104 ? 0.4462 0.4112 0.2699 0.0406  0.0189  -0.0237 107 THR A CA  
1641 C C   . THR A 104 ? 0.3927 0.3781 0.2543 0.0325  0.0075  -0.0134 107 THR A C   
1642 O O   . THR A 104 ? 0.3736 0.3555 0.2550 0.0280  0.0029  -0.0184 107 THR A O   
1643 C CB  . THR A 104 ? 0.4888 0.4392 0.2829 0.0312  0.0069  -0.0366 107 THR A CB  
1644 O OG1 . THR A 104 ? 0.5432 0.4651 0.2921 0.0391  0.0188  -0.0471 107 THR A OG1 
1645 C CG2 . THR A 104 ? 0.5410 0.4844 0.3461 0.0168  -0.0072 -0.0482 107 THR A CG2 
1653 N N   . ILE A 105 ? 0.3600 0.3621 0.2282 0.0308  0.0034  0.0012  108 ILE A N   
1654 C CA  . ILE A 105 ? 0.3500 0.3595 0.2451 0.0237  -0.0072 0.0103  108 ILE A CA  
1655 C C   . ILE A 105 ? 0.3629 0.3787 0.2806 0.0240  -0.0002 0.0160  108 ILE A C   
1656 O O   . ILE A 105 ? 0.3278 0.3390 0.2631 0.0196  -0.0071 0.0132  108 ILE A O   
1657 C CB  . ILE A 105 ? 0.3674 0.3842 0.2564 0.0204  -0.0125 0.0259  108 ILE A CB  
1658 C CG1 . ILE A 105 ? 0.4498 0.4623 0.3180 0.0210  -0.0218 0.0208  108 ILE A CG1 
1659 C CG2 . ILE A 105 ? 0.4236 0.4356 0.3317 0.0134  -0.0220 0.0347  108 ILE A CG2 
1660 C CD1 . ILE A 105 ? 0.4791 0.4955 0.3377 0.0190  -0.0258 0.0386  108 ILE A CD1 
1672 N N   . LEU A 106 ? 0.3382 0.3686 0.2562 0.0302  0.0138  0.0260  109 LEU A N   
1673 C CA  A LEU A 106 ? 0.3210 0.3650 0.2620 0.0309  0.0198  0.0340  109 LEU A CA  
1674 C CA  B LEU A 106 ? 0.3221 0.3664 0.2627 0.0313  0.0204  0.0341  109 LEU A CA  
1675 C C   . LEU A 106 ? 0.3141 0.3419 0.2588 0.0358  0.0222  0.0194  109 LEU A C   
1676 O O   . LEU A 106 ? 0.3255 0.3557 0.2907 0.0306  0.0175  0.0212  109 LEU A O   
1677 C CB  A LEU A 106 ? 0.3545 0.4269 0.2961 0.0402  0.0360  0.0504  109 LEU A CB  
1678 C CB  B LEU A 106 ? 0.3572 0.4273 0.2958 0.0427  0.0379  0.0482  109 LEU A CB  
1679 C CG  A LEU A 106 ? 0.3745 0.4704 0.3422 0.0409  0.0411  0.0624  109 LEU A CG  
1680 C CG  B LEU A 106 ? 0.4328 0.5322 0.3771 0.0349  0.0381  0.0705  109 LEU A CG  
1681 C CD1 A LEU A 106 ? 0.4333 0.5350 0.4202 0.0204  0.0254  0.0721  109 LEU A CD1 
1682 C CD1 B LEU A 106 ? 0.4331 0.5564 0.3652 0.0520  0.0580  0.0804  109 LEU A CD1 
1683 C CD2 A LEU A 106 ? 0.4086 0.5416 0.3789 0.0538  0.0586  0.0809  109 LEU A CD2 
1684 C CD2 B LEU A 106 ? 0.4758 0.5967 0.4483 0.0210  0.0319  0.0865  109 LEU A CD2 
1707 N N   . ALA A 107 ? 0.3311 0.3383 0.2529 0.0435  0.0283  0.0046  110 ALA A N   
1708 C CA  . ALA A 107 ? 0.3583 0.3447 0.2803 0.0446  0.0295  -0.0086 110 ALA A CA  
1709 C C   . ALA A 107 ? 0.3405 0.3239 0.2786 0.0317  0.0141  -0.0149 110 ALA A C   
1710 O O   . ALA A 107 ? 0.3408 0.3224 0.2950 0.0303  0.0139  -0.0162 110 ALA A O   
1711 C CB  . ALA A 107 ? 0.3957 0.3516 0.2807 0.0495  0.0353  -0.0239 110 ALA A CB  
1717 N N   . LEU A 108 ? 0.3210 0.3066 0.2558 0.0243  0.0018  -0.0170 111 LEU A N   
1718 C CA  . LEU A 108 ? 0.3231 0.3102 0.2721 0.0171  -0.0109 -0.0213 111 LEU A CA  
1719 C C   . LEU A 108 ? 0.3006 0.2946 0.2697 0.0164  -0.0140 -0.0116 111 LEU A C   
1720 O O   . LEU A 108 ? 0.2895 0.2815 0.2718 0.0149  -0.0167 -0.0153 111 LEU A O   
1721 C CB  . LEU A 108 ? 0.3102 0.3023 0.2490 0.0140  -0.0222 -0.0223 111 LEU A CB  
1722 C CG  . LEU A 108 ? 0.4169 0.4041 0.3357 0.0087  -0.0260 -0.0337 111 LEU A CG  
1723 C CD1 . LEU A 108 ? 0.4752 0.4748 0.3855 0.0077  -0.0375 -0.0296 111 LEU A CD1 
1724 C CD2 . LEU A 108 ? 0.5169 0.5051 0.4471 0.0007  -0.0310 -0.0423 111 LEU A CD2 
1736 N N   . VAL A 109 ? 0.2927 0.2928 0.2616 0.0156  -0.0143 0.0012  112 VAL A N   
1737 C CA  . VAL A 109 ? 0.2793 0.2784 0.2598 0.0104  -0.0198 0.0101  112 VAL A CA  
1738 C C   . VAL A 109 ? 0.3040 0.3098 0.2985 0.0102  -0.0132 0.0122  112 VAL A C   
1739 O O   . VAL A 109 ? 0.2759 0.2759 0.2787 0.0070  -0.0179 0.0111  112 VAL A O   
1740 C CB  . VAL A 109 ? 0.2899 0.2915 0.2630 0.0043  -0.0232 0.0251  112 VAL A CB  
1741 C CG1 . VAL A 109 ? 0.3535 0.3486 0.3322 -0.0064 -0.0297 0.0349  112 VAL A CG1 
1742 C CG2 . VAL A 109 ? 0.3684 0.3591 0.3266 0.0066  -0.0315 0.0232  112 VAL A CG2 
1752 N N   . GLY A 110 ? 0.2692 0.2868 0.2644 0.0162  -0.0009 0.0155  113 GLY A N   
1753 C CA  . GLY A 110 ? 0.2702 0.2971 0.2791 0.0189  0.0055  0.0199  113 GLY A CA  
1754 C C   . GLY A 110 ? 0.2692 0.2803 0.2802 0.0217  0.0059  0.0065  113 GLY A C   
1755 O O   . GLY A 110 ? 0.2457 0.2587 0.2687 0.0191  0.0038  0.0087  113 GLY A O   
1759 N N   . ALA A 111 ? 0.2487 0.2440 0.2464 0.0242  0.0075  -0.0069 114 ALA A N   
1760 C CA  . ALA A 111 ? 0.2549 0.2381 0.2556 0.0220  0.0063  -0.0171 114 ALA A CA  
1761 C C   . ALA A 111 ? 0.2518 0.2388 0.2646 0.0159  -0.0046 -0.0181 114 ALA A C   
1762 O O   . ALA A 111 ? 0.2394 0.2248 0.2610 0.0151  -0.0042 -0.0199 114 ALA A O   
1763 C CB  . ALA A 111 ? 0.2945 0.2609 0.2761 0.0192  0.0066  -0.0303 114 ALA A CB  
1769 N N   . ASP A 112 ? 0.2591 0.2486 0.2689 0.0141  -0.0132 -0.0160 115 ASP A N   
1770 C CA  . ASP A 112 ? 0.2236 0.2111 0.2379 0.0139  -0.0217 -0.0163 115 ASP A CA  
1771 C C   . ASP A 112 ? 0.2256 0.2091 0.2444 0.0116  -0.0224 -0.0095 115 ASP A C   
1772 O O   . ASP A 112 ? 0.2173 0.1960 0.2388 0.0130  -0.0244 -0.0126 115 ASP A O   
1773 C CB  . ASP A 112 ? 0.2269 0.2121 0.2308 0.0159  -0.0299 -0.0135 115 ASP A CB  
1774 C CG  . ASP A 112 ? 0.2910 0.2716 0.2945 0.0220  -0.0361 -0.0149 115 ASP A CG  
1775 O OD1 . ASP A 112 ? 0.3090 0.2740 0.3069 0.0220  -0.0386 -0.0108 115 ASP A OD1 
1776 O OD2 . ASP A 112 ? 0.3735 0.3664 0.3809 0.0267  -0.0383 -0.0193 115 ASP A OD2 
1781 N N   . GLY A 113 ? 0.2271 0.2147 0.2450 0.0069  -0.0218 0.0010  116 GLY A N   
1782 C CA  . GLY A 113 ? 0.2379 0.2266 0.2595 0.0000  -0.0246 0.0094  116 GLY A CA  
1783 C C   . GLY A 113 ? 0.2399 0.2346 0.2721 0.0034  -0.0187 0.0066  116 GLY A C   
1784 O O   . GLY A 113 ? 0.2463 0.2349 0.2776 0.0001  -0.0232 0.0069  116 GLY A O   
1788 N N   . ILE A 114 ? 0.2137 0.2163 0.2513 0.0104  -0.0082 0.0047  117 ILE A N   
1789 C CA  . ILE A 114 ? 0.2217 0.2248 0.2659 0.0149  -0.0015 0.0031  117 ILE A CA  
1790 C C   . ILE A 114 ? 0.2255 0.2170 0.2687 0.0140  -0.0045 -0.0075 117 ILE A C   
1791 O O   . ILE A 114 ? 0.2192 0.2105 0.2661 0.0134  -0.0050 -0.0063 117 ILE A O   
1792 C CB  . ILE A 114 ? 0.2142 0.2161 0.2546 0.0243  0.0109  0.0024  117 ILE A CB  
1793 C CG1 . ILE A 114 ? 0.2472 0.2715 0.2927 0.0293  0.0163  0.0179  117 ILE A CG1 
1794 C CG2 . ILE A 114 ? 0.2594 0.2514 0.3011 0.0286  0.0173  -0.0006 117 ILE A CG2 
1795 C CD1 . ILE A 114 ? 0.3175 0.3359 0.3512 0.0447  0.0313  0.0170  117 ILE A CD1 
1807 N N   . MET A 115 ? 0.2061 0.1931 0.2450 0.0137  -0.0073 -0.0160 118 MET A N   
1808 C CA  . MET A 115 ? 0.2072 0.1943 0.2489 0.0137  -0.0095 -0.0227 118 MET A CA  
1809 C C   . MET A 115 ? 0.2312 0.2146 0.2702 0.0159  -0.0148 -0.0204 118 MET A C   
1810 O O   . MET A 115 ? 0.2167 0.2008 0.2581 0.0175  -0.0127 -0.0216 118 MET A O   
1811 C CB  . MET A 115 ? 0.2106 0.2028 0.2494 0.0132  -0.0134 -0.0281 118 MET A CB  
1812 C CG  . MET A 115 ? 0.2044 0.2089 0.2501 0.0141  -0.0154 -0.0314 118 MET A CG  
1813 S SD  . MET A 115 ? 0.2395 0.2613 0.2848 0.0130  -0.0223 -0.0339 118 MET A SD  
1814 C CE  . MET A 115 ? 0.3000 0.3141 0.3362 0.0262  -0.0284 -0.0288 118 MET A CE  
1824 N N   . ILE A 116 ? 0.2086 0.1828 0.2373 0.0159  -0.0219 -0.0172 119 ILE A N   
1825 C CA  . ILE A 116 ? 0.2554 0.2140 0.2712 0.0184  -0.0272 -0.0172 119 ILE A CA  
1826 C C   . ILE A 116 ? 0.2385 0.1939 0.2525 0.0108  -0.0282 -0.0118 119 ILE A C   
1827 O O   . ILE A 116 ? 0.2545 0.2004 0.2594 0.0133  -0.0291 -0.0143 119 ILE A O   
1828 C CB  . ILE A 116 ? 0.2390 0.1794 0.2376 0.0191  -0.0349 -0.0149 119 ILE A CB  
1829 C CG1 . ILE A 116 ? 0.2600 0.2080 0.2604 0.0286  -0.0347 -0.0182 119 ILE A CG1 
1830 C CG2 . ILE A 116 ? 0.3100 0.2197 0.2834 0.0212  -0.0407 -0.0157 119 ILE A CG2 
1831 C CD1 . ILE A 116 ? 0.2664 0.2281 0.2736 0.0404  -0.0310 -0.0233 119 ILE A CD1 
1843 N N   . GLY A 117 ? 0.2270 0.1928 0.2478 0.0027  -0.0284 -0.0033 120 GLY A N   
1844 C CA  . GLY A 117 ? 0.2385 0.2098 0.2596 -0.0054 -0.0313 0.0050  120 GLY A CA  
1845 C C   . GLY A 117 ? 0.2458 0.2254 0.2760 0.0005  -0.0240 0.0030  120 GLY A C   
1846 O O   . GLY A 117 ? 0.2485 0.2227 0.2701 -0.0028 -0.0281 0.0045  120 GLY A O   
1850 N N   . THR A 118 ? 0.2147 0.2025 0.2570 0.0078  -0.0140 -0.0004 121 THR A N   
1851 C CA  . THR A 118 ? 0.2223 0.2127 0.2699 0.0117  -0.0071 -0.0010 121 THR A CA  
1852 C C   . THR A 118 ? 0.2570 0.2396 0.2978 0.0141  -0.0080 -0.0089 121 THR A C   
1853 O O   . THR A 118 ? 0.2211 0.2045 0.2605 0.0152  -0.0053 -0.0075 121 THR A O   
1854 C CB  . THR A 118 ? 0.2297 0.2211 0.2843 0.0164  0.0033  -0.0020 121 THR A CB  
1855 O OG1 . THR A 118 ? 0.2394 0.2254 0.2920 0.0155  0.0035  -0.0113 121 THR A OG1 
1856 C CG2 . THR A 118 ? 0.2477 0.2486 0.3061 0.0202  0.0071  0.0078  121 THR A CG2 
1864 N N   . GLY A 119 ? 0.2366 0.2151 0.2734 0.0173  -0.0102 -0.0158 122 GLY A N   
1865 C CA  . GLY A 119 ? 0.2585 0.2349 0.2880 0.0244  -0.0096 -0.0206 122 GLY A CA  
1866 C C   . GLY A 119 ? 0.2399 0.1989 0.2487 0.0254  -0.0146 -0.0198 122 GLY A C   
1867 O O   . GLY A 119 ? 0.2626 0.2213 0.2647 0.0309  -0.0109 -0.0213 122 GLY A O   
1871 N N   . LEU A 120 ? 0.2522 0.1943 0.2466 0.0185  -0.0240 -0.0172 123 LEU A N   
1872 C CA  . LEU A 120 ? 0.2693 0.1880 0.2369 0.0139  -0.0317 -0.0168 123 LEU A CA  
1873 C C   . LEU A 120 ? 0.2598 0.1912 0.2325 0.0072  -0.0312 -0.0107 123 LEU A C   
1874 O O   . LEU A 120 ? 0.2745 0.1922 0.2265 0.0092  -0.0325 -0.0134 123 LEU A O   
1875 C CB  . LEU A 120 ? 0.2855 0.1875 0.2398 0.0010  -0.0432 -0.0123 123 LEU A CB  
1876 C CG  . LEU A 120 ? 0.3299 0.2039 0.2523 -0.0119 -0.0551 -0.0104 123 LEU A CG  
1877 C CD1 . LEU A 120 ? 0.3926 0.2268 0.2766 -0.0017 -0.0562 -0.0203 123 LEU A CD1 
1878 C CD2 . LEU A 120 ? 0.4362 0.2993 0.3505 -0.0294 -0.0664 -0.0029 123 LEU A CD2 
1890 N N   . VAL A 121 ? 0.2349 0.1905 0.2308 0.0017  -0.0288 -0.0020 124 VAL A N   
1891 C CA  . VAL A 121 ? 0.2316 0.2024 0.2339 -0.0010 -0.0273 0.0063  124 VAL A CA  
1892 C C   . VAL A 121 ? 0.2382 0.2098 0.2418 0.0087  -0.0175 0.0017  124 VAL A C   
1893 O O   . VAL A 121 ? 0.2612 0.2289 0.2507 0.0080  -0.0194 0.0033  124 VAL A O   
1894 C CB  . VAL A 121 ? 0.2277 0.2230 0.2533 -0.0014 -0.0229 0.0169  124 VAL A CB  
1895 C CG1 . VAL A 121 ? 0.2560 0.2672 0.2886 0.0015  -0.0189 0.0270  124 VAL A CG1 
1896 C CG2 . VAL A 121 ? 0.2705 0.2762 0.2973 -0.0130 -0.0326 0.0266  124 VAL A CG2 
1906 N N   . GLY A 122 ? 0.2371 0.2125 0.2525 0.0156  -0.0089 -0.0038 125 GLY A N   
1907 C CA  . GLY A 122 ? 0.2427 0.2232 0.2601 0.0216  0.0000  -0.0062 125 GLY A CA  
1908 C C   . GLY A 122 ? 0.2702 0.2402 0.2657 0.0285  -0.0009 -0.0116 125 GLY A C   
1909 O O   . GLY A 122 ? 0.2809 0.2547 0.2699 0.0317  0.0042  -0.0095 125 GLY A O   
1913 N N   . ALA A 123 ? 0.2527 0.2058 0.2315 0.0331  -0.0064 -0.0180 126 ALA A N   
1914 C CA  . ALA A 123 ? 0.2777 0.2130 0.2278 0.0449  -0.0054 -0.0239 126 ALA A CA  
1915 C C   . ALA A 123 ? 0.3060 0.2192 0.2259 0.0390  -0.0124 -0.0232 126 ALA A C   
1916 O O   . ALA A 123 ? 0.3452 0.2466 0.2404 0.0493  -0.0082 -0.0270 126 ALA A O   
1917 C CB  . ALA A 123 ? 0.3203 0.2325 0.2530 0.0525  -0.0104 -0.0300 126 ALA A CB  
1923 N N   . LEU A 124 ? 0.3037 0.2149 0.2247 0.0224  -0.0232 -0.0172 127 LEU A N   
1924 C CA  . LEU A 124 ? 0.3335 0.2277 0.2254 0.0121  -0.0334 -0.0151 127 LEU A CA  
1925 C C   . LEU A 124 ? 0.3177 0.2395 0.2260 0.0062  -0.0319 -0.0041 127 LEU A C   
1926 O O   . LEU A 124 ? 0.3630 0.2773 0.2487 -0.0039 -0.0418 -0.0003 127 LEU A O   
1927 C CB  . LEU A 124 ? 0.3479 0.2268 0.2287 -0.0070 -0.0498 -0.0116 127 LEU A CB  
1928 C CG  . LEU A 124 ? 0.3736 0.2166 0.2305 -0.0021 -0.0527 -0.0208 127 LEU A CG  
1929 C CD1 . LEU A 124 ? 0.4936 0.3213 0.3385 -0.0257 -0.0695 -0.0149 127 LEU A CD1 
1930 C CD2 . LEU A 124 ? 0.4461 0.2448 0.2534 0.0095  -0.0523 -0.0319 127 LEU A CD2 
1942 N N   . THR A 125 ? 0.2851 0.2340 0.2267 0.0128  -0.0198 0.0008  128 THR A N   
1943 C CA  . THR A 125 ? 0.2749 0.2450 0.2302 0.0108  -0.0167 0.0126  128 THR A CA  
1944 C C   . THR A 125 ? 0.3174 0.2840 0.2541 0.0172  -0.0107 0.0118  128 THR A C   
1945 O O   . THR A 125 ? 0.3428 0.3060 0.2748 0.0277  -0.0006 0.0049  128 THR A O   
1946 C CB  . THR A 125 ? 0.2595 0.2461 0.2476 0.0154  -0.0056 0.0164  128 THR A CB  
1947 O OG1 . THR A 125 ? 0.2840 0.2786 0.2860 0.0101  -0.0112 0.0217  128 THR A OG1 
1948 C CG2 . THR A 125 ? 0.3101 0.3088 0.3075 0.0186  0.0024  0.0274  128 THR A CG2 
1956 N N   . LYS A 126 ? 0.3184 0.2891 0.2425 0.0112  -0.0174 0.0203  129 LYS A N   
1957 C CA  . LYS A 126 ? 0.3316 0.2971 0.2313 0.0164  -0.0134 0.0200  129 LYS A CA  
1958 C C   . LYS A 126 ? 0.3351 0.3207 0.2551 0.0226  -0.0001 0.0304  129 LYS A C   
1959 O O   . LYS A 126 ? 0.4346 0.4188 0.3377 0.0288  0.0073  0.0302  129 LYS A O   
1960 C CB  . LYS A 126 ? 0.3852 0.3464 0.2578 0.0038  -0.0295 0.0261  129 LYS A CB  
1961 C CG  . LYS A 126 ? 0.4828 0.4136 0.3238 -0.0069 -0.0444 0.0158  129 LYS A CG  
1962 C CD  . LYS A 126 ? 0.5767 0.5045 0.3869 -0.0251 -0.0630 0.0229  129 LYS A CD  
1963 C CE  . LYS A 126 ? 0.8420 0.7385 0.6192 -0.0446 -0.0821 0.0165  129 LYS A CE  
1964 N NZ  . LYS A 126 ? 1.0330 0.8764 0.7679 -0.0344 -0.0781 -0.0031 129 LYS A NZ  
1978 N N   . VAL A 127 ? 0.3007 0.3006 0.2517 0.0222  0.0044  0.0391  130 VAL A N   
1979 C CA  . VAL A 127 ? 0.3052 0.3130 0.2695 0.0268  0.0173  0.0488  130 VAL A CA  
1980 C C   . VAL A 127 ? 0.3106 0.3165 0.2894 0.0284  0.0285  0.0409  130 VAL A C   
1981 O O   . VAL A 127 ? 0.3102 0.3139 0.3051 0.0266  0.0279  0.0361  130 VAL A O   
1982 C CB  . VAL A 127 ? 0.2993 0.3152 0.2810 0.0278  0.0166  0.0624  130 VAL A CB  
1983 C CG1 . VAL A 127 ? 0.3413 0.3526 0.3291 0.0326  0.0305  0.0723  130 VAL A CG1 
1984 C CG2 . VAL A 127 ? 0.3637 0.3938 0.3362 0.0253  0.0041  0.0740  130 VAL A CG2 
1994 N N   . TYR A 128 ? 0.3032 0.3824 0.2448 0.0135  0.0066  0.0615  131 TYR A N   
1995 C CA  . TYR A 128 ? 0.2972 0.3814 0.2530 0.0156  0.0189  0.0585  131 TYR A CA  
1996 C C   . TYR A 128 ? 0.2766 0.3547 0.2651 0.0093  0.0197  0.0660  131 TYR A C   
1997 O O   . TYR A 128 ? 0.2655 0.3377 0.2677 0.0089  0.0212  0.0564  131 TYR A O   
1998 C CB  . TYR A 128 ? 0.3131 0.4172 0.2561 0.0194  0.0314  0.0687  131 TYR A CB  
1999 C CG  . TYR A 128 ? 0.3424 0.4561 0.3003 0.0221  0.0440  0.0679  131 TYR A CG  
2000 C CD1 . TYR A 128 ? 0.3726 0.4816 0.3265 0.0285  0.0468  0.0511  131 TYR A CD1 
2001 C CD2 . TYR A 128 ? 0.3865 0.5150 0.3668 0.0174  0.0519  0.0867  131 TYR A CD2 
2002 C CE1 . TYR A 128 ? 0.3732 0.4958 0.3452 0.0313  0.0589  0.0540  131 TYR A CE1 
2003 C CE2 . TYR A 128 ? 0.3859 0.5271 0.3839 0.0183  0.0620  0.0898  131 TYR A CE2 
2004 C CZ  . TYR A 128 ? 0.3884 0.5276 0.3819 0.0257  0.0655  0.0737  131 TYR A CZ  
2005 O OH  . TYR A 128 ? 0.4612 0.6169 0.4757 0.0269  0.0755  0.0801  131 TYR A OH  
2015 N N   A SER A 129 ? 0.3114 0.3900 0.3116 0.0044  0.0188  0.0832  132 SER A N   
2016 N N   B SER A 129 ? 0.3119 0.3903 0.3122 0.0043  0.0187  0.0831  132 SER A N   
2017 C CA  A SER A 129 ? 0.3128 0.3801 0.3402 -0.0013 0.0201  0.0884  132 SER A CA  
2018 C CA  B SER A 129 ? 0.3115 0.3786 0.3390 -0.0013 0.0201  0.0879  132 SER A CA  
2019 C C   A SER A 129 ? 0.2831 0.3315 0.3191 -0.0007 0.0139  0.0760  132 SER A C   
2020 C C   B SER A 129 ? 0.2836 0.3319 0.3194 -0.0006 0.0139  0.0753  132 SER A C   
2021 O O   A SER A 129 ? 0.2880 0.3256 0.3386 -0.0039 0.0155  0.0713  132 SER A O   
2022 O O   B SER A 129 ? 0.2859 0.3237 0.3360 -0.0036 0.0155  0.0700  132 SER A O   
2023 C CB  A SER A 129 ? 0.3251 0.3924 0.3634 -0.0053 0.0201  0.1092  132 SER A CB  
2024 C CB  B SER A 129 ? 0.3259 0.3924 0.3646 -0.0052 0.0200  0.1082  132 SER A CB  
2025 O OG  A SER A 129 ? 0.3563 0.4190 0.3899 -0.0031 0.0126  0.1137  132 SER A OG  
2026 O OG  B SER A 129 ? 0.4024 0.4890 0.4368 -0.0062 0.0269  0.1223  132 SER A OG  
2037 N N   . TYR A 130 ? 0.2654 0.3103 0.2918 0.0030  0.0062  0.0709  133 TYR A N   
2038 C CA  . TYR A 130 ? 0.2586 0.2890 0.2958 0.0047  0.0017  0.0627  133 TYR A CA  
2039 C C   . TYR A 130 ? 0.2561 0.2854 0.2922 0.0064  0.0023  0.0461  133 TYR A C   
2040 O O   . TYR A 130 ? 0.2452 0.2642 0.2921 0.0072  0.0013  0.0404  133 TYR A O   
2041 C CB  . TYR A 130 ? 0.2491 0.2798 0.2815 0.0069  -0.0079 0.0664  133 TYR A CB  
2042 C CG  . TYR A 130 ? 0.2988 0.3312 0.3376 0.0061  -0.0101 0.0853  133 TYR A CG  
2043 C CD1 . TYR A 130 ? 0.2867 0.3156 0.3376 0.0044  -0.0030 0.0974  133 TYR A CD1 
2044 C CD2 . TYR A 130 ? 0.3402 0.3783 0.3746 0.0062  -0.0211 0.0921  133 TYR A CD2 
2045 C CE1 . TYR A 130 ? 0.3653 0.3973 0.4248 0.0044  -0.0049 0.1179  133 TYR A CE1 
2046 C CE2 . TYR A 130 ? 0.4078 0.4514 0.4499 0.0053  -0.0243 0.1120  133 TYR A CE2 
2047 C CZ  . TYR A 130 ? 0.3515 0.3923 0.4063 0.0053  -0.0152 0.1249  133 TYR A CZ  
2048 O OH  . TYR A 130 ? 0.4931 0.5398 0.5599 0.0053  -0.0174 0.1482  133 TYR A OH  
2058 N N   . ARG A 131 ? 0.2253 0.2651 0.2497 0.0079  0.0054  0.0393  134 ARG A N   
2059 C CA  . ARG A 131 ? 0.2111 0.2509 0.2389 0.0100  0.0068  0.0261  134 ARG A CA  
2060 C C   . ARG A 131 ? 0.2532 0.2893 0.2983 0.0056  0.0103  0.0268  134 ARG A C   
2061 O O   . ARG A 131 ? 0.2368 0.2685 0.2892 0.0061  0.0084  0.0184  134 ARG A O   
2062 C CB  . ARG A 131 ? 0.2446 0.2962 0.2582 0.0143  0.0126  0.0212  134 ARG A CB  
2063 C CG  . ARG A 131 ? 0.2757 0.3260 0.2639 0.0184  0.0072  0.0171  134 ARG A CG  
2064 C CD  . ARG A 131 ? 0.2902 0.3492 0.2584 0.0255  0.0162  0.0110  134 ARG A CD  
2065 N NE  . ARG A 131 ? 0.2861 0.3435 0.2602 0.0309  0.0205  -0.0011 134 ARG A NE  
2066 C CZ  . ARG A 131 ? 0.2815 0.3258 0.2474 0.0347  0.0135  -0.0152 134 ARG A CZ  
2067 N NH1 . ARG A 131 ? 0.2849 0.3169 0.2345 0.0326  0.0007  -0.0195 134 ARG A NH1 
2068 N NH2 . ARG A 131 ? 0.2837 0.3278 0.2593 0.0400  0.0187  -0.0234 134 ARG A NH2 
2082 N N   . PHE A 132 ? 0.2273 0.2650 0.2789 0.0001  0.0145  0.0376  135 PHE A N   
2083 C CA  . PHE A 132 ? 0.2384 0.2702 0.3039 -0.0067 0.0154  0.0380  135 PHE A CA  
2084 C C   . PHE A 132 ? 0.2410 0.2513 0.3106 -0.0079 0.0117  0.0354  135 PHE A C   
2085 O O   . PHE A 132 ? 0.2399 0.2414 0.3144 -0.0121 0.0102  0.0295  135 PHE A O   
2086 C CB  . PHE A 132 ? 0.2307 0.2715 0.3038 -0.0133 0.0199  0.0519  135 PHE A CB  
2087 C CG  . PHE A 132 ? 0.2286 0.2934 0.2974 -0.0096 0.0268  0.0555  135 PHE A CG  
2088 C CD1 . PHE A 132 ? 0.2448 0.3214 0.3217 -0.0096 0.0296  0.0514  135 PHE A CD1 
2089 C CD2 . PHE A 132 ? 0.2932 0.3678 0.3483 -0.0047 0.0306  0.0628  135 PHE A CD2 
2090 C CE1 . PHE A 132 ? 0.3159 0.4142 0.3887 -0.0030 0.0389  0.0557  135 PHE A CE1 
2091 C CE2 . PHE A 132 ? 0.3180 0.4125 0.3635 0.0016  0.0390  0.0646  135 PHE A CE2 
2092 C CZ  . PHE A 132 ? 0.3096 0.4156 0.3647 0.0034  0.0445  0.0613  135 PHE A CZ  
2102 N N   . VAL A 133 ? 0.2292 0.2313 0.2959 -0.0034 0.0103  0.0400  136 VAL A N   
2103 C CA  . VAL A 133 ? 0.2404 0.2230 0.3106 -0.0003 0.0095  0.0375  136 VAL A CA  
2104 C C   . VAL A 133 ? 0.2429 0.2264 0.3117 0.0038  0.0072  0.0260  136 VAL A C   
2105 O O   . VAL A 133 ? 0.2299 0.2003 0.2991 0.0039  0.0079  0.0198  136 VAL A O   
2106 C CB  . VAL A 133 ? 0.2528 0.2331 0.3246 0.0048  0.0090  0.0490  136 VAL A CB  
2107 C CG1 . VAL A 133 ? 0.3100 0.2729 0.3871 0.0113  0.0109  0.0484  136 VAL A CG1 
2108 C CG2 . VAL A 133 ? 0.3056 0.2836 0.3820 0.0006  0.0118  0.0628  136 VAL A CG2 
2118 N N   . TRP A 134 ? 0.2203 0.2173 0.2861 0.0074  0.0040  0.0230  137 TRP A N   
2119 C CA  . TRP A 134 ? 0.1986 0.1973 0.2671 0.0112  0.0013  0.0146  137 TRP A CA  
2120 C C   . TRP A 134 ? 0.2038 0.2067 0.2741 0.0069  0.0026  0.0073  137 TRP A C   
2121 O O   . TRP A 134 ? 0.2089 0.2079 0.2816 0.0083  0.0017  0.0022  137 TRP A O   
2122 C CB  . TRP A 134 ? 0.1952 0.2042 0.2604 0.0143  -0.0040 0.0132  137 TRP A CB  
2123 C CG  . TRP A 134 ? 0.2053 0.2119 0.2712 0.0168  -0.0085 0.0223  137 TRP A CG  
2124 C CD1 . TRP A 134 ? 0.2044 0.2158 0.2617 0.0153  -0.0120 0.0287  137 TRP A CD1 
2125 C CD2 . TRP A 134 ? 0.2064 0.2080 0.2831 0.0214  -0.0099 0.0288  137 TRP A CD2 
2126 N NE1 . TRP A 134 ? 0.2213 0.2316 0.2851 0.0171  -0.0172 0.0393  137 TRP A NE1 
2127 C CE2 . TRP A 134 ? 0.2131 0.2182 0.2910 0.0216  -0.0155 0.0404  137 TRP A CE2 
2128 C CE3 . TRP A 134 ? 0.2286 0.2253 0.3137 0.0260  -0.0066 0.0272  137 TRP A CE3 
2129 C CZ2 . TRP A 134 ? 0.2459 0.2510 0.3380 0.0263  -0.0176 0.0527  137 TRP A CZ2 
2130 C CZ3 . TRP A 134 ? 0.2597 0.2560 0.3562 0.0323  -0.0070 0.0382  137 TRP A CZ3 
2131 C CH2 . TRP A 134 ? 0.2638 0.2645 0.3657 0.0324  -0.0119 0.0514  137 TRP A CH2 
2142 N N   . TRP A 135 ? 0.2029 0.2156 0.2730 0.0022  0.0048  0.0086  138 TRP A N   
2143 C CA  . TRP A 135 ? 0.2112 0.2306 0.2876 -0.0032 0.0051  0.0054  138 TRP A CA  
2144 C C   . TRP A 135 ? 0.2077 0.2114 0.2838 -0.0093 0.0030  0.0040  138 TRP A C   
2145 O O   . TRP A 135 ? 0.2164 0.2213 0.2938 -0.0116 0.0001  -0.0015 138 TRP A O   
2146 C CB  . TRP A 135 ? 0.2118 0.2464 0.2914 -0.0066 0.0093  0.0118  138 TRP A CB  
2147 C CG  . TRP A 135 ? 0.1767 0.2222 0.2679 -0.0135 0.0089  0.0132  138 TRP A CG  
2148 C CD1 . TRP A 135 ? 0.2029 0.2654 0.3022 -0.0104 0.0106  0.0115  138 TRP A CD1 
2149 C CD2 . TRP A 135 ? 0.1909 0.2314 0.2888 -0.0251 0.0054  0.0180  138 TRP A CD2 
2150 N NE1 . TRP A 135 ? 0.2180 0.2903 0.3303 -0.0194 0.0085  0.0172  138 TRP A NE1 
2151 C CE2 . TRP A 135 ? 0.2195 0.2777 0.3301 -0.0296 0.0041  0.0206  138 TRP A CE2 
2152 C CE3 . TRP A 135 ? 0.2538 0.2753 0.3493 -0.0327 0.0026  0.0213  138 TRP A CE3 
2153 C CZ2 . TRP A 135 ? 0.2808 0.3407 0.4015 -0.0429 -0.0019 0.0267  138 TRP A CZ2 
2154 C CZ3 . TRP A 135 ? 0.3129 0.3315 0.4169 -0.0464 -0.0034 0.0252  138 TRP A CZ3 
2155 C CH2 . TRP A 135 ? 0.3294 0.3671 0.4449 -0.0520 -0.0068 0.0275  138 TRP A CH2 
2166 N N   . ALA A 136 ? 0.2152 0.2023 0.2880 -0.0117 0.0041  0.0083  139 ALA A N   
2167 C CA  . ALA A 136 ? 0.2367 0.2018 0.3049 -0.0174 0.0020  0.0043  139 ALA A CA  
2168 C C   . ALA A 136 ? 0.2528 0.2063 0.3124 -0.0094 0.0026  -0.0036 139 ALA A C   
2169 O O   . ALA A 136 ? 0.2753 0.2181 0.3266 -0.0134 -0.0003 -0.0112 139 ALA A O   
2170 C CB  . ALA A 136 ? 0.2587 0.2066 0.3274 -0.0203 0.0040  0.0113  139 ALA A CB  
2176 N N   . ILE A 137 ? 0.2315 0.1862 0.2921 0.0014  0.0060  -0.0006 140 ILE A N   
2177 C CA  . ILE A 137 ? 0.2497 0.1976 0.3056 0.0103  0.0082  -0.0044 140 ILE A CA  
2178 C C   . ILE A 137 ? 0.2445 0.2087 0.3021 0.0094  0.0045  -0.0097 140 ILE A C   
2179 O O   . ILE A 137 ? 0.2461 0.2030 0.2945 0.0111  0.0049  -0.0153 140 ILE A O   
2180 C CB  . ILE A 137 ? 0.2321 0.1854 0.2958 0.0200  0.0106  0.0043  140 ILE A CB  
2181 C CG1 . ILE A 137 ? 0.2672 0.2041 0.3307 0.0215  0.0150  0.0115  140 ILE A CG1 
2182 C CG2 . ILE A 137 ? 0.3004 0.2550 0.3649 0.0299  0.0133  0.0041  140 ILE A CG2 
2183 C CD1 . ILE A 137 ? 0.3257 0.2727 0.3999 0.0279  0.0148  0.0244  140 ILE A CD1 
2195 N N   . SER A 138 ? 0.2013 0.1858 0.2686 0.0075  0.0015  -0.0081 141 SER A N   
2196 C CA  . SER A 138 ? 0.2001 0.2001 0.2730 0.0074  -0.0016 -0.0112 141 SER A CA  
2197 C C   . SER A 138 ? 0.2200 0.2197 0.2886 -0.0019 -0.0048 -0.0150 141 SER A C   
2198 O O   . SER A 138 ? 0.2264 0.2306 0.2926 -0.0014 -0.0071 -0.0176 141 SER A O   
2199 C CB  . SER A 138 ? 0.2002 0.2162 0.2828 0.0080  -0.0026 -0.0093 141 SER A CB  
2200 O OG  . SER A 138 ? 0.2024 0.2336 0.2946 0.0088  -0.0049 -0.0109 141 SER A OG  
2206 N N   . THR A 139 ? 0.2109 0.2059 0.2785 -0.0111 -0.0060 -0.0138 142 THR A N   
2207 C CA  . THR A 139 ? 0.2347 0.2292 0.3000 -0.0231 -0.0122 -0.0156 142 THR A CA  
2208 C C   . THR A 139 ? 0.2598 0.2297 0.3049 -0.0239 -0.0141 -0.0236 142 THR A C   
2209 O O   . THR A 139 ? 0.2739 0.2459 0.3119 -0.0304 -0.0206 -0.0274 142 THR A O   
2210 C CB  . THR A 139 ? 0.2248 0.2200 0.2976 -0.0330 -0.0132 -0.0092 142 THR A CB  
2211 O OG1 . THR A 139 ? 0.2380 0.2587 0.3262 -0.0297 -0.0095 -0.0024 142 THR A OG1 
2212 C CG2 . THR A 139 ? 0.3010 0.2961 0.3750 -0.0481 -0.0223 -0.0085 142 THR A CG2 
2220 N N   . ALA A 140 ? 0.2674 0.2140 0.3020 -0.0169 -0.0084 -0.0259 143 ALA A N   
2221 C CA  . ALA A 140 ? 0.3008 0.2208 0.3126 -0.0144 -0.0074 -0.0349 143 ALA A CA  
2222 C C   . ALA A 140 ? 0.2952 0.2274 0.3015 -0.0053 -0.0056 -0.0369 143 ALA A C   
2223 O O   . ALA A 140 ? 0.3235 0.2443 0.3088 -0.0085 -0.0091 -0.0449 143 ALA A O   
2224 C CB  . ALA A 140 ? 0.3352 0.2305 0.3414 -0.0050 0.0012  -0.0343 143 ALA A CB  
2230 N N   . ALA A 141 ? 0.2577 0.2107 0.2799 0.0044  -0.0016 -0.0298 144 ALA A N   
2231 C CA  . ALA A 141 ? 0.2564 0.2240 0.2785 0.0120  -0.0005 -0.0284 144 ALA A CA  
2232 C C   . ALA A 141 ? 0.2611 0.2475 0.2864 0.0020  -0.0093 -0.0289 144 ALA A C   
2233 O O   . ALA A 141 ? 0.2793 0.2668 0.2904 0.0030  -0.0108 -0.0315 144 ALA A O   
2234 C CB  . ALA A 141 ? 0.2293 0.2163 0.2737 0.0210  0.0022  -0.0190 144 ALA A CB  
2240 N N   . MET A 142 ? 0.2570 0.2575 0.2983 -0.0074 -0.0146 -0.0257 145 MET A N   
2241 C CA  . MET A 142 ? 0.2327 0.2519 0.2801 -0.0172 -0.0228 -0.0235 145 MET A CA  
2242 C C   . MET A 142 ? 0.2740 0.2770 0.2983 -0.0282 -0.0303 -0.0303 145 MET A C   
2243 O O   . MET A 142 ? 0.2927 0.3070 0.3109 -0.0323 -0.0367 -0.0297 145 MET A O   
2244 C CB  . MET A 142 ? 0.2391 0.2736 0.3078 -0.0245 -0.0248 -0.0174 145 MET A CB  
2245 C CG  . MET A 142 ? 0.2473 0.3105 0.3345 -0.0289 -0.0300 -0.0098 145 MET A CG  
2246 S SD  . MET A 142 ? 0.2753 0.3571 0.3851 -0.0383 -0.0315 -0.0005 145 MET A SD  
2247 C CE  . MET A 142 ? 0.3221 0.3831 0.4171 -0.0542 -0.0391 -0.0032 145 MET A CE  
2257 N N   . LEU A 143 ? 0.2811 0.2564 0.2911 -0.0348 -0.0315 -0.0367 146 LEU A N   
2258 C CA  . LEU A 143 ? 0.3205 0.2737 0.3045 -0.0470 -0.0411 -0.0456 146 LEU A CA  
2259 C C   . LEU A 143 ? 0.3226 0.2610 0.2760 -0.0377 -0.0378 -0.0547 146 LEU A C   
2260 O O   . LEU A 143 ? 0.3643 0.2974 0.2957 -0.0473 -0.0480 -0.0606 146 LEU A O   
2261 C CB  . LEU A 143 ? 0.3701 0.2943 0.3489 -0.0540 -0.0419 -0.0496 146 LEU A CB  
2262 C CG  . LEU A 143 ? 0.3968 0.3387 0.4045 -0.0653 -0.0462 -0.0382 146 LEU A CG  
2263 C CD1 . LEU A 143 ? 0.4667 0.3789 0.4701 -0.0699 -0.0454 -0.0402 146 LEU A CD1 
2264 C CD2 . LEU A 143 ? 0.4642 0.4247 0.4805 -0.0829 -0.0607 -0.0326 146 LEU A CD2 
2276 N N   . TYR A 144 ? 0.3220 0.2545 0.2723 -0.0196 -0.0243 -0.0549 147 TYR A N   
2277 C CA  . TYR A 144 ? 0.3364 0.2614 0.2604 -0.0084 -0.0186 -0.0601 147 TYR A CA  
2278 C C   . TYR A 144 ? 0.3129 0.2709 0.2440 -0.0100 -0.0243 -0.0528 147 TYR A C   
2279 O O   . TYR A 144 ? 0.3459 0.2988 0.2481 -0.0117 -0.0283 -0.0587 147 TYR A O   
2280 C CB  . TYR A 144 ? 0.3507 0.2717 0.2815 0.0122  -0.0022 -0.0554 147 TYR A CB  
2281 C CG  . TYR A 144 ? 0.3961 0.3138 0.3033 0.0269  0.0070  -0.0571 147 TYR A CG  
2282 C CD1 . TYR A 144 ? 0.4681 0.3504 0.3369 0.0319  0.0123  -0.0702 147 TYR A CD1 
2283 C CD2 . TYR A 144 ? 0.3924 0.3424 0.3154 0.0350  0.0097  -0.0452 147 TYR A CD2 
2284 C CE1 . TYR A 144 ? 0.5023 0.3831 0.3456 0.0467  0.0222  -0.0716 147 TYR A CE1 
2285 C CE2 . TYR A 144 ? 0.4678 0.4197 0.3695 0.0486  0.0186  -0.0440 147 TYR A CE2 
2286 C CZ  . TYR A 144 ? 0.4905 0.4086 0.3523 0.0548  0.0255  -0.0571 147 TYR A CZ  
2287 O OH  . TYR A 144 ? 0.5828 0.5005 0.4172 0.0708  0.0370  -0.0568 147 TYR A OH  
2297 N N   . ILE A 145 ? 0.2840 0.2742 0.2507 -0.0081 -0.0240 -0.0401 148 ILE A N   
2298 C CA  . ILE A 145 ? 0.2744 0.2967 0.2533 -0.0089 -0.0289 -0.0308 148 ILE A CA  
2299 C C   . ILE A 145 ? 0.3154 0.3431 0.2842 -0.0269 -0.0439 -0.0325 148 ILE A C   
2300 O O   . ILE A 145 ? 0.3218 0.3590 0.2734 -0.0289 -0.0493 -0.0315 148 ILE A O   
2301 C CB  . ILE A 145 ? 0.2524 0.3010 0.2720 -0.0057 -0.0271 -0.0191 148 ILE A CB  
2302 C CG1 . ILE A 145 ? 0.2656 0.3125 0.2937 0.0106  -0.0159 -0.0151 148 ILE A CG1 
2303 C CG2 . ILE A 145 ? 0.2816 0.3628 0.3197 -0.0091 -0.0336 -0.0080 148 ILE A CG2 
2304 C CD1 . ILE A 145 ? 0.3234 0.3841 0.3848 0.0124  -0.0153 -0.0083 148 ILE A CD1 
2316 N N   . LEU A 146 ? 0.3157 0.3374 0.2929 -0.0410 -0.0516 -0.0340 149 LEU A N   
2317 C CA  . LEU A 146 ? 0.3347 0.3648 0.3077 -0.0600 -0.0679 -0.0321 149 LEU A CA  
2318 C C   . LEU A 146 ? 0.3735 0.3734 0.2996 -0.0671 -0.0759 -0.0465 149 LEU A C   
2319 O O   . LEU A 146 ? 0.4045 0.4154 0.3164 -0.0781 -0.0890 -0.0449 149 LEU A O   
2320 C CB  . LEU A 146 ? 0.3801 0.4124 0.3763 -0.0734 -0.0739 -0.0274 149 LEU A CB  
2321 C CG  . LEU A 146 ? 0.4273 0.4865 0.4639 -0.0654 -0.0650 -0.0151 149 LEU A CG  
2322 C CD1 . LEU A 146 ? 0.4806 0.5455 0.5376 -0.0792 -0.0707 -0.0081 149 LEU A CD1 
2323 C CD2 . LEU A 146 ? 0.4352 0.5291 0.4942 -0.0598 -0.0646 -0.0033 149 LEU A CD2 
2335 N N   . TYR A 147 ? 0.3714 0.3319 0.2705 -0.0601 -0.0680 -0.0607 150 TYR A N   
2336 C CA  . TYR A 147 ? 0.4336 0.3584 0.2818 -0.0631 -0.0727 -0.0775 150 TYR A CA  
2337 C C   . TYR A 147 ? 0.4411 0.3800 0.2664 -0.0517 -0.0685 -0.0768 150 TYR A C   
2338 O O   . TYR A 147 ? 0.4808 0.4139 0.2721 -0.0614 -0.0806 -0.0833 150 TYR A O   
2339 C CB  . TYR A 147 ? 0.4822 0.3653 0.3126 -0.0512 -0.0595 -0.0899 150 TYR A CB  
2340 C CG  . TYR A 147 ? 0.6031 0.4443 0.3789 -0.0504 -0.0610 -0.1090 150 TYR A CG  
2341 C CD1 . TYR A 147 ? 0.7589 0.5669 0.5107 -0.0703 -0.0778 -0.1217 150 TYR A CD1 
2342 C CD2 . TYR A 147 ? 0.7268 0.5611 0.4748 -0.0292 -0.0456 -0.1139 150 TYR A CD2 
2343 C CE1 . TYR A 147 ? 0.8598 0.6235 0.5557 -0.0693 -0.0799 -0.1422 150 TYR A CE1 
2344 C CE2 . TYR A 147 ? 0.7853 0.5783 0.4769 -0.0257 -0.0447 -0.1333 150 TYR A CE2 
2345 C CZ  . TYR A 147 ? 0.8328 0.5885 0.4967 -0.0458 -0.0621 -0.1489 150 TYR A CZ  
2346 O OH  . TYR A 147 ? 1.0279 0.7364 0.6308 -0.0425 -0.0620 -0.1710 150 TYR A OH  
2356 N N   . VAL A 148 ? 0.4086 0.3676 0.2519 -0.0320 -0.0526 -0.0673 151 VAL A N   
2357 C CA  . VAL A 148 ? 0.4316 0.4072 0.2567 -0.0206 -0.0476 -0.0632 151 VAL A CA  
2358 C C   . VAL A 148 ? 0.4101 0.4231 0.2490 -0.0342 -0.0630 -0.0507 151 VAL A C   
2359 O O   . VAL A 148 ? 0.4658 0.4844 0.2736 -0.0363 -0.0689 -0.0519 151 VAL A O   
2360 C CB  . VAL A 148 ? 0.4271 0.4193 0.2782 0.0014  -0.0289 -0.0516 151 VAL A CB  
2361 C CG1 . VAL A 148 ? 0.4390 0.4588 0.2838 0.0128  -0.0238 -0.0405 151 VAL A CG1 
2362 C CG2 . VAL A 148 ? 0.4719 0.4286 0.3073 0.0156  -0.0137 -0.0616 151 VAL A CG2 
2372 N N   . LEU A 149 ? 0.3765 0.4174 0.2618 -0.0425 -0.0687 -0.0374 152 LEU A N   
2373 C CA  . LEU A 149 ? 0.3920 0.4711 0.2965 -0.0532 -0.0815 -0.0223 152 LEU A CA  
2374 C C   . LEU A 149 ? 0.4810 0.5497 0.3540 -0.0747 -0.1018 -0.0293 152 LEU A C   
2375 O O   . LEU A 149 ? 0.4843 0.5783 0.3509 -0.0820 -0.1129 -0.0200 152 LEU A O   
2376 C CB  . LEU A 149 ? 0.3799 0.4861 0.3383 -0.0567 -0.0823 -0.0079 152 LEU A CB  
2377 C CG  . LEU A 149 ? 0.4006 0.5195 0.3908 -0.0382 -0.0665 0.0002  152 LEU A CG  
2378 C CD1 . LEU A 149 ? 0.4116 0.5549 0.4500 -0.0422 -0.0681 0.0127  152 LEU A CD1 
2379 C CD2 . LEU A 149 ? 0.4189 0.5607 0.4101 -0.0266 -0.0619 0.0111  152 LEU A CD2 
2391 N N   . PHE A 150 ? 0.4821 0.5120 0.3313 -0.0861 -0.1085 -0.0456 153 PHE A N   
2392 C CA  . PHE A 150 ? 0.5504 0.5649 0.3664 -0.1095 -0.1313 -0.0537 153 PHE A CA  
2393 C C   . PHE A 150 ? 0.6566 0.6291 0.4060 -0.1070 -0.1323 -0.0758 153 PHE A C   
2394 O O   . PHE A 150 ? 0.7415 0.7077 0.4549 -0.1240 -0.1521 -0.0814 153 PHE A O   
2395 C CB  . PHE A 150 ? 0.6139 0.6089 0.4456 -0.1260 -0.1405 -0.0571 153 PHE A CB  
2396 C CG  . PHE A 150 ? 0.6254 0.6605 0.5094 -0.1386 -0.1494 -0.0358 153 PHE A CG  
2397 C CD1 . PHE A 150 ? 0.6104 0.6685 0.4970 -0.1596 -0.1715 -0.0250 153 PHE A CD1 
2398 C CD2 . PHE A 150 ? 0.6258 0.6772 0.5556 -0.1289 -0.1356 -0.0254 153 PHE A CD2 
2399 C CE1 . PHE A 150 ? 0.7053 0.8023 0.6444 -0.1672 -0.1758 -0.0024 153 PHE A CE1 
2400 C CE2 . PHE A 150 ? 0.6695 0.7583 0.6463 -0.1384 -0.1417 -0.0052 153 PHE A CE2 
2401 C CZ  . PHE A 150 ? 0.5876 0.7007 0.5702 -0.1581 -0.1623 0.0072  153 PHE A CZ  
2411 N N   . PHE A 151 ? 0.7024 0.6439 0.4308 -0.0869 -0.1127 -0.0889 154 PHE A N   
2412 C CA  . PHE A 151 ? 0.7535 0.6490 0.4160 -0.0824 -0.1113 -0.1118 154 PHE A CA  
2413 C C   . PHE A 151 ? 1.0015 0.9045 0.6419 -0.0557 -0.0903 -0.1110 154 PHE A C   
2414 O O   . PHE A 151 ? 1.1068 0.9743 0.6891 -0.0471 -0.0850 -0.1291 154 PHE A O   
2415 C CB  . PHE A 151 ? 0.7853 0.6279 0.4348 -0.0831 -0.1075 -0.1298 154 PHE A CB  
2416 C CG  . PHE A 151 ? 0.7229 0.5576 0.3924 -0.1112 -0.1297 -0.1290 154 PHE A CG  
2417 C CD1 . PHE A 151 ? 0.8805 0.7422 0.6085 -0.1163 -0.1291 -0.1122 154 PHE A CD1 
2418 C CD2 . PHE A 151 ? 0.8143 0.6201 0.4497 -0.1298 -0.1492 -0.1426 154 PHE A CD2 
2419 C CE1 . PHE A 151 ? 0.8191 0.6773 0.5671 -0.1410 -0.1481 -0.1082 154 PHE A CE1 
2420 C CE2 . PHE A 151 ? 0.9342 0.7423 0.6022 -0.1516 -0.1658 -0.1357 154 PHE A CE2 
2421 C CZ  . PHE A 151 ? 0.8979 0.7310 0.6192 -0.1583 -0.1660 -0.1184 154 PHE A CZ  
2431 N N   . GLY A 152 ? 1.4401 0.4422 0.8684 -0.0791 -0.0905 -0.1797 155 GLY A N   
2432 C CA  . GLY A 152 ? 1.4151 0.4832 0.8098 -0.0221 -0.0532 -0.1970 155 GLY A CA  
2433 C C   . GLY A 152 ? 1.3435 0.5235 0.7604 -0.0413 -0.0441 -0.1741 155 GLY A C   
2434 O O   . GLY A 152 ? 1.3953 0.5972 0.7548 -0.0201 -0.0501 -0.2017 155 GLY A O   
2438 N N   . PHE A 153 ? 1.2304 0.4828 0.7278 -0.0786 -0.0325 -0.1240 156 PHE A N   
2439 C CA  . PHE A 153 ? 1.1483 0.5141 0.6753 -0.0898 -0.0198 -0.0986 156 PHE A CA  
2440 C C   . PHE A 153 ? 1.4346 0.7977 0.9341 -0.1343 -0.0576 -0.1088 156 PHE A C   
2441 O O   . PHE A 153 ? 1.2888 0.7147 0.7656 -0.1264 -0.0538 -0.1155 156 PHE A O   
2442 C CB  . PHE A 153 ? 1.0257 0.4637 0.6407 -0.1077 -0.0024 -0.0465 156 PHE A CB  
2443 C CG  . PHE A 153 ? 0.9479 0.4245 0.5989 -0.0623 0.0326  -0.0300 156 PHE A CG  
2444 C CD1 . PHE A 153 ? 1.0548 0.4882 0.6692 -0.0149 0.0501  -0.0549 156 PHE A CD1 
2445 C CD2 . PHE A 153 ? 0.9033 0.4590 0.6243 -0.0645 0.0429  0.0108  156 PHE A CD2 
2446 C CE1 . PHE A 153 ? 0.9273 0.3985 0.5821 0.0230  0.0783  -0.0338 156 PHE A CE1 
2447 C CE2 . PHE A 153 ? 0.9164 0.5013 0.6756 -0.0243 0.0651  0.0278  156 PHE A CE2 
2448 C CZ  . PHE A 153 ? 0.8894 0.4332 0.6186 0.0167  0.0836  0.0080  156 PHE A CZ  
2458 N N   . THR A 154 ? 1.3196 0.6173 0.8280 -0.1834 -0.0957 -0.1035 157 THR A N   
2459 C CA  . THR A 154 ? 1.4916 0.7901 0.9875 -0.2328 -0.1363 -0.1041 157 THR A CA  
2460 C C   . THR A 154 ? 1.6473 0.9019 1.0510 -0.2067 -0.1596 -0.1603 157 THR A C   
2461 O O   . THR A 154 ? 1.4792 0.7855 0.8679 -0.2225 -0.1704 -0.1625 157 THR A O   
2462 C CB  . THR A 154 ? 1.4085 0.6386 0.9350 -0.2883 -0.1791 -0.0822 157 THR A CB  
2463 O OG1 . THR A 154 ? 1.2296 0.5332 0.8411 -0.3081 -0.1546 -0.0231 157 THR A OG1 
2464 C CG2 . THR A 154 ? 1.4629 0.6724 0.9705 -0.3401 -0.2328 -0.0865 157 THR A CG2 
2472 N N   . SER A 155 ? 1.9027 1.0682 1.2403 -0.1592 -0.1661 -0.2071 158 SER A N   
2473 C CA  . SER A 155 ? 2.0801 1.1976 1.3167 -0.1204 -0.1930 -0.2667 158 SER A CA  
2474 C C   . SER A 155 ? 2.0374 1.2674 1.2495 -0.0684 -0.1482 -0.2696 158 SER A C   
2475 O O   . SER A 155 ? 2.0987 1.3257 1.2335 -0.0407 -0.1680 -0.3088 158 SER A O   
2476 C CB  . SER A 155 ? 2.2245 1.2126 1.3941 -0.0771 -0.2167 -0.3166 158 SER A CB  
2477 O OG  . SER A 155 ? 2.2551 1.2742 1.4365 -0.0241 -0.1627 -0.3100 158 SER A OG  
2480 N N   . LYS A 156 ? 1.6924 1.0225 0.9695 -0.0526 -0.0932 -0.2266 159 LYS A N   
2481 C CA  . LYS A 156 ? 1.6602 1.1087 0.9319 -0.0114 -0.0557 -0.2149 159 LYS A CA  
2482 C C   . LYS A 156 ? 1.5654 1.1119 0.8861 -0.0571 -0.0562 -0.1790 159 LYS A C   
2483 O O   . LYS A 156 ? 1.5427 1.1542 0.8268 -0.0383 -0.0536 -0.1871 159 LYS A O   
2484 C CB  . LYS A 156 ? 1.5114 1.0188 0.8338 0.0284  -0.0056 -0.1824 159 LYS A CB  
2485 C CG  . LYS A 156 ? 1.4840 1.1117 0.8007 0.0781  0.0292  -0.1649 159 LYS A CG  
2486 C CD  . LYS A 156 ? 1.3493 0.9867 0.6591 0.1429  0.0638  -0.1621 159 LYS A CD  
2487 C CE  . LYS A 156 ? 1.3955 1.1577 0.6904 0.1974  0.0938  -0.1420 159 LYS A CE  
2488 N NZ  . LYS A 156 ? 1.1556 1.0419 0.5502 0.1667  0.1103  -0.0756 159 LYS A NZ  
2502 N N   . ALA A 157 ? 1.4937 1.0551 0.8935 -0.1130 -0.0602 -0.1391 160 ALA A N   
2503 C CA  . ALA A 157 ? 1.2590 0.9113 0.7064 -0.1551 -0.0630 -0.1049 160 ALA A CA  
2504 C C   . ALA A 157 ? 1.3784 1.0101 0.7662 -0.1789 -0.1009 -0.1346 160 ALA A C   
2505 O O   . ALA A 157 ? 1.2256 0.9442 0.6197 -0.1871 -0.0964 -0.1211 160 ALA A O   
2506 C CB  . ALA A 157 ? 1.1621 0.8171 0.6867 -0.2045 -0.0693 -0.0649 160 ALA A CB  
2512 N N   . GLU A 158 ? 1.5511 1.0641 0.8844 -0.1919 -0.1443 -0.1734 161 GLU A N   
2513 C CA  . GLU A 158 ? 1.5811 1.0516 0.8568 -0.2167 -0.1939 -0.2049 161 GLU A CA  
2514 C C   . GLU A 158 ? 1.7223 1.2179 0.9103 -0.1582 -0.1902 -0.2473 161 GLU A C   
2515 O O   . GLU A 158 ? 1.7071 1.1720 0.8381 -0.1694 -0.2324 -0.2784 161 GLU A O   
2516 C CB  . GLU A 158 ? 1.7705 1.0948 1.0151 -0.2411 -0.2506 -0.2338 161 GLU A CB  
2517 C CG  . GLU A 158 ? 1.7975 1.1098 1.1310 -0.3056 -0.2611 -0.1828 161 GLU A CG  
2518 C CD  . GLU A 158 ? 1.9333 1.1279 1.2535 -0.3549 -0.3334 -0.1938 161 GLU A CD  
2519 O OE1 . GLU A 158 ? 2.0098 1.0918 1.2476 -0.3274 -0.3774 -0.2513 161 GLU A OE1 
2520 O OE2 . GLU A 158 ? 1.8393 1.0554 1.2337 -0.4184 -0.3500 -0.1418 161 GLU A OE2 
2527 N N   . SER A 159 ? 1.6297 1.1850 0.8064 -0.0938 -0.1430 -0.2460 162 SER A N   
2528 C CA  . SER A 159 ? 1.6388 1.2512 0.7404 -0.0300 -0.1303 -0.2728 162 SER A CA  
2529 C C   . SER A 159 ? 1.5033 1.2770 0.6664 -0.0233 -0.0828 -0.2189 162 SER A C   
2530 O O   . SER A 159 ? 1.4983 1.3492 0.6158 0.0334  -0.0622 -0.2244 162 SER A O   
2531 C CB  . SER A 159 ? 1.7571 1.3168 0.7868 0.0492  -0.1190 -0.3124 162 SER A CB  
2532 O OG  . SER A 159 ? 1.6876 1.2493 0.7828 0.0536  -0.0833 -0.2807 162 SER A OG  
2538 N N   . MET A 160 ? 1.2976 1.1265 0.5629 -0.0768 -0.0689 -0.1650 163 MET A N   
2539 C CA  . MET A 160 ? 1.1759 1.1453 0.5113 -0.0758 -0.0347 -0.1105 163 MET A CA  
2540 C C   . MET A 160 ? 1.1318 1.1520 0.4975 -0.1329 -0.0548 -0.0916 163 MET A C   
2541 O O   . MET A 160 ? 1.2023 1.1567 0.5263 -0.1677 -0.0933 -0.1219 163 MET A O   
2542 C CB  . MET A 160 ? 1.1617 1.1498 0.5876 -0.0804 -0.0086 -0.0667 163 MET A CB  
2543 C CG  . MET A 160 ? 1.3374 1.2435 0.7345 -0.0394 0.0025  -0.0906 163 MET A CG  
2544 S SD  . MET A 160 ? 1.1922 1.1373 0.6845 -0.0222 0.0377  -0.0400 163 MET A SD  
2545 C CE  . MET A 160 ? 0.9831 1.0914 0.5472 -0.0144 0.0583  0.0218  163 MET A CE  
2555 N N   . ARG A 161 ? 1.0483 1.1845 0.4906 -0.1431 -0.0332 -0.0389 164 ARG A N   
2556 C CA  . ARG A 161 ? 0.9603 1.1556 0.4378 -0.1936 -0.0496 -0.0165 164 ARG A CA  
2557 C C   . ARG A 161 ? 0.9604 1.0802 0.4564 -0.2526 -0.0799 -0.0218 164 ARG A C   
2558 O O   . ARG A 161 ? 0.9395 1.0034 0.4669 -0.2588 -0.0777 -0.0156 164 ARG A O   
2559 C CB  . ARG A 161 ? 0.8287 1.1382 0.4022 -0.1969 -0.0290 0.0445  164 ARG A CB  
2560 C CG  . ARG A 161 ? 0.8191 1.2307 0.3936 -0.1492 -0.0036 0.0685  164 ARG A CG  
2561 C CD  . ARG A 161 ? 0.7950 1.2779 0.4702 -0.1404 0.0121  0.1278  164 ARG A CD  
2562 N NE  . ARG A 161 ? 0.7736 1.2911 0.5254 -0.1871 -0.0075 0.1609  164 ARG A NE  
2563 C CZ  . ARG A 161 ? 0.6991 1.2551 0.5411 -0.1873 -0.0107 0.2067  164 ARG A CZ  
2564 N NH1 . ARG A 161 ? 0.6037 1.1793 0.4817 -0.1495 0.0052  0.2331  164 ARG A NH1 
2565 N NH2 . ARG A 161 ? 0.6351 1.2001 0.5419 -0.2186 -0.0367 0.2189  164 ARG A NH2 
2579 N N   . PRO A 162 ? 0.6908 0.5688 0.2878 0.0287  -0.1828 -0.0191 165 PRO A N   
2580 C CA  . PRO A 162 ? 0.6866 0.5768 0.3101 0.0121  -0.1975 -0.0247 165 PRO A CA  
2581 C C   . PRO A 162 ? 0.6507 0.5715 0.3284 0.0118  -0.1934 -0.0157 165 PRO A C   
2582 O O   . PRO A 162 ? 0.6396 0.5647 0.3420 0.0017  -0.1947 -0.0208 165 PRO A O   
2583 C CB  . PRO A 162 ? 0.6935 0.5932 0.3023 0.0031  -0.2193 -0.0255 165 PRO A CB  
2584 C CG  . PRO A 162 ? 0.7451 0.6252 0.3106 0.0125  -0.2135 -0.0261 165 PRO A CG  
2585 C CD  . PRO A 162 ? 0.7311 0.6042 0.2920 0.0309  -0.1943 -0.0178 165 PRO A CD  
2593 N N   . GLU A 163 ? 0.6393 0.5792 0.3348 0.0224  -0.1877 -0.0023 166 GLU A N   
2594 C CA  . GLU A 163 ? 0.6010 0.5649 0.3440 0.0224  -0.1830 0.0054  166 GLU A CA  
2595 C C   . GLU A 163 ? 0.6318 0.5878 0.3887 0.0253  -0.1645 0.0036  166 GLU A C   
2596 O O   . GLU A 163 ? 0.5953 0.5648 0.3868 0.0206  -0.1623 0.0043  166 GLU A O   
2597 C CB  . GLU A 163 ? 0.7428 0.7239 0.4973 0.0327  -0.1816 0.0202  166 GLU A CB  
2598 C CG  . GLU A 163 ? 0.7266 0.6952 0.4629 0.0448  -0.1649 0.0267  166 GLU A CG  
2599 C CD  . GLU A 163 ? 0.8684 0.8228 0.5609 0.0503  -0.1691 0.0268  166 GLU A CD  
2600 O OE1 . GLU A 163 ? 0.8276 0.7724 0.4959 0.0434  -0.1823 0.0169  166 GLU A OE1 
2601 O OE2 . GLU A 163 ? 1.0116 0.9633 0.6915 0.0607  -0.1592 0.0366  166 GLU A OE2 
2608 N N   . VAL A 164 ? 0.6007 0.5365 0.3306 0.0333  -0.1511 0.0015  167 VAL A N   
2609 C CA  . VAL A 164 ? 0.5582 0.4894 0.3008 0.0361  -0.1347 0.0000  167 VAL A CA  
2610 C C   . VAL A 164 ? 0.5278 0.4454 0.2688 0.0263  -0.1392 -0.0123 167 VAL A C   
2611 O O   . VAL A 164 ? 0.5583 0.4830 0.3271 0.0223  -0.1342 -0.0131 167 VAL A O   
2612 C CB  . VAL A 164 ? 0.6092 0.5262 0.3235 0.0489  -0.1190 0.0027  167 VAL A CB  
2613 C CG1 . VAL A 164 ? 0.6645 0.5782 0.3895 0.0524  -0.1034 0.0009  167 VAL A CG1 
2614 C CG2 . VAL A 164 ? 0.6689 0.6004 0.3887 0.0564  -0.1134 0.0163  167 VAL A CG2 
2624 N N   . ALA A 165 ? 0.6263 0.5232 0.3338 0.0207  -0.1497 -0.0220 168 ALA A N   
2625 C CA  . ALA A 165 ? 0.6000 0.4793 0.3033 0.0099  -0.1531 -0.0336 168 ALA A CA  
2626 C C   . ALA A 165 ? 0.6167 0.5190 0.3594 -0.0040 -0.1641 -0.0331 168 ALA A C   
2627 O O   . ALA A 165 ? 0.5906 0.4893 0.3495 -0.0096 -0.1592 -0.0371 168 ALA A O   
2628 C CB  . ALA A 165 ? 0.7077 0.5564 0.3633 0.0046  -0.1630 -0.0447 168 ALA A CB  
2634 N N   . SER A 166 ? 0.5952 0.5219 0.3534 -0.0093 -0.1786 -0.0279 169 SER A N   
2635 C CA  . SER A 166 ? 0.6101 0.5604 0.4047 -0.0219 -0.1887 -0.0271 169 SER A CA  
2636 C C   . SER A 166 ? 0.5702 0.5386 0.4045 -0.0162 -0.1761 -0.0198 169 SER A C   
2637 O O   . SER A 166 ? 0.5470 0.5217 0.4052 -0.0247 -0.1755 -0.0224 169 SER A O   
2638 C CB  . SER A 166 ? 0.5787 0.5548 0.3821 -0.0270 -0.2072 -0.0218 169 SER A CB  
2639 O OG  . SER A 166 ? 0.7272 0.7139 0.5297 -0.0127 -0.2038 -0.0110 169 SER A OG  
2645 N N   . THR A 167 ? 0.5019 0.4767 0.3412 -0.0028 -0.1653 -0.0107 170 THR A N   
2646 C CA  . THR A 167 ? 0.4707 0.4598 0.3433 0.0015  -0.1536 -0.0042 170 THR A CA  
2647 C C   . THR A 167 ? 0.4458 0.4199 0.3175 0.0014  -0.1406 -0.0098 170 THR A C   
2648 O O   . THR A 167 ? 0.4396 0.4232 0.3389 -0.0024 -0.1362 -0.0094 170 THR A O   
2649 C CB  . THR A 167 ? 0.4970 0.4933 0.3711 0.0133  -0.1463 0.0067  170 THR A CB  
2650 O OG1 . THR A 167 ? 0.5314 0.5424 0.4090 0.0146  -0.1583 0.0132  170 THR A OG1 
2651 C CG2 . THR A 167 ? 0.5105 0.5163 0.4139 0.0159  -0.1336 0.0120  170 THR A CG2 
2659 N N   . PHE A 168 ? 0.4721 0.4232 0.3120 0.0070  -0.1336 -0.0142 171 PHE A N   
2660 C CA  . PHE A 168 ? 0.4712 0.4090 0.3098 0.0088  -0.1214 -0.0184 171 PHE A CA  
2661 C C   . PHE A 168 ? 0.4762 0.4072 0.3220 -0.0039 -0.1282 -0.0265 171 PHE A C   
2662 O O   . PHE A 168 ? 0.4556 0.3899 0.3211 -0.0053 -0.1208 -0.0264 171 PHE A O   
2663 C CB  . PHE A 168 ? 0.4771 0.3898 0.2769 0.0187  -0.1128 -0.0218 171 PHE A CB  
2664 C CG  . PHE A 168 ? 0.5461 0.4424 0.3399 0.0222  -0.1014 -0.0262 171 PHE A CG  
2665 C CD1 . PHE A 168 ? 0.4971 0.4075 0.3114 0.0295  -0.0880 -0.0194 171 PHE A CD1 
2666 C CD2 . PHE A 168 ? 0.6303 0.4977 0.3989 0.0173  -0.1046 -0.0365 171 PHE A CD2 
2667 C CE1 . PHE A 168 ? 0.5778 0.4764 0.3881 0.0341  -0.0779 -0.0218 171 PHE A CE1 
2668 C CE2 . PHE A 168 ? 0.6060 0.4573 0.3691 0.0222  -0.0933 -0.0392 171 PHE A CE2 
2669 C CZ  . PHE A 168 ? 0.5803 0.4486 0.3647 0.0316  -0.0800 -0.0314 171 PHE A CZ  
2679 N N   . LYS A 169 ? 0.5034 0.4234 0.3310 -0.0141 -0.1421 -0.0336 172 LYS A N   
2680 C CA  . LYS A 169 ? 0.5146 0.4254 0.3457 -0.0287 -0.1486 -0.0413 172 LYS A CA  
2681 C C   . LYS A 169 ? 0.4914 0.4315 0.3670 -0.0356 -0.1504 -0.0361 172 LYS A C   
2682 O O   . LYS A 169 ? 0.4853 0.4208 0.3730 -0.0412 -0.1453 -0.0387 172 LYS A O   
2683 C CB  . LYS A 169 ? 0.5600 0.4582 0.3649 -0.0413 -0.1655 -0.0488 172 LYS A CB  
2684 C CG  . LYS A 169 ? 0.6791 0.5346 0.4350 -0.0378 -0.1609 -0.0583 172 LYS A CG  
2685 C CD  . LYS A 169 ? 0.8587 0.6974 0.5846 -0.0541 -0.1792 -0.0676 172 LYS A CD  
2686 C CE  . LYS A 169 ? 1.0865 0.8947 0.7618 -0.0447 -0.1776 -0.0727 172 LYS A CE  
2687 N NZ  . LYS A 169 ? 1.2311 1.0127 0.8684 -0.0616 -0.1938 -0.0844 172 LYS A NZ  
2690 N N   . VAL A 170 ? 0.4437 0.4125 0.3423 -0.0342 -0.1567 -0.0284 173 VAL A N   
2691 C CA  . VAL A 170 ? 0.4366 0.4324 0.3761 -0.0376 -0.1560 -0.0229 173 VAL A CA  
2692 C C   . VAL A 170 ? 0.4232 0.4183 0.3770 -0.0297 -0.1398 -0.0199 173 VAL A C   
2693 O O   . VAL A 170 ? 0.3855 0.3865 0.3600 -0.0352 -0.1362 -0.0206 173 VAL A O   
2694 C CB  . VAL A 170 ? 0.3857 0.4093 0.3435 -0.0335 -0.1638 -0.0141 173 VAL A CB  
2695 C CG1 . VAL A 170 ? 0.4236 0.4722 0.4208 -0.0331 -0.1598 -0.0077 173 VAL A CG1 
2696 C CG2 . VAL A 170 ? 0.4854 0.5152 0.4318 -0.0428 -0.1819 -0.0162 173 VAL A CG2 
2706 N N   . LEU A 171 ? 0.3728 0.3643 0.3181 -0.0172 -0.1299 -0.0155 174 LEU A N   
2707 C CA  . LEU A 171 ? 0.3456 0.3406 0.3059 -0.0114 -0.1158 -0.0120 174 LEU A CA  
2708 C C   . LEU A 171 ? 0.3847 0.3611 0.3335 -0.0122 -0.1082 -0.0177 174 LEU A C   
2709 O O   . LEU A 171 ? 0.3608 0.3433 0.3277 -0.0125 -0.1006 -0.0162 174 LEU A O   
2710 C CB  . LEU A 171 ? 0.3709 0.3669 0.3221 -0.0005 -0.1085 -0.0057 174 LEU A CB  
2711 C CG  . LEU A 171 ? 0.3811 0.3925 0.3438 0.0022  -0.1130 0.0019  174 LEU A CG  
2712 C CD1 . LEU A 171 ? 0.4564 0.4656 0.4075 0.0111  -0.1047 0.0084  174 LEU A CD1 
2713 C CD2 . LEU A 171 ? 0.4131 0.4407 0.4079 -0.0003 -0.1108 0.0055  174 LEU A CD2 
2725 N N   A ARG A 172 ? 0.3937 0.3461 0.3111 -0.0118 -0.1097 -0.0240 175 ARG A N   
2726 N N   B ARG A 172 ? 0.3944 0.3469 0.3120 -0.0120 -0.1099 -0.0241 175 ARG A N   
2727 C CA  A ARG A 172 ? 0.4195 0.3498 0.3231 -0.0114 -0.1022 -0.0293 175 ARG A CA  
2728 C CA  B ARG A 172 ? 0.4205 0.3513 0.3245 -0.0114 -0.1021 -0.0291 175 ARG A CA  
2729 C C   A ARG A 172 ? 0.4208 0.3526 0.3419 -0.0246 -0.1068 -0.0326 175 ARG A C   
2730 C C   B ARG A 172 ? 0.4217 0.3521 0.3414 -0.0246 -0.1068 -0.0329 175 ARG A C   
2731 O O   A ARG A 172 ? 0.4064 0.3360 0.3372 -0.0237 -0.0982 -0.0319 175 ARG A O   
2732 O O   B ARG A 172 ? 0.4148 0.3398 0.3407 -0.0236 -0.0981 -0.0329 175 ARG A O   
2733 C CB  A ARG A 172 ? 0.5548 0.4543 0.4171 -0.0085 -0.1034 -0.0361 175 ARG A CB  
2734 C CB  B ARG A 172 ? 0.5507 0.4508 0.4134 -0.0077 -0.1026 -0.0357 175 ARG A CB  
2735 C CG  A ARG A 172 ? 0.5677 0.4348 0.4076 -0.0095 -0.0979 -0.0432 175 ARG A CG  
2736 C CG  B ARG A 172 ? 0.5285 0.4001 0.3707 -0.0035 -0.0929 -0.0403 175 ARG A CG  
2737 C CD  A ARG A 172 ? 0.6040 0.4379 0.4034 -0.0152 -0.1062 -0.0528 175 ARG A CD  
2738 C CD  B ARG A 172 ? 0.6314 0.4751 0.4529 -0.0172 -0.1021 -0.0502 175 ARG A CD  
2739 N NE  A ARG A 172 ? 0.6547 0.4917 0.4611 -0.0351 -0.1225 -0.0577 175 ARG A NE  
2740 N NE  B ARG A 172 ? 0.6065 0.4268 0.3903 -0.0177 -0.1091 -0.0567 175 ARG A NE  
2741 C CZ  A ARG A 172 ? 0.6501 0.4632 0.4249 -0.0450 -0.1336 -0.0662 175 ARG A CZ  
2742 C CZ  B ARG A 172 ? 0.6859 0.5087 0.4655 -0.0319 -0.1253 -0.0610 175 ARG A CZ  
2743 N NH1 A ARG A 172 ? 0.7485 0.5293 0.4802 -0.0358 -0.1293 -0.0715 175 ARG A NH1 
2744 N NH1 B ARG A 172 ? 0.6002 0.4511 0.4136 -0.0455 -0.1359 -0.0583 175 ARG A NH1 
2745 N NH2 A ARG A 172 ? 0.6636 0.4866 0.4500 -0.0648 -0.1491 -0.0692 175 ARG A NH2 
2746 N NH2 B ARG A 172 ? 0.6877 0.4855 0.4276 -0.0319 -0.1309 -0.0675 175 ARG A NH2 
2773 N N   . ASN A 173 ? 0.4581 0.3968 0.3853 -0.0371 -0.1204 -0.0351 176 ASN A N   
2774 C CA  . ASN A 173 ? 0.4477 0.3898 0.3917 -0.0513 -0.1248 -0.0376 176 ASN A CA  
2775 C C   . ASN A 173 ? 0.4120 0.3809 0.3930 -0.0499 -0.1190 -0.0308 176 ASN A C   
2776 O O   . ASN A 173 ? 0.4005 0.3668 0.3924 -0.0548 -0.1135 -0.0314 176 ASN A O   
2777 C CB  . ASN A 173 ? 0.4235 0.3736 0.3673 -0.0657 -0.1420 -0.0403 176 ASN A CB  
2778 C CG  . ASN A 173 ? 0.4985 0.4154 0.4015 -0.0720 -0.1488 -0.0495 176 ASN A CG  
2779 O OD1 . ASN A 173 ? 0.6150 0.4992 0.4894 -0.0656 -0.1393 -0.0542 176 ASN A OD1 
2780 N ND2 . ASN A 173 ? 0.5930 0.5174 0.4907 -0.0841 -0.1652 -0.0518 176 ASN A ND2 
2787 N N   . VAL A 174 ? 0.3515 0.3435 0.3498 -0.0425 -0.1189 -0.0242 177 VAL A N   
2788 C CA  . VAL A 174 ? 0.3319 0.3437 0.3592 -0.0393 -0.1118 -0.0184 177 VAL A CA  
2789 C C   . VAL A 174 ? 0.3291 0.3301 0.3526 -0.0333 -0.0986 -0.0184 177 VAL A C   
2790 O O   . VAL A 174 ? 0.3348 0.3416 0.3749 -0.0362 -0.0933 -0.0173 177 VAL A O   
2791 C CB  . VAL A 174 ? 0.3495 0.3790 0.3877 -0.0311 -0.1125 -0.0117 177 VAL A CB  
2792 C CG1 . VAL A 174 ? 0.3939 0.4351 0.4538 -0.0266 -0.1025 -0.0070 177 VAL A CG1 
2793 C CG2 . VAL A 174 ? 0.3849 0.4316 0.4341 -0.0362 -0.1253 -0.0098 177 VAL A CG2 
2803 N N   . THR A 175 ? 0.3336 0.3218 0.3358 -0.0239 -0.0930 -0.0183 178 THR A N   
2804 C CA  . THR A 175 ? 0.3285 0.3127 0.3287 -0.0165 -0.0809 -0.0163 178 THR A CA  
2805 C C   . THR A 175 ? 0.3265 0.2933 0.3189 -0.0202 -0.0776 -0.0204 178 THR A C   
2806 O O   . THR A 175 ? 0.3203 0.2926 0.3252 -0.0192 -0.0702 -0.0178 178 THR A O   
2807 C CB  . THR A 175 ? 0.3343 0.3114 0.3130 -0.0055 -0.0761 -0.0144 178 THR A CB  
2808 O OG1 . THR A 175 ? 0.3571 0.3500 0.3445 -0.0030 -0.0779 -0.0093 178 THR A OG1 
2809 C CG2 . THR A 175 ? 0.3584 0.3356 0.3349 0.0031  -0.0639 -0.0109 178 THR A CG2 
2817 N N   . VAL A 176 ? 0.3607 0.3039 0.3304 -0.0248 -0.0823 -0.0266 179 VAL A N   
2818 C CA  . VAL A 176 ? 0.3624 0.2828 0.3203 -0.0281 -0.0781 -0.0302 179 VAL A CA  
2819 C C   . VAL A 176 ? 0.3782 0.3104 0.3613 -0.0395 -0.0795 -0.0292 179 VAL A C   
2820 O O   . VAL A 176 ? 0.4030 0.3296 0.3890 -0.0380 -0.0713 -0.0275 179 VAL A O   
2821 C CB  . VAL A 176 ? 0.4568 0.3446 0.3812 -0.0323 -0.0831 -0.0378 179 VAL A CB  
2822 C CG1 . VAL A 176 ? 0.5210 0.3822 0.4341 -0.0386 -0.0792 -0.0413 179 VAL A CG1 
2823 C CG2 . VAL A 176 ? 0.5532 0.4276 0.4502 -0.0171 -0.0776 -0.0379 179 VAL A CG2 
2833 N N   . VAL A 177 ? 0.3431 0.2940 0.3455 -0.0500 -0.0891 -0.0291 180 VAL A N   
2834 C CA  . VAL A 177 ? 0.3509 0.3157 0.3781 -0.0600 -0.0892 -0.0272 180 VAL A CA  
2835 C C   . VAL A 177 ? 0.3215 0.3051 0.3697 -0.0524 -0.0801 -0.0215 180 VAL A C   
2836 O O   . VAL A 177 ? 0.3239 0.3064 0.3798 -0.0545 -0.0733 -0.0200 180 VAL A O   
2837 C CB  . VAL A 177 ? 0.3538 0.3389 0.3977 -0.0713 -0.1017 -0.0271 180 VAL A CB  
2838 C CG1 . VAL A 177 ? 0.3989 0.4047 0.4726 -0.0793 -0.0997 -0.0232 180 VAL A CG1 
2839 C CG2 . VAL A 177 ? 0.4587 0.4247 0.4805 -0.0830 -0.1124 -0.0335 180 VAL A CG2 
2849 N N   . LEU A 178 ? 0.2555 0.2558 0.3126 -0.0442 -0.0795 -0.0179 181 LEU A N   
2850 C CA  . LEU A 178 ? 0.2375 0.2533 0.3125 -0.0395 -0.0717 -0.0134 181 LEU A CA  
2851 C C   . LEU A 178 ? 0.2612 0.2672 0.3249 -0.0320 -0.0620 -0.0122 181 LEU A C   
2852 O O   . LEU A 178 ? 0.2582 0.2695 0.3320 -0.0325 -0.0557 -0.0101 181 LEU A O   
2853 C CB  . LEU A 178 ? 0.2528 0.2834 0.3357 -0.0335 -0.0732 -0.0100 181 LEU A CB  
2854 C CG  . LEU A 178 ? 0.2838 0.3292 0.3815 -0.0375 -0.0817 -0.0088 181 LEU A CG  
2855 C CD1 . LEU A 178 ? 0.3666 0.4195 0.4657 -0.0292 -0.0811 -0.0048 181 LEU A CD1 
2856 C CD2 . LEU A 178 ? 0.3469 0.4065 0.4675 -0.0425 -0.0795 -0.0070 181 LEU A CD2 
2868 N N   . TRP A 179 ? 0.2592 0.2530 0.3021 -0.0245 -0.0604 -0.0128 182 TRP A N   
2869 C CA  . TRP A 179 ? 0.2535 0.2445 0.2892 -0.0160 -0.0510 -0.0096 182 TRP A CA  
2870 C C   . TRP A 179 ? 0.2851 0.2600 0.3137 -0.0177 -0.0467 -0.0107 182 TRP A C   
2871 O O   . TRP A 179 ? 0.2713 0.2518 0.3042 -0.0136 -0.0397 -0.0068 182 TRP A O   
2872 C CB  . TRP A 179 ? 0.2697 0.2531 0.2852 -0.0057 -0.0485 -0.0087 182 TRP A CB  
2873 C CG  . TRP A 179 ? 0.2457 0.2457 0.2668 -0.0025 -0.0496 -0.0053 182 TRP A CG  
2874 C CD1 . TRP A 179 ? 0.2481 0.2589 0.2818 -0.0076 -0.0554 -0.0052 182 TRP A CD1 
2875 C CD2 . TRP A 179 ? 0.2581 0.2648 0.2708 0.0072  -0.0436 -0.0005 182 TRP A CD2 
2876 N NE1 . TRP A 179 ? 0.2822 0.3028 0.3138 -0.0024 -0.0534 -0.0008 182 TRP A NE1 
2877 C CE2 . TRP A 179 ? 0.2464 0.2660 0.2664 0.0055  -0.0466 0.0020  182 TRP A CE2 
2878 C CE3 . TRP A 179 ? 0.2770 0.2809 0.2771 0.0177  -0.0356 0.0029  182 TRP A CE3 
2879 C CZ2 . TRP A 179 ? 0.2763 0.3069 0.2917 0.0119  -0.0417 0.0079  182 TRP A CZ2 
2880 C CZ3 . TRP A 179 ? 0.2924 0.3126 0.2907 0.0255  -0.0307 0.0094  182 TRP A CZ3 
2881 C CH2 . TRP A 179 ? 0.2670 0.2987 0.2725 0.0210  -0.0342 0.0112  182 TRP A CH2 
2892 N N   A SER A 180 ? 0.2886 0.2438 0.3066 -0.0254 -0.0513 -0.0156 183 SER A N   
2893 N N   B SER A 180 ? 0.2885 0.2440 0.3067 -0.0254 -0.0512 -0.0155 183 SER A N   
2894 C CA  A SER A 180 ? 0.2807 0.2155 0.2893 -0.0286 -0.0469 -0.0164 183 SER A CA  
2895 C CA  B SER A 180 ? 0.2834 0.2187 0.2923 -0.0285 -0.0468 -0.0163 183 SER A CA  
2896 C C   A SER A 180 ? 0.2987 0.2482 0.3294 -0.0352 -0.0442 -0.0134 183 SER A C   
2897 C C   B SER A 180 ? 0.2990 0.2493 0.3302 -0.0349 -0.0440 -0.0132 183 SER A C   
2898 O O   A SER A 180 ? 0.3233 0.2610 0.3481 -0.0343 -0.0377 -0.0114 183 SER A O   
2899 O O   B SER A 180 ? 0.3212 0.2606 0.3470 -0.0337 -0.0373 -0.0110 183 SER A O   
2900 C CB  A SER A 180 ? 0.3569 0.2661 0.3483 -0.0386 -0.0531 -0.0226 183 SER A CB  
2901 C CB  B SER A 180 ? 0.3572 0.2676 0.3499 -0.0392 -0.0534 -0.0225 183 SER A CB  
2902 O OG  A SER A 180 ? 0.3922 0.2818 0.3567 -0.0307 -0.0537 -0.0258 183 SER A OG  
2903 O OG  B SER A 180 ? 0.3535 0.2800 0.3660 -0.0533 -0.0625 -0.0241 183 SER A OG  
2914 N N   . ALA A 181 ? 0.2563 0.2306 0.3111 -0.0406 -0.0481 -0.0124 184 ALA A N   
2915 C CA  . ALA A 181 ? 0.2730 0.2606 0.3467 -0.0452 -0.0439 -0.0095 184 ALA A CA  
2916 C C   . ALA A 181 ? 0.2423 0.2382 0.3176 -0.0363 -0.0359 -0.0053 184 ALA A C   
2917 O O   . ALA A 181 ? 0.2464 0.2443 0.3278 -0.0387 -0.0305 -0.0029 184 ALA A O   
2918 C CB  . ALA A 181 ? 0.2747 0.2855 0.3719 -0.0508 -0.0493 -0.0092 184 ALA A CB  
2924 N N   . TYR A 182 ? 0.2179 0.2204 0.2880 -0.0274 -0.0352 -0.0039 185 TYR A N   
2925 C CA  . TYR A 182 ? 0.2006 0.2147 0.2729 -0.0214 -0.0291 0.0004  185 TYR A CA  
2926 C C   . TYR A 182 ? 0.2244 0.2284 0.2860 -0.0170 -0.0227 0.0036  185 TYR A C   
2927 O O   . TYR A 182 ? 0.2195 0.2325 0.2879 -0.0180 -0.0187 0.0063  185 TYR A O   
2928 C CB  . TYR A 182 ? 0.2176 0.2415 0.2857 -0.0145 -0.0300 0.0022  185 TYR A CB  
2929 C CG  . TYR A 182 ? 0.1887 0.2242 0.2680 -0.0181 -0.0344 0.0010  185 TYR A CG  
2930 C CD1 . TYR A 182 ? 0.2088 0.2396 0.2876 -0.0202 -0.0406 -0.0019 185 TYR A CD1 
2931 C CD2 . TYR A 182 ? 0.2068 0.2561 0.2944 -0.0194 -0.0322 0.0030  185 TYR A CD2 
2932 C CE1 . TYR A 182 ? 0.2254 0.2662 0.3132 -0.0214 -0.0439 -0.0016 185 TYR A CE1 
2933 C CE2 . TYR A 182 ? 0.1978 0.2525 0.2920 -0.0216 -0.0351 0.0023  185 TYR A CE2 
2934 C CZ  . TYR A 182 ? 0.1919 0.2427 0.2863 -0.0215 -0.0404 0.0006  185 TYR A CZ  
2935 O OH  . TYR A 182 ? 0.2044 0.2592 0.3043 -0.0221 -0.0432 0.0011  185 TYR A OH  
2945 N N   . PRO A 183 ? 0.2423 0.2270 0.2854 -0.0110 -0.0207 0.0039  186 PRO A N   
2946 C CA  . PRO A 183 ? 0.2437 0.2176 0.2761 -0.0053 -0.0137 0.0083  186 PRO A CA  
2947 C C   . PRO A 183 ? 0.2517 0.2170 0.2889 -0.0144 -0.0117 0.0081  186 PRO A C   
2948 O O   . PRO A 183 ? 0.2594 0.2242 0.2936 -0.0109 -0.0057 0.0130  186 PRO A O   
2949 C CB  . PRO A 183 ? 0.2897 0.2387 0.2981 0.0038  -0.0116 0.0080  186 PRO A CB  
2950 C CG  . PRO A 183 ? 0.3075 0.2492 0.3135 -0.0024 -0.0191 0.0011  186 PRO A CG  
2951 C CD  . PRO A 183 ? 0.2586 0.2303 0.2865 -0.0063 -0.0237 0.0012  186 PRO A CD  
2959 N N   . VAL A 184 ? 0.2683 0.2290 0.3136 -0.0265 -0.0165 0.0034  187 VAL A N   
2960 C CA  . VAL A 184 ? 0.2924 0.2490 0.3455 -0.0371 -0.0141 0.0042  187 VAL A CA  
2961 C C   . VAL A 184 ? 0.2435 0.2246 0.3151 -0.0379 -0.0113 0.0068  187 VAL A C   
2962 O O   . VAL A 184 ? 0.2664 0.2455 0.3374 -0.0387 -0.0048 0.0107  187 VAL A O   
2963 C CB  . VAL A 184 ? 0.3116 0.2632 0.3709 -0.0504 -0.0211 -0.0006 187 VAL A CB  
2964 C CG1 . VAL A 184 ? 0.3156 0.2647 0.3839 -0.0624 -0.0173 0.0018  187 VAL A CG1 
2965 C CG2 . VAL A 184 ? 0.3347 0.2556 0.3693 -0.0506 -0.0238 -0.0043 187 VAL A CG2 
2975 N N   . VAL A 185 ? 0.2386 0.2393 0.3233 -0.0375 -0.0151 0.0049  188 VAL A N   
2976 C CA  . VAL A 185 ? 0.2229 0.2420 0.3205 -0.0376 -0.0116 0.0065  188 VAL A CA  
2977 C C   . VAL A 185 ? 0.2485 0.2695 0.3360 -0.0305 -0.0064 0.0105  188 VAL A C   
2978 O O   . VAL A 185 ? 0.2614 0.2871 0.3513 -0.0318 -0.0011 0.0128  188 VAL A O   
2979 C CB  . VAL A 185 ? 0.2229 0.2565 0.3315 -0.0373 -0.0162 0.0039  188 VAL A CB  
2980 C CG1 . VAL A 185 ? 0.2549 0.3008 0.3705 -0.0367 -0.0115 0.0048  188 VAL A CG1 
2981 C CG2 . VAL A 185 ? 0.2465 0.2825 0.3671 -0.0441 -0.0217 0.0014  188 VAL A CG2 
2991 N N   . TRP A 186 ? 0.2150 0.2346 0.2906 -0.0223 -0.0076 0.0121  189 TRP A N   
2992 C CA  . TRP A 186 ? 0.2372 0.2643 0.3049 -0.0154 -0.0040 0.0172  189 TRP A CA  
2993 C C   . TRP A 186 ? 0.2464 0.2599 0.3044 -0.0132 0.0021  0.0216  189 TRP A C   
2994 O O   . TRP A 186 ? 0.2558 0.2772 0.3121 -0.0120 0.0058  0.0254  189 TRP A O   
2995 C CB  . TRP A 186 ? 0.2188 0.2487 0.2778 -0.0065 -0.0062 0.0191  189 TRP A CB  
2996 C CG  . TRP A 186 ? 0.2059 0.2535 0.2607 0.0005  -0.0048 0.0252  189 TRP A CG  
2997 C CD1 . TRP A 186 ? 0.2163 0.2846 0.2770 -0.0012 -0.0084 0.0255  189 TRP A CD1 
2998 C CD2 . TRP A 186 ? 0.2117 0.2591 0.2553 0.0102  -0.0003 0.0326  189 TRP A CD2 
2999 N NE1 . TRP A 186 ? 0.2232 0.3071 0.2785 0.0056  -0.0071 0.0327  189 TRP A NE1 
3000 C CE2 . TRP A 186 ? 0.2285 0.3015 0.2739 0.0137  -0.0023 0.0374  189 TRP A CE2 
3001 C CE3 . TRP A 186 ? 0.2504 0.2790 0.2824 0.0156  0.0052  0.0363  189 TRP A CE3 
3002 C CZ2 . TRP A 186 ? 0.2643 0.3485 0.3017 0.0244  0.0005  0.0465  189 TRP A CZ2 
3003 C CZ3 . TRP A 186 ? 0.3013 0.3353 0.3226 0.0276  0.0091  0.0453  189 TRP A CZ3 
3004 C CH2 . TRP A 186 ? 0.2842 0.3488 0.3096 0.0321  0.0063  0.0506  189 TRP A CH2 
3015 N N   . LEU A 187 ? 0.2576 0.2487 0.3065 -0.0132 0.0031  0.0212  190 LEU A N   
3016 C CA  . LEU A 187 ? 0.2829 0.2558 0.3191 -0.0108 0.0096  0.0261  190 LEU A CA  
3017 C C   . LEU A 187 ? 0.3172 0.2925 0.3626 -0.0202 0.0134  0.0269  190 LEU A C   
3018 O O   . LEU A 187 ? 0.3279 0.3009 0.3653 -0.0162 0.0193  0.0328  190 LEU A O   
3019 C CB  . LEU A 187 ? 0.3101 0.2531 0.3318 -0.0111 0.0095  0.0241  190 LEU A CB  
3020 C CG  . LEU A 187 ? 0.3656 0.2817 0.3688 -0.0076 0.0168  0.0294  190 LEU A CG  
3021 C CD1 . LEU A 187 ? 0.4523 0.3707 0.4415 0.0100  0.0210  0.0366  190 LEU A CD1 
3022 C CD2 . LEU A 187 ? 0.4552 0.3382 0.4438 -0.0131 0.0148  0.0242  190 LEU A CD2 
3034 N N   . ILE A 188 ? 0.3006 0.2835 0.3629 -0.0311 0.0107  0.0222  191 ILE A N   
3035 C CA  . ILE A 188 ? 0.3159 0.3036 0.3887 -0.0395 0.0159  0.0238  191 ILE A CA  
3036 C C   . ILE A 188 ? 0.2958 0.3045 0.3765 -0.0374 0.0178  0.0238  191 ILE A C   
3037 O O   . ILE A 188 ? 0.3267 0.3398 0.4119 -0.0409 0.0241  0.0261  191 ILE A O   
3038 C CB  . ILE A 188 ? 0.2979 0.2847 0.3851 -0.0520 0.0126  0.0203  191 ILE A CB  
3039 C CG1 . ILE A 188 ? 0.3595 0.3649 0.4620 -0.0525 0.0062  0.0155  191 ILE A CG1 
3040 C CG2 . ILE A 188 ? 0.4946 0.4541 0.5672 -0.0558 0.0107  0.0198  191 ILE A CG2 
3041 C CD1 . ILE A 188 ? 0.5434 0.5518 0.6610 -0.0644 0.0011  0.0130  191 ILE A CD1 
3053 N N   . GLY A 189 ? 0.2789 0.3002 0.3603 -0.0324 0.0133  0.0212  192 GLY A N   
3054 C CA  . GLY A 189 ? 0.2800 0.3165 0.3656 -0.0322 0.0143  0.0196  192 GLY A CA  
3055 C C   . GLY A 189 ? 0.2835 0.3246 0.3550 -0.0268 0.0164  0.0234  192 GLY A C   
3056 O O   . GLY A 189 ? 0.2878 0.3214 0.3479 -0.0222 0.0193  0.0291  192 GLY A O   
3060 N N   A SER A 190 ? 0.2882 0.3405 0.3593 -0.0276 0.0148  0.0207  193 SER A N   
3061 N N   B SER A 190 ? 0.2896 0.3421 0.3605 -0.0276 0.0147  0.0207  193 SER A N   
3062 C CA  A SER A 190 ? 0.3107 0.3704 0.3686 -0.0255 0.0156  0.0235  193 SER A CA  
3063 C CA  B SER A 190 ? 0.3111 0.3708 0.3688 -0.0254 0.0157  0.0237  193 SER A CA  
3064 C C   A SER A 190 ? 0.3206 0.3864 0.3696 -0.0189 0.0116  0.0290  193 SER A C   
3065 C C   B SER A 190 ? 0.3189 0.3865 0.3682 -0.0194 0.0109  0.0285  193 SER A C   
3066 O O   A SER A 190 ? 0.3626 0.4331 0.4003 -0.0151 0.0132  0.0345  193 SER A O   
3067 O O   B SER A 190 ? 0.2899 0.3663 0.3282 -0.0172 0.0108  0.0327  193 SER A O   
3068 C CB  A SER A 190 ? 0.3438 0.4110 0.4008 -0.0301 0.0133  0.0180  193 SER A CB  
3069 C CB  B SER A 190 ? 0.3519 0.4181 0.4085 -0.0301 0.0144  0.0182  193 SER A CB  
3070 O OG  A SER A 190 ? 0.3649 0.4372 0.4267 -0.0313 0.0067  0.0152  193 SER A OG  
3071 O OG  B SER A 190 ? 0.3841 0.4450 0.4419 -0.0323 0.0216  0.0162  193 SER A OG  
3082 N N   . GLU A 191 ? 0.2726 0.3395 0.3262 -0.0163 0.0070  0.0283  194 GLU A N   
3083 C CA  . GLU A 191 ? 0.2676 0.3433 0.3141 -0.0080 0.0044  0.0345  194 GLU A CA  
3084 C C   . GLU A 191 ? 0.2851 0.3469 0.3226 0.0008  0.0091  0.0407  194 GLU A C   
3085 O O   . GLU A 191 ? 0.2867 0.3559 0.3157 0.0107  0.0091  0.0480  194 GLU A O   
3086 C CB  . GLU A 191 ? 0.2790 0.3577 0.3320 -0.0069 -0.0004 0.0319  194 GLU A CB  
3087 C CG  . GLU A 191 ? 0.3293 0.4218 0.3884 -0.0145 -0.0053 0.0277  194 GLU A CG  
3088 C CD  . GLU A 191 ? 0.3429 0.4253 0.4106 -0.0218 -0.0052 0.0202  194 GLU A CD  
3089 O OE1 . GLU A 191 ? 0.3219 0.3911 0.3939 -0.0221 -0.0021 0.0184  194 GLU A OE1 
3090 O OE2 . GLU A 191 ? 0.4756 0.5639 0.5458 -0.0275 -0.0084 0.0167  194 GLU A OE2 
3097 N N   . GLY A 192 ? 0.2695 0.3112 0.3083 -0.0026 0.0133  0.0386  195 GLY A N   
3098 C CA  . GLY A 192 ? 0.3159 0.3359 0.3437 0.0036  0.0182  0.0434  195 GLY A CA  
3099 C C   . GLY A 192 ? 0.3317 0.3410 0.3541 0.0009  0.0249  0.0470  195 GLY A C   
3100 O O   . GLY A 192 ? 0.3797 0.3994 0.3955 0.0039  0.0270  0.0519  195 GLY A O   
3104 N N   . ALA A 193 ? 0.3093 0.2980 0.3339 -0.0063 0.0283  0.0449  196 ALA A N   
3105 C CA  . ALA A 193 ? 0.3462 0.3226 0.3655 -0.0100 0.0359  0.0494  196 ALA A CA  
3106 C C   . ALA A 193 ? 0.3847 0.3763 0.4147 -0.0177 0.0386  0.0475  196 ALA A C   
3107 O O   . ALA A 193 ? 0.4173 0.4027 0.4412 -0.0193 0.0461  0.0527  196 ALA A O   
3108 C CB  . ALA A 193 ? 0.3992 0.3497 0.4178 -0.0178 0.0381  0.0480  196 ALA A CB  
3114 N N   . GLY A 194 ? 0.3267 0.3352 0.3710 -0.0223 0.0341  0.0405  197 GLY A N   
3115 C CA  . GLY A 194 ? 0.3359 0.3564 0.3855 -0.0265 0.0379  0.0389  197 GLY A CA  
3116 C C   . GLY A 194 ? 0.3886 0.4058 0.4510 -0.0350 0.0440  0.0384  197 GLY A C   
3117 O O   . GLY A 194 ? 0.4201 0.4429 0.4820 -0.0362 0.0508  0.0397  197 GLY A O   
3121 N N   . ILE A 195 ? 0.3212 0.3309 0.3940 -0.0411 0.0417  0.0368  198 ILE A N   
3122 C CA  . ILE A 195 ? 0.3222 0.3331 0.4102 -0.0512 0.0467  0.0378  198 ILE A CA  
3123 C C   . ILE A 195 ? 0.4133 0.4440 0.5206 -0.0532 0.0451  0.0328  198 ILE A C   
3124 O O   . ILE A 195 ? 0.4309 0.4714 0.5489 -0.0566 0.0525  0.0350  198 ILE A O   
3125 C CB  . ILE A 195 ? 0.3989 0.3932 0.4879 -0.0589 0.0433  0.0381  198 ILE A CB  
3126 C CG1 . ILE A 195 ? 0.5256 0.4945 0.5913 -0.0544 0.0459  0.0432  198 ILE A CG1 
3127 C CG2 . ILE A 195 ? 0.4948 0.4950 0.6015 -0.0720 0.0471  0.0400  198 ILE A CG2 
3128 C CD1 . ILE A 195 ? 0.6816 0.6465 0.7362 -0.0516 0.0557  0.0508  198 ILE A CD1 
3140 N N   . VAL A 196 ? 0.3235 0.3596 0.4347 -0.0502 0.0367  0.0272  199 VAL A N   
3141 C CA  . VAL A 196 ? 0.3181 0.3697 0.4451 -0.0500 0.0350  0.0229  199 VAL A CA  
3142 C C   . VAL A 196 ? 0.3132 0.3683 0.4292 -0.0431 0.0365  0.0203  199 VAL A C   
3143 O O   . VAL A 196 ? 0.3116 0.3620 0.4133 -0.0394 0.0319  0.0194  199 VAL A O   
3144 C CB  . VAL A 196 ? 0.3574 0.4091 0.4910 -0.0513 0.0245  0.0188  199 VAL A CB  
3145 C CG1 . VAL A 196 ? 0.4170 0.4823 0.5635 -0.0486 0.0216  0.0149  199 VAL A CG1 
3146 C CG2 . VAL A 196 ? 0.4028 0.4493 0.5448 -0.0609 0.0223  0.0207  199 VAL A CG2 
3156 N N   . PRO A 197 ? 0.2768 0.3397 0.3977 -0.0412 0.0431  0.0192  200 PRO A N   
3157 C CA  . PRO A 197 ? 0.2754 0.3365 0.3811 -0.0365 0.0444  0.0155  200 PRO A CA  
3158 C C   . PRO A 197 ? 0.2859 0.3467 0.3905 -0.0351 0.0357  0.0102  200 PRO A C   
3159 O O   . PRO A 197 ? 0.2847 0.3491 0.4030 -0.0358 0.0309  0.0090  200 PRO A O   
3160 C CB  . PRO A 197 ? 0.3691 0.4351 0.4802 -0.0340 0.0548  0.0155  200 PRO A CB  
3161 C CG  . PRO A 197 ? 0.4557 0.5319 0.5893 -0.0369 0.0570  0.0191  200 PRO A CG  
3162 C CD  . PRO A 197 ? 0.3376 0.4107 0.4758 -0.0435 0.0506  0.0220  200 PRO A CD  
3170 N N   . LEU A 198 ? 0.3019 0.3588 0.3891 -0.0341 0.0342  0.0074  201 LEU A N   
3171 C CA  . LEU A 198 ? 0.2609 0.3168 0.3450 -0.0347 0.0265  0.0031  201 LEU A CA  
3172 C C   . LEU A 198 ? 0.2897 0.3444 0.3843 -0.0327 0.0276  -0.0002 201 LEU A C   
3173 O O   . LEU A 198 ? 0.2731 0.3284 0.3731 -0.0330 0.0208  -0.0016 201 LEU A O   
3174 C CB  . LEU A 198 ? 0.2880 0.3405 0.3503 -0.0369 0.0252  0.0008  201 LEU A CB  
3175 C CG  . LEU A 198 ? 0.2930 0.3447 0.3496 -0.0404 0.0177  -0.0028 201 LEU A CG  
3176 C CD1 . LEU A 198 ? 0.2890 0.3490 0.3543 -0.0403 0.0097  0.0003  201 LEU A CD1 
3177 C CD2 . LEU A 198 ? 0.3801 0.4311 0.4154 -0.0454 0.0159  -0.0042 201 LEU A CD2 
3189 N N   A ASN A 199 ? 0.2858 0.3394 0.3837 -0.0292 0.0366  -0.0007 202 ASN A N   
3190 N N   B ASN A 199 ? 0.2893 0.3429 0.3865 -0.0293 0.0368  -0.0006 202 ASN A N   
3191 C CA  A ASN A 199 ? 0.2832 0.3363 0.3907 -0.0244 0.0383  -0.0026 202 ASN A CA  
3192 C CA  B ASN A 199 ? 0.2847 0.3380 0.3920 -0.0243 0.0393  -0.0024 202 ASN A CA  
3193 C C   A ASN A 199 ? 0.3088 0.3741 0.4395 -0.0244 0.0331  0.0006  202 ASN A C   
3194 C C   B ASN A 199 ? 0.3076 0.3725 0.4373 -0.0247 0.0330  0.0006  202 ASN A C   
3195 O O   A ASN A 199 ? 0.2893 0.3541 0.4251 -0.0220 0.0282  -0.0007 202 ASN A O   
3196 O O   B ASN A 199 ? 0.2774 0.3409 0.4108 -0.0224 0.0282  -0.0011 202 ASN A O   
3197 C CB  A ASN A 199 ? 0.3413 0.3905 0.4450 -0.0180 0.0506  -0.0032 202 ASN A CB  
3198 C CB  B ASN A 199 ? 0.3246 0.3780 0.4327 -0.0182 0.0520  -0.0015 202 ASN A CB  
3199 C CG  A ASN A 199 ? 0.3606 0.4237 0.4806 -0.0166 0.0580  0.0024  202 ASN A CG  
3200 C CG  B ASN A 199 ? 0.3188 0.3671 0.4292 -0.0100 0.0563  -0.0035 202 ASN A CG  
3201 O OD1 A ASN A 199 ? 0.3881 0.4548 0.5077 -0.0217 0.0577  0.0055  202 ASN A OD1 
3202 O OD1 B ASN A 199 ? 0.3823 0.4257 0.4930 -0.0097 0.0494  -0.0056 202 ASN A OD1 
3203 N ND2 A ASN A 199 ? 0.4616 0.5333 0.5963 -0.0092 0.0655  0.0048  202 ASN A ND2 
3204 N ND2 B ASN A 199 ? 0.5117 0.5602 0.6222 -0.0021 0.0687  -0.0023 202 ASN A ND2 
3217 N N   . ILE A 200 ? 0.2882 0.3628 0.4308 -0.0280 0.0334  0.0049  203 ILE A N   
3218 C CA  . ILE A 200 ? 0.2692 0.3539 0.4307 -0.0307 0.0268  0.0071  203 ILE A CA  
3219 C C   . ILE A 200 ? 0.2462 0.3244 0.4004 -0.0338 0.0163  0.0052  203 ILE A C   
3220 O O   . ILE A 200 ? 0.2491 0.3309 0.4116 -0.0336 0.0093  0.0046  203 ILE A O   
3221 C CB  . ILE A 200 ? 0.2583 0.3517 0.4317 -0.0360 0.0309  0.0120  203 ILE A CB  
3222 C CG1 . ILE A 200 ? 0.3121 0.4152 0.4936 -0.0313 0.0428  0.0148  203 ILE A CG1 
3223 C CG2 . ILE A 200 ? 0.3202 0.4232 0.5110 -0.0418 0.0228  0.0138  203 ILE A CG2 
3224 C CD1 . ILE A 200 ? 0.3476 0.4604 0.5415 -0.0237 0.0443  0.0150  203 ILE A CD1 
3236 N N   . GLU A 201 ? 0.2222 0.2922 0.3607 -0.0354 0.0153  0.0048  204 GLU A N   
3237 C CA  . GLU A 201 ? 0.2205 0.2861 0.3516 -0.0361 0.0070  0.0039  204 GLU A CA  
3238 C C   . GLU A 201 ? 0.2459 0.3111 0.3753 -0.0339 0.0027  0.0009  204 GLU A C   
3239 O O   . GLU A 201 ? 0.2180 0.2836 0.3501 -0.0338 -0.0043 0.0005  204 GLU A O   
3240 C CB  . GLU A 201 ? 0.2755 0.3367 0.3906 -0.0359 0.0082  0.0054  204 GLU A CB  
3241 C CG  . GLU A 201 ? 0.2707 0.3308 0.3778 -0.0344 0.0011  0.0056  204 GLU A CG  
3242 C CD  . GLU A 201 ? 0.3551 0.4164 0.4484 -0.0326 0.0020  0.0085  204 GLU A CD  
3243 O OE1 . GLU A 201 ? 0.3130 0.3736 0.4012 -0.0328 0.0072  0.0102  204 GLU A OE1 
3244 O OE2 . GLU A 201 ? 0.4516 0.5173 0.5388 -0.0307 -0.0025 0.0096  204 GLU A OE2 
3251 N N   . THR A 202 ? 0.2267 0.2885 0.3492 -0.0323 0.0070  -0.0013 205 THR A N   
3252 C CA  . THR A 202 ? 0.2326 0.2892 0.3500 -0.0313 0.0037  -0.0038 205 THR A CA  
3253 C C   . THR A 202 ? 0.2316 0.2917 0.3634 -0.0274 0.0017  -0.0031 205 THR A C   
3254 O O   . THR A 202 ? 0.2113 0.2695 0.3423 -0.0269 -0.0042 -0.0033 205 THR A O   
3255 C CB  . THR A 202 ? 0.2244 0.2711 0.3275 -0.0313 0.0095  -0.0069 205 THR A CB  
3256 O OG1 . THR A 202 ? 0.2452 0.2922 0.3344 -0.0360 0.0091  -0.0069 205 THR A OG1 
3257 C CG2 . THR A 202 ? 0.2169 0.2533 0.3107 -0.0324 0.0066  -0.0094 205 THR A CG2 
3265 N N   . LEU A 203 ? 0.2028 0.2698 0.3478 -0.0242 0.0069  -0.0013 206 LEU A N   
3266 C CA  . LEU A 203 ? 0.2262 0.3030 0.3883 -0.0205 0.0038  0.0011  206 LEU A CA  
3267 C C   . LEU A 203 ? 0.2198 0.3021 0.3878 -0.0249 -0.0062 0.0020  206 LEU A C   
3268 O O   . LEU A 203 ? 0.1978 0.2812 0.3683 -0.0226 -0.0124 0.0024  206 LEU A O   
3269 C CB  . LEU A 203 ? 0.2179 0.3079 0.3963 -0.0178 0.0113  0.0045  206 LEU A CB  
3270 C CG  . LEU A 203 ? 0.2141 0.3223 0.4144 -0.0157 0.0073  0.0087  206 LEU A CG  
3271 C CD1 . LEU A 203 ? 0.2636 0.3689 0.4633 -0.0069 0.0059  0.0092  206 LEU A CD1 
3272 C CD2 . LEU A 203 ? 0.2609 0.3846 0.4766 -0.0141 0.0170  0.0130  206 LEU A CD2 
3284 N N   . LEU A 204 ? 0.2022 0.2846 0.3689 -0.0307 -0.0075 0.0022  207 LEU A N   
3285 C CA  . LEU A 204 ? 0.2280 0.3103 0.3955 -0.0350 -0.0162 0.0021  207 LEU A CA  
3286 C C   . LEU A 204 ? 0.1898 0.2638 0.3438 -0.0328 -0.0215 0.0003  207 LEU A C   
3287 O O   . LEU A 204 ? 0.1996 0.2751 0.3555 -0.0325 -0.0285 0.0002  207 LEU A O   
3288 C CB  . LEU A 204 ? 0.2110 0.2883 0.3743 -0.0407 -0.0145 0.0028  207 LEU A CB  
3289 C CG  . LEU A 204 ? 0.2255 0.3126 0.4040 -0.0452 -0.0098 0.0057  207 LEU A CG  
3290 C CD1 . LEU A 204 ? 0.2863 0.3628 0.4560 -0.0509 -0.0076 0.0067  207 LEU A CD1 
3291 C CD2 . LEU A 204 ? 0.3045 0.4041 0.4993 -0.0496 -0.0163 0.0070  207 LEU A CD2 
3303 N N   . PHE A 205 ? 0.1899 0.2578 0.3310 -0.0319 -0.0185 -0.0005 208 PHE A N   
3304 C CA  . PHE A 205 ? 0.2095 0.2736 0.3402 -0.0306 -0.0230 -0.0008 208 PHE A CA  
3305 C C   . PHE A 205 ? 0.2104 0.2741 0.3434 -0.0280 -0.0248 -0.0009 208 PHE A C   
3306 O O   . PHE A 205 ? 0.1966 0.2587 0.3249 -0.0270 -0.0298 -0.0003 208 PHE A O   
3307 C CB  . PHE A 205 ? 0.1922 0.2548 0.3104 -0.0315 -0.0200 -0.0005 208 PHE A CB  
3308 C CG  . PHE A 205 ? 0.1819 0.2444 0.2939 -0.0311 -0.0195 0.0013  208 PHE A CG  
3309 C CD1 . PHE A 205 ? 0.2251 0.2840 0.3337 -0.0290 -0.0232 0.0020  208 PHE A CD1 
3310 C CD2 . PHE A 205 ? 0.2215 0.2858 0.3272 -0.0318 -0.0151 0.0027  208 PHE A CD2 
3311 C CE1 . PHE A 205 ? 0.2600 0.3151 0.3596 -0.0263 -0.0211 0.0043  208 PHE A CE1 
3312 C CE2 . PHE A 205 ? 0.2517 0.3159 0.3497 -0.0291 -0.0141 0.0058  208 PHE A CE2 
3313 C CZ  . PHE A 205 ? 0.2683 0.3265 0.3638 -0.0259 -0.0165 0.0067  208 PHE A CZ  
3323 N N   . MET A 206 ? 0.2009 0.2637 0.3386 -0.0256 -0.0200 -0.0011 209 MET A N   
3324 C CA  . MET A 206 ? 0.2026 0.2612 0.3402 -0.0213 -0.0209 -0.0004 209 MET A CA  
3325 C C   . MET A 206 ? 0.2100 0.2770 0.3588 -0.0184 -0.0275 0.0019  209 MET A C   
3326 O O   . MET A 206 ? 0.2220 0.2855 0.3660 -0.0161 -0.0320 0.0032  209 MET A O   
3327 C CB  . MET A 206 ? 0.2540 0.3066 0.3914 -0.0171 -0.0127 -0.0009 209 MET A CB  
3328 C CG  . MET A 206 ? 0.2621 0.3058 0.3958 -0.0116 -0.0132 0.0005  209 MET A CG  
3329 S SD  . MET A 206 ? 0.4087 0.4628 0.5594 -0.0014 -0.0133 0.0049  209 MET A SD  
3330 C CE  . MET A 206 ? 0.2168 0.2619 0.3615 0.0008  -0.0014 0.0023  209 MET A CE  
3340 N N   . VAL A 207 ? 0.1816 0.2605 0.3448 -0.0193 -0.0285 0.0030  210 VAL A N   
3341 C CA  . VAL A 207 ? 0.1833 0.2727 0.3569 -0.0188 -0.0365 0.0051  210 VAL A CA  
3342 C C   . VAL A 207 ? 0.1937 0.2772 0.3558 -0.0226 -0.0441 0.0034  210 VAL A C   
3343 O O   . VAL A 207 ? 0.2070 0.2916 0.3671 -0.0201 -0.0508 0.0047  210 VAL A O   
3344 C CB  . VAL A 207 ? 0.2137 0.3181 0.4045 -0.0227 -0.0363 0.0066  210 VAL A CB  
3345 C CG1 . VAL A 207 ? 0.2788 0.3959 0.4792 -0.0253 -0.0464 0.0086  210 VAL A CG1 
3346 C CG2 . VAL A 207 ? 0.2259 0.3386 0.4285 -0.0154 -0.0278 0.0097  210 VAL A CG2 
3356 N N   . LEU A 208 ? 0.1900 0.2664 0.3428 -0.0270 -0.0427 0.0010  211 LEU A N   
3357 C CA  . LEU A 208 ? 0.1889 0.2579 0.3284 -0.0281 -0.0481 -0.0004 211 LEU A CA  
3358 C C   . LEU A 208 ? 0.1876 0.2521 0.3165 -0.0239 -0.0485 0.0008  211 LEU A C   
3359 O O   . LEU A 208 ? 0.1985 0.2612 0.3211 -0.0222 -0.0542 0.0012  211 LEU A O   
3360 C CB  . LEU A 208 ? 0.1922 0.2533 0.3219 -0.0307 -0.0447 -0.0019 211 LEU A CB  
3361 C CG  . LEU A 208 ? 0.1887 0.2499 0.3253 -0.0367 -0.0450 -0.0028 211 LEU A CG  
3362 C CD1 . LEU A 208 ? 0.2648 0.3157 0.3899 -0.0367 -0.0394 -0.0029 211 LEU A CD1 
3363 C CD2 . LEU A 208 ? 0.2817 0.3393 0.4151 -0.0412 -0.0539 -0.0046 211 LEU A CD2 
3375 N N   . ASP A 209 ? 0.1778 0.2400 0.3036 -0.0231 -0.0427 0.0014  212 ASP A N   
3376 C CA  . ASP A 209 ? 0.1782 0.2361 0.2934 -0.0220 -0.0424 0.0031  212 ASP A CA  
3377 C C   . ASP A 209 ? 0.1935 0.2495 0.3102 -0.0182 -0.0455 0.0053  212 ASP A C   
3378 O O   . ASP A 209 ? 0.2025 0.2562 0.3108 -0.0167 -0.0488 0.0073  212 ASP A O   
3379 C CB  . ASP A 209 ? 0.1839 0.2391 0.2954 -0.0249 -0.0362 0.0029  212 ASP A CB  
3380 C CG  . ASP A 209 ? 0.1939 0.2529 0.3002 -0.0279 -0.0337 0.0027  212 ASP A CG  
3381 O OD1 . ASP A 209 ? 0.2271 0.2888 0.3300 -0.0262 -0.0356 0.0034  212 ASP A OD1 
3382 O OD2 . ASP A 209 ? 0.1910 0.2495 0.2936 -0.0316 -0.0299 0.0023  212 ASP A OD2 
3387 N N   . VAL A 210 ? 0.2024 0.2605 0.3297 -0.0152 -0.0443 0.0060  213 VAL A N   
3388 C CA  . VAL A 210 ? 0.2202 0.2763 0.3479 -0.0093 -0.0469 0.0096  213 VAL A CA  
3389 C C   . VAL A 210 ? 0.2207 0.2848 0.3507 -0.0081 -0.0559 0.0107  213 VAL A C   
3390 O O   . VAL A 210 ? 0.2262 0.2870 0.3485 -0.0046 -0.0598 0.0137  213 VAL A O   
3391 C CB  . VAL A 210 ? 0.2064 0.2638 0.3448 -0.0038 -0.0419 0.0109  213 VAL A CB  
3392 C CG1 . VAL A 210 ? 0.2713 0.3294 0.4124 0.0052  -0.0448 0.0161  213 VAL A CG1 
3393 C CG2 . VAL A 210 ? 0.2540 0.2977 0.3836 -0.0051 -0.0333 0.0090  213 VAL A CG2 
3403 N N   . SER A 211 ? 0.1925 0.2657 0.3307 -0.0120 -0.0596 0.0083  214 SER A N   
3404 C CA  . SER A 211 ? 0.2031 0.2817 0.3400 -0.0133 -0.0695 0.0083  214 SER A CA  
3405 C C   . SER A 211 ? 0.1992 0.2669 0.3165 -0.0138 -0.0715 0.0068  214 SER A C   
3406 O O   . SER A 211 ? 0.2325 0.2997 0.3420 -0.0115 -0.0780 0.0083  214 SER A O   
3407 C CB  . SER A 211 ? 0.2314 0.3173 0.3777 -0.0204 -0.0722 0.0055  214 SER A CB  
3408 O OG  . SER A 211 ? 0.2439 0.3446 0.4103 -0.0188 -0.0699 0.0085  214 SER A OG  
3414 N N   . ALA A 212 ? 0.2079 0.2683 0.3167 -0.0159 -0.0657 0.0046  215 ALA A N   
3415 C CA  . ALA A 212 ? 0.2116 0.2644 0.3029 -0.0148 -0.0662 0.0039  215 ALA A CA  
3416 C C   . ALA A 212 ? 0.2410 0.2919 0.3243 -0.0113 -0.0638 0.0078  215 ALA A C   
3417 O O   . ALA A 212 ? 0.2671 0.3143 0.3365 -0.0089 -0.0642 0.0087  215 ALA A O   
3418 C CB  . ALA A 212 ? 0.2322 0.2816 0.3194 -0.0164 -0.0600 0.0019  215 ALA A CB  
3424 N N   . LYS A 213 ? 0.2127 0.2643 0.3030 -0.0109 -0.0605 0.0107  216 LYS A N   
3425 C CA  . LYS A 213 ? 0.2263 0.2731 0.3075 -0.0098 -0.0575 0.0151  216 LYS A CA  
3426 C C   . LYS A 213 ? 0.2607 0.3042 0.3427 -0.0051 -0.0609 0.0189  216 LYS A C   
3427 O O   . LYS A 213 ? 0.2631 0.3042 0.3346 -0.0020 -0.0642 0.0221  216 LYS A O   
3428 C CB  . LYS A 213 ? 0.2055 0.2502 0.2881 -0.0147 -0.0502 0.0155  216 LYS A CB  
3429 C CG  . LYS A 213 ? 0.1948 0.2460 0.2761 -0.0184 -0.0469 0.0137  216 LYS A CG  
3430 C CD  . LYS A 213 ? 0.2071 0.2591 0.2882 -0.0244 -0.0418 0.0145  216 LYS A CD  
3431 C CE  . LYS A 213 ? 0.2146 0.2777 0.2930 -0.0263 -0.0395 0.0156  216 LYS A CE  
3432 N NZ  . LYS A 213 ? 0.1949 0.2607 0.2780 -0.0243 -0.0392 0.0122  216 LYS A NZ  
3443 N N   . VAL A 214 ? 0.2255 0.2690 0.3185 -0.0029 -0.0597 0.0193  217 VAL A N   
3444 C CA  . VAL A 214 ? 0.2759 0.3162 0.3689 0.0043  -0.0620 0.0244  217 VAL A CA  
3445 C C   . VAL A 214 ? 0.2576 0.3101 0.3558 0.0079  -0.0718 0.0252  217 VAL A C   
3446 O O   . VAL A 214 ? 0.2615 0.3132 0.3524 0.0130  -0.0767 0.0298  217 VAL A O   
3447 C CB  . VAL A 214 ? 0.2384 0.2731 0.3395 0.0076  -0.0555 0.0252  217 VAL A CB  
3448 C CG1 . VAL A 214 ? 0.2773 0.3085 0.3784 0.0182  -0.0571 0.0318  217 VAL A CG1 
3449 C CG2 . VAL A 214 ? 0.3160 0.3362 0.4079 0.0016  -0.0473 0.0235  217 VAL A CG2 
3459 N N   . GLY A 215 ? 0.2382 0.3023 0.3480 0.0042  -0.0754 0.0210  218 GLY A N   
3460 C CA  . GLY A 215 ? 0.2555 0.3320 0.3691 0.0040  -0.0864 0.0211  218 GLY A CA  
3461 C C   . GLY A 215 ? 0.2617 0.3311 0.3554 0.0025  -0.0919 0.0197  218 GLY A C   
3462 O O   . GLY A 215 ? 0.2692 0.3416 0.3564 0.0064  -0.0995 0.0231  218 GLY A O   
3466 N N   . PHE A 216 ? 0.2584 0.3183 0.3409 -0.0014 -0.0872 0.0156  219 PHE A N   
3467 C CA  . PHE A 216 ? 0.2626 0.3144 0.3244 -0.0006 -0.0896 0.0147  219 PHE A CA  
3468 C C   . PHE A 216 ? 0.2720 0.3197 0.3234 0.0053  -0.0887 0.0210  219 PHE A C   
3469 O O   . PHE A 216 ? 0.2780 0.3241 0.3159 0.0082  -0.0953 0.0225  219 PHE A O   
3470 C CB  . PHE A 216 ? 0.2594 0.3046 0.3148 -0.0030 -0.0815 0.0115  219 PHE A CB  
3471 C CG  . PHE A 216 ? 0.2766 0.3134 0.3103 0.0000  -0.0801 0.0111  219 PHE A CG  
3472 C CD1 . PHE A 216 ? 0.3080 0.3436 0.3328 0.0038  -0.0754 0.0166  219 PHE A CD1 
3473 C CD2 . PHE A 216 ? 0.3135 0.3421 0.3346 -0.0011 -0.0820 0.0054  219 PHE A CD2 
3474 C CE1 . PHE A 216 ? 0.3216 0.3521 0.3268 0.0079  -0.0722 0.0173  219 PHE A CE1 
3475 C CE2 . PHE A 216 ? 0.3510 0.3707 0.3505 0.0044  -0.0778 0.0056  219 PHE A CE2 
3476 C CZ  . PHE A 216 ? 0.3186 0.3415 0.3118 0.0091  -0.0731 0.0117  219 PHE A CZ  
3486 N N   . GLY A 217 ? 0.2493 0.2936 0.3046 0.0067  -0.0810 0.0252  220 GLY A N   
3487 C CA  . GLY A 217 ? 0.2793 0.3165 0.3230 0.0111  -0.0792 0.0321  220 GLY A CA  
3488 C C   . GLY A 217 ? 0.3029 0.3426 0.3475 0.0181  -0.0865 0.0373  220 GLY A C   
3489 O O   . GLY A 217 ? 0.3504 0.3853 0.3800 0.0225  -0.0888 0.0424  220 GLY A O   
3493 N N   . LEU A 218 ? 0.2561 0.3051 0.3183 0.0202  -0.0897 0.0372  221 LEU A N   
3494 C CA  . LEU A 218 ? 0.2856 0.3423 0.3507 0.0282  -0.0973 0.0433  221 LEU A CA  
3495 C C   . LEU A 218 ? 0.3194 0.3840 0.3744 0.0270  -0.1091 0.0419  221 LEU A C   
3496 O O   . LEU A 218 ? 0.3643 0.4294 0.4090 0.0336  -0.1148 0.0482  221 LEU A O   
3497 C CB  . LEU A 218 ? 0.2954 0.3663 0.3839 0.0305  -0.0981 0.0435  221 LEU A CB  
3498 C CG  . LEU A 218 ? 0.3315 0.3908 0.4250 0.0358  -0.0868 0.0468  221 LEU A CG  
3499 C CD1 . LEU A 218 ? 0.3908 0.4653 0.5072 0.0375  -0.0855 0.0456  221 LEU A CD1 
3500 C CD2 . LEU A 218 ? 0.3531 0.4009 0.4362 0.0470  -0.0850 0.0563  221 LEU A CD2 
3512 N N   . ILE A 219 ? 0.2766 0.3447 0.3312 0.0187  -0.1130 0.0340  222 ILE A N   
3513 C CA  . ILE A 219 ? 0.3328 0.4029 0.3724 0.0159  -0.1243 0.0310  222 ILE A CA  
3514 C C   . ILE A 219 ? 0.3485 0.4037 0.3613 0.0196  -0.1217 0.0327  222 ILE A C   
3515 O O   . ILE A 219 ? 0.3662 0.4222 0.3641 0.0234  -0.1299 0.0361  222 ILE A O   
3516 C CB  . ILE A 219 ? 0.3307 0.4009 0.3724 0.0056  -0.1269 0.0216  222 ILE A CB  
3517 C CG1 . ILE A 219 ? 0.3451 0.4337 0.4142 0.0013  -0.1302 0.0215  222 ILE A CG1 
3518 C CG2 . ILE A 219 ? 0.4225 0.4883 0.4426 0.0013  -0.1382 0.0171  222 ILE A CG2 
3519 C CD1 . ILE A 219 ? 0.3770 0.4617 0.4503 -0.0095 -0.1282 0.0131  222 ILE A CD1 
3531 N N   . LEU A 220 ? 0.3282 0.3720 0.3341 0.0188  -0.1104 0.0315  223 LEU A N   
3532 C CA  . LEU A 220 ? 0.3285 0.3612 0.3100 0.0222  -0.1064 0.0336  223 LEU A CA  
3533 C C   . LEU A 220 ? 0.3695 0.3995 0.3446 0.0290  -0.1051 0.0435  223 LEU A C   
3534 O O   . LEU A 220 ? 0.3787 0.4043 0.3328 0.0334  -0.1089 0.0468  223 LEU A O   
3535 C CB  . LEU A 220 ? 0.3103 0.3378 0.2919 0.0196  -0.0938 0.0319  223 LEU A CB  
3536 C CG  . LEU A 220 ? 0.3226 0.3432 0.2832 0.0234  -0.0868 0.0358  223 LEU A CG  
3537 C CD1 . LEU A 220 ? 0.4356 0.4491 0.3718 0.0263  -0.0917 0.0312  223 LEU A CD1 
3538 C CD2 . LEU A 220 ? 0.3399 0.3624 0.3055 0.0208  -0.0748 0.0366  223 LEU A CD2 
3550 N N   . LEU A 221 ? 0.3692 0.3990 0.3589 0.0305  -0.0995 0.0488  224 LEU A N   
3551 C CA  . LEU A 221 ? 0.3533 0.3740 0.3330 0.0364  -0.0954 0.0587  224 LEU A CA  
3552 C C   . LEU A 221 ? 0.4302 0.4559 0.4085 0.0448  -0.1052 0.0649  224 LEU A C   
3553 O O   . LEU A 221 ? 0.4755 0.4918 0.4421 0.0513  -0.1026 0.0742  224 LEU A O   
3554 C CB  . LEU A 221 ? 0.3513 0.3637 0.3417 0.0338  -0.0847 0.0614  224 LEU A CB  
3555 C CG  . LEU A 221 ? 0.3809 0.3913 0.3717 0.0251  -0.0754 0.0575  224 LEU A CG  
3556 C CD1 . LEU A 221 ? 0.3891 0.3901 0.3890 0.0210  -0.0671 0.0596  224 LEU A CD1 
3557 C CD2 . LEU A 221 ? 0.3945 0.4009 0.3658 0.0247  -0.0707 0.0622  224 LEU A CD2 
3569 N N   A ARG A 222 ? 0.4334 0.6317 0.4023 -0.0462 -0.0927 0.1068  225 ARG A N   
3570 N N   B ARG A 222 ? 0.4332 0.6312 0.4019 -0.0464 -0.0925 0.1070  225 ARG A N   
3571 C CA  A ARG A 222 ? 0.4594 0.6770 0.4477 -0.0142 -0.1250 0.0851  225 ARG A CA  
3572 C CA  B ARG A 222 ? 0.4582 0.6777 0.4489 -0.0154 -0.1245 0.0852  225 ARG A CA  
3573 C C   A ARG A 222 ? 0.4872 0.6788 0.4585 -0.0027 -0.1631 0.0712  225 ARG A C   
3574 C C   B ARG A 222 ? 0.4840 0.6822 0.4643 -0.0060 -0.1632 0.0703  225 ARG A C   
3575 O O   A ARG A 222 ? 0.5246 0.7320 0.4915 0.0378  -0.1984 0.0480  225 ARG A O   
3576 O O   B ARG A 222 ? 0.5164 0.7407 0.5060 0.0303  -0.1996 0.0443  225 ARG A O   
3577 C CB  A ARG A 222 ? 0.4408 0.7424 0.5273 -0.0274 -0.1273 0.0686  225 ARG A CB  
3578 C CB  B ARG A 222 ? 0.4380 0.7403 0.5242 -0.0296 -0.1226 0.0710  225 ARG A CB  
3579 C CG  A ARG A 222 ? 0.4224 0.7541 0.5826 -0.0723 -0.1158 0.0683  225 ARG A CG  
3580 C CG  B ARG A 222 ? 0.4233 0.7510 0.5159 -0.0320 -0.0856 0.0807  225 ARG A CG  
3581 C CD  A ARG A 222 ? 0.4371 0.7645 0.6260 -0.0778 -0.1478 0.0444  225 ARG A CD  
3582 C CD  B ARG A 222 ? 0.4048 0.8079 0.5946 -0.0532 -0.0736 0.0682  225 ARG A CD  
3583 N NE  A ARG A 222 ? 0.4305 0.7904 0.7172 -0.1211 -0.1231 0.0352  225 ARG A NE  
3584 N NE  B ARG A 222 ? 0.4474 0.8983 0.6923 -0.0230 -0.1070 0.0331  225 ARG A NE  
3585 C CZ  A ARG A 222 ? 0.4402 0.7776 0.7543 -0.1458 -0.1214 0.0290  225 ARG A CZ  
3586 C CZ  B ARG A 222 ? 0.4430 0.8944 0.6612 0.0212  -0.1151 0.0270  225 ARG A CZ  
3587 N NH1 A ARG A 222 ? 0.4493 0.7320 0.6930 -0.1351 -0.1444 0.0367  225 ARG A NH1 
3588 N NH1 B ARG A 222 ? 0.4485 0.8598 0.6070 0.0289  -0.0811 0.0485  225 ARG A NH1 
3589 N NH2 A ARG A 222 ? 0.4540 0.8211 0.8767 -0.1835 -0.0890 0.0106  225 ARG A NH2 
3590 N NH2 B ARG A 222 ? 0.4747 0.9702 0.7302 0.0625  -0.1563 -0.0061 225 ARG A NH2 
3617 N N   . SER A 223 ? 0.4780 0.6327 0.4345 -0.0304 -0.1587 0.0819  226 SER A N   
3618 C CA  . SER A 223 ? 0.4998 0.6405 0.4587 -0.0295 -0.1916 0.0632  226 SER A CA  
3619 C C   . SER A 223 ? 0.5501 0.6146 0.4059 0.0100  -0.2036 0.0645  226 SER A C   
3620 O O   . SER A 223 ? 0.6157 0.6187 0.4063 0.0162  -0.1718 0.0848  226 SER A O   
3621 C CB  . SER A 223 ? 0.5301 0.6508 0.5134 -0.0744 -0.1737 0.0781  226 SER A CB  
3622 O OG  . SER A 223 ? 0.5803 0.6896 0.5736 -0.0746 -0.2044 0.0521  226 SER A OG  
3628 N N   . ARG A 224 ? 0.5932 0.6616 0.4360 0.0375  -0.2454 0.0369  227 ARG A N   
3629 C CA  . ARG A 224 ? 0.6588 0.6423 0.3902 0.0770  -0.2508 0.0417  227 ARG A CA  
3630 C C   . ARG A 224 ? 0.6789 0.5996 0.3881 0.0396  -0.2311 0.0540  227 ARG A C   
3631 O O   . ARG A 224 ? 0.7584 0.5971 0.3815 0.0618  -0.2150 0.0614  227 ARG A O   
3632 C CB  . ARG A 224 ? 0.7996 0.8175 0.5191 0.1251  -0.2985 0.0049  227 ARG A CB  
3633 C CG  . ARG A 224 ? 0.8865 1.0181 0.7008 0.1367  -0.3340 -0.0311 227 ARG A CG  
3634 C CD  . ARG A 224 ? 1.0491 1.1942 0.8582 0.1624  -0.3175 -0.0111 227 ARG A CD  
3635 N NE  . ARG A 224 ? 1.0225 1.2738 0.9644 0.1303  -0.3242 -0.0367 227 ARG A NE  
3636 C CZ  . ARG A 224 ? 0.9282 1.2067 0.9021 0.1293  -0.2993 -0.0232 227 ARG A CZ  
3637 N NH1 . ARG A 224 ? 0.8258 1.0390 0.7154 0.1598  -0.2680 0.0121  227 ARG A NH1 
3638 N NH2 . ARG A 224 ? 0.9406 1.3092 1.0403 0.0931  -0.2971 -0.0486 227 ARG A NH2 
3652 N N   . ALA A 225 ? 0.5852 0.5392 0.3736 -0.0142 -0.2214 0.0578  228 ALA A N   
3653 C CA  . ALA A 225 ? 0.6062 0.5102 0.3840 -0.0444 -0.2086 0.0662  228 ALA A CA  
3654 C C   . ALA A 225 ? 0.6814 0.5234 0.4018 -0.0468 -0.1697 0.0891  228 ALA A C   
3655 O O   . ALA A 225 ? 0.7310 0.5215 0.4272 -0.0606 -0.1589 0.0911  228 ALA A O   
3656 C CB  . ALA A 225 ? 0.5551 0.5025 0.4253 -0.0920 -0.1957 0.0743  228 ALA A CB  
3662 N N   . ILE A 226 ? 0.6010 0.4536 0.3111 -0.0353 -0.1465 0.0982  229 ILE A N   
3663 C CA  . ILE A 226 ? 0.6242 0.4356 0.3057 -0.0441 -0.1066 0.1032  229 ILE A CA  
3664 C C   . ILE A 226 ? 0.7276 0.4518 0.3344 -0.0140 -0.0806 0.0939  229 ILE A C   
3665 O O   . ILE A 226 ? 0.7267 0.4084 0.3191 -0.0225 -0.0401 0.0848  229 ILE A O   
3666 C CB  . ILE A 226 ? 0.5385 0.4072 0.2556 -0.0507 -0.0852 0.1073  229 ILE A CB  
3667 C CG1 . ILE A 226 ? 0.6125 0.4846 0.3124 -0.0180 -0.0806 0.1046  229 ILE A CG1 
3668 C CG2 . ILE A 226 ? 0.5054 0.4465 0.2868 -0.0774 -0.0953 0.1215  229 ILE A CG2 
3669 C CD1 . ILE A 226 ? 0.6084 0.5276 0.3394 -0.0252 -0.0492 0.1017  229 ILE A CD1 
3681 N N   . PHE A 227 ? 0.6365 0.4989 0.2355 0.1147  -0.0175 -0.0027 230 PHE A N   
3682 C CA  . PHE A 227 ? 0.6779 0.4916 0.2524 0.0846  -0.0420 0.0028  230 PHE A CA  
3683 C C   . PHE A 227 ? 0.7613 0.5624 0.3177 0.0388  -0.0160 0.0127  230 PHE A C   
3684 O O   . PHE A 227 ? 0.7543 0.5775 0.3143 0.0254  0.0078  0.0144  230 PHE A O   
3685 C CB  . PHE A 227 ? 0.6973 0.5001 0.2652 0.0856  -0.0808 0.0055  230 PHE A CB  
3686 C CG  . PHE A 227 ? 0.7058 0.5121 0.2864 0.1291  -0.1156 -0.0057 230 PHE A CG  
3687 C CD1 . PHE A 227 ? 0.8083 0.6601 0.4076 0.1688  -0.1124 -0.0135 230 PHE A CD1 
3688 C CD2 . PHE A 227 ? 0.7492 0.5170 0.3268 0.1346  -0.1520 -0.0086 230 PHE A CD2 
3689 C CE1 . PHE A 227 ? 0.8602 0.7193 0.4687 0.2139  -0.1455 -0.0266 230 PHE A CE1 
3690 C CE2 . PHE A 227 ? 0.8610 0.6306 0.4514 0.1779  -0.1883 -0.0229 230 PHE A CE2 
3691 C CZ  . PHE A 227 ? 0.8881 0.7045 0.4915 0.2197  -0.1846 -0.0338 230 PHE A CZ  
3701 N N   . GLY A 228 ? 0.7612 0.5281 0.2998 0.0158  -0.0231 0.0196  231 GLY A N   
3702 C CA  . GLY A 228 ? 0.7645 0.5217 0.2808 -0.0250 -0.0041 0.0293  231 GLY A CA  
3703 C C   . GLY A 228 ? 0.8952 0.6517 0.3979 -0.0429 -0.0198 0.0351  231 GLY A C   
3704 O O   . GLY A 228 ? 0.8357 0.5861 0.3416 -0.0304 -0.0531 0.0361  231 GLY A O   
3708 N N   . GLU A 229 ? 0.8974 0.6614 0.3857 -0.0700 0.0032  0.0369  232 GLU A N   
3709 C CA  . GLU A 229 ? 0.8319 0.5933 0.3032 -0.0894 -0.0123 0.0420  232 GLU A CA  
3710 C C   . GLU A 229 ? 1.0198 0.7540 0.4674 -0.1080 -0.0390 0.0579  232 GLU A C   
3711 O O   . GLU A 229 ? 1.0009 0.7277 0.4375 -0.1258 -0.0276 0.0665  232 GLU A O   
3712 C CB  . GLU A 229 ? 1.0968 0.8725 0.5587 -0.1113 0.0165  0.0370  232 GLU A CB  
3713 C CG  . GLU A 229 ? 1.0587 0.8568 0.5392 -0.1054 0.0173  0.0293  232 GLU A CG  
3714 C CD  . GLU A 229 ? 1.0879 0.8906 0.5542 -0.1306 0.0295  0.0245  232 GLU A CD  
3715 O OE1 . GLU A 229 ? 1.0863 0.8955 0.5639 -0.1382 0.0515  0.0194  232 GLU A OE1 
3716 O OE2 . GLU A 229 ? 0.8418 0.6499 0.3091 -0.1352 0.0146  0.0229  232 GLU A OE2 
3723 N N   . ALA A 230 ? 0.8676 0.5916 0.3154 -0.1028 -0.0747 0.0633  233 ALA A N   
3724 C CA  . ALA A 230 ? 0.9119 0.6126 0.3430 -0.1214 -0.1023 0.0826  233 ALA A CA  
3725 C C   . ALA A 230 ? 0.9500 0.6487 0.3749 -0.1245 -0.1316 0.0867  233 ALA A C   
3726 O O   . ALA A 230 ? 1.0631 0.7741 0.5014 -0.1057 -0.1372 0.0742  233 ALA A O   
3727 C CB  . ALA A 230 ? 1.0258 0.7038 0.4744 -0.1065 -0.1270 0.0888  233 ALA A CB  
3733 N N   . GLU A 231 ? 0.9399 0.6291 0.3499 -0.1478 -0.1478 0.1056  234 GLU A N   
3734 C CA  . GLU A 231 ? 1.0012 0.6897 0.4109 -0.1519 -0.1754 0.1111  234 GLU A CA  
3735 C C   . GLU A 231 ? 1.2106 0.8767 0.6397 -0.1336 -0.2180 0.1158  234 GLU A C   
3736 O O   . GLU A 231 ? 1.3090 0.9580 0.7496 -0.1415 -0.2387 0.1332  234 GLU A O   
3737 C CB  . GLU A 231 ? 0.9743 0.6716 0.3759 -0.1786 -0.1722 0.1282  234 GLU A CB  
3738 C CG  . GLU A 231 ? 0.9616 0.6658 0.3576 -0.1846 -0.1879 0.1295  234 GLU A CG  
3739 C CD  . GLU A 231 ? 0.9380 0.6599 0.3241 -0.1814 -0.1683 0.1088  234 GLU A CD  
3740 O OE1 . GLU A 231 ? 0.9220 0.6572 0.3025 -0.1854 -0.1365 0.0986  234 GLU A OE1 
3741 O OE2 . GLU A 231 ? 0.9450 0.6682 0.3326 -0.1761 -0.1857 0.1041  234 GLU A OE2 
4239 C C1  . RET S .   ? 0.2078 0.2597 0.2527 0.0156  -0.0122 0.0235  318 RET A C1  
4240 C C2  . RET S .   ? 0.3512 0.3996 0.3908 0.0203  -0.0073 0.0280  318 RET A C2  
4241 C C3  . RET S .   ? 0.4478 0.4727 0.4704 0.0304  -0.0021 0.0302  318 RET A C3  
4242 C C4  . RET S .   ? 0.2413 0.2452 0.2496 0.0364  -0.0016 0.0271  318 RET A C4  
4243 C C5  . RET S .   ? 0.2310 0.2390 0.2457 0.0294  -0.0076 0.0213  318 RET A C5  
4244 C C6  . RET S .   ? 0.2203 0.2500 0.2517 0.0209  -0.0121 0.0203  318 RET A C6  
4245 C C7  . RET S .   ? 0.2040 0.2320 0.2382 0.0156  -0.0175 0.0152  318 RET A C7  
4246 C C8  . RET S .   ? 0.1995 0.2435 0.2466 0.0084  -0.0219 0.0141  318 RET A C8  
4247 C C9  . RET S .   ? 0.2080 0.2486 0.2552 0.0054  -0.0267 0.0106  318 RET A C9  
4248 C C10 . RET S .   ? 0.2055 0.2588 0.2654 -0.0019 -0.0298 0.0103  318 RET A C10 
4249 C C11 . RET S .   ? 0.2044 0.2564 0.2666 -0.0050 -0.0344 0.0081  318 RET A C11 
4250 C C12 . RET S .   ? 0.2134 0.2748 0.2860 -0.0109 -0.0359 0.0086  318 RET A C12 
4251 C C13 . RET S .   ? 0.2031 0.2635 0.2770 -0.0126 -0.0398 0.0082  318 RET A C13 
4252 C C14 . RET S .   ? 0.2244 0.2903 0.3057 -0.0178 -0.0392 0.0093  318 RET A C14 
4253 C C15 . RET S .   ? 0.2298 0.2952 0.3097 -0.0189 -0.0408 0.0112  318 RET A C15 
4254 C C16 . RET S .   ? 0.2174 0.2676 0.2748 0.0025  -0.0158 0.0177  318 RET A C16 
4255 C C17 . RET S .   ? 0.2516 0.3307 0.3023 0.0172  -0.0131 0.0285  318 RET A C17 
4256 C C18 . RET S .   ? 0.2802 0.2628 0.2754 0.0355  -0.0069 0.0177  318 RET A C18 
4257 C C19 . RET S .   ? 0.2457 0.2649 0.2774 0.0087  -0.0287 0.0065  318 RET A C19 
4258 C C20 . RET S .   ? 0.2304 0.2816 0.2950 -0.0090 -0.0440 0.0065  318 RET A C20 
# 
