data_9F9D
# 
_entry.id   9F9D 
# 
_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   9F9D         pdb_00009f9d 10.2210/pdb9f9d/pdb 
WWPDB D_1292138399 ?            ?                   
# 
_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                        9F9D 
_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                                                                        25261.807 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    51 ? ? ? ? 
# 
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       
;ATGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
ADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESM
RPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARY
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   ALA 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   ALA 1   4   4   ALA ALA 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  401 432 HOH HOH A . 
T 5 HOH 2  402 480 HOH HOH A . 
T 5 HOH 3  403 441 HOH HOH A . 
T 5 HOH 4  404 434 HOH HOH A . 
T 5 HOH 5  405 482 HOH HOH A . 
T 5 HOH 6  406 498 HOH HOH A . 
T 5 HOH 7  407 495 HOH HOH A . 
T 5 HOH 8  408 485 HOH HOH A . 
T 5 HOH 9  409 403 HOH HOH A . 
T 5 HOH 10 410 400 HOH HOH A . 
T 5 HOH 11 411 489 HOH HOH A . 
T 5 HOH 12 412 402 HOH HOH A . 
T 5 HOH 13 413 456 HOH HOH A . 
T 5 HOH 14 414 404 HOH HOH A . 
T 5 HOH 15 415 423 HOH HOH A . 
T 5 HOH 16 416 401 HOH HOH A . 
T 5 HOH 17 417 411 HOH HOH A . 
T 5 HOH 18 418 477 HOH HOH A . 
T 5 HOH 19 419 412 HOH HOH A . 
T 5 HOH 20 420 478 HOH HOH A . 
T 5 HOH 21 421 407 HOH HOH A . 
T 5 HOH 22 422 417 HOH HOH A . 
T 5 HOH 23 423 409 HOH HOH A . 
T 5 HOH 24 424 492 HOH HOH A . 
T 5 HOH 25 425 479 HOH HOH A . 
T 5 HOH 26 426 426 HOH HOH A . 
T 5 HOH 27 427 414 HOH HOH A . 
T 5 HOH 28 428 413 HOH HOH A . 
T 5 HOH 29 429 416 HOH HOH A . 
T 5 HOH 30 430 419 HOH HOH A . 
T 5 HOH 31 431 415 HOH HOH A . 
T 5 HOH 32 432 421 HOH HOH A . 
T 5 HOH 33 433 493 HOH HOH A . 
T 5 HOH 34 434 420 HOH HOH A . 
T 5 HOH 35 435 486 HOH HOH A . 
T 5 HOH 36 436 497 HOH HOH A . 
T 5 HOH 37 437 475 HOH HOH A . 
T 5 HOH 38 438 422 HOH HOH A . 
T 5 HOH 39 439 488 HOH HOH A . 
T 5 HOH 40 440 494 HOH HOH A . 
T 5 HOH 41 441 418 HOH HOH A . 
T 5 HOH 42 442 496 HOH HOH A . 
T 5 HOH 43 443 487 HOH HOH A . 
T 5 HOH 44 444 491 HOH HOH A . 
T 5 HOH 45 445 483 HOH HOH A . 
T 5 HOH 46 446 490 HOH HOH A . 
T 5 HOH 47 447 484 HOH HOH A . 
T 5 HOH 48 448 448 HOH HOH A . 
T 5 HOH 49 449 453 HOH HOH A . 
T 5 HOH 50 450 452 HOH HOH A . 
T 5 HOH 51 451 476 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 74  ? CG  ? A GLU 71  CG  
2   1 Y 1 A GLU 74  ? CD  ? A GLU 71  CD  
3   1 Y 1 A GLU 74  ? OE1 ? A GLU 71  OE1 
4   1 Y 1 A GLU 74  ? OE2 ? A GLU 71  OE2 
5   1 Y 1 A SER 158 ? OG  ? A SER 155 OG  
6   1 Y 1 A LYS 172 ? CG  ? A LYS 169 CG  
7   1 Y 1 A LYS 172 ? CD  ? A LYS 169 CD  
8   1 Y 1 A LYS 172 ? CE  ? A LYS 169 CE  
9   1 Y 1 A LYS 172 ? NZ  ? A LYS 169 NZ  
10  1 N 1 A LI1 301 ? C1  ? B LI1 1   C1  
11  1 N 1 A LI1 301 ? C2  ? B LI1 1   C2  
12  1 N 1 A LI1 301 ? C3  ? B LI1 1   C3  
13  1 N 1 A LI1 301 ? O1  ? B LI1 1   O1  
14  1 N 1 A LI1 301 ? O2  ? B LI1 1   O2  
15  1 N 1 A LI1 301 ? O3  ? B LI1 1   O3  
16  1 N 1 A LI1 301 ? C41 ? B LI1 1   C41 
17  1 N 1 A LI1 301 ? C42 ? B LI1 1   C42 
18  1 N 1 A LI1 301 ? C43 ? B LI1 1   C43 
19  1 N 1 A LI1 301 ? C44 ? B LI1 1   C44 
20  1 N 1 A LI1 301 ? C45 ? B LI1 1   C45 
21  1 N 1 A LI1 301 ? C46 ? B LI1 1   C46 
22  1 N 1 A LI1 301 ? C47 ? B LI1 1   C47 
23  1 N 1 A LI1 301 ? C48 ? B LI1 1   C48 
24  1 N 1 A LI1 301 ? C49 ? B LI1 1   C49 
25  1 N 1 A LI1 301 ? C50 ? B LI1 1   C50 
26  1 N 1 A LI1 301 ? C51 ? B LI1 1   C51 
27  1 N 1 A LI1 301 ? C59 ? B LI1 1   C59 
28  1 N 1 A LI1 301 ? C60 ? B LI1 1   C60 
29  1 N 1 A LI1 301 ? C11 ? B LI1 1   C11 
30  1 N 1 A LI1 301 ? C12 ? B LI1 1   C12 
31  1 N 1 A LI1 301 ? C13 ? B LI1 1   C13 
32  1 N 1 A LI1 301 ? C14 ? B LI1 1   C14 
33  1 N 1 A LI1 301 ? C15 ? B LI1 1   C15 
34  1 N 1 A LI1 301 ? C16 ? B LI1 1   C16 
35  1 N 1 A LI1 301 ? C17 ? B LI1 1   C17 
36  1 N 1 A LI1 301 ? C18 ? B LI1 1   C18 
37  1 N 1 A LI1 301 ? C19 ? B LI1 1   C19 
38  1 N 1 A LI1 301 ? C20 ? B LI1 1   C20 
39  1 N 1 A LI1 301 ? C21 ? B LI1 1   C21 
40  1 N 1 A LI1 301 ? C22 ? B LI1 1   C22 
41  1 N 1 A LI1 301 ? C23 ? B LI1 1   C23 
42  1 N 1 A LI1 301 ? C24 ? B LI1 1   C24 
43  1 N 1 A LI1 301 ? C25 ? B LI1 1   C25 
44  1 N 1 A LI1 301 ? C26 ? B LI1 1   C26 
45  1 N 1 A LI1 301 ? C27 ? B LI1 1   C27 
46  1 N 1 A LI1 301 ? C28 ? B LI1 1   C28 
47  1 N 1 A LI1 301 ? C29 ? B LI1 1   C29 
48  1 N 1 A LI1 301 ? C30 ? B LI1 1   C30 
49  1 N 1 A LI1 302 ? C1  ? C LI1 1   C1  
50  1 N 1 A LI1 302 ? C2  ? C LI1 1   C2  
51  1 N 1 A LI1 302 ? C3  ? C LI1 1   C3  
52  1 N 1 A LI1 302 ? O1  ? C LI1 1   O1  
53  1 N 1 A LI1 302 ? O2  ? C LI1 1   O2  
54  1 N 1 A LI1 302 ? O3  ? C LI1 1   O3  
55  1 N 1 A LI1 302 ? C41 ? C LI1 1   C41 
56  1 N 1 A LI1 302 ? C42 ? C LI1 1   C42 
57  1 N 1 A LI1 302 ? C43 ? C LI1 1   C43 
58  1 N 1 A LI1 302 ? C44 ? C LI1 1   C44 
59  1 N 1 A LI1 302 ? C45 ? C LI1 1   C45 
60  1 N 1 A LI1 302 ? C11 ? C LI1 1   C11 
61  1 N 1 A LI1 302 ? C12 ? C LI1 1   C12 
62  1 N 1 A LI1 302 ? C13 ? C LI1 1   C13 
63  1 N 1 A LI1 302 ? C14 ? C LI1 1   C14 
64  1 N 1 A LI1 302 ? C15 ? C LI1 1   C15 
65  1 N 1 A LI1 302 ? C16 ? C LI1 1   C16 
66  1 N 1 A LI1 302 ? C17 ? C LI1 1   C17 
67  1 N 1 A LI1 302 ? C18 ? C LI1 1   C18 
68  1 N 1 A LI1 302 ? C19 ? C LI1 1   C19 
69  1 N 1 A LI1 302 ? C20 ? C LI1 1   C20 
70  1 N 1 A LI1 302 ? C21 ? C LI1 1   C21 
71  1 N 1 A LI1 302 ? C22 ? C LI1 1   C22 
72  1 N 1 A LI1 302 ? C23 ? C LI1 1   C23 
73  1 N 1 A LI1 302 ? C24 ? C LI1 1   C24 
74  1 N 1 A LI1 302 ? C25 ? C LI1 1   C25 
75  1 N 1 A LI1 302 ? C26 ? C LI1 1   C26 
76  1 N 1 A LI1 302 ? C27 ? C LI1 1   C27 
77  1 N 1 A LI1 302 ? C28 ? C LI1 1   C28 
78  1 N 1 A LI1 302 ? C29 ? C LI1 1   C29 
79  1 N 1 A LI1 302 ? C30 ? C LI1 1   C30 
80  1 N 1 A LI1 303 ? C1  ? D LI1 1   C1  
81  1 N 1 A LI1 303 ? C2  ? D LI1 1   C2  
82  1 N 1 A LI1 303 ? C3  ? D LI1 1   C3  
83  1 N 1 A LI1 303 ? O1  ? D LI1 1   O1  
84  1 N 1 A LI1 303 ? O2  ? D LI1 1   O2  
85  1 N 1 A LI1 303 ? O3  ? D LI1 1   O3  
86  1 N 1 A LI1 303 ? C41 ? D LI1 1   C41 
87  1 N 1 A LI1 303 ? C42 ? D LI1 1   C42 
88  1 N 1 A LI1 303 ? C43 ? D LI1 1   C43 
89  1 N 1 A LI1 303 ? C44 ? D LI1 1   C44 
90  1 N 1 A LI1 303 ? C45 ? D LI1 1   C45 
91  1 N 1 A LI1 303 ? C46 ? D LI1 1   C46 
92  1 N 1 A LI1 303 ? C47 ? D LI1 1   C47 
93  1 N 1 A LI1 303 ? C48 ? D LI1 1   C48 
94  1 N 1 A LI1 303 ? C49 ? D LI1 1   C49 
95  1 N 1 A LI1 303 ? C59 ? D LI1 1   C59 
96  1 N 1 A LI1 303 ? C60 ? D LI1 1   C60 
97  1 N 1 A LI1 303 ? C11 ? D LI1 1   C11 
98  1 N 1 A LI1 303 ? C12 ? D LI1 1   C12 
99  1 N 1 A LI1 303 ? C13 ? D LI1 1   C13 
100 1 N 1 A LI1 303 ? C14 ? D LI1 1   C14 
101 1 N 1 A LI1 303 ? C15 ? D LI1 1   C15 
102 1 N 1 A LI1 303 ? C16 ? D LI1 1   C16 
103 1 N 1 A LI1 303 ? C17 ? D LI1 1   C17 
104 1 N 1 A LI1 303 ? C18 ? D LI1 1   C18 
105 1 N 1 A LI1 303 ? C19 ? D LI1 1   C19 
106 1 N 1 A LI1 303 ? C20 ? D LI1 1   C20 
107 1 N 1 A LI1 303 ? C21 ? D LI1 1   C21 
108 1 N 1 A LI1 303 ? C22 ? D LI1 1   C22 
109 1 N 1 A LI1 303 ? C23 ? D LI1 1   C23 
110 1 N 1 A LI1 303 ? C24 ? D LI1 1   C24 
111 1 N 1 A LI1 303 ? C25 ? D LI1 1   C25 
112 1 N 1 A LI1 303 ? C26 ? D LI1 1   C26 
113 1 N 1 A LI1 303 ? C27 ? D LI1 1   C27 
114 1 N 1 A LI1 303 ? C28 ? D LI1 1   C28 
115 1 N 1 A LI1 303 ? C29 ? D LI1 1   C29 
116 1 N 1 A LI1 303 ? C30 ? D LI1 1   C30 
117 1 N 1 A LI1 304 ? C1  ? E LI1 1   C1  
118 1 N 1 A LI1 304 ? C2  ? E LI1 1   C2  
119 1 N 1 A LI1 304 ? C3  ? E LI1 1   C3  
120 1 N 1 A LI1 304 ? O1  ? E LI1 1   O1  
121 1 N 1 A LI1 304 ? O2  ? E LI1 1   O2  
122 1 N 1 A LI1 304 ? O3  ? E LI1 1   O3  
123 1 N 1 A LI1 304 ? C41 ? E LI1 1   C41 
124 1 N 1 A LI1 304 ? C42 ? E LI1 1   C42 
125 1 N 1 A LI1 304 ? C43 ? E LI1 1   C43 
126 1 N 1 A LI1 304 ? C44 ? E LI1 1   C44 
127 1 N 1 A LI1 304 ? C49 ? E LI1 1   C49 
128 1 N 1 A LI1 304 ? C59 ? E LI1 1   C59 
129 1 N 1 A LI1 304 ? C60 ? E LI1 1   C60 
130 1 N 1 A LI1 304 ? C11 ? E LI1 1   C11 
131 1 N 1 A LI1 304 ? C12 ? E LI1 1   C12 
132 1 N 1 A LI1 304 ? C13 ? E LI1 1   C13 
133 1 N 1 A LI1 304 ? C14 ? E LI1 1   C14 
134 1 N 1 A LI1 304 ? C15 ? E LI1 1   C15 
135 1 N 1 A LI1 304 ? C16 ? E LI1 1   C16 
136 1 N 1 A LI1 304 ? C17 ? E LI1 1   C17 
137 1 N 1 A LI1 304 ? C18 ? E LI1 1   C18 
138 1 N 1 A LI1 304 ? C19 ? E LI1 1   C19 
139 1 N 1 A LI1 304 ? C20 ? E LI1 1   C20 
140 1 N 1 A LI1 304 ? C21 ? E LI1 1   C21 
141 1 N 1 A LI1 304 ? C22 ? E LI1 1   C22 
142 1 N 1 A LI1 304 ? C23 ? E LI1 1   C23 
143 1 N 1 A LI1 304 ? C24 ? E LI1 1   C24 
144 1 N 1 A LI1 304 ? C25 ? E LI1 1   C25 
145 1 N 1 A LI1 304 ? C26 ? E LI1 1   C26 
146 1 N 1 A LI1 304 ? C27 ? E LI1 1   C27 
147 1 N 1 A LI1 304 ? C28 ? E LI1 1   C28 
148 1 N 1 A LI1 304 ? C29 ? E LI1 1   C29 
149 1 N 1 A LI1 304 ? C30 ? E LI1 1   C30 
150 1 N 1 A LI1 305 ? C1  ? F LI1 1   C1  
151 1 N 1 A LI1 305 ? C2  ? F LI1 1   C2  
152 1 N 1 A LI1 305 ? C3  ? F LI1 1   C3  
153 1 N 1 A LI1 305 ? O1  ? F LI1 1   O1  
154 1 N 1 A LI1 305 ? O2  ? F LI1 1   O2  
155 1 N 1 A LI1 305 ? O3  ? F LI1 1   O3  
156 1 N 1 A LI1 305 ? C41 ? F LI1 1   C41 
157 1 N 1 A LI1 305 ? C42 ? F LI1 1   C42 
158 1 N 1 A LI1 305 ? C43 ? F LI1 1   C43 
159 1 N 1 A LI1 305 ? C44 ? F LI1 1   C44 
160 1 N 1 A LI1 305 ? C49 ? F LI1 1   C49 
161 1 N 1 A LI1 305 ? C60 ? F LI1 1   C60 
162 1 N 1 A LI1 305 ? C11 ? F LI1 1   C11 
163 1 N 1 A LI1 305 ? C12 ? F LI1 1   C12 
164 1 N 1 A LI1 305 ? C13 ? F LI1 1   C13 
165 1 N 1 A LI1 305 ? C14 ? F LI1 1   C14 
166 1 N 1 A LI1 305 ? C15 ? F LI1 1   C15 
167 1 N 1 A LI1 305 ? C16 ? F LI1 1   C16 
168 1 N 1 A LI1 305 ? C17 ? F LI1 1   C17 
169 1 N 1 A LI1 305 ? C18 ? F LI1 1   C18 
170 1 N 1 A LI1 305 ? C19 ? F LI1 1   C19 
171 1 N 1 A LI1 305 ? C20 ? F LI1 1   C20 
172 1 N 1 A LI1 305 ? C21 ? F LI1 1   C21 
173 1 N 1 A LI1 305 ? C22 ? F LI1 1   C22 
174 1 N 1 A LI1 305 ? C23 ? F LI1 1   C23 
175 1 N 1 A LI1 305 ? C24 ? F LI1 1   C24 
176 1 N 1 A LI1 305 ? C25 ? F LI1 1   C25 
177 1 N 1 A LI1 305 ? C26 ? F LI1 1   C26 
178 1 N 1 A LI1 305 ? C27 ? F LI1 1   C27 
179 1 N 1 A LI1 305 ? C28 ? F LI1 1   C28 
180 1 N 1 A LI1 305 ? C29 ? F LI1 1   C29 
181 1 N 1 A LI1 305 ? C30 ? F LI1 1   C30 
182 1 N 1 A LI1 306 ? C1  ? G LI1 1   C1  
183 1 N 1 A LI1 306 ? C2  ? G LI1 1   C2  
184 1 N 1 A LI1 306 ? C3  ? G LI1 1   C3  
185 1 N 1 A LI1 306 ? O1  ? G LI1 1   O1  
186 1 N 1 A LI1 306 ? O2  ? G LI1 1   O2  
187 1 N 1 A LI1 306 ? O3  ? G LI1 1   O3  
188 1 N 1 A LI1 306 ? C41 ? G LI1 1   C41 
189 1 N 1 A LI1 306 ? C42 ? G LI1 1   C42 
190 1 N 1 A LI1 306 ? C43 ? G LI1 1   C43 
191 1 N 1 A LI1 306 ? C44 ? G LI1 1   C44 
192 1 N 1 A LI1 306 ? C45 ? G LI1 1   C45 
193 1 N 1 A LI1 306 ? C49 ? G LI1 1   C49 
194 1 N 1 A LI1 306 ? C11 ? G LI1 1   C11 
195 1 N 1 A LI1 306 ? C12 ? G LI1 1   C12 
196 1 N 1 A LI1 306 ? C13 ? G LI1 1   C13 
197 1 N 1 A LI1 306 ? C14 ? G LI1 1   C14 
198 1 N 1 A LI1 306 ? C15 ? G LI1 1   C15 
199 1 N 1 A LI1 306 ? C16 ? G LI1 1   C16 
200 1 N 1 A LI1 306 ? C17 ? G LI1 1   C17 
201 1 N 1 A LI1 306 ? C18 ? G LI1 1   C18 
202 1 N 1 A LI1 306 ? C19 ? G LI1 1   C19 
203 1 N 1 A LI1 306 ? C20 ? G LI1 1   C20 
204 1 N 1 A LI1 306 ? C21 ? G LI1 1   C21 
205 1 N 1 A LI1 306 ? C22 ? G LI1 1   C22 
206 1 N 1 A LI1 306 ? C23 ? G LI1 1   C23 
207 1 N 1 A LI1 306 ? C24 ? G LI1 1   C24 
208 1 N 1 A LI1 306 ? C25 ? G LI1 1   C25 
209 1 N 1 A LI1 306 ? C26 ? G LI1 1   C26 
210 1 N 1 A LI1 306 ? C27 ? G LI1 1   C27 
211 1 N 1 A LI1 306 ? C28 ? G LI1 1   C28 
212 1 N 1 A LI1 306 ? C29 ? G LI1 1   C29 
213 1 N 1 A LI1 306 ? C30 ? G LI1 1   C30 
214 1 N 1 A LI1 312 ? C1  ? M LI1 1   C1  
215 1 N 1 A LI1 312 ? C2  ? M LI1 1   C2  
216 1 N 1 A LI1 312 ? C3  ? M LI1 1   C3  
217 1 N 1 A LI1 312 ? O1  ? M LI1 1   O1  
218 1 N 1 A LI1 312 ? O2  ? M LI1 1   O2  
219 1 N 1 A LI1 312 ? O3  ? M LI1 1   O3  
220 1 N 1 A LI1 312 ? C41 ? M LI1 1   C41 
221 1 N 1 A LI1 312 ? C42 ? M LI1 1   C42 
222 1 N 1 A LI1 312 ? C43 ? M LI1 1   C43 
223 1 N 1 A LI1 312 ? C44 ? M LI1 1   C44 
224 1 N 1 A LI1 312 ? C49 ? M LI1 1   C49 
225 1 N 1 A LI1 312 ? C57 ? M LI1 1   C57 
226 1 N 1 A LI1 312 ? C58 ? M LI1 1   C58 
227 1 N 1 A LI1 312 ? C59 ? M LI1 1   C59 
228 1 N 1 A LI1 312 ? C60 ? M LI1 1   C60 
229 1 N 1 A LI1 312 ? C11 ? M LI1 1   C11 
230 1 N 1 A LI1 312 ? C12 ? M LI1 1   C12 
231 1 N 1 A LI1 312 ? C13 ? M LI1 1   C13 
232 1 N 1 A LI1 312 ? C14 ? M LI1 1   C14 
233 1 N 1 A LI1 312 ? C15 ? M LI1 1   C15 
234 1 N 1 A LI1 312 ? C16 ? M LI1 1   C16 
235 1 N 1 A LI1 312 ? C17 ? M LI1 1   C17 
236 1 N 1 A LI1 312 ? C18 ? M LI1 1   C18 
237 1 N 1 A LI1 312 ? C19 ? M LI1 1   C19 
238 1 N 1 A LI1 312 ? C20 ? M LI1 1   C20 
239 1 N 1 A LI1 312 ? C21 ? M LI1 1   C21 
240 1 N 1 A LI1 312 ? C22 ? M LI1 1   C22 
241 1 N 1 A LI1 312 ? C23 ? M LI1 1   C23 
242 1 N 1 A LI1 312 ? C24 ? M LI1 1   C24 
243 1 N 1 A LI1 312 ? C25 ? M LI1 1   C25 
244 1 N 1 A LI1 312 ? C26 ? M LI1 1   C26 
245 1 N 1 A LI1 312 ? C27 ? M LI1 1   C27 
246 1 N 1 A LI1 312 ? C28 ? M LI1 1   C28 
247 1 N 1 A LI1 312 ? C29 ? M LI1 1   C29 
248 1 N 1 A LI1 312 ? C30 ? M LI1 1   C30 
249 1 N 1 A LI1 313 ? C1  ? N LI1 1   C1  
250 1 N 1 A LI1 313 ? C2  ? N LI1 1   C2  
251 1 N 1 A LI1 313 ? C3  ? N LI1 1   C3  
252 1 N 1 A LI1 313 ? O1  ? N LI1 1   O1  
253 1 N 1 A LI1 313 ? O2  ? N LI1 1   O2  
254 1 N 1 A LI1 313 ? O3  ? N LI1 1   O3  
255 1 N 1 A LI1 313 ? C41 ? N LI1 1   C41 
256 1 N 1 A LI1 313 ? C42 ? N LI1 1   C42 
257 1 N 1 A LI1 313 ? C43 ? N LI1 1   C43 
258 1 N 1 A LI1 313 ? C44 ? N LI1 1   C44 
259 1 N 1 A LI1 313 ? C49 ? N LI1 1   C49 
260 1 N 1 A LI1 313 ? C60 ? N LI1 1   C60 
261 1 N 1 A LI1 313 ? C11 ? N LI1 1   C11 
262 1 N 1 A LI1 313 ? C12 ? N LI1 1   C12 
263 1 N 1 A LI1 313 ? C13 ? N LI1 1   C13 
264 1 N 1 A LI1 313 ? C14 ? N LI1 1   C14 
265 1 N 1 A LI1 313 ? C15 ? N LI1 1   C15 
266 1 N 1 A LI1 313 ? C16 ? N LI1 1   C16 
267 1 N 1 A LI1 313 ? C17 ? N LI1 1   C17 
268 1 N 1 A LI1 313 ? C18 ? N LI1 1   C18 
269 1 N 1 A LI1 313 ? C19 ? N LI1 1   C19 
270 1 N 1 A LI1 313 ? C20 ? N LI1 1   C20 
271 1 N 1 A LI1 313 ? C21 ? N LI1 1   C21 
272 1 N 1 A LI1 313 ? C22 ? N LI1 1   C22 
273 1 N 1 A LI1 313 ? C23 ? N LI1 1   C23 
274 1 N 1 A LI1 313 ? C24 ? N LI1 1   C24 
275 1 N 1 A LI1 313 ? C25 ? N LI1 1   C25 
276 1 N 1 A LI1 313 ? C26 ? N LI1 1   C26 
277 1 N 1 A LI1 313 ? C27 ? N LI1 1   C27 
278 1 N 1 A LI1 313 ? C28 ? N LI1 1   C28 
279 1 N 1 A LI1 313 ? C29 ? N LI1 1   C29 
280 1 N 1 A LI1 313 ? C30 ? N LI1 1   C30 
281 1 N 1 A LI1 314 ? C1  ? O LI1 1   C1  
282 1 N 1 A LI1 314 ? C2  ? O LI1 1   C2  
283 1 N 1 A LI1 314 ? C3  ? O LI1 1   C3  
284 1 N 1 A LI1 314 ? O1  ? O LI1 1   O1  
285 1 N 1 A LI1 314 ? O2  ? O LI1 1   O2  
286 1 N 1 A LI1 314 ? O3  ? O LI1 1   O3  
287 1 N 1 A LI1 314 ? C41 ? O LI1 1   C41 
288 1 N 1 A LI1 314 ? C42 ? O LI1 1   C42 
289 1 N 1 A LI1 314 ? C43 ? O LI1 1   C43 
290 1 N 1 A LI1 314 ? C44 ? O LI1 1   C44 
291 1 N 1 A LI1 314 ? C45 ? O LI1 1   C45 
292 1 N 1 A LI1 314 ? C46 ? O LI1 1   C46 
293 1 N 1 A LI1 314 ? C47 ? O LI1 1   C47 
294 1 N 1 A LI1 314 ? C48 ? O LI1 1   C48 
295 1 N 1 A LI1 314 ? C49 ? O LI1 1   C49 
296 1 N 1 A LI1 314 ? C59 ? O LI1 1   C59 
297 1 N 1 A LI1 314 ? C60 ? O LI1 1   C60 
298 1 N 1 A LI1 314 ? C11 ? O LI1 1   C11 
299 1 N 1 A LI1 314 ? C12 ? O LI1 1   C12 
300 1 N 1 A LI1 314 ? C13 ? O LI1 1   C13 
301 1 N 1 A LI1 314 ? C14 ? O LI1 1   C14 
302 1 N 1 A LI1 314 ? C15 ? O LI1 1   C15 
303 1 N 1 A LI1 314 ? C16 ? O LI1 1   C16 
304 1 N 1 A LI1 314 ? C17 ? O LI1 1   C17 
305 1 N 1 A LI1 314 ? C18 ? O LI1 1   C18 
306 1 N 1 A LI1 314 ? C19 ? O LI1 1   C19 
307 1 N 1 A LI1 314 ? C20 ? O LI1 1   C20 
308 1 N 1 A LI1 314 ? C21 ? O LI1 1   C21 
309 1 N 1 A LI1 314 ? C22 ? O LI1 1   C22 
310 1 N 1 A LI1 314 ? C23 ? O LI1 1   C23 
311 1 N 1 A LI1 314 ? C24 ? O LI1 1   C24 
312 1 N 1 A LI1 314 ? C25 ? O LI1 1   C25 
313 1 N 1 A LI1 314 ? C26 ? O LI1 1   C26 
314 1 N 1 A LI1 314 ? C27 ? O LI1 1   C27 
315 1 N 1 A LI1 314 ? C28 ? O LI1 1   C28 
316 1 N 1 A LI1 314 ? C29 ? O LI1 1   C29 
317 1 N 1 A LI1 314 ? C30 ? O LI1 1   C30 
318 1 N 1 A LI1 315 ? C1  ? P LI1 1   C1  
319 1 N 1 A LI1 315 ? C2  ? P LI1 1   C2  
320 1 N 1 A LI1 315 ? C3  ? P LI1 1   C3  
321 1 N 1 A LI1 315 ? O1  ? P LI1 1   O1  
322 1 N 1 A LI1 315 ? O2  ? P LI1 1   O2  
323 1 N 1 A LI1 315 ? O3  ? P LI1 1   O3  
324 1 N 1 A LI1 315 ? C41 ? P LI1 1   C41 
325 1 N 1 A LI1 315 ? C42 ? P LI1 1   C42 
326 1 N 1 A LI1 315 ? C43 ? P LI1 1   C43 
327 1 N 1 A LI1 315 ? C44 ? P LI1 1   C44 
328 1 N 1 A LI1 315 ? C45 ? P LI1 1   C45 
329 1 N 1 A LI1 315 ? C49 ? P LI1 1   C49 
330 1 N 1 A LI1 315 ? C11 ? P LI1 1   C11 
331 1 N 1 A LI1 315 ? C12 ? P LI1 1   C12 
332 1 N 1 A LI1 315 ? C13 ? P LI1 1   C13 
333 1 N 1 A LI1 315 ? C14 ? P LI1 1   C14 
334 1 N 1 A LI1 315 ? C15 ? P LI1 1   C15 
335 1 N 1 A LI1 315 ? C16 ? P LI1 1   C16 
336 1 N 1 A LI1 315 ? C17 ? P LI1 1   C17 
337 1 N 1 A LI1 315 ? C18 ? P LI1 1   C18 
338 1 N 1 A LI1 315 ? C19 ? P LI1 1   C19 
339 1 N 1 A LI1 315 ? C20 ? P LI1 1   C20 
340 1 N 1 A LI1 315 ? C21 ? P LI1 1   C21 
341 1 N 1 A LI1 315 ? C22 ? P LI1 1   C22 
342 1 N 1 A LI1 315 ? C23 ? P LI1 1   C23 
343 1 N 1 A LI1 315 ? C24 ? P LI1 1   C24 
344 1 N 1 A LI1 315 ? C25 ? P LI1 1   C25 
345 1 N 1 A LI1 315 ? C26 ? P LI1 1   C26 
346 1 N 1 A LI1 315 ? C27 ? P LI1 1   C27 
347 1 N 1 A LI1 315 ? C28 ? P LI1 1   C28 
348 1 N 1 A LI1 315 ? C29 ? P LI1 1   C29 
349 1 N 1 A LI1 315 ? C30 ? P LI1 1   C30 
350 1 N 1 A LI1 316 ? C1  ? Q LI1 1   C1  
351 1 N 1 A LI1 316 ? C2  ? Q LI1 1   C2  
352 1 N 1 A LI1 316 ? C3  ? Q LI1 1   C3  
353 1 N 1 A LI1 316 ? O1  ? Q LI1 1   O1  
354 1 N 1 A LI1 316 ? O2  ? Q LI1 1   O2  
355 1 N 1 A LI1 316 ? O3  ? Q LI1 1   O3  
356 1 N 1 A LI1 316 ? C41 ? Q LI1 1   C41 
357 1 N 1 A LI1 316 ? C42 ? Q LI1 1   C42 
358 1 N 1 A LI1 316 ? C43 ? Q LI1 1   C43 
359 1 N 1 A LI1 316 ? C44 ? Q LI1 1   C44 
360 1 N 1 A LI1 316 ? C49 ? Q LI1 1   C49 
361 1 N 1 A LI1 316 ? C60 ? Q LI1 1   C60 
362 1 N 1 A LI1 316 ? C11 ? Q LI1 1   C11 
363 1 N 1 A LI1 316 ? C12 ? Q LI1 1   C12 
364 1 N 1 A LI1 316 ? C13 ? Q LI1 1   C13 
365 1 N 1 A LI1 316 ? C14 ? Q LI1 1   C14 
366 1 N 1 A LI1 316 ? C15 ? Q LI1 1   C15 
367 1 N 1 A LI1 316 ? C16 ? Q LI1 1   C16 
368 1 N 1 A LI1 316 ? C17 ? Q LI1 1   C17 
369 1 N 1 A LI1 316 ? C18 ? Q LI1 1   C18 
370 1 N 1 A LI1 316 ? C19 ? Q LI1 1   C19 
371 1 N 1 A LI1 316 ? C20 ? Q LI1 1   C20 
372 1 N 1 A LI1 316 ? C21 ? Q LI1 1   C21 
373 1 N 1 A LI1 316 ? C22 ? Q LI1 1   C22 
374 1 N 1 A LI1 316 ? C23 ? Q LI1 1   C23 
375 1 N 1 A LI1 316 ? C24 ? Q LI1 1   C24 
376 1 N 1 A LI1 316 ? C25 ? Q LI1 1   C25 
377 1 N 1 A LI1 316 ? C26 ? Q LI1 1   C26 
378 1 N 1 A LI1 316 ? C27 ? Q LI1 1   C27 
379 1 N 1 A LI1 316 ? C28 ? Q LI1 1   C28 
380 1 N 1 A LI1 316 ? C29 ? Q LI1 1   C29 
381 1 N 1 A LI1 316 ? C30 ? Q LI1 1   C30 
382 1 N 1 A LI1 317 ? C1  ? R LI1 1   C1  
383 1 N 1 A LI1 317 ? C2  ? R LI1 1   C2  
384 1 N 1 A LI1 317 ? C3  ? R LI1 1   C3  
385 1 N 1 A LI1 317 ? O1  ? R LI1 1   O1  
386 1 N 1 A LI1 317 ? O2  ? R LI1 1   O2  
387 1 N 1 A LI1 317 ? O3  ? R LI1 1   O3  
388 1 N 1 A LI1 317 ? C41 ? R LI1 1   C41 
389 1 N 1 A LI1 317 ? C42 ? R LI1 1   C42 
390 1 N 1 A LI1 317 ? C43 ? R LI1 1   C43 
391 1 N 1 A LI1 317 ? C44 ? R LI1 1   C44 
392 1 N 1 A LI1 317 ? C45 ? R LI1 1   C45 
393 1 N 1 A LI1 317 ? C46 ? R LI1 1   C46 
394 1 N 1 A LI1 317 ? C47 ? R LI1 1   C47 
395 1 N 1 A LI1 317 ? C48 ? R LI1 1   C48 
396 1 N 1 A LI1 317 ? C49 ? R LI1 1   C49 
397 1 N 1 A LI1 317 ? C50 ? R LI1 1   C50 
398 1 N 1 A LI1 317 ? C51 ? R LI1 1   C51 
399 1 N 1 A LI1 317 ? C59 ? R LI1 1   C59 
400 1 N 1 A LI1 317 ? C60 ? R LI1 1   C60 
401 1 N 1 A LI1 317 ? C11 ? R LI1 1   C11 
402 1 N 1 A LI1 317 ? C12 ? R LI1 1   C12 
403 1 N 1 A LI1 317 ? C13 ? R LI1 1   C13 
404 1 N 1 A LI1 317 ? C14 ? R LI1 1   C14 
405 1 N 1 A LI1 317 ? C15 ? R LI1 1   C15 
406 1 N 1 A LI1 317 ? C16 ? R LI1 1   C16 
407 1 N 1 A LI1 317 ? C17 ? R LI1 1   C17 
408 1 N 1 A LI1 317 ? C18 ? R LI1 1   C18 
409 1 N 1 A LI1 317 ? C19 ? R LI1 1   C19 
410 1 N 1 A LI1 317 ? C20 ? R LI1 1   C20 
411 1 N 1 A LI1 317 ? C21 ? R LI1 1   C21 
412 1 N 1 A LI1 317 ? C22 ? R LI1 1   C22 
413 1 N 1 A LI1 317 ? C23 ? R LI1 1   C23 
414 1 N 1 A LI1 317 ? C24 ? R LI1 1   C24 
415 1 N 1 A LI1 317 ? C25 ? R LI1 1   C25 
416 1 N 1 A LI1 317 ? C26 ? R LI1 1   C26 
417 1 N 1 A LI1 317 ? C27 ? R LI1 1   C27 
418 1 N 1 A LI1 317 ? C28 ? R LI1 1   C28 
419 1 N 1 A LI1 317 ? C29 ? R LI1 1   C29 
420 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                     9F9D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.950 
_cell.length_a_esd                 ? 
_cell.length_b                     62.950 
_cell.length_b_esd                 ? 
_cell.length_c                     111.700 
_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                         9F9D 
_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                   9F9D 
_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             2.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.85 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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                         'PSI JUNGFRAU 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-12-08 
_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   1.02989 
_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                        'SwissFEL ARAMIS BEAMLINE ESA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.02989 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ESA 
_diffrn_source.pdbx_synchrotron_site       'SwissFEL ARAMIS' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F9D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               16.02 
_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                                     30124 
_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                                186 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.20 
_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                                   0.996 
_reflns.pdbx_R_split                                   0.0966 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.7 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.07 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2996 
_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                               123 
_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                                  0.833 
_reflns_shell.pdbx_R_split                                  0.7139 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F9D 
_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                            1.70 
_refine.ls_d_res_low                             16.02 
_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                     27497 
_refine.ls_number_reflns_R_free                  2004 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 7.29 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1405 
_refine.ls_R_factor_R_free                       0.1718 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1381 
_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                          1.36 
_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                 18.32 
_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                            0.17 
_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.pdbx_number_atoms_protein        1795 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         254 
_refine_hist.number_atoms_solvent             51 
_refine_hist.number_atoms_total               2100 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        16.02 
# 
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' ? 0.019  ? 2158 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.524  ? 2872 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.374 ? 456  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.114  ? 314  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.016  ? 340  ? 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' 1.70 1.74  . . 141 1781 100.00 . . . . 0.2483 . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 1.74 1.79  . . 140 1838 100.00 . . . . 0.2106 . . . . . . . . . . . 0.2803 
'X-RAY DIFFRACTION' 1.79 1.84  . . 144 1816 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 1.84 1.90  . . 142 1801 100.00 . . . . 0.1855 . . . . . . . . . . . 0.2239 
'X-RAY DIFFRACTION' 1.90 1.97  . . 143 1827 100.00 . . . . 0.1384 . . . . . . . . . . . 0.1839 
'X-RAY DIFFRACTION' 1.97 2.05  . . 142 1796 100.00 . . . . 0.1310 . . . . . . . . . . . 0.1768 
'X-RAY DIFFRACTION' 2.05 2.14  . . 147 1819 100.00 . . . . 0.1084 . . . . . . . . . . . 0.1516 
'X-RAY DIFFRACTION' 2.14 2.25  . . 148 1837 100.00 . . . . 0.1159 . . . . . . . . . . . 0.1443 
'X-RAY DIFFRACTION' 2.25 2.39  . . 137 1798 100.00 . . . . 0.1080 . . . . . . . . . . . 0.1690 
'X-RAY DIFFRACTION' 2.39 2.58  . . 141 1840 100.00 . . . . 0.1210 . . . . . . . . . . . 0.1525 
'X-RAY DIFFRACTION' 2.58 2.84  . . 142 1831 100.00 . . . . 0.1268 . . . . . . . . . . . 0.1461 
'X-RAY DIFFRACTION' 2.84 3.24  . . 143 1822 100.00 . . . . 0.1430 . . . . . . . . . . . 0.1535 
'X-RAY DIFFRACTION' 3.25 4.07  . . 149 1829 100.00 . . . . 0.1327 . . . . . . . . . . . 0.1629 
'X-RAY DIFFRACTION' 4.08 16.02 . . 145 1858 100.00 . . . . 0.1470 . . . . . . . . . . . 0.1851 
# 
_struct.entry_id                     9F9D 
_struct.title                        'Laser excitation effects on BR: Dark dataset recorded at SwissFEL' 
_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        9F9D 
_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   
;TGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYA
DWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMR
PEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_struct_ref.pdbx_align_begin           18 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F9D 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 231 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02945 
_struct_ref_seq.db_align_beg                  18 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       5 
_struct_ref_seq.pdbx_auth_seq_align_end       234 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9F9D 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P02945 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            4 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3520  ? 
1 MORE         -52   ? 
1 'SSA (A^2)'  12820 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 6   ? GLY A 28  ? GLU A 9   GLY A 31  1 ? 23 
HELX_P HELX_P2 AA2 ASP A 33  ? LEU A 59  ? ASP A 36  LEU A 62  1 ? 27 
HELX_P HELX_P3 AA3 TRP A 77  ? VAL A 98  ? TRP A 80  VAL A 101 1 ? 22 
HELX_P HELX_P4 AA4 ASP A 101 ? THR A 125 ? ASP A 104 THR A 128 1 ? 25 
HELX_P HELX_P5 AA5 VAL A 127 ? GLY A 152 ? VAL A 130 GLY A 155 1 ? 26 
HELX_P HELX_P6 AA6 GLY A 152 ? GLU A 158 ? GLY A 155 GLU A 161 1 ? 7  
HELX_P HELX_P7 AA7 ARG A 161 ? GLY A 189 ? ARG A 164 GLY A 192 1 ? 29 
HELX_P HELX_P8 AA8 PRO A 197 ? SER A 223 ? PRO A 200 SER A 226 1 ? 27 
HELX_P HELX_P9 AA9 ARG A 224 ? PHE A 227 ? ARG A 227 PHE A 230 5 ? 4  
# 
_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               1.348 
_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                   9F9D 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   MET 
_pdbx_validate_close_contact.auth_seq_id_1    32 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.90 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              209 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              209 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              209 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                86.33 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -13.87 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     7 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.119 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 444 ? T HOH . 
2 1 A HOH 449 ? T HOH . 
3 1 A HOH 450 ? T HOH . 
# 
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 23.7508 27.2941 30.3950 0.1875 ? 0.0253  ? -0.0054 ? 0.2204 ? -0.0186 ? 0.3038 ? 2.9055 ? 0.3585  
? -1.5285 ? 4.7688 ? -3.1408 ? 9.0261 ? -0.0875 ? 0.1360  ? -0.1733 ? -0.2297 ? -0.0649 ? -0.3981 ? 0.3928  ? 0.4691  ? 0.1979  ? 
2  'X-RAY DIFFRACTION' ? refined 15.2865 28.0681 41.0101 0.2668 ? 0.0062  ? -0.0287 ? 0.2261 ? 0.0354  ? 0.2696 ? 1.7502 ? -0.2387 
? -0.4343 ? 2.1642 ? 1.0460  ? 4.3828 ? -0.0495 ? -0.2726 ? -0.1006 ? 0.3748  ? 0.0535  ? -0.0475 ? 0.5250  ? -0.1241 ? -0.0074 ? 
3  'X-RAY DIFFRACTION' ? refined 13.0940 40.0019 14.8358 0.5221 ? 0.0314  ? 0.0077  ? 0.4563 ? 0.0172  ? 0.2857 ? 4.9739 ? -0.9752 
? 0.4309  ? 2.1410 ? -1.4255 ? 4.0674 ? 0.0778  ? 0.5483  ? 0.1997  ? -0.8759 ? -0.0953 ? 0.1143  ? -0.3896 ? -0.4822 ? 0.0276  ? 
4  'X-RAY DIFFRACTION' ? refined 12.0654 39.2968 40.6839 0.2086 ? 0.0229  ? -0.0292 ? 0.2088 ? 0.0150  ? 0.2196 ? 2.2587 ? -0.0419 
? 0.1470  ? 2.2271 ? 1.0637  ? 5.3068 ? -0.0355 ? -0.1836 ? -0.0398 ? 0.2122  ? 0.0478  ? 0.0309  ? 0.0324  ? -0.1916 ? -0.0272 ? 
5  'X-RAY DIFFRACTION' ? refined 7.1752  46.6644 34.1745 0.1879 ? 0.0141  ? -0.0297 ? 0.1639 ? 0.0020  ? 0.2259 ? 2.0479 ? 0.1975  
? -1.5322 ? 2.1679 ? -0.3493 ? 2.2639 ? 0.1625  ? -0.0426 ? 0.0780  ? -0.0433 ? 0.1789  ? 0.0235  ? 0.1652  ? -0.0624 ? -0.3309 ? 
6  'X-RAY DIFFRACTION' ? refined 13.2064 53.6215 32.7616 0.2219 ? -0.0215 ? -0.0138 ? 0.1881 ? -0.0146 ? 0.2687 ? 3.0918 ? -0.0286 
? 0.3209  ? 2.8246 ? -1.5627 ? 7.4359 ? 0.0539  ? -0.0483 ? 0.2309  ? 0.2524  ? -0.0478 ? -0.1702 ? -0.5832 ? 0.2785  ? 0.0141  ? 
7  'X-RAY DIFFRACTION' ? refined 21.3783 45.7895 45.9182 0.3593 ? -0.0221 ? -0.0798 ? 0.2933 ? -0.0239 ? 0.2385 ? 1.8138 ? -0.2461 
? 1.0056  ? 1.4916 ? -1.2326 ? 5.1006 ? 0.0016  ? -0.4910 ? 0.0520  ? 0.5915  ? 0.0270  ? -0.2338 ? -0.6706 ? 0.1265  ? -0.0788 ? 
8  'X-RAY DIFFRACTION' ? refined 23.5018 39.7920 29.7715 0.1958 ? -0.0271 ? -0.0246 ? 0.2344 ? 0.0024  ? 0.2889 ? 1.5373 ? -0.3250 
? 0.0877  ? 1.1437 ? -0.4876 ? 3.7734 ? 0.0005  ? 0.0899  ? 0.0979  ? 0.0006  ? 0.0492  ? -0.1984 ? -0.2569 ? 0.1469  ? -0.0263 ? 
9  'X-RAY DIFFRACTION' ? refined 24.4914 31.9009 54.4407 0.5209 ? 0.0396  ? -0.1601 ? 0.5571 ? 0.1163  ? 0.4288 ? 5.4858 ? -2.0798 
? -5.3823 ? 4.4805 ? 2.7188  ? 5.7488 ? -0.4474 ? -0.5747 ? -0.2111 ? 1.0912  ? 0.1153  ? -0.9383 ? 0.6005  ? 0.8855  ? 0.4167  ? 
10 'X-RAY DIFFRACTION' ? refined 19.2382 30.3321 64.8258 0.9920 ? -0.0831 ? -0.1201 ? 0.5582 ? 0.0585  ? 0.3690 ? 4.0153 ? -1.9376 
? 3.5701  ? 0.9648 ? -1.8643 ? 3.8409 ? 0.9800  ? -0.3561 ? -0.5777 ? 1.1096  ? -0.0832 ? 0.0636  ? 0.8041  ? 0.5807  ? -0.9252 ? 
# 
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 5 through 31 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 32 through 62 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 63 through 79 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 80 through 104 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 105 through 130 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 131 through 154 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 155 through 191 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 192 through 224 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 225 through 229 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;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                    9F9D 
_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]   0.015886 
_atom_sites.fract_transf_matrix[1][2]   0.009172 
_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]   0.018343 
_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]   0.008953 
_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    . ALA A 1 1   ? 20.301 25.940 13.609 1.00 96.08  ? 4   ALA A N    1 
ATOM   2    C CA   . ALA A 1 1   ? 20.772 26.316 14.940 1.00 95.45  ? 4   ALA A CA   1 
ATOM   3    C C    . ALA A 1 1   ? 22.156 26.944 14.861 1.00 86.42  ? 4   ALA A C    1 
ATOM   4    O O    . ALA A 1 1   ? 22.339 28.104 15.242 1.00 74.70  ? 4   ALA A O    1 
ATOM   5    C CB   . ALA A 1 1   ? 20.794 25.106 15.882 1.00 82.95  ? 4   ALA A CB   1 
ATOM   6    N N    . THR A 1 2   ? 23.137 26.185 14.363 1.00 66.72  ? 5   THR A N    1 
ATOM   7    C CA   . THR A 1 2   ? 24.472 26.748 14.261 1.00 62.47  ? 5   THR A CA   1 
ATOM   8    C C    . THR A 1 2   ? 24.565 27.813 13.178 1.00 58.69  ? 5   THR A C    1 
ATOM   9    O O    . THR A 1 2   ? 25.610 28.465 13.062 1.00 74.90  ? 5   THR A O    1 
ATOM   10   C CB   . THR A 1 2   ? 25.489 25.638 14.003 1.00 77.78  ? 5   THR A CB   1 
ATOM   11   O OG1  . THR A 1 2   ? 25.079 24.878 12.858 1.00 69.84  ? 5   THR A OG1  1 
ATOM   12   C CG2  . THR A 1 2   ? 25.600 24.730 15.224 1.00 76.13  ? 5   THR A CG2  1 
ATOM   13   H HA   . THR A 1 2   ? 24.709 27.163 15.105 0.00 74.94  ? 5   THR A HA   1 
ATOM   14   H HB   . THR A 1 2   ? 26.365 26.018 13.832 0.00 93.31  ? 5   THR A HB   1 
ATOM   15   H HG1  . THR A 1 2   ? 24.346 24.497 13.014 0.00 83.79  ? 5   THR A HG1  1 
ATOM   16   H HG21 . THR A 1 2   ? 24.738 24.330 15.419 0.00 91.34  ? 5   THR A HG21 1 
ATOM   17   H HG22 . THR A 1 2   ? 26.243 24.024 15.055 0.00 91.34  ? 5   THR A HG22 1 
ATOM   18   H HG23 . THR A 1 2   ? 25.890 25.244 15.994 0.00 91.34  ? 5   THR A HG23 1 
ATOM   19   N N    . GLY A 1 3   ? 23.511 28.006 12.383 1.00 72.69  ? 6   GLY A N    1 
ATOM   20   C CA   . GLY A 1 3   ? 23.530 29.055 11.373 1.00 56.89  ? 6   GLY A CA   1 
ATOM   21   C C    . GLY A 1 3   ? 23.483 30.472 11.936 1.00 64.08  ? 6   GLY A C    1 
ATOM   22   O O    . GLY A 1 3   ? 23.650 31.429 11.174 1.00 65.91  ? 6   GLY A O    1 
ATOM   23   H H    . GLY A 1 3   ? 22.784 27.547 12.411 0.00 87.21  ? 6   GLY A H    1 
ATOM   24   H HA2  . GLY A 1 3   ? 24.342 28.970 10.850 0.00 68.25  ? 6   GLY A HA2  1 
ATOM   25   H HA3  . GLY A 1 3   ? 22.764 28.941 10.789 0.00 68.25  ? 6   GLY A HA3  1 
ATOM   26   N N    . ARG A 1 4   ? 23.228 30.629 13.237 1.00 53.00  ? 7   ARG A N    1 
ATOM   27   C CA   . ARG A 1 4   ? 23.244 31.952 13.867 1.00 48.52  ? 7   ARG A CA   1 
ATOM   28   C C    . ARG A 1 4   ? 24.521 32.127 14.683 1.00 43.40  ? 7   ARG A C    1 
ATOM   29   O O    . ARG A 1 4   ? 24.771 31.324 15.595 1.00 40.93  ? 7   ARG A O    1 
ATOM   30   C CB   . ARG A 1 4   ? 22.021 32.128 14.768 1.00 39.11  ? 7   ARG A CB   1 
ATOM   31   C CG   . ARG A 1 4   ? 20.611 32.231 14.039 1.00 40.79  ? 7   ARG A CG   1 
ATOM   32   C CD   . ARG A 1 4   ? 19.525 32.063 15.139 1.00 47.38  ? 7   ARG A CD   1 
ATOM   33   N NE   . ARG A 1 4   ? 19.489 30.684 15.615 1.00 54.51  ? 7   ARG A NE   1 
ATOM   34   C CZ   . ARG A 1 4   ? 18.860 30.228 16.695 1.00 49.18  ? 7   ARG A CZ   1 
ATOM   35   N NH1  . ARG A 1 4   ? 18.677 30.987 17.788 1.00 31.39  ? 7   ARG A NH1  1 
ATOM   36   N NH2  . ARG A 1 4   ? 18.503 28.941 16.723 1.00 53.54  ? 7   ARG A NH2  1 
ATOM   37   H H    . ARG A 1 4   ? 23.043 29.985 13.777 0.00 63.58  ? 7   ARG A H    1 
ATOM   38   H HA   . ARG A 1 4   ? 23.227 32.633 13.176 0.00 58.21  ? 7   ARG A HA   1 
ATOM   39   H HB2  . ARG A 1 4   ? 21.976 31.367 15.367 0.00 46.91  ? 7   ARG A HB2  1 
ATOM   40   H HB3  . ARG A 1 4   ? 22.137 32.946 15.277 0.00 46.91  ? 7   ARG A HB3  1 
ATOM   41   H HG2  . ARG A 1 4   ? 20.511 33.097 13.614 0.00 48.92  ? 7   ARG A HG2  1 
ATOM   42   H HG3  . ARG A 1 4   ? 20.518 31.525 13.380 0.00 48.92  ? 7   ARG A HG3  1 
ATOM   43   H HD2  . ARG A 1 4   ? 19.729 32.644 15.889 0.00 56.84  ? 7   ARG A HD2  1 
ATOM   44   H HD3  . ARG A 1 4   ? 18.655 32.286 14.774 0.00 56.84  ? 7   ARG A HD3  1 
ATOM   45   H HE   . ARG A 1 4   ? 19.921 30.105 15.149 0.00 65.40  ? 7   ARG A HE   1 
ATOM   46   H HH11 . ARG A 1 4   ? 18.971 31.795 17.804 0.00 37.64  ? 7   ARG A HH11 1 
ATOM   47   H HH12 . ARG A 1 4   ? 18.267 30.665 18.471 0.00 37.64  ? 7   ARG A HH12 1 
ATOM   48   H HH21 . ARG A 1 4   ? 18.680 28.430 16.054 0.00 64.23  ? 7   ARG A HH21 1 
ATOM   49   H HH22 . ARG A 1 4   ? 18.095 28.623 17.410 0.00 64.23  ? 7   ARG A HH22 1 
ATOM   50   N N    . PRO A 1 5   ? 25.323 33.166 14.453 1.00 38.54  ? 8   PRO A N    1 
ATOM   51   C CA   . PRO A 1 5   ? 26.630 33.226 15.143 1.00 38.34  ? 8   PRO A CA   1 
ATOM   52   C C    . PRO A 1 5   ? 26.538 33.347 16.638 1.00 39.46  ? 8   PRO A C    1 
ATOM   53   O O    . PRO A 1 5   ? 27.471 32.928 17.336 1.00 38.29  ? 8   PRO A O    1 
ATOM   54   C CB   . PRO A 1 5   ? 27.315 34.462 14.526 1.00 43.94  ? 8   PRO A CB   1 
ATOM   55   C CG   . PRO A 1 5   ? 26.215 35.241 13.824 1.00 54.99  ? 8   PRO A CG   1 
ATOM   56   C CD   . PRO A 1 5   ? 25.134 34.264 13.477 1.00 37.89  ? 8   PRO A CD   1 
ATOM   57   H HA   . PRO A 1 5   ? 27.140 32.432 14.921 0.00 45.99  ? 8   PRO A HA   1 
ATOM   58   H HB2  . PRO A 1 5   ? 27.720 34.995 15.228 0.00 52.71  ? 8   PRO A HB2  1 
ATOM   59   H HB3  . PRO A 1 5   ? 27.993 34.177 13.892 0.00 52.71  ? 8   PRO A HB3  1 
ATOM   60   H HG2  . PRO A 1 5   ? 25.874 35.925 14.421 0.00 65.97  ? 8   PRO A HG2  1 
ATOM   61   H HG3  . PRO A 1 5   ? 26.572 35.650 13.020 0.00 65.97  ? 8   PRO A HG3  1 
ATOM   62   H HD2  . PRO A 1 5   ? 24.259 34.669 13.581 0.00 45.45  ? 8   PRO A HD2  1 
ATOM   63   H HD3  . PRO A 1 5   ? 25.243 33.939 12.570 0.00 45.45  ? 8   PRO A HD3  1 
ATOM   64   N N    . GLU A 1 6   ? 25.432 33.867 17.177 1.00 31.40  ? 9   GLU A N    1 
ATOM   65   C CA   . GLU A 1 6   ? 25.276 33.941 18.615 1.00 29.16  ? 9   GLU A CA   1 
ATOM   66   C C    . GLU A 1 6   ? 24.912 32.621 19.283 1.00 29.56  ? 9   GLU A C    1 
ATOM   67   O O    . GLU A 1 6   ? 24.782 32.590 20.497 1.00 26.27  ? 9   GLU A O    1 
ATOM   68   C CB   . GLU A 1 6   ? 24.192 35.013 18.953 1.00 33.11  ? 9   GLU A CB   1 
ATOM   69   C CG   . GLU A 1 6   ? 22.706 34.608 18.541 1.00 31.71  ? 9   GLU A CG   1 
ATOM   70   C CD   . GLU A 1 6   ? 22.326 35.025 17.151 1.00 34.90  ? 9   GLU A CD   1 
ATOM   71   O OE1  . GLU A 1 6   ? 23.189 35.345 16.289 1.00 36.32  ? 9   GLU A OE1  1 
ATOM   72   O OE2  . GLU A 1 6   ? 21.118 35.003 16.852 1.00 34.12  ? 9   GLU A OE2  1 
ATOM   73   H H    . GLU A 1 6   ? 24.768 34.179 16.728 0.00 37.66  ? 9   GLU A H    1 
ATOM   74   H HA   . GLU A 1 6   ? 26.126 34.211 18.995 0.00 34.97  ? 9   GLU A HA   1 
ATOM   75   H HB2  . GLU A 1 6   ? 24.198 35.166 19.911 0.00 39.71  ? 9   GLU A HB2  1 
ATOM   76   H HB3  . GLU A 1 6   ? 24.412 35.833 18.484 0.00 39.71  ? 9   GLU A HB3  1 
ATOM   77   H HG2  . GLU A 1 6   ? 22.620 33.643 18.594 0.00 38.04  ? 9   GLU A HG2  1 
ATOM   78   H HG3  . GLU A 1 6   ? 22.086 35.030 19.156 0.00 38.04  ? 9   GLU A HG3  1 
ATOM   79   N N    . TRP A 1 7   ? 24.792 31.507 18.545 1.00 29.58  ? 10  TRP A N    1 
ATOM   80   C CA   . TRP A 1 7   ? 24.309 30.277 19.186 1.00 28.84  ? 10  TRP A CA   1 
ATOM   81   C C    . TRP A 1 7   ? 25.265 29.846 20.300 1.00 30.67  ? 10  TRP A C    1 
ATOM   82   O O    . TRP A 1 7   ? 24.844 29.286 21.304 1.00 29.09  ? 10  TRP A O    1 
ATOM   83   C CB   . TRP A 1 7   ? 24.174 29.167 18.108 1.00 32.26  ? 10  TRP A CB   1 
ATOM   84   C CG   . TRP A 1 7   ? 25.481 28.528 17.739 1.00 41.37  ? 10  TRP A CG   1 
ATOM   85   C CD1  . TRP A 1 7   ? 26.325 28.917 16.728 1.00 44.14  ? 10  TRP A CD1  1 
ATOM   86   C CD2  . TRP A 1 7   ? 26.104 27.390 18.359 1.00 38.48  ? 10  TRP A CD2  1 
ATOM   87   N NE1  . TRP A 1 7   ? 27.436 28.094 16.687 1.00 52.53  ? 10  TRP A NE1  1 
ATOM   88   C CE2  . TRP A 1 7   ? 27.324 27.154 17.674 1.00 44.89  ? 10  TRP A CE2  1 
ATOM   89   C CE3  . TRP A 1 7   ? 25.746 26.544 19.410 1.00 39.70  ? 10  TRP A CE3  1 
ATOM   90   C CZ2  . TRP A 1 7   ? 28.185 26.102 18.013 1.00 58.52  ? 10  TRP A CZ2  1 
ATOM   91   C CZ3  . TRP A 1 7   ? 26.604 25.513 19.763 1.00 52.93  ? 10  TRP A CZ3  1 
ATOM   92   C CH2  . TRP A 1 7   ? 27.813 25.302 19.061 1.00 51.84  ? 10  TRP A CH2  1 
ATOM   93   H H    . TRP A 1 7   ? 24.976 31.440 17.708 0.00 35.47  ? 10  TRP A H    1 
ATOM   94   H HA   . TRP A 1 7   ? 23.435 30.419 19.581 0.00 34.59  ? 10  TRP A HA   1 
ATOM   95   H HB2  . TRP A 1 7   ? 23.589 28.472 18.447 0.00 38.70  ? 10  TRP A HB2  1 
ATOM   96   H HB3  . TRP A 1 7   ? 23.796 29.556 17.304 0.00 38.70  ? 10  TRP A HB3  1 
ATOM   97   H HD1  . TRP A 1 7   ? 26.172 29.632 16.154 0.00 52.94  ? 10  TRP A HD1  1 
ATOM   98   H HE1  . TRP A 1 7   ? 28.089 28.162 16.131 0.00 63.02  ? 10  TRP A HE1  1 
ATOM   99   H HE3  . TRP A 1 7   ? 24.946 26.671 19.866 0.00 47.62  ? 10  TRP A HE3  1 
ATOM   100  H HZ2  . TRP A 1 7   ? 28.976 25.953 17.547 0.00 70.21  ? 10  TRP A HZ2  1 
ATOM   101  H HZ3  . TRP A 1 7   ? 26.381 24.953 20.471 0.00 63.50  ? 10  TRP A HZ3  1 
ATOM   102  H HH2  . TRP A 1 7   ? 28.370 24.603 19.317 0.00 62.19  ? 10  TRP A HH2  1 
ATOM   103  N N    . ILE A 1 8   ? 26.590 30.099 20.136 1.00 29.43  ? 11  ILE A N    1 
ATOM   104  C CA   . ILE A 1 8   ? 27.495 29.550 21.153 1.00 29.09  ? 11  ILE A CA   1 
ATOM   105  C C    . ILE A 1 8   ? 27.215 30.168 22.509 1.00 27.00  ? 11  ILE A C    1 
ATOM   106  O O    . ILE A 1 8   ? 27.308 29.498 23.543 1.00 29.13  ? 11  ILE A O    1 
ATOM   107  C CB   . ILE A 1 8   ? 28.960 29.757 20.723 1.00 36.82  ? 11  ILE A CB   1 
ATOM   108  C CG1  . ILE A 1 8   ? 29.905 29.443 21.878 1.00 42.95  ? 11  ILE A CG1  1 
ATOM   109  C CG2  . ILE A 1 8   ? 29.182 31.224 20.341 1.00 38.13  ? 11  ILE A CG2  1 
ATOM   110  C CD1  . ILE A 1 8   ? 29.775 28.026 22.458 1.00 59.80  ? 11  ILE A CD1  1 
ATOM   111  H H    . ILE A 1 8   ? 26.950 30.547 19.496 0.00 35.29  ? 11  ILE A H    1 
ATOM   112  H HA   . ILE A 1 8   ? 27.334 28.597 21.228 0.00 34.89  ? 11  ILE A HA   1 
ATOM   113  H HB   . ILE A 1 8   ? 29.135 29.166 19.973 0.00 44.16  ? 11  ILE A HB   1 
ATOM   114  H HG12 . ILE A 1 8   ? 30.817 29.546 21.565 0.00 51.52  ? 11  ILE A HG12 1 
ATOM   115  H HG13 . ILE A 1 8   ? 29.728 30.068 22.598 0.00 51.52  ? 11  ILE A HG13 1 
ATOM   116  H HG21 . ILE A 1 8   ? 30.110 31.347 20.084 0.00 45.74  ? 11  ILE A HG21 1 
ATOM   117  H HG22 . ILE A 1 8   ? 28.601 31.449 19.597 0.00 45.74  ? 11  ILE A HG22 1 
ATOM   118  H HG23 . ILE A 1 8   ? 28.973 31.785 21.104 0.00 45.74  ? 11  ILE A HG23 1 
ATOM   119  H HD11 . ILE A 1 8   ? 30.410 27.922 23.184 0.00 71.74  ? 11  ILE A HD11 1 
ATOM   120  H HD12 . ILE A 1 8   ? 28.871 27.901 22.788 0.00 71.74  ? 11  ILE A HD12 1 
ATOM   121  H HD13 . ILE A 1 8   ? 29.963 27.380 21.759 0.00 71.74  ? 11  ILE A HD13 1 
ATOM   122  N N    . TRP A 1 9   ? 26.842 31.469 22.552 1.00 25.94  ? 12  TRP A N    1 
ATOM   123  C CA   . TRP A 1 9   ? 26.556 32.069 23.862 1.00 24.35  ? 12  TRP A CA   1 
ATOM   124  C C    . TRP A 1 9   ? 25.210 31.613 24.434 1.00 26.07  ? 12  TRP A C    1 
ATOM   125  O O    . TRP A 1 9   ? 25.050 31.525 25.659 1.00 24.72  ? 12  TRP A O    1 
ATOM   126  C CB   . TRP A 1 9   ? 26.563 33.627 23.748 1.00 24.95  ? 12  TRP A CB   1 
ATOM   127  C CG   . TRP A 1 9   ? 27.828 34.104 22.995 1.00 27.23  ? 12  TRP A CG   1 
ATOM   128  C CD1  . TRP A 1 9   ? 27.872 34.853 21.833 1.00 28.61  ? 12  TRP A CD1  1 
ATOM   129  C CD2  . TRP A 1 9   ? 29.198 33.846 23.348 1.00 30.61  ? 12  TRP A CD2  1 
ATOM   130  N NE1  . TRP A 1 9   ? 29.197 35.048 21.450 1.00 34.85  ? 12  TRP A NE1  1 
ATOM   131  C CE2  . TRP A 1 9   ? 30.004 34.438 22.363 1.00 35.42  ? 12  TRP A CE2  1 
ATOM   132  C CE3  . TRP A 1 9   ? 29.805 33.153 24.404 1.00 32.97  ? 12  TRP A CE3  1 
ATOM   133  C CZ2  . TRP A 1 9   ? 31.404 34.391 22.403 1.00 39.69  ? 12  TRP A CZ2  1 
ATOM   134  C CZ3  . TRP A 1 9   ? 31.244 33.100 24.387 1.00 32.70  ? 12  TRP A CZ3  1 
ATOM   135  C CH2  . TRP A 1 9   ? 31.965 33.713 23.423 1.00 37.01  ? 12  TRP A CH2  1 
ATOM   136  H H    . TRP A 1 9   ? 26.754 31.990 21.873 0.00 31.11  ? 12  TRP A H    1 
ATOM   137  H HA   . TRP A 1 9   ? 27.255 31.790 24.474 0.00 29.21  ? 12  TRP A HA   1 
ATOM   138  H HB2  . TRP A 1 9   ? 25.780 33.921 23.257 0.00 29.93  ? 12  TRP A HB2  1 
ATOM   139  H HB3  . TRP A 1 9   ? 26.565 34.018 24.636 0.00 29.93  ? 12  TRP A HB3  1 
ATOM   140  H HD1  . TRP A 1 9   ? 27.130 35.177 21.376 0.00 34.31  ? 12  TRP A HD1  1 
ATOM   141  H HE1  . TRP A 1 9   ? 29.462 35.479 20.754 0.00 41.80  ? 12  TRP A HE1  1 
ATOM   142  H HE3  . TRP A 1 9   ? 29.307 32.751 25.078 0.00 39.55  ? 12  TRP A HE3  1 
ATOM   143  H HZ2  . TRP A 1 9   ? 31.923 34.810 21.754 0.00 47.61  ? 12  TRP A HZ2  1 
ATOM   144  H HZ3  . TRP A 1 9   ? 31.688 32.631 25.056 0.00 39.23  ? 12  TRP A HZ3  1 
ATOM   145  H HH2  . TRP A 1 9   ? 32.893 33.665 23.466 0.00 44.40  ? 12  TRP A HH2  1 
ATOM   146  N N    . LEU A 1 10  ? 24.233 31.363 23.577 1.00 24.38  ? 13  LEU A N    1 
ATOM   147  C CA   . LEU A 1 10  ? 22.982 30.774 24.044 1.00 23.34  ? 13  LEU A CA   1 
ATOM   148  C C    . LEU A 1 10  ? 23.177 29.372 24.607 1.00 23.31  ? 13  LEU A C    1 
ATOM   149  O O    . LEU A 1 10  ? 22.526 29.025 25.610 1.00 24.46  ? 13  LEU A O    1 
ATOM   150  C CB   . LEU A 1 10  ? 21.960 30.741 22.863 1.00 22.80  ? 13  LEU A CB   1 
ATOM   151  C CG   . LEU A 1 10  ? 21.552 32.143 22.341 1.00 24.37  ? 13  LEU A CG   1 
ATOM   152  C CD1  . LEU A 1 10  ? 20.655 31.947 21.085 1.00 26.80  ? 13  LEU A CD1  1 
ATOM   153  C CD2  . LEU A 1 10  ? 20.819 32.870 23.452 1.00 25.83  ? 13  LEU A CD2  1 
ATOM   154  H H    . LEU A 1 10  ? 24.264 31.521 22.732 0.00 29.24  ? 13  LEU A H    1 
ATOM   155  H HA   . LEU A 1 10  ? 22.630 31.326 24.760 0.00 27.99  ? 13  LEU A HA   1 
ATOM   156  H HB2  . LEU A 1 10  ? 22.357 30.254 22.124 0.00 27.35  ? 13  LEU A HB2  1 
ATOM   157  H HB3  . LEU A 1 10  ? 21.155 30.291 23.163 0.00 27.35  ? 13  LEU A HB3  1 
ATOM   158  H HG   . LEU A 1 10  ? 22.317 32.681 22.086 0.00 29.23  ? 13  LEU A HG   1 
ATOM   159  H HD11 . LEU A 1 10  ? 20.408 32.818 20.735 0.00 32.14  ? 13  LEU A HD11 1 
ATOM   160  H HD12 . LEU A 1 10  ? 21.152 31.451 20.416 0.00 32.14  ? 13  LEU A HD12 1 
ATOM   161  H HD13 . LEU A 1 10  ? 19.859 31.455 21.339 0.00 32.14  ? 13  LEU A HD13 1 
ATOM   162  H HD21 . LEU A 1 10  ? 20.391 33.659 23.085 0.00 30.98  ? 13  LEU A HD21 1 
ATOM   163  H HD22 . LEU A 1 10  ? 20.150 32.277 23.830 0.00 30.98  ? 13  LEU A HD22 1 
ATOM   164  H HD23 . LEU A 1 10  ? 21.457 33.127 24.136 0.00 30.98  ? 13  LEU A HD23 1 
ATOM   165  N N    . ALA A 1 11  ? 24.088 28.564 23.993 1.00 26.39  ? 14  ALA A N    1 
ATOM   166  C CA   . ALA A 1 11  ? 24.383 27.194 24.451 1.00 23.54  ? 14  ALA A CA   1 
ATOM   167  C C    . ALA A 1 11  ? 25.078 27.245 25.815 1.00 25.75  ? 14  ALA A C    1 
ATOM   168  O O    . ALA A 1 11  ? 24.707 26.504 26.759 1.00 25.34  ? 14  ALA A O    1 
ATOM   169  C CB   . ALA A 1 11  ? 25.230 26.459 23.374 1.00 26.19  ? 14  ALA A CB   1 
ATOM   170  H H    . ALA A 1 11  ? 24.547 28.796 23.303 0.00 31.65  ? 14  ALA A H    1 
ATOM   171  H HA   . ALA A 1 11  ? 23.567 26.681 24.559 0.00 28.23  ? 14  ALA A HA   1 
ATOM   172  H HB1  . ALA A 1 11  ? 25.420 25.559 23.682 0.00 31.41  ? 14  ALA A HB1  1 
ATOM   173  H HB2  . ALA A 1 11  ? 24.728 26.427 22.545 0.00 31.41  ? 14  ALA A HB2  1 
ATOM   174  H HB3  . ALA A 1 11  ? 26.060 26.944 23.240 0.00 31.41  ? 14  ALA A HB3  1 
ATOM   175  N N    A LEU A 1 12  ? 26.081 28.124 25.941 0.58 29.16  ? 15  LEU A N    1 
ATOM   176  N N    B LEU A 1 12  ? 26.083 28.123 25.960 0.42 29.10  ? 15  LEU A N    1 
ATOM   177  C CA   A LEU A 1 12  ? 26.771 28.297 27.206 0.58 27.22  ? 15  LEU A CA   1 
ATOM   178  C CA   B LEU A 1 12  ? 26.746 28.256 27.252 0.42 27.20  ? 15  LEU A CA   1 
ATOM   179  C C    A LEU A 1 12  ? 25.833 28.803 28.293 0.58 28.10  ? 15  LEU A C    1 
ATOM   180  C C    B LEU A 1 12  ? 25.800 28.789 28.315 0.42 28.12  ? 15  LEU A C    1 
ATOM   181  O O    A LEU A 1 12  ? 25.872 28.303 29.416 0.58 26.94  ? 15  LEU A O    1 
ATOM   182  O O    B LEU A 1 12  ? 25.819 28.314 29.451 0.42 26.98  ? 15  LEU A O    1 
ATOM   183  C CB   A LEU A 1 12  ? 27.979 29.249 27.022 0.58 26.89  ? 15  LEU A CB   1 
ATOM   184  C CB   B LEU A 1 12  ? 27.994 29.155 27.162 0.42 27.16  ? 15  LEU A CB   1 
ATOM   185  C CG   A LEU A 1 12  ? 28.940 29.389 28.198 0.58 34.39  ? 15  LEU A CG   1 
ATOM   186  C CG   B LEU A 1 12  ? 29.169 28.553 26.404 0.42 29.57  ? 15  LEU A CG   1 
ATOM   187  C CD1  A LEU A 1 12  ? 29.477 28.037 28.741 0.58 37.06  ? 15  LEU A CD1  1 
ATOM   188  C CD1  B LEU A 1 12  ? 30.138 29.659 26.014 0.42 31.59  ? 15  LEU A CD1  1 
ATOM   189  C CD2  A LEU A 1 12  ? 30.119 30.241 27.706 0.58 36.37  ? 15  LEU A CD2  1 
ATOM   190  C CD2  B LEU A 1 12  ? 29.895 27.506 27.202 0.42 36.36  ? 15  LEU A CD2  1 
ATOM   191  H H    A LEU A 1 12  ? 26.375 28.626 25.307 0.58 34.97  ? 15  LEU A H    1 
ATOM   192  H H    B LEU A 1 12  ? 26.388 28.636 25.341 0.42 34.90  ? 15  LEU A H    1 
ATOM   193  H HA   A LEU A 1 12  ? 27.112 27.437 27.498 0.58 32.65  ? 15  LEU A HA   1 
ATOM   194  H HA   B LEU A 1 12  ? 27.042 27.370 27.513 0.42 32.62  ? 15  LEU A HA   1 
ATOM   195  H HB2  A LEU A 1 12  ? 28.499 28.928 26.269 0.58 32.25  ? 15  LEU A HB2  1 
ATOM   196  H HB2  B LEU A 1 12  ? 27.747 29.977 26.710 0.42 32.57  ? 15  LEU A HB2  1 
ATOM   197  H HB3  A LEU A 1 12  ? 27.633 30.135 26.833 0.58 32.25  ? 15  LEU A HB3  1 
ATOM   198  H HB3  B LEU A 1 12  ? 28.297 29.350 28.063 0.42 32.57  ? 15  LEU A HB3  1 
ATOM   199  H HG   A LEU A 1 12  ? 28.467 29.794 28.942 0.58 41.25  ? 15  LEU A HG   1 
ATOM   200  H HG   B LEU A 1 12  ? 28.822 28.114 25.612 0.42 35.47  ? 15  LEU A HG   1 
ATOM   201  H HD11 A LEU A 1 12  ? 30.152 28.214 29.415 0.58 44.46  ? 15  LEU A HD11 1 
ATOM   202  H HD11 B LEU A 1 12  ? 30.847 29.281 25.471 0.42 37.89  ? 15  LEU A HD11 1 
ATOM   203  H HD12 A LEU A 1 12  ? 28.742 27.539 29.130 0.58 44.46  ? 15  LEU A HD12 1 
ATOM   204  H HD12 B LEU A 1 12  ? 29.659 30.335 25.509 0.42 37.89  ? 15  LEU A HD12 1 
ATOM   205  H HD13 A LEU A 1 12  ? 29.866 27.535 28.008 0.58 44.46  ? 15  LEU A HD13 1 
ATOM   206  H HD13 B LEU A 1 12  ? 30.511 30.051 26.819 0.42 37.89  ? 15  LEU A HD13 1 
ATOM   207  H HD21 A LEU A 1 12  ? 30.671 30.485 28.465 0.58 43.62  ? 15  LEU A HD21 1 
ATOM   208  H HD21 B LEU A 1 12  ? 30.625 27.154 26.669 0.42 43.61  ? 15  LEU A HD21 1 
ATOM   209  H HD22 A LEU A 1 12  ? 30.639 29.724 27.071 0.58 43.62  ? 15  LEU A HD22 1 
ATOM   210  H HD22 B LEU A 1 12  ? 30.241 27.911 28.012 0.42 43.61  ? 15  LEU A HD22 1 
ATOM   211  H HD23 A LEU A 1 12  ? 29.774 31.040 27.277 0.58 43.62  ? 15  LEU A HD23 1 
ATOM   212  H HD23 B LEU A 1 12  ? 29.275 26.794 27.426 0.42 43.61  ? 15  LEU A HD23 1 
ATOM   213  N N    . GLY A 1 13  ? 24.941 29.762 27.975 1.00 24.27  ? 16  GLY A N    1 
ATOM   214  C CA   . GLY A 1 13  ? 23.961 30.238 28.960 1.00 23.98  ? 16  GLY A CA   1 
ATOM   215  C C    . GLY A 1 13  ? 23.005 29.132 29.432 1.00 25.28  ? 16  GLY A C    1 
ATOM   216  O O    . GLY A 1 13  ? 22.727 28.987 30.627 1.00 25.53  ? 16  GLY A O    1 
ATOM   217  H H    . GLY A 1 13  ? 24.890 30.143 27.206 0.00 29.10  ? 16  GLY A H    1 
ATOM   218  H HA2  . GLY A 1 13  ? 24.431 30.585 29.734 0.00 28.75  ? 16  GLY A HA2  1 
ATOM   219  H HA3  . GLY A 1 13  ? 23.432 30.949 28.566 0.00 28.75  ? 16  GLY A HA3  1 
ATOM   220  N N    . THR A 1 14  ? 22.527 28.325 28.493 1.00 23.03  ? 17  THR A N    1 
ATOM   221  C CA   . THR A 1 14  ? 21.661 27.196 28.863 1.00 25.65  ? 17  THR A CA   1 
ATOM   222  C C    . THR A 1 14  ? 22.414 26.263 29.815 1.00 25.79  ? 17  THR A C    1 
ATOM   223  O O    . THR A 1 14  ? 21.858 25.804 30.824 1.00 25.67  ? 17  THR A O    1 
ATOM   224  C CB   . THR A 1 14  ? 21.266 26.437 27.583 1.00 24.22  ? 17  THR A CB   1 
ATOM   225  O OG1  . THR A 1 14  ? 20.575 27.312 26.662 1.00 24.48  ? 17  THR A OG1  1 
ATOM   226  C CG2  . THR A 1 14  ? 20.282 25.265 27.918 1.00 27.98  ? 17  THR A CG2  1 
ATOM   227  H H    . THR A 1 14  ? 22.682 28.402 27.651 0.00 27.61  ? 17  THR A H    1 
ATOM   228  H HA   . THR A 1 14  ? 20.856 27.515 29.300 0.00 30.76  ? 17  THR A HA   1 
ATOM   229  H HB   . THR A 1 14  ? 22.078 26.092 27.179 0.00 29.05  ? 17  THR A HB   1 
ATOM   230  H HG1  . THR A 1 14  ? 21.066 27.964 26.463 0.00 29.36  ? 17  THR A HG1  1 
ATOM   231  H HG21 . THR A 1 14  ? 19.907 24.902 27.100 0.00 33.56  ? 17  THR A HG21 1 
ATOM   232  H HG22 . THR A 1 14  ? 20.753 24.560 28.388 0.00 33.56  ? 17  THR A HG22 1 
ATOM   233  H HG23 . THR A 1 14  ? 19.559 25.589 28.478 0.00 33.56  ? 17  THR A HG23 1 
ATOM   234  N N    . ALA A 1 15  ? 23.657 25.929 29.469 1.00 24.26  ? 18  ALA A N    1 
ATOM   235  C CA   . ALA A 1 15  ? 24.408 24.965 30.288 1.00 24.53  ? 18  ALA A CA   1 
ATOM   236  C C    . ALA A 1 15  ? 24.621 25.516 31.707 1.00 27.47  ? 18  ALA A C    1 
ATOM   237  O O    . ALA A 1 15  ? 24.449 24.796 32.704 1.00 30.14  ? 18  ALA A O    1 
ATOM   238  C CB   . ALA A 1 15  ? 25.778 24.656 29.611 1.00 28.15  ? 18  ALA A CB   1 
ATOM   239  H H    . ALA A 1 15  ? 24.081 26.234 28.786 0.00 29.10  ? 18  ALA A H    1 
ATOM   240  H HA   . ALA A 1 15  ? 23.906 24.137 30.351 0.00 29.41  ? 18  ALA A HA   1 
ATOM   241  H HB1  . ALA A 1 15  ? 26.269 24.029 30.164 0.00 33.76  ? 18  ALA A HB1  1 
ATOM   242  H HB2  . ALA A 1 15  ? 25.618 24.271 28.735 0.00 33.76  ? 18  ALA A HB2  1 
ATOM   243  H HB3  . ALA A 1 15  ? 26.280 25.482 29.523 0.00 33.76  ? 18  ALA A HB3  1 
ATOM   244  N N    . LEU A 1 16  ? 25.039 26.787 31.817 1.00 24.58  ? 19  LEU A N    1 
ATOM   245  C CA   . LEU A 1 16  ? 25.345 27.347 33.135 1.00 24.56  ? 19  LEU A CA   1 
ATOM   246  C C    . LEU A 1 16  ? 24.069 27.519 33.983 1.00 27.09  ? 19  LEU A C    1 
ATOM   247  O O    . LEU A 1 16  ? 24.115 27.295 35.200 1.00 25.73  ? 19  LEU A O    1 
ATOM   248  C CB   . LEU A 1 16  ? 26.097 28.682 33.003 1.00 26.67  ? 19  LEU A CB   1 
ATOM   249  C CG   . LEU A 1 16  ? 27.538 28.638 32.388 1.00 26.40  ? 19  LEU A CG   1 
ATOM   250  C CD1  . LEU A 1 16  ? 28.084 30.039 32.094 1.00 30.69  ? 19  LEU A CD1  1 
ATOM   251  C CD2  . LEU A 1 16  ? 28.450 27.849 33.302 1.00 38.46  ? 19  LEU A CD2  1 
ATOM   252  H H    . LEU A 1 16  ? 25.150 27.329 31.159 0.00 29.48  ? 19  LEU A H    1 
ATOM   253  H HA   . LEU A 1 16  ? 25.933 26.729 33.597 0.00 29.46  ? 19  LEU A HA   1 
ATOM   254  H HB2  . LEU A 1 16  ? 25.567 29.267 32.439 0.00 31.98  ? 19  LEU A HB2  1 
ATOM   255  H HB3  . LEU A 1 16  ? 26.181 29.064 33.891 0.00 31.98  ? 19  LEU A HB3  1 
ATOM   256  H HG   . LEU A 1 16  ? 27.505 28.190 31.528 0.00 31.67  ? 19  LEU A HG   1 
ATOM   257  H HD11 . LEU A 1 16  ? 28.979 29.959 31.729 0.00 36.81  ? 19  LEU A HD11 1 
ATOM   258  H HD12 . LEU A 1 16  ? 27.503 30.476 31.453 0.00 36.81  ? 19  LEU A HD12 1 
ATOM   259  H HD13 . LEU A 1 16  ? 28.108 30.548 32.920 0.00 36.81  ? 19  LEU A HD13 1 
ATOM   260  H HD21 . LEU A 1 16  ? 29.349 27.859 32.936 0.00 46.14  ? 19  LEU A HD21 1 
ATOM   261  H HD22 . LEU A 1 16  ? 28.447 28.258 34.181 0.00 46.14  ? 19  LEU A HD22 1 
ATOM   262  H HD23 . LEU A 1 16  ? 28.127 26.937 33.360 0.00 46.14  ? 19  LEU A HD23 1 
ATOM   263  N N    . MET A 1 17  ? 22.925 27.890 33.372 1.00 24.42  ? 20  MET A N    1 
ATOM   264  C CA   . MET A 1 17  ? 21.673 28.002 34.175 1.00 23.76  ? 20  MET A CA   1 
ATOM   265  C C    . MET A 1 17  ? 21.215 26.598 34.618 1.00 24.11  ? 20  MET A C    1 
ATOM   266  O O    . MET A 1 17  ? 20.708 26.436 35.742 1.00 25.28  ? 20  MET A O    1 
ATOM   267  C CB   . MET A 1 17  ? 20.469 28.697 33.412 1.00 22.58  ? 20  MET A CB   1 
ATOM   268  C CG   . MET A 1 17  ? 20.977 30.135 32.962 1.00 21.33  ? 20  MET A CG   1 
ATOM   269  S SD   . MET A 1 17  ? 20.987 31.175 34.448 1.00 24.74  ? 20  MET A SD   1 
ATOM   270  C CE   . MET A 1 17  ? 21.027 32.764 33.495 1.00 24.69  ? 20  MET A CE   1 
ATOM   271  H H    . MET A 1 17  ? 22.844 28.075 32.536 0.00 29.28  ? 20  MET A H    1 
ATOM   272  H HA   . MET A 1 17  ? 21.886 28.583 34.922 0.00 28.49  ? 20  MET A HA   1 
ATOM   273  H HB2  . MET A 1 17  ? 20.222 28.181 32.629 0.00 27.08  ? 20  MET A HB2  1 
ATOM   274  H HB3  . MET A 1 17  ? 19.705 28.793 34.001 0.00 27.08  ? 20  MET A HB3  1 
ATOM   275  H HG2  . MET A 1 17  ? 21.874 30.079 32.598 0.00 25.57  ? 20  MET A HG2  1 
ATOM   276  H HG3  . MET A 1 17  ? 20.375 30.516 32.303 0.00 25.57  ? 20  MET A HG3  1 
ATOM   277  H HE1  . MET A 1 17  ? 21.042 33.506 34.118 0.00 29.61  ? 20  MET A HE1  1 
ATOM   278  H HE2  . MET A 1 17  ? 21.824 32.780 32.942 0.00 29.61  ? 20  MET A HE2  1 
ATOM   279  H HE3  . MET A 1 17  ? 20.236 32.817 32.936 0.00 29.61  ? 20  MET A HE3  1 
ATOM   280  N N    . GLY A 1 18  ? 21.400 25.626 33.760 1.00 25.13  ? 21  GLY A N    1 
ATOM   281  C CA   . GLY A 1 18  ? 21.016 24.255 34.107 1.00 28.34  ? 21  GLY A CA   1 
ATOM   282  C C    . GLY A 1 18  ? 21.857 23.741 35.271 1.00 27.21  ? 21  GLY A C    1 
ATOM   283  O O    . GLY A 1 18  ? 21.319 23.132 36.211 1.00 29.04  ? 21  GLY A O    1 
ATOM   284  H H    . GLY A 1 18  ? 21.741 25.717 32.976 0.00 30.14  ? 21  GLY A H    1 
ATOM   285  H HA2  . GLY A 1 18  ? 20.081 24.231 34.361 0.00 33.99  ? 21  GLY A HA2  1 
ATOM   286  H HA3  . GLY A 1 18  ? 21.151 23.673 33.342 0.00 33.99  ? 21  GLY A HA3  1 
ATOM   287  N N    . LEU A 1 19  ? 23.184 23.880 35.167 1.00 29.92  ? 22  LEU A N    1 
ATOM   288  C CA   . LEU A 1 19  ? 24.089 23.459 36.241 1.00 30.20  ? 22  LEU A CA   1 
ATOM   289  C C    . LEU A 1 19  ? 23.815 24.230 37.533 1.00 29.74  ? 22  LEU A C    1 
ATOM   290  O O    . LEU A 1 19  ? 23.848 23.649 38.621 1.00 30.08  ? 22  LEU A O    1 
ATOM   291  C CB   . LEU A 1 19  ? 25.544 23.659 35.798 1.00 32.04  ? 22  LEU A CB   1 
ATOM   292  C CG   . LEU A 1 19  ? 26.038 22.689 34.749 1.00 44.19  ? 22  LEU A CG   1 
ATOM   293  C CD1  . LEU A 1 19  ? 27.432 23.180 34.338 1.00 48.57  ? 22  LEU A CD1  1 
ATOM   294  C CD2  . LEU A 1 19  ? 26.049 21.222 35.256 1.00 55.38  ? 22  LEU A CD2  1 
ATOM   295  H H    . LEU A 1 19  ? 23.586 24.214 34.484 1.00 35.89  ? 22  LEU A H    1 
ATOM   296  H HA   . LEU A 1 19  ? 23.948 22.516 36.420 1.00 36.23  ? 22  LEU A HA   1 
ATOM   297  H HB2  . LEU A 1 19  ? 25.631 24.553 35.431 1.00 38.43  ? 22  LEU A HB2  1 
ATOM   298  H HB3  . LEU A 1 19  ? 26.116 23.562 36.575 1.00 38.43  ? 22  LEU A HB3  1 
ATOM   299  H HG   . LEU A 1 19  ? 25.446 22.666 33.981 1.00 53.01  ? 22  LEU A HG   1 
ATOM   300  H HD11 . LEU A 1 19  ? 27.788 22.587 33.658 1.00 58.26  ? 22  LEU A HD11 1 
ATOM   301  H HD12 . LEU A 1 19  ? 27.359 24.081 33.986 1.00 58.26  ? 22  LEU A HD12 1 
ATOM   302  H HD13 . LEU A 1 19  ? 28.011 23.175 35.117 1.00 58.26  ? 22  LEU A HD13 1 
ATOM   303  H HD21 . LEU A 1 19  ? 26.396 20.648 34.554 1.00 66.43  ? 22  LEU A HD21 1 
ATOM   304  H HD22 . LEU A 1 19  ? 26.615 21.163 36.041 1.00 66.43  ? 22  LEU A HD22 1 
ATOM   305  H HD23 . LEU A 1 19  ? 25.143 20.958 35.480 1.00 66.43  ? 22  LEU A HD23 1 
ATOM   306  N N    . GLY A 1 20  ? 23.574 25.554 37.439 1.00 27.05  ? 23  GLY A N    1 
ATOM   307  C CA   . GLY A 1 20  ? 23.185 26.326 38.611 1.00 28.48  ? 23  GLY A CA   1 
ATOM   308  C C    . GLY A 1 20  ? 21.923 25.797 39.286 1.00 29.33  ? 23  GLY A C    1 
ATOM   309  O O    . GLY A 1 20  ? 21.906 25.638 40.506 1.00 27.11  ? 23  GLY A O    1 
ATOM   310  H H    . GLY A 1 20  ? 23.631 26.013 36.714 0.00 32.45  ? 23  GLY A H    1 
ATOM   311  H HA2  . GLY A 1 20  ? 23.906 26.306 39.260 0.00 34.16  ? 23  GLY A HA2  1 
ATOM   312  H HA3  . GLY A 1 20  ? 23.023 27.246 38.347 0.00 34.16  ? 23  GLY A HA3  1 
ATOM   313  N N    . THR A 1 21  ? 20.901 25.437 38.494 1.00 25.91  ? 24  THR A N    1 
ATOM   314  C CA   . THR A 1 21  ? 19.650 24.914 39.056 1.00 25.49  ? 24  THR A CA   1 
ATOM   315  C C    . THR A 1 21  ? 19.912 23.617 39.818 1.00 29.04  ? 24  THR A C    1 
ATOM   316  O O    . THR A 1 21  ? 19.399 23.406 40.920 1.00 27.06  ? 24  THR A O    1 
ATOM   317  C CB   . THR A 1 21  ? 18.637 24.624 37.919 1.00 26.03  ? 24  THR A CB   1 
ATOM   318  O OG1  . THR A 1 21  ? 18.338 25.857 37.215 1.00 25.24  ? 24  THR A OG1  1 
ATOM   319  C CG2  . THR A 1 21  ? 17.312 24.090 38.495 1.00 26.69  ? 24  THR A CG2  1 
ATOM   320  H H    . THR A 1 21  ? 20.908 25.485 37.635 0.00 31.07  ? 24  THR A H    1 
ATOM   321  H HA   . THR A 1 21  ? 19.278 25.581 39.655 0.00 30.57  ? 24  THR A HA   1 
ATOM   322  H HB   . THR A 1 21  ? 19.019 23.965 37.318 0.00 31.22  ? 24  THR A HB   1 
ATOM   323  H HG1  . THR A 1 21  ? 19.044 26.190 36.906 0.00 30.27  ? 24  THR A HG1  1 
ATOM   324  H HG21 . THR A 1 21  ? 16.626 24.094 37.809 0.00 32.01  ? 24  THR A HG21 1 
ATOM   325  H HG22 . THR A 1 21  ? 17.431 23.182 38.816 0.00 32.01  ? 24  THR A HG22 1 
ATOM   326  H HG23 . THR A 1 21  ? 17.022 24.648 39.233 0.00 32.01  ? 24  THR A HG23 1 
ATOM   327  N N    . LEU A 1 22  ? 20.669 22.721 39.207 1.00 27.66  ? 25  LEU A N    1 
ATOM   328  C CA   . LEU A 1 22  ? 20.935 21.430 39.861 1.00 29.80  ? 25  LEU A CA   1 
ATOM   329  C C    . LEU A 1 22  ? 21.732 21.601 41.153 1.00 30.07  ? 25  LEU A C    1 
ATOM   330  O O    . LEU A 1 22  ? 21.490 20.882 42.138 1.00 30.95  ? 25  LEU A O    1 
ATOM   331  C CB   . LEU A 1 22  ? 21.692 20.531 38.880 1.00 31.53  ? 25  LEU A CB   1 
ATOM   332  C CG   . LEU A 1 22  ? 20.861 20.057 37.679 1.00 46.65  ? 25  LEU A CG   1 
ATOM   333  C CD1  . LEU A 1 22  ? 21.761 19.313 36.692 1.00 48.26  ? 25  LEU A CD1  1 
ATOM   334  C CD2  . LEU A 1 22  ? 19.685 19.167 38.103 1.00 47.56  ? 25  LEU A CD2  1 
ATOM   335  H H    . LEU A 1 22  ? 21.036 22.823 38.436 0.00 33.17  ? 25  LEU A H    1 
ATOM   336  H HA   . LEU A 1 22  ? 20.093 21.011 40.096 0.00 35.74  ? 25  LEU A HA   1 
ATOM   337  H HB2  . LEU A 1 22  ? 22.453 21.024 38.534 0.00 37.82  ? 25  LEU A HB2  1 
ATOM   338  H HB3  . LEU A 1 22  ? 21.997 19.743 39.356 0.00 37.82  ? 25  LEU A HB3  1 
ATOM   339  H HG   . LEU A 1 22  ? 20.480 20.836 37.244 0.00 55.96  ? 25  LEU A HG   1 
ATOM   340  H HD11 . LEU A 1 22  ? 21.207 18.874 36.028 0.00 57.89  ? 25  LEU A HD11 1 
ATOM   341  H HD12 . LEU A 1 22  ? 22.352 19.950 36.261 0.00 57.89  ? 25  LEU A HD12 1 
ATOM   342  H HD13 . LEU A 1 22  ? 22.283 18.653 37.176 0.00 57.89  ? 25  LEU A HD13 1 
ATOM   343  H HD21 . LEU A 1 22  ? 19.249 18.820 37.309 0.00 57.06  ? 25  LEU A HD21 1 
ATOM   344  H HD22 . LEU A 1 22  ? 20.022 18.434 38.642 0.00 57.06  ? 25  LEU A HD22 1 
ATOM   345  H HD23 . LEU A 1 22  ? 19.059 19.697 38.620 0.00 57.06  ? 25  LEU A HD23 1 
ATOM   346  N N    . TYR A 1 23  ? 22.704 22.514 41.164 1.00 26.40  ? 26  TYR A N    1 
ATOM   347  C CA   . TYR A 1 23  ? 23.516 22.682 42.373 1.00 31.78  ? 26  TYR A CA   1 
ATOM   348  C C    . TYR A 1 23  ? 22.636 23.182 43.521 1.00 28.57  ? 26  TYR A C    1 
ATOM   349  O O    . TYR A 1 23  ? 22.680 22.651 44.622 1.00 30.94  ? 26  TYR A O    1 
ATOM   350  C CB   . TYR A 1 23  ? 24.666 23.644 42.081 1.00 28.12  ? 26  TYR A CB   1 
ATOM   351  C CG   . TYR A 1 23  ? 25.504 23.949 43.295 1.00 33.24  ? 26  TYR A CG   1 
ATOM   352  C CD1  . TYR A 1 23  ? 26.328 22.975 43.858 1.00 49.07  ? 26  TYR A CD1  1 
ATOM   353  C CD2  . TYR A 1 23  ? 25.445 25.201 43.902 1.00 35.87  ? 26  TYR A CD2  1 
ATOM   354  C CE1  . TYR A 1 23  ? 27.096 23.235 45.001 1.00 46.72  ? 26  TYR A CE1  1 
ATOM   355  C CE2  . TYR A 1 23  ? 26.251 25.460 45.100 1.00 38.57  ? 26  TYR A CE2  1 
ATOM   356  C CZ   . TYR A 1 23  ? 27.051 24.485 45.594 1.00 47.67  ? 26  TYR A CZ   1 
ATOM   357  O OH   . TYR A 1 23  ? 27.800 24.760 46.730 1.00 58.38  ? 26  TYR A OH   1 
ATOM   358  H H    . TYR A 1 23  ? 22.910 23.031 40.508 0.00 31.66  ? 26  TYR A H    1 
ATOM   359  H HA   . TYR A 1 23  ? 23.908 21.836 42.642 0.00 38.11  ? 26  TYR A HA   1 
ATOM   360  H HB2  . TYR A 1 23  ? 25.245 23.247 41.411 0.00 33.72  ? 26  TYR A HB2  1 
ATOM   361  H HB3  . TYR A 1 23  ? 24.301 24.480 41.752 0.00 33.72  ? 26  TYR A HB3  1 
ATOM   362  H HD1  . TYR A 1 23  ? 26.368 22.133 43.466 0.00 58.86  ? 26  TYR A HD1  1 
ATOM   363  H HD2  . TYR A 1 23  ? 24.899 25.867 43.551 0.00 43.02  ? 26  TYR A HD2  1 
ATOM   364  H HE1  . TYR A 1 23  ? 27.636 22.569 45.361 0.00 56.04  ? 26  TYR A HE1  1 
ATOM   365  H HE2  . TYR A 1 23  ? 26.213 26.290 45.518 0.00 46.27  ? 26  TYR A HE2  1 
ATOM   366  H HH   . TYR A 1 23  ? 27.654 25.546 46.987 0.00 70.04  ? 26  TYR A HH   1 
ATOM   367  N N    . PHE A 1 24  ? 21.796 24.217 43.252 1.00 27.87  ? 27  PHE A N    1 
ATOM   368  C CA   . PHE A 1 24  ? 20.960 24.771 44.325 1.00 29.36  ? 27  PHE A CA   1 
ATOM   369  C C    . PHE A 1 24  ? 19.931 23.737 44.786 1.00 29.51  ? 27  PHE A C    1 
ATOM   370  O O    . PHE A 1 24  ? 19.573 23.682 45.977 1.00 32.50  ? 27  PHE A O    1 
ATOM   371  C CB   . PHE A 1 24  ? 20.229 26.041 43.840 1.00 26.54  ? 27  PHE A CB   1 
ATOM   372  C CG   . PHE A 1 24  ? 21.139 27.241 43.542 1.00 25.17  ? 27  PHE A CG   1 
ATOM   373  C CD1  . PHE A 1 24  ? 22.386 27.377 44.149 1.00 28.77  ? 27  PHE A CD1  1 
ATOM   374  C CD2  . PHE A 1 24  ? 20.724 28.219 42.650 1.00 26.03  ? 27  PHE A CD2  1 
ATOM   375  C CE1  . PHE A 1 24  ? 23.208 28.482 43.874 1.00 34.39  ? 27  PHE A CE1  1 
ATOM   376  C CE2  . PHE A 1 24  ? 21.538 29.357 42.377 1.00 28.88  ? 27  PHE A CE2  1 
ATOM   377  C CZ   . PHE A 1 24  ? 22.805 29.464 42.960 1.00 31.33  ? 27  PHE A CZ   1 
ATOM   378  H H    . PHE A 1 24  ? 21.702 24.594 42.485 0.00 33.43  ? 27  PHE A H    1 
ATOM   379  H HA   . PHE A 1 24  ? 21.532 25.016 45.070 0.00 35.21  ? 27  PHE A HA   1 
ATOM   380  H HB2  . PHE A 1 24  ? 19.753 25.827 43.022 0.00 31.83  ? 27  PHE A HB2  1 
ATOM   381  H HB3  . PHE A 1 24  ? 19.601 26.315 44.527 0.00 31.83  ? 27  PHE A HB3  1 
ATOM   382  H HD1  . PHE A 1 24  ? 22.678 26.726 44.745 0.00 34.51  ? 27  PHE A HD1  1 
ATOM   383  H HD2  . PHE A 1 24  ? 19.902 28.131 42.224 0.00 31.22  ? 27  PHE A HD2  1 
ATOM   384  H HE1  . PHE A 1 24  ? 24.029 28.564 44.304 0.00 41.25  ? 27  PHE A HE1  1 
ATOM   385  H HE2  . PHE A 1 24  ? 21.228 30.027 41.812 0.00 34.63  ? 27  PHE A HE2  1 
ATOM   386  H HZ   . PHE A 1 24  ? 23.368 30.172 42.745 0.00 37.58  ? 27  PHE A HZ   1 
ATOM   387  N N    . LEU A 1 25  ? 19.403 22.934 43.846 1.00 29.36  ? 28  LEU A N    1 
ATOM   388  C CA   . LEU A 1 25  ? 18.441 21.905 44.225 1.00 33.05  ? 28  LEU A CA   1 
ATOM   389  C C    . LEU A 1 25  ? 19.075 20.849 45.133 1.00 38.93  ? 28  LEU A C    1 
ATOM   390  O O    . LEU A 1 25  ? 18.510 20.458 46.170 1.00 39.63  ? 28  LEU A O    1 
ATOM   391  C CB   . LEU A 1 25  ? 17.881 21.288 42.953 1.00 37.34  ? 28  LEU A CB   1 
ATOM   392  C CG   . LEU A 1 25  ? 16.755 20.316 43.224 1.00 55.45  ? 28  LEU A CG   1 
ATOM   393  C CD1  . LEU A 1 25  ? 15.463 21.102 43.023 1.00 48.13  ? 28  LEU A CD1  1 
ATOM   394  C CD2  . LEU A 1 25  ? 16.843 19.155 42.283 1.00 65.76  ? 28  LEU A CD2  1 
ATOM   395  H H    . LEU A 1 25  ? 19.584 22.970 43.006 0.00 35.21  ? 28  LEU A H    1 
ATOM   396  H HA   . LEU A 1 25  ? 17.711 22.296 44.730 0.00 39.64  ? 28  LEU A HA   1 
ATOM   397  H HB2  . LEU A 1 25  ? 17.538 21.995 42.384 0.00 44.79  ? 28  LEU A HB2  1 
ATOM   398  H HB3  . LEU A 1 25  ? 18.590 20.809 42.496 0.00 44.79  ? 28  LEU A HB3  1 
ATOM   399  H HG   . LEU A 1 25  ? 16.789 19.945 44.120 0.00 66.52  ? 28  LEU A HG   1 
ATOM   400  H HD11 . LEU A 1 25  ? 14.708 20.517 43.189 0.00 57.73  ? 28  LEU A HD11 1 
ATOM   401  H HD12 . LEU A 1 25  ? 15.447 21.847 43.644 0.00 57.73  ? 28  LEU A HD12 1 
ATOM   402  H HD13 . LEU A 1 25  ? 15.433 21.432 42.111 0.00 57.73  ? 28  LEU A HD13 1 
ATOM   403  H HD21 . LEU A 1 25  ? 16.115 18.542 42.468 0.00 78.89  ? 28  LEU A HD21 1 
ATOM   404  H HD22 . LEU A 1 25  ? 16.777 19.481 41.372 0.00 78.89  ? 28  LEU A HD22 1 
ATOM   405  H HD23 . LEU A 1 25  ? 17.694 18.707 42.413 0.00 78.89  ? 28  LEU A HD23 1 
ATOM   406  N N    . VAL A 1 26  ? 20.273 20.390 44.807 1.00 33.40  ? 29  VAL A N    1 
ATOM   407  C CA   . VAL A 1 26  ? 20.886 19.390 45.688 1.00 37.63  ? 29  VAL A CA   1 
ATOM   408  C C    . VAL A 1 26  ? 21.252 20.020 47.026 1.00 39.65  ? 29  VAL A C    1 
ATOM   409  O O    . VAL A 1 26  ? 21.068 19.402 48.097 1.00 40.95  ? 29  VAL A O    1 
ATOM   410  C CB   . VAL A 1 26  ? 22.119 18.760 45.012 1.00 38.10  ? 29  VAL A CB   1 
ATOM   411  C CG1  . VAL A 1 26  ? 22.823 17.821 45.968 1.00 43.78  ? 29  VAL A CG1  1 
ATOM   412  C CG2  . VAL A 1 26  ? 21.694 18.041 43.734 1.00 48.47  ? 29  VAL A CG2  1 
ATOM   413  H H    . VAL A 1 26  ? 20.734 20.624 44.119 0.00 40.06  ? 29  VAL A H    1 
ATOM   414  H HA   . VAL A 1 26  ? 20.239 18.685 45.849 0.00 45.13  ? 29  VAL A HA   1 
ATOM   415  H HB   . VAL A 1 26  ? 22.751 19.455 44.770 0.00 45.70  ? 29  VAL A HB   1 
ATOM   416  H HG11 . VAL A 1 26  ? 23.455 17.279 45.470 0.00 52.51  ? 29  VAL A HG11 1 
ATOM   417  H HG12 . VAL A 1 26  ? 23.291 18.345 46.637 0.00 52.51  ? 29  VAL A HG12 1 
ATOM   418  H HG13 . VAL A 1 26  ? 22.164 17.252 46.395 0.00 52.51  ? 29  VAL A HG13 1 
ATOM   419  H HG21 . VAL A 1 26  ? 22.479 17.658 43.311 0.00 58.15  ? 29  VAL A HG21 1 
ATOM   420  H HG22 . VAL A 1 26  ? 21.064 17.339 43.960 0.00 58.15  ? 29  VAL A HG22 1 
ATOM   421  H HG23 . VAL A 1 26  ? 21.276 18.681 43.136 0.00 58.15  ? 29  VAL A HG23 1 
ATOM   422  N N    . LYS A 1 27  ? 21.814 21.234 46.991 1.00 34.90  ? 30  LYS A N    1 
ATOM   423  C CA   . LYS A 1 27  ? 22.173 21.910 48.237 1.00 35.07  ? 30  LYS A CA   1 
ATOM   424  C C    . LYS A 1 27  ? 20.979 22.071 49.165 1.00 38.58  ? 30  LYS A C    1 
ATOM   425  O O    . LYS A 1 27  ? 21.122 21.958 50.391 1.00 45.97  ? 30  LYS A O    1 
ATOM   426  C CB   . LYS A 1 27  ? 22.795 23.278 47.938 1.00 39.44  ? 30  LYS A CB   1 
ATOM   427  C CG   . LYS A 1 27  ? 23.928 23.620 48.879 1.00 59.10  ? 30  LYS A CG   1 
ATOM   428  C CD   . LYS A 1 27  ? 24.974 24.529 48.247 1.00 72.65  ? 30  LYS A CD   1 
ATOM   429  C CE   . LYS A 1 27  ? 25.725 25.331 49.317 1.00 80.95  ? 30  LYS A CE   1 
ATOM   430  N NZ   . LYS A 1 27  ? 24.923 26.470 49.849 1.00 69.50  ? 30  LYS A NZ   1 
ATOM   431  H H    . LYS A 1 27  ? 21.993 21.676 46.275 0.00 41.86  ? 30  LYS A H    1 
ATOM   432  H HA   . LYS A 1 27  ? 22.832 21.364 48.694 0.00 42.06  ? 30  LYS A HA   1 
ATOM   433  H HB2  . LYS A 1 27  ? 23.146 23.274 47.034 0.00 47.31  ? 30  LYS A HB2  1 
ATOM   434  H HB3  . LYS A 1 27  ? 22.113 23.962 48.027 0.00 47.31  ? 30  LYS A HB3  1 
ATOM   435  H HG2  . LYS A 1 27  ? 23.566 24.076 49.655 0.00 70.90  ? 30  LYS A HG2  1 
ATOM   436  H HG3  . LYS A 1 27  ? 24.370 22.801 49.152 0.00 70.90  ? 30  LYS A HG3  1 
ATOM   437  H HD2  . LYS A 1 27  ? 25.617 23.992 47.759 0.00 87.16  ? 30  LYS A HD2  1 
ATOM   438  H HD3  . LYS A 1 27  ? 24.539 25.153 47.645 0.00 87.16  ? 30  LYS A HD3  1 
ATOM   439  H HE2  . LYS A 1 27  ? 25.942 24.744 50.058 0.00 97.12  ? 30  LYS A HE2  1 
ATOM   440  H HE3  . LYS A 1 27  ? 26.539 25.691 48.930 0.00 97.12  ? 30  LYS A HE3  1 
ATOM   441  H HZ1  . LYS A 1 27  ? 25.397 26.920 50.454 0.00 83.38  ? 30  LYS A HZ1  1 
ATOM   442  H HZ2  . LYS A 1 27  ? 24.702 27.022 49.187 0.00 83.38  ? 30  LYS A HZ2  1 
ATOM   443  H HZ3  . LYS A 1 27  ? 24.180 26.167 50.233 0.00 83.38  ? 30  LYS A HZ3  1 
ATOM   444  N N    . GLY A 1 28  ? 19.794 22.345 48.615 1.00 36.88  ? 31  GLY A N    1 
ATOM   445  C CA   . GLY A 1 28  ? 18.669 22.604 49.501 1.00 42.75  ? 31  GLY A CA   1 
ATOM   446  C C    . GLY A 1 28  ? 17.969 21.365 50.001 1.00 47.43  ? 31  GLY A C    1 
ATOM   447  O O    . GLY A 1 28  ? 17.004 21.485 50.768 1.00 44.14  ? 31  GLY A O    1 
ATOM   448  H H    . GLY A 1 28  ? 19.630 22.384 47.772 0.00 44.24  ? 31  GLY A H    1 
ATOM   449  H HA2  . GLY A 1 28  ? 18.986 23.099 50.273 0.00 51.28  ? 31  GLY A HA2  1 
ATOM   450  H HA3  . GLY A 1 28  ? 18.016 23.143 49.027 0.00 51.28  ? 31  GLY A HA3  1 
ATOM   451  N N    . MET A 1 29  ? 18.438 20.178 49.585 1.00 52.71  ? 32  MET A N    1 
ATOM   452  C CA   . MET A 1 29  ? 17.866 18.922 50.049 1.00 61.76  ? 32  MET A CA   1 
ATOM   453  C C    . MET A 1 29  ? 18.124 18.772 51.532 1.00 55.49  ? 32  MET A C    1 
ATOM   454  O O    . MET A 1 29  ? 19.267 18.870 51.993 1.00 70.23  ? 32  MET A O    1 
ATOM   455  C CB   . MET A 1 29  ? 18.499 17.736 49.319 1.00 62.21  ? 32  MET A CB   1 
ATOM   456  C CG   . MET A 1 29  ? 17.694 17.193 48.184 1.00 79.39  ? 32  MET A CG   1 
ATOM   457  S SD   . MET A 1 29  ? 18.654 15.857 47.424 1.00 75.83  ? 32  MET A SD   1 
ATOM   458  C CE   . MET A 1 29  ? 18.124 14.509 48.457 1.00 65.91  ? 32  MET A CE   1 
ATOM   459  H H    . MET A 1 29  ? 19.088 20.081 49.031 0.00 63.23  ? 32  MET A H    1 
ATOM   460  H HA   . MET A 1 29  ? 16.915 18.925 49.861 0.00 74.09  ? 32  MET A HA   1 
ATOM   461  H HB2  . MET A 1 29  ? 19.355 18.017 48.960 0.00 74.64  ? 32  MET A HB2  1 
ATOM   462  H HB3  . MET A 1 29  ? 18.626 17.016 49.957 0.00 74.64  ? 32  MET A HB3  1 
ATOM   463  H HG2  . MET A 1 29  ? 16.851 16.839 48.509 0.00 95.24  ? 32  MET A HG2  1 
ATOM   464  H HG3  . MET A 1 29  ? 17.530 17.886 47.526 0.00 95.24  ? 32  MET A HG3  1 
ATOM   465  H HE1  . MET A 1 29  ? 18.542 13.690 48.148 0.00 79.07  ? 32  MET A HE1  1 
ATOM   466  H HE2  . MET A 1 29  ? 18.388 14.690 49.373 0.00 79.07  ? 32  MET A HE2  1 
ATOM   467  H HE3  . MET A 1 29  ? 17.159 14.429 48.401 0.00 79.07  ? 32  MET A HE3  1 
ATOM   468  N N    . GLY A 1 30  ? 17.083 18.535 52.291 1.00 63.67  ? 33  GLY A N    1 
ATOM   469  C CA   . GLY A 1 30  ? 17.266 18.313 53.701 1.00 69.45  ? 33  GLY A CA   1 
ATOM   470  C C    . GLY A 1 30  ? 17.299 19.560 54.547 1.00 69.55  ? 33  GLY A C    1 
ATOM   471  O O    . GLY A 1 30  ? 17.268 19.446 55.774 1.00 71.95  ? 33  GLY A O    1 
ATOM   472  H H    . GLY A 1 30  ? 16.269 18.499 52.016 0.00 76.39  ? 33  GLY A H    1 
ATOM   473  H HA2  . GLY A 1 30  ? 16.540 17.757 54.023 0.00 83.32  ? 33  GLY A HA2  1 
ATOM   474  H HA3  . GLY A 1 30  ? 18.105 17.845 53.834 0.00 83.32  ? 33  GLY A HA3  1 
ATOM   475  N N    . VAL A 1 31  ? 17.354 20.755 53.951 1.00 55.49  ? 34  VAL A N    1 
ATOM   476  C CA   . VAL A 1 31  ? 17.171 21.940 54.773 1.00 50.82  ? 34  VAL A CA   1 
ATOM   477  C C    . VAL A 1 31  ? 15.777 21.867 55.388 1.00 54.88  ? 34  VAL A C    1 
ATOM   478  O O    . VAL A 1 31  ? 14.784 21.652 54.687 1.00 57.83  ? 34  VAL A O    1 
ATOM   479  C CB   . VAL A 1 31  ? 17.384 23.213 53.934 1.00 55.43  ? 34  VAL A CB   1 
ATOM   480  C CG1  . VAL A 1 31  ? 17.030 24.456 54.749 1.00 56.16  ? 34  VAL A CG1  1 
ATOM   481  C CG2  . VAL A 1 31  ? 18.832 23.281 53.451 1.00 54.47  ? 34  VAL A CG2  1 
ATOM   482  H H    . VAL A 1 31  ? 17.489 20.894 53.113 0.00 66.57  ? 34  VAL A H    1 
ATOM   483  H HA   . VAL A 1 31  ? 17.826 21.964 55.488 0.00 60.97  ? 34  VAL A HA   1 
ATOM   484  H HB   . VAL A 1 31  ? 16.801 23.188 53.159 0.00 66.50  ? 34  VAL A HB   1 
ATOM   485  H HG11 . VAL A 1 31  ? 17.269 25.247 54.240 0.00 67.37  ? 34  VAL A HG11 1 
ATOM   486  H HG12 . VAL A 1 31  ? 16.076 24.455 54.928 0.00 67.37  ? 34  VAL A HG12 1 
ATOM   487  H HG13 . VAL A 1 31  ? 17.524 24.438 55.583 0.00 67.37  ? 34  VAL A HG13 1 
ATOM   488  H HG21 . VAL A 1 31  ? 18.957 24.096 52.940 0.00 65.35  ? 34  VAL A HG21 1 
ATOM   489  H HG22 . VAL A 1 31  ? 19.422 23.280 54.221 0.00 65.35  ? 34  VAL A HG22 1 
ATOM   490  H HG23 . VAL A 1 31  ? 19.015 22.509 52.893 0.00 65.35  ? 34  VAL A HG23 1 
ATOM   491  N N    . SER A 1 32  ? 15.696 22.005 56.716 1.00 53.86  ? 35  SER A N    1 
ATOM   492  C CA   . SER A 1 32  ? 14.422 21.902 57.406 1.00 57.68  ? 35  SER A CA   1 
ATOM   493  C C    . SER A 1 32  ? 13.923 23.209 58.003 1.00 65.90  ? 35  SER A C    1 
ATOM   494  O O    . SER A 1 32  ? 12.722 23.313 58.279 1.00 67.04  ? 35  SER A O    1 
ATOM   495  C CB   . SER A 1 32  ? 14.507 20.851 58.529 1.00 67.58  ? 35  SER A CB   1 
ATOM   496  O OG   . SER A 1 32  ? 15.677 21.025 59.306 1.00 76.90  ? 35  SER A OG   1 
ATOM   497  H H    . SER A 1 32  ? 16.368 22.157 57.231 0.00 64.62  ? 35  SER A H    1 
ATOM   498  H HA   . SER A 1 32  ? 13.757 21.607 56.765 0.00 69.20  ? 35  SER A HA   1 
ATOM   499  H HB2  . SER A 1 32  ? 13.732 20.942 59.104 0.00 81.08  ? 35  SER A HB2  1 
ATOM   500  H HB3  . SER A 1 32  ? 14.523 19.966 58.131 0.00 81.08  ? 35  SER A HB3  1 
ATOM   501  H HG   . SER A 1 32  ? 15.641 21.755 59.720 0.00 92.26  ? 35  SER A HG   1 
ATOM   502  N N    . ASP A 1 33  ? 14.796 24.203 58.196 1.00 50.38  ? 36  ASP A N    1 
ATOM   503  C CA   . ASP A 1 33  ? 14.368 25.472 58.779 1.00 47.75  ? 36  ASP A CA   1 
ATOM   504  C C    . ASP A 1 33  ? 13.363 26.160 57.848 1.00 41.01  ? 36  ASP A C    1 
ATOM   505  O O    . ASP A 1 33  ? 13.691 26.412 56.700 1.00 38.82  ? 36  ASP A O    1 
ATOM   506  C CB   . ASP A 1 33  ? 15.578 26.385 58.985 1.00 55.53  ? 36  ASP A CB   1 
ATOM   507  C CG   . ASP A 1 33  ? 15.196 27.736 59.590 1.00 55.92  ? 36  ASP A CG   1 
ATOM   508  O OD1  . ASP A 1 33  ? 14.828 27.769 60.761 1.00 58.06  ? 36  ASP A OD1  1 
ATOM   509  O OD2  . ASP A 1 33  ? 15.211 28.763 58.886 1.00 50.89  ? 36  ASP A OD2  1 
ATOM   510  H H    . ASP A 1 33  ? 15.633 24.166 57.999 0.00 60.44  ? 36  ASP A H    1 
ATOM   511  H HA   . ASP A 1 33  ? 13.944 25.309 59.636 0.00 57.29  ? 36  ASP A HA   1 
ATOM   512  H HB2  . ASP A 1 33  ? 16.203 25.951 59.587 0.00 66.62  ? 36  ASP A HB2  1 
ATOM   513  H HB3  . ASP A 1 33  ? 16.002 26.548 58.128 0.00 66.62  ? 36  ASP A HB3  1 
ATOM   514  N N    . PRO A 1 34  ? 12.181 26.564 58.338 1.00 49.16  ? 37  PRO A N    1 
ATOM   515  C CA   . PRO A 1 34  ? 11.169 27.146 57.432 1.00 52.04  ? 37  PRO A CA   1 
ATOM   516  C C    . PRO A 1 34  ? 11.589 28.443 56.781 1.00 47.39  ? 37  PRO A C    1 
ATOM   517  O O    . PRO A 1 34  ? 11.170 28.710 55.665 1.00 41.18  ? 37  PRO A O    1 
ATOM   518  C CB   . PRO A 1 34  ? 9.942  27.372 58.331 1.00 54.65  ? 37  PRO A CB   1 
ATOM   519  C CG   . PRO A 1 34  ? 10.400 27.159 59.739 1.00 58.70  ? 37  PRO A CG   1 
ATOM   520  C CD   . PRO A 1 34  ? 11.723 26.470 59.745 1.00 48.01  ? 37  PRO A CD   1 
ATOM   521  H HA   . PRO A 1 34  ? 10.962 26.489 56.750 0.00 62.43  ? 37  PRO A HA   1 
ATOM   522  H HB2  . PRO A 1 34  ? 9.615  28.277 58.211 0.00 65.56  ? 37  PRO A HB2  1 
ATOM   523  H HB3  . PRO A 1 34  ? 9.248  26.736 58.097 0.00 65.56  ? 37  PRO A HB3  1 
ATOM   524  H HG2  . PRO A 1 34  ? 10.478 28.022 60.174 0.00 70.42  ? 37  PRO A HG2  1 
ATOM   525  H HG3  . PRO A 1 34  ? 9.744  26.613 60.200 0.00 70.42  ? 37  PRO A HG3  1 
ATOM   526  H HD2  . PRO A 1 34  ? 12.343 26.922 60.338 0.00 57.59  ? 37  PRO A HD2  1 
ATOM   527  H HD3  . PRO A 1 34  ? 11.625 25.542 60.012 0.00 57.59  ? 37  PRO A HD3  1 
ATOM   528  N N    . ASP A 1 35  ? 12.379 29.279 57.445 1.00 41.17  ? 38  ASP A N    1 
ATOM   529  C CA   . ASP A 1 35  ? 12.822 30.520 56.817 1.00 41.03  ? 38  ASP A CA   1 
ATOM   530  C C    . ASP A 1 35  ? 13.828 30.245 55.717 1.00 37.12  ? 38  ASP A C    1 
ATOM   531  O O    . ASP A 1 35  ? 13.724 30.807 54.610 1.00 35.73  ? 38  ASP A O    1 
ATOM   532  C CB   . ASP A 1 35  ? 13.428 31.443 57.880 1.00 43.05  ? 38  ASP A CB   1 
ATOM   533  C CG   . ASP A 1 35  ? 12.368 32.125 58.721 1.00 66.15  ? 38  ASP A CG   1 
ATOM   534  O OD1  . ASP A 1 35  ? 11.181 32.063 58.335 1.00 78.63  ? 38  ASP A OD1  1 
ATOM   535  O OD2  . ASP A 1 35  ? 12.720 32.718 59.761 1.00 101.03 ? 38  ASP A OD2  1 
ATOM   536  H H    . ASP A 1 35  ? 12.668 29.156 58.246 0.00 49.39  ? 38  ASP A H    1 
ATOM   537  H HA   . ASP A 1 35  ? 12.059 30.969 56.420 0.00 49.22  ? 38  ASP A HA   1 
ATOM   538  H HB2  . ASP A 1 35  ? 13.992 30.919 58.471 0.00 51.64  ? 38  ASP A HB2  1 
ATOM   539  H HB3  . ASP A 1 35  ? 13.954 32.130 57.442 0.00 51.64  ? 38  ASP A HB3  1 
ATOM   540  N N    . ALA A 1 36  ? 14.777 29.330 55.975 1.00 35.12  ? 39  ALA A N    1 
ATOM   541  C CA   . ALA A 1 36  ? 15.735 28.963 54.929 1.00 34.16  ? 39  ALA A CA   1 
ATOM   542  C C    . ALA A 1 36  ? 15.042 28.313 53.725 1.00 32.60  ? 39  ALA A C    1 
ATOM   543  O O    . ALA A 1 36  ? 15.422 28.555 52.579 1.00 30.88  ? 39  ALA A O    1 
ATOM   544  C CB   . ALA A 1 36  ? 16.794 28.020 55.493 1.00 37.56  ? 39  ALA A CB   1 
ATOM   545  H H    . ALA A 1 36  ? 14.882 28.921 56.725 0.00 42.12  ? 39  ALA A H    1 
ATOM   546  H HA   . ALA A 1 36  ? 16.174 29.772 54.623 0.00 40.97  ? 39  ALA A HA   1 
ATOM   547  H HB1  . ALA A 1 36  ? 17.420 27.790 54.789 0.00 45.05  ? 39  ALA A HB1  1 
ATOM   548  H HB2  . ALA A 1 36  ? 17.259 28.466 56.218 0.00 45.05  ? 39  ALA A HB2  1 
ATOM   549  H HB3  . ALA A 1 36  ? 16.359 27.218 55.823 0.00 45.05  ? 39  ALA A HB3  1 
ATOM   550  N N    . LYS A 1 37  ? 14.047 27.446 53.972 1.00 33.94  ? 40  LYS A N    1 
ATOM   551  C CA   . LYS A 1 37  ? 13.295 26.839 52.854 1.00 33.75  ? 40  LYS A CA   1 
ATOM   552  C C    . LYS A 1 37  ? 12.741 27.886 51.899 1.00 32.12  ? 40  LYS A C    1 
ATOM   553  O O    . LYS A 1 37  ? 12.718 27.695 50.643 1.00 34.59  ? 40  LYS A O    1 
ATOM   554  C CB   . LYS A 1 37  ? 12.133 26.007 53.449 1.00 36.38  ? 40  LYS A CB   1 
ATOM   555  C CG   . LYS A 1 37  ? 12.503 24.718 54.164 1.00 49.27  ? 40  LYS A CG   1 
ATOM   556  C CD   . LYS A 1 37  ? 11.546 23.577 53.810 1.00 59.50  ? 40  LYS A CD   1 
ATOM   557  C CE   . LYS A 1 37  ? 10.932 22.956 55.014 1.00 66.26  ? 40  LYS A CE   1 
ATOM   558  N NZ   . LYS A 1 37  ? 9.733  22.161 54.638 1.00 76.63  ? 40  LYS A NZ   1 
ATOM   559  H H    . LYS A 1 37  ? 13.792 27.198 54.755 0.00 40.71  ? 40  LYS A H    1 
ATOM   560  H HA   . LYS A 1 37  ? 13.889 26.266 52.344 0.00 40.48  ? 40  LYS A HA   1 
ATOM   561  H HB2  . LYS A 1 37  ? 11.666 26.562 54.092 0.00 43.64  ? 40  LYS A HB2  1 
ATOM   562  H HB3  . LYS A 1 37  ? 11.535 25.766 52.723 0.00 43.64  ? 40  LYS A HB3  1 
ATOM   563  H HG2  . LYS A 1 37  ? 13.400 24.454 53.903 0.00 59.11  ? 40  LYS A HG2  1 
ATOM   564  H HG3  . LYS A 1 37  ? 12.464 24.860 55.122 0.00 59.11  ? 40  LYS A HG3  1 
ATOM   565  H HD2  . LYS A 1 37  ? 10.832 23.923 53.252 0.00 71.39  ? 40  LYS A HD2  1 
ATOM   566  H HD3  . LYS A 1 37  ? 12.035 22.889 53.333 0.00 71.39  ? 40  LYS A HD3  1 
ATOM   567  H HE2  . LYS A 1 37  ? 11.574 22.366 55.438 0.00 79.50  ? 40  LYS A HE2  1 
ATOM   568  H HE3  . LYS A 1 37  ? 10.659 23.651 55.634 0.00 79.50  ? 40  LYS A HE3  1 
ATOM   569  H HZ1  . LYS A 1 37  ? 9.375  21.789 55.363 0.00 91.94  ? 40  LYS A HZ1  1 
ATOM   570  H HZ2  . LYS A 1 37  ? 9.127  22.687 54.254 0.00 91.94  ? 40  LYS A HZ2  1 
ATOM   571  H HZ3  . LYS A 1 37  ? 9.962  21.518 54.067 0.00 91.94  ? 40  LYS A HZ3  1 
ATOM   572  N N    . LYS A 1 38  ? 12.229 28.999 52.428 1.00 30.82  ? 41  LYS A N    1 
ATOM   573  C CA   . LYS A 1 38  ? 11.693 30.056 51.557 1.00 29.26  ? 41  LYS A CA   1 
ATOM   574  C C    . LYS A 1 38  ? 12.771 30.623 50.613 1.00 29.03  ? 41  LYS A C    1 
ATOM   575  O O    . LYS A 1 38  ? 12.572 30.761 49.396 1.00 27.23  ? 41  LYS A O    1 
ATOM   576  C CB   . LYS A 1 38  ? 11.171 31.230 52.433 1.00 35.41  ? 41  LYS A CB   1 
ATOM   577  C CG   . LYS A 1 38  ? 9.781  31.074 52.959 1.00 44.61  ? 41  LYS A CG   1 
ATOM   578  C CD   . LYS A 1 38  ? 9.555  32.098 54.089 1.00 47.69  ? 41  LYS A CD   1 
ATOM   579  C CE   . LYS A 1 38  ? 9.235  33.480 53.559 1.00 77.23  ? 41  LYS A CE   1 
ATOM   580  N NZ   . LYS A 1 38  ? 8.851  34.421 54.666 1.00 103.55 ? 41  LYS A NZ   1 
ATOM   581  H H    . LYS A 1 38  ? 12.179 29.168 53.269 0.00 36.97  ? 41  LYS A H    1 
ATOM   582  H HA   . LYS A 1 38  ? 10.974 29.669 51.032 0.00 35.10  ? 41  LYS A HA   1 
ATOM   583  H HB2  . LYS A 1 38  ? 11.760 31.324 53.197 0.00 42.47  ? 41  LYS A HB2  1 
ATOM   584  H HB3  . LYS A 1 38  ? 11.188 32.039 51.898 0.00 42.47  ? 41  LYS A HB3  1 
ATOM   585  H HG2  . LYS A 1 38  ? 9.139  31.238 52.251 0.00 53.51  ? 41  LYS A HG2  1 
ATOM   586  H HG3  . LYS A 1 38  ? 9.661  30.180 53.315 0.00 53.51  ? 41  LYS A HG3  1 
ATOM   587  H HD2  . LYS A 1 38  ? 8.811  31.807 54.638 0.00 57.21  ? 41  LYS A HD2  1 
ATOM   588  H HD3  . LYS A 1 38  ? 10.360 32.161 54.627 0.00 57.21  ? 41  LYS A HD3  1 
ATOM   589  H HE2  . LYS A 1 38  ? 10.016 33.840 53.110 0.00 92.66  ? 41  LYS A HE2  1 
ATOM   590  H HE3  . LYS A 1 38  ? 8.493  33.421 52.937 0.00 92.66  ? 41  LYS A HE3  1 
ATOM   591  H HZ1  . LYS A 1 38  ? 8.669  35.226 54.332 0.00 124.25 ? 41  LYS A HZ1  1 
ATOM   592  H HZ2  . LYS A 1 38  ? 8.130  34.115 55.090 0.00 124.25 ? 41  LYS A HZ2  1 
ATOM   593  H HZ3  . LYS A 1 38  ? 9.519  34.495 55.249 0.00 124.25 ? 41  LYS A HZ3  1 
ATOM   594  N N    . PHE A 1 39  ? 13.944 30.973 51.162 1.00 27.84  ? 42  PHE A N    1 
ATOM   595  C CA   . PHE A 1 39  ? 15.012 31.480 50.299 1.00 27.71  ? 42  PHE A CA   1 
ATOM   596  C C    . PHE A 1 39  ? 15.514 30.437 49.300 1.00 25.83  ? 42  PHE A C    1 
ATOM   597  O O    . PHE A 1 39  ? 15.804 30.777 48.146 1.00 26.08  ? 42  PHE A O    1 
ATOM   598  C CB   . PHE A 1 39  ? 16.183 31.962 51.184 1.00 30.12  ? 42  PHE A CB   1 
ATOM   599  C CG   . PHE A 1 39  ? 15.857 33.214 51.979 1.00 28.35  ? 42  PHE A CG   1 
ATOM   600  C CD1  . PHE A 1 39  ? 15.744 34.466 51.318 1.00 31.92  ? 42  PHE A CD1  1 
ATOM   601  C CD2  . PHE A 1 39  ? 15.622 33.155 53.336 1.00 31.64  ? 42  PHE A CD2  1 
ATOM   602  C CE1  . PHE A 1 39  ? 15.439 35.631 52.041 1.00 32.85  ? 42  PHE A CE1  1 
ATOM   603  C CE2  . PHE A 1 39  ? 15.320 34.341 54.081 1.00 36.73  ? 42  PHE A CE2  1 
ATOM   604  C CZ   . PHE A 1 39  ? 15.231 35.575 53.421 1.00 40.26  ? 42  PHE A CZ   1 
ATOM   605  H H    . PHE A 1 39  ? 14.137 30.927 51.998 0.00 33.38  ? 42  PHE A H    1 
ATOM   606  H HA   . PHE A 1 39  ? 14.659 32.222 49.783 0.00 33.23  ? 42  PHE A HA   1 
ATOM   607  H HB2  . PHE A 1 39  ? 16.410 31.259 51.813 0.00 36.13  ? 42  PHE A HB2  1 
ATOM   608  H HB3  . PHE A 1 39  ? 16.945 32.158 50.617 0.00 36.13  ? 42  PHE A HB3  1 
ATOM   609  H HD1  . PHE A 1 39  ? 15.873 34.514 50.398 0.00 38.29  ? 42  PHE A HD1  1 
ATOM   610  H HD2  . PHE A 1 39  ? 15.661 32.335 53.773 0.00 37.95  ? 42  PHE A HD2  1 
ATOM   611  H HE1  . PHE A 1 39  ? 15.375 36.446 51.597 0.00 39.40  ? 42  PHE A HE1  1 
ATOM   612  H HE2  . PHE A 1 39  ? 15.182 34.292 55.000 0.00 44.05  ? 42  PHE A HE2  1 
ATOM   613  H HZ   . PHE A 1 39  ? 15.035 36.350 53.898 0.00 48.30  ? 42  PHE A HZ   1 
ATOM   614  N N    . TYR A 1 40  ? 15.634 29.170 49.706 1.00 26.98  ? 43  TYR A N    1 
ATOM   615  C CA   . TYR A 1 40  ? 16.047 28.164 48.700 1.00 26.54  ? 43  TYR A CA   1 
ATOM   616  C C    . TYR A 1 40  ? 15.002 28.005 47.601 1.00 25.76  ? 43  TYR A C    1 
ATOM   617  O O    . TYR A 1 40  ? 15.347 27.800 46.422 1.00 27.06  ? 43  TYR A O    1 
ATOM   618  C CB   . TYR A 1 40  ? 16.270 26.799 49.355 1.00 28.33  ? 43  TYR A CB   1 
ATOM   619  C CG   . TYR A 1 40  ? 17.706 26.587 49.822 1.00 30.85  ? 43  TYR A CG   1 
ATOM   620  C CD1  . TYR A 1 40  ? 18.666 26.097 48.938 1.00 31.06  ? 43  TYR A CD1  1 
ATOM   621  C CD2  . TYR A 1 40  ? 18.077 26.925 51.086 1.00 32.86  ? 43  TYR A CD2  1 
ATOM   622  C CE1  . TYR A 1 40  ? 19.981 25.910 49.369 1.00 36.29  ? 43  TYR A CE1  1 
ATOM   623  C CE2  . TYR A 1 40  ? 19.409 26.751 51.522 1.00 35.74  ? 43  TYR A CE2  1 
ATOM   624  C CZ   . TYR A 1 40  ? 20.335 26.253 50.599 1.00 37.07  ? 43  TYR A CZ   1 
ATOM   625  O OH   . TYR A 1 40  ? 21.651 26.036 51.021 1.00 42.89  ? 43  TYR A OH   1 
ATOM   626  H H    . TYR A 1 40  ? 15.494 28.878 50.502 0.00 32.35  ? 43  TYR A H    1 
ATOM   627  H HA   . TYR A 1 40  ? 16.881 28.472 48.312 0.00 31.83  ? 43  TYR A HA   1 
ATOM   628  H HB2  . TYR A 1 40  ? 15.690 26.722 50.129 0.00 33.98  ? 43  TYR A HB2  1 
ATOM   629  H HB3  . TYR A 1 40  ? 16.060 26.104 48.712 0.00 33.98  ? 43  TYR A HB3  1 
ATOM   630  H HD1  . TYR A 1 40  ? 18.431 25.895 48.061 0.00 37.25  ? 43  TYR A HD1  1 
ATOM   631  H HD2  . TYR A 1 40  ? 17.445 27.276 51.671 0.00 39.41  ? 43  TYR A HD2  1 
ATOM   632  H HE1  . TYR A 1 40  ? 20.610 25.543 48.791 0.00 43.53  ? 43  TYR A HE1  1 
ATOM   633  H HE2  . TYR A 1 40  ? 19.662 26.960 52.392 0.00 42.87  ? 43  TYR A HE2  1 
ATOM   634  H HH   . TYR A 1 40  ? 21.733 26.251 51.829 0.00 51.45  ? 43  TYR A HH   1 
ATOM   635  N N    . ALA A 1 41  ? 13.708 28.078 47.940 1.00 26.42  ? 44  ALA A N    1 
ATOM   636  C CA   . ALA A 1 41  ? 12.686 27.885 46.876 1.00 27.51  ? 44  ALA A CA   1 
ATOM   637  C C    . ALA A 1 41  ? 12.724 29.036 45.877 1.00 29.60  ? 44  ALA A C    1 
ATOM   638  O O    . ALA A 1 41  ? 12.736 28.826 44.642 1.00 26.45  ? 44  ALA A O    1 
ATOM   639  C CB   . ALA A 1 41  ? 11.289 27.778 47.527 1.00 29.21  ? 44  ALA A CB   1 
ATOM   640  H H    . ALA A 1 41  ? 13.404 28.228 48.730 0.00 31.69  ? 44  ALA A H    1 
ATOM   641  H HA   . ALA A 1 41  ? 12.867 27.062 46.395 0.00 32.99  ? 44  ALA A HA   1 
ATOM   642  H HB1  . ALA A 1 41  ? 10.625 27.656 46.830 0.00 35.03  ? 44  ALA A HB1  1 
ATOM   643  H HB2  . ALA A 1 41  ? 11.279 27.018 48.129 0.00 35.03  ? 44  ALA A HB2  1 
ATOM   644  H HB3  . ALA A 1 41  ? 11.107 28.593 48.019 0.00 35.03  ? 44  ALA A HB3  1 
ATOM   645  N N    . ILE A 1 42  ? 12.780 30.269 46.381 1.00 24.52  ? 45  ILE A N    1 
ATOM   646  C CA   . ILE A 1 42  ? 12.802 31.436 45.488 1.00 26.92  ? 45  ILE A CA   1 
ATOM   647  C C    . ILE A 1 42  ? 14.048 31.389 44.644 1.00 28.13  ? 45  ILE A C    1 
ATOM   648  O O    . ILE A 1 42  ? 14.009 31.590 43.428 1.00 26.46  ? 45  ILE A O    1 
ATOM   649  C CB   . ILE A 1 42  ? 12.729 32.770 46.305 1.00 23.93  ? 45  ILE A CB   1 
ATOM   650  C CG1  . ILE A 1 42  ? 11.380 32.919 47.022 1.00 27.63  ? 45  ILE A CG1  1 
ATOM   651  C CG2  . ILE A 1 42  ? 13.063 34.005 45.370 1.00 27.72  ? 45  ILE A CG2  1 
ATOM   652  C CD1  . ILE A 1 42  ? 11.382 33.984 48.123 1.00 34.24  ? 45  ILE A CD1  1 
ATOM   653  H H    . ILE A 1 42  ? 12.805 30.458 47.219 0.00 29.41  ? 45  ILE A H    1 
ATOM   654  H HA   . ILE A 1 42  ? 12.021 31.403 44.914 0.00 32.28  ? 45  ILE A HA   1 
ATOM   655  H HB   . ILE A 1 42  ? 13.402 32.740 47.002 0.00 28.69  ? 45  ILE A HB   1 
ATOM   656  H HG12 . ILE A 1 42  ? 10.705 33.167 46.371 0.00 33.14  ? 45  ILE A HG12 1 
ATOM   657  H HG13 . ILE A 1 42  ? 11.149 32.070 47.432 0.00 33.14  ? 45  ILE A HG13 1 
ATOM   658  H HG21 . ILE A 1 42  ? 12.819 34.823 45.830 0.00 33.24  ? 45  ILE A HG21 1 
ATOM   659  H HG22 . ILE A 1 42  ? 14.013 34.005 45.176 0.00 33.24  ? 45  ILE A HG22 1 
ATOM   660  H HG23 . ILE A 1 42  ? 12.557 33.924 44.547 0.00 33.24  ? 45  ILE A HG23 1 
ATOM   661  H HD11 . ILE A 1 42  ? 10.532 33.957 48.591 0.00 41.07  ? 45  ILE A HD11 1 
ATOM   662  H HD12 . ILE A 1 42  ? 12.106 33.798 48.741 0.00 41.07  ? 45  ILE A HD12 1 
ATOM   663  H HD13 . ILE A 1 42  ? 11.508 34.856 47.718 0.00 41.07  ? 45  ILE A HD13 1 
ATOM   664  N N    . THR A 1 43  ? 15.195 31.088 45.256 1.00 22.21  ? 46  THR A N    1 
ATOM   665  C CA   . THR A 1 43  ? 16.464 31.260 44.570 1.00 23.84  ? 46  THR A CA   1 
ATOM   666  C C    . THR A 1 43  ? 16.725 30.113 43.574 1.00 30.61  ? 46  THR A C    1 
ATOM   667  O O    . THR A 1 43  ? 17.478 30.308 42.618 1.00 28.66  ? 46  THR A O    1 
ATOM   668  C CB   . THR A 1 43  ? 17.593 31.334 45.595 1.00 25.65  ? 46  THR A CB   1 
ATOM   669  O OG1  . THR A 1 43  ? 17.265 32.416 46.543 1.00 26.77  ? 46  THR A OG1  1 
ATOM   670  C CG2  . THR A 1 43  ? 18.969 31.680 44.932 1.00 33.25  ? 46  THR A CG2  1 
ATOM   671  H H    . THR A 1 43  ? 15.261 30.786 46.058 0.00 26.63  ? 46  THR A H    1 
ATOM   672  H HA   . THR A 1 43  ? 16.455 32.094 44.073 0.00 28.58  ? 46  THR A HA   1 
ATOM   673  H HB   . THR A 1 43  ? 17.683 30.474 46.035 0.00 30.76  ? 46  THR A HB   1 
ATOM   674  H HG1  . THR A 1 43  ? 16.558 32.231 46.958 0.00 32.11  ? 46  THR A HG1  1 
ATOM   675  H HG21 . THR A 1 43  ? 19.637 31.840 45.617 0.00 39.88  ? 46  THR A HG21 1 
ATOM   676  H HG22 . THR A 1 43  ? 19.262 30.943 44.373 0.00 39.88  ? 46  THR A HG22 1 
ATOM   677  H HG23 . THR A 1 43  ? 18.883 32.476 44.384 0.00 39.88  ? 46  THR A HG23 1 
ATOM   678  N N    . THR A 1 44  ? 16.161 28.921 43.813 1.00 23.44  ? 47  THR A N    1 
ATOM   679  C CA   . THR A 1 44  ? 16.336 27.808 42.859 1.00 24.18  ? 47  THR A CA   1 
ATOM   680  C C    . THR A 1 44  ? 15.400 27.996 41.656 1.00 25.13  ? 47  THR A C    1 
ATOM   681  O O    . THR A 1 44  ? 15.769 27.643 40.519 1.00 23.61  ? 47  THR A O    1 
ATOM   682  C CB   . THR A 1 44  ? 16.018 26.471 43.530 1.00 25.05  ? 47  THR A CB   1 
ATOM   683  O OG1  . THR A 1 44  ? 16.903 26.309 44.680 1.00 28.13  ? 47  THR A OG1  1 
ATOM   684  C CG2  . THR A 1 44  ? 16.244 25.207 42.564 1.00 26.70  ? 47  THR A CG2  1 
ATOM   685  H H    . THR A 1 44  ? 15.684 28.732 44.502 0.00 28.11  ? 47  THR A H    1 
ATOM   686  H HA   . THR A 1 44  ? 17.259 27.778 42.565 0.00 29.00  ? 47  THR A HA   1 
ATOM   687  H HB   . THR A 1 44  ? 15.081 26.480 43.782 0.00 30.04  ? 47  THR A HB   1 
ATOM   688  H HG1  . THR A 1 44  ? 16.788 26.941 45.222 0.00 33.74  ? 47  THR A HG1  1 
ATOM   689  H HG21 . THR A 1 44  ? 16.100 24.383 43.057 0.00 32.02  ? 47  THR A HG21 1 
ATOM   690  H HG22 . THR A 1 44  ? 15.622 25.242 41.821 0.00 32.02  ? 47  THR A HG22 1 
ATOM   691  H HG23 . THR A 1 44  ? 17.150 25.212 42.218 0.00 32.02  ? 47  THR A HG23 1 
ATOM   692  N N    . LEU A 1 45  ? 14.216 28.570 41.876 1.00 23.25  ? 48  LEU A N    1 
ATOM   693  C CA   . LEU A 1 45  ? 13.305 28.807 40.748 1.00 20.46  ? 48  LEU A CA   1 
ATOM   694  C C    . LEU A 1 45  ? 13.876 29.775 39.729 1.00 22.99  ? 48  LEU A C    1 
ATOM   695  O O    . LEU A 1 45  ? 13.567 29.646 38.544 1.00 22.56  ? 48  LEU A O    1 
ATOM   696  C CB   . LEU A 1 45  ? 11.947 29.373 41.229 1.00 22.34  ? 48  LEU A CB   1 
ATOM   697  C CG   . LEU A 1 45  ? 10.930 28.383 41.722 1.00 32.15  ? 48  LEU A CG   1 
ATOM   698  C CD1  . LEU A 1 45  ? 9.749  29.150 42.427 1.00 35.30  ? 48  LEU A CD1  1 
ATOM   699  C CD2  . LEU A 1 45  ? 10.427 27.606 40.424 1.00 27.53  ? 48  LEU A CD2  1 
ATOM   700  H H    . LEU A 1 45  ? 13.922 28.824 42.643 0.00 27.89  ? 48  LEU A H    1 
ATOM   701  H HA   . LEU A 1 45  ? 13.162 27.944 40.329 0.00 24.54  ? 48  LEU A HA   1 
ATOM   702  H HB2  . LEU A 1 45  ? 12.122 29.986 41.960 0.00 26.78  ? 48  LEU A HB2  1 
ATOM   703  H HB3  . LEU A 1 45  ? 11.542 29.848 40.486 0.00 26.78  ? 48  LEU A HB3  1 
ATOM   704  H HG   . LEU A 1 45  ? 11.286 27.760 42.375 0.00 38.56  ? 48  LEU A HG   1 
ATOM   705  H HD11 . LEU A 1 45  ? 9.111  28.504 42.768 0.00 42.34  ? 48  LEU A HD11 1 
ATOM   706  H HD12 . LEU A 1 45  ? 10.107 29.679 43.157 0.00 42.34  ? 48  LEU A HD12 1 
ATOM   707  H HD13 . LEU A 1 45  ? 9.318  29.730 41.780 0.00 42.34  ? 48  LEU A HD13 1 
ATOM   708  H HD21 . LEU A 1 45  ? 9.703  27.011 40.672 0.00 33.02  ? 48  LEU A HD21 1 
ATOM   709  H HD22 . LEU A 1 45  ? 10.115 28.252 39.771 0.00 33.02  ? 48  LEU A HD22 1 
ATOM   710  H HD23 . LEU A 1 45  ? 11.165 27.095 40.057 0.00 33.02  ? 48  LEU A HD23 1 
ATOM   711  N N    . VAL A 1 46  ? 14.683 30.772 40.145 1.00 20.97  ? 49  VAL A N    1 
ATOM   712  C CA   . VAL A 1 46  ? 15.226 31.789 39.245 1.00 21.98  ? 49  VAL A CA   1 
ATOM   713  C C    . VAL A 1 46  ? 16.083 31.186 38.115 1.00 24.80  ? 49  VAL A C    1 
ATOM   714  O O    . VAL A 1 46  ? 15.734 31.385 36.917 1.00 21.49  ? 49  VAL A O    1 
ATOM   715  C CB   . VAL A 1 46  ? 15.995 32.856 40.081 1.00 21.64  ? 49  VAL A CB   1 
ATOM   716  C CG1  . VAL A 1 46  ? 16.842 33.742 39.124 1.00 23.30  ? 49  VAL A CG1  1 
ATOM   717  C CG2  . VAL A 1 46  ? 14.884 33.743 40.823 1.00 24.95  ? 49  VAL A CG2  1 
ATOM   718  H H    . VAL A 1 46  ? 14.930 30.876 40.962 0.00 25.15  ? 49  VAL A H    1 
ATOM   719  H HA   . VAL A 1 46  ? 14.487 32.206 38.775 0.00 26.36  ? 49  VAL A HA   1 
ATOM   720  H HB   . VAL A 1 46  ? 16.596 32.451 40.726 0.00 25.95  ? 49  VAL A HB   1 
ATOM   721  H HG11 . VAL A 1 46  ? 17.122 34.541 39.598 0.00 27.94  ? 49  VAL A HG11 1 
ATOM   722  H HG12 . VAL A 1 46  ? 17.620 33.240 38.835 0.00 27.94  ? 49  VAL A HG12 1 
ATOM   723  H HG13 . VAL A 1 46  ? 16.301 33.985 38.357 0.00 27.94  ? 49  VAL A HG13 1 
ATOM   724  H HG21 . VAL A 1 46  ? 15.326 34.425 41.353 0.00 29.92  ? 49  VAL A HG21 1 
ATOM   725  H HG22 . VAL A 1 46  ? 14.315 34.160 40.156 0.00 29.92  ? 49  VAL A HG22 1 
ATOM   726  H HG23 . VAL A 1 46  ? 14.354 33.170 41.398 0.00 29.92  ? 49  VAL A HG23 1 
ATOM   727  N N    . PRO A 1 47  ? 17.119 30.399 38.365 1.00 21.80  ? 50  PRO A N    1 
ATOM   728  C CA   . PRO A 1 47  ? 17.837 29.813 37.198 1.00 20.46  ? 50  PRO A CA   1 
ATOM   729  C C    . PRO A 1 47  ? 17.035 28.707 36.501 1.00 22.81  ? 50  PRO A C    1 
ATOM   730  O O    . PRO A 1 47  ? 17.325 28.423 35.339 1.00 23.23  ? 50  PRO A O    1 
ATOM   731  C CB   . PRO A 1 47  ? 19.182 29.291 37.801 1.00 21.24  ? 50  PRO A CB   1 
ATOM   732  C CG   . PRO A 1 47  ? 18.836 29.041 39.311 1.00 23.50  ? 50  PRO A CG   1 
ATOM   733  C CD   . PRO A 1 47  ? 17.842 30.132 39.672 1.00 21.82  ? 50  PRO A CD   1 
ATOM   734  H HA   . PRO A 1 47  ? 18.056 30.503 36.552 0.00 24.53  ? 50  PRO A HA   1 
ATOM   735  H HB2  . PRO A 1 47  ? 19.450 28.469 37.361 0.00 25.47  ? 50  PRO A HB2  1 
ATOM   736  H HB3  . PRO A 1 47  ? 19.876 29.961 37.705 0.00 25.47  ? 50  PRO A HB3  1 
ATOM   737  H HG2  . PRO A 1 47  ? 18.440 28.162 39.419 0.00 28.19  ? 50  PRO A HG2  1 
ATOM   738  H HG3  . PRO A 1 47  ? 19.639 29.112 39.850 0.00 28.19  ? 50  PRO A HG3  1 
ATOM   739  H HD2  . PRO A 1 47  ? 17.222 29.822 40.351 0.00 26.16  ? 50  PRO A HD2  1 
ATOM   740  H HD3  . PRO A 1 47  ? 18.301 30.928 39.981 0.00 26.16  ? 50  PRO A HD3  1 
ATOM   741  N N    . ALA A 1 48  ? 16.036 28.074 37.150 1.00 19.41  ? 51  ALA A N    1 
ATOM   742  C CA   . ALA A 1 48  ? 15.272 27.023 36.444 1.00 20.83  ? 51  ALA A CA   1 
ATOM   743  C C    . ALA A 1 48  ? 14.407 27.682 35.344 1.00 21.92  ? 51  ALA A C    1 
ATOM   744  O O    . ALA A 1 48  ? 14.280 27.156 34.218 1.00 21.84  ? 51  ALA A O    1 
ATOM   745  C CB   . ALA A 1 48  ? 14.389 26.282 37.444 1.00 22.47  ? 51  ALA A CB   1 
ATOM   746  H H    . ALA A 1 48  ? 15.792 28.228 37.960 0.00 23.27  ? 51  ALA A H    1 
ATOM   747  H HA   . ALA A 1 48  ? 15.872 26.376 36.040 0.00 24.98  ? 51  ALA A HA   1 
ATOM   748  H HB1  . ALA A 1 48  ? 13.885 25.600 36.974 0.00 26.94  ? 51  ALA A HB1  1 
ATOM   749  H HB2  . ALA A 1 48  ? 14.952 25.872 38.119 0.00 26.94  ? 51  ALA A HB2  1 
ATOM   750  H HB3  . ALA A 1 48  ? 13.783 26.915 37.859 0.00 26.94  ? 51  ALA A HB3  1 
ATOM   751  N N    . ILE A 1 49  ? 13.822 28.840 35.651 1.00 20.93  ? 52  ILE A N    1 
ATOM   752  C CA   . ILE A 1 49  ? 13.039 29.564 34.624 1.00 19.96  ? 52  ILE A CA   1 
ATOM   753  C C    . ILE A 1 49  ? 13.991 30.052 33.535 1.00 19.00  ? 52  ILE A C    1 
ATOM   754  O O    . ILE A 1 49  ? 13.663 29.964 32.321 1.00 19.99  ? 52  ILE A O    1 
ATOM   755  C CB   . ILE A 1 49  ? 12.291 30.774 35.267 1.00 20.85  ? 52  ILE A CB   1 
ATOM   756  C CG1  . ILE A 1 49  ? 11.163 30.222 36.125 1.00 22.05  ? 52  ILE A CG1  1 
ATOM   757  C CG2  . ILE A 1 49  ? 11.722 31.745 34.157 1.00 23.80  ? 52  ILE A CG2  1 
ATOM   758  C CD1  . ILE A 1 49  ? 10.567 31.360 37.119 1.00 26.97  ? 52  ILE A CD1  1 
ATOM   759  H H    . ILE A 1 49  ? 13.856 29.224 36.420 0.00 25.10  ? 52  ILE A H    1 
ATOM   760  H HA   . ILE A 1 49  ? 12.379 28.963 34.243 0.00 23.94  ? 52  ILE A HA   1 
ATOM   761  H HB   . ILE A 1 49  ? 12.908 31.290 35.810 0.00 25.00  ? 52  ILE A HB   1 
ATOM   762  H HG12 . ILE A 1 49  ? 10.446 29.911 35.551 0.00 26.44  ? 52  ILE A HG12 1 
ATOM   763  H HG13 . ILE A 1 49  ? 11.499 29.489 36.664 0.00 26.44  ? 52  ILE A HG13 1 
ATOM   764  H HG21 . ILE A 1 49  ? 11.113 32.376 34.571 0.00 28.54  ? 52  ILE A HG21 1 
ATOM   765  H HG22 . ILE A 1 49  ? 12.461 32.220 33.744 0.00 28.54  ? 52  ILE A HG22 1 
ATOM   766  H HG23 . ILE A 1 49  ? 11.252 31.221 33.490 0.00 28.54  ? 52  ILE A HG23 1 
ATOM   767  H HD11 . ILE A 1 49  ? 9.898  30.957 37.694 0.00 32.34  ? 52  ILE A HD11 1 
ATOM   768  H HD12 . ILE A 1 49  ? 11.290 31.721 37.655 0.00 32.34  ? 52  ILE A HD12 1 
ATOM   769  H HD13 . ILE A 1 49  ? 10.165 32.065 36.587 0.00 32.34  ? 52  ILE A HD13 1 
ATOM   770  N N    . ALA A 1 50  ? 15.125 30.649 33.929 1.00 19.16  ? 53  ALA A N    1 
ATOM   771  C CA   . ALA A 1 50  ? 16.023 31.164 32.888 1.00 20.66  ? 53  ALA A CA   1 
ATOM   772  C C    . ALA A 1 50  ? 16.562 30.024 32.009 1.00 20.51  ? 53  ALA A C    1 
ATOM   773  O O    . ALA A 1 50  ? 16.741 30.226 30.787 1.00 21.56  ? 53  ALA A O    1 
ATOM   774  C CB   . ALA A 1 50  ? 17.228 31.938 33.547 1.00 23.47  ? 53  ALA A CB   1 
ATOM   775  H H    . ALA A 1 50  ? 15.382 30.761 34.742 0.00 22.97  ? 53  ALA A H    1 
ATOM   776  H HA   . ALA A 1 50  ? 15.526 31.781 32.329 0.00 24.78  ? 53  ALA A HA   1 
ATOM   777  H HB1  . ALA A 1 50  ? 17.811 32.270 32.847 0.00 28.14  ? 53  ALA A HB1  1 
ATOM   778  H HB2  . ALA A 1 50  ? 16.880 32.680 34.067 0.00 28.14  ? 53  ALA A HB2  1 
ATOM   779  H HB3  . ALA A 1 50  ? 17.716 31.330 34.124 0.00 28.14  ? 53  ALA A HB3  1 
ATOM   780  N N    . PHE A 1 51  ? 16.829 28.821 32.603 1.00 19.25  ? 54  PHE A N    1 
ATOM   781  C CA   . PHE A 1 51  ? 17.243 27.647 31.805 1.00 19.83  ? 54  PHE A CA   1 
ATOM   782  C C    . PHE A 1 51  ? 16.227 27.411 30.670 1.00 22.64  ? 54  PHE A C    1 
ATOM   783  O O    . PHE A 1 51  ? 16.638 27.159 29.514 1.00 22.06  ? 54  PHE A O    1 
ATOM   784  C CB   . PHE A 1 51  ? 17.362 26.375 32.712 1.00 21.19  ? 54  PHE A CB   1 
ATOM   785  C CG   . PHE A 1 51  ? 17.392 25.083 31.924 1.00 24.34  ? 54  PHE A CG   1 
ATOM   786  C CD1  . PHE A 1 51  ? 18.577 24.640 31.321 1.00 24.24  ? 54  PHE A CD1  1 
ATOM   787  C CD2  . PHE A 1 51  ? 16.238 24.321 31.761 1.00 26.92  ? 54  PHE A CD2  1 
ATOM   788  C CE1  . PHE A 1 51  ? 18.597 23.409 30.571 1.00 27.26  ? 54  PHE A CE1  1 
ATOM   789  C CE2  . PHE A 1 51  ? 16.234 23.125 31.012 1.00 34.14  ? 54  PHE A CE2  1 
ATOM   790  C CZ   . PHE A 1 51  ? 17.390 22.676 30.419 1.00 30.06  ? 54  PHE A CZ   1 
ATOM   791  H H    . PHE A 1 51  ? 16.776 28.671 33.449 0.00 23.09  ? 54  PHE A H    1 
ATOM   792  H HA   . PHE A 1 51  ? 18.120 27.809 31.424 0.00 23.77  ? 54  PHE A HA   1 
ATOM   793  H HB2  . PHE A 1 51  ? 18.184 26.431 33.225 0.00 25.40  ? 54  PHE A HB2  1 
ATOM   794  H HB3  . PHE A 1 51  ? 16.599 26.343 33.310 0.00 25.40  ? 54  PHE A HB3  1 
ATOM   795  H HD1  . PHE A 1 51  ? 19.355 25.143 31.405 0.00 29.06  ? 54  PHE A HD1  1 
ATOM   796  H HD2  . PHE A 1 51  ? 15.447 24.609 32.158 0.00 32.29  ? 54  PHE A HD2  1 
ATOM   797  H HE1  . PHE A 1 51  ? 19.388 23.099 30.193 0.00 32.70  ? 54  PHE A HE1  1 
ATOM   798  H HE2  . PHE A 1 51  ? 15.447 22.639 30.920 0.00 40.95  ? 54  PHE A HE2  1 
ATOM   799  H HZ   . PHE A 1 51  ? 17.382 21.893 29.917 0.00 36.06  ? 54  PHE A HZ   1 
ATOM   800  N N    . THR A 1 52  ? 14.907 27.382 30.995 1.00 20.36  ? 55  THR A N    1 
ATOM   801  C CA   . THR A 1 52  ? 13.905 27.048 29.966 1.00 19.28  ? 55  THR A CA   1 
ATOM   802  C C    . THR A 1 52  ? 13.892 28.103 28.870 1.00 19.30  ? 55  THR A C    1 
ATOM   803  O O    . THR A 1 52  ? 13.622 27.772 27.693 1.00 21.39  ? 55  THR A O    1 
ATOM   804  C CB   . THR A 1 52  ? 12.473 26.857 30.529 1.00 25.13  ? 55  THR A CB   1 
ATOM   805  O OG1  . THR A 1 52  ? 11.980 28.091 31.020 1.00 28.48  ? 55  THR A OG1  1 
ATOM   806  C CG2  . THR A 1 52  ? 12.530 25.917 31.695 1.00 26.99  ? 55  THR A CG2  1 
ATOM   807  H H    . THR A 1 52  ? 14.585 27.547 31.775 0.00 24.41  ? 55  THR A H    1 
ATOM   808  H HA   . THR A 1 52  ? 14.161 26.186 29.602 0.00 23.11  ? 55  THR A HA   1 
ATOM   809  H HB   . THR A 1 52  ? 11.894 26.515 29.830 0.00 30.14  ? 55  THR A HB   1 
ATOM   810  H HG1  . THR A 1 52  ? 11.202 27.991 31.318 0.00 34.16  ? 55  THR A HG1  1 
ATOM   811  H HG21 . THR A 1 52  ? 11.632 25.671 31.966 0.00 32.36  ? 55  THR A HG21 1 
ATOM   812  H HG22 . THR A 1 52  ? 13.015 25.114 31.450 0.00 32.36  ? 55  THR A HG22 1 
ATOM   813  H HG23 . THR A 1 52  ? 12.980 26.342 32.442 0.00 32.36  ? 55  THR A HG23 1 
ATOM   814  N N    . MET A 1 53  ? 14.108 29.394 29.227 1.00 19.42  ? 56  MET A N    1 
ATOM   815  C CA   . MET A 1 53  ? 13.978 30.447 28.213 1.00 20.46  ? 56  MET A CA   1 
ATOM   816  C C    . MET A 1 53  ? 15.267 30.575 27.401 1.00 20.72  ? 56  MET A C    1 
ATOM   817  O O    . MET A 1 53  ? 15.181 30.782 26.171 1.00 20.81  ? 56  MET A O    1 
ATOM   818  C CB   . MET A 1 53  ? 13.619 31.788 28.920 1.00 20.27  ? 56  MET A CB   1 
ATOM   819  C CG   . MET A 1 53  ? 12.156 31.813 29.431 1.00 23.92  ? 56  MET A CG   1 
ATOM   820  S SD   . MET A 1 53  ? 10.915 31.613 28.189 1.00 30.73  ? 56  MET A SD   1 
ATOM   821  C CE   . MET A 1 53  ? 10.479 29.880 28.353 1.00 40.15  ? 56  MET A CE   1 
ATOM   822  H H    . MET A 1 53  ? 14.321 29.665 30.015 0.00 23.28  ? 56  MET A H    1 
ATOM   823  H HA   . MET A 1 53  ? 13.254 30.244 27.602 0.00 24.54  ? 56  MET A HA   1 
ATOM   824  H HB2  . MET A 1 53  ? 14.207 31.913 29.682 0.00 24.31  ? 56  MET A HB2  1 
ATOM   825  H HB3  . MET A 1 53  ? 13.732 32.518 28.291 0.00 24.31  ? 56  MET A HB3  1 
ATOM   826  H HG2  . MET A 1 53  ? 12.044 31.092 30.070 0.00 28.68  ? 56  MET A HG2  1 
ATOM   827  H HG3  . MET A 1 53  ? 11.998 32.667 29.862 0.00 28.68  ? 56  MET A HG3  1 
ATOM   828  H HE1  . MET A 1 53  ? 9.900  29.629 27.617 0.00 48.16  ? 56  MET A HE1  1 
ATOM   829  H HE2  . MET A 1 53  ? 11.290 29.347 28.333 0.00 48.16  ? 56  MET A HE2  1 
ATOM   830  H HE3  . MET A 1 53  ? 10.018 29.749 29.197 0.00 48.16  ? 56  MET A HE3  1 
ATOM   831  N N    . TYR A 1 54  ? 16.461 30.281 27.988 1.00 18.36  ? 57  TYR A N    1 
ATOM   832  C CA   . TYR A 1 54  ? 17.688 30.134 27.176 1.00 21.23  ? 57  TYR A CA   1 
ATOM   833  C C    . TYR A 1 54  ? 17.532 28.965 26.203 1.00 21.26  ? 57  TYR A C    1 
ATOM   834  O O    . TYR A 1 54  ? 17.931 29.065 25.036 1.00 22.33  ? 57  TYR A O    1 
ATOM   835  C CB   . TYR A 1 54  ? 18.938 29.907 28.106 1.00 18.56  ? 57  TYR A CB   1 
ATOM   836  C CG   . TYR A 1 54  ? 19.627 31.261 28.361 1.00 19.12  ? 57  TYR A CG   1 
ATOM   837  C CD1  . TYR A 1 54  ? 19.242 32.094 29.417 1.00 22.24  ? 57  TYR A CD1  1 
ATOM   838  C CD2  . TYR A 1 54  ? 20.652 31.706 27.479 1.00 22.90  ? 57  TYR A CD2  1 
ATOM   839  C CE1  . TYR A 1 54  ? 19.837 33.365 29.595 1.00 19.48  ? 57  TYR A CE1  1 
ATOM   840  C CE2  . TYR A 1 54  ? 21.303 32.949 27.664 1.00 23.29  ? 57  TYR A CE2  1 
ATOM   841  C CZ   . TYR A 1 54  ? 20.908 33.754 28.722 1.00 21.58  ? 57  TYR A CZ   1 
ATOM   842  O OH   . TYR A 1 54  ? 21.477 35.018 28.881 1.00 23.74  ? 57  TYR A OH   1 
ATOM   843  H H    . TYR A 1 54  ? 16.578 30.165 28.833 0.00 22.02  ? 57  TYR A H    1 
ATOM   844  H HA   . TYR A 1 54  ? 17.840 30.950 26.674 0.00 25.46  ? 57  TYR A HA   1 
ATOM   845  H HB2  . TYR A 1 54  ? 18.654 29.533 28.954 0.00 22.26  ? 57  TYR A HB2  1 
ATOM   846  H HB3  . TYR A 1 54  ? 19.567 29.309 27.673 0.00 22.26  ? 57  TYR A HB3  1 
ATOM   847  H HD1  . TYR A 1 54  ? 18.585 31.808 30.010 0.00 26.67  ? 57  TYR A HD1  1 
ATOM   848  H HD2  . TYR A 1 54  ? 20.900 31.166 26.763 0.00 27.46  ? 57  TYR A HD2  1 
ATOM   849  H HE1  . TYR A 1 54  ? 19.540 33.937 30.266 0.00 23.35  ? 57  TYR A HE1  1 
ATOM   850  H HE2  . TYR A 1 54  ? 21.981 33.220 27.088 0.00 27.93  ? 57  TYR A HE2  1 
ATOM   851  H HH   . TYR A 1 54  ? 21.123 35.412 29.534 0.00 28.47  ? 57  TYR A HH   1 
ATOM   852  N N    . LEU A 1 55  ? 16.971 27.839 26.664 1.00 19.69  ? 58  LEU A N    1 
ATOM   853  C CA   . LEU A 1 55  ? 16.826 26.708 25.729 1.00 22.05  ? 58  LEU A CA   1 
ATOM   854  C C    . LEU A 1 55  ? 15.900 27.113 24.594 1.00 21.11  ? 58  LEU A C    1 
ATOM   855  O O    . LEU A 1 55  ? 16.129 26.717 23.427 1.00 23.03  ? 58  LEU A O    1 
ATOM   856  C CB   . LEU A 1 55  ? 16.260 25.463 26.485 1.00 20.33  ? 58  LEU A CB   1 
ATOM   857  C CG   . LEU A 1 55  ? 16.096 24.173 25.609 1.00 22.03  ? 58  LEU A CG   1 
ATOM   858  C CD1  . LEU A 1 55  ? 17.487 23.657 25.007 1.00 26.81  ? 58  LEU A CD1  1 
ATOM   859  C CD2  . LEU A 1 55  ? 15.457 23.113 26.463 1.00 25.41  ? 58  LEU A CD2  1 
ATOM   860  H H    . LEU A 1 55  ? 16.683 27.710 27.464 0.00 23.61  ? 58  LEU A H    1 
ATOM   861  H HA   . LEU A 1 55  ? 17.689 26.458 25.365 0.00 26.45  ? 58  LEU A HA   1 
ATOM   862  H HB2  . LEU A 1 55  ? 16.864 25.246 27.212 0.00 24.37  ? 58  LEU A HB2  1 
ATOM   863  H HB3  . LEU A 1 55  ? 15.385 25.690 26.836 0.00 24.37  ? 58  LEU A HB3  1 
ATOM   864  H HG   . LEU A 1 55  ? 15.537 24.371 24.841 0.00 26.41  ? 58  LEU A HG   1 
ATOM   865  H HD11 . LEU A 1 55  ? 17.336 22.829 24.525 0.00 32.16  ? 58  LEU A HD11 1 
ATOM   866  H HD12 . LEU A 1 55  ? 17.840 24.330 24.404 0.00 32.16  ? 58  LEU A HD12 1 
ATOM   867  H HD13 . LEU A 1 55  ? 18.110 23.506 25.735 0.00 32.16  ? 58  LEU A HD13 1 
ATOM   868  H HD21 . LEU A 1 55  ? 15.339 22.309 25.934 0.00 30.47  ? 58  LEU A HD21 1 
ATOM   869  H HD22 . LEU A 1 55  ? 16.034 22.928 27.221 0.00 30.47  ? 58  LEU A HD22 1 
ATOM   870  H HD23 . LEU A 1 55  ? 14.596 23.434 26.774 0.00 30.47  ? 58  LEU A HD23 1 
ATOM   871  N N    . SER A 1 56  ? 14.823 27.868 24.895 1.00 19.15  ? 59  SER A N    1 
ATOM   872  C CA   . SER A 1 56  ? 13.883 28.206 23.825 1.00 19.54  ? 59  SER A CA   1 
ATOM   873  C C    . SER A 1 56  ? 14.563 29.135 22.809 1.00 23.81  ? 59  SER A C    1 
ATOM   874  O O    . SER A 1 56  ? 14.233 29.113 21.635 1.00 24.12  ? 59  SER A O    1 
ATOM   875  C CB   . SER A 1 56  ? 12.614 28.927 24.369 1.00 25.80  ? 59  SER A CB   1 
ATOM   876  O OG   . SER A 1 56  ? 12.869 30.312 24.623 1.00 28.67  ? 59  SER A OG   1 
ATOM   877  H H    . SER A 1 56  ? 14.630 28.179 25.673 0.00 22.96  ? 59  SER A H    1 
ATOM   878  H HA   . SER A 1 56  ? 13.594 27.378 23.410 0.00 23.43  ? 59  SER A HA   1 
ATOM   879  H HB2  . SER A 1 56  ? 11.906 28.855 23.710 0.00 30.94  ? 59  SER A HB2  1 
ATOM   880  H HB3  . SER A 1 56  ? 12.342 28.502 25.197 0.00 30.94  ? 59  SER A HB3  1 
ATOM   881  H HG   . SER A 1 56  ? 13.460 30.392 25.214 0.00 34.38  ? 59  SER A HG   1 
ATOM   882  N N    . MET A 1 57  ? 15.502 29.980 23.270 1.00 22.00  ? 60  MET A N    1 
ATOM   883  C CA   . MET A 1 57  ? 16.221 30.823 22.313 1.00 21.43  ? 60  MET A CA   1 
ATOM   884  C C    . MET A 1 57  ? 17.198 29.996 21.497 1.00 22.38  ? 60  MET A C    1 
ATOM   885  O O    . MET A 1 57  ? 17.297 30.203 20.281 1.00 23.63  ? 60  MET A O    1 
ATOM   886  C CB   . MET A 1 57  ? 17.008 31.959 23.052 1.00 21.66  ? 60  MET A CB   1 
ATOM   887  C CG   . MET A 1 57  ? 16.015 32.967 23.575 1.00 21.73  ? 60  MET A CG   1 
ATOM   888  S SD   . MET A 1 57  ? 16.835 34.485 24.357 1.00 26.87  ? 60  MET A SD   1 
ATOM   889  C CE   . MET A 1 57  ? 17.404 33.824 25.956 1.00 30.02  ? 60  MET A CE   1 
ATOM   890  H H    . MET A 1 57  ? 15.728 30.077 24.094 0.00 26.38  ? 60  MET A H    1 
ATOM   891  H HA   . MET A 1 57  ? 15.564 31.239 21.733 0.00 25.70  ? 60  MET A HA   1 
ATOM   892  H HB2  . MET A 1 57  ? 17.507 31.587 23.796 0.00 25.97  ? 60  MET A HB2  1 
ATOM   893  H HB3  . MET A 1 57  ? 17.613 32.399 22.434 0.00 25.97  ? 60  MET A HB3  1 
ATOM   894  H HG2  . MET A 1 57  ? 15.461 33.274 22.840 0.00 26.06  ? 60  MET A HG2  1 
ATOM   895  H HG3  . MET A 1 57  ? 15.464 32.544 24.252 0.00 26.06  ? 60  MET A HG3  1 
ATOM   896  H HE1  . MET A 1 57  ? 17.850 34.530 26.449 0.00 36.00  ? 60  MET A HE1  1 
ATOM   897  H HE2  . MET A 1 57  ? 16.637 33.505 26.456 0.00 36.00  ? 60  MET A HE2  1 
ATOM   898  H HE3  . MET A 1 57  ? 18.021 33.093 25.794 0.00 36.00  ? 60  MET A HE3  1 
ATOM   899  N N    . LEU A 1 58  ? 17.919 29.058 22.148 1.00 21.49  ? 61  LEU A N    1 
ATOM   900  C CA   . LEU A 1 58  ? 18.869 28.213 21.388 1.00 21.85  ? 61  LEU A CA   1 
ATOM   901  C C    . LEU A 1 58  ? 18.148 27.448 20.276 1.00 28.81  ? 61  LEU A C    1 
ATOM   902  O O    . LEU A 1 58  ? 18.671 27.320 19.159 1.00 27.38  ? 61  LEU A O    1 
ATOM   903  C CB   . LEU A 1 58  ? 19.541 27.231 22.378 1.00 21.47  ? 61  LEU A CB   1 
ATOM   904  C CG   . LEU A 1 58  ? 20.517 26.192 21.769 1.00 25.30  ? 61  LEU A CG   1 
ATOM   905  C CD1  . LEU A 1 58  ? 21.722 26.923 21.231 1.00 29.45  ? 61  LEU A CD1  1 
ATOM   906  C CD2  . LEU A 1 58  ? 20.914 25.166 22.843 1.00 30.29  ? 61  LEU A CD2  1 
ATOM   907  H H    . LEU A 1 58  ? 17.880 28.897 22.992 0.00 25.77  ? 61  LEU A H    1 
ATOM   908  H HA   . LEU A 1 58  ? 19.551 28.763 20.972 0.00 26.20  ? 61  LEU A HA   1 
ATOM   909  H HB2  . LEU A 1 58  ? 20.046 27.753 23.021 0.00 25.75  ? 61  LEU A HB2  1 
ATOM   910  H HB3  . LEU A 1 58  ? 18.842 26.734 22.829 0.00 25.75  ? 61  LEU A HB3  1 
ATOM   911  H HG   . LEU A 1 58  ? 20.102 25.704 21.040 0.00 30.34  ? 61  LEU A HG   1 
ATOM   912  H HD11 . LEU A 1 58  ? 22.373 26.274 20.921 0.00 35.32  ? 61  LEU A HD11 1 
ATOM   913  H HD12 . LEU A 1 58  ? 21.445 27.491 20.495 0.00 35.32  ? 61  LEU A HD12 1 
ATOM   914  H HD13 . LEU A 1 58  ? 22.106 27.464 21.940 0.00 35.32  ? 61  LEU A HD13 1 
ATOM   915  H HD21 . LEU A 1 58  ? 21.499 24.502 22.445 0.00 36.33  ? 61  LEU A HD21 1 
ATOM   916  H HD22 . LEU A 1 58  ? 21.375 25.624 23.563 0.00 36.33  ? 61  LEU A HD22 1 
ATOM   917  H HD23 . LEU A 1 58  ? 20.112 24.738 23.183 0.00 36.33  ? 61  LEU A HD23 1 
ATOM   918  N N    . LEU A 1 59  ? 16.953 26.877 20.575 1.00 23.21  ? 62  LEU A N    1 
ATOM   919  C CA   . LEU A 1 59  ? 16.249 26.055 19.584 1.00 22.90  ? 62  LEU A CA   1 
ATOM   920  C C    . LEU A 1 59  ? 15.470 26.893 18.574 1.00 28.01  ? 62  LEU A C    1 
ATOM   921  O O    . LEU A 1 59  ? 14.959 26.315 17.595 1.00 32.38  ? 62  LEU A O    1 
ATOM   922  C CB   . LEU A 1 59  ? 15.261 25.057 20.273 1.00 25.61  ? 62  LEU A CB   1 
ATOM   923  C CG   . LEU A 1 59  ? 15.899 24.117 21.283 1.00 26.07  ? 62  LEU A CG   1 
ATOM   924  C CD1  . LEU A 1 59  ? 14.843 23.205 21.899 1.00 28.33  ? 62  LEU A CD1  1 
ATOM   925  C CD2  . LEU A 1 59  ? 16.975 23.232 20.559 1.00 32.44  ? 62  LEU A CD2  1 
ATOM   926  H H    . LEU A 1 59  ? 16.547 26.954 21.330 0.00 27.84  ? 62  LEU A H    1 
ATOM   927  H HA   . LEU A 1 59  ? 16.914 25.530 19.111 0.00 27.46  ? 62  LEU A HA   1 
ATOM   928  H HB2  . LEU A 1 59  ? 14.583 25.571 20.740 0.00 30.72  ? 62  LEU A HB2  1 
ATOM   929  H HB3  . LEU A 1 59  ? 14.849 24.511 19.586 0.00 30.72  ? 62  LEU A HB3  1 
ATOM   930  H HG   . LEU A 1 59  ? 16.317 24.636 21.988 0.00 31.27  ? 62  LEU A HG   1 
ATOM   931  H HD11 . LEU A 1 59  ? 15.275 22.590 22.512 0.00 33.97  ? 62  LEU A HD11 1 
ATOM   932  H HD12 . LEU A 1 59  ? 14.196 23.749 22.376 0.00 33.97  ? 62  LEU A HD12 1 
ATOM   933  H HD13 . LEU A 1 59  ? 14.401 22.711 21.191 0.00 33.97  ? 62  LEU A HD13 1 
ATOM   934  H HD21 . LEU A 1 59  ? 17.293 22.555 21.176 0.00 38.91  ? 62  LEU A HD21 1 
ATOM   935  H HD22 . LEU A 1 59  ? 16.568 22.811 19.786 0.00 38.91  ? 62  LEU A HD22 1 
ATOM   936  H HD23 . LEU A 1 59  ? 17.711 23.797 20.279 0.00 38.91  ? 62  LEU A HD23 1 
ATOM   937  N N    . GLY A 1 60  ? 15.426 28.209 18.759 1.00 30.25  ? 63  GLY A N    1 
ATOM   938  C CA   . GLY A 1 60  ? 14.865 29.134 17.791 1.00 30.79  ? 63  GLY A CA   1 
ATOM   939  C C    . GLY A 1 60  ? 13.403 29.516 18.031 1.00 31.25  ? 63  GLY A C    1 
ATOM   940  O O    . GLY A 1 60  ? 12.841 30.294 17.216 1.00 31.81  ? 63  GLY A O    1 
ATOM   941  H H    . GLY A 1 60  ? 15.727 28.600 19.463 0.00 36.28  ? 63  GLY A H    1 
ATOM   942  H HA2  . GLY A 1 60  ? 15.388 29.951 17.803 0.00 36.93  ? 63  GLY A HA2  1 
ATOM   943  H HA3  . GLY A 1 60  ? 14.924 28.734 16.909 0.00 36.93  ? 63  GLY A HA3  1 
ATOM   944  N N    . TYR A 1 61  ? 12.765 28.980 19.078 1.00 30.86  ? 64  TYR A N    1 
ATOM   945  C CA   . TYR A 1 61  ? 11.349 29.263 19.351 1.00 31.51  ? 64  TYR A CA   1 
ATOM   946  C C    . TYR A 1 61  ? 11.166 30.697 19.874 1.00 29.98  ? 64  TYR A C    1 
ATOM   947  O O    . TYR A 1 61  ? 10.153 31.349 19.569 1.00 32.71  ? 64  TYR A O    1 
ATOM   948  C CB   . TYR A 1 61  ? 10.801 28.211 20.381 1.00 32.09  ? 64  TYR A CB   1 
ATOM   949  C CG   . TYR A 1 61  ? 9.320  28.373 20.669 1.00 33.25  ? 64  TYR A CG   1 
ATOM   950  C CD1  . TYR A 1 61  ? 8.358  27.792 19.866 1.00 35.80  ? 64  TYR A CD1  1 
ATOM   951  C CD2  . TYR A 1 61  ? 8.893  29.169 21.753 1.00 32.07  ? 64  TYR A CD2  1 
ATOM   952  C CE1  . TYR A 1 61  ? 6.992  27.983 20.102 1.00 43.78  ? 64  TYR A CE1  1 
ATOM   953  C CE2  . TYR A 1 61  ? 7.495  29.383 21.981 1.00 33.45  ? 64  TYR A CE2  1 
ATOM   954  C CZ   . TYR A 1 61  ? 6.588  28.778 21.184 1.00 37.17  ? 64  TYR A CZ   1 
ATOM   955  O OH   . TYR A 1 61  ? 5.222  28.922 21.365 1.00 46.33  ? 64  TYR A OH   1 
ATOM   956  H H    . TYR A 1 61  ? 13.128 28.448 19.648 0.00 37.02  ? 64  TYR A H    1 
ATOM   957  H HA   . TYR A 1 61  ? 10.834 29.182 18.532 0.00 37.80  ? 64  TYR A HA   1 
ATOM   958  H HB2  . TYR A 1 61  ? 10.941 27.319 20.024 0.00 38.49  ? 64  TYR A HB2  1 
ATOM   959  H HB3  . TYR A 1 61  ? 11.281 28.311 21.218 0.00 38.49  ? 64  TYR A HB3  1 
ATOM   960  H HD1  . TYR A 1 61  ? 8.625  27.260 19.151 0.00 42.94  ? 64  TYR A HD1  1 
ATOM   961  H HD2  . TYR A 1 61  ? 9.520  29.555 22.321 0.00 38.46  ? 64  TYR A HD2  1 
ATOM   962  H HE1  . TYR A 1 61  ? 6.359  27.588 19.547 0.00 52.52  ? 64  TYR A HE1  1 
ATOM   963  H HE2  . TYR A 1 61  ? 7.213  29.936 22.673 0.00 40.13  ? 64  TYR A HE2  1 
ATOM   964  H HH   . TYR A 1 61  ? 5.070  29.404 22.037 0.00 55.58  ? 64  TYR A HH   1 
ATOM   965  N N    . GLY A 1 62  ? 12.111 31.173 20.644 1.00 28.15  ? 65  GLY A N    1 
ATOM   966  C CA   . GLY A 1 62  ? 11.948 32.444 21.373 1.00 31.72  ? 65  GLY A CA   1 
ATOM   967  C C    . GLY A 1 62  ? 12.472 33.653 20.589 1.00 30.77  ? 65  GLY A C    1 
ATOM   968  O O    . GLY A 1 62  ? 12.910 34.642 21.196 1.00 27.86  ? 65  GLY A O    1 
ATOM   969  H H    . GLY A 1 62  ? 12.870 30.790 20.775 0.00 33.76  ? 65  GLY A H    1 
ATOM   970  H HA2  . GLY A 1 62  ? 11.006 32.587 21.557 0.00 38.05  ? 65  GLY A HA2  1 
ATOM   971  H HA3  . GLY A 1 62  ? 12.430 32.394 22.213 0.00 38.05  ? 65  GLY A HA3  1 
ATOM   972  N N    . LEU A 1 63  ? 12.481 33.540 19.261 1.00 29.07  ? 66  LEU A N    1 
ATOM   973  C CA   . LEU A 1 63  ? 12.983 34.605 18.362 1.00 28.29  ? 66  LEU A CA   1 
ATOM   974  C C    . LEU A 1 63  ? 11.874 34.998 17.401 1.00 33.12  ? 66  LEU A C    1 
ATOM   975  O O    . LEU A 1 63  ? 11.146 34.121 16.881 1.00 34.34  ? 66  LEU A O    1 
ATOM   976  C CB   . LEU A 1 63  ? 14.222 34.059 17.616 1.00 28.86  ? 66  LEU A CB   1 
ATOM   977  C CG   . LEU A 1 63  ? 14.844 34.834 16.487 1.00 34.46  ? 66  LEU A CG   1 
ATOM   978  C CD1  . LEU A 1 63  ? 15.427 36.120 17.052 1.00 36.23  ? 66  LEU A CD1  1 
ATOM   979  C CD2  . LEU A 1 63  ? 15.923 33.979 15.809 1.00 43.83  ? 66  LEU A CD2  1 
ATOM   980  H H    . LEU A 1 63  ? 12.198 32.846 18.841 0.00 34.87  ? 66  LEU A H    1 
ATOM   981  H HA   . LEU A 1 63  ? 13.235 35.411 18.839 0.00 33.93  ? 66  LEU A HA   1 
ATOM   982  H HB2  . LEU A 1 63  ? 14.923 33.943 18.276 0.00 34.62  ? 66  LEU A HB2  1 
ATOM   983  H HB3  . LEU A 1 63  ? 13.972 33.199 17.242 0.00 34.62  ? 66  LEU A HB3  1 
ATOM   984  H HG   . LEU A 1 63  ? 14.186 35.062 15.812 0.00 41.34  ? 66  LEU A HG   1 
ATOM   985  H HD11 . LEU A 1 63  ? 15.824 36.630 16.329 0.00 43.45  ? 66  LEU A HD11 1 
ATOM   986  H HD12 . LEU A 1 63  ? 14.717 36.633 17.468 0.00 43.45  ? 66  LEU A HD12 1 
ATOM   987  H HD13 . LEU A 1 63  ? 16.104 35.897 17.711 0.00 43.45  ? 66  LEU A HD13 1 
ATOM   988  H HD21 . LEU A 1 63  ? 16.332 34.494 15.095 0.00 52.58  ? 66  LEU A HD21 1 
ATOM   989  H HD22 . LEU A 1 63  ? 16.593 33.735 16.466 0.00 52.58  ? 66  LEU A HD22 1 
ATOM   990  H HD23 . LEU A 1 63  ? 15.511 33.179 15.445 0.00 52.58  ? 66  LEU A HD23 1 
ATOM   991  N N    . THR A 1 64  ? 11.746 36.317 17.101 1.00 30.42  ? 67  THR A N    1 
ATOM   992  C CA   . THR A 1 64  ? 10.815 36.792 16.087 1.00 32.38  ? 67  THR A CA   1 
ATOM   993  C C    . THR A 1 64  ? 11.476 37.907 15.260 1.00 33.06  ? 67  THR A C    1 
ATOM   994  O O    . THR A 1 64  ? 12.521 38.431 15.623 1.00 35.11  ? 67  THR A O    1 
ATOM   995  C CB   . THR A 1 64  ? 9.498  37.266 16.740 1.00 32.84  ? 67  THR A CB   1 
ATOM   996  O OG1  . THR A 1 64  ? 8.511  37.426 15.711 1.00 37.78  ? 67  THR A OG1  1 
ATOM   997  C CG2  . THR A 1 64  ? 9.649  38.610 17.512 1.00 33.93  ? 67  THR A CG2  1 
ATOM   998  H H    . THR A 1 64  ? 12.196 36.944 17.482 0.00 36.49  ? 67  THR A H    1 
ATOM   999  H HA   . THR A 1 64  ? 10.607 36.075 15.468 0.00 38.83  ? 67  THR A HA   1 
ATOM   1000 H HB   . THR A 1 64  ? 9.224  36.602 17.392 0.00 39.39  ? 67  THR A HB   1 
ATOM   1001 H HG1  . THR A 1 64  ? 7.791  37.701 16.044 0.00 45.31  ? 67  THR A HG1  1 
ATOM   1002 H HG21 . THR A 1 64  ? 8.807  38.848 17.931 0.00 40.69  ? 67  THR A HG21 1 
ATOM   1003 H HG22 . THR A 1 64  ? 10.329 38.524 18.198 0.00 40.69  ? 67  THR A HG22 1 
ATOM   1004 H HG23 . THR A 1 64  ? 9.906  39.317 16.900 0.00 40.69  ? 67  THR A HG23 1 
ATOM   1005 N N    . MET A 1 65  ? 10.903 38.262 14.118 1.00 35.13  ? 68  MET A N    1 
ATOM   1006 C CA   . MET A 1 65  ? 11.488 39.345 13.294 1.00 36.22  ? 68  MET A CA   1 
ATOM   1007 C C    . MET A 1 65  ? 10.596 40.582 13.337 1.00 43.36  ? 68  MET A C    1 
ATOM   1008 O O    . MET A 1 65  ? 9.390  40.487 13.088 1.00 41.10  ? 68  MET A O    1 
ATOM   1009 C CB   . MET A 1 65  ? 11.708 38.922 11.838 1.00 39.67  ? 68  MET A CB   1 
ATOM   1010 C CG   . MET A 1 65  ? 12.443 37.576 11.775 1.00 58.36  ? 68  MET A CG   1 
ATOM   1011 S SD   . MET A 1 65  ? 14.269 37.786 11.950 1.00 58.07  ? 68  MET A SD   1 
ATOM   1012 C CE   . MET A 1 65  ? 14.666 39.328 11.159 1.00 62.47  ? 68  MET A CE   1 
ATOM   1013 H H    . MET A 1 65  ? 10.189 37.906 13.796 0.00 42.14  ? 68  MET A H    1 
ATOM   1014 H HA   . MET A 1 65  ? 12.356 39.557 13.672 0.00 43.45  ? 68  MET A HA   1 
ATOM   1015 H HB2  . MET A 1 65  ? 10.851 38.828 11.394 0.00 47.58  ? 68  MET A HB2  1 
ATOM   1016 H HB3  . MET A 1 65  ? 12.245 39.590 11.384 0.00 47.58  ? 68  MET A HB3  1 
ATOM   1017 H HG2  . MET A 1 65  ? 12.132 37.007 12.497 0.00 70.01  ? 68  MET A HG2  1 
ATOM   1018 H HG3  . MET A 1 65  ? 12.266 37.154 10.920 0.00 70.01  ? 68  MET A HG3  1 
ATOM   1019 H HE1  . MET A 1 65  ? 15.628 39.452 11.174 0.00 74.94  ? 68  MET A HE1  1 
ATOM   1020 H HE2  . MET A 1 65  ? 14.351 39.303 10.242 0.00 74.94  ? 68  MET A HE2  1 
ATOM   1021 H HE3  . MET A 1 65  ? 14.232 40.050 11.639 0.00 74.94  ? 68  MET A HE3  1 
ATOM   1022 N N    . VAL A 1 66  ? 11.189 41.733 13.643 1.00 37.40  ? 69  VAL A N    1 
ATOM   1023 C CA   . VAL A 1 66  ? 10.428 42.979 13.805 1.00 38.63  ? 69  VAL A CA   1 
ATOM   1024 C C    . VAL A 1 66  ? 10.937 43.957 12.744 1.00 40.69  ? 69  VAL A C    1 
ATOM   1025 O O    . VAL A 1 66  ? 12.133 44.265 12.706 1.00 40.32  ? 69  VAL A O    1 
ATOM   1026 C CB   . VAL A 1 66  ? 10.542 43.584 15.217 1.00 37.36  ? 69  VAL A CB   1 
ATOM   1027 C CG1  . VAL A 1 66  ? 9.714  44.904 15.291 1.00 42.33  ? 69  VAL A CG1  1 
ATOM   1028 C CG2  . VAL A 1 66  ? 10.071 42.595 16.334 1.00 35.90  ? 69  VAL A CG2  1 
ATOM   1029 H H    . VAL A 1 66  ? 12.036 41.821 13.764 0.00 44.86  ? 69  VAL A H    1 
ATOM   1030 H HA   . VAL A 1 66  ? 9.488  42.801 13.647 0.00 46.34  ? 69  VAL A HA   1 
ATOM   1031 H HB   . VAL A 1 66  ? 11.479 43.772 15.383 0.00 44.82  ? 69  VAL A HB   1 
ATOM   1032 H HG11 . VAL A 1 66  ? 9.648  45.184 16.218 0.00 50.78  ? 69  VAL A HG11 1 
ATOM   1033 H HG12 . VAL A 1 66  ? 10.162 45.588 14.770 0.00 50.78  ? 69  VAL A HG12 1 
ATOM   1034 H HG13 . VAL A 1 66  ? 8.828  44.742 14.932 0.00 50.78  ? 69  VAL A HG13 1 
ATOM   1035 H HG21 . VAL A 1 66  ? 10.167 43.025 17.198 0.00 43.06  ? 69  VAL A HG21 1 
ATOM   1036 H HG22 . VAL A 1 66  ? 9.142  42.364 16.180 0.00 43.06  ? 69  VAL A HG22 1 
ATOM   1037 H HG23 . VAL A 1 66  ? 10.620 41.796 16.299 0.00 43.06  ? 69  VAL A HG23 1 
ATOM   1038 N N    . PRO A 1 67  ? 10.085 44.463 11.849 1.00 43.16  ? 70  PRO A N    1 
ATOM   1039 C CA   . PRO A 1 67  ? 10.555 45.441 10.870 1.00 45.47  ? 70  PRO A CA   1 
ATOM   1040 C C    . PRO A 1 67  ? 10.646 46.820 11.509 1.00 54.52  ? 70  PRO A C    1 
ATOM   1041 O O    . PRO A 1 67  ? 9.693  47.286 12.133 1.00 52.59  ? 70  PRO A O    1 
ATOM   1042 C CB   . PRO A 1 67  ? 9.475  45.408 9.788  1.00 48.92  ? 70  PRO A CB   1 
ATOM   1043 C CG   . PRO A 1 67  ? 8.218  45.100 10.550 1.00 47.49  ? 70  PRO A CG   1 
ATOM   1044 C CD   . PRO A 1 67  ? 8.630  44.230 11.731 1.00 44.31  ? 70  PRO A CD   1 
ATOM   1045 H HA   . PRO A 1 67  ? 11.411 45.184 10.493 0.00 54.55  ? 70  PRO A HA   1 
ATOM   1046 H HB2  . PRO A 1 67  ? 9.416  46.269 9.346  0.00 58.69  ? 70  PRO A HB2  1 
ATOM   1047 H HB3  . PRO A 1 67  ? 9.671  44.714 9.139  0.00 58.69  ? 70  PRO A HB3  1 
ATOM   1048 H HG2  . PRO A 1 67  ? 7.816  45.926 10.860 0.00 56.96  ? 70  PRO A HG2  1 
ATOM   1049 H HG3  . PRO A 1 67  ? 7.599  44.624 9.976  0.00 56.96  ? 70  PRO A HG3  1 
ATOM   1050 H HD2  . PRO A 1 67  ? 8.171  44.509 12.539 0.00 53.15  ? 70  PRO A HD2  1 
ATOM   1051 H HD3  . PRO A 1 67  ? 8.445  43.295 11.550 0.00 53.15  ? 70  PRO A HD3  1 
ATOM   1052 N N    . PHE A 1 68  ? 11.805 47.451 11.370 1.00 49.83  ? 71  PHE A N    1 
ATOM   1053 C CA   . PHE A 1 68  ? 11.975 48.870 11.673 1.00 50.29  ? 71  PHE A CA   1 
ATOM   1054 C C    . PHE A 1 68  ? 13.279 49.325 11.015 1.00 60.11  ? 71  PHE A C    1 
ATOM   1055 O O    . PHE A 1 68  ? 14.211 48.536 10.812 1.00 53.40  ? 71  PHE A O    1 
ATOM   1056 C CB   . PHE A 1 68  ? 11.915 49.160 13.195 1.00 50.35  ? 71  PHE A CB   1 
ATOM   1057 C CG   . PHE A 1 68  ? 12.990 48.482 14.028 1.00 44.20  ? 71  PHE A CG   1 
ATOM   1058 C CD1  . PHE A 1 68  ? 14.281 49.008 14.084 1.00 54.54  ? 71  PHE A CD1  1 
ATOM   1059 C CD2  . PHE A 1 68  ? 12.698 47.351 14.768 1.00 41.52  ? 71  PHE A CD2  1 
ATOM   1060 C CE1  . PHE A 1 68  ? 15.262 48.410 14.863 1.00 43.44  ? 71  PHE A CE1  1 
ATOM   1061 C CE2  . PHE A 1 68  ? 13.681 46.719 15.545 1.00 41.17  ? 71  PHE A CE2  1 
ATOM   1062 C CZ   . PHE A 1 68  ? 14.978 47.252 15.607 1.00 41.78  ? 71  PHE A CZ   1 
ATOM   1063 H H    . PHE A 1 68  ? 12.527 47.073 11.095 0.00 59.78  ? 71  PHE A H    1 
ATOM   1064 H HA   . PHE A 1 68  ? 11.256 49.395 11.289 0.00 60.33  ? 71  PHE A HA   1 
ATOM   1065 H HB2  . PHE A 1 68  ? 12.005 50.116 13.327 0.00 60.40  ? 71  PHE A HB2  1 
ATOM   1066 H HB3  . PHE A 1 68  ? 11.056 48.858 13.530 0.00 60.40  ? 71  PHE A HB3  1 
ATOM   1067 H HD1  . PHE A 1 68  ? 14.487 49.769 13.592 0.00 65.42  ? 71  PHE A HD1  1 
ATOM   1068 H HD2  . PHE A 1 68  ? 11.836 47.002 14.749 0.00 49.80  ? 71  PHE A HD2  1 
ATOM   1069 H HE1  . PHE A 1 68  ? 16.115 48.780 14.893 0.00 52.11  ? 71  PHE A HE1  1 
ATOM   1070 H HE2  . PHE A 1 68  ? 13.472 45.947 16.020 0.00 49.38  ? 71  PHE A HE2  1 
ATOM   1071 H HZ   . PHE A 1 68  ? 15.634 46.848 16.128 0.00 50.12  ? 71  PHE A HZ   1 
ATOM   1072 N N    . GLY A 1 69  ? 13.315 50.598 10.631 1.00 72.05  ? 72  GLY A N    1 
ATOM   1073 C CA   . GLY A 1 69  ? 14.454 51.088 9.871  1.00 67.86  ? 72  GLY A CA   1 
ATOM   1074 C C    . GLY A 1 69  ? 14.638 50.396 8.536  1.00 73.69  ? 72  GLY A C    1 
ATOM   1075 O O    . GLY A 1 69  ? 15.773 50.259 8.055  1.00 70.57  ? 72  GLY A O    1 
ATOM   1076 H H    . GLY A 1 69  ? 12.706 51.182 10.795 0.00 86.44  ? 72  GLY A H    1 
ATOM   1077 H HA2  . GLY A 1 69  ? 14.337 52.037 9.704  0.00 81.41  ? 72  GLY A HA2  1 
ATOM   1078 H HA3  . GLY A 1 69  ? 15.261 50.956 10.392 0.00 81.41  ? 72  GLY A HA3  1 
ATOM   1079 N N    . GLY A 1 70  ? 13.550 49.961 7.913  1.00 63.96  ? 73  GLY A N    1 
ATOM   1080 C CA   . GLY A 1 70  ? 13.675 49.348 6.611  1.00 63.64  ? 73  GLY A CA   1 
ATOM   1081 C C    . GLY A 1 70  ? 14.437 48.050 6.594  1.00 80.51  ? 73  GLY A C    1 
ATOM   1082 O O    . GLY A 1 70  ? 14.983 47.683 5.551  1.00 76.84  ? 73  GLY A O    1 
ATOM   1083 H H    . GLY A 1 70  ? 12.748 50.011 8.219  0.00 76.73  ? 73  GLY A H    1 
ATOM   1084 H HA2  . GLY A 1 70  ? 12.787 49.173 6.262  0.00 76.34  ? 73  GLY A HA2  1 
ATOM   1085 H HA3  . GLY A 1 70  ? 14.131 49.966 6.018  0.00 76.34  ? 73  GLY A HA3  1 
ATOM   1086 N N    . GLU A 1 71  ? 14.503 47.351 7.728  1.00 60.22  ? 74  GLU A N    1 
ATOM   1087 C CA   . GLU A 1 71  ? 15.136 46.043 7.823  1.00 56.96  ? 74  GLU A CA   1 
ATOM   1088 C C    . GLU A 1 71  ? 14.201 45.123 8.588  1.00 53.61  ? 74  GLU A C    1 
ATOM   1089 O O    . GLU A 1 71  ? 13.282 45.587 9.261  1.00 47.67  ? 74  GLU A O    1 
ATOM   1090 C CB   . GLU A 1 71  ? 16.483 46.101 8.560  1.00 60.64  ? 74  GLU A CB   1 
ATOM   1091 H H    . GLU A 1 71  ? 14.178 47.625 8.475  0.00 72.24  ? 74  GLU A H    1 
ATOM   1092 H HA   . GLU A 1 71  ? 15.295 45.696 6.932  0.00 68.34  ? 74  GLU A HA   1 
ATOM   1093 N N    . GLN A 1 72  ? 14.434 43.814 8.471  1.00 46.82  ? 75  GLN A N    1 
ATOM   1094 C CA   . GLN A 1 72  ? 13.852 42.845 9.411  1.00 48.51  ? 75  GLN A CA   1 
ATOM   1095 C C    . GLN A 1 72  ? 14.862 42.519 10.501 1.00 49.22  ? 75  GLN A C    1 
ATOM   1096 O O    . GLN A 1 72  ? 15.935 41.975 10.233 1.00 52.37  ? 75  GLN A O    1 
ATOM   1097 C CB   . GLN A 1 72  ? 13.386 41.571 8.709  1.00 74.39  ? 75  GLN A CB   1 
ATOM   1098 C CG   . GLN A 1 72  ? 12.722 41.798 7.379  1.00 78.93  ? 75  GLN A CG   1 
ATOM   1099 C CD   . GLN A 1 72  ? 11.217 41.779 7.512  1.00 90.48  ? 75  GLN A CD   1 
ATOM   1100 O OE1  . GLN A 1 72  ? 10.641 40.802 7.990  1.00 99.65  ? 75  GLN A OE1  1 
ATOM   1101 N NE2  . GLN A 1 72  ? 10.567 42.859 7.078  1.00 91.53  ? 75  GLN A NE2  1 
ATOM   1102 H H    . GLN A 1 72  ? 14.924 43.462 7.859  0.00 56.16  ? 75  GLN A H    1 
ATOM   1103 H HA   . GLN A 1 72  ? 13.075 43.253 9.824  0.00 58.20  ? 75  GLN A HA   1 
ATOM   1104 H HB2  . GLN A 1 72  ? 14.158 41.002 8.558  0.00 89.25  ? 75  GLN A HB2  1 
ATOM   1105 H HB3  . GLN A 1 72  ? 12.748 41.118 9.282  0.00 89.25  ? 75  GLN A HB3  1 
ATOM   1106 H HG2  . GLN A 1 72  ? 12.988 42.663 7.029  0.00 94.70  ? 75  GLN A HG2  1 
ATOM   1107 H HG3  . GLN A 1 72  ? 12.985 41.096 6.763  0.00 94.70  ? 75  GLN A HG3  1 
ATOM   1108 H HE21 . GLN A 1 72  ? 11.005 43.519 6.743  0.00 109.81 ? 75  GLN A HE21 1 
ATOM   1109 H HE22 . GLN A 1 72  ? 9.709  42.896 7.132  0.00 109.81 ? 75  GLN A HE22 1 
ATOM   1110 N N    . ASN A 1 73  ? 14.514 42.850 11.736 1.00 39.31  ? 76  ASN A N    1 
ATOM   1111 C CA   . ASN A 1 73  ? 15.470 42.772 12.793 1.00 37.32  ? 76  ASN A CA   1 
ATOM   1112 C C    . ASN A 1 73  ? 15.143 41.582 13.674 1.00 41.90  ? 76  ASN A C    1 
ATOM   1113 O O    . ASN A 1 73  ? 14.009 41.487 14.142 1.00 34.81  ? 76  ASN A O    1 
ATOM   1114 C CB   . ASN A 1 73  ? 15.408 44.060 13.640 1.00 37.67  ? 76  ASN A CB   1 
ATOM   1115 C CG   . ASN A 1 73  ? 15.718 45.297 12.789 1.00 46.82  ? 76  ASN A CG   1 
ATOM   1116 O OD1  . ASN A 1 73  ? 16.890 45.611 12.562 1.00 50.00  ? 76  ASN A OD1  1 
ATOM   1117 N ND2  . ASN A 1 73  ? 14.680 45.950 12.266 1.00 41.97  ? 76  ASN A ND2  1 
ATOM   1118 H H    . ASN A 1 73  ? 13.732 43.119 11.971 0.00 47.16  ? 76  ASN A H    1 
ATOM   1119 H HA   . ASN A 1 73  ? 16.365 42.668 12.432 0.00 44.76  ? 76  ASN A HA   1 
ATOM   1120 H HB2  . ASN A 1 73  ? 14.518 44.159 14.012 0.00 45.18  ? 76  ASN A HB2  1 
ATOM   1121 H HB3  . ASN A 1 73  ? 16.062 44.008 14.355 0.00 45.18  ? 76  ASN A HB3  1 
ATOM   1122 H HD21 . ASN A 1 73  ? 14.810 46.649 11.782 0.00 50.35  ? 76  ASN A HD21 1 
ATOM   1123 H HD22 . ASN A 1 73  ? 13.879 45.673 12.412 0.00 50.35  ? 76  ASN A HD22 1 
ATOM   1124 N N    . PRO A 1 74  ? 16.105 40.710 13.972 1.00 35.96  ? 77  PRO A N    1 
ATOM   1125 C CA   . PRO A 1 74  ? 15.856 39.592 14.917 1.00 32.06  ? 77  PRO A CA   1 
ATOM   1126 C C    . PRO A 1 74  ? 15.720 40.065 16.357 1.00 36.09  ? 77  PRO A C    1 
ATOM   1127 O O    . PRO A 1 74  ? 16.632 40.694 16.908 1.00 36.40  ? 77  PRO A O    1 
ATOM   1128 C CB   . PRO A 1 74  ? 17.084 38.686 14.729 1.00 39.92  ? 77  PRO A CB   1 
ATOM   1129 C CG   . PRO A 1 74  ? 18.160 39.559 14.175 1.00 48.31  ? 77  PRO A CG   1 
ATOM   1130 C CD   . PRO A 1 74  ? 17.503 40.744 13.461 1.00 39.84  ? 77  PRO A CD   1 
ATOM   1131 H HA   . PRO A 1 74  ? 15.045 39.124 14.665 0.00 38.45  ? 77  PRO A HA   1 
ATOM   1132 H HB2  . PRO A 1 74  ? 17.349 38.315 15.585 0.00 47.89  ? 77  PRO A HB2  1 
ATOM   1133 H HB3  . PRO A 1 74  ? 16.869 37.971 14.110 0.00 47.89  ? 77  PRO A HB3  1 
ATOM   1134 H HG2  . PRO A 1 74  ? 18.717 39.875 14.903 0.00 57.95  ? 77  PRO A HG2  1 
ATOM   1135 H HG3  . PRO A 1 74  ? 18.692 39.045 13.548 0.00 57.95  ? 77  PRO A HG3  1 
ATOM   1136 H HD2  . PRO A 1 74  ? 17.939 41.577 13.700 0.00 47.79  ? 77  PRO A HD2  1 
ATOM   1137 H HD3  . PRO A 1 74  ? 17.523 40.624 12.499 0.00 47.79  ? 77  PRO A HD3  1 
ATOM   1138 N N    . ILE A 1 75  ? 14.558 39.796 16.980 1.00 29.98  ? 78  ILE A N    1 
ATOM   1139 C CA   . ILE A 1 75  ? 14.304 40.194 18.361 1.00 28.97  ? 78  ILE A CA   1 
ATOM   1140 C C    . ILE A 1 75  ? 14.037 38.926 19.176 1.00 27.84  ? 78  ILE A C    1 
ATOM   1141 O O    . ILE A 1 75  ? 13.049 38.205 18.929 1.00 28.09  ? 78  ILE A O    1 
ATOM   1142 C CB   . ILE A 1 75  ? 13.098 41.162 18.467 1.00 30.19  ? 78  ILE A CB   1 
ATOM   1143 C CG1  . ILE A 1 75  ? 13.401 42.487 17.690 1.00 31.89  ? 78  ILE A CG1  1 
ATOM   1144 C CG2  . ILE A 1 75  ? 12.749 41.424 19.876 1.00 30.62  ? 78  ILE A CG2  1 
ATOM   1145 C CD1  . ILE A 1 75  ? 14.621 43.342 18.249 1.00 33.08  ? 78  ILE A CD1  1 
ATOM   1146 H H    . ILE A 1 75  ? 13.902 39.380 16.612 0.00 35.96  ? 78  ILE A H    1 
ATOM   1147 H HA   . ILE A 1 75  ? 15.092 40.633 18.716 0.00 34.74  ? 78  ILE A HA   1 
ATOM   1148 H HB   . ILE A 1 75  ? 12.327 40.741 18.055 0.00 36.21  ? 78  ILE A HB   1 
ATOM   1149 H HG12 . ILE A 1 75  ? 13.603 42.261 16.769 0.00 38.25  ? 78  ILE A HG12 1 
ATOM   1150 H HG13 . ILE A 1 75  ? 12.612 43.050 17.728 0.00 38.25  ? 78  ILE A HG13 1 
ATOM   1151 H HG21 . ILE A 1 75  ? 12.190 42.215 19.922 0.00 36.72  ? 78  ILE A HG21 1 
ATOM   1152 H HG22 . ILE A 1 75  ? 12.270 40.659 20.230 0.00 36.72  ? 78  ILE A HG22 1 
ATOM   1153 H HG23 . ILE A 1 75  ? 13.565 41.566 20.382 0.00 36.72  ? 78  ILE A HG23 1 
ATOM   1154 H HD11 . ILE A 1 75  ? 14.761 44.108 17.671 0.00 39.68  ? 78  ILE A HD11 1 
ATOM   1155 H HD12 . ILE A 1 75  ? 14.413 43.640 19.148 0.00 39.68  ? 78  ILE A HD12 1 
ATOM   1156 H HD13 . ILE A 1 75  ? 15.417 42.787 18.260 0.00 39.68  ? 78  ILE A HD13 1 
ATOM   1157 N N    . TYR A 1 76  ? 14.922 38.648 20.137 1.00 26.33  ? 79  TYR A N    1 
ATOM   1158 C CA   . TYR A 1 76  ? 14.672 37.537 21.064 1.00 25.46  ? 79  TYR A CA   1 
ATOM   1159 C C    . TYR A 1 76  ? 13.648 37.954 22.133 1.00 27.03  ? 79  TYR A C    1 
ATOM   1160 O O    . TYR A 1 76  ? 13.999 38.549 23.152 1.00 27.19  ? 79  TYR A O    1 
ATOM   1161 C CB   . TYR A 1 76  ? 15.995 37.129 21.722 1.00 24.21  ? 79  TYR A CB   1 
ATOM   1162 C CG   . TYR A 1 76  ? 16.858 36.267 20.779 1.00 24.35  ? 79  TYR A CG   1 
ATOM   1163 C CD1  . TYR A 1 76  ? 16.568 34.917 20.599 1.00 25.80  ? 79  TYR A CD1  1 
ATOM   1164 C CD2  . TYR A 1 76  ? 17.928 36.805 20.107 1.00 25.86  ? 79  TYR A CD2  1 
ATOM   1165 C CE1  . TYR A 1 76  ? 17.404 34.075 19.772 1.00 25.01  ? 79  TYR A CE1  1 
ATOM   1166 C CE2  . TYR A 1 76  ? 18.769 35.999 19.219 1.00 27.59  ? 79  TYR A CE2  1 
ATOM   1167 C CZ   . TYR A 1 76  ? 18.468 34.617 19.085 1.00 27.04  ? 79  TYR A CZ   1 
ATOM   1168 O OH   . TYR A 1 76  ? 19.235 33.872 18.191 1.00 30.01  ? 79  TYR A OH   1 
ATOM   1169 H H    . TYR A 1 76  ? 15.656 39.076 20.269 0.00 31.57  ? 79  TYR A H    1 
ATOM   1170 H HA   . TYR A 1 76  ? 14.290 36.794 20.571 0.00 30.53  ? 79  TYR A HA   1 
ATOM   1171 H HB2  . TYR A 1 76  ? 16.498 37.926 21.951 0.00 29.04  ? 79  TYR A HB2  1 
ATOM   1172 H HB3  . TYR A 1 76  ? 15.809 36.613 22.521 0.00 29.04  ? 79  TYR A HB3  1 
ATOM   1173 H HD1  . TYR A 1 76  ? 15.822 34.550 21.017 0.00 30.95  ? 79  TYR A HD1  1 
ATOM   1174 H HD2  . TYR A 1 76  ? 18.125 37.707 20.220 0.00 31.01  ? 79  TYR A HD2  1 
ATOM   1175 H HE1  . TYR A 1 76  ? 17.223 33.165 19.704 0.00 29.99  ? 79  TYR A HE1  1 
ATOM   1176 H HE2  . TYR A 1 76  ? 19.479 36.382 18.756 0.00 33.09  ? 79  TYR A HE2  1 
ATOM   1177 H HH   . TYR A 1 76  ? 19.841 34.352 17.864 0.00 35.99  ? 79  TYR A HH   1 
ATOM   1178 N N    . TRP A 1 77  ? 12.366 37.629 21.919 1.00 24.09  ? 80  TRP A N    1 
ATOM   1179 C CA   . TRP A 1 77  ? 11.338 38.049 22.852 1.00 22.72  ? 80  TRP A CA   1 
ATOM   1180 C C    . TRP A 1 77  ? 11.321 37.184 24.081 1.00 20.81  ? 80  TRP A C    1 
ATOM   1181 O O    . TRP A 1 77  ? 10.811 37.608 25.138 1.00 21.21  ? 80  TRP A O    1 
ATOM   1182 C CB   . TRP A 1 77  ? 9.932  37.998 22.205 1.00 23.52  ? 80  TRP A CB   1 
ATOM   1183 C CG   . TRP A 1 77  ? 9.536  36.579 21.687 1.00 24.24  ? 80  TRP A CG   1 
ATOM   1184 C CD1  . TRP A 1 77  ? 9.694  36.058 20.415 1.00 29.68  ? 80  TRP A CD1  1 
ATOM   1185 C CD2  . TRP A 1 77  ? 8.966  35.518 22.489 1.00 26.69  ? 80  TRP A CD2  1 
ATOM   1186 N NE1  . TRP A 1 77  ? 9.192  34.747 20.355 1.00 35.25  ? 80  TRP A NE1  1 
ATOM   1187 C CE2  . TRP A 1 77  ? 8.765  34.387 21.621 1.00 29.51  ? 80  TRP A CE2  1 
ATOM   1188 C CE3  . TRP A 1 77  ? 8.580  35.431 23.822 1.00 28.82  ? 80  TRP A CE3  1 
ATOM   1189 C CZ2  . TRP A 1 77  ? 8.204  33.188 22.068 1.00 35.88  ? 80  TRP A CZ2  1 
ATOM   1190 C CZ3  . TRP A 1 77  ? 8.027  34.214 24.285 1.00 31.05  ? 80  TRP A CZ3  1 
ATOM   1191 C CH2  . TRP A 1 77  ? 7.846  33.108 23.388 1.00 32.66  ? 80  TRP A CH2  1 
ATOM   1192 H H    . TRP A 1 77  ? 12.079 37.173 21.248 0.00 28.89  ? 80  TRP A H    1 
ATOM   1193 H HA   . TRP A 1 77  ? 11.514 38.971 23.097 0.00 27.25  ? 80  TRP A HA   1 
ATOM   1194 H HB2  . TRP A 1 77  ? 9.274  38.267 22.865 0.00 28.20  ? 80  TRP A HB2  1 
ATOM   1195 H HB3  . TRP A 1 77  ? 9.913  38.606 21.450 0.00 28.20  ? 80  TRP A HB3  1 
ATOM   1196 H HD1  . TRP A 1 77  ? 10.078 36.512 19.700 0.00 35.59  ? 80  TRP A HD1  1 
ATOM   1197 H HE1  . TRP A 1 77  ? 9.156  34.253 19.652 0.00 42.28  ? 80  TRP A HE1  1 
ATOM   1198 H HE3  . TRP A 1 77  ? 8.683  36.156 24.395 0.00 34.56  ? 80  TRP A HE3  1 
ATOM   1199 H HZ2  . TRP A 1 77  ? 8.077  32.470 21.490 0.00 43.03  ? 80  TRP A HZ2  1 
ATOM   1200 H HZ3  . TRP A 1 77  ? 7.779  34.130 25.177 0.00 37.24  ? 80  TRP A HZ3  1 
ATOM   1201 H HH2  . TRP A 1 77  ? 7.477  32.317 23.711 0.00 39.17  ? 80  TRP A HH2  1 
ATOM   1202 N N    . ALA A 1 78  ? 11.929 35.968 23.996 1.00 22.45  ? 81  ALA A N    1 
ATOM   1203 C CA   . ALA A 1 78  ? 11.915 35.145 25.210 1.00 21.03  ? 81  ALA A CA   1 
ATOM   1204 C C    . ALA A 1 78  ? 12.621 35.764 26.405 1.00 23.74  ? 81  ALA A C    1 
ATOM   1205 O O    . ALA A 1 78  ? 12.370 35.353 27.545 1.00 23.04  ? 81  ALA A O    1 
ATOM   1206 C CB   . ALA A 1 78  ? 12.528 33.743 24.894 1.00 26.93  ? 81  ALA A CB   1 
ATOM   1207 H H    . ALA A 1 78  ? 12.318 35.637 23.304 0.00 26.92  ? 81  ALA A H    1 
ATOM   1208 H HA   . ALA A 1 78  ? 10.989 35.038 25.477 0.00 25.22  ? 81  ALA A HA   1 
ATOM   1209 H HB1  . ALA A 1 78  ? 12.534 33.211 25.704 0.00 32.30  ? 81  ALA A HB1  1 
ATOM   1210 H HB2  . ALA A 1 78  ? 11.988 33.308 24.216 0.00 32.30  ? 81  ALA A HB2  1 
ATOM   1211 H HB3  . ALA A 1 78  ? 13.435 33.861 24.569 0.00 32.30  ? 81  ALA A HB3  1 
ATOM   1212 N N    . ARG A 1 79  ? 13.583 36.717 26.211 1.00 20.24  ? 82  ARG A N    1 
ATOM   1213 C CA   . ARG A 1 79  ? 14.217 37.329 27.348 1.00 23.14  ? 82  ARG A CA   1 
ATOM   1214 C C    . ARG A 1 79  ? 13.205 37.976 28.256 1.00 20.21  ? 82  ARG A C    1 
ATOM   1215 O O    . ARG A 1 79  ? 13.367 37.956 29.487 1.00 22.68  ? 82  ARG A O    1 
ATOM   1216 C CB   . ARG A 1 79  ? 15.222 38.443 26.874 1.00 26.34  ? 82  ARG A CB   1 
ATOM   1217 C CG   . ARG A 1 79  ? 16.299 37.925 26.053 1.00 28.37  ? 82  ARG A CG   1 
ATOM   1218 C CD   . ARG A 1 79  ? 17.455 39.050 25.925 1.00 25.82  ? 82  ARG A CD   1 
ATOM   1219 N NE   . ARG A 1 79  ? 18.430 38.686 24.909 1.00 27.97  ? 82  ARG A NE   1 
ATOM   1220 C CZ   . ARG A 1 79  ? 19.364 37.764 25.148 1.00 28.34  ? 82  ARG A CZ   1 
ATOM   1221 N NH1  . ARG A 1 79  ? 19.516 37.216 26.359 1.00 29.86  ? 82  ARG A NH1  1 
ATOM   1222 N NH2  . ARG A 1 79  ? 20.254 37.512 24.216 1.00 34.33  ? 82  ARG A NH2  1 
ATOM   1223 H H    . ARG A 1 79  ? 13.857 36.997 25.446 0.00 24.27  ? 82  ARG A H    1 
ATOM   1224 H HA   . ARG A 1 79  ? 14.695 36.636 27.830 0.00 27.75  ? 82  ARG A HA   1 
ATOM   1225 H HB2  . ARG A 1 79  ? 14.738 39.101 26.351 0.00 31.59  ? 82  ARG A HB2  1 
ATOM   1226 H HB3  . ARG A 1 79  ? 15.617 38.863 27.654 0.00 31.59  ? 82  ARG A HB3  1 
ATOM   1227 H HG2  . ARG A 1 79  ? 16.676 37.131 26.464 0.00 34.03  ? 82  ARG A HG2  1 
ATOM   1228 H HG3  . ARG A 1 79  ? 15.966 37.713 25.167 0.00 34.03  ? 82  ARG A HG3  1 
ATOM   1229 H HD2  . ARG A 1 79  ? 17.054 39.897 25.675 0.00 30.96  ? 82  ARG A HD2  1 
ATOM   1230 H HD3  . ARG A 1 79  ? 17.915 39.138 26.774 0.00 30.96  ? 82  ARG A HD3  1 
ATOM   1231 H HE   . ARG A 1 79  ? 18.404 39.073 24.141 0.00 33.54  ? 82  ARG A HE   1 
ATOM   1232 H HH11 . ARG A 1 79  ? 19.004 37.457 27.007 0.00 35.81  ? 82  ARG A HH11 1 
ATOM   1233 H HH12 . ARG A 1 79  ? 20.125 36.623 26.490 0.00 35.81  ? 82  ARG A HH12 1 
ATOM   1234 H HH21 . ARG A 1 79  ? 20.227 37.939 23.469 0.00 41.18  ? 82  ARG A HH21 1 
ATOM   1235 H HH22 . ARG A 1 79  ? 20.863 36.921 24.351 0.00 41.18  ? 82  ARG A HH22 1 
ATOM   1236 N N    . TYR A 1 80  ? 12.172 38.630 27.663 1.00 21.20  ? 83  TYR A N    1 
ATOM   1237 C CA   . TYR A 1 80  ? 11.215 39.362 28.516 1.00 19.72  ? 83  TYR A CA   1 
ATOM   1238 C C    . TYR A 1 80  ? 10.318 38.404 29.276 1.00 20.73  ? 83  TYR A C    1 
ATOM   1239 O O    . TYR A 1 80  ? 9.881  38.736 30.382 1.00 23.28  ? 83  TYR A O    1 
ATOM   1240 C CB   . TYR A 1 80  ? 10.291 40.348 27.686 1.00 19.28  ? 83  TYR A CB   1 
ATOM   1241 C CG   . TYR A 1 80  ? 11.243 41.265 26.916 1.00 23.03  ? 83  TYR A CG   1 
ATOM   1242 C CD1  . TYR A 1 80  ? 11.736 42.418 27.473 1.00 25.49  ? 83  TYR A CD1  1 
ATOM   1243 C CD2  . TYR A 1 80  ? 11.713 40.907 25.638 1.00 25.56  ? 83  TYR A CD2  1 
ATOM   1244 C CE1  . TYR A 1 80  ? 12.692 43.218 26.766 1.00 25.09  ? 83  TYR A CE1  1 
ATOM   1245 C CE2  . TYR A 1 80  ? 12.661 41.685 24.934 1.00 24.58  ? 83  TYR A CE2  1 
ATOM   1246 C CZ   . TYR A 1 80  ? 13.154 42.829 25.509 1.00 24.84  ? 83  TYR A CZ   1 
ATOM   1247 O OH   . TYR A 1 80  ? 14.061 43.610 24.874 1.00 27.77  ? 83  TYR A OH   1 
ATOM   1248 H H    . TYR A 1 80  ? 12.017 38.660 26.817 0.00 25.42  ? 83  TYR A H    1 
ATOM   1249 H HA   . TYR A 1 80  ? 11.742 39.899 29.128 0.00 23.64  ? 83  TYR A HA   1 
ATOM   1250 H HB2  . TYR A 1 80  ? 9.736  39.853 27.063 0.00 23.11  ? 83  TYR A HB2  1 
ATOM   1251 H HB3  . TYR A 1 80  ? 9.734  40.875 28.279 0.00 23.11  ? 83  TYR A HB3  1 
ATOM   1252 H HD1  . TYR A 1 80  ? 11.447 42.683 28.316 0.00 30.57  ? 83  TYR A HD1  1 
ATOM   1253 H HD2  . TYR A 1 80  ? 11.388 40.130 25.242 0.00 30.65  ? 83  TYR A HD2  1 
ATOM   1254 H HE1  . TYR A 1 80  ? 13.008 44.004 27.149 0.00 30.09  ? 83  TYR A HE1  1 
ATOM   1255 H HE2  . TYR A 1 80  ? 12.947 41.424 24.088 0.00 29.48  ? 83  TYR A HE2  1 
ATOM   1256 H HH   . TYR A 1 80  ? 14.233 43.292 24.116 0.00 33.30  ? 83  TYR A HH   1 
ATOM   1257 N N    . ALA A 1 81  ? 10.046 37.212 28.691 1.00 20.47  ? 84  ALA A N    1 
ATOM   1258 C CA   . ALA A 1 81  ? 9.232  36.214 29.412 1.00 20.11  ? 84  ALA A CA   1 
ATOM   1259 C C    . ALA A 1 81  ? 9.997  35.697 30.628 1.00 24.87  ? 84  ALA A C    1 
ATOM   1260 O O    . ALA A 1 81  ? 9.411  35.515 31.709 1.00 24.32  ? 84  ALA A O    1 
ATOM   1261 C CB   . ALA A 1 81  ? 8.834  35.077 28.433 1.00 21.29  ? 84  ALA A CB   1 
ATOM   1262 H H    . ALA A 1 81  ? 10.312 36.970 27.910 0.00 24.55  ? 84  ALA A H    1 
ATOM   1263 H HA   . ALA A 1 81  ? 8.407  36.609 29.735 0.00 24.11  ? 84  ALA A HA   1 
ATOM   1264 H HB1  . ALA A 1 81  ? 8.304  34.420 28.911 0.00 25.53  ? 84  ALA A HB1  1 
ATOM   1265 H HB2  . ALA A 1 81  ? 8.315  35.454 27.705 0.00 25.53  ? 84  ALA A HB2  1 
ATOM   1266 H HB3  . ALA A 1 81  ? 9.639  34.663 28.085 0.00 25.53  ? 84  ALA A HB3  1 
ATOM   1267 N N    . ASP A 1 82  ? 11.323 35.516 30.485 1.00 19.07  ? 85  ASP A N    1 
ATOM   1268 C CA   . ASP A 1 82  ? 12.179 35.146 31.630 1.00 19.40  ? 85  ASP A CA   1 
ATOM   1269 C C    . ASP A 1 82  ? 12.144 36.253 32.693 1.00 20.29  ? 85  ASP A C    1 
ATOM   1270 O O    . ASP A 1 82  ? 11.723 36.041 33.862 1.00 21.41  ? 85  ASP A O    1 
ATOM   1271 C CB   . ASP A 1 82  ? 13.605 34.977 31.001 1.00 17.28  ? 85  ASP A CB   1 
ATOM   1272 C CG   . ASP A 1 82  ? 14.760 34.799 32.020 1.00 22.10  ? 85  ASP A CG   1 
ATOM   1273 O OD1  . ASP A 1 82  ? 14.624 35.154 33.178 1.00 22.34  ? 85  ASP A OD1  1 
ATOM   1274 O OD2  . ASP A 1 82  ? 15.837 34.325 31.565 1.00 22.36  ? 85  ASP A OD2  1 
ATOM   1275 H H    . ASP A 1 82  ? 11.749 35.600 29.742 0.00 22.86  ? 85  ASP A H    1 
ATOM   1276 H HA   . ASP A 1 82  ? 11.900 34.333 32.080 0.00 23.26  ? 85  ASP A HA   1 
ATOM   1277 H HB2  . ASP A 1 82  ? 13.598 34.191 30.432 0.00 20.71  ? 85  ASP A HB2  1 
ATOM   1278 H HB3  . ASP A 1 82  ? 13.803 35.767 30.474 0.00 20.71  ? 85  ASP A HB3  1 
ATOM   1279 N N    . TRP A 1 83  ? 12.472 37.485 32.273 1.00 19.55  ? 86  TRP A N    1 
ATOM   1280 C CA   . TRP A 1 83  ? 12.644 38.595 33.238 1.00 19.82  ? 86  TRP A CA   1 
ATOM   1281 C C    . TRP A 1 83  ? 11.324 38.956 33.938 1.00 20.44  ? 86  TRP A C    1 
ATOM   1282 O O    . TRP A 1 83  ? 11.342 39.344 35.109 1.00 20.85  ? 86  TRP A O    1 
ATOM   1283 C CB   . TRP A 1 83  ? 13.206 39.823 32.506 1.00 20.13  ? 86  TRP A CB   1 
ATOM   1284 C CG   . TRP A 1 83  ? 14.588 39.595 31.897 1.00 20.05  ? 86  TRP A CG   1 
ATOM   1285 C CD1  . TRP A 1 83  ? 15.476 38.559 32.161 1.00 21.27  ? 86  TRP A CD1  1 
ATOM   1286 C CD2  . TRP A 1 83  ? 15.195 40.436 30.897 1.00 18.81  ? 86  TRP A CD2  1 
ATOM   1287 N NE1  . TRP A 1 83  ? 16.642 38.744 31.357 1.00 20.88  ? 86  TRP A NE1  1 
ATOM   1288 C CE2  . TRP A 1 83  ? 16.465 39.883 30.597 1.00 21.39  ? 86  TRP A CE2  1 
ATOM   1289 C CE3  . TRP A 1 83  ? 14.768 41.612 30.240 1.00 21.34  ? 86  TRP A CE3  1 
ATOM   1290 C CZ2  . TRP A 1 83  ? 17.333 40.453 29.642 1.00 21.85  ? 86  TRP A CZ2  1 
ATOM   1291 C CZ3  . TRP A 1 83  ? 15.641 42.207 29.266 1.00 24.65  ? 86  TRP A CZ3  1 
ATOM   1292 C CH2  . TRP A 1 83  ? 16.927 41.605 28.996 1.00 27.29  ? 86  TRP A CH2  1 
ATOM   1293 H H    . TRP A 1 83  ? 12.600 37.705 31.452 0.00 23.44  ? 86  TRP A H    1 
ATOM   1294 H HA   . TRP A 1 83  ? 13.275 38.323 33.922 0.00 23.77  ? 86  TRP A HA   1 
ATOM   1295 H HB2  . TRP A 1 83  ? 12.601 40.062 31.787 0.00 24.14  ? 86  TRP A HB2  1 
ATOM   1296 H HB3  . TRP A 1 83  ? 13.278 40.557 33.137 0.00 24.14  ? 86  TRP A HB3  1 
ATOM   1297 H HD1  . TRP A 1 83  ? 15.335 37.862 32.761 0.00 25.50  ? 86  TRP A HD1  1 
ATOM   1298 H HE1  . TRP A 1 83  ? 17.335 38.234 31.347 0.00 25.04  ? 86  TRP A HE1  1 
ATOM   1299 H HE3  . TRP A 1 83  ? 13.942 41.992 30.433 0.00 25.59  ? 86  TRP A HE3  1 
ATOM   1300 H HZ2  . TRP A 1 83  ? 18.156 40.063 29.452 0.00 26.21  ? 86  TRP A HZ2  1 
ATOM   1301 H HZ3  . TRP A 1 83  ? 15.380 42.975 28.811 0.00 29.56  ? 86  TRP A HZ3  1 
ATOM   1302 H HH2  . TRP A 1 83  ? 17.494 42.002 28.374 0.00 32.73  ? 86  TRP A HH2  1 
ATOM   1303 N N    . LEU A 1 84  ? 10.188 38.791 33.269 1.00 19.02  ? 87  LEU A N    1 
ATOM   1304 C CA   . LEU A 1 84  ? 8.885  39.063 33.906 1.00 20.12  ? 87  LEU A CA   1 
ATOM   1305 C C    . LEU A 1 84  ? 8.735  38.281 35.193 1.00 23.42  ? 87  LEU A C    1 
ATOM   1306 O O    . LEU A 1 84  ? 8.131  38.781 36.162 1.00 24.16  ? 87  LEU A O    1 
ATOM   1307 C CB   . LEU A 1 84  ? 7.733  38.702 32.934 1.00 20.39  ? 87  LEU A CB   1 
ATOM   1308 C CG   . LEU A 1 84  ? 6.312  38.987 33.442 1.00 33.81  ? 87  LEU A CG   1 
ATOM   1309 C CD1  . LEU A 1 84  ? 6.121  40.542 33.610 1.00 39.51  ? 87  LEU A CD1  1 
ATOM   1310 C CD2  . LEU A 1 84  ? 5.244  38.371 32.464 1.00 39.06  ? 87  LEU A CD2  1 
ATOM   1311 H H    . LEU A 1 84  ? 10.135 38.525 32.453 0.00 22.81  ? 87  LEU A H    1 
ATOM   1312 H HA   . LEU A 1 84  ? 8.829  40.010 34.109 0.00 24.12  ? 87  LEU A HA   1 
ATOM   1313 H HB2  . LEU A 1 84  ? 7.854  39.213 32.118 0.00 24.45  ? 87  LEU A HB2  1 
ATOM   1314 H HB3  . LEU A 1 84  ? 7.785  37.753 32.742 0.00 24.45  ? 87  LEU A HB3  1 
ATOM   1315 H HG   . LEU A 1 84  ? 6.174  38.571 34.308 0.00 40.56  ? 87  LEU A HG   1 
ATOM   1316 H HD11 . LEU A 1 84  ? 5.200  40.722 33.856 0.00 47.39  ? 87  LEU A HD11 1 
ATOM   1317 H HD12 . LEU A 1 84  ? 6.718  40.860 34.306 0.00 47.39  ? 87  LEU A HD12 1 
ATOM   1318 H HD13 . LEU A 1 84  ? 6.331  40.978 32.770 0.00 47.39  ? 87  LEU A HD13 1 
ATOM   1319 H HD21 . LEU A 1 84  ? 4.357  38.531 32.823 0.00 46.86  ? 87  LEU A HD21 1 
ATOM   1320 H HD22 . LEU A 1 84  ? 5.330  38.794 31.595 0.00 46.86  ? 87  LEU A HD22 1 
ATOM   1321 H HD23 . LEU A 1 84  ? 5.401  37.417 32.385 0.00 46.86  ? 87  LEU A HD23 1 
ATOM   1322 N N    . PHE A 1 85  ? 9.187  37.016 35.200 1.00 21.27  ? 88  PHE A N    1 
ATOM   1323 C CA   . PHE A 1 85  ? 9.047  36.206 36.417 1.00 22.44  ? 88  PHE A CA   1 
ATOM   1324 C C    . PHE A 1 85  ? 10.308 36.193 37.279 1.00 27.15  ? 88  PHE A C    1 
ATOM   1325 O O    . PHE A 1 85  ? 10.186 36.138 38.518 1.00 24.59  ? 88  PHE A O    1 
ATOM   1326 C CB   . PHE A 1 85  ? 8.709  34.751 36.029 1.00 24.17  ? 88  PHE A CB   1 
ATOM   1327 C CG   . PHE A 1 85  ? 7.373  34.661 35.357 1.00 26.17  ? 88  PHE A CG   1 
ATOM   1328 C CD1  . PHE A 1 85  ? 6.211  34.819 36.095 1.00 36.98  ? 88  PHE A CD1  1 
ATOM   1329 C CD2  . PHE A 1 85  ? 7.331  34.479 34.016 1.00 26.67  ? 88  PHE A CD2  1 
ATOM   1330 C CE1  . PHE A 1 85  ? 4.957  34.754 35.447 1.00 37.95  ? 88  PHE A CE1  1 
ATOM   1331 C CE2  . PHE A 1 85  ? 6.084  34.465 33.330 1.00 39.19  ? 88  PHE A CE2  1 
ATOM   1332 C CZ   . PHE A 1 85  ? 4.910  34.620 34.056 1.00 35.62  ? 88  PHE A CZ   1 
ATOM   1333 H H    . PHE A 1 85  ? 9.564  36.621 34.535 0.00 25.50  ? 88  PHE A H    1 
ATOM   1334 H HA   . PHE A 1 85  ? 8.321  36.563 36.953 0.00 26.91  ? 88  PHE A HA   1 
ATOM   1335 H HB2  . PHE A 1 85  ? 9.383  34.417 35.416 0.00 28.99  ? 88  PHE A HB2  1 
ATOM   1336 H HB3  . PHE A 1 85  ? 8.688  34.202 36.828 0.00 28.99  ? 88  PHE A HB3  1 
ATOM   1337 H HD1  . PHE A 1 85  ? 6.256  34.968 37.012 0.00 44.35  ? 88  PHE A HD1  1 
ATOM   1338 H HD2  . PHE A 1 85  ? 8.121  34.362 33.540 0.00 31.99  ? 88  PHE A HD2  1 
ATOM   1339 H HE1  . PHE A 1 85  ? 4.170  34.800 35.941 0.00 45.52  ? 88  PHE A HE1  1 
ATOM   1340 H HE2  . PHE A 1 85  ? 6.056  34.353 32.407 0.00 47.00  ? 88  PHE A HE2  1 
ATOM   1341 H HZ   . PHE A 1 85  ? 4.091  34.635 33.615 0.00 42.73  ? 88  PHE A HZ   1 
ATOM   1342 N N    . THR A 1 86  ? 11.517 36.241 36.693 1.00 22.05  ? 89  THR A N    1 
ATOM   1343 C CA   . THR A 1 86  ? 12.690 36.093 37.561 1.00 19.72  ? 89  THR A CA   1 
ATOM   1344 C C    . THR A 1 86  ? 13.057 37.431 38.293 1.00 23.99  ? 89  THR A C    1 
ATOM   1345 O O    . THR A 1 86  ? 13.604 37.377 39.395 1.00 23.05  ? 89  THR A O    1 
ATOM   1346 C CB   . THR A 1 86  ? 13.949 35.611 36.791 1.00 23.37  ? 89  THR A CB   1 
ATOM   1347 O OG1  . THR A 1 86  ? 14.226 36.498 35.680 1.00 20.64  ? 89  THR A OG1  1 
ATOM   1348 C CG2  . THR A 1 86  ? 13.694 34.172 36.294 1.00 21.12  ? 89  THR A CG2  1 
ATOM   1349 H H    . THR A 1 86  ? 11.670 36.350 35.854 0.00 26.44  ? 89  THR A H    1 
ATOM   1350 H HA   . THR A 1 86  ? 12.459 35.408 38.208 0.00 23.64  ? 89  THR A HA   1 
ATOM   1351 H HB   . THR A 1 86  ? 14.731 35.613 37.365 0.00 28.02  ? 89  THR A HB   1 
ATOM   1352 H HG1  . THR A 1 86  ? 14.896 36.224 35.253 0.00 24.74  ? 89  THR A HG1  1 
ATOM   1353 H HG21 . THR A 1 86  ? 14.462 33.852 35.796 0.00 25.33  ? 89  THR A HG21 1 
ATOM   1354 H HG22 . THR A 1 86  ? 13.539 33.583 37.048 0.00 25.33  ? 89  THR A HG22 1 
ATOM   1355 H HG23 . THR A 1 86  ? 12.915 34.154 35.716 0.00 25.33  ? 89  THR A HG23 1 
ATOM   1356 N N    . THR A 1 87  ? 12.804 38.604 37.671 1.00 20.30  ? 90  THR A N    1 
ATOM   1357 C CA   . THR A 1 87  ? 13.221 39.864 38.355 1.00 19.62  ? 90  THR A CA   1 
ATOM   1358 C C    . THR A 1 87  ? 12.356 40.146 39.581 1.00 25.10  ? 90  THR A C    1 
ATOM   1359 O O    . THR A 1 87  ? 12.934 40.521 40.601 1.00 22.82  ? 90  THR A O    1 
ATOM   1360 C CB   . THR A 1 87  ? 13.307 41.086 37.435 1.00 19.95  ? 90  THR A CB   1 
ATOM   1361 O OG1  . THR A 1 87  ? 12.082 41.370 36.684 1.00 21.13  ? 90  THR A OG1  1 
ATOM   1362 C CG2  . THR A 1 87  ? 14.447 40.800 36.379 1.00 23.18  ? 90  THR A CG2  1 
ATOM   1363 H H    . THR A 1 87  ? 12.420 38.695 36.907 0.00 24.34  ? 90  THR A H    1 
ATOM   1364 H HA   . THR A 1 87  ? 14.129 39.712 38.659 0.00 23.52  ? 90  THR A HA   1 
ATOM   1365 H HB   . THR A 1 87  ? 13.476 41.862 37.992 0.00 23.92  ? 90  THR A HB   1 
ATOM   1366 H HG1  . THR A 1 87  ? 11.474 41.616 37.208 0.00 25.34  ? 90  THR A HG1  1 
ATOM   1367 H HG21 . THR A 1 87  ? 14.532 41.551 35.771 0.00 27.79  ? 90  THR A HG21 1 
ATOM   1368 H HG22 . THR A 1 87  ? 15.293 40.665 36.833 0.00 27.79  ? 90  THR A HG22 1 
ATOM   1369 H HG23 . THR A 1 87  ? 14.233 40.004 35.868 0.00 27.79  ? 90  THR A HG23 1 
ATOM   1370 N N    . PRO A 1 88  ? 11.067 39.853 39.619 1.00 23.41  ? 91  PRO A N    1 
ATOM   1371 C CA   . PRO A 1 88  ? 10.370 40.028 40.898 1.00 21.02  ? 91  PRO A CA   1 
ATOM   1372 C C    . PRO A 1 88  ? 10.811 39.037 41.940 1.00 23.31  ? 91  PRO A C    1 
ATOM   1373 O O    . PRO A 1 88  ? 10.797 39.357 43.144 1.00 26.08  ? 91  PRO A O    1 
ATOM   1374 C CB   . PRO A 1 88  ? 8.860  39.879 40.566 1.00 30.70  ? 91  PRO A CB   1 
ATOM   1375 C CG   . PRO A 1 88  ? 8.804  39.264 39.237 1.00 39.88  ? 91  PRO A CG   1 
ATOM   1376 C CD   . PRO A 1 88  ? 10.102 39.566 38.503 1.00 24.31  ? 91  PRO A CD   1 
ATOM   1377 H HA   . PRO A 1 88  ? 10.512 40.933 41.216 0.00 25.20  ? 91  PRO A HA   1 
ATOM   1378 H HB2  . PRO A 1 88  ? 8.434  39.310 41.227 0.00 36.82  ? 91  PRO A HB2  1 
ATOM   1379 H HB3  . PRO A 1 88  ? 8.439  40.752 40.560 0.00 36.82  ? 91  PRO A HB3  1 
ATOM   1380 H HG2  . PRO A 1 88  ? 8.694  38.306 39.338 0.00 47.83  ? 91  PRO A HG2  1 
ATOM   1381 H HG3  . PRO A 1 88  ? 8.052  39.635 38.750 0.00 47.83  ? 91  PRO A HG3  1 
ATOM   1382 H HD2  . PRO A 1 88  ? 10.391 38.800 37.983 0.00 29.16  ? 91  PRO A HD2  1 
ATOM   1383 H HD3  . PRO A 1 88  ? 10.001 40.339 37.925 0.00 29.16  ? 91  PRO A HD3  1 
ATOM   1384 N N    . LEU A 1 89  ? 11.132 37.780 41.525 1.00 22.87  ? 92  LEU A N    1 
ATOM   1385 C CA   . LEU A 1 89  ? 11.638 36.813 42.516 1.00 21.07  ? 92  LEU A CA   1 
ATOM   1386 C C    . LEU A 1 89  ? 12.926 37.294 43.157 1.00 24.95  ? 92  LEU A C    1 
ATOM   1387 O O    . LEU A 1 89  ? 13.142 37.120 44.354 1.00 26.70  ? 92  LEU A O    1 
ATOM   1388 C CB   . LEU A 1 89  ? 11.848 35.425 41.819 1.00 23.32  ? 92  LEU A CB   1 
ATOM   1389 C CG   . LEU A 1 89  ? 10.518 34.689 41.513 1.00 27.09  ? 92  LEU A CG   1 
ATOM   1390 C CD1  . LEU A 1 89  ? 10.816 33.392 40.685 1.00 24.80  ? 92  LEU A CD1  1 
ATOM   1391 C CD2  . LEU A 1 89  ? 9.757  34.278 42.850 1.00 30.92  ? 92  LEU A CD2  1 
ATOM   1392 H H    . LEU A 1 89  ? 11.067 37.487 40.719 0.00 27.43  ? 92  LEU A H    1 
ATOM   1393 H HA   . LEU A 1 89  ? 10.983 36.708 43.224 0.00 25.27  ? 92  LEU A HA   1 
ATOM   1394 H HB2  . LEU A 1 89  ? 12.314 35.563 40.979 0.00 27.97  ? 92  LEU A HB2  1 
ATOM   1395 H HB3  . LEU A 1 89  ? 12.377 34.858 42.402 0.00 27.97  ? 92  LEU A HB3  1 
ATOM   1396 H HG   . LEU A 1 89  ? 9.946  35.288 41.009 0.00 32.49  ? 92  LEU A HG   1 
ATOM   1397 H HD11 . LEU A 1 89  ? 9.978  32.951 40.478 0.00 29.74  ? 92  LEU A HD11 1 
ATOM   1398 H HD12 . LEU A 1 89  ? 11.272 33.639 39.865 0.00 29.74  ? 92  LEU A HD12 1 
ATOM   1399 H HD13 . LEU A 1 89  ? 11.379 32.804 41.212 0.00 29.74  ? 92  LEU A HD13 1 
ATOM   1400 H HD21 . LEU A 1 89  ? 9.030  33.676 42.627 0.00 37.09  ? 92  LEU A HD21 1 
ATOM   1401 H HD22 . LEU A 1 89  ? 10.381 33.836 43.446 0.00 37.09  ? 92  LEU A HD22 1 
ATOM   1402 H HD23 . LEU A 1 89  ? 9.406  35.078 43.272 0.00 37.09  ? 92  LEU A HD23 1 
ATOM   1403 N N    . LEU A 1 90  ? 13.836 37.890 42.361 1.00 22.06  ? 93  LEU A N    1 
ATOM   1404 C CA   . LEU A 1 90  ? 15.085 38.361 42.972 1.00 21.75  ? 93  LEU A CA   1 
ATOM   1405 C C    . LEU A 1 90  ? 14.807 39.520 43.944 1.00 21.22  ? 93  LEU A C    1 
ATOM   1406 O O    . LEU A 1 90  ? 15.463 39.610 45.000 1.00 24.06  ? 93  LEU A O    1 
ATOM   1407 C CB   . LEU A 1 90  ? 16.035 38.778 41.842 1.00 22.52  ? 93  LEU A CB   1 
ATOM   1408 C CG   . LEU A 1 90  ? 16.648 37.602 41.039 1.00 25.31  ? 93  LEU A CG   1 
ATOM   1409 C CD1  . LEU A 1 90  ? 17.296 38.218 39.709 1.00 25.41  ? 93  LEU A CD1  1 
ATOM   1410 C CD2  . LEU A 1 90  ? 17.681 36.848 41.915 1.00 26.61  ? 93  LEU A CD2  1 
ATOM   1411 H H    . LEU A 1 90  ? 13.756 38.023 41.515 0.00 26.45  ? 93  LEU A H    1 
ATOM   1412 H HA   . LEU A 1 90  ? 15.511 37.657 43.486 0.00 26.09  ? 93  LEU A HA   1 
ATOM   1413 H HB2  . LEU A 1 90  ? 15.543 39.333 41.218 0.00 27.01  ? 93  LEU A HB2  1 
ATOM   1414 H HB3  . LEU A 1 90  ? 16.768 39.281 42.229 0.00 27.01  ? 93  LEU A HB3  1 
ATOM   1415 H HG   . LEU A 1 90  ? 15.983 36.945 40.782 0.00 30.35  ? 93  LEU A HG   1 
ATOM   1416 H HD11 . LEU A 1 90  ? 17.685 37.500 39.185 0.00 30.47  ? 93  LEU A HD11 1 
ATOM   1417 H HD12 . LEU A 1 90  ? 16.602 38.662 39.196 0.00 30.47  ? 93  LEU A HD12 1 
ATOM   1418 H HD13 . LEU A 1 90  ? 17.983 38.856 39.958 0.00 30.47  ? 93  LEU A HD13 1 
ATOM   1419 H HD21 . LEU A 1 90  ? 18.133 36.184 41.370 0.00 31.91  ? 93  LEU A HD21 1 
ATOM   1420 H HD22 . LEU A 1 90  ? 18.325 37.484 42.262 0.00 31.91  ? 93  LEU A HD22 1 
ATOM   1421 H HD23 . LEU A 1 90  ? 17.217 36.414 42.647 0.00 31.91  ? 93  LEU A HD23 1 
ATOM   1422 N N    . LEU A 1 91  ? 13.867 40.405 43.618 1.00 23.29  ? 94  LEU A N    1 
ATOM   1423 C CA   . LEU A 1 91  ? 13.492 41.487 44.548 1.00 22.14  ? 94  LEU A CA   1 
ATOM   1424 C C    . LEU A 1 91  ? 12.826 40.928 45.812 1.00 23.58  ? 94  LEU A C    1 
ATOM   1425 O O    . LEU A 1 91  ? 13.049 41.454 46.926 1.00 26.06  ? 94  LEU A O    1 
ATOM   1426 C CB   . LEU A 1 91  ? 12.509 42.491 43.855 1.00 22.94  ? 94  LEU A CB   1 
ATOM   1427 C CG   . LEU A 1 91  ? 13.188 43.294 42.763 1.00 25.24  ? 94  LEU A CG   1 
ATOM   1428 C CD1  . LEU A 1 91  ? 12.137 44.189 42.017 1.00 28.43  ? 94  LEU A CD1  1 
ATOM   1429 C CD2  . LEU A 1 91  ? 14.373 44.112 43.247 1.00 29.32  ? 94  LEU A CD2  1 
ATOM   1430 H H    . LEU A 1 91  ? 13.431 40.409 42.877 0.00 27.93  ? 94  LEU A H    1 
ATOM   1431 H HA   . LEU A 1 91  ? 14.301 41.962 44.795 0.00 26.54  ? 94  LEU A HA   1 
ATOM   1432 H HB2  . LEU A 1 91  ? 11.777 41.995 43.457 0.00 27.51  ? 94  LEU A HB2  1 
ATOM   1433 H HB3  . LEU A 1 91  ? 12.168 43.110 44.519 0.00 27.51  ? 94  LEU A HB3  1 
ATOM   1434 H HG   . LEU A 1 91  ? 13.566 42.660 42.133 0.00 30.27  ? 94  LEU A HG   1 
ATOM   1435 H HD11 . LEU A 1 91  ? 12.586 44.683 41.313 0.00 34.09  ? 94  LEU A HD11 1 
ATOM   1436 H HD12 . LEU A 1 91  ? 11.451 43.619 41.636 0.00 34.09  ? 94  LEU A HD12 1 
ATOM   1437 H HD13 . LEU A 1 91  ? 11.740 44.805 42.652 0.00 34.09  ? 94  LEU A HD13 1 
ATOM   1438 H HD21 . LEU A 1 91  ? 14.636 44.730 42.548 0.00 35.16  ? 94  LEU A HD21 1 
ATOM   1439 H HD22 . LEU A 1 91  ? 14.114 44.603 44.043 0.00 35.16  ? 94  LEU A HD22 1 
ATOM   1440 H HD23 . LEU A 1 91  ? 15.107 43.513 43.453 0.00 35.16  ? 94  LEU A HD23 1 
ATOM   1441 N N    A LEU A 1 92  ? 12.045 39.844 45.690 0.60 23.53  ? 95  LEU A N    1 
ATOM   1442 N N    B LEU A 1 92  ? 12.041 39.847 45.696 0.40 23.61  ? 95  LEU A N    1 
ATOM   1443 C CA   A LEU A 1 92  ? 11.459 39.213 46.886 0.60 25.84  ? 95  LEU A CA   1 
ATOM   1444 C CA   B LEU A 1 92  ? 11.489 39.224 46.907 0.40 25.85  ? 95  LEU A CA   1 
ATOM   1445 C C    A LEU A 1 92  ? 12.524 38.614 47.805 0.60 29.08  ? 95  LEU A C    1 
ATOM   1446 C C    B LEU A 1 92  ? 12.580 38.689 47.817 0.40 29.02  ? 95  LEU A C    1 
ATOM   1447 O O    A LEU A 1 92  ? 12.381 38.658 49.047 0.60 29.23  ? 95  LEU A O    1 
ATOM   1448 O O    B LEU A 1 92  ? 12.494 38.826 49.054 0.40 29.47  ? 95  LEU A O    1 
ATOM   1449 C CB   A LEU A 1 92  ? 10.412 38.175 46.457 0.60 24.90  ? 95  LEU A CB   1 
ATOM   1450 C CB   B LEU A 1 92  ? 10.522 38.101 46.555 0.40 25.46  ? 95  LEU A CB   1 
ATOM   1451 C CG   A LEU A 1 92  ? 9.594  37.500 47.562 0.60 27.43  ? 95  LEU A CG   1 
ATOM   1452 C CG   B LEU A 1 92  ? 9.204  38.466 45.914 0.40 29.50  ? 95  LEU A CG   1 
ATOM   1453 C CD1  A LEU A 1 92  ? 8.703  38.503 48.258 0.60 34.63  ? 95  LEU A CD1  1 
ATOM   1454 C CD1  B LEU A 1 92  ? 8.484  37.157 45.611 0.40 30.36  ? 95  LEU A CD1  1 
ATOM   1455 C CD2  A LEU A 1 92  ? 8.820  36.338 46.995 0.60 26.06  ? 95  LEU A CD2  1 
ATOM   1456 C CD2  B LEU A 1 92  ? 8.352  39.333 46.819 0.40 33.39  ? 95  LEU A CD2  1 
ATOM   1457 H H    A LEU A 1 92  ? 11.842 39.463 44.947 0.60 28.21  ? 95  LEU A H    1 
ATOM   1458 H H    B LEU A 1 92  ? 11.820 39.470 44.956 0.40 28.31  ? 95  LEU A H    1 
ATOM   1459 H HA   A LEU A 1 92  ? 11.004 39.889 47.411 0.60 30.99  ? 95  LEU A HA   1 
ATOM   1460 H HA   B LEU A 1 92  ? 10.997 39.910 47.383 0.40 31.01  ? 95  LEU A HA   1 
ATOM   1461 H HB2  A LEU A 1 92  ? 9.780  38.617 45.869 0.60 29.86  ? 95  LEU A HB2  1 
ATOM   1462 H HB2  B LEU A 1 92  ? 10.975 37.505 45.938 0.40 30.53  ? 95  LEU A HB2  1 
ATOM   1463 H HB3  A LEU A 1 92  ? 10.873 37.469 45.977 0.60 29.86  ? 95  LEU A HB3  1 
ATOM   1464 H HB3  B LEU A 1 92  ? 10.309 37.629 47.376 0.40 30.53  ? 95  LEU A HB3  1 
ATOM   1465 H HG   A LEU A 1 92  ? 10.188 37.144 48.242 0.60 32.89  ? 95  LEU A HG   1 
ATOM   1466 H HG   B LEU A 1 92  ? 9.353  38.984 45.108 0.40 35.38  ? 95  LEU A HG   1 
ATOM   1467 H HD11 A LEU A 1 92  ? 8.107  38.032 48.861 0.60 41.54  ? 95  LEU A HD11 1 
ATOM   1468 H HD11 B LEU A 1 92  ? 7.528  37.293 45.704 0.40 36.41  ? 95  LEU A HD11 1 
ATOM   1469 H HD12 A LEU A 1 92  ? 9.257  39.123 48.758 0.60 41.54  ? 95  LEU A HD12 1 
ATOM   1470 H HD12 B LEU A 1 92  ? 8.692  36.884 44.704 0.40 36.41  ? 95  LEU A HD12 1 
ATOM   1471 H HD13 A LEU A 1 92  ? 8.188  38.983 47.591 0.60 41.54  ? 95  LEU A HD13 1 
ATOM   1472 H HD13 B LEU A 1 92  ? 8.783  36.479 46.237 0.40 36.41  ? 95  LEU A HD13 1 
ATOM   1473 H HD21 A LEU A 1 92  ? 8.332  35.904 47.712 0.60 31.25  ? 95  LEU A HD21 1 
ATOM   1474 H HD21 B LEU A 1 92  ? 7.569  39.628 46.329 0.40 40.05  ? 95  LEU A HD21 1 
ATOM   1475 H HD22 A LEU A 1 92  ? 8.200  36.668 46.326 0.60 31.25  ? 95  LEU A HD22 1 
ATOM   1476 H HD22 B LEU A 1 92  ? 8.081  38.813 47.592 0.40 40.05  ? 95  LEU A HD22 1 
ATOM   1477 H HD23 A LEU A 1 92  ? 9.441  35.712 46.591 0.60 31.25  ? 95  LEU A HD23 1 
ATOM   1478 H HD23 B LEU A 1 92  ? 8.873  40.101 47.104 0.40 40.05  ? 95  LEU A HD23 1 
ATOM   1479 N N    . ASP A 1 93  ? 13.601 38.037 47.251 1.00 25.25  ? 96  ASP A N    1 
ATOM   1480 C CA   . ASP A 1 93  ? 14.699 37.562 48.122 1.00 25.20  ? 96  ASP A CA   1 
ATOM   1481 C C    . ASP A 1 93  ? 15.243 38.739 48.954 1.00 29.05  ? 96  ASP A C    1 
ATOM   1482 O O    . ASP A 1 93  ? 15.483 38.611 50.158 1.00 31.56  ? 96  ASP A O    1 
ATOM   1483 C CB   . ASP A 1 93  ? 15.837 37.016 47.248 1.00 27.09  ? 96  ASP A CB   1 
ATOM   1484 C CG   . ASP A 1 93  ? 15.859 35.506 47.093 1.00 26.99  ? 96  ASP A CG   1 
ATOM   1485 O OD1  . ASP A 1 93  ? 15.289 34.736 47.886 1.00 27.41  ? 96  ASP A OD1  1 
ATOM   1486 O OD2  . ASP A 1 93  ? 16.647 35.058 46.186 1.00 29.98  ? 96  ASP A OD2  1 
ATOM   1487 H H    . ASP A 1 93  ? 13.718 37.913 46.408 0.00 30.28  ? 96  ASP A H    1 
ATOM   1488 H HA   . ASP A 1 93  ? 14.372 36.861 48.706 0.00 30.22  ? 96  ASP A HA   1 
ATOM   1489 H HB2  . ASP A 1 93  ? 15.753 37.398 46.361 0.00 32.49  ? 96  ASP A HB2  1 
ATOM   1490 H HB3  . ASP A 1 93  ? 16.682 37.279 47.645 0.00 32.49  ? 96  ASP A HB3  1 
ATOM   1491 N N    . LEU A 1 94  ? 15.476 39.888 48.299 1.00 26.43  ? 97  LEU A N    1 
ATOM   1492 C CA   . LEU A 1 94  ? 16.000 41.055 49.045 1.00 26.96  ? 97  LEU A CA   1 
ATOM   1493 C C    . LEU A 1 94  ? 15.003 41.549 50.066 1.00 29.32  ? 97  LEU A C    1 
ATOM   1494 O O    . LEU A 1 94  ? 15.377 41.884 51.195 1.00 29.37  ? 97  LEU A O    1 
ATOM   1495 C CB   . LEU A 1 94  ? 16.341 42.213 48.080 1.00 28.67  ? 97  LEU A CB   1 
ATOM   1496 C CG   . LEU A 1 94  ? 17.505 41.896 47.171 1.00 28.31  ? 97  LEU A CG   1 
ATOM   1497 C CD1  . LEU A 1 94  ? 17.648 42.950 46.054 1.00 35.55  ? 97  LEU A CD1  1 
ATOM   1498 C CD2  . LEU A 1 94  ? 18.821 41.757 48.043 1.00 35.44  ? 97  LEU A CD2  1 
ATOM   1499 H H    . LEU A 1 94  ? 15.347 40.017 47.459 0.00 31.70  ? 97  LEU A H    1 
ATOM   1500 H HA   . LEU A 1 94  ? 16.810 40.771 49.497 0.00 32.33  ? 97  LEU A HA   1 
ATOM   1501 H HB2  . LEU A 1 94  ? 15.567 42.397 47.525 0.00 34.38  ? 97  LEU A HB2  1 
ATOM   1502 H HB3  . LEU A 1 94  ? 16.571 42.998 48.600 0.00 34.38  ? 97  LEU A HB3  1 
ATOM   1503 H HG   . LEU A 1 94  ? 17.353 41.053 46.718 0.00 33.96  ? 97  LEU A HG   1 
ATOM   1504 H HD11 . LEU A 1 94  ? 18.368 42.684 45.460 0.00 42.64  ? 97  LEU A HD11 1 
ATOM   1505 H HD12 . LEU A 1 94  ? 16.815 43.002 45.561 0.00 42.64  ? 97  LEU A HD12 1 
ATOM   1506 H HD13 . LEU A 1 94  ? 17.850 43.810 46.455 0.00 42.64  ? 97  LEU A HD13 1 
ATOM   1507 H HD21 . LEU A 1 94  ? 19.591 41.746 47.453 0.00 42.51  ? 97  LEU A HD21 1 
ATOM   1508 H HD22 . LEU A 1 94  ? 18.880 42.511 48.650 0.00 42.51  ? 97  LEU A HD22 1 
ATOM   1509 H HD23 . LEU A 1 94  ? 18.780 40.929 48.547 0.00 42.51  ? 97  LEU A HD23 1 
ATOM   1510 N N    . ALA A 1 95  ? 13.728 41.668 49.686 1.00 27.99  ? 98  ALA A N    1 
ATOM   1511 C CA   . ALA A 1 95  ? 12.724 42.192 50.626 1.00 29.33  ? 98  ALA A CA   1 
ATOM   1512 C C    . ALA A 1 95  ? 12.498 41.275 51.813 1.00 34.24  ? 98  ALA A C    1 
ATOM   1513 O O    . ALA A 1 95  ? 12.218 41.738 52.942 1.00 33.31  ? 98  ALA A O    1 
ATOM   1514 C CB   . ALA A 1 95  ? 11.374 42.364 49.848 1.00 30.05  ? 98  ALA A CB   1 
ATOM   1515 H H    . ALA A 1 95  ? 13.422 41.460 48.910 0.00 33.57  ? 98  ALA A H    1 
ATOM   1516 H HA   . ALA A 1 95  ? 13.037 43.042 50.973 0.00 35.18  ? 98  ALA A HA   1 
ATOM   1517 H HB1  . ALA A 1 95  ? 10.702 42.712 50.454 0.00 36.04  ? 98  ALA A HB1  1 
ATOM   1518 H HB2  . ALA A 1 95  ? 11.510 42.983 49.113 0.00 36.04  ? 98  ALA A HB2  1 
ATOM   1519 H HB3  . ALA A 1 95  ? 11.094 41.500 49.505 0.00 36.04  ? 98  ALA A HB3  1 
ATOM   1520 N N    . LEU A 1 96  ? 12.524 39.970 51.598 1.00 28.25  ? 99  LEU A N    1 
ATOM   1521 C CA   . LEU A 1 96  ? 12.333 39.069 52.747 1.00 31.67  ? 99  LEU A CA   1 
ATOM   1522 C C    . LEU A 1 96  ? 13.526 39.130 53.690 1.00 32.86  ? 99  LEU A C    1 
ATOM   1523 O O    . LEU A 1 96  ? 13.391 38.935 54.899 1.00 36.38  ? 99  LEU A O    1 
ATOM   1524 C CB   . LEU A 1 96  ? 12.143 37.625 52.251 1.00 36.17  ? 99  LEU A CB   1 
ATOM   1525 C CG   . LEU A 1 96  ? 10.846 37.429 51.434 1.00 41.56  ? 99  LEU A CG   1 
ATOM   1526 C CD1  . LEU A 1 96  ? 10.714 35.970 51.025 1.00 44.43  ? 99  LEU A CD1  1 
ATOM   1527 C CD2  . LEU A 1 96  ? 9.583  37.876 52.219 1.00 56.54  ? 99  LEU A CD2  1 
ATOM   1528 H H    . LEU A 1 96  ? 12.645 39.587 50.837 0.00 33.88  ? 99  LEU A H    1 
ATOM   1529 H HA   . LEU A 1 96  ? 11.536 39.336 53.232 0.00 37.98  ? 99  LEU A HA   1 
ATOM   1530 H HB2  . LEU A 1 96  ? 12.893 37.387 51.684 0.00 43.38  ? 99  LEU A HB2  1 
ATOM   1531 H HB3  . LEU A 1 96  ? 12.106 37.032 53.018 0.00 43.38  ? 99  LEU A HB3  1 
ATOM   1532 H HG   . LEU A 1 96  ? 10.900 37.987 50.643 0.00 49.85  ? 99  LEU A HG   1 
ATOM   1533 H HD11 . LEU A 1 96  ? 9.886  35.854 50.534 0.00 53.29  ? 99  LEU A HD11 1 
ATOM   1534 H HD12 . LEU A 1 96  ? 11.468 35.730 50.464 0.00 53.29  ? 99  LEU A HD12 1 
ATOM   1535 H HD13 . LEU A 1 96  ? 10.706 35.418 51.823 0.00 53.29  ? 99  LEU A HD13 1 
ATOM   1536 H HD21 . LEU A 1 96  ? 8.792  37.589 51.735 0.00 67.83  ? 99  LEU A HD21 1 
ATOM   1537 H HD22 . LEU A 1 96  ? 9.597  37.468 53.100 0.00 67.83  ? 99  LEU A HD22 1 
ATOM   1538 H HD23 . LEU A 1 96  ? 9.588  38.842 52.302 0.00 67.83  ? 99  LEU A HD23 1 
ATOM   1539 N N    . LEU A 1 97  ? 14.709 39.357 53.139 1.00 33.37  ? 100 LEU A N    1 
ATOM   1540 C CA   . LEU A 1 97  ? 15.894 39.411 53.976 1.00 36.24  ? 100 LEU A CA   1 
ATOM   1541 C C    . LEU A 1 97  ? 15.787 40.550 54.992 1.00 36.46  ? 100 LEU A C    1 
ATOM   1542 O O    . LEU A 1 97  ? 16.187 40.394 56.149 1.00 40.22  ? 100 LEU A O    1 
ATOM   1543 C CB   . LEU A 1 97  ? 17.097 39.570 53.049 1.00 37.75  ? 100 LEU A CB   1 
ATOM   1544 C CG   . LEU A 1 97  ? 18.497 39.353 53.536 1.00 51.20  ? 100 LEU A CG   1 
ATOM   1545 C CD1  . LEU A 1 97  ? 18.601 37.903 53.990 1.00 43.29  ? 100 LEU A CD1  1 
ATOM   1546 C CD2  . LEU A 1 97  ? 19.433 39.701 52.390 1.00 41.87  ? 100 LEU A CD2  1 
ATOM   1547 H H    . LEU A 1 97  ? 14.850 39.481 52.300 0.00 40.02  ? 100 LEU A H    1 
ATOM   1548 H HA   . LEU A 1 97  ? 16.006 38.597 54.492 0.00 43.47  ? 100 LEU A HA   1 
ATOM   1549 H HB2  . LEU A 1 97  ? 16.973 38.943 52.319 0.00 45.28  ? 100 LEU A HB2  1 
ATOM   1550 H HB3  . LEU A 1 97  ? 17.073 40.479 52.713 0.00 45.28  ? 100 LEU A HB3  1 
ATOM   1551 H HG   . LEU A 1 97  ? 18.746 39.909 54.291 0.00 61.43  ? 100 LEU A HG   1 
ATOM   1552 H HD11 . LEU A 1 97  ? 19.525 37.707 54.212 0.00 51.93  ? 100 LEU A HD11 1 
ATOM   1553 H HD12 . LEU A 1 97  ? 18.039 37.775 54.770 0.00 51.93  ? 100 LEU A HD12 1 
ATOM   1554 H HD13 . LEU A 1 97  ? 18.304 37.325 53.270 0.00 51.93  ? 100 LEU A HD13 1 
ATOM   1555 H HD21 . LEU A 1 97  ? 20.350 39.594 52.688 0.00 50.23  ? 100 LEU A HD21 1 
ATOM   1556 H HD22 . LEU A 1 97  ? 19.256 39.106 51.645 0.00 50.23  ? 100 LEU A HD22 1 
ATOM   1557 H HD23 . LEU A 1 97  ? 19.278 40.621 52.123 0.00 50.23  ? 100 LEU A HD23 1 
ATOM   1558 N N    . VAL A 1 98  ? 15.221 41.700 54.596 1.00 35.39  ? 101 VAL A N    1 
ATOM   1559 C CA   . VAL A 1 98  ? 15.095 42.855 55.494 1.00 36.42  ? 101 VAL A CA   1 
ATOM   1560 C C    . VAL A 1 98  ? 13.707 42.962 56.135 1.00 42.81  ? 101 VAL A C    1 
ATOM   1561 O O    . VAL A 1 98  ? 13.408 43.963 56.793 1.00 40.88  ? 101 VAL A O    1 
ATOM   1562 C CB   . VAL A 1 98  ? 15.438 44.183 54.774 1.00 39.76  ? 101 VAL A CB   1 
ATOM   1563 C CG1  . VAL A 1 98  ? 16.831 44.092 54.116 1.00 44.80  ? 101 VAL A CG1  1 
ATOM   1564 C CG2  . VAL A 1 98  ? 14.392 44.563 53.762 1.00 39.41  ? 101 VAL A CG2  1 
ATOM   1565 H H    . VAL A 1 98  ? 14.902 41.835 53.809 0.00 42.45  ? 101 VAL A H    1 
ATOM   1566 H HA   . VAL A 1 98  ? 15.736 42.715 56.208 0.00 43.68  ? 101 VAL A HA   1 
ATOM   1567 H HB   . VAL A 1 98  ? 15.456 44.888 55.439 0.00 47.69  ? 101 VAL A HB   1 
ATOM   1568 H HG11 . VAL A 1 98  ? 17.016 44.923 53.651 0.00 53.74  ? 101 VAL A HG11 1 
ATOM   1569 H HG12 . VAL A 1 98  ? 17.497 43.944 54.806 0.00 53.74  ? 101 VAL A HG12 1 
ATOM   1570 H HG13 . VAL A 1 98  ? 16.836 43.354 53.487 0.00 53.74  ? 101 VAL A HG13 1 
ATOM   1571 H HG21 . VAL A 1 98  ? 14.682 45.361 53.292 0.00 47.27  ? 101 VAL A HG21 1 
ATOM   1572 H HG22 . VAL A 1 98  ? 14.279 43.832 53.134 0.00 47.27  ? 101 VAL A HG22 1 
ATOM   1573 H HG23 . VAL A 1 98  ? 13.555 44.735 54.222 0.00 47.27  ? 101 VAL A HG23 1 
ATOM   1574 N N    . ASP A 1 99  ? 12.854 41.960 55.977 1.00 38.36  ? 102 ASP A N    1 
ATOM   1575 C CA   . ASP A 1 99  ? 11.515 41.994 56.587 1.00 34.08  ? 102 ASP A CA   1 
ATOM   1576 C C    . ASP A 1 99  ? 10.720 43.237 56.158 1.00 32.39  ? 102 ASP A C    1 
ATOM   1577 O O    . ASP A 1 99  ? 10.076 43.897 56.979 1.00 38.21  ? 102 ASP A O    1 
ATOM   1578 C CB   . ASP A 1 99  ? 11.594 41.913 58.114 1.00 40.20  ? 102 ASP A CB   1 
ATOM   1579 C CG   . ASP A 1 99  ? 10.290 41.447 58.729 1.00 60.30  ? 102 ASP A CG   1 
ATOM   1580 O OD1  . ASP A 1 99  ? 9.550  40.708 58.041 1.00 63.74  ? 102 ASP A OD1  1 
ATOM   1581 O OD2  . ASP A 1 99  ? 10.002 41.818 59.889 1.00 73.39  ? 102 ASP A OD2  1 
ATOM   1582 H H    . ASP A 1 99  ? 13.018 41.249 55.522 0.00 46.01  ? 102 ASP A H    1 
ATOM   1583 H HA   . ASP A 1 99  ? 11.035 41.215 56.264 0.00 40.88  ? 102 ASP A HA   1 
ATOM   1584 H HB2  . ASP A 1 99  ? 12.289 41.285 58.364 0.00 48.22  ? 102 ASP A HB2  1 
ATOM   1585 H HB3  . ASP A 1 99  ? 11.798 42.793 58.469 0.00 48.22  ? 102 ASP A HB3  1 
ATOM   1586 N N    . ALA A 1 100 ? 10.717 43.493 54.852 1.00 34.03  ? 103 ALA A N    1 
ATOM   1587 C CA   . ALA A 1 100 ? 10.019 44.662 54.313 1.00 37.88  ? 103 ALA A CA   1 
ATOM   1588 C C    . ALA A 1 100 ? 8.516  44.546 54.549 1.00 39.85  ? 103 ALA A C    1 
ATOM   1589 O O    . ALA A 1 100 ? 7.945  43.454 54.547 1.00 39.09  ? 103 ALA A O    1 
ATOM   1590 C CB   . ALA A 1 100 ? 10.299 44.805 52.816 1.00 33.34  ? 103 ALA A CB   1 
ATOM   1591 H H    . ALA A 1 100 ? 11.109 43.010 54.258 0.00 40.82  ? 103 ALA A H    1 
ATOM   1592 H HA   . ALA A 1 100 ? 10.339 45.461 54.761 0.00 45.44  ? 103 ALA A HA   1 
ATOM   1593 H HB1  . ALA A 1 100 ? 9.825  45.581 52.478 0.00 39.99  ? 103 ALA A HB1  1 
ATOM   1594 H HB2  . ALA A 1 100 ? 11.253 44.916 52.682 0.00 39.99  ? 103 ALA A HB2  1 
ATOM   1595 H HB3  . ALA A 1 100 ? 9.992  44.006 52.359 0.00 39.99  ? 103 ALA A HB3  1 
ATOM   1596 N N    . ASP A 1 101 ? 7.871  45.697 54.734 1.00 34.47  ? 104 ASP A N    1 
ATOM   1597 C CA   A ASP A 1 101 ? 6.430  45.741 54.897 0.78 41.13  ? 104 ASP A CA   1 
ATOM   1598 C CA   B ASP A 1 101 ? 6.429  45.749 54.892 0.22 41.21  ? 104 ASP A CA   1 
ATOM   1599 C C    . ASP A 1 101 ? 5.728  45.451 53.567 1.00 40.89  ? 104 ASP A C    1 
ATOM   1600 O O    . ASP A 1 101 ? 6.278  45.632 52.474 1.00 37.18  ? 104 ASP A O    1 
ATOM   1601 C CB   A ASP A 1 101 ? 5.999  47.116 55.426 0.78 47.63  ? 104 ASP A CB   1 
ATOM   1602 C CB   B ASP A 1 101 ? 6.007  47.129 55.393 0.22 47.45  ? 104 ASP A CB   1 
ATOM   1603 C CG   A ASP A 1 101 ? 6.174  48.217 54.394 0.78 44.19  ? 104 ASP A CG   1 
ATOM   1604 C CG   B ASP A 1 101 ? 6.470  47.401 56.801 0.22 39.61  ? 104 ASP A CG   1 
ATOM   1605 O OD1  A ASP A 1 101 ? 7.289  48.748 54.261 0.78 52.55  ? 104 ASP A OD1  1 
ATOM   1606 O OD1  B ASP A 1 101 ? 6.078  46.652 57.723 0.22 59.84  ? 104 ASP A OD1  1 
ATOM   1607 O OD2  A ASP A 1 101 ? 5.193  48.554 53.693 0.78 55.99  ? 104 ASP A OD2  1 
ATOM   1608 O OD2  B ASP A 1 101 ? 7.246  48.361 56.979 0.22 46.59  ? 104 ASP A OD2  1 
ATOM   1609 H H    . ASP A 1 101 ? 8.250  46.469 54.769 0.00 41.34  ? 104 ASP A H    1 
ATOM   1610 H HA   . ASP A 1 101 ? 6.155  45.066 55.538 0.00 49.43  ? 104 ASP A HA   1 
ATOM   1611 H HB2  A ASP A 1 101 ? 5.061  47.081 55.672 0.78 57.13  ? 104 ASP A HB2  1 
ATOM   1612 H HB2  B ASP A 1 101 ? 6.390  47.807 54.815 0.22 56.92  ? 104 ASP A HB2  1 
ATOM   1613 H HB3  A ASP A 1 101 ? 6.537  47.341 56.200 0.78 57.13  ? 104 ASP A HB3  1 
ATOM   1614 H HB3  B ASP A 1 101 ? 5.039  47.189 55.379 0.22 56.92  ? 104 ASP A HB3  1 
ATOM   1615 N N    . GLN A 1 102 ? 4.471  45.011 53.675 1.00 35.21  ? 105 GLN A N    1 
ATOM   1616 C CA   . GLN A 1 102 ? 3.737  44.534 52.520 1.00 37.17  ? 105 GLN A CA   1 
ATOM   1617 C C    . GLN A 1 102 ? 3.546  45.626 51.479 1.00 36.43  ? 105 GLN A C    1 
ATOM   1618 O O    . GLN A 1 102 ? 3.576  45.337 50.280 1.00 34.27  ? 105 GLN A O    1 
ATOM   1619 C CB   . GLN A 1 102 ? 2.371  44.000 52.963 1.00 53.82  ? 105 GLN A CB   1 
ATOM   1620 C CG   . GLN A 1 102 ? 2.299  42.495 52.958 1.00 71.45  ? 105 GLN A CG   1 
ATOM   1621 C CD   . GLN A 1 102 ? 1.033  41.981 53.605 1.00 96.72  ? 105 GLN A CD   1 
ATOM   1622 O OE1  . GLN A 1 102 ? 0.669  42.412 54.698 1.00 110.10 ? 105 GLN A OE1  1 
ATOM   1623 N NE2  . GLN A 1 102 ? 0.354  41.059 52.935 1.00 100.79 ? 105 GLN A NE2  1 
ATOM   1624 H H    . GLN A 1 102 ? 4.026  44.981 54.410 0.00 42.24  ? 105 GLN A H    1 
ATOM   1625 H HA   . GLN A 1 102 ? 4.244  43.815 52.112 0.00 44.58  ? 105 GLN A HA   1 
ATOM   1626 H HB2  . GLN A 1 102 ? 2.191  44.306 53.866 0.00 64.57  ? 105 GLN A HB2  1 
ATOM   1627 H HB3  . GLN A 1 102 ? 1.691  44.334 52.358 0.00 64.57  ? 105 GLN A HB3  1 
ATOM   1628 H HG2  . GLN A 1 102 ? 2.321  42.178 52.042 0.00 85.72  ? 105 GLN A HG2  1 
ATOM   1629 H HG3  . GLN A 1 102 ? 3.056  42.139 53.450 0.00 85.72  ? 105 GLN A HG3  1 
ATOM   1630 H HE21 . GLN A 1 102 ? 0.641  40.782 52.173 0.00 120.93 ? 105 GLN A HE21 1 
ATOM   1631 H HE22 . GLN A 1 102 ? -0.373 40.737 53.264 0.00 120.93 ? 105 GLN A HE22 1 
ATOM   1632 N N    . GLY A 1 103 ? 3.314  46.876 51.912 1.00 33.34  ? 106 GLY A N    1 
ATOM   1633 C CA   . GLY A 1 103 ? 3.116  47.962 50.931 1.00 36.78  ? 106 GLY A CA   1 
ATOM   1634 C C    . GLY A 1 103 ? 4.344  48.233 50.071 1.00 36.61  ? 106 GLY A C    1 
ATOM   1635 O O    . GLY A 1 103 ? 4.241  48.484 48.854 1.00 33.43  ? 106 GLY A O    1 
ATOM   1636 H H    . GLY A 1 103 ? 3.267  47.116 52.736 0.00 39.99  ? 106 GLY A H    1 
ATOM   1637 H HA2  . GLY A 1 103 ? 2.382  47.728 50.342 0.00 44.12  ? 106 GLY A HA2  1 
ATOM   1638 H HA3  . GLY A 1 103 ? 2.894  48.779 51.404 0.00 44.12  ? 106 GLY A HA3  1 
ATOM   1639 N N    . THR A 1 104 ? 5.526  48.167 50.680 1.00 29.24  ? 107 THR A N    1 
ATOM   1640 C CA   . THR A 1 104 ? 6.753  48.386 49.939 1.00 33.47  ? 107 THR A CA   1 
ATOM   1641 C C    . THR A 1 104 ? 7.003  47.240 48.959 1.00 32.77  ? 107 THR A C    1 
ATOM   1642 O O    . THR A 1 104 ? 7.463  47.461 47.829 1.00 29.85  ? 107 THR A O    1 
ATOM   1643 C CB   . THR A 1 104 ? 7.900  48.534 50.949 1.00 34.68  ? 107 THR A CB   1 
ATOM   1644 O OG1  . THR A 1 104 ? 7.635  49.679 51.816 1.00 37.54  ? 107 THR A OG1  1 
ATOM   1645 C CG2  . THR A 1 104 ? 9.197  48.737 50.243 1.00 39.51  ? 107 THR A CG2  1 
ATOM   1646 H H    . THR A 1 104 ? 5.640  47.997 51.515 0.00 35.07  ? 107 THR A H    1 
ATOM   1647 H HA   . THR A 1 104 ? 6.701  49.200 49.414 0.00 40.14  ? 107 THR A HA   1 
ATOM   1648 H HB   . THR A 1 104 ? 7.970  47.728 51.485 0.00 41.59  ? 107 THR A HB   1 
ATOM   1649 H HG1  . THR A 1 104 ? 8.261  49.774 52.367 0.00 45.03  ? 107 THR A HG1  1 
ATOM   1650 H HG21 . THR A 1 104 ? 9.879  49.014 50.875 0.00 47.39  ? 107 THR A HG21 1 
ATOM   1651 H HG22 . THR A 1 104 ? 9.477  47.911 49.819 0.00 47.39  ? 107 THR A HG22 1 
ATOM   1652 H HG23 . THR A 1 104 ? 9.101  49.423 49.564 0.00 47.39  ? 107 THR A HG23 1 
ATOM   1653 N N    . ILE A 1 105 ? 6.693  46.004 49.356 1.00 27.36  ? 108 ILE A N    1 
ATOM   1654 C CA   . ILE A 1 105 ? 6.842  44.856 48.429 1.00 29.66  ? 108 ILE A CA   1 
ATOM   1655 C C    . ILE A 1 105 ? 5.948  45.008 47.199 1.00 32.99  ? 108 ILE A C    1 
ATOM   1656 O O    . ILE A 1 105 ? 6.373  44.786 46.045 1.00 28.34  ? 108 ILE A O    1 
ATOM   1657 C CB   . ILE A 1 105 ? 6.544  43.536 49.168 1.00 28.50  ? 108 ILE A CB   1 
ATOM   1658 C CG1  . ILE A 1 105 ? 7.624  43.236 50.188 1.00 30.68  ? 108 ILE A CG1  1 
ATOM   1659 C CG2  . ILE A 1 105 ? 6.450  42.374 48.193 1.00 36.55  ? 108 ILE A CG2  1 
ATOM   1660 C CD1  . ILE A 1 105 ? 7.339  41.870 50.995 1.00 37.43  ? 108 ILE A CD1  1 
ATOM   1661 H H    . ILE A 1 105 ? 6.399  45.797 50.138 0.00 32.82  ? 108 ILE A H    1 
ATOM   1662 H HA   . ILE A 1 105 ? 7.762  44.845 48.120 0.00 35.57  ? 108 ILE A HA   1 
ATOM   1663 H HB   . ILE A 1 105 ? 5.692  43.645 49.619 0.00 34.18  ? 108 ILE A HB   1 
ATOM   1664 H HG12 . ILE A 1 105 ? 8.475  43.147 49.732 0.00 36.79  ? 108 ILE A HG12 1 
ATOM   1665 H HG13 . ILE A 1 105 ? 7.665  43.963 50.829 0.00 36.79  ? 108 ILE A HG13 1 
ATOM   1666 H HG21 . ILE A 1 105 ? 6.294  41.556 48.690 0.00 43.84  ? 108 ILE A HG21 1 
ATOM   1667 H HG22 . ILE A 1 105 ? 5.715  42.534 47.581 0.00 43.84  ? 108 ILE A HG22 1 
ATOM   1668 H HG23 . ILE A 1 105 ? 7.283  42.308 47.700 0.00 43.84  ? 108 ILE A HG23 1 
ATOM   1669 H HD11 . ILE A 1 105 ? 7.864  41.870 51.811 0.00 44.90  ? 108 ILE A HD11 1 
ATOM   1670 H HD12 . ILE A 1 105 ? 6.394  41.820 51.209 0.00 44.90  ? 108 ILE A HD12 1 
ATOM   1671 H HD13 . ILE A 1 105 ? 7.593  41.116 50.439 0.00 44.90  ? 108 ILE A HD13 1 
ATOM   1672 N N    . LEU A 1 106 ? 4.677  45.364 47.414 1.00 30.30  ? 109 LEU A N    1 
ATOM   1673 C CA   A LEU A 1 106 ? 3.787  45.568 46.280 0.60 29.02  ? 109 LEU A CA   1 
ATOM   1674 C CA   B LEU A 1 106 ? 3.750  45.619 46.311 0.40 29.11  ? 109 LEU A CA   1 
ATOM   1675 C C    . LEU A 1 106 ? 4.269  46.696 45.377 1.00 30.29  ? 109 LEU A C    1 
ATOM   1676 O O    . LEU A 1 106 ? 4.212  46.557 44.124 1.00 29.45  ? 109 LEU A O    1 
ATOM   1677 C CB   A LEU A 1 106 ? 2.354  45.826 46.778 0.60 31.62  ? 109 LEU A CB   1 
ATOM   1678 C CB   B LEU A 1 106 ? 2.391  46.047 46.878 0.40 31.47  ? 109 LEU A CB   1 
ATOM   1679 C CG   A LEU A 1 106 ? 1.370  46.025 45.620 0.60 35.07  ? 109 LEU A CG   1 
ATOM   1680 C CG   B LEU A 1 106 ? 1.546  44.966 47.506 0.40 33.94  ? 109 LEU A CG   1 
ATOM   1681 C CD1  A LEU A 1 106 ? 1.292  44.786 44.749 0.60 42.30  ? 109 LEU A CD1  1 
ATOM   1682 C CD1  B LEU A 1 106 ? 0.588  45.571 48.543 0.40 31.19  ? 109 LEU A CD1  1 
ATOM   1683 C CD2  A LEU A 1 106 ? 0.014  46.362 46.166 0.60 41.51  ? 109 LEU A CD2  1 
ATOM   1684 C CD2  B LEU A 1 106 ? 0.784  44.262 46.415 0.40 38.08  ? 109 LEU A CD2  1 
ATOM   1685 H H    A LEU A 1 106 ? 4.320  45.488 48.186 0.60 36.34  ? 109 LEU A H    1 
ATOM   1686 H H    B LEU A 1 106 ? 4.327  45.465 48.193 0.40 36.34  ? 109 LEU A H    1 
ATOM   1687 H HA   A LEU A 1 106 ? 3.774  44.760 45.743 0.60 34.81  ? 109 LEU A HA   1 
ATOM   1688 H HA   B LEU A 1 106 ? 3.649  44.799 45.802 0.40 34.92  ? 109 LEU A HA   1 
ATOM   1689 H HB2  A LEU A 1 106 ? 2.058  45.065 47.302 0.60 37.92  ? 109 LEU A HB2  1 
ATOM   1690 H HB2  B LEU A 1 106 ? 2.549  46.717 47.561 0.40 37.74  ? 109 LEU A HB2  1 
ATOM   1691 H HB3  A LEU A 1 106 ? 2.347  46.628 47.324 0.60 37.92  ? 109 LEU A HB3  1 
ATOM   1692 H HB3  B LEU A 1 106 ? 1.871  46.429 46.153 0.40 37.74  ? 109 LEU A HB3  1 
ATOM   1693 H HG   A LEU A 1 106 ? 1.681  46.755 45.062 0.60 42.06  ? 109 LEU A HG   1 
ATOM   1694 H HG   B LEU A 1 106 ? 2.104  44.323 47.971 0.40 40.71  ? 109 LEU A HG   1 
ATOM   1695 H HD11 A LEU A 1 106 ? 0.506  44.846 44.184 0.60 50.74  ? 109 LEU A HD11 1 
ATOM   1696 H HD11 B LEU A 1 106 ? 0.131  44.853 49.008 0.40 37.40  ? 109 LEU A HD11 1 
ATOM   1697 H HD12 A LEU A 1 106 ? 2.090  44.735 44.200 0.60 50.74  ? 109 LEU A HD12 1 
ATOM   1698 H HD12 B LEU A 1 106 ? 1.100  46.100 49.175 0.40 37.40  ? 109 LEU A HD12 1 
ATOM   1699 H HD13 A LEU A 1 106 ? 1.232  44.002 45.317 0.60 50.74  ? 109 LEU A HD13 1 
ATOM   1700 H HD13 B LEU A 1 106 ? -0.057 46.133 48.087 0.40 37.40  ? 109 LEU A HD13 1 
ATOM   1701 H HD21 A LEU A 1 106 ? -0.592 46.526 45.427 0.60 49.79  ? 109 LEU A HD21 1 
ATOM   1702 H HD21 B LEU A 1 106 ? 0.246  43.558 46.810 0.40 45.68  ? 109 LEU A HD21 1 
ATOM   1703 H HD22 A LEU A 1 106 ? -0.307 45.618 46.699 0.60 49.79  ? 109 LEU A HD22 1 
ATOM   1704 H HD22 B LEU A 1 106 ? 0.212  44.902 45.965 0.40 45.68  ? 109 LEU A HD22 1 
ATOM   1705 H HD23 A LEU A 1 106 ? 0.085  47.157 46.718 0.60 49.79  ? 109 LEU A HD23 1 
ATOM   1706 H HD23 B LEU A 1 106 ? 1.415  43.881 45.785 0.40 45.68  ? 109 LEU A HD23 1 
ATOM   1707 N N    . ALA A 1 107 ? 4.751  47.793 45.946 1.00 26.40  ? 110 ALA A N    1 
ATOM   1708 C CA   . ALA A 1 107 ? 5.295  48.892 45.132 1.00 26.87  ? 110 ALA A CA   1 
ATOM   1709 C C    . ALA A 1 107 ? 6.430  48.399 44.238 1.00 29.56  ? 110 ALA A C    1 
ATOM   1710 O O    . ALA A 1 107 ? 6.545  48.796 43.073 1.00 29.51  ? 110 ALA A O    1 
ATOM   1711 C CB   . ALA A 1 107 ? 5.811  50.000 46.044 1.00 34.34  ? 110 ALA A CB   1 
ATOM   1712 H H    . ALA A 1 107 ? 4.779  47.933 46.794 0.00 31.67  ? 110 ALA A H    1 
ATOM   1713 H HA   . ALA A 1 107 ? 4.585  49.246 44.574 0.00 32.23  ? 110 ALA A HA   1 
ATOM   1714 H HB1  . ALA A 1 107 ? 6.245  50.678 45.503 0.00 41.19  ? 110 ALA A HB1  1 
ATOM   1715 H HB2  . ALA A 1 107 ? 5.063  50.389 46.524 0.00 41.19  ? 110 ALA A HB2  1 
ATOM   1716 H HB3  . ALA A 1 107 ? 6.446  49.622 46.673 0.00 41.19  ? 110 ALA A HB3  1 
ATOM   1717 N N    . LEU A 1 108 ? 7.338  47.601 44.814 1.00 26.36  ? 111 LEU A N    1 
ATOM   1718 C CA   . LEU A 1 108 ? 8.525  47.136 44.110 1.00 28.90  ? 111 LEU A CA   1 
ATOM   1719 C C    . LEU A 1 108 ? 8.134  46.183 42.994 1.00 31.45  ? 111 LEU A C    1 
ATOM   1720 O O    . LEU A 1 108 ? 8.651  46.273 41.873 1.00 29.23  ? 111 LEU A O    1 
ATOM   1721 C CB   . LEU A 1 108 ? 9.504  46.414 45.084 1.00 29.06  ? 111 LEU A CB   1 
ATOM   1722 C CG   . LEU A 1 108 ? 10.411 47.240 45.989 1.00 35.70  ? 111 LEU A CG   1 
ATOM   1723 C CD1  . LEU A 1 108 ? 11.140 46.337 47.012 1.00 42.04  ? 111 LEU A CD1  1 
ATOM   1724 C CD2  . LEU A 1 108 ? 11.468 48.033 45.166 1.00 42.70  ? 111 LEU A CD2  1 
ATOM   1725 H H    . LEU A 1 108 ? 7.284  47.314 45.623 0.00 31.61  ? 111 LEU A H    1 
ATOM   1726 H HA   . LEU A 1 108 ? 8.982  47.908 43.741 0.00 34.67  ? 111 LEU A HA   1 
ATOM   1727 H HB2  . LEU A 1 108 ? 8.969  45.857 45.671 0.00 34.85  ? 111 LEU A HB2  1 
ATOM   1728 H HB3  . LEU A 1 108 ? 10.090 45.859 44.546 0.00 34.85  ? 111 LEU A HB3  1 
ATOM   1729 H HG   . LEU A 1 108 ? 9.851  47.873 46.465 0.00 42.82  ? 111 LEU A HG   1 
ATOM   1730 H HD11 . LEU A 1 108 ? 11.760 46.878 47.525 0.00 50.43  ? 111 LEU A HD11 1 
ATOM   1731 H HD12 . LEU A 1 108 ? 10.484 45.935 47.603 0.00 50.43  ? 111 LEU A HD12 1 
ATOM   1732 H HD13 . LEU A 1 108 ? 11.622 45.644 46.534 0.00 50.43  ? 111 LEU A HD13 1 
ATOM   1733 H HD21 . LEU A 1 108 ? 12.060 48.498 45.777 0.00 51.22  ? 111 LEU A HD21 1 
ATOM   1734 H HD22 . LEU A 1 108 ? 11.976 47.412 44.621 0.00 51.22  ? 111 LEU A HD22 1 
ATOM   1735 H HD23 . LEU A 1 108 ? 11.010 48.673 44.598 0.00 51.22  ? 111 LEU A HD23 1 
ATOM   1736 N N    . VAL A 1 109 ? 7.313  45.166 43.324 1.00 26.56  ? 112 VAL A N    1 
ATOM   1737 C CA   . VAL A 1 109 ? 6.899  44.195 42.296 1.00 26.14  ? 112 VAL A CA   1 
ATOM   1738 C C    . VAL A 1 109 ? 6.110  44.889 41.191 1.00 27.66  ? 112 VAL A C    1 
ATOM   1739 O O    . VAL A 1 109 ? 6.248  44.549 40.015 1.00 24.94  ? 112 VAL A O    1 
ATOM   1740 C CB   . VAL A 1 109 ? 6.096  43.061 42.954 1.00 28.94  ? 112 VAL A CB   1 
ATOM   1741 C CG1  . VAL A 1 109 ? 5.415  42.179 41.843 1.00 32.68  ? 112 VAL A CG1  1 
ATOM   1742 C CG2  . VAL A 1 109 ? 7.024  42.220 43.797 1.00 33.65  ? 112 VAL A CG2  1 
ATOM   1743 H H    . VAL A 1 109 ? 6.993  45.022 44.109 0.00 31.85  ? 112 VAL A H    1 
ATOM   1744 H HA   . VAL A 1 109 ? 7.689  43.809 41.887 0.00 31.35  ? 112 VAL A HA   1 
ATOM   1745 H HB   . VAL A 1 109 ? 5.401  43.429 43.522 0.00 34.71  ? 112 VAL A HB   1 
ATOM   1746 H HG11 . VAL A 1 109 ? 5.120  41.344 42.239 0.00 39.19  ? 112 VAL A HG11 1 
ATOM   1747 H HG12 . VAL A 1 109 ? 4.655  42.660 41.480 0.00 39.19  ? 112 VAL A HG12 1 
ATOM   1748 H HG13 . VAL A 1 109 ? 6.061  42.002 41.141 0.00 39.19  ? 112 VAL A HG13 1 
ATOM   1749 H HG21 . VAL A 1 109 ? 6.504  41.544 44.260 0.00 40.36  ? 112 VAL A HG21 1 
ATOM   1750 H HG22 . VAL A 1 109 ? 7.678  41.797 43.220 0.00 40.36  ? 112 VAL A HG22 1 
ATOM   1751 H HG23 . VAL A 1 109 ? 7.471  42.792 44.441 0.00 40.36  ? 112 VAL A HG23 1 
ATOM   1752 N N    . GLY A 1 110 ? 5.252  45.871 41.535 1.00 23.39  ? 113 GLY A N    1 
ATOM   1753 C CA   . GLY A 1 110 ? 4.461  46.524 40.492 1.00 25.92  ? 113 GLY A CA   1 
ATOM   1754 C C    . GLY A 1 110 ? 5.322  47.396 39.584 1.00 27.28  ? 113 GLY A C    1 
ATOM   1755 O O    . GLY A 1 110 ? 5.144  47.416 38.354 1.00 23.63  ? 113 GLY A O    1 
ATOM   1756 H H    . GLY A 1 110 ? 5.119  46.160 42.333 0.00 28.05  ? 113 GLY A H    1 
ATOM   1757 H HA2  . GLY A 1 110 ? 4.025  45.850 39.948 0.00 31.08  ? 113 GLY A HA2  1 
ATOM   1758 H HA3  . GLY A 1 110 ? 3.784  47.083 40.904 0.00 31.08  ? 113 GLY A HA3  1 
ATOM   1759 N N    . ALA A 1 111 ? 6.291  48.131 40.173 1.00 22.56  ? 114 ALA A N    1 
ATOM   1760 C CA   . ALA A 1 111 ? 7.185  48.933 39.332 1.00 20.89  ? 114 ALA A CA   1 
ATOM   1761 C C    . ALA A 1 111 ? 8.021  48.024 38.434 1.00 21.11  ? 114 ALA A C    1 
ATOM   1762 O O    . ALA A 1 111 ? 8.411  48.389 37.329 1.00 22.07  ? 114 ALA A O    1 
ATOM   1763 C CB   . ALA A 1 111 ? 8.107  49.779 40.273 1.00 26.63  ? 114 ALA A CB   1 
ATOM   1764 H H    . ALA A 1 111 ? 6.440  48.175 41.019 0.00 27.06  ? 114 ALA A H    1 
ATOM   1765 H HA   . ALA A 1 111 ? 6.678  49.532 38.763 0.00 25.05  ? 114 ALA A HA   1 
ATOM   1766 H HB1  . ALA A 1 111 ? 8.711  50.310 39.729 0.00 31.94  ? 114 ALA A HB1  1 
ATOM   1767 H HB2  . ALA A 1 111 ? 7.554  50.361 40.817 0.00 31.94  ? 114 ALA A HB2  1 
ATOM   1768 H HB3  . ALA A 1 111 ? 8.615  49.179 40.841 0.00 31.94  ? 114 ALA A HB3  1 
ATOM   1769 N N    . ASP A 1 112 ? 8.406  46.835 38.966 1.00 20.97  ? 115 ASP A N    1 
ATOM   1770 C CA   . ASP A 1 112 ? 9.203  45.905 38.152 1.00 21.04  ? 115 ASP A CA   1 
ATOM   1771 C C    . ASP A 1 112 ? 8.398  45.395 36.977 1.00 22.93  ? 115 ASP A C    1 
ATOM   1772 O O    . ASP A 1 112 ? 8.942  45.263 35.846 1.00 22.37  ? 115 ASP A O    1 
ATOM   1773 C CB   . ASP A 1 112 ? 9.658  44.750 39.070 1.00 20.18  ? 115 ASP A CB   1 
ATOM   1774 C CG   . ASP A 1 112 ? 10.699 43.817 38.383 1.00 27.10  ? 115 ASP A CG   1 
ATOM   1775 O OD1  . ASP A 1 112 ? 10.281 42.967 37.623 1.00 28.91  ? 115 ASP A OD1  1 
ATOM   1776 O OD2  . ASP A 1 112 ? 11.887 44.025 38.612 1.00 34.44  ? 115 ASP A OD2  1 
ATOM   1777 H H    . ASP A 1 112 ? 8.224  46.562 39.761 0.00 25.15  ? 115 ASP A H    1 
ATOM   1778 H HA   . ASP A 1 112 ? 9.987  46.346 37.788 0.00 25.23  ? 115 ASP A HA   1 
ATOM   1779 H HB2  . ASP A 1 112 ? 10.066 45.121 39.867 0.00 24.20  ? 115 ASP A HB2  1 
ATOM   1780 H HB3  . ASP A 1 112 ? 8.886  44.214 39.310 0.00 24.20  ? 115 ASP A HB3  1 
ATOM   1781 N N    . GLY A 1 113 ? 7.125  45.050 37.199 1.00 22.47  ? 116 GLY A N    1 
ATOM   1782 C CA   . GLY A 1 113 ? 6.244  44.650 36.084 1.00 22.54  ? 116 GLY A CA   1 
ATOM   1783 C C    . GLY A 1 113 ? 6.158  45.736 35.029 1.00 23.13  ? 116 GLY A C    1 
ATOM   1784 O O    . GLY A 1 113 ? 6.122  45.457 33.822 1.00 23.67  ? 116 GLY A O    1 
ATOM   1785 H H    . GLY A 1 113 ? 6.747  45.037 37.971 0.00 26.94  ? 116 GLY A H    1 
ATOM   1786 H HA2  . GLY A 1 113 ? 6.590  43.843 35.671 0.00 27.03  ? 116 GLY A HA2  1 
ATOM   1787 H HA3  . GLY A 1 113 ? 5.352  44.474 36.422 0.00 27.03  ? 116 GLY A HA3  1 
ATOM   1788 N N    . ILE A 1 114 ? 6.027  47.005 35.468 1.00 20.24  ? 117 ILE A N    1 
ATOM   1789 C CA   . ILE A 1 114 ? 5.947  48.081 34.487 1.00 19.38  ? 117 ILE A CA   1 
ATOM   1790 C C    . ILE A 1 114 ? 7.274  48.135 33.700 1.00 20.63  ? 117 ILE A C    1 
ATOM   1791 O O    . ILE A 1 114 ? 7.255  48.364 32.484 1.00 22.00  ? 117 ILE A O    1 
ATOM   1792 C CB   . ILE A 1 114 ? 5.616  49.419 35.184 1.00 22.40  ? 117 ILE A CB   1 
ATOM   1793 C CG1  . ILE A 1 114 ? 4.152  49.359 35.655 1.00 26.48  ? 117 ILE A CG1  1 
ATOM   1794 C CG2  . ILE A 1 114 ? 5.827  50.612 34.243 1.00 27.11  ? 117 ILE A CG2  1 
ATOM   1795 C CD1  . ILE A 1 114 ? 3.737  50.538 36.555 1.00 32.06  ? 117 ILE A CD1  1 
ATOM   1796 H H    . ILE A 1 114 ? 5.984  47.248 36.292 0.00 24.26  ? 117 ILE A H    1 
ATOM   1797 H HA   . ILE A 1 114 ? 5.227  47.906 33.862 0.00 23.23  ? 117 ILE A HA   1 
ATOM   1798 H HB   . ILE A 1 114 ? 6.213  49.543 35.939 0.00 26.86  ? 117 ILE A HB   1 
ATOM   1799 H HG12 . ILE A 1 114 ? 3.574  49.365 34.876 0.00 31.76  ? 117 ILE A HG12 1 
ATOM   1800 H HG13 . ILE A 1 114 ? 4.020  48.542 36.160 0.00 31.76  ? 117 ILE A HG13 1 
ATOM   1801 H HG21 . ILE A 1 114 ? 5.430  51.403 34.641 0.00 32.51  ? 117 ILE A HG21 1 
ATOM   1802 H HG22 . ILE A 1 114 ? 6.778  50.749 34.114 0.00 32.51  ? 117 ILE A HG22 1 
ATOM   1803 H HG23 . ILE A 1 114 ? 5.401  50.422 33.392 0.00 32.51  ? 117 ILE A HG23 1 
ATOM   1804 H HD11 . ILE A 1 114 ? 2.829  50.396 36.864 0.00 38.45  ? 117 ILE A HD11 1 
ATOM   1805 H HD12 . ILE A 1 114 ? 4.340  50.584 37.314 0.00 38.45  ? 117 ILE A HD12 1 
ATOM   1806 H HD13 . ILE A 1 114 ? 3.787  51.360 36.043 0.00 38.45  ? 117 ILE A HD13 1 
ATOM   1807 N N    . MET A 1 115 ? 8.408  48.001 34.396 1.00 20.31  ? 118 MET A N    1 
ATOM   1808 C CA   . MET A 1 115 ? 9.736  48.111 33.759 1.00 19.51  ? 118 MET A CA   1 
ATOM   1809 C C    . MET A 1 115 ? 9.841  47.047 32.672 1.00 22.62  ? 118 MET A C    1 
ATOM   1810 O O    . MET A 1 115 ? 10.265 47.328 31.541 1.00 21.69  ? 118 MET A O    1 
ATOM   1811 C CB   . MET A 1 115 ? 10.854 47.860 34.814 1.00 20.29  ? 118 MET A CB   1 
ATOM   1812 C CG   . MET A 1 115 ? 12.264 47.737 34.181 1.00 23.94  ? 118 MET A CG   1 
ATOM   1813 S SD   . MET A 1 115 ? 13.506 47.583 35.580 1.00 24.60  ? 118 MET A SD   1 
ATOM   1814 C CE   . MET A 1 115 ? 13.369 45.849 35.913 1.00 24.57  ? 118 MET A CE   1 
ATOM   1815 H H    . MET A 1 115 ? 8.442  47.846 35.241 0.00 24.36  ? 118 MET A H    1 
ATOM   1816 H HA   . MET A 1 115 ? 9.851  49.004 33.398 0.00 23.40  ? 118 MET A HA   1 
ATOM   1817 H HB2  . MET A 1 115 ? 10.870 48.602 35.439 0.00 24.32  ? 118 MET A HB2  1 
ATOM   1818 H HB3  . MET A 1 115 ? 10.664 47.033 35.284 0.00 24.32  ? 118 MET A HB3  1 
ATOM   1819 H HG2  . MET A 1 115 ? 12.312 46.947 33.621 0.00 28.71  ? 118 MET A HG2  1 
ATOM   1820 H HG3  . MET A 1 115 ? 12.466 48.528 33.657 0.00 28.71  ? 118 MET A HG3  1 
ATOM   1821 H HE1  . MET A 1 115 ? 13.971 45.618 36.639 0.00 29.46  ? 118 MET A HE1  1 
ATOM   1822 H HE2  . MET A 1 115 ? 12.455 45.647 36.165 0.00 29.46  ? 118 MET A HE2  1 
ATOM   1823 H HE3  . MET A 1 115 ? 13.610 45.354 35.114 0.00 29.46  ? 118 MET A HE3  1 
ATOM   1824 N N    . ILE A 1 116 ? 9.476  45.787 33.006 1.00 20.22  ? 119 ILE A N    1 
ATOM   1825 C CA   . ILE A 1 116 ? 9.693  44.722 31.999 1.00 22.59  ? 119 ILE A CA   1 
ATOM   1826 C C    . ILE A 1 116 ? 8.632  44.838 30.896 1.00 21.78  ? 119 ILE A C    1 
ATOM   1827 O O    . ILE A 1 116 ? 8.936  44.607 29.712 1.00 21.35  ? 119 ILE A O    1 
ATOM   1828 C CB   . ILE A 1 116 ? 9.647  43.317 32.634 1.00 22.88  ? 119 ILE A CB   1 
ATOM   1829 C CG1  . ILE A 1 116 ? 10.775 43.125 33.674 1.00 22.49  ? 119 ILE A CG1  1 
ATOM   1830 C CG2  . ILE A 1 116 ? 9.797  42.253 31.498 1.00 25.90  ? 119 ILE A CG2  1 
ATOM   1831 C CD1  . ILE A 1 116 ? 12.199 43.490 33.098 1.00 23.07  ? 119 ILE A CD1  1 
ATOM   1832 H H    . ILE A 1 116 ? 9.127  45.542 33.752 0.00 24.24  ? 119 ILE A H    1 
ATOM   1833 H HA   . ILE A 1 116 ? 10.579 44.846 31.625 0.00 27.08  ? 119 ILE A HA   1 
ATOM   1834 H HB   . ILE A 1 116 ? 8.800  43.214 33.096 0.00 27.43  ? 119 ILE A HB   1 
ATOM   1835 H HG12 . ILE A 1 116 ? 10.603 43.698 34.437 0.00 26.97  ? 119 ILE A HG12 1 
ATOM   1836 H HG13 . ILE A 1 116 ? 10.793 42.196 33.953 0.00 26.97  ? 119 ILE A HG13 1 
ATOM   1837 H HG21 . ILE A 1 116 ? 10.024 41.397 31.894 0.00 31.06  ? 119 ILE A HG21 1 
ATOM   1838 H HG22 . ILE A 1 116 ? 8.956  42.183 31.018 0.00 31.06  ? 119 ILE A HG22 1 
ATOM   1839 H HG23 . ILE A 1 116 ? 10.500 42.535 30.893 0.00 31.06  ? 119 ILE A HG23 1 
ATOM   1840 H HD11 . ILE A 1 116 ? 12.879 43.193 33.723 0.00 27.67  ? 119 ILE A HD11 1 
ATOM   1841 H HD12 . ILE A 1 116 ? 12.319 43.045 32.244 0.00 27.67  ? 119 ILE A HD12 1 
ATOM   1842 H HD13 . ILE A 1 116 ? 12.255 44.451 32.980 0.00 27.67  ? 119 ILE A HD13 1 
ATOM   1843 N N    . GLY A 1 117 ? 7.380  45.129 31.248 1.00 19.05  ? 120 GLY A N    1 
ATOM   1844 C CA   . GLY A 1 117 ? 6.313  45.184 30.231 1.00 20.85  ? 120 GLY A CA   1 
ATOM   1845 C C    . GLY A 1 117 ? 6.557  46.303 29.207 1.00 23.76  ? 120 GLY A C    1 
ATOM   1846 O O    . GLY A 1 117 ? 6.328  46.119 27.996 1.00 22.72  ? 120 GLY A O    1 
ATOM   1847 H H    . GLY A 1 117 ? 7.120  45.297 32.050 0.00 22.85  ? 120 GLY A H    1 
ATOM   1848 H HA2  . GLY A 1 117 ? 6.272  44.338 29.760 0.00 25.00  ? 120 GLY A HA2  1 
ATOM   1849 H HA3  . GLY A 1 117 ? 5.461  45.345 30.666 0.00 25.00  ? 120 GLY A HA3  1 
ATOM   1850 N N    . THR A 1 118 ? 7.033  47.478 29.666 1.00 21.32  ? 121 THR A N    1 
ATOM   1851 C CA   . THR A 1 118 ? 7.291  48.543 28.713 1.00 19.74  ? 121 THR A CA   1 
ATOM   1852 C C    . THR A 1 118 ? 8.566  48.245 27.897 1.00 23.94  ? 121 THR A C    1 
ATOM   1853 O O    . THR A 1 118 ? 8.673  48.692 26.748 1.00 22.57  ? 121 THR A O    1 
ATOM   1854 C CB   . THR A 1 118 ? 7.382  49.947 29.395 1.00 22.23  ? 121 THR A CB   1 
ATOM   1855 O OG1  . THR A 1 118 ? 8.403  49.926 30.436 1.00 22.74  ? 121 THR A OG1  1 
ATOM   1856 C CG2  . THR A 1 118 ? 6.065  50.374 29.975 1.00 24.71  ? 121 THR A CG2  1 
ATOM   1857 H H    . THR A 1 118 ? 7.202  47.663 30.489 0.00 25.57  ? 121 THR A H    1 
ATOM   1858 H HA   . THR A 1 118 ? 6.533  48.595 28.110 0.00 23.67  ? 121 THR A HA   1 
ATOM   1859 H HB   . THR A 1 118 ? 7.622  50.603 28.722 0.00 26.66  ? 121 THR A HB   1 
ATOM   1860 H HG1  . THR A 1 118 ? 8.211  49.348 31.015 0.00 27.27  ? 121 THR A HG1  1 
ATOM   1861 H HG21 . THR A 1 118 ? 6.153  51.246 30.392 0.00 29.63  ? 121 THR A HG21 1 
ATOM   1862 H HG22 . THR A 1 118 ? 5.395  50.426 29.276 0.00 29.63  ? 121 THR A HG22 1 
ATOM   1863 H HG23 . THR A 1 118 ? 5.774  49.734 30.644 0.00 29.63  ? 121 THR A HG23 1 
ATOM   1864 N N    . GLY A 1 119 ? 9.552  47.563 28.495 1.00 21.83  ? 122 GLY A N    1 
ATOM   1865 C CA   . GLY A 1 119 ? 10.679 47.047 27.714 1.00 24.15  ? 122 GLY A CA   1 
ATOM   1866 C C    . GLY A 1 119 ? 10.241 46.154 26.569 1.00 25.88  ? 122 GLY A C    1 
ATOM   1867 O O    . GLY A 1 119 ? 10.755 46.278 25.472 1.00 23.18  ? 122 GLY A O    1 
ATOM   1868 H H    . GLY A 1 119 ? 9.592  47.389 29.336 0.00 26.17  ? 122 GLY A H    1 
ATOM   1869 H HA2  . GLY A 1 119 ? 11.179 47.792 27.344 0.00 28.96  ? 122 GLY A HA2  1 
ATOM   1870 H HA3  . GLY A 1 119 ? 11.261 46.534 28.295 0.00 28.96  ? 122 GLY A HA3  1 
ATOM   1871 N N    . LEU A 1 120 ? 9.294  45.243 26.820 1.00 21.76  ? 123 LEU A N    1 
ATOM   1872 C CA   . LEU A 1 120 ? 8.795  44.364 25.760 1.00 20.16  ? 123 LEU A CA   1 
ATOM   1873 C C    . LEU A 1 120 ? 8.070  45.167 24.661 1.00 20.30  ? 123 LEU A C    1 
ATOM   1874 O O    . LEU A 1 120 ? 8.234  44.886 23.452 1.00 23.37  ? 123 LEU A O    1 
ATOM   1875 C CB   . LEU A 1 120 ? 7.814  43.364 26.403 1.00 20.10  ? 123 LEU A CB   1 
ATOM   1876 C CG   . LEU A 1 120 ? 7.090  42.414 25.422 1.00 26.94  ? 123 LEU A CG   1 
ATOM   1877 C CD1  . LEU A 1 120 ? 8.043  41.516 24.651 1.00 25.90  ? 123 LEU A CD1  1 
ATOM   1878 C CD2  . LEU A 1 120 ? 6.123  41.589 26.280 1.00 32.55  ? 123 LEU A CD2  1 
ATOM   1879 H H    . LEU A 1 120 ? 8.928  45.116 27.587 0.00 26.10  ? 123 LEU A H    1 
ATOM   1880 H HA   . LEU A 1 120 ? 9.535  43.894 25.346 0.00 24.17  ? 123 LEU A HA   1 
ATOM   1881 H HB2  . LEU A 1 120 ? 8.310  42.811 27.028 0.00 24.11  ? 123 LEU A HB2  1 
ATOM   1882 H HB3  . LEU A 1 120 ? 7.132  43.867 26.875 0.00 24.11  ? 123 LEU A HB3  1 
ATOM   1883 H HG   . LEU A 1 120 ? 6.625  42.918 24.736 0.00 32.30  ? 123 LEU A HG   1 
ATOM   1884 H HD11 . LEU A 1 120 ? 7.527  40.903 24.104 0.00 31.06  ? 123 LEU A HD11 1 
ATOM   1885 H HD12 . LEU A 1 120 ? 8.609  42.066 24.087 0.00 31.06  ? 123 LEU A HD12 1 
ATOM   1886 H HD13 . LEU A 1 120 ? 8.588  41.018 25.281 0.00 31.06  ? 123 LEU A HD13 1 
ATOM   1887 H HD21 . LEU A 1 120 ? 5.634  40.979 25.706 0.00 39.04  ? 123 LEU A HD21 1 
ATOM   1888 H HD22 . LEU A 1 120 ? 6.632  41.089 26.937 0.00 39.04  ? 123 LEU A HD22 1 
ATOM   1889 H HD23 . LEU A 1 120 ? 5.507  42.190 26.727 0.00 39.04  ? 123 LEU A HD23 1 
ATOM   1890 N N    . VAL A 1 121 ? 7.190  46.110 25.062 1.00 19.27  ? 124 VAL A N    1 
ATOM   1891 C CA   . VAL A 1 121 ? 6.526  46.935 24.060 1.00 20.90  ? 124 VAL A CA   1 
ATOM   1892 C C    . VAL A 1 121 ? 7.553  47.696 23.209 1.00 21.33  ? 124 VAL A C    1 
ATOM   1893 O O    . VAL A 1 121 ? 7.442  47.762 21.997 1.00 23.43  ? 124 VAL A O    1 
ATOM   1894 C CB   . VAL A 1 121 ? 5.552  47.923 24.716 1.00 22.45  ? 124 VAL A CB   1 
ATOM   1895 C CG1  . VAL A 1 121 ? 5.025  48.924 23.672 1.00 25.65  ? 124 VAL A CG1  1 
ATOM   1896 C CG2  . VAL A 1 121 ? 4.359  47.127 25.391 1.00 28.35  ? 124 VAL A CG2  1 
ATOM   1897 H H    . VAL A 1 121 ? 6.976  46.277 25.878 0.00 23.11  ? 124 VAL A H    1 
ATOM   1898 H HA   . VAL A 1 121 ? 6.022  46.337 23.487 0.00 25.06  ? 124 VAL A HA   1 
ATOM   1899 H HB   . VAL A 1 121 ? 6.012  48.428 25.405 0.00 26.92  ? 124 VAL A HB   1 
ATOM   1900 H HG11 . VAL A 1 121 ? 4.231  49.358 24.023 0.00 30.76  ? 124 VAL A HG11 1 
ATOM   1901 H HG12 . VAL A 1 121 ? 5.712  49.586 23.493 0.00 30.76  ? 124 VAL A HG12 1 
ATOM   1902 H HG13 . VAL A 1 121 ? 4.808  48.445 22.857 0.00 30.76  ? 124 VAL A HG13 1 
ATOM   1903 H HG21 . VAL A 1 121 ? 3.768  47.757 25.831 0.00 34.01  ? 124 VAL A HG21 1 
ATOM   1904 H HG22 . VAL A 1 121 ? 3.875  46.642 24.704 0.00 34.01  ? 124 VAL A HG22 1 
ATOM   1905 H HG23 . VAL A 1 121 ? 4.722  46.505 26.040 0.00 34.01  ? 124 VAL A HG23 1 
ATOM   1906 N N    . GLY A 1 122 ? 8.592  48.259 23.850 1.00 22.83  ? 125 GLY A N    1 
ATOM   1907 C CA   . GLY A 1 122 ? 9.590  48.960 23.054 1.00 23.71  ? 125 GLY A CA   1 
ATOM   1908 C C    . GLY A 1 122 ? 10.306 48.025 22.106 1.00 22.97  ? 125 GLY A C    1 
ATOM   1909 O O    . GLY A 1 122 ? 10.640 48.403 20.987 1.00 25.21  ? 125 GLY A O    1 
ATOM   1910 H H    . GLY A 1 122 ? 8.728  48.246 24.699 0.00 27.38  ? 125 GLY A H    1 
ATOM   1911 H HA2  . GLY A 1 122 ? 9.159  49.656 22.534 0.00 28.44  ? 125 GLY A HA2  1 
ATOM   1912 H HA3  . GLY A 1 122 ? 10.247 49.365 23.642 0.00 28.44  ? 125 GLY A HA3  1 
ATOM   1913 N N    . ALA A 1 123 ? 10.602 46.786 22.573 1.00 21.64  ? 126 ALA A N    1 
ATOM   1914 C CA   . ALA A 1 123 ? 11.298 45.817 21.736 1.00 23.46  ? 126 ALA A CA   1 
ATOM   1915 C C    . ALA A 1 123 ? 10.497 45.426 20.483 1.00 27.09  ? 126 ALA A C    1 
ATOM   1916 O O    . ALA A 1 123 ? 11.075 45.105 19.426 1.00 23.82  ? 126 ALA A O    1 
ATOM   1917 C CB   . ALA A 1 123 ? 11.621 44.556 22.569 1.00 25.37  ? 126 ALA A CB   1 
ATOM   1918 H H    . ALA A 1 123 ? 10.407 46.499 23.360 0.00 25.94  ? 126 ALA A H    1 
ATOM   1919 H HA   . ALA A 1 123 ? 12.126 46.221 21.432 0.00 28.13  ? 126 ALA A HA   1 
ATOM   1920 H HB1  . ALA A 1 123 ? 12.090 43.919 22.008 0.00 30.43  ? 126 ALA A HB1  1 
ATOM   1921 H HB2  . ALA A 1 123 ? 12.179 44.809 23.321 0.00 30.43  ? 126 ALA A HB2  1 
ATOM   1922 H HB3  . ALA A 1 123 ? 10.791 44.168 22.888 0.00 30.43  ? 126 ALA A HB3  1 
ATOM   1923 N N    . LEU A 1 124 ? 9.164  45.433 20.566 1.00 21.14  ? 127 LEU A N    1 
ATOM   1924 C CA   . LEU A 1 124 ? 8.307  44.995 19.463 1.00 22.55  ? 127 LEU A CA   1 
ATOM   1925 C C    . LEU A 1 124 ? 7.682  46.160 18.672 1.00 23.45  ? 127 LEU A C    1 
ATOM   1926 O O    . LEU A 1 124 ? 6.958  45.912 17.686 1.00 25.11  ? 127 LEU A O    1 
ATOM   1927 C CB   . LEU A 1 124 ? 7.173  44.114 20.027 1.00 25.82  ? 127 LEU A CB   1 
ATOM   1928 C CG   . LEU A 1 124 ? 7.627  42.818 20.742 1.00 25.51  ? 127 LEU A CG   1 
ATOM   1929 C CD1  . LEU A 1 124 ? 6.398  42.071 21.299 1.00 31.00  ? 127 LEU A CD1  1 
ATOM   1930 C CD2  . LEU A 1 124 ? 8.324  41.950 19.711 1.00 28.86  ? 127 LEU A CD2  1 
ATOM   1931 H H    . LEU A 1 124 ? 8.728  45.692 21.261 0.00 25.35  ? 127 LEU A H    1 
ATOM   1932 H HA   . LEU A 1 124 ? 8.842  44.475 18.844 0.00 27.04  ? 127 LEU A HA   1 
ATOM   1933 H HB2  . LEU A 1 124 ? 6.671  44.638 20.671 0.00 30.96  ? 127 LEU A HB2  1 
ATOM   1934 H HB3  . LEU A 1 124 ? 6.597  43.852 19.292 0.00 30.96  ? 127 LEU A HB3  1 
ATOM   1935 H HG   . LEU A 1 124 ? 8.224  43.017 21.480 0.00 30.60  ? 127 LEU A HG   1 
ATOM   1936 H HD11 . LEU A 1 124 ? 6.698  41.281 21.774 0.00 37.18  ? 127 LEU A HD11 1 
ATOM   1937 H HD12 . LEU A 1 124 ? 5.919  42.659 21.904 0.00 37.18  ? 127 LEU A HD12 1 
ATOM   1938 H HD13 . LEU A 1 124 ? 5.823  41.816 20.561 0.00 37.18  ? 127 LEU A HD13 1 
ATOM   1939 H HD21 . LEU A 1 124 ? 8.472  41.069 20.089 0.00 34.61  ? 127 LEU A HD21 1 
ATOM   1940 H HD22 . LEU A 1 124 ? 7.762  41.881 18.924 0.00 34.61  ? 127 LEU A HD22 1 
ATOM   1941 H HD23 . LEU A 1 124 ? 9.173  42.357 19.477 0.00 34.61  ? 127 LEU A HD23 1 
ATOM   1942 N N    . THR A 1 125 ? 8.037  47.405 18.980 1.00 23.26  ? 128 THR A N    1 
ATOM   1943 C CA   . THR A 1 125 ? 7.450  48.576 18.305 1.00 23.62  ? 128 THR A CA   1 
ATOM   1944 C C    . THR A 1 125 ? 8.083  48.846 16.935 1.00 28.06  ? 128 THR A C    1 
ATOM   1945 O O    . THR A 1 125 ? 9.309  48.826 16.777 1.00 29.71  ? 128 THR A O    1 
ATOM   1946 C CB   . THR A 1 125 ? 7.632  49.796 19.250 1.00 25.09  ? 128 THR A CB   1 
ATOM   1947 O OG1  . THR A 1 125 ? 6.641  49.769 20.268 1.00 28.43  ? 128 THR A OG1  1 
ATOM   1948 C CG2  . THR A 1 125 ? 7.521  51.181 18.526 1.00 28.12  ? 128 THR A CG2  1 
ATOM   1949 H H    . THR A 1 125 ? 8.620  47.607 19.579 0.00 27.90  ? 128 THR A H    1 
ATOM   1950 H HA   . THR A 1 125 ? 6.510  48.418 18.123 0.00 28.32  ? 128 THR A HA   1 
ATOM   1951 H HB   . THR A 1 125 ? 8.528  49.729 19.616 0.00 30.09  ? 128 THR A HB   1 
ATOM   1952 H HG1  . THR A 1 125 ? 6.756  50.409 20.799 0.00 34.09  ? 128 THR A HG1  1 
ATOM   1953 H HG21 . THR A 1 125 ? 7.448  51.893 19.180 0.00 33.73  ? 128 THR A HG21 1 
ATOM   1954 H HG22 . THR A 1 125 ? 8.308  51.334 17.980 0.00 33.73  ? 128 THR A HG22 1 
ATOM   1955 H HG23 . THR A 1 125 ? 6.735  51.196 17.957 0.00 33.73  ? 128 THR A HG23 1 
ATOM   1956 N N    . LYS A 1 126 ? 7.233  49.091 15.917 1.00 26.31  ? 129 LYS A N    1 
ATOM   1957 C CA   . LYS A 1 126 ? 7.767  49.206 14.559 1.00 27.73  ? 129 LYS A CA   1 
ATOM   1958 C C    . LYS A 1 126 ? 8.153  50.617 14.161 1.00 36.44  ? 129 LYS A C    1 
ATOM   1959 O O    . LYS A 1 126 ? 8.787  50.776 13.121 1.00 37.14  ? 129 LYS A O    1 
ATOM   1960 C CB   . LYS A 1 126 ? 6.726  48.728 13.522 1.00 32.16  ? 129 LYS A CB   1 
ATOM   1961 C CG   . LYS A 1 126 ? 6.431  47.217 13.702 1.00 39.50  ? 129 LYS A CG   1 
ATOM   1962 C CD   . LYS A 1 126 ? 5.283  46.787 12.747 1.00 47.56  ? 129 LYS A CD   1 
ATOM   1963 C CE   . LYS A 1 126 ? 4.507  45.603 13.303 1.00 68.39  ? 129 LYS A CE   1 
ATOM   1964 N NZ   . LYS A 1 126 ? 3.063  45.933 13.434 1.00 99.41  ? 129 LYS A NZ   1 
ATOM   1965 H H    . LYS A 1 126 ? 6.382  49.189 15.992 0.00 31.55  ? 129 LYS A H    1 
ATOM   1966 H HA   . LYS A 1 126 ? 8.554  48.640 14.523 0.00 33.26  ? 129 LYS A HA   1 
ATOM   1967 H HB2  . LYS A 1 126 ? 5.900  49.222 13.641 0.00 38.57  ? 129 LYS A HB2  1 
ATOM   1968 H HB3  . LYS A 1 126 ? 7.072  48.872 12.627 0.00 38.57  ? 129 LYS A HB3  1 
ATOM   1969 H HG2  . LYS A 1 126 ? 7.224  46.701 13.489 0.00 47.38  ? 129 LYS A HG2  1 
ATOM   1970 H HG3  . LYS A 1 126 ? 6.158  47.043 14.616 0.00 47.38  ? 129 LYS A HG3  1 
ATOM   1971 H HD2  . LYS A 1 126 ? 4.668  47.528 12.632 0.00 57.06  ? 129 LYS A HD2  1 
ATOM   1972 H HD3  . LYS A 1 126 ? 5.658  46.531 11.890 0.00 57.06  ? 129 LYS A HD3  1 
ATOM   1973 H HE2  . LYS A 1 126 ? 4.598  44.846 12.702 0.00 82.04  ? 129 LYS A HE2  1 
ATOM   1974 H HE3  . LYS A 1 126 ? 4.852  45.373 14.180 0.00 82.04  ? 129 LYS A HE3  1 
ATOM   1975 H HZ1  . LYS A 1 126 ? 2.619  45.232 13.757 0.00 119.27 ? 129 LYS A HZ1  1 
ATOM   1976 H HZ2  . LYS A 1 126 ? 2.957  46.622 13.986 0.00 119.27 ? 129 LYS A HZ2  1 
ATOM   1977 H HZ3  . LYS A 1 126 ? 2.726  46.146 12.638 0.00 119.27 ? 129 LYS A HZ3  1 
ATOM   1978 N N    . VAL A 1 127 ? 7.717  51.637 14.880 1.00 28.38  ? 130 VAL A N    1 
ATOM   1979 C CA   . VAL A 1 127 ? 8.116  53.005 14.583 1.00 29.75  ? 130 VAL A CA   1 
ATOM   1980 C C    . VAL A 1 127 ? 9.397  53.301 15.367 1.00 31.26  ? 130 VAL A C    1 
ATOM   1981 O O    . VAL A 1 127 ? 9.369  53.349 16.587 1.00 29.08  ? 130 VAL A O    1 
ATOM   1982 C CB   . VAL A 1 127 ? 7.016  54.003 14.961 1.00 34.68  ? 130 VAL A CB   1 
ATOM   1983 C CG1  . VAL A 1 127 ? 7.549  55.430 14.727 1.00 34.74  ? 130 VAL A CG1  1 
ATOM   1984 C CG2  . VAL A 1 127 ? 5.731  53.744 14.120 1.00 41.36  ? 130 VAL A CG2  1 
ATOM   1985 H H    . VAL A 1 127 ? 7.184  51.564 15.551 0.00 34.03  ? 130 VAL A H    1 
ATOM   1986 H HA   . VAL A 1 127 ? 8.294  53.089 13.633 0.00 35.68  ? 130 VAL A HA   1 
ATOM   1987 H HB   . VAL A 1 127 ? 6.775  53.900 15.895 0.00 41.60  ? 130 VAL A HB   1 
ATOM   1988 H HG11 . VAL A 1 127 ? 6.803  56.051 14.737 0.00 41.67  ? 130 VAL A HG11 1 
ATOM   1989 H HG12 . VAL A 1 127 ? 8.175  55.653 15.433 0.00 41.67  ? 130 VAL A HG12 1 
ATOM   1990 H HG13 . VAL A 1 127 ? 7.995  55.463 13.866 0.00 41.67  ? 130 VAL A HG13 1 
ATOM   1991 H HG21 . VAL A 1 127 ? 5.067  54.415 14.342 0.00 49.61  ? 130 VAL A HG21 1 
ATOM   1992 H HG22 . VAL A 1 127 ? 5.954  53.799 13.177 0.00 49.61  ? 130 VAL A HG22 1 
ATOM   1993 H HG23 . VAL A 1 127 ? 5.390  52.860 14.328 0.00 49.61  ? 130 VAL A HG23 1 
ATOM   1994 N N    . TYR A 1 128 ? 10.495 53.589 14.652 1.00 27.73  ? 131 TYR A N    1 
ATOM   1995 C CA   . TYR A 1 128 ? 11.818 53.560 15.309 1.00 28.99  ? 131 TYR A CA   1 
ATOM   1996 C C    . TYR A 1 128 ? 11.911 54.548 16.460 1.00 30.22  ? 131 TYR A C    1 
ATOM   1997 O O    . TYR A 1 128 ? 12.381 54.192 17.540 1.00 25.59  ? 131 TYR A O    1 
ATOM   1998 C CB   . TYR A 1 128 ? 12.891 53.894 14.263 1.00 35.14  ? 131 TYR A CB   1 
ATOM   1999 C CG   . TYR A 1 128 ? 14.342 53.765 14.767 1.00 33.79  ? 131 TYR A CG   1 
ATOM   2000 C CD1  . TYR A 1 128 ? 14.859 52.538 15.154 1.00 39.93  ? 131 TYR A CD1  1 
ATOM   2001 C CD2  . TYR A 1 128 ? 15.182 54.893 14.833 1.00 43.10  ? 131 TYR A CD2  1 
ATOM   2002 C CE1  . TYR A 1 128 ? 16.216 52.434 15.597 1.00 38.47  ? 131 TYR A CE1  1 
ATOM   2003 C CE2  . TYR A 1 128 ? 16.511 54.800 15.259 1.00 39.46  ? 131 TYR A CE2  1 
ATOM   2004 C CZ   . TYR A 1 128 ? 17.016 53.568 15.634 1.00 47.86  ? 131 TYR A CZ   1 
ATOM   2005 O OH   . TYR A 1 128 ? 18.332 53.475 16.033 1.00 50.16  ? 131 TYR A OH   1 
ATOM   2006 H H    . TYR A 1 128 ? 10.504 53.796 13.817 0.00 33.26  ? 131 TYR A H    1 
ATOM   2007 H HA   . TYR A 1 128 ? 11.963 52.672 15.671 0.00 34.77  ? 131 TYR A HA   1 
ATOM   2008 H HB2  . TYR A 1 128 ? 12.787 53.289 13.512 0.00 42.15  ? 131 TYR A HB2  1 
ATOM   2009 H HB3  . TYR A 1 128 ? 12.763 54.810 13.971 0.00 42.15  ? 131 TYR A HB3  1 
ATOM   2010 H HD1  . TYR A 1 128 ? 14.321 51.780 15.125 0.00 47.90  ? 131 TYR A HD1  1 
ATOM   2011 H HD2  . TYR A 1 128 ? 14.844 55.724 14.587 0.00 51.71  ? 131 TYR A HD2  1 
ATOM   2012 H HE1  . TYR A 1 128 ? 16.560 51.610 15.858 0.00 46.15  ? 131 TYR A HE1  1 
ATOM   2013 H HE2  . TYR A 1 128 ? 17.049 55.557 15.289 0.00 47.33  ? 131 TYR A HE2  1 
ATOM   2014 H HH   . TYR A 1 128 ? 18.477 54.006 16.668 0.00 60.18  ? 131 TYR A HH   1 
ATOM   2015 N N    A SER A 1 129 ? 11.478 55.815 16.244 0.40 28.87  ? 132 SER A N    1 
ATOM   2016 N N    B SER A 1 129 ? 11.481 55.822 16.240 0.60 28.80  ? 132 SER A N    1 
ATOM   2017 C CA   A SER A 1 129 ? 11.641 56.819 17.294 0.40 30.86  ? 132 SER A CA   1 
ATOM   2018 C CA   B SER A 1 129 ? 11.624 56.824 17.295 0.60 30.85  ? 132 SER A CA   1 
ATOM   2019 C C    A SER A 1 129 ? 10.843 56.478 18.544 0.40 30.29  ? 132 SER A C    1 
ATOM   2020 C C    B SER A 1 129 ? 10.843 56.470 18.547 0.60 30.36  ? 132 SER A C    1 
ATOM   2021 O O    A SER A 1 129 ? 11.257 56.824 19.664 0.40 29.30  ? 132 SER A O    1 
ATOM   2022 O O    B SER A 1 129 ? 11.271 56.799 19.671 0.60 29.32  ? 132 SER A O    1 
ATOM   2023 C CB   A SER A 1 129 ? 11.223 58.205 16.782 0.40 34.97  ? 132 SER A CB   1 
ATOM   2024 C CB   B SER A 1 129 ? 11.158 58.190 16.785 0.60 34.97  ? 132 SER A CB   1 
ATOM   2025 O OG   A SER A 1 129 ? 9.821  58.284 16.607 0.40 28.72  ? 132 SER A OG   1 
ATOM   2026 O OG   B SER A 1 129 ? 12.005 58.624 15.757 0.60 45.00  ? 132 SER A OG   1 
ATOM   2027 H H    A SER A 1 129 ? 11.103 56.096 15.523 0.40 34.62  ? 132 SER A H    1 
ATOM   2028 H H    B SER A 1 129 ? 11.120 56.105 15.513 0.60 34.54  ? 132 SER A H    1 
ATOM   2029 H HA   A SER A 1 129 ? 12.581 56.850 17.531 0.40 37.02  ? 132 SER A HA   1 
ATOM   2030 H HA   B SER A 1 129 ? 12.564 56.872 17.529 0.60 37.00  ? 132 SER A HA   1 
ATOM   2031 H HB2  A SER A 1 129 ? 11.498 58.875 17.427 0.40 41.94  ? 132 SER A HB2  1 
ATOM   2032 H HB2  B SER A 1 129 ? 10.253 58.113 16.444 0.60 41.95  ? 132 SER A HB2  1 
ATOM   2033 H HB3  A SER A 1 129 ? 11.656 58.369 15.929 0.40 41.94  ? 132 SER A HB3  1 
ATOM   2034 H HB3  B SER A 1 129 ? 11.184 58.830 17.514 0.60 41.95  ? 132 SER A HB3  1 
ATOM   2035 H HG   A SER A 1 129 ? 9.612  59.038 16.302 0.40 34.44  ? 132 SER A HG   1 
ATOM   2036 H HG   B SER A 1 129 ? 11.749 59.371 15.470 0.60 53.98  ? 132 SER A HG   1 
ATOM   2037 N N    . TYR A 1 130 ? 9.710  55.779 18.392 1.00 26.80  ? 133 TYR A N    1 
ATOM   2038 C CA   . TYR A 1 130 ? 8.918  55.457 19.571 1.00 23.94  ? 133 TYR A CA   1 
ATOM   2039 C C    . TYR A 1 130 ? 9.549  54.371 20.413 1.00 24.60  ? 133 TYR A C    1 
ATOM   2040 O O    . TYR A 1 130 ? 9.205  54.247 21.586 1.00 24.73  ? 133 TYR A O    1 
ATOM   2041 C CB   . TYR A 1 130 ? 7.507  54.952 19.217 1.00 26.23  ? 133 TYR A CB   1 
ATOM   2042 C CG   . TYR A 1 130 ? 6.591  55.917 18.516 1.00 34.98  ? 133 TYR A CG   1 
ATOM   2043 C CD1  . TYR A 1 130 ? 6.844  57.269 18.493 1.00 34.37  ? 133 TYR A CD1  1 
ATOM   2044 C CD2  . TYR A 1 130 ? 5.464  55.435 17.874 1.00 30.68  ? 133 TYR A CD2  1 
ATOM   2045 C CE1  . TYR A 1 130 ? 5.980  58.149 17.793 1.00 38.06  ? 133 TYR A CE1  1 
ATOM   2046 C CE2  . TYR A 1 130 ? 4.605  56.252 17.204 1.00 38.73  ? 133 TYR A CE2  1 
ATOM   2047 C CZ   . TYR A 1 130 ? 4.861  57.617 17.161 1.00 40.97  ? 133 TYR A CZ   1 
ATOM   2048 O OH   . TYR A 1 130 ? 3.959  58.429 16.477 1.00 49.61  ? 133 TYR A OH   1 
ATOM   2049 H H    . TYR A 1 130 ? 9.397  55.498 17.642 0.00 32.14  ? 133 TYR A H    1 
ATOM   2050 H HA   . TYR A 1 130 ? 8.842  56.288 20.065 0.00 28.71  ? 133 TYR A HA   1 
ATOM   2051 H HB2  . TYR A 1 130 ? 7.602  54.181 18.637 0.00 31.46  ? 133 TYR A HB2  1 
ATOM   2052 H HB3  . TYR A 1 130 ? 7.066  54.694 20.042 0.00 31.46  ? 133 TYR A HB3  1 
ATOM   2053 H HD1  . TYR A 1 130 ? 7.586  57.608 18.940 0.00 41.23  ? 133 TYR A HD1  1 
ATOM   2054 H HD2  . TYR A 1 130 ? 5.287  54.523 17.901 0.00 36.79  ? 133 TYR A HD2  1 
ATOM   2055 H HE1  . TYR A 1 130 ? 6.157  59.061 17.757 0.00 45.66  ? 133 TYR A HE1  1 
ATOM   2056 H HE2  . TYR A 1 130 ? 3.855  55.901 16.781 0.00 46.46  ? 133 TYR A HE2  1 
ATOM   2057 H HH   . TYR A 1 130 ? 3.390  57.955 16.080 0.00 59.51  ? 133 TYR A HH   1 
ATOM   2058 N N    . ARG A 1 131 ? 10.440 53.558 19.851 1.00 24.39  ? 134 ARG A N    1 
ATOM   2059 C CA   . ARG A 1 131 ? 11.135 52.560 20.694 1.00 23.64  ? 134 ARG A CA   1 
ATOM   2060 C C    . ARG A 1 131 ? 11.836 53.222 21.889 1.00 25.84  ? 134 ARG A C    1 
ATOM   2061 O O    . ARG A 1 131 ? 11.895 52.647 22.980 1.00 25.01  ? 134 ARG A O    1 
ATOM   2062 C CB   . ARG A 1 131 ? 12.177 51.801 19.853 1.00 25.69  ? 134 ARG A CB   1 
ATOM   2063 C CG   . ARG A 1 131 ? 11.458 50.954 18.714 1.00 25.90  ? 134 ARG A CG   1 
ATOM   2064 C CD   . ARG A 1 131 ? 12.509 50.274 17.726 1.00 26.43  ? 134 ARG A CD   1 
ATOM   2065 N NE   . ARG A 1 131 ? 13.267 49.189 18.397 1.00 27.95  ? 134 ARG A NE   1 
ATOM   2066 C CZ   . ARG A 1 131 ? 12.788 47.948 18.517 1.00 30.10  ? 134 ARG A CZ   1 
ATOM   2067 N NH1  . ARG A 1 131 ? 11.591 47.605 18.000 1.00 28.57  ? 134 ARG A NH1  1 
ATOM   2068 N NH2  . ARG A 1 131 ? 13.537 47.014 19.109 1.00 30.74  ? 134 ARG A NH2  1 
ATOM   2069 H H    . ARG A 1 131 ? 10.659 53.555 19.019 0.00 29.25  ? 134 ARG A H    1 
ATOM   2070 H HA   . ARG A 1 131 ? 10.476 51.931 21.028 0.00 28.35  ? 134 ARG A HA   1 
ATOM   2071 H HB2  . ARG A 1 131 ? 12.781 52.435 19.434 0.00 30.81  ? 134 ARG A HB2  1 
ATOM   2072 H HB3  . ARG A 1 131 ? 12.676 51.195 20.423 0.00 30.81  ? 134 ARG A HB3  1 
ATOM   2073 H HG2  . ARG A 1 131 ? 10.928 50.252 19.124 0.00 31.07  ? 134 ARG A HG2  1 
ATOM   2074 H HG3  . ARG A 1 131 ? 10.886 51.540 18.193 0.00 31.07  ? 134 ARG A HG3  1 
ATOM   2075 H HD2  . ARG A 1 131 ? 12.038 49.893 16.968 0.00 31.70  ? 134 ARG A HD2  1 
ATOM   2076 H HD3  . ARG A 1 131 ? 13.142 50.943 17.420 0.00 31.70  ? 134 ARG A HD3  1 
ATOM   2077 H HE   . ARG A 1 131 ? 14.043 49.365 18.721 0.00 33.52  ? 134 ARG A HE   1 
ATOM   2078 H HH11 . ARG A 1 131 ? 11.119 48.191 17.582 0.00 34.27  ? 134 ARG A HH11 1 
ATOM   2079 H HH12 . ARG A 1 131 ? 11.299 46.801 18.087 0.00 34.27  ? 134 ARG A HH12 1 
ATOM   2080 H HH21 . ARG A 1 131 ? 14.318 47.214 19.408 0.00 36.87  ? 134 ARG A HH21 1 
ATOM   2081 H HH22 . ARG A 1 131 ? 13.238 46.211 19.191 0.00 36.87  ? 134 ARG A HH22 1 
ATOM   2082 N N    . PHE A 1 132 ? 12.373 54.429 21.704 1.00 23.94  ? 135 PHE A N    1 
ATOM   2083 C CA   . PHE A 1 132 ? 13.135 55.072 22.770 1.00 23.90  ? 135 PHE A CA   1 
ATOM   2084 C C    . PHE A 1 132 ? 12.237 55.745 23.800 1.00 25.28  ? 135 PHE A C    1 
ATOM   2085 O O    . PHE A 1 132 ? 12.665 55.961 24.932 1.00 24.93  ? 135 PHE A O    1 
ATOM   2086 C CB   . PHE A 1 132 ? 14.103 56.095 22.110 1.00 23.52  ? 135 PHE A CB   1 
ATOM   2087 C CG   . PHE A 1 132 ? 15.080 55.405 21.150 1.00 25.86  ? 135 PHE A CG   1 
ATOM   2088 C CD1  . PHE A 1 132 ? 16.166 54.681 21.681 1.00 28.65  ? 135 PHE A CD1  1 
ATOM   2089 C CD2  . PHE A 1 132 ? 14.876 55.443 19.781 1.00 26.15  ? 135 PHE A CD2  1 
ATOM   2090 C CE1  . PHE A 1 132 ? 17.054 54.015 20.838 1.00 36.35  ? 135 PHE A CE1  1 
ATOM   2091 C CE2  . PHE A 1 132 ? 15.752 54.767 18.948 1.00 36.75  ? 135 PHE A CE2  1 
ATOM   2092 C CZ   . PHE A 1 132 ? 16.843 54.054 19.489 1.00 35.88  ? 135 PHE A CZ   1 
ATOM   2093 H H    . PHE A 1 132 ? 12.311 54.888 20.980 0.00 28.71  ? 135 PHE A H    1 
ATOM   2094 H HA   . PHE A 1 132 ? 13.665 54.423 23.258 0.00 28.67  ? 135 PHE A HA   1 
ATOM   2095 H HB2  . PHE A 1 132 ? 13.588 56.745 21.607 0.00 28.20  ? 135 PHE A HB2  1 
ATOM   2096 H HB3  . PHE A 1 132 ? 14.617 56.542 22.800 0.00 28.20  ? 135 PHE A HB3  1 
ATOM   2097 H HD1  . PHE A 1 132 ? 16.292 54.648 22.601 0.00 34.37  ? 135 PHE A HD1  1 
ATOM   2098 H HD2  . PHE A 1 132 ? 14.159 55.917 19.426 0.00 31.36  ? 135 PHE A HD2  1 
ATOM   2099 H HE1  . PHE A 1 132 ? 17.779 53.551 21.189 0.00 43.61  ? 135 PHE A HE1  1 
ATOM   2100 H HE2  . PHE A 1 132 ? 15.620 54.783 18.028 0.00 44.08  ? 135 PHE A HE2  1 
ATOM   2101 H HZ   . PHE A 1 132 ? 17.426 53.605 18.920 0.00 43.04  ? 135 PHE A HZ   1 
ATOM   2102 N N    . VAL A 1 133 ? 11.005 56.059 23.428 1.00 22.36  ? 136 VAL A N    1 
ATOM   2103 C CA   . VAL A 1 133 ? 10.003 56.539 24.398 1.00 20.87  ? 136 VAL A CA   1 
ATOM   2104 C C    . VAL A 1 133 ? 9.743  55.447 25.406 1.00 23.21  ? 136 VAL A C    1 
ATOM   2105 O O    . VAL A 1 133 ? 9.721  55.682 26.614 1.00 22.88  ? 136 VAL A O    1 
ATOM   2106 C CB   . VAL A 1 133 ? 8.696  56.947 23.687 1.00 26.56  ? 136 VAL A CB   1 
ATOM   2107 C CG1  . VAL A 1 133 ? 7.562  57.253 24.743 1.00 29.04  ? 136 VAL A CG1  1 
ATOM   2108 C CG2  . VAL A 1 133 ? 8.964  58.191 22.775 1.00 33.34  ? 136 VAL A CG2  1 
ATOM   2109 H H    . VAL A 1 133 ? 10.712 56.007 22.621 0.00 26.82  ? 136 VAL A H    1 
ATOM   2110 H HA   . VAL A 1 133 ? 10.351 57.325 24.847 0.00 25.03  ? 136 VAL A HA   1 
ATOM   2111 H HB   . VAL A 1 133 ? 8.387  56.215 23.130 0.00 31.86  ? 136 VAL A HB   1 
ATOM   2112 H HG11 . VAL A 1 133 ? 6.832  57.711 24.298 0.00 34.82  ? 136 VAL A HG11 1 
ATOM   2113 H HG12 . VAL A 1 133 ? 7.247  56.417 25.120 0.00 34.82  ? 136 VAL A HG12 1 
ATOM   2114 H HG13 . VAL A 1 133 ? 7.927  57.816 25.444 0.00 34.82  ? 136 VAL A HG13 1 
ATOM   2115 H HG21 . VAL A 1 133 ? 8.132  58.459 22.356 0.00 39.99  ? 136 VAL A HG21 1 
ATOM   2116 H HG22 . VAL A 1 133 ? 9.307  58.915 23.322 0.00 39.99  ? 136 VAL A HG22 1 
ATOM   2117 H HG23 . VAL A 1 133 ? 9.614  57.951 22.097 0.00 39.99  ? 136 VAL A HG23 1 
ATOM   2118 N N    . TRP A 1 134 ? 9.536  54.199 24.910 1.00 21.25  ? 137 TRP A N    1 
ATOM   2119 C CA   . TRP A 1 134 ? 9.277  53.116 25.878 1.00 18.80  ? 137 TRP A CA   1 
ATOM   2120 C C    . TRP A 1 134 ? 10.522 52.810 26.703 1.00 23.17  ? 137 TRP A C    1 
ATOM   2121 O O    . TRP A 1 134 ? 10.404 52.481 27.903 1.00 21.76  ? 137 TRP A O    1 
ATOM   2122 C CB   . TRP A 1 134 ? 8.830  51.822 25.141 1.00 19.29  ? 137 TRP A CB   1 
ATOM   2123 C CG   . TRP A 1 134 ? 7.457  52.059 24.469 1.00 19.73  ? 137 TRP A CG   1 
ATOM   2124 C CD1  . TRP A 1 134 ? 7.193  52.161 23.121 1.00 22.98  ? 137 TRP A CD1  1 
ATOM   2125 C CD2  . TRP A 1 134 ? 6.235  52.208 25.137 1.00 23.35  ? 137 TRP A CD2  1 
ATOM   2126 N NE1  . TRP A 1 134 ? 5.849  52.443 22.923 1.00 21.75  ? 137 TRP A NE1  1 
ATOM   2127 C CE2  . TRP A 1 134 ? 5.219  52.414 24.150 1.00 24.95  ? 137 TRP A CE2  1 
ATOM   2128 C CE3  . TRP A 1 134 ? 5.868  52.162 26.497 1.00 21.17  ? 137 TRP A CE3  1 
ATOM   2129 C CZ2  . TRP A 1 134 ? 3.852  52.605 24.465 1.00 25.61  ? 137 TRP A CZ2  1 
ATOM   2130 C CZ3  . TRP A 1 134 ? 4.444  52.343 26.822 1.00 23.57  ? 137 TRP A CZ3  1 
ATOM   2131 C CH2  . TRP A 1 134 ? 3.472  52.529 25.798 1.00 25.52  ? 137 TRP A CH2  1 
ATOM   2132 H H    . TRP A 1 134 ? 9.540  53.976 24.080 0.00 25.48  ? 137 TRP A H    1 
ATOM   2133 H HA   . TRP A 1 134 ? 8.562  53.403 26.466 0.00 22.55  ? 137 TRP A HA   1 
ATOM   2134 H HB2  . TRP A 1 134 ? 9.479  51.592 24.457 0.00 23.13  ? 137 TRP A HB2  1 
ATOM   2135 H HB3  . TRP A 1 134 ? 8.747  51.094 25.777 0.00 23.13  ? 137 TRP A HB3  1 
ATOM   2136 H HD1  . TRP A 1 134 ? 7.822  52.057 22.444 0.00 27.55  ? 137 TRP A HD1  1 
ATOM   2137 H HE1  . TRP A 1 134 ? 5.474  52.608 22.167 0.00 26.09  ? 137 TRP A HE1  1 
ATOM   2138 H HE3  . TRP A 1 134 ? 6.501  52.023 27.163 0.00 25.39  ? 137 TRP A HE3  1 
ATOM   2139 H HZ2  . TRP A 1 134 ? 3.227  52.777 23.798 0.00 30.71  ? 137 TRP A HZ2  1 
ATOM   2140 H HZ3  . TRP A 1 134 ? 4.175  52.335 27.712 0.00 28.26  ? 137 TRP A HZ3  1 
ATOM   2141 H HH2  . TRP A 1 134 ? 2.573  52.601 26.025 0.00 30.60  ? 137 TRP A HH2  1 
ATOM   2142 N N    . TRP A 1 135 ? 11.697 52.889 26.094 1.00 21.66  ? 138 TRP A N    1 
ATOM   2143 C CA   . TRP A 1 135 ? 12.935 52.695 26.863 1.00 19.85  ? 138 TRP A CA   1 
ATOM   2144 C C    . TRP A 1 135 ? 13.030 53.709 28.017 1.00 23.41  ? 138 TRP A C    1 
ATOM   2145 O O    . TRP A 1 135 ? 13.451 53.351 29.135 1.00 23.45  ? 138 TRP A O    1 
ATOM   2146 C CB   . TRP A 1 135 ? 14.172 52.842 25.922 1.00 22.71  ? 138 TRP A CB   1 
ATOM   2147 C CG   . TRP A 1 135 ? 15.543 52.742 26.637 1.00 22.86  ? 138 TRP A CG   1 
ATOM   2148 C CD1  . TRP A 1 135 ? 16.308 51.606 26.841 1.00 23.99  ? 138 TRP A CD1  1 
ATOM   2149 C CD2  . TRP A 1 135 ? 16.274 53.817 27.226 1.00 21.40  ? 138 TRP A CD2  1 
ATOM   2150 N NE1  . TRP A 1 135 ? 17.513 51.931 27.513 1.00 25.75  ? 138 TRP A NE1  1 
ATOM   2151 C CE2  . TRP A 1 135 ? 17.486 53.288 27.763 1.00 25.86  ? 138 TRP A CE2  1 
ATOM   2152 C CE3  . TRP A 1 135 ? 16.039 55.210 27.330 1.00 30.09  ? 138 TRP A CE3  1 
ATOM   2153 C CZ2  . TRP A 1 135 ? 18.441 54.092 28.383 1.00 33.17  ? 138 TRP A CZ2  1 
ATOM   2154 C CZ3  . TRP A 1 135 ? 17.005 56.004 27.957 1.00 34.02  ? 138 TRP A CZ3  1 
ATOM   2155 C CH2  . TRP A 1 135 ? 18.171 55.459 28.474 1.00 34.88  ? 138 TRP A CH2  1 
ATOM   2156 H H    . TRP A 1 135 ? 11.812 53.050 25.257 0.00 25.98  ? 138 TRP A H    1 
ATOM   2157 H HA   . TRP A 1 135 ? 12.937 51.800 27.237 0.00 23.80  ? 138 TRP A HA   1 
ATOM   2158 H HB2  . TRP A 1 135 ? 14.138 52.138 25.256 0.00 27.23  ? 138 TRP A HB2  1 
ATOM   2159 H HB3  . TRP A 1 135 ? 14.129 53.710 25.490 0.00 27.23  ? 138 TRP A HB3  1 
ATOM   2160 H HD1  . TRP A 1 135 ? 16.064 50.749 26.575 0.00 28.77  ? 138 TRP A HD1  1 
ATOM   2161 H HE1  . TRP A 1 135 ? 18.143 51.385 27.724 0.00 30.89  ? 138 TRP A HE1  1 
ATOM   2162 H HE3  . TRP A 1 135 ? 15.261 55.588 26.988 0.00 36.09  ? 138 TRP A HE3  1 
ATOM   2163 H HZ2  . TRP A 1 135 ? 19.228 53.731 28.724 0.00 39.79  ? 138 TRP A HZ2  1 
ATOM   2164 H HZ3  . TRP A 1 135 ? 16.862 56.920 28.029 0.00 40.81  ? 138 TRP A HZ3  1 
ATOM   2165 H HH2  . TRP A 1 135 ? 18.788 56.017 28.890 0.00 41.84  ? 138 TRP A HH2  1 
ATOM   2166 N N    . ALA A 1 136 ? 12.614 54.957 27.776 1.00 21.91  ? 139 ALA A N    1 
ATOM   2167 C CA   . ALA A 1 136 ? 12.761 55.997 28.839 1.00 23.98  ? 139 ALA A CA   1 
ATOM   2168 C C    . ALA A 1 136 ? 11.775 55.752 29.982 1.00 26.60  ? 139 ALA A C    1 
ATOM   2169 O O    . ALA A 1 136 ? 12.126 55.952 31.155 1.00 25.18  ? 139 ALA A O    1 
ATOM   2170 C CB   . ALA A 1 136 ? 12.556 57.395 28.235 1.00 26.53  ? 139 ALA A CB   1 
ATOM   2171 H H    . ALA A 1 136 ? 12.257 55.230 27.042 0.00 26.27  ? 139 ALA A H    1 
ATOM   2172 H HA   . ALA A 1 136 ? 13.659 55.956 29.202 0.00 28.75  ? 139 ALA A HA   1 
ATOM   2173 H HB1  . ALA A 1 136 ? 12.649 58.059 28.936 0.00 31.81  ? 139 ALA A HB1  1 
ATOM   2174 H HB2  . ALA A 1 136 ? 13.224 57.543 27.548 0.00 31.81  ? 139 ALA A HB2  1 
ATOM   2175 H HB3  . ALA A 1 136 ? 11.668 57.445 27.848 0.00 31.81  ? 139 ALA A HB3  1 
ATOM   2176 N N    . ILE A 1 137 ? 10.532 55.338 29.652 1.00 22.40  ? 140 ILE A N    1 
ATOM   2177 C CA   . ILE A 1 137 ? 9.552  54.997 30.703 1.00 22.86  ? 140 ILE A CA   1 
ATOM   2178 C C    . ILE A 1 137 ? 10.048 53.818 31.529 1.00 23.94  ? 140 ILE A C    1 
ATOM   2179 O O    . ILE A 1 137 ? 9.944  53.792 32.756 1.00 24.80  ? 140 ILE A O    1 
ATOM   2180 C CB   . ILE A 1 137 ? 8.170  54.704 30.071 1.00 24.42  ? 140 ILE A CB   1 
ATOM   2181 C CG1  . ILE A 1 137 ? 7.541  56.007 29.533 1.00 25.85  ? 140 ILE A CG1  1 
ATOM   2182 C CG2  . ILE A 1 137 ? 7.247  54.083 31.117 1.00 26.70  ? 140 ILE A CG2  1 
ATOM   2183 C CD1  . ILE A 1 137 ? 6.331  55.700 28.536 1.00 29.51  ? 140 ILE A CD1  1 
ATOM   2184 H H    . ILE A 1 137 ? 10.240 55.249 28.848 0.00 26.86  ? 140 ILE A H    1 
ATOM   2185 H HA   . ILE A 1 137 ? 9.457  55.759 31.295 0.00 27.42  ? 140 ILE A HA   1 
ATOM   2186 H HB   . ILE A 1 137 ? 8.292  54.085 29.335 0.00 29.29  ? 140 ILE A HB   1 
ATOM   2187 H HG12 . ILE A 1 137 ? 7.201  56.530 30.275 0.00 31.00  ? 140 ILE A HG12 1 
ATOM   2188 H HG13 . ILE A 1 137 ? 8.214  56.513 29.051 0.00 31.00  ? 140 ILE A HG13 1 
ATOM   2189 H HG21 . ILE A 1 137 ? 6.328  54.165 30.815 0.00 32.03  ? 140 ILE A HG21 1 
ATOM   2190 H HG22 . ILE A 1 137 ? 7.477  53.147 31.225 0.00 32.03  ? 140 ILE A HG22 1 
ATOM   2191 H HG23 . ILE A 1 137 ? 7.362  54.552 31.958 0.00 32.03  ? 140 ILE A HG23 1 
ATOM   2192 H HD11 . ILE A 1 137 ? 6.020  56.534 28.151 0.00 35.39  ? 140 ILE A HD11 1 
ATOM   2193 H HD12 . ILE A 1 137 ? 6.642  55.108 27.834 0.00 35.39  ? 140 ILE A HD12 1 
ATOM   2194 H HD13 . ILE A 1 137 ? 5.613  55.277 29.032 0.00 35.39  ? 140 ILE A HD13 1 
ATOM   2195 N N    . SER A 1 138 ? 10.605 52.787 30.859 1.00 21.31  ? 141 SER A N    1 
ATOM   2196 C CA   . SER A 1 138 ? 11.088 51.584 31.588 1.00 23.04  ? 141 SER A CA   1 
ATOM   2197 C C    . SER A 1 138 ? 12.282 51.958 32.483 1.00 23.17  ? 141 SER A C    1 
ATOM   2198 O O    . SER A 1 138 ? 12.382 51.478 33.645 1.00 23.11  ? 141 SER A O    1 
ATOM   2199 C CB   . SER A 1 138 ? 11.512 50.525 30.559 1.00 22.84  ? 141 SER A CB   1 
ATOM   2200 O OG   . SER A 1 138 ? 12.064 49.301 31.129 1.00 24.21  ? 141 SER A OG   1 
ATOM   2201 H H    . SER A 1 138 ? 10.714 52.756 30.006 0.00 25.55  ? 141 SER A H    1 
ATOM   2202 H HA   . SER A 1 138 ? 10.383 51.218 32.144 0.00 27.63  ? 141 SER A HA   1 
ATOM   2203 H HB2  . SER A 1 138 ? 10.731 50.287 30.036 0.00 27.39  ? 141 SER A HB2  1 
ATOM   2204 H HB3  . SER A 1 138 ? 12.188 50.919 29.985 0.00 27.39  ? 141 SER A HB3  1 
ATOM   2205 H HG   . SER A 1 138 ? 11.509 48.953 31.655 0.00 29.03  ? 141 SER A HG   1 
ATOM   2206 N N    . THR A 1 139 ? 13.157 52.803 31.981 1.00 20.60  ? 142 THR A N    1 
ATOM   2207 C CA   . THR A 1 139 ? 14.320 53.244 32.799 1.00 20.20  ? 142 THR A CA   1 
ATOM   2208 C C    . THR A 1 139 ? 13.863 54.084 33.994 1.00 24.95  ? 142 THR A C    1 
ATOM   2209 O O    . THR A 1 139 ? 14.417 53.958 35.112 1.00 26.91  ? 142 THR A O    1 
ATOM   2210 C CB   . THR A 1 139 ? 15.306 54.052 31.894 1.00 22.46  ? 142 THR A CB   1 
ATOM   2211 O OG1  . THR A 1 139 ? 15.808 53.138 30.922 1.00 26.12  ? 142 THR A OG1  1 
ATOM   2212 C CG2  . THR A 1 139 ? 16.549 54.555 32.694 1.00 27.84  ? 142 THR A CG2  1 
ATOM   2213 H H    . THR A 1 139 ? 13.122 53.141 31.190 0.00 24.70  ? 142 THR A H    1 
ATOM   2214 H HA   . THR A 1 139 ? 14.789 52.469 33.147 0.00 24.22  ? 142 THR A HA   1 
ATOM   2215 H HB   . THR A 1 139 ? 14.845 54.817 31.516 0.00 26.94  ? 142 THR A HB   1 
ATOM   2216 H HG1  . THR A 1 139 ? 15.177 52.844 30.451 0.00 31.32  ? 142 THR A HG1  1 
ATOM   2217 H HG21 . THR A 1 139 ? 17.201 54.938 32.087 0.00 33.39  ? 142 THR A HG21 1 
ATOM   2218 H HG22 . THR A 1 139 ? 16.279 55.232 33.334 0.00 33.39  ? 142 THR A HG22 1 
ATOM   2219 H HG23 . THR A 1 139 ? 16.958 53.817 33.171 0.00 33.39  ? 142 THR A HG23 1 
ATOM   2220 N N    . ALA A 1 140 ? 12.813 54.898 33.834 1.00 23.48  ? 143 ALA A N    1 
ATOM   2221 C CA   . ALA A 1 140 ? 12.310 55.609 35.010 1.00 23.06  ? 143 ALA A CA   1 
ATOM   2222 C C    . ALA A 1 140 ? 11.763 54.624 36.076 1.00 24.00  ? 143 ALA A C    1 
ATOM   2223 O O    . ALA A 1 140 ? 11.994 54.826 37.276 1.00 27.27  ? 143 ALA A O    1 
ATOM   2224 C CB   . ALA A 1 140 ? 11.173 56.592 34.598 1.00 25.66  ? 143 ALA A CB   1 
ATOM   2225 H H    . ALA A 1 140 ? 12.397 55.046 33.095 0.00 28.15  ? 143 ALA A H    1 
ATOM   2226 H HA   . ALA A 1 140 ? 13.044 56.115 35.392 0.00 27.65  ? 143 ALA A HA   1 
ATOM   2227 H HB1  . ALA A 1 140 ? 10.869 57.071 35.386 0.00 30.78  ? 143 ALA A HB1  1 
ATOM   2228 H HB2  . ALA A 1 140 ? 11.519 57.219 33.944 0.00 30.78  ? 143 ALA A HB2  1 
ATOM   2229 H HB3  . ALA A 1 140 ? 10.440 56.085 34.216 0.00 30.78  ? 143 ALA A HB3  1 
ATOM   2230 N N    . ALA A 1 141 ? 11.088 53.552 35.655 1.00 23.06  ? 144 ALA A N    1 
ATOM   2231 C CA   . ALA A 1 141 ? 10.642 52.533 36.615 1.00 24.55  ? 144 ALA A CA   1 
ATOM   2232 C C    . ALA A 1 141 ? 11.836 51.877 37.316 1.00 25.32  ? 144 ALA A C    1 
ATOM   2233 O O    . ALA A 1 141 ? 11.771 51.595 38.516 1.00 24.03  ? 144 ALA A O    1 
ATOM   2234 C CB   . ALA A 1 141 ? 9.804  51.460 35.902 1.00 21.20  ? 144 ALA A CB   1 
ATOM   2235 H H    . ALA A 1 141 ? 10.878 53.391 34.836 0.00 27.65  ? 144 ALA A H    1 
ATOM   2236 H HA   . ALA A 1 141 ? 10.085 52.962 37.283 0.00 29.45  ? 144 ALA A HA   1 
ATOM   2237 H HB1  . ALA A 1 141 ? 9.518  50.799 36.551 0.00 25.42  ? 144 ALA A HB1  1 
ATOM   2238 H HB2  . ALA A 1 141 ? 9.030  51.882 35.496 0.00 25.42  ? 144 ALA A HB2  1 
ATOM   2239 H HB3  . ALA A 1 141 ? 10.347 51.038 35.218 0.00 25.42  ? 144 ALA A HB3  1 
ATOM   2240 N N    . MET A 1 142 ? 12.912 51.588 36.561 1.00 24.32  ? 145 MET A N    1 
ATOM   2241 C CA   . MET A 1 142 ? 14.118 51.010 37.191 1.00 23.69  ? 145 MET A CA   1 
ATOM   2242 C C    . MET A 1 142 ? 14.703 51.986 38.209 1.00 27.57  ? 145 MET A C    1 
ATOM   2243 O O    . MET A 1 142 ? 15.122 51.549 39.282 1.00 26.65  ? 145 MET A O    1 
ATOM   2244 C CB   . MET A 1 142 ? 15.195 50.690 36.145 1.00 24.24  ? 145 MET A CB   1 
ATOM   2245 C CG   . MET A 1 142 ? 16.432 50.079 36.803 1.00 28.28  ? 145 MET A CG   1 
ATOM   2246 S SD   . MET A 1 142 ? 17.784 49.757 35.638 1.00 31.43  ? 145 MET A SD   1 
ATOM   2247 C CE   . MET A 1 142 ? 18.544 51.223 35.961 1.00 35.12  ? 145 MET A CE   1 
ATOM   2248 H H    . MET A 1 142 ? 12.969 51.712 35.712 0.00 29.16  ? 145 MET A H    1 
ATOM   2249 H HA   . MET A 1 142 ? 13.856 50.178 37.616 0.00 28.41  ? 145 MET A HA   1 
ATOM   2250 H HB2  . MET A 1 142 ? 14.843 50.055 35.503 0.00 29.07  ? 145 MET A HB2  1 
ATOM   2251 H HB3  . MET A 1 142 ? 15.459 51.507 35.694 0.00 29.07  ? 145 MET A HB3  1 
ATOM   2252 H HG2  . MET A 1 142 ? 16.762 50.691 37.480 0.00 33.91  ? 145 MET A HG2  1 
ATOM   2253 H HG3  . MET A 1 142 ? 16.185 49.235 37.212 0.00 33.91  ? 145 MET A HG3  1 
ATOM   2254 H HE1  . MET A 1 142 ? 19.336 51.298 35.406 0.00 42.13  ? 145 MET A HE1  1 
ATOM   2255 H HE2  . MET A 1 142 ? 17.931 51.948 35.762 0.00 42.13  ? 145 MET A HE2  1 
ATOM   2256 H HE3  . MET A 1 142 ? 18.794 51.249 36.898 0.00 42.13  ? 145 MET A HE3  1 
ATOM   2257 N N    . LEU A 1 143 ? 14.741 53.301 37.914 1.00 25.26  ? 146 LEU A N    1 
ATOM   2258 C CA   . LEU A 1 143 ? 15.306 54.218 38.890 1.00 27.09  ? 146 LEU A CA   1 
ATOM   2259 C C    . LEU A 1 143 ? 14.477 54.279 40.171 1.00 28.04  ? 146 LEU A C    1 
ATOM   2260 O O    . LEU A 1 143 ? 15.041 54.468 41.273 1.00 30.17  ? 146 LEU A O    1 
ATOM   2261 C CB   . LEU A 1 143 ? 15.462 55.647 38.319 1.00 27.91  ? 146 LEU A CB   1 
ATOM   2262 C CG   . LEU A 1 143 ? 16.514 55.744 37.190 1.00 37.65  ? 146 LEU A CG   1 
ATOM   2263 C CD1  . LEU A 1 143 ? 16.424 57.133 36.546 1.00 48.83  ? 146 LEU A CD1  1 
ATOM   2264 C CD2  . LEU A 1 143 ? 17.906 55.481 37.740 1.00 40.21  ? 146 LEU A CD2  1 
ATOM   2265 H H    . LEU A 1 143 ? 14.457 53.659 37.186 0.00 30.29  ? 146 LEU A H    1 
ATOM   2266 H HA   . LEU A 1 143 ? 16.193 53.887 39.101 0.00 32.48  ? 146 LEU A HA   1 
ATOM   2267 H HB2  . LEU A 1 143 ? 14.609 55.934 37.958 0.00 33.48  ? 146 LEU A HB2  1 
ATOM   2268 H HB3  . LEU A 1 143 ? 15.737 56.241 39.034 0.00 33.48  ? 146 LEU A HB3  1 
ATOM   2269 H HG   . LEU A 1 143 ? 16.344 55.074 36.509 0.00 45.17  ? 146 LEU A HG   1 
ATOM   2270 H HD11 . LEU A 1 143 ? 17.094 57.201 35.848 0.00 58.58  ? 146 LEU A HD11 1 
ATOM   2271 H HD12 . LEU A 1 143 ? 15.538 57.248 36.166 0.00 58.58  ? 146 LEU A HD12 1 
ATOM   2272 H HD13 . LEU A 1 143 ? 16.583 57.807 37.225 0.00 58.58  ? 146 LEU A HD13 1 
ATOM   2273 H HD21 . LEU A 1 143 ? 18.562 55.698 37.059 0.00 48.23  ? 146 LEU A HD21 1 
ATOM   2274 H HD22 . LEU A 1 143 ? 18.047 56.036 38.523 0.00 48.23  ? 146 LEU A HD22 1 
ATOM   2275 H HD23 . LEU A 1 143 ? 17.979 54.544 37.982 0.00 48.23  ? 146 LEU A HD23 1 
ATOM   2276 N N    . TYR A 1 144 ? 13.154 54.138 40.057 1.00 25.45  ? 147 TYR A N    1 
ATOM   2277 C CA   . TYR A 1 144 ? 12.327 54.050 41.271 1.00 28.84  ? 147 TYR A CA   1 
ATOM   2278 C C    . TYR A 1 144 ? 12.726 52.846 42.116 1.00 27.87  ? 147 TYR A C    1 
ATOM   2279 O O    . TYR A 1 144 ? 12.856 52.960 43.323 1.00 28.71  ? 147 TYR A O    1 
ATOM   2280 C CB   . TYR A 1 144 ? 10.822 53.974 40.886 1.00 28.91  ? 147 TYR A CB   1 
ATOM   2281 C CG   . TYR A 1 144 ? 9.925  53.793 42.085 1.00 29.85  ? 147 TYR A CG   1 
ATOM   2282 C CD1  . TYR A 1 144 ? 9.609  54.888 42.894 1.00 36.87  ? 147 TYR A CD1  1 
ATOM   2283 C CD2  . TYR A 1 144 ? 9.483  52.541 42.467 1.00 34.49  ? 147 TYR A CD2  1 
ATOM   2284 C CE1  . TYR A 1 144 ? 8.827  54.736 44.032 1.00 39.38  ? 147 TYR A CE1  1 
ATOM   2285 C CE2  . TYR A 1 144 ? 8.712  52.368 43.604 1.00 38.00  ? 147 TYR A CE2  1 
ATOM   2286 C CZ   . TYR A 1 144 ? 8.384  53.481 44.385 1.00 33.98  ? 147 TYR A CZ   1 
ATOM   2287 O OH   . TYR A 1 144 ? 7.635  53.322 45.555 1.00 43.26  ? 147 TYR A OH   1 
ATOM   2288 H H    . TYR A 1 144 ? 12.721 54.092 39.315 0.00 30.52  ? 147 TYR A H    1 
ATOM   2289 H HA   . TYR A 1 144 ? 12.459 54.851 41.803 0.00 34.59  ? 147 TYR A HA   1 
ATOM   2290 H HB2  . TYR A 1 144 ? 10.568 54.797 40.440 0.00 34.67  ? 147 TYR A HB2  1 
ATOM   2291 H HB3  . TYR A 1 144 ? 10.686 53.219 40.291 0.00 34.67  ? 147 TYR A HB3  1 
ATOM   2292 H HD1  . TYR A 1 144 ? 9.926  55.732 42.666 0.00 44.23  ? 147 TYR A HD1  1 
ATOM   2293 H HD2  . TYR A 1 144 ? 9.708  51.800 41.951 0.00 41.37  ? 147 TYR A HD2  1 
ATOM   2294 H HE1  . TYR A 1 144 ? 8.606  55.475 44.552 0.00 47.24  ? 147 TYR A HE1  1 
ATOM   2295 H HE2  . TYR A 1 144 ? 8.414  51.521 43.845 0.00 45.58  ? 147 TYR A HE2  1 
ATOM   2296 H HH   . TYR A 1 144 ? 7.393  52.521 45.635 0.00 51.89  ? 147 TYR A HH   1 
ATOM   2297 N N    . ILE A 1 145 ? 12.937 51.668 41.466 1.00 24.73  ? 148 ILE A N    1 
ATOM   2298 C CA   . ILE A 1 145 ? 13.328 50.471 42.214 1.00 24.49  ? 148 ILE A CA   1 
ATOM   2299 C C    . ILE A 1 145 ? 14.666 50.691 42.899 1.00 27.30  ? 148 ILE A C    1 
ATOM   2300 O O    . ILE A 1 145 ? 14.817 50.406 44.101 1.00 27.29  ? 148 ILE A O    1 
ATOM   2301 C CB   . ILE A 1 145 ? 13.375 49.253 41.241 1.00 25.04  ? 148 ILE A CB   1 
ATOM   2302 C CG1  . ILE A 1 145 ? 11.933 48.859 40.908 1.00 24.78  ? 148 ILE A CG1  1 
ATOM   2303 C CG2  . ILE A 1 145 ? 14.124 48.066 41.921 1.00 26.50  ? 148 ILE A CG2  1 
ATOM   2304 C CD1  . ILE A 1 145 ? 11.838 47.939 39.574 1.00 27.90  ? 148 ILE A CD1  1 
ATOM   2305 H H    . ILE A 1 145 ? 12.859 51.553 40.617 0.00 29.65  ? 148 ILE A H    1 
ATOM   2306 H HA   . ILE A 1 145 ? 12.671 50.294 42.904 0.00 29.37  ? 148 ILE A HA   1 
ATOM   2307 H HB   . ILE A 1 145 ? 13.849 49.486 40.428 0.00 30.02  ? 148 ILE A HB   1 
ATOM   2308 H HG12 . ILE A 1 145 ? 11.561 48.356 41.649 0.00 29.72  ? 148 ILE A HG12 1 
ATOM   2309 H HG13 . ILE A 1 145 ? 11.410 49.663 40.758 0.00 29.72  ? 148 ILE A HG13 1 
ATOM   2310 H HG21 . ILE A 1 145 ? 13.930 47.250 41.433 0.00 31.78  ? 148 ILE A HG21 1 
ATOM   2311 H HG22 . ILE A 1 145 ? 15.077 48.243 41.904 0.00 31.78  ? 148 ILE A HG22 1 
ATOM   2312 H HG23 . ILE A 1 145 ? 13.819 47.983 42.838 0.00 31.78  ? 148 ILE A HG23 1 
ATOM   2313 H HD11 . ILE A 1 145 ? 10.905 47.834 39.328 0.00 33.47  ? 148 ILE A HD11 1 
ATOM   2314 H HD12 . ILE A 1 145 ? 12.322 48.374 38.855 0.00 33.47  ? 148 ILE A HD12 1 
ATOM   2315 H HD13 . ILE A 1 145 ? 12.230 47.071 39.760 0.00 33.47  ? 148 ILE A HD13 1 
ATOM   2316 N N    . LEU A 1 146 ? 15.637 51.295 42.192 1.00 26.79  ? 149 LEU A N    1 
ATOM   2317 C CA   . LEU A 1 146 ? 16.946 51.449 42.823 1.00 30.81  ? 149 LEU A CA   1 
ATOM   2318 C C    . LEU A 1 146 ? 16.875 52.449 43.979 1.00 36.13  ? 149 LEU A C    1 
ATOM   2319 O O    . LEU A 1 146 ? 17.567 52.286 44.984 1.00 35.22  ? 149 LEU A O    1 
ATOM   2320 C CB   . LEU A 1 146 ? 18.004 51.955 41.807 1.00 31.01  ? 149 LEU A CB   1 
ATOM   2321 C CG   . LEU A 1 146 ? 18.250 51.099 40.562 1.00 40.69  ? 149 LEU A CG   1 
ATOM   2322 C CD1  . LEU A 1 146 ? 19.474 51.647 39.788 1.00 49.02  ? 149 LEU A CD1  1 
ATOM   2323 C CD2  . LEU A 1 146 ? 18.444 49.667 40.936 1.00 43.02  ? 149 LEU A CD2  1 
ATOM   2324 H H    . LEU A 1 146 ? 15.562 51.605 41.393 0.00 32.13  ? 149 LEU A H    1 
ATOM   2325 H HA   . LEU A 1 146 ? 17.226 50.578 43.145 0.00 36.95  ? 149 LEU A HA   1 
ATOM   2326 H HB2  . LEU A 1 146 ? 17.723 52.829 41.496 0.00 37.19  ? 149 LEU A HB2  1 
ATOM   2327 H HB3  . LEU A 1 146 ? 18.853 52.025 42.272 0.00 37.19  ? 149 LEU A HB3  1 
ATOM   2328 H HG   . LEU A 1 146 ? 17.476 51.140 39.978 0.00 48.80  ? 149 LEU A HG   1 
ATOM   2329 H HD11 . LEU A 1 146 ? 19.634 51.087 39.012 0.00 58.81  ? 149 LEU A HD11 1 
ATOM   2330 H HD12 . LEU A 1 146 ? 19.288 52.557 39.506 0.00 58.81  ? 149 LEU A HD12 1 
ATOM   2331 H HD13 . LEU A 1 146 ? 20.249 51.633 40.371 0.00 58.81  ? 149 LEU A HD13 1 
ATOM   2332 H HD21 . LEU A 1 146 ? 18.740 49.174 40.155 0.00 51.60  ? 149 LEU A HD21 1 
ATOM   2333 H HD22 . LEU A 1 146 ? 19.114 49.611 41.635 0.00 51.60  ? 149 LEU A HD22 1 
ATOM   2334 H HD23 . LEU A 1 146 ? 17.602 49.307 41.256 0.00 51.60  ? 149 LEU A HD23 1 
ATOM   2335 N N    . TYR A 1 147 ? 16.024 53.476 43.854 1.00 28.65  ? 150 TYR A N    1 
ATOM   2336 C CA   . TYR A 1 147 ? 15.846 54.430 44.959 1.00 31.89  ? 150 TYR A CA   1 
ATOM   2337 C C    . TYR A 1 147 ? 15.360 53.705 46.206 1.00 32.61  ? 150 TYR A C    1 
ATOM   2338 O O    . TYR A 1 147 ? 15.904 53.852 47.303 1.00 37.20  ? 150 TYR A O    1 
ATOM   2339 C CB   . TYR A 1 147 ? 14.825 55.487 44.516 1.00 30.83  ? 150 TYR A CB   1 
ATOM   2340 C CG   . TYR A 1 147 ? 14.496 56.440 45.645 1.00 42.91  ? 150 TYR A CG   1 
ATOM   2341 C CD1  . TYR A 1 147 ? 15.400 57.393 46.055 1.00 62.40  ? 150 TYR A CD1  1 
ATOM   2342 C CD2  . TYR A 1 147 ? 13.286 56.327 46.323 1.00 52.27  ? 150 TYR A CD2  1 
ATOM   2343 C CE1  . TYR A 1 147 ? 15.095 58.264 47.099 1.00 63.40  ? 150 TYR A CE1  1 
ATOM   2344 C CE2  . TYR A 1 147 ? 12.968 57.191 47.370 1.00 63.96  ? 150 TYR A CE2  1 
ATOM   2345 C CZ   . TYR A 1 147 ? 13.882 58.148 47.751 1.00 64.80  ? 150 TYR A CZ   1 
ATOM   2346 O OH   . TYR A 1 147 ? 13.576 59.008 48.789 1.00 74.20  ? 150 TYR A OH   1 
ATOM   2347 H H    . TYR A 1 147 ? 15.548 53.640 43.157 0.00 34.36  ? 150 TYR A H    1 
ATOM   2348 H HA   . TYR A 1 147 ? 16.686 54.868 45.171 0.00 38.24  ? 150 TYR A HA   1 
ATOM   2349 H HB2  . TYR A 1 147 ? 15.192 56.000 43.779 0.00 36.97  ? 150 TYR A HB2  1 
ATOM   2350 H HB3  . TYR A 1 147 ? 14.007 55.047 44.238 0.00 36.97  ? 150 TYR A HB3  1 
ATOM   2351 H HD1  . TYR A 1 147 ? 16.224 57.456 45.629 0.00 74.86  ? 150 TYR A HD1  1 
ATOM   2352 H HD2  . TYR A 1 147 ? 12.682 55.665 46.074 0.00 62.70  ? 150 TYR A HD2  1 
ATOM   2353 H HE1  . TYR A 1 147 ? 15.703 58.918 47.355 0.00 76.06  ? 150 TYR A HE1  1 
ATOM   2354 H HE2  . TYR A 1 147 ? 12.149 57.122 47.805 0.00 76.73  ? 150 TYR A HE2  1 
ATOM   2355 H HH   . TYR A 1 147 ? 12.811 58.835 49.089 0.00 89.02  ? 150 TYR A HH   1 
ATOM   2356 N N    . VAL A 1 148 ? 14.339 52.852 46.049 1.00 30.64  ? 151 VAL A N    1 
ATOM   2357 C CA   . VAL A 1 148 ? 13.795 52.171 47.233 1.00 33.34  ? 151 VAL A CA   1 
ATOM   2358 C C    . VAL A 1 148 ? 14.848 51.240 47.863 1.00 32.52  ? 151 VAL A C    1 
ATOM   2359 O O    . VAL A 1 148 ? 14.995 51.161 49.088 1.00 37.66  ? 151 VAL A O    1 
ATOM   2360 C CB   . VAL A 1 148 ? 12.528 51.401 46.813 1.00 36.12  ? 151 VAL A CB   1 
ATOM   2361 C CG1  . VAL A 1 148 ? 12.051 50.476 47.943 1.00 35.93  ? 151 VAL A CG1  1 
ATOM   2362 C CG2  . VAL A 1 148 ? 11.424 52.403 46.377 1.00 36.05  ? 151 VAL A CG2  1 
ATOM   2363 H H    . VAL A 1 148 ? 13.959 52.659 45.302 0.00 36.75  ? 151 VAL A H    1 
ATOM   2364 H HA   . VAL A 1 148 ? 13.561 52.828 47.908 0.00 39.99  ? 151 VAL A HA   1 
ATOM   2365 H HB   . VAL A 1 148 ? 12.729 50.832 46.054 0.00 43.33  ? 151 VAL A HB   1 
ATOM   2366 H HG11 . VAL A 1 148 ? 11.133 50.213 47.770 0.00 43.10  ? 151 VAL A HG11 1 
ATOM   2367 H HG12 . VAL A 1 148 ? 12.620 49.691 47.970 0.00 43.10  ? 151 VAL A HG12 1 
ATOM   2368 H HG13 . VAL A 1 148 ? 12.104 50.953 48.786 0.00 43.10  ? 151 VAL A HG13 1 
ATOM   2369 H HG21 . VAL A 1 148 ? 10.627 51.908 46.132 0.00 43.24  ? 151 VAL A HG21 1 
ATOM   2370 H HG22 . VAL A 1 148 ? 11.229 52.999 47.117 0.00 43.24  ? 151 VAL A HG22 1 
ATOM   2371 H HG23 . VAL A 1 148 ? 11.744 52.913 45.616 0.00 43.24  ? 151 VAL A HG23 1 
ATOM   2372 N N    . LEU A 1 149 ? 15.589 50.518 47.023 1.00 34.21  ? 152 LEU A N    1 
ATOM   2373 C CA   . LEU A 1 149 ? 16.605 49.608 47.562 1.00 33.00  ? 152 LEU A CA   1 
ATOM   2374 C C    . LEU A 1 149 ? 17.658 50.368 48.361 1.00 41.97  ? 152 LEU A C    1 
ATOM   2375 O O    . LEU A 1 149 ? 18.230 49.814 49.318 1.00 42.40  ? 152 LEU A O    1 
ATOM   2376 C CB   . LEU A 1 149 ? 17.254 48.808 46.417 1.00 34.81  ? 152 LEU A CB   1 
ATOM   2377 C CG   . LEU A 1 149 ? 16.358 47.845 45.673 1.00 35.04  ? 152 LEU A CG   1 
ATOM   2378 C CD1  . LEU A 1 149 ? 17.185 47.097 44.565 1.00 45.49  ? 152 LEU A CD1  1 
ATOM   2379 C CD2  . LEU A 1 149 ? 15.642 46.840 46.582 1.00 39.58  ? 152 LEU A CD2  1 
ATOM   2380 H H    . LEU A 1 149 ? 15.528 50.535 46.165 0.00 41.04  ? 152 LEU A H    1 
ATOM   2381 H HA   . LEU A 1 149 ? 16.182 48.972 48.160 0.00 39.58  ? 152 LEU A HA   1 
ATOM   2382 H HB2  . LEU A 1 149 ? 17.596 49.440 45.765 0.00 41.76  ? 152 LEU A HB2  1 
ATOM   2383 H HB3  . LEU A 1 149 ? 17.984 48.289 46.789 0.00 41.76  ? 152 LEU A HB3  1 
ATOM   2384 H HG   . LEU A 1 149 ? 15.653 48.367 45.260 0.00 42.03  ? 152 LEU A HG   1 
ATOM   2385 H HD11 . LEU A 1 149 ? 16.592 46.510 44.071 0.00 54.57  ? 152 LEU A HD11 1 
ATOM   2386 H HD12 . LEU A 1 149 ? 17.576 47.752 43.966 0.00 54.57  ? 152 LEU A HD12 1 
ATOM   2387 H HD13 . LEU A 1 149 ? 17.886 46.578 44.990 0.00 54.57  ? 152 LEU A HD13 1 
ATOM   2388 H HD21 . LEU A 1 149 ? 15.159 46.205 46.031 0.00 47.47  ? 152 LEU A HD21 1 
ATOM   2389 H HD22 . LEU A 1 149 ? 16.301 46.376 47.122 0.00 47.47  ? 152 LEU A HD22 1 
ATOM   2390 H HD23 . LEU A 1 149 ? 15.022 47.319 47.155 0.00 47.47  ? 152 LEU A HD23 1 
ATOM   2391 N N    . PHE A 1 150 ? 17.898 51.660 48.047 1.00 39.81  ? 153 PHE A N    1 
ATOM   2392 C CA   . PHE A 1 150 ? 18.878 52.450 48.824 1.00 41.37  ? 153 PHE A CA   1 
ATOM   2393 C C    . PHE A 1 150 ? 18.290 53.285 49.935 1.00 51.63  ? 153 PHE A C    1 
ATOM   2394 O O    . PHE A 1 150 ? 18.917 53.424 50.992 1.00 66.38  ? 153 PHE A O    1 
ATOM   2395 C CB   . PHE A 1 150 ? 19.651 53.389 47.909 1.00 54.40  ? 153 PHE A CB   1 
ATOM   2396 C CG   . PHE A 1 150 ? 20.810 52.743 47.259 1.00 53.24  ? 153 PHE A CG   1 
ATOM   2397 C CD1  . PHE A 1 150 ? 21.979 52.545 47.986 1.00 50.76  ? 153 PHE A CD1  1 
ATOM   2398 C CD2  . PHE A 1 150 ? 20.753 52.352 45.948 1.00 55.05  ? 153 PHE A CD2  1 
ATOM   2399 C CE1  . PHE A 1 150 ? 23.059 51.933 47.415 1.00 65.56  ? 153 PHE A CE1  1 
ATOM   2400 C CE2  . PHE A 1 150 ? 21.842 51.748 45.363 1.00 72.61  ? 153 PHE A CE2  1 
ATOM   2401 C CZ   . PHE A 1 150 ? 23.002 51.537 46.116 1.00 56.81  ? 153 PHE A CZ   1 
ATOM   2402 H H    . PHE A 1 150 ? 17.516 52.087 47.407 0.00 47.76  ? 153 PHE A H    1 
ATOM   2403 H HA   . PHE A 1 150 ? 19.486 51.810 49.226 0.00 49.63  ? 153 PHE A HA   1 
ATOM   2404 H HB2  . PHE A 1 150 ? 19.057 53.709 47.212 0.00 65.26  ? 153 PHE A HB2  1 
ATOM   2405 H HB3  . PHE A 1 150 ? 19.980 54.137 48.432 0.00 65.26  ? 153 PHE A HB3  1 
ATOM   2406 H HD1  . PHE A 1 150 ? 22.026 52.832 48.869 0.00 60.89  ? 153 PHE A HD1  1 
ATOM   2407 H HD2  . PHE A 1 150 ? 19.978 52.494 45.453 0.00 66.04  ? 153 PHE A HD2  1 
ATOM   2408 H HE1  . PHE A 1 150 ? 23.831 51.789 47.913 0.00 78.65  ? 153 PHE A HE1  1 
ATOM   2409 H HE2  . PHE A 1 150 ? 21.808 51.483 44.472 0.00 87.12  ? 153 PHE A HE2  1 
ATOM   2410 H HZ   . PHE A 1 150 ? 23.737 51.122 45.726 0.00 68.15  ? 153 PHE A HZ   1 
ATOM   2411 N N    . PHE A 1 151 ? 17.132 53.890 49.734 1.00 57.86  ? 154 PHE A N    1 
ATOM   2412 C CA   . PHE A 1 151 ? 16.608 54.799 50.736 1.00 58.74  ? 154 PHE A CA   1 
ATOM   2413 C C    . PHE A 1 151 ? 15.384 54.234 51.436 1.00 80.26  ? 154 PHE A C    1 
ATOM   2414 O O    . PHE A 1 151 ? 14.788 54.932 52.264 1.00 86.16  ? 154 PHE A O    1 
ATOM   2415 C CB   . PHE A 1 151 ? 16.300 56.162 50.106 1.00 52.46  ? 154 PHE A CB   1 
ATOM   2416 C CG   . PHE A 1 151 ? 17.491 56.794 49.417 1.00 58.95  ? 154 PHE A CG   1 
ATOM   2417 C CD1  . PHE A 1 151 ? 17.855 56.431 48.140 1.00 63.08  ? 154 PHE A CD1  1 
ATOM   2418 C CD2  . PHE A 1 151 ? 18.265 57.751 50.084 1.00 74.49  ? 154 PHE A CD2  1 
ATOM   2419 C CE1  . PHE A 1 151 ? 18.945 57.001 47.515 1.00 58.08  ? 154 PHE A CE1  1 
ATOM   2420 C CE2  . PHE A 1 151 ? 19.370 58.329 49.469 1.00 75.28  ? 154 PHE A CE2  1 
ATOM   2421 C CZ   . PHE A 1 151 ? 19.719 57.950 48.187 1.00 70.04  ? 154 PHE A CZ   1 
ATOM   2422 H H    . PHE A 1 151 ? 16.639 53.791 49.036 0.00 69.42  ? 154 PHE A H    1 
ATOM   2423 H HA   . PHE A 1 151 ? 17.282 54.956 51.415 0.00 70.47  ? 154 PHE A HA   1 
ATOM   2424 H HB2  . PHE A 1 151 ? 15.600 56.050 49.445 0.00 62.93  ? 154 PHE A HB2  1 
ATOM   2425 H HB3  . PHE A 1 151 ? 16.004 56.769 50.803 0.00 62.93  ? 154 PHE A HB3  1 
ATOM   2426 H HD1  . PHE A 1 151 ? 17.357 55.788 47.689 0.00 75.68  ? 154 PHE A HD1  1 
ATOM   2427 H HD2  . PHE A 1 151 ? 18.037 58.004 50.949 0.00 89.36  ? 154 PHE A HD2  1 
ATOM   2428 H HE1  . PHE A 1 151 ? 19.164 56.754 46.646 0.00 69.68  ? 154 PHE A HE1  1 
ATOM   2429 H HE2  . PHE A 1 151 ? 19.872 58.969 49.920 0.00 90.32  ? 154 PHE A HE2  1 
ATOM   2430 H HZ   . PHE A 1 151 ? 20.464 58.324 47.775 0.00 84.02  ? 154 PHE A HZ   1 
ATOM   2431 N N    . GLY A 1 152 ? 14.997 52.994 51.128 1.00 54.21  ? 155 GLY A N    1 
ATOM   2432 C CA   . GLY A 1 152 ? 14.122 52.257 52.022 1.00 69.69  ? 155 GLY A CA   1 
ATOM   2433 C C    . GLY A 1 152 ? 14.831 51.077 52.670 1.00 49.47  ? 155 GLY A C    1 
ATOM   2434 O O    . GLY A 1 152 ? 14.913 50.946 53.889 1.00 54.38  ? 155 GLY A O    1 
ATOM   2435 H H    . GLY A 1 152 ? 15.227 52.568 50.417 0.00 65.04  ? 155 GLY A H    1 
ATOM   2436 H HA2  . GLY A 1 152 ? 13.806 52.848 52.723 0.00 83.61  ? 155 GLY A HA2  1 
ATOM   2437 H HA3  . GLY A 1 152 ? 13.360 51.922 51.524 0.00 83.61  ? 155 GLY A HA3  1 
ATOM   2438 N N    . PHE A 1 153 ? 15.380 50.184 51.851 1.00 56.91  ? 156 PHE A N    1 
ATOM   2439 C CA   . PHE A 1 153 ? 15.810 48.908 52.410 1.00 56.21  ? 156 PHE A CA   1 
ATOM   2440 C C    . PHE A 1 153 ? 17.063 49.062 53.270 1.00 70.49  ? 156 PHE A C    1 
ATOM   2441 O O    . PHE A 1 153 ? 17.180 48.425 54.328 1.00 69.56  ? 156 PHE A O    1 
ATOM   2442 C CB   . PHE A 1 153 ? 16.059 47.910 51.298 1.00 52.17  ? 156 PHE A CB   1 
ATOM   2443 C CG   . PHE A 1 153 ? 14.819 47.278 50.769 1.00 54.03  ? 156 PHE A CG   1 
ATOM   2444 C CD1  . PHE A 1 153 ? 13.588 47.834 51.008 1.00 52.20  ? 156 PHE A CD1  1 
ATOM   2445 C CD2  . PHE A 1 153 ? 14.896 46.079 50.089 1.00 49.60  ? 156 PHE A CD2  1 
ATOM   2446 C CE1  . PHE A 1 153 ? 12.457 47.229 50.532 1.00 52.54  ? 156 PHE A CE1  1 
ATOM   2447 C CE2  . PHE A 1 153 ? 13.772 45.470 49.614 1.00 50.30  ? 156 PHE A CE2  1 
ATOM   2448 C CZ   . PHE A 1 153 ? 12.544 46.040 49.844 1.00 57.18  ? 156 PHE A CZ   1 
ATOM   2449 H H    . PHE A 1 153 ? 15.509 50.288 51.007 0.00 68.28  ? 156 PHE A H    1 
ATOM   2450 H HA   . PHE A 1 153 ? 15.099 48.567 52.975 0.00 67.43  ? 156 PHE A HA   1 
ATOM   2451 H HB2  . PHE A 1 153 ? 16.496 48.366 50.562 0.00 62.58  ? 156 PHE A HB2  1 
ATOM   2452 H HB3  . PHE A 1 153 ? 16.631 47.203 51.636 0.00 62.58  ? 156 PHE A HB3  1 
ATOM   2453 H HD1  . PHE A 1 153 ? 13.521 48.624 51.494 0.00 62.62  ? 156 PHE A HD1  1 
ATOM   2454 H HD2  . PHE A 1 153 ? 15.725 45.681 49.953 0.00 59.50  ? 156 PHE A HD2  1 
ATOM   2455 H HE1  . PHE A 1 153 ? 11.626 47.622 50.673 0.00 63.03  ? 156 PHE A HE1  1 
ATOM   2456 H HE2  . PHE A 1 153 ? 13.837 44.674 49.137 0.00 60.34  ? 156 PHE A HE2  1 
ATOM   2457 H HZ   . PHE A 1 153 ? 11.772 45.623 49.536 0.00 68.60  ? 156 PHE A HZ   1 
ATOM   2458 N N    . THR A 1 154 ? 18.025 49.877 52.821 1.00 59.97  ? 157 THR A N    1 
ATOM   2459 C CA   . THR A 1 154 ? 19.244 50.076 53.603 1.00 69.36  ? 157 THR A CA   1 
ATOM   2460 C C    . THR A 1 154 ? 18.920 50.571 55.003 1.00 67.99  ? 157 THR A C    1 
ATOM   2461 O O    . THR A 1 154 ? 19.490 50.085 55.991 1.00 66.91  ? 157 THR A O    1 
ATOM   2462 C CB   . THR A 1 154 ? 20.169 51.056 52.886 1.00 67.79  ? 157 THR A CB   1 
ATOM   2463 O OG1  . THR A 1 154 ? 20.597 50.469 51.644 1.00 54.26  ? 157 THR A OG1  1 
ATOM   2464 C CG2  . THR A 1 154 ? 21.380 51.407 53.759 1.00 81.13  ? 157 THR A CG2  1 
ATOM   2465 H H    . THR A 1 154 ? 17.995 50.316 52.082 0.00 71.94  ? 157 THR A H    1 
ATOM   2466 H HA   . THR A 1 154 ? 19.709 49.229 53.684 0.00 83.21  ? 157 THR A HA   1 
ATOM   2467 H HB   . THR A 1 154 ? 19.699 51.885 52.705 0.00 81.33  ? 157 THR A HB   1 
ATOM   2468 H HG1  . THR A 1 154 ? 19.929 50.290 51.166 0.00 65.09  ? 157 THR A HG1  1 
ATOM   2469 H HG21 . THR A 1 154 ? 22.037 51.891 53.235 0.00 97.33  ? 157 THR A HG21 1 
ATOM   2470 H HG22 . THR A 1 154 ? 21.102 51.960 54.505 0.00 97.33  ? 157 THR A HG22 1 
ATOM   2471 H HG23 . THR A 1 154 ? 21.787 50.596 54.102 0.00 97.33  ? 157 THR A HG23 1 
ATOM   2472 N N    . SER A 1 155 ? 17.998 51.526 55.111 1.00 64.34  ? 158 SER A N    1 
ATOM   2473 C CA   . SER A 1 155 ? 17.655 52.072 56.422 1.00 84.56  ? 158 SER A CA   1 
ATOM   2474 C C    . SER A 1 155 ? 17.140 50.983 57.361 1.00 92.42  ? 158 SER A C    1 
ATOM   2475 O O    . SER A 1 155 ? 17.470 50.974 58.555 1.00 81.89  ? 158 SER A O    1 
ATOM   2476 C CB   . SER A 1 155 ? 16.618 53.190 56.269 1.00 66.12  ? 158 SER A CB   1 
ATOM   2477 H H    . SER A 1 155 ? 17.564 51.870 54.453 0.00 77.19  ? 158 SER A H    1 
ATOM   2478 H HA   . SER A 1 155 ? 18.453 52.455 56.820 0.00 101.45 ? 158 SER A HA   1 
ATOM   2479 N N    . LYS A 1 156 ? 16.335 50.047 56.848 1.00 78.61  ? 159 LYS A N    1 
ATOM   2480 C CA   . LYS A 1 156 ? 15.769 49.048 57.749 1.00 85.81  ? 159 LYS A CA   1 
ATOM   2481 C C    . LYS A 1 156 ? 16.770 47.938 58.053 1.00 81.56  ? 159 LYS A C    1 
ATOM   2482 O O    . LYS A 1 156 ? 16.858 47.483 59.197 1.00 71.39  ? 159 LYS A O    1 
ATOM   2483 C CB   . LYS A 1 156 ? 14.478 48.469 57.169 1.00 81.06  ? 159 LYS A CB   1 
ATOM   2484 C CG   . LYS A 1 156 ? 13.478 48.074 58.259 1.00 97.26  ? 159 LYS A CG   1 
ATOM   2485 C CD   . LYS A 1 156 ? 12.153 47.591 57.677 1.00 79.72  ? 159 LYS A CD   1 
ATOM   2486 C CE   . LYS A 1 156 ? 11.482 46.510 58.521 1.00 76.02  ? 159 LYS A CE   1 
ATOM   2487 N NZ   . LYS A 1 156 ? 12.415 45.525 59.130 1.00 78.94  ? 159 LYS A NZ   1 
ATOM   2488 H H    . LYS A 1 156 ? 16.113 49.975 56.021 0.00 94.32  ? 159 LYS A H    1 
ATOM   2489 H HA   . LYS A 1 156 ? 15.541 49.482 58.586 0.00 102.95 ? 159 LYS A HA   1 
ATOM   2490 H HB2  . LYS A 1 156 ? 14.059 49.134 56.601 0.00 97.25  ? 159 LYS A HB2  1 
ATOM   2491 H HB3  . LYS A 1 156 ? 14.690 47.676 56.652 0.00 97.25  ? 159 LYS A HB3  1 
ATOM   2492 H HG2  . LYS A 1 156 ? 13.854 47.356 58.791 0.00 116.69 ? 159 LYS A HG2  1 
ATOM   2493 H HG3  . LYS A 1 156 ? 13.299 48.844 58.821 0.00 116.69 ? 159 LYS A HG3  1 
ATOM   2494 H HD2  . LYS A 1 156 ? 11.543 48.343 57.618 0.00 95.64  ? 159 LYS A HD2  1 
ATOM   2495 H HD3  . LYS A 1 156 ? 12.313 47.223 56.794 0.00 95.64  ? 159 LYS A HD3  1 
ATOM   2496 H HE2  . LYS A 1 156 ? 10.998 46.939 59.245 0.00 91.21  ? 159 LYS A HE2  1 
ATOM   2497 H HE3  . LYS A 1 156 ? 10.866 46.016 57.957 0.00 91.21  ? 159 LYS A HE3  1 
ATOM   2498 H HZ1  . LYS A 1 156 ? 11.963 44.815 59.418 0.00 94.71  ? 159 LYS A HZ1  1 
ATOM   2499 H HZ2  . LYS A 1 156 ? 13.015 45.262 58.528 0.00 94.71  ? 159 LYS A HZ2  1 
ATOM   2500 H HZ3  . LYS A 1 156 ? 12.841 45.895 59.819 0.00 94.71  ? 159 LYS A HZ3  1 
ATOM   2501 N N    . ALA A 1 157 ? 17.541 47.505 57.051 1.00 70.85  ? 160 ALA A N    1 
ATOM   2502 C CA   . ALA A 1 157 ? 18.544 46.465 57.276 1.00 65.41  ? 160 ALA A CA   1 
ATOM   2503 C C    . ALA A 1 157 ? 19.432 46.801 58.463 1.00 76.51  ? 160 ALA A C    1 
ATOM   2504 O O    . ALA A 1 157 ? 19.800 45.919 59.250 1.00 75.00  ? 160 ALA A O    1 
ATOM   2505 C CB   . ALA A 1 157 ? 19.398 46.291 56.019 1.00 56.48  ? 160 ALA A CB   1 
ATOM   2506 H H    . ALA A 1 157 ? 17.503 47.794 56.242 0.00 85.00  ? 160 ALA A H    1 
ATOM   2507 H HA   . ALA A 1 157 ? 18.091 45.627 57.462 0.00 78.47  ? 160 ALA A HA   1 
ATOM   2508 H HB1  . ALA A 1 157 ? 20.057 45.598 56.179 0.00 67.76  ? 160 ALA A HB1  1 
ATOM   2509 H HB2  . ALA A 1 157 ? 18.823 46.037 55.280 0.00 67.76  ? 160 ALA A HB2  1 
ATOM   2510 H HB3  . ALA A 1 157 ? 19.841 47.130 55.820 0.00 67.76  ? 160 ALA A HB3  1 
ATOM   2511 N N    . GLU A 1 158 ? 19.774 48.082 58.612 1.00 63.69  ? 161 GLU A N    1 
ATOM   2512 C CA   . GLU A 1 158 ? 20.768 48.514 59.584 1.00 80.59  ? 161 GLU A CA   1 
ATOM   2513 C C    . GLU A 1 158 ? 20.293 48.342 61.013 1.00 76.91  ? 161 GLU A C    1 
ATOM   2514 O O    . GLU A 1 158 ? 21.105 48.449 61.939 1.00 83.02  ? 161 GLU A O    1 
ATOM   2515 C CB   . GLU A 1 158 ? 21.127 49.976 59.317 1.00 84.91  ? 161 GLU A CB   1 
ATOM   2516 C CG   . GLU A 1 158 ? 21.966 50.157 58.051 1.00 95.59  ? 161 GLU A CG   1 
ATOM   2517 C CD   . GLU A 1 158 ? 22.928 51.318 58.120 1.00 109.10 ? 161 GLU A CD   1 
ATOM   2518 O OE1  . GLU A 1 158 ? 22.614 52.309 58.812 1.00 120.95 ? 161 GLU A OE1  1 
ATOM   2519 O OE2  . GLU A 1 158 ? 23.977 51.253 57.440 1.00 99.89  ? 161 GLU A OE2  1 
ATOM   2520 H H    . GLU A 1 158 ? 19.437 48.727 58.154 0.00 76.41  ? 161 GLU A H    1 
ATOM   2521 H HA   . GLU A 1 158 ? 21.574 47.984 59.482 0.00 96.69  ? 161 GLU A HA   1 
ATOM   2522 H HB2  . GLU A 1 158 ? 20.309 50.488 59.211 0.00 101.88 ? 161 GLU A HB2  1 
ATOM   2523 H HB3  . GLU A 1 158 ? 21.637 50.318 60.068 0.00 101.88 ? 161 GLU A HB3  1 
ATOM   2524 H HG2  . GLU A 1 158 ? 22.485 49.351 57.903 0.00 114.69 ? 161 GLU A HG2  1 
ATOM   2525 H HG3  . GLU A 1 158 ? 21.371 50.310 57.300 0.00 114.69 ? 161 GLU A HG3  1 
ATOM   2526 N N    . SER A 1 159 ? 19.005 48.079 61.217 1.00 84.42  ? 162 SER A N    1 
ATOM   2527 C CA   . SER A 1 159 ? 18.444 47.860 62.543 1.00 86.93  ? 162 SER A CA   1 
ATOM   2528 C C    . SER A 1 159 ? 18.183 46.383 62.831 1.00 86.06  ? 162 SER A C    1 
ATOM   2529 O O    . SER A 1 159 ? 17.533 46.063 63.830 1.00 77.66  ? 162 SER A O    1 
ATOM   2530 C CB   . SER A 1 159 ? 17.158 48.679 62.692 1.00 91.62  ? 162 SER A CB   1 
ATOM   2531 O OG   . SER A 1 159 ? 16.171 48.259 61.765 1.00 88.92  ? 162 SER A OG   1 
ATOM   2532 H H    . SER A 1 159 ? 18.423 48.021 60.586 0.00 101.28 ? 162 SER A H    1 
ATOM   2533 H HA   . SER A 1 159 ? 19.072 48.171 63.213 0.00 104.30 ? 162 SER A HA   1 
ATOM   2534 H HB2  . SER A 1 159 ? 16.814 48.562 63.591 0.00 109.93 ? 162 SER A HB2  1 
ATOM   2535 H HB3  . SER A 1 159 ? 17.361 49.614 62.533 0.00 109.93 ? 162 SER A HB3  1 
ATOM   2536 H HG   . SER A 1 159 ? 16.444 48.378 60.980 0.00 106.68 ? 162 SER A HG   1 
ATOM   2537 N N    . MET A 1 160 ? 18.704 45.480 61.993 1.00 68.57  ? 163 MET A N    1 
ATOM   2538 C CA   . MET A 1 160 ? 18.484 44.046 62.101 1.00 66.54  ? 163 MET A CA   1 
ATOM   2539 C C    . MET A 1 160 ? 19.754 43.335 62.573 1.00 62.88  ? 163 MET A C    1 
ATOM   2540 O O    . MET A 1 160 ? 20.770 43.964 62.887 1.00 61.30  ? 163 MET A O    1 
ATOM   2541 C CB   . MET A 1 160 ? 18.021 43.506 60.750 1.00 59.89  ? 163 MET A CB   1 
ATOM   2542 C CG   . MET A 1 160 ? 16.998 44.413 60.105 1.00 82.84  ? 163 MET A CG   1 
ATOM   2543 S SD   . MET A 1 160 ? 15.781 43.612 59.040 1.00 78.16  ? 163 MET A SD   1 
ATOM   2544 C CE   . MET A 1 160 ? 15.253 42.162 59.961 1.00 65.75  ? 163 MET A CE   1 
ATOM   2545 H H    . MET A 1 160 ? 19.209 45.690 61.329 0.00 82.27  ? 163 MET A H    1 
ATOM   2546 H HA   . MET A 1 160 ? 17.793 43.886 62.762 0.00 79.83  ? 163 MET A HA   1 
ATOM   2547 H HB2  . MET A 1 160 ? 18.784 43.435 60.155 0.00 71.85  ? 163 MET A HB2  1 
ATOM   2548 H HB3  . MET A 1 160 ? 17.617 42.633 60.877 0.00 71.85  ? 163 MET A HB3  1 
ATOM   2549 H HG2  . MET A 1 160 ? 16.507 44.864 60.809 0.00 99.39  ? 163 MET A HG2  1 
ATOM   2550 H HG3  . MET A 1 160 ? 17.470 45.062 59.560 0.00 99.39  ? 163 MET A HG3  1 
ATOM   2551 H HE1  . MET A 1 160 ? 14.577 41.692 59.448 0.00 78.88  ? 163 MET A HE1  1 
ATOM   2552 H HE2  . MET A 1 160 ? 16.018 41.584 60.107 0.00 78.88  ? 163 MET A HE2  1 
ATOM   2553 H HE3  . MET A 1 160 ? 14.885 42.445 60.812 0.00 78.88  ? 163 MET A HE3  1 
ATOM   2554 N N    . ARG A 1 161 ? 19.672 42.002 62.641 1.00 57.57  ? 164 ARG A N    1 
ATOM   2555 C CA   . ARG A 1 161 ? 20.828 41.190 63.012 1.00 64.68  ? 164 ARG A CA   1 
ATOM   2556 C C    . ARG A 1 161 ? 22.028 41.607 62.161 1.00 43.67  ? 164 ARG A C    1 
ATOM   2557 O O    . ARG A 1 161 ? 21.858 41.934 60.986 1.00 43.10  ? 164 ARG A O    1 
ATOM   2558 C CB   . ARG A 1 161 ? 20.542 39.693 62.788 1.00 65.10  ? 164 ARG A CB   1 
ATOM   2559 C CG   . ARG A 1 161 ? 19.424 39.089 63.647 1.00 66.88  ? 164 ARG A CG   1 
ATOM   2560 C CD   . ARG A 1 161 ? 18.694 37.951 62.927 1.00 76.91  ? 164 ARG A CD   1 
ATOM   2561 N NE   . ARG A 1 161 ? 19.598 36.880 62.515 1.00 72.12  ? 164 ARG A NE   1 
ATOM   2562 C CZ   . ARG A 1 161 ? 19.260 35.874 61.717 1.00 66.16  ? 164 ARG A CZ   1 
ATOM   2563 N NH1  . ARG A 1 161 ? 18.040 35.760 61.225 1.00 54.51  ? 164 ARG A NH1  1 
ATOM   2564 N NH2  . ARG A 1 161 ? 20.170 34.956 61.408 1.00 67.27  ? 164 ARG A NH2  1 
ATOM   2565 H H    . ARG A 1 161 ? 18.960 41.548 62.478 0.00 69.07  ? 164 ARG A H    1 
ATOM   2566 H HA   . ARG A 1 161 ? 21.029 41.324 63.952 0.00 77.59  ? 164 ARG A HA   1 
ATOM   2567 H HB2  . ARG A 1 161 ? 20.290 39.568 61.860 0.00 78.11  ? 164 ARG A HB2  1 
ATOM   2568 H HB3  . ARG A 1 161 ? 21.353 39.197 62.982 0.00 78.11  ? 164 ARG A HB3  1 
ATOM   2569 H HG2  . ARG A 1 161 ? 19.806 38.733 64.465 0.00 80.24  ? 164 ARG A HG2  1 
ATOM   2570 H HG3  . ARG A 1 161 ? 18.775 39.778 63.857 0.00 80.24  ? 164 ARG A HG3  1 
ATOM   2571 H HD2  . ARG A 1 161 ? 18.031 37.571 63.525 0.00 92.27  ? 164 ARG A HD2  1 
ATOM   2572 H HD3  . ARG A 1 161 ? 18.263 38.303 62.133 0.00 92.27  ? 164 ARG A HD3  1 
ATOM   2573 H HE   . ARG A 1 161 ? 20.406 36.903 62.810 0.00 86.52  ? 164 ARG A HE   1 
ATOM   2574 H HH11 . ARG A 1 161 ? 17.441 36.347 61.419 0.00 65.39  ? 164 ARG A HH11 1 
ATOM   2575 H HH12 . ARG A 1 161 ? 17.844 35.100 60.710 0.00 65.39  ? 164 ARG A HH12 1 
ATOM   2576 H HH21 . ARG A 1 161 ? 20.968 35.018 61.724 0.00 80.70  ? 164 ARG A HH21 1 
ATOM   2577 H HH22 . ARG A 1 161 ? 19.962 34.301 60.892 0.00 80.70  ? 164 ARG A HH22 1 
ATOM   2578 N N    . PRO A 1 162 ? 23.245 41.624 62.717 1.00 45.79  ? 165 PRO A N    1 
ATOM   2579 C CA   . PRO A 1 162 ? 24.395 42.069 61.906 1.00 44.39  ? 165 PRO A CA   1 
ATOM   2580 C C    . PRO A 1 162 ? 24.650 41.228 60.681 1.00 50.64  ? 165 PRO A C    1 
ATOM   2581 O O    . PRO A 1 162 ? 25.081 41.773 59.648 1.00 46.87  ? 165 PRO A O    1 
ATOM   2582 C CB   . PRO A 1 162 ? 25.574 41.992 62.892 1.00 46.18  ? 165 PRO A CB   1 
ATOM   2583 C CG   . PRO A 1 162 ? 24.953 42.050 64.241 1.00 54.03  ? 165 PRO A CG   1 
ATOM   2584 C CD   . PRO A 1 162 ? 23.592 41.478 64.135 1.00 52.94  ? 165 PRO A CD   1 
ATOM   2585 H HA   . PRO A 1 162 ? 24.256 42.989 61.633 0.00 53.25  ? 165 PRO A HA   1 
ATOM   2586 H HB2  . PRO A 1 162 ? 26.055 41.158 62.767 0.00 55.39  ? 165 PRO A HB2  1 
ATOM   2587 H HB3  . PRO A 1 162 ? 26.171 42.743 62.753 0.00 55.39  ? 165 PRO A HB3  1 
ATOM   2588 H HG2  . PRO A 1 162 ? 25.489 41.532 64.862 0.00 64.81  ? 165 PRO A HG2  1 
ATOM   2589 H HG3  . PRO A 1 162 ? 24.909 42.974 64.533 0.00 64.81  ? 165 PRO A HG3  1 
ATOM   2590 H HD2  . PRO A 1 162 ? 23.595 40.543 64.392 0.00 63.50  ? 165 PRO A HD2  1 
ATOM   2591 H HD3  . PRO A 1 162 ? 22.971 41.973 64.692 0.00 63.50  ? 165 PRO A HD3  1 
ATOM   2592 N N    . GLU A 1 163 ? 24.390 39.915 60.734 1.00 46.65  ? 166 GLU A N    1 
ATOM   2593 C CA   . GLU A 1 163 ? 24.622 39.111 59.531 1.00 48.70  ? 166 GLU A CA   1 
ATOM   2594 C C    . GLU A 1 163 ? 23.597 39.418 58.450 1.00 39.56  ? 166 GLU A C    1 
ATOM   2595 O O    . GLU A 1 163 ? 23.888 39.247 57.277 1.00 44.69  ? 166 GLU A O    1 
ATOM   2596 C CB   . GLU A 1 163 ? 24.614 37.614 59.866 1.00 58.14  ? 166 GLU A CB   1 
ATOM   2597 C CG   . GLU A 1 163 ? 23.288 37.056 60.324 1.00 61.06  ? 166 GLU A CG   1 
ATOM   2598 C CD   . GLU A 1 163 ? 23.106 37.136 61.808 1.00 69.45  ? 166 GLU A CD   1 
ATOM   2599 O OE1  . GLU A 1 163 ? 23.733 38.022 62.421 1.00 62.50  ? 166 GLU A OE1  1 
ATOM   2600 O OE2  . GLU A 1 163 ? 22.346 36.311 62.373 1.00 76.57  ? 166 GLU A OE2  1 
ATOM   2601 H H    . GLU A 1 163 ? 24.094 39.488 61.420 0.00 55.96  ? 166 GLU A H    1 
ATOM   2602 H HA   . GLU A 1 163 ? 25.502 39.325 59.185 0.00 58.43  ? 166 GLU A HA   1 
ATOM   2603 H HB2  . GLU A 1 163 ? 24.875 37.122 59.072 0.00 69.74  ? 166 GLU A HB2  1 
ATOM   2604 H HB3  . GLU A 1 163 ? 25.254 37.457 60.578 0.00 69.74  ? 166 GLU A HB3  1 
ATOM   2605 H HG2  . GLU A 1 163 ? 22.572 37.561 59.907 0.00 73.25  ? 166 GLU A HG2  1 
ATOM   2606 H HG3  . GLU A 1 163 ? 23.231 36.123 60.064 0.00 73.25  ? 166 GLU A HG3  1 
ATOM   2607 N N    . VAL A 1 164 ? 22.383 39.829 58.831 1.00 41.58  ? 167 VAL A N    1 
ATOM   2608 C CA   . VAL A 1 164 ? 21.400 40.221 57.830 1.00 35.93  ? 167 VAL A CA   1 
ATOM   2609 C C    . VAL A 1 164 ? 21.841 41.516 57.167 1.00 36.01  ? 167 VAL A C    1 
ATOM   2610 O O    . VAL A 1 164 ? 21.797 41.657 55.947 1.00 40.01  ? 167 VAL A O    1 
ATOM   2611 C CB   . VAL A 1 164 ? 20.017 40.365 58.496 1.00 46.36  ? 167 VAL A CB   1 
ATOM   2612 C CG1  . VAL A 1 164 ? 19.027 41.058 57.550 1.00 49.03  ? 167 VAL A CG1  1 
ATOM   2613 C CG2  . VAL A 1 164 ? 19.500 39.007 58.968 1.00 45.76  ? 167 VAL A CG2  1 
ATOM   2614 H H    . VAL A 1 164 ? 22.114 39.889 59.646 0.00 49.88  ? 167 VAL A H    1 
ATOM   2615 H HA   . VAL A 1 164 ? 21.337 39.535 57.147 0.00 43.09  ? 167 VAL A HA   1 
ATOM   2616 H HB   . VAL A 1 164 ? 20.102 40.926 59.283 0.00 55.62  ? 167 VAL A HB   1 
ATOM   2617 H HG11 . VAL A 1 164 ? 18.151 41.073 57.966 0.00 58.82  ? 167 VAL A HG11 1 
ATOM   2618 H HG12 . VAL A 1 164 ? 19.331 41.964 57.385 0.00 58.82  ? 167 VAL A HG12 1 
ATOM   2619 H HG13 . VAL A 1 164 ? 18.990 40.564 56.716 0.00 58.82  ? 167 VAL A HG13 1 
ATOM   2620 H HG21 . VAL A 1 164 ? 18.625 39.125 59.371 0.00 54.89  ? 167 VAL A HG21 1 
ATOM   2621 H HG22 . VAL A 1 164 ? 19.435 38.412 58.205 0.00 54.89  ? 167 VAL A HG22 1 
ATOM   2622 H HG23 . VAL A 1 164 ? 20.118 38.643 59.620 0.00 54.89  ? 167 VAL A HG23 1 
ATOM   2623 N N    . ALA A 1 165 ? 22.320 42.470 57.973 1.00 45.24  ? 168 ALA A N    1 
ATOM   2624 C CA   . ALA A 1 165 ? 22.716 43.765 57.420 1.00 41.85  ? 168 ALA A CA   1 
ATOM   2625 C C    . ALA A 1 165 ? 23.887 43.630 56.450 1.00 43.54  ? 168 ALA A C    1 
ATOM   2626 O O    . ALA A 1 165 ? 23.872 44.227 55.363 1.00 45.92  ? 168 ALA A O    1 
ATOM   2627 C CB   . ALA A 1 165 ? 23.065 44.727 58.566 1.00 50.04  ? 168 ALA A CB   1 
ATOM   2628 H H    . ALA A 1 165 ? 22.423 42.394 58.823 0.00 54.27  ? 168 ALA A H    1 
ATOM   2629 H HA   . ALA A 1 165 ? 21.970 44.137 56.924 0.00 50.20  ? 168 ALA A HA   1 
ATOM   2630 H HB1  . ALA A 1 165 ? 23.326 45.583 58.191 0.00 60.03  ? 168 ALA A HB1  1 
ATOM   2631 H HB2  . ALA A 1 165 ? 22.287 44.838 59.134 0.00 60.03  ? 168 ALA A HB2  1 
ATOM   2632 H HB3  . ALA A 1 165 ? 23.799 44.353 59.079 0.00 60.03  ? 168 ALA A HB3  1 
ATOM   2633 N N    . SER A 1 166 ? 24.911 42.842 56.810 1.00 44.45  ? 169 SER A N    1 
ATOM   2634 C CA   . SER A 1 166 ? 26.084 42.731 55.953 1.00 40.90  ? 169 SER A CA   1 
ATOM   2635 C C    . SER A 1 166 ? 25.781 41.961 54.677 1.00 39.03  ? 169 SER A C    1 
ATOM   2636 O O    . SER A 1 166 ? 26.269 42.325 53.596 1.00 38.57  ? 169 SER A O    1 
ATOM   2637 C CB   . SER A 1 166 ? 27.249 42.074 56.703 1.00 55.90  ? 169 SER A CB   1 
ATOM   2638 O OG   . SER A 1 166 ? 26.817 40.899 57.353 1.00 67.42  ? 169 SER A OG   1 
ATOM   2639 H H    . SER A 1 166 ? 24.944 42.374 57.531 0.00 53.33  ? 169 SER A H    1 
ATOM   2640 H HA   . SER A 1 166 ? 26.356 43.630 55.707 0.00 49.06  ? 169 SER A HA   1 
ATOM   2641 H HB2  . SER A 1 166 ? 27.948 41.847 56.069 0.00 67.06  ? 169 SER A HB2  1 
ATOM   2642 H HB3  . SER A 1 166 ? 27.591 42.695 57.365 0.00 67.06  ? 169 SER A HB3  1 
ATOM   2643 H HG   . SER A 1 166 ? 27.451 40.560 57.787 0.00 80.89  ? 169 SER A HG   1 
ATOM   2644 N N    . THR A 1 167 ? 24.970 40.901 54.763 1.00 36.64  ? 170 THR A N    1 
ATOM   2645 C CA   . THR A 1 167 ? 24.596 40.202 53.528 1.00 31.03  ? 170 THR A CA   1 
ATOM   2646 C C    . THR A 1 167 ? 23.694 41.056 52.630 1.00 34.00  ? 170 THR A C    1 
ATOM   2647 O O    . THR A 1 167 ? 23.844 41.024 51.407 1.00 35.51  ? 170 THR A O    1 
ATOM   2648 C CB   . THR A 1 167 ? 23.917 38.859 53.818 1.00 37.84  ? 170 THR A CB   1 
ATOM   2649 O OG1  . THR A 1 167 ? 24.738 38.108 54.705 1.00 42.70  ? 170 THR A OG1  1 
ATOM   2650 C CG2  . THR A 1 167 ? 23.680 38.059 52.518 1.00 39.56  ? 170 THR A CG2  1 
ATOM   2651 H H    . THR A 1 167 ? 24.639 40.580 55.489 0.00 43.95  ? 170 THR A H    1 
ATOM   2652 H HA   . THR A 1 167 ? 25.420 40.020 53.052 0.00 37.21  ? 170 THR A HA   1 
ATOM   2653 H HB   . THR A 1 167 ? 23.050 39.014 54.224 0.00 45.39  ? 170 THR A HB   1 
ATOM   2654 H HG1  . THR A 1 167 ? 24.323 37.428 54.974 0.00 51.22  ? 170 THR A HG1  1 
ATOM   2655 H HG21 . THR A 1 167 ? 23.242 37.218 52.722 0.00 47.46  ? 170 THR A HG21 1 
ATOM   2656 H HG22 . THR A 1 167 ? 23.118 38.568 51.913 0.00 47.46  ? 170 THR A HG22 1 
ATOM   2657 H HG23 . THR A 1 167 ? 24.527 37.875 52.083 0.00 47.46  ? 170 THR A HG23 1 
ATOM   2658 N N    . PHE A 1 168 ? 22.747 41.783 53.216 1.00 35.58  ? 171 PHE A N    1 
ATOM   2659 C CA   . PHE A 1 168 ? 21.926 42.667 52.388 1.00 36.51  ? 171 PHE A CA   1 
ATOM   2660 C C    . PHE A 1 168 ? 22.798 43.714 51.669 1.00 33.60  ? 171 PHE A C    1 
ATOM   2661 O O    . PHE A 1 168 ? 22.679 43.905 50.452 1.00 34.54  ? 171 PHE A O    1 
ATOM   2662 C CB   . PHE A 1 168 ? 20.854 43.339 53.250 1.00 35.36  ? 171 PHE A CB   1 
ATOM   2663 C CG   . PHE A 1 168 ? 20.090 44.411 52.473 1.00 41.63  ? 171 PHE A CG   1 
ATOM   2664 C CD1  . PHE A 1 168 ? 19.151 44.057 51.523 1.00 36.70  ? 171 PHE A CD1  1 
ATOM   2665 C CD2  . PHE A 1 168 ? 20.375 45.752 52.666 1.00 45.27  ? 171 PHE A CD2  1 
ATOM   2666 C CE1  . PHE A 1 168 ? 18.492 45.046 50.807 1.00 45.20  ? 171 PHE A CE1  1 
ATOM   2667 C CE2  . PHE A 1 168 ? 19.716 46.718 51.952 1.00 42.31  ? 171 PHE A CE2  1 
ATOM   2668 C CZ   . PHE A 1 168 ? 18.794 46.368 51.030 1.00 40.89  ? 171 PHE A CZ   1 
ATOM   2669 H H    . PHE A 1 168 ? 22.564 41.785 54.056 0.00 42.68  ? 171 PHE A H    1 
ATOM   2670 H HA   . PHE A 1 168 ? 21.474 42.141 51.710 0.00 43.80  ? 171 PHE A HA   1 
ATOM   2671 H HB2  . PHE A 1 168 ? 20.219 42.669 53.549 0.00 42.41  ? 171 PHE A HB2  1 
ATOM   2672 H HB3  . PHE A 1 168 ? 21.277 43.760 54.014 0.00 42.41  ? 171 PHE A HB3  1 
ATOM   2673 H HD1  . PHE A 1 168 ? 18.963 43.160 51.363 0.00 44.02  ? 171 PHE A HD1  1 
ATOM   2674 H HD2  . PHE A 1 168 ? 21.022 45.999 53.286 0.00 54.31  ? 171 PHE A HD2  1 
ATOM   2675 H HE1  . PHE A 1 168 ? 17.847 44.814 50.177 0.00 54.22  ? 171 PHE A HE1  1 
ATOM   2676 H HE2  . PHE A 1 168 ? 19.903 47.616 52.103 0.00 50.75  ? 171 PHE A HE2  1 
ATOM   2677 H HZ   . PHE A 1 168 ? 18.359 47.029 50.540 0.00 49.05  ? 171 PHE A HZ   1 
ATOM   2678 N N    . LYS A 1 169 ? 23.706 44.384 52.405 1.00 36.65  ? 172 LYS A N    1 
ATOM   2679 C CA   . LYS A 1 169 ? 24.533 45.434 51.787 1.00 39.33  ? 172 LYS A CA   1 
ATOM   2680 C C    . LYS A 1 169 ? 25.267 44.916 50.546 1.00 40.92  ? 172 LYS A C    1 
ATOM   2681 O O    . LYS A 1 169 ? 25.300 45.575 49.494 1.00 38.90  ? 172 LYS A O    1 
ATOM   2682 C CB   . LYS A 1 169 ? 25.542 45.970 52.827 1.00 37.01  ? 172 LYS A CB   1 
ATOM   2683 H H    . LYS A 1 169 ? 23.857 44.252 53.242 0.00 43.97  ? 172 LYS A H    1 
ATOM   2684 H HA   . LYS A 1 169 ? 23.957 46.163 51.507 0.00 47.18  ? 172 LYS A HA   1 
ATOM   2685 N N    . VAL A 1 170 ? 25.857 43.724 50.655 1.00 37.48  ? 173 VAL A N    1 
ATOM   2686 C CA   . VAL A 1 170 ? 26.572 43.131 49.524 1.00 36.07  ? 173 VAL A CA   1 
ATOM   2687 C C    . VAL A 1 170 ? 25.622 42.810 48.382 1.00 34.82  ? 173 VAL A C    1 
ATOM   2688 O O    . VAL A 1 170 ? 25.929 43.100 47.215 1.00 32.04  ? 173 VAL A O    1 
ATOM   2689 C CB   . VAL A 1 170 ? 27.314 41.862 49.978 1.00 43.63  ? 173 VAL A CB   1 
ATOM   2690 C CG1  . VAL A 1 170 ? 27.957 41.188 48.767 1.00 39.33  ? 173 VAL A CG1  1 
ATOM   2691 C CG2  . VAL A 1 170 ? 28.328 42.225 51.046 1.00 45.09  ? 173 VAL A CG2  1 
ATOM   2692 H H    . VAL A 1 170 ? 25.859 43.242 51.367 0.00 44.96  ? 173 VAL A H    1 
ATOM   2693 H HA   . VAL A 1 170 ? 27.216 43.783 49.204 0.00 43.26  ? 173 VAL A HA   1 
ATOM   2694 H HB   . VAL A 1 170 ? 26.699 41.223 50.371 0.00 52.33  ? 173 VAL A HB   1 
ATOM   2695 H HG11 . VAL A 1 170 ? 28.643 40.576 49.074 0.00 47.17  ? 173 VAL A HG11 1 
ATOM   2696 H HG12 . VAL A 1 170 ? 27.275 40.703 48.277 0.00 47.17  ? 173 VAL A HG12 1 
ATOM   2697 H HG13 . VAL A 1 170 ? 28.351 41.869 48.199 0.00 47.17  ? 173 VAL A HG13 1 
ATOM   2698 H HG21 . VAL A 1 170 ? 28.792 41.421 51.327 0.00 54.09  ? 173 VAL A HG21 1 
ATOM   2699 H HG22 . VAL A 1 170 ? 28.961 42.860 50.677 0.00 54.09  ? 173 VAL A HG22 1 
ATOM   2700 H HG23 . VAL A 1 170 ? 27.864 42.620 51.800 0.00 54.09  ? 173 VAL A HG23 1 
ATOM   2701 N N    . LEU A 1 171 ? 24.485 42.154 48.675 1.00 31.73  ? 174 LEU A N    1 
ATOM   2702 C CA   . LEU A 1 171 ? 23.558 41.810 47.589 1.00 28.50  ? 174 LEU A CA   1 
ATOM   2703 C C    . LEU A 1 171 ? 22.943 43.046 46.940 1.00 30.44  ? 174 LEU A C    1 
ATOM   2704 O O    . LEU A 1 171 ? 22.703 43.055 45.733 1.00 31.02  ? 174 LEU A O    1 
ATOM   2705 C CB   . LEU A 1 171 ? 22.428 40.890 48.094 1.00 29.45  ? 174 LEU A CB   1 
ATOM   2706 C CG   . LEU A 1 171 ? 22.906 39.482 48.506 1.00 35.55  ? 174 LEU A CG   1 
ATOM   2707 C CD1  . LEU A 1 171 ? 21.774 38.728 49.129 1.00 38.00  ? 174 LEU A CD1  1 
ATOM   2708 C CD2  . LEU A 1 171 ? 23.399 38.665 47.285 1.00 33.10  ? 174 LEU A CD2  1 
ATOM   2709 H H    . LEU A 1 171 ? 24.239 41.908 49.461 0.00 38.06  ? 174 LEU A H    1 
ATOM   2710 H HA   . LEU A 1 171 ? 24.067 41.328 46.919 0.00 34.18  ? 174 LEU A HA   1 
ATOM   2711 H HB2  . LEU A 1 171 ? 22.016 41.301 48.870 0.00 35.32  ? 174 LEU A HB2  1 
ATOM   2712 H HB3  . LEU A 1 171 ? 21.773 40.785 47.387 0.00 35.32  ? 174 LEU A HB3  1 
ATOM   2713 H HG   . LEU A 1 171 ? 23.639 39.590 49.132 0.00 42.64  ? 174 LEU A HG   1 
ATOM   2714 H HD11 . LEU A 1 171 ? 22.091 37.853 49.404 0.00 45.58  ? 174 LEU A HD11 1 
ATOM   2715 H HD12 . LEU A 1 171 ? 21.453 39.221 49.900 0.00 45.58  ? 174 LEU A HD12 1 
ATOM   2716 H HD13 . LEU A 1 171 ? 21.062 38.632 48.477 0.00 45.58  ? 174 LEU A HD13 1 
ATOM   2717 H HD21 . LEU A 1 171 ? 23.598 37.759 47.571 0.00 39.70  ? 174 LEU A HD21 1 
ATOM   2718 H HD22 . LEU A 1 171 ? 22.703 38.653 46.610 0.00 39.70  ? 174 LEU A HD22 1 
ATOM   2719 H HD23 . LEU A 1 171 ? 24.199 39.082 46.928 0.00 39.70  ? 174 LEU A HD23 1 
ATOM   2720 N N    A ARG A 1 172 ? 22.694 44.084 47.742 0.71 31.44  ? 175 ARG A N    1 
ATOM   2721 N N    B ARG A 1 172 ? 22.706 44.097 47.724 0.29 31.50  ? 175 ARG A N    1 
ATOM   2722 C CA   A ARG A 1 172 ? 22.187 45.352 47.227 0.71 32.06  ? 175 ARG A CA   1 
ATOM   2723 C CA   B ARG A 1 172 ? 22.160 45.332 47.169 0.29 32.10  ? 175 ARG A CA   1 
ATOM   2724 C C    A ARG A 1 172 ? 23.162 45.938 46.215 0.71 30.09  ? 175 ARG A C    1 
ATOM   2725 C C    B ARG A 1 172 ? 23.156 45.997 46.225 0.29 30.38  ? 175 ARG A C    1 
ATOM   2726 O O    A ARG A 1 172 ? 22.775 46.386 45.120 0.71 32.29  ? 175 ARG A O    1 
ATOM   2727 O O    B ARG A 1 172 ? 22.769 46.544 45.182 0.29 32.22  ? 175 ARG A O    1 
ATOM   2728 C CB   A ARG A 1 172 ? 21.992 46.317 48.430 0.71 38.05  ? 175 ARG A CB   1 
ATOM   2729 C CB   B ARG A 1 172 ? 21.784 46.275 48.320 0.29 38.51  ? 175 ARG A CB   1 
ATOM   2730 C CG   A ARG A 1 172 ? 21.677 47.783 48.062 0.71 40.77  ? 175 ARG A CG   1 
ATOM   2731 C CG   B ARG A 1 172 ? 21.086 47.563 47.896 0.29 39.99  ? 175 ARG A CG   1 
ATOM   2732 C CD   A ARG A 1 172 ? 22.046 48.765 49.186 0.71 40.26  ? 175 ARG A CD   1 
ATOM   2733 C CD   B ARG A 1 172 ? 21.980 48.760 48.164 0.29 44.46  ? 175 ARG A CD   1 
ATOM   2734 N NE   A ARG A 1 172 ? 23.479 49.000 49.296 0.71 45.43  ? 175 ARG A NE   1 
ATOM   2735 N NE   B ARG A 1 172 ? 22.056 49.080 49.588 0.29 38.25  ? 175 ARG A NE   1 
ATOM   2736 C CZ   A ARG A 1 172 ? 24.019 49.705 50.284 0.71 51.46  ? 175 ARG A CZ   1 
ATOM   2737 C CZ   B ARG A 1 172 ? 23.181 49.113 50.292 0.29 51.20  ? 175 ARG A CZ   1 
ATOM   2738 N NH1  A ARG A 1 172 ? 23.266 50.293 51.198 0.71 52.18  ? 175 ARG A NH1  1 
ATOM   2739 N NH1  B ARG A 1 172 ? 24.347 48.789 49.754 0.29 46.87  ? 175 ARG A NH1  1 
ATOM   2740 N NH2  A ARG A 1 172 ? 25.340 49.831 50.349 0.71 50.50  ? 175 ARG A NH2  1 
ATOM   2741 N NH2  B ARG A 1 172 ? 23.134 49.470 51.570 0.29 50.23  ? 175 ARG A NH2  1 
ATOM   2742 H H    A ARG A 1 172 ? 22.811 44.078 48.593 0.71 37.71  ? 175 ARG A H    1 
ATOM   2743 H H    B ARG A 1 172 ? 22.850 44.121 48.571 0.29 37.78  ? 175 ARG A H    1 
ATOM   2744 H HA   A ARG A 1 172 ? 21.335 45.225 46.781 0.71 38.46  ? 175 ARG A HA   1 
ATOM   2745 H HA   B ARG A 1 172 ? 21.359 45.134 46.659 0.29 38.50  ? 175 ARG A HA   1 
ATOM   2746 H HB2  A ARG A 1 172 ? 21.255 45.989 48.968 0.71 45.64  ? 175 ARG A HB2  1 
ATOM   2747 H HB2  B ARG A 1 172 ? 21.184 45.804 48.919 0.29 46.19  ? 175 ARG A HB2  1 
ATOM   2748 H HB3  A ARG A 1 172 ? 22.809 46.320 48.954 0.71 45.64  ? 175 ARG A HB3  1 
ATOM   2749 H HB3  B ARG A 1 172 ? 22.595 46.525 48.789 0.29 46.19  ? 175 ARG A HB3  1 
ATOM   2750 H HG2  A ARG A 1 172 ? 22.183 48.027 47.271 0.71 48.91  ? 175 ARG A HG2  1 
ATOM   2751 H HG2  B ARG A 1 172 ? 20.889 47.530 46.947 0.29 47.97  ? 175 ARG A HG2  1 
ATOM   2752 H HG3  A ARG A 1 172 ? 20.727 47.869 47.887 0.71 48.91  ? 175 ARG A HG3  1 
ATOM   2753 H HG3  B ARG A 1 172 ? 20.266 47.670 48.402 0.29 47.97  ? 175 ARG A HG3  1 
ATOM   2754 H HD2  A ARG A 1 172 ? 21.617 49.617 49.013 0.71 48.30  ? 175 ARG A HD2  1 
ATOM   2755 H HD2  B ARG A 1 172 ? 22.876 48.566 47.849 0.29 53.33  ? 175 ARG A HD2  1 
ATOM   2756 H HD3  A ARG A 1 172 ? 21.738 48.404 50.032 0.71 48.30  ? 175 ARG A HD3  1 
ATOM   2757 H HD3  B ARG A 1 172 ? 21.625 49.534 47.698 0.29 53.33  ? 175 ARG A HD3  1 
ATOM   2758 H HE   A ARG A 1 172 ? 23.998 48.668 48.696 0.71 54.50  ? 175 ARG A HE   1 
ATOM   2759 H HE   B ARG A 1 172 ? 21.321 49.259 49.998 0.29 45.88  ? 175 ARG A HE   1 
ATOM   2760 H HH11 A ARG A 1 172 ? 22.409 50.223 51.160 0.71 62.60  ? 175 ARG A HH11 1 
ATOM   2761 H HH11 B ARG A 1 172 ? 24.389 48.551 48.929 0.29 56.22  ? 175 ARG A HH11 1 
ATOM   2762 H HH12 A ARG A 1 172 ? 23.632 50.746 51.831 0.71 62.60  ? 175 ARG A HH12 1 
ATOM   2763 H HH12 B ARG A 1 172 ? 25.063 48.818 50.231 0.29 56.22  ? 175 ARG A HH12 1 
ATOM   2764 H HH21 A ARG A 1 172 ? 25.837 49.458 49.755 0.71 60.58  ? 175 ARG A HH21 1 
ATOM   2765 H HH21 B ARG A 1 172 ? 23.856 49.495 52.037 0.29 60.25  ? 175 ARG A HH21 1 
ATOM   2766 H HH22 A ARG A 1 172 ? 25.698 50.286 50.985 0.71 60.58  ? 175 ARG A HH22 1 
ATOM   2767 H HH22 B ARG A 1 172 ? 22.381 49.676 51.932 0.29 60.25  ? 175 ARG A HH22 1 
ATOM   2768 N N    . ASN A 1 173 ? 24.446 45.987 46.584 1.00 35.34  ? 176 ASN A N    1 
ATOM   2769 C CA   . ASN A 1 173 ? 25.456 46.589 45.714 1.00 32.64  ? 176 ASN A CA   1 
ATOM   2770 C C    . ASN A 1 173 ? 25.639 45.790 44.427 1.00 35.60  ? 176 ASN A C    1 
ATOM   2771 O O    . ASN A 1 173 ? 25.848 46.386 43.355 1.00 35.83  ? 176 ASN A O    1 
ATOM   2772 C CB   . ASN A 1 173 ? 26.802 46.658 46.481 1.00 33.82  ? 176 ASN A CB   1 
ATOM   2773 C CG   . ASN A 1 173 ? 26.783 47.699 47.596 1.00 44.33  ? 176 ASN A CG   1 
ATOM   2774 O OD1  . ASN A 1 173 ? 25.819 48.445 47.731 1.00 49.34  ? 176 ASN A OD1  1 
ATOM   2775 N ND2  . ASN A 1 173 ? 27.819 47.709 48.445 1.00 49.55  ? 176 ASN A ND2  1 
ATOM   2776 H H    . ASN A 1 173 ? 24.752 45.681 47.328 0.00 42.39  ? 176 ASN A H    1 
ATOM   2777 H HA   . ASN A 1 173 ? 25.172 47.484 45.472 0.00 39.15  ? 176 ASN A HA   1 
ATOM   2778 H HB2  . ASN A 1 173 ? 26.985 45.792 46.879 0.00 40.56  ? 176 ASN A HB2  1 
ATOM   2779 H HB3  . ASN A 1 173 ? 27.509 46.894 45.860 0.00 40.56  ? 176 ASN A HB3  1 
ATOM   2780 H HD21 . ASN A 1 173 ? 27.844 48.281 49.087 0.00 59.44  ? 176 ASN A HD21 1 
ATOM   2781 H HD22 . ASN A 1 173 ? 28.460 47.143 48.348 0.00 59.44  ? 176 ASN A HD22 1 
ATOM   2782 N N    . VAL A 1 174 ? 25.650 44.444 44.525 1.00 29.44  ? 177 VAL A N    1 
ATOM   2783 C CA   . VAL A 1 174 ? 25.693 43.592 43.318 1.00 26.50  ? 177 VAL A CA   1 
ATOM   2784 C C    . VAL A 1 174 ? 24.529 43.914 42.405 1.00 31.92  ? 177 VAL A C    1 
ATOM   2785 O O    . VAL A 1 174 ? 24.703 44.062 41.190 1.00 30.23  ? 177 VAL A O    1 
ATOM   2786 C CB   . VAL A 1 174 ? 25.694 42.097 43.703 1.00 27.50  ? 177 VAL A CB   1 
ATOM   2787 C CG1  . VAL A 1 174 ? 25.398 41.210 42.472 1.00 35.42  ? 177 VAL A CG1  1 
ATOM   2788 C CG2  . VAL A 1 174 ? 27.050 41.810 44.346 1.00 32.35  ? 177 VAL A CG2  1 
ATOM   2789 H H    . VAL A 1 174 ? 25.634 44.008 45.266 0.00 35.30  ? 177 VAL A H    1 
ATOM   2790 H HA   . VAL A 1 174 ? 26.517 43.784 42.844 0.00 31.78  ? 177 VAL A HA   1 
ATOM   2791 H HB   . VAL A 1 174 ? 24.992 41.881 44.336 0.00 32.98  ? 177 VAL A HB   1 
ATOM   2792 H HG11 . VAL A 1 174 ? 25.678 40.301 42.662 0.00 42.48  ? 177 VAL A HG11 1 
ATOM   2793 H HG12 . VAL A 1 174 ? 24.445 41.231 42.289 0.00 42.48  ? 177 VAL A HG12 1 
ATOM   2794 H HG13 . VAL A 1 174 ? 25.888 41.554 41.709 0.00 42.48  ? 177 VAL A HG13 1 
ATOM   2795 H HG21 . VAL A 1 174 ? 27.081 40.879 44.616 0.00 38.80  ? 177 VAL A HG21 1 
ATOM   2796 H HG22 . VAL A 1 174 ? 27.751 41.990 43.700 0.00 38.80  ? 177 VAL A HG22 1 
ATOM   2797 H HG23 . VAL A 1 174 ? 27.160 42.383 45.121 0.00 38.80  ? 177 VAL A HG23 1 
ATOM   2798 N N    . THR A 1 175 ? 23.331 44.035 42.980 1.00 27.89  ? 178 THR A N    1 
ATOM   2799 C CA   . THR A 1 175 ? 22.116 44.224 42.191 1.00 30.73  ? 178 THR A CA   1 
ATOM   2800 C C    . THR A 1 175 ? 22.137 45.569 41.483 1.00 29.83  ? 178 THR A C    1 
ATOM   2801 O O    . THR A 1 175 ? 21.804 45.637 40.287 1.00 30.70  ? 178 THR A O    1 
ATOM   2802 C CB   . THR A 1 175 ? 20.872 44.072 43.099 1.00 30.40  ? 178 THR A CB   1 
ATOM   2803 O OG1  . THR A 1 175 ? 20.795 42.703 43.571 1.00 31.43  ? 178 THR A OG1  1 
ATOM   2804 C CG2  . THR A 1 175 ? 19.573 44.414 42.345 1.00 30.24  ? 178 THR A CG2  1 
ATOM   2805 H H    . THR A 1 175 ? 23.194 44.010 43.828 0.00 33.45  ? 178 THR A H    1 
ATOM   2806 H HA   . THR A 1 175 ? 22.059 43.537 41.509 0.00 36.85  ? 178 THR A HA   1 
ATOM   2807 H HB   . THR A 1 175 ? 20.950 44.686 43.846 0.00 36.46  ? 178 THR A HB   1 
ATOM   2808 H HG1  . THR A 1 175 ? 21.474 42.518 44.028 0.00 37.70  ? 178 THR A HG1  1 
ATOM   2809 H HG21 . THR A 1 175 ? 18.803 44.175 42.885 0.00 36.27  ? 178 THR A HG21 1 
ATOM   2810 H HG22 . THR A 1 175 ? 19.541 45.365 42.154 0.00 36.27  ? 178 THR A HG22 1 
ATOM   2811 H HG23 . THR A 1 175 ? 19.535 43.924 41.509 0.00 36.27  ? 178 THR A HG23 1 
ATOM   2812 N N    . VAL A 1 176 ? 22.560 46.639 42.171 1.00 30.05  ? 179 VAL A N    1 
ATOM   2813 C CA   . VAL A 1 176 ? 22.482 47.973 41.561 1.00 27.81  ? 179 VAL A CA   1 
ATOM   2814 C C    . VAL A 1 176 ? 23.435 48.089 40.388 1.00 29.74  ? 179 VAL A C    1 
ATOM   2815 O O    . VAL A 1 176 ? 23.099 48.664 39.332 1.00 32.47  ? 179 VAL A O    1 
ATOM   2816 C CB   . VAL A 1 176 ? 22.746 49.059 42.620 1.00 40.25  ? 179 VAL A CB   1 
ATOM   2817 C CG1  . VAL A 1 176 ? 22.974 50.411 41.924 1.00 49.27  ? 179 VAL A CG1  1 
ATOM   2818 C CG2  . VAL A 1 176 ? 21.590 49.102 43.604 1.00 39.35  ? 179 VAL A CG2  1 
ATOM   2819 H H    . VAL A 1 176 ? 22.887 46.620 42.967 0.00 36.04  ? 179 VAL A H    1 
ATOM   2820 H HA   . VAL A 1 176 ? 21.583 48.097 41.219 0.00 33.35  ? 179 VAL A HA   1 
ATOM   2821 H HB   . VAL A 1 176 ? 23.548 48.857 43.128 0.00 48.29  ? 179 VAL A HB   1 
ATOM   2822 H HG11 . VAL A 1 176 ? 22.859 51.124 42.572 0.00 59.10  ? 179 VAL A HG11 1 
ATOM   2823 H HG12 . VAL A 1 176 ? 23.875 50.433 41.564 0.00 59.10  ? 179 VAL A HG12 1 
ATOM   2824 H HG13 . VAL A 1 176 ? 22.329 50.510 41.206 0.00 59.10  ? 179 VAL A HG13 1 
ATOM   2825 H HG21 . VAL A 1 176 ? 21.941 49.233 44.498 0.00 47.20  ? 179 VAL A HG21 1 
ATOM   2826 H HG22 . VAL A 1 176 ? 21.002 49.837 43.368 0.00 47.20  ? 179 VAL A HG22 1 
ATOM   2827 H HG23 . VAL A 1 176 ? 21.105 48.263 43.558 0.00 47.20  ? 179 VAL A HG23 1 
ATOM   2828 N N    . VAL A 1 177 ? 24.659 47.555 40.548 1.00 31.13  ? 180 VAL A N    1 
ATOM   2829 C CA   . VAL A 1 177 ? 25.639 47.566 39.460 1.00 29.72  ? 180 VAL A CA   1 
ATOM   2830 C C    . VAL A 1 177 ? 25.195 46.734 38.275 1.00 30.55  ? 180 VAL A C    1 
ATOM   2831 O O    . VAL A 1 177 ? 25.256 47.188 37.116 1.00 30.07  ? 180 VAL A O    1 
ATOM   2832 C CB   . VAL A 1 177 ? 26.995 47.057 40.006 1.00 33.32  ? 180 VAL A CB   1 
ATOM   2833 C CG1  . VAL A 1 177 ? 27.999 46.889 38.811 1.00 40.82  ? 180 VAL A CG1  1 
ATOM   2834 C CG2  . VAL A 1 177 ? 27.515 48.042 40.991 1.00 39.91  ? 180 VAL A CG2  1 
ATOM   2835 H H    . VAL A 1 177 ? 24.940 47.184 41.272 0.00 37.34  ? 180 VAL A H    1 
ATOM   2836 H HA   . VAL A 1 177 ? 25.721 48.479 39.142 0.00 35.65  ? 180 VAL A HA   1 
ATOM   2837 H HB   . VAL A 1 177 ? 26.891 46.199 40.447 0.00 39.96  ? 180 VAL A HB   1 
ATOM   2838 H HG11 . VAL A 1 177 ? 28.902 46.844 39.161 0.00 48.97  ? 180 VAL A HG11 1 
ATOM   2839 H HG12 . VAL A 1 177 ? 27.788 46.070 38.334 0.00 48.97  ? 180 VAL A HG12 1 
ATOM   2840 H HG13 . VAL A 1 177 ? 27.912 47.650 38.216 0.00 48.97  ? 180 VAL A HG13 1 
ATOM   2841 H HG21 . VAL A 1 177 ? 28.390 47.752 41.296 0.00 47.87  ? 180 VAL A HG21 1 
ATOM   2842 H HG22 . VAL A 1 177 ? 27.585 48.910 40.564 0.00 47.87  ? 180 VAL A HG22 1 
ATOM   2843 H HG23 . VAL A 1 177 ? 26.903 48.091 41.742 0.00 47.87  ? 180 VAL A HG23 1 
ATOM   2844 N N    . LEU A 1 178 ? 24.811 45.470 38.509 1.00 24.13  ? 181 LEU A N    1 
ATOM   2845 C CA   . LEU A 1 178 ? 24.447 44.607 37.381 1.00 25.46  ? 181 LEU A CA   1 
ATOM   2846 C C    . LEU A 1 178 ? 23.138 45.073 36.700 1.00 27.61  ? 181 LEU A C    1 
ATOM   2847 O O    . LEU A 1 178 ? 23.052 45.059 35.457 1.00 25.07  ? 181 LEU A O    1 
ATOM   2848 C CB   . LEU A 1 178 ? 24.271 43.140 37.868 1.00 25.15  ? 181 LEU A CB   1 
ATOM   2849 C CG   . LEU A 1 178 ? 25.569 42.459 38.319 1.00 34.08  ? 181 LEU A CG   1 
ATOM   2850 C CD1  . LEU A 1 178 ? 25.240 41.044 38.863 1.00 32.51  ? 181 LEU A CD1  1 
ATOM   2851 C CD2  . LEU A 1 178 ? 26.597 42.379 37.234 1.00 31.55  ? 181 LEU A CD2  1 
ATOM   2852 H H    . LEU A 1 178 ? 24.756 45.102 39.284 0.00 28.93  ? 181 LEU A H    1 
ATOM   2853 H HA   . LEU A 1 178 ? 25.166 44.646 36.732 0.00 30.54  ? 181 LEU A HA   1 
ATOM   2854 H HB2  . LEU A 1 178 ? 23.661 43.136 38.622 0.00 30.17  ? 181 LEU A HB2  1 
ATOM   2855 H HB3  . LEU A 1 178 ? 23.902 42.616 37.140 0.00 30.17  ? 181 LEU A HB3  1 
ATOM   2856 H HG   . LEU A 1 178 ? 25.967 42.999 39.020 0.00 40.88  ? 181 LEU A HG   1 
ATOM   2857 H HD11 . LEU A 1 178 ? 26.057 40.629 39.179 0.00 39.00  ? 181 LEU A HD11 1 
ATOM   2858 H HD12 . LEU A 1 178 ? 24.607 41.126 39.593 0.00 39.00  ? 181 LEU A HD12 1 
ATOM   2859 H HD13 . LEU A 1 178 ? 24.854 40.513 38.149 0.00 39.00  ? 181 LEU A HD13 1 
ATOM   2860 H HD21 . LEU A 1 178 ? 27.318 41.799 37.525 0.00 37.84  ? 181 LEU A HD21 1 
ATOM   2861 H HD22 . LEU A 1 178 ? 26.184 42.018 36.434 0.00 37.84  ? 181 LEU A HD22 1 
ATOM   2862 H HD23 . LEU A 1 178 ? 26.939 43.269 37.057 0.00 37.84  ? 181 LEU A HD23 1 
ATOM   2863 N N    . TRP A 1 179 ? 22.092 45.435 37.481 1.00 22.68  ? 182 TRP A N    1 
ATOM   2864 C CA   . TRP A 1 179 ? 20.809 45.775 36.785 1.00 24.90  ? 182 TRP A CA   1 
ATOM   2865 C C    . TRP A 1 179 ? 20.967 47.043 35.939 1.00 26.89  ? 182 TRP A C    1 
ATOM   2866 O O    . TRP A 1 179 ? 20.394 47.150 34.831 1.00 25.16  ? 182 TRP A O    1 
ATOM   2867 C CB   . TRP A 1 179 ? 19.674 45.963 37.800 1.00 24.23  ? 182 TRP A CB   1 
ATOM   2868 C CG   . TRP A 1 179 ? 19.177 44.642 38.411 1.00 23.06  ? 182 TRP A CG   1 
ATOM   2869 C CD1  . TRP A 1 179 ? 19.921 43.534 38.726 1.00 24.55  ? 182 TRP A CD1  1 
ATOM   2870 C CD2  . TRP A 1 179 ? 17.796 44.341 38.800 1.00 24.02  ? 182 TRP A CD2  1 
ATOM   2871 N NE1  . TRP A 1 179 ? 19.051 42.529 39.301 1.00 26.00  ? 182 TRP A NE1  1 
ATOM   2872 C CE2  . TRP A 1 179 ? 17.778 43.043 39.341 1.00 24.07  ? 182 TRP A CE2  1 
ATOM   2873 C CE3  . TRP A 1 179 ? 16.606 45.071 38.710 1.00 26.98  ? 182 TRP A CE3  1 
ATOM   2874 C CZ2  . TRP A 1 179 ? 16.556 42.429 39.835 1.00 27.24  ? 182 TRP A CZ2  1 
ATOM   2875 C CZ3  . TRP A 1 179 ? 15.394 44.460 39.170 1.00 27.64  ? 182 TRP A CZ3  1 
ATOM   2876 C CH2  . TRP A 1 179 ? 15.404 43.175 39.725 1.00 22.27  ? 182 TRP A CH2  1 
ATOM   2877 H H    . TRP A 1 179 ? 22.092 45.489 38.340 0.00 27.20  ? 182 TRP A H    1 
ATOM   2878 H HA   . TRP A 1 179 ? 20.564 45.037 36.206 0.00 29.87  ? 182 TRP A HA   1 
ATOM   2879 H HB2  . TRP A 1 179 ? 19.990 46.525 38.524 0.00 29.05  ? 182 TRP A HB2  1 
ATOM   2880 H HB3  . TRP A 1 179 ? 18.922 46.386 37.355 0.00 29.05  ? 182 TRP A HB3  1 
ATOM   2881 H HD1  . TRP A 1 179 ? 20.837 43.443 38.592 0.00 29.44  ? 182 TRP A HD1  1 
ATOM   2882 H HE1  . TRP A 1 179 ? 19.289 41.747 39.569 0.00 31.19  ? 182 TRP A HE1  1 
ATOM   2883 H HE3  . TRP A 1 179 ? 16.601 45.933 38.360 0.00 32.36  ? 182 TRP A HE3  1 
ATOM   2884 H HZ2  . TRP A 1 179 ? 16.553 41.576 40.206 0.00 32.67  ? 182 TRP A HZ2  1 
ATOM   2885 H HZ3  . TRP A 1 179 ? 14.591 44.924 39.100 0.00 33.15  ? 182 TRP A HZ3  1 
ATOM   2886 H HH2  . TRP A 1 179 ? 14.603 42.812 40.030 0.00 26.70  ? 182 TRP A HH2  1 
ATOM   2887 N N    . SER A 1 180 ? 21.803 47.996 36.396 1.00 27.13  ? 183 SER A N    1 
ATOM   2888 C CA   . SER A 1 180 ? 21.947 49.254 35.639 1.00 24.59  ? 183 SER A CA   1 
ATOM   2889 C C    . SER A 1 180 ? 22.572 49.053 34.279 1.00 27.45  ? 183 SER A C    1 
ATOM   2890 O O    . SER A 1 180 ? 22.429 49.932 33.410 1.00 27.75  ? 183 SER A O    1 
ATOM   2891 C CB   . SER A 1 180 ? 22.832 50.246 36.397 1.00 28.20  ? 183 SER A CB   1 
ATOM   2892 O OG   . SER A 1 180 ? 22.184 50.615 37.602 1.00 33.98  ? 183 SER A OG   1 
ATOM   2893 H H    . SER A 1 180 ? 22.277 47.941 37.112 0.00 32.53  ? 183 SER A H    1 
ATOM   2894 H HA   . SER A 1 180 ? 21.056 49.623 35.536 0.00 29.49  ? 183 SER A HA   1 
ATOM   2895 H HB2  . SER A 1 180 ? 23.683 49.828 36.602 0.00 33.82  ? 183 SER A HB2  1 
ATOM   2896 H HB3  . SER A 1 180 ? 22.973 51.036 35.851 0.00 33.82  ? 183 SER A HB3  1 
ATOM   2897 H HG   . SER A 1 180 ? 22.712 51.046 38.092 0.00 40.75  ? 183 SER A HG   1 
ATOM   2898 N N    . ALA A 1 181 ? 23.319 47.955 34.084 1.00 24.98  ? 184 ALA A N    1 
ATOM   2899 C CA   . ALA A 1 181 ? 23.937 47.669 32.798 1.00 26.92  ? 184 ALA A CA   1 
ATOM   2900 C C    . ALA A 1 181 ? 22.930 47.241 31.734 1.00 24.72  ? 184 ALA A C    1 
ATOM   2901 O O    . ALA A 1 181 ? 23.144 47.517 30.563 1.00 26.13  ? 184 ALA A O    1 
ATOM   2902 C CB   . ALA A 1 181 ? 25.018 46.574 32.937 1.00 27.78  ? 184 ALA A CB   1 
ATOM   2903 H H    . ALA A 1 181 ? 23.479 47.362 34.686 0.00 29.96  ? 184 ALA A H    1 
ATOM   2904 H HA   . ALA A 1 181 ? 24.359 48.490 32.502 0.00 32.28  ? 184 ALA A HA   1 
ATOM   2905 H HB1  . ALA A 1 181 ? 25.411 46.406 32.067 0.00 33.31  ? 184 ALA A HB1  1 
ATOM   2906 H HB2  . ALA A 1 181 ? 25.700 46.880 33.555 0.00 33.31  ? 184 ALA A HB2  1 
ATOM   2907 H HB3  . ALA A 1 181 ? 24.605 45.764 33.275 0.00 33.31  ? 184 ALA A HB3  1 
ATOM   2908 N N    . TYR A 1 182 ? 21.818 46.617 32.118 1.00 21.59  ? 185 TYR A N    1 
ATOM   2909 C CA   . TYR A 1 182 ? 20.888 46.112 31.102 1.00 21.10  ? 185 TYR A CA   1 
ATOM   2910 C C    . TYR A 1 182 ? 20.343 47.226 30.198 1.00 21.91  ? 185 TYR A C    1 
ATOM   2911 O O    . TYR A 1 182 ? 20.293 46.999 28.984 1.00 24.20  ? 185 TYR A O    1 
ATOM   2912 C CB   . TYR A 1 182 ? 19.728 45.355 31.789 1.00 23.71  ? 185 TYR A CB   1 
ATOM   2913 C CG   . TYR A 1 182 ? 20.081 43.968 32.292 1.00 21.50  ? 185 TYR A CG   1 
ATOM   2914 C CD1  . TYR A 1 182 ? 20.766 43.771 33.501 1.00 22.53  ? 185 TYR A CD1  1 
ATOM   2915 C CD2  . TYR A 1 182 ? 19.704 42.822 31.555 1.00 21.66  ? 185 TYR A CD2  1 
ATOM   2916 C CE1  . TYR A 1 182 ? 21.110 42.500 33.911 1.00 25.17  ? 185 TYR A CE1  1 
ATOM   2917 C CE2  . TYR A 1 182 ? 20.019 41.548 31.987 1.00 21.84  ? 185 TYR A CE2  1 
ATOM   2918 C CZ   . TYR A 1 182 ? 20.686 41.385 33.184 1.00 21.59  ? 185 TYR A CZ   1 
ATOM   2919 O OH   . TYR A 1 182 ? 21.005 40.120 33.632 1.00 21.97  ? 185 TYR A OH   1 
ATOM   2920 H H    . TYR A 1 182 ? 21.583 46.475 32.932 0.00 25.89  ? 185 TYR A H    1 
ATOM   2921 H HA   . TYR A 1 182 ? 21.380 45.487 30.547 0.00 25.30  ? 185 TYR A HA   1 
ATOM   2922 H HB2  . TYR A 1 182 ? 19.430 45.875 32.553 0.00 28.44  ? 185 TYR A HB2  1 
ATOM   2923 H HB3  . TYR A 1 182 ? 19.003 45.258 31.152 0.00 28.44  ? 185 TYR A HB3  1 
ATOM   2924 H HD1  . TYR A 1 182 ? 20.990 44.503 34.030 0.00 27.02  ? 185 TYR A HD1  1 
ATOM   2925 H HD2  . TYR A 1 182 ? 19.233 42.928 30.761 0.00 25.98  ? 185 TYR A HD2  1 
ATOM   2926 H HE1  . TYR A 1 182 ? 21.627 42.385 34.676 0.00 30.18  ? 185 TYR A HE1  1 
ATOM   2927 H HE2  . TYR A 1 182 ? 19.783 40.808 31.476 0.00 26.19  ? 185 TYR A HE2  1 
ATOM   2928 H HH   . TYR A 1 182 ? 20.701 39.542 33.103 0.00 26.35  ? 185 TYR A HH   1 
ATOM   2929 N N    . PRO A 1 183 ? 19.843 48.357 30.707 1.00 22.90  ? 186 PRO A N    1 
ATOM   2930 C CA   . PRO A 1 183 ? 19.324 49.425 29.797 1.00 23.22  ? 186 PRO A CA   1 
ATOM   2931 C C    . PRO A 1 183 ? 20.383 49.972 28.893 1.00 26.55  ? 186 PRO A C    1 
ATOM   2932 O O    . PRO A 1 183 ? 20.068 50.411 27.788 1.00 24.49  ? 186 PRO A O    1 
ATOM   2933 C CB   . PRO A 1 183 ? 18.852 50.525 30.754 1.00 27.02  ? 186 PRO A CB   1 
ATOM   2934 C CG   . PRO A 1 183 ? 19.381 50.188 32.125 1.00 27.89  ? 186 PRO A CG   1 
ATOM   2935 C CD   . PRO A 1 183 ? 19.492 48.686 32.130 1.00 20.83  ? 186 PRO A CD   1 
ATOM   2936 H HA   . PRO A 1 183 ? 18.573 49.079 29.290 0.00 27.85  ? 186 PRO A HA   1 
ATOM   2937 H HB2  . PRO A 1 183 ? 19.202 51.379 30.457 0.00 32.40  ? 186 PRO A HB2  1 
ATOM   2938 H HB3  . PRO A 1 183 ? 17.882 50.548 30.762 0.00 32.40  ? 186 PRO A HB3  1 
ATOM   2939 H HG2  . PRO A 1 183 ? 20.248 50.602 32.258 0.00 33.45  ? 186 PRO A HG2  1 
ATOM   2940 H HG3  . PRO A 1 183 ? 18.760 50.493 32.805 0.00 33.45  ? 186 PRO A HG3  1 
ATOM   2941 H HD2  . PRO A 1 183 ? 20.194 48.395 32.734 0.00 24.97  ? 186 PRO A HD2  1 
ATOM   2942 H HD3  . PRO A 1 183 ? 18.649 48.279 32.380 0.00 24.97  ? 186 PRO A HD3  1 
ATOM   2943 N N    . VAL A 1 184 ? 21.657 49.967 29.324 1.00 24.35  ? 187 VAL A N    1 
ATOM   2944 C CA   . VAL A 1 184 ? 22.712 50.451 28.417 1.00 25.17  ? 187 VAL A CA   1 
ATOM   2945 C C    . VAL A 1 184 ? 22.926 49.465 27.260 1.00 27.23  ? 187 VAL A C    1 
ATOM   2946 O O    . VAL A 1 184 ? 23.084 49.875 26.100 1.00 26.04  ? 187 VAL A O    1 
ATOM   2947 C CB   . VAL A 1 184 ? 24.017 50.695 29.190 1.00 28.70  ? 187 VAL A CB   1 
ATOM   2948 C CG1  . VAL A 1 184 ? 25.133 51.208 28.246 1.00 30.80  ? 187 VAL A CG1  1 
ATOM   2949 C CG2  . VAL A 1 184 ? 23.801 51.670 30.376 1.00 28.12  ? 187 VAL A CG2  1 
ATOM   2950 H H    . VAL A 1 184 ? 21.924 49.702 30.097 0.00 29.20  ? 187 VAL A H    1 
ATOM   2951 H HA   . VAL A 1 184 ? 22.422 51.297 28.039 0.00 30.18  ? 187 VAL A HA   1 
ATOM   2952 H HB   . VAL A 1 184 ? 24.307 49.848 29.562 0.00 34.42  ? 187 VAL A HB   1 
ATOM   2953 H HG11 . VAL A 1 184 ? 25.871 51.540 28.781 0.00 36.95  ? 187 VAL A HG11 1 
ATOM   2954 H HG12 . VAL A 1 184 ? 25.435 50.475 27.686 0.00 36.95  ? 187 VAL A HG12 1 
ATOM   2955 H HG13 . VAL A 1 184 ? 24.777 51.921 27.694 0.00 36.95  ? 187 VAL A HG13 1 
ATOM   2956 H HG21 . VAL A 1 184 ? 24.641 51.787 30.846 0.00 33.72  ? 187 VAL A HG21 1 
ATOM   2957 H HG22 . VAL A 1 184 ? 23.493 52.523 30.031 0.00 33.72  ? 187 VAL A HG22 1 
ATOM   2958 H HG23 . VAL A 1 184 ? 23.136 51.296 30.975 0.00 33.72  ? 187 VAL A HG23 1 
ATOM   2959 N N    . VAL A 1 185 ? 23.003 48.164 27.557 1.00 24.04  ? 188 VAL A N    1 
ATOM   2960 C CA   . VAL A 1 185 ? 23.203 47.146 26.493 1.00 23.55  ? 188 VAL A CA   1 
ATOM   2961 C C    . VAL A 1 185 ? 22.073 47.208 25.484 1.00 25.57  ? 188 VAL A C    1 
ATOM   2962 O O    . VAL A 1 185 ? 22.284 47.101 24.270 1.00 27.66  ? 188 VAL A O    1 
ATOM   2963 C CB   . VAL A 1 185 ? 23.318 45.740 27.130 1.00 25.83  ? 188 VAL A CB   1 
ATOM   2964 C CG1  . VAL A 1 185 ? 23.364 44.615 26.025 1.00 28.99  ? 188 VAL A CG1  1 
ATOM   2965 C CG2  . VAL A 1 185 ? 24.613 45.638 27.975 1.00 27.31  ? 188 VAL A CG2  1 
ATOM   2966 H H    . VAL A 1 185 ? 22.946 47.838 28.351 0.00 28.83  ? 188 VAL A H    1 
ATOM   2967 H HA   . VAL A 1 185 ? 24.030 47.340 26.025 0.00 28.25  ? 188 VAL A HA   1 
ATOM   2968 H HB   . VAL A 1 185 ? 22.539 45.606 27.691 0.00 30.97  ? 188 VAL A HB   1 
ATOM   2969 H HG11 . VAL A 1 185 ? 23.641 43.781 26.435 0.00 34.77  ? 188 VAL A HG11 1 
ATOM   2970 H HG12 . VAL A 1 185 ? 22.480 44.516 25.638 0.00 34.77  ? 188 VAL A HG12 1 
ATOM   2971 H HG13 . VAL A 1 185 ? 23.999 44.873 25.338 0.00 34.77  ? 188 VAL A HG13 1 
ATOM   2972 H HG21 . VAL A 1 185 ? 24.671 44.748 28.356 0.00 32.75  ? 188 VAL A HG21 1 
ATOM   2973 H HG22 . VAL A 1 185 ? 25.378 45.803 27.402 0.00 32.75  ? 188 VAL A HG22 1 
ATOM   2974 H HG23 . VAL A 1 185 ? 24.581 46.300 28.683 0.00 32.75  ? 188 VAL A HG23 1 
ATOM   2975 N N    . TRP A 1 186 ? 20.851 47.409 25.978 1.00 22.95  ? 189 TRP A N    1 
ATOM   2976 C CA   . TRP A 1 186 ? 19.679 47.461 25.064 1.00 22.70  ? 189 TRP A CA   1 
ATOM   2977 C C    . TRP A 1 186 ? 19.766 48.684 24.148 1.00 24.33  ? 189 TRP A C    1 
ATOM   2978 O O    . TRP A 1 186 ? 19.510 48.597 22.939 1.00 27.28  ? 189 TRP A O    1 
ATOM   2979 C CB   . TRP A 1 186 ? 18.438 47.556 25.963 1.00 22.98  ? 189 TRP A CB   1 
ATOM   2980 C CG   . TRP A 1 186 ? 17.030 47.330 25.292 1.00 25.04  ? 189 TRP A CG   1 
ATOM   2981 C CD1  . TRP A 1 186 ? 16.288 46.193 25.400 1.00 29.83  ? 189 TRP A CD1  1 
ATOM   2982 C CD2  . TRP A 1 186 ? 16.215 48.282 24.535 1.00 22.08  ? 189 TRP A CD2  1 
ATOM   2983 N NE1  . TRP A 1 186 ? 15.048 46.367 24.757 1.00 24.95  ? 189 TRP A NE1  1 
ATOM   2984 C CE2  . TRP A 1 186 ? 14.962 47.621 24.255 1.00 26.43  ? 189 TRP A CE2  1 
ATOM   2985 C CE3  . TRP A 1 186 ? 16.388 49.582 24.081 1.00 23.65  ? 189 TRP A CE3  1 
ATOM   2986 C CZ2  . TRP A 1 186 ? 13.940 48.232 23.525 1.00 30.56  ? 189 TRP A CZ2  1 
ATOM   2987 C CZ3  . TRP A 1 186 ? 15.358 50.219 23.371 1.00 28.97  ? 189 TRP A CZ3  1 
ATOM   2988 C CH2  . TRP A 1 186 ? 14.149 49.516 23.082 1.00 30.76  ? 189 TRP A CH2  1 
ATOM   2989 H H    . TRP A 1 186 ? 20.665 47.517 26.811 0.00 27.53  ? 189 TRP A H    1 
ATOM   2990 H HA   . TRP A 1 186 ? 19.632 46.675 24.498 0.00 27.22  ? 189 TRP A HA   1 
ATOM   2991 H HB2  . TRP A 1 186 ? 18.525 46.888 26.660 0.00 27.55  ? 189 TRP A HB2  1 
ATOM   2992 H HB3  . TRP A 1 186 ? 18.422 48.444 26.353 0.00 27.55  ? 189 TRP A HB3  1 
ATOM   2993 H HD1  . TRP A 1 186 ? 16.561 45.417 25.833 0.00 35.77  ? 189 TRP A HD1  1 
ATOM   2994 H HE1  . TRP A 1 186 ? 14.436 45.766 24.693 0.00 29.93  ? 189 TRP A HE1  1 
ATOM   2995 H HE3  . TRP A 1 186 ? 17.185 50.031 24.247 0.00 28.36  ? 189 TRP A HE3  1 
ATOM   2996 H HZ2  . TRP A 1 186 ? 13.145 47.785 23.344 0.00 36.65  ? 189 TRP A HZ2  1 
ATOM   2997 H HZ3  . TRP A 1 186 ? 15.463 51.099 23.089 0.00 34.75  ? 189 TRP A HZ3  1 
ATOM   2998 H HH2  . TRP A 1 186 ? 13.487 49.937 22.582 0.00 36.90  ? 189 TRP A HH2  1 
ATOM   2999 N N    . LEU A 1 187 ? 20.181 49.821 24.701 1.00 24.82  ? 190 LEU A N    1 
ATOM   3000 C CA   . LEU A 1 187 ? 20.218 51.072 23.958 1.00 24.20  ? 190 LEU A CA   1 
ATOM   3001 C C    . LEU A 1 187 ? 21.267 51.005 22.858 1.00 31.49  ? 190 LEU A C    1 
ATOM   3002 O O    . LEU A 1 187 ? 20.997 51.468 21.741 1.00 31.48  ? 190 LEU A O    1 
ATOM   3003 C CB   . LEU A 1 187 ? 20.495 52.226 24.948 1.00 25.25  ? 190 LEU A CB   1 
ATOM   3004 C CG   . LEU A 1 187 ? 20.478 53.624 24.392 1.00 35.08  ? 190 LEU A CG   1 
ATOM   3005 C CD1  . LEU A 1 187 ? 19.025 53.967 23.941 1.00 41.11  ? 190 LEU A CD1  1 
ATOM   3006 C CD2  . LEU A 1 187 ? 20.992 54.606 25.491 1.00 36.92  ? 190 LEU A CD2  1 
ATOM   3007 H H    . LEU A 1 187 ? 20.451 49.894 25.514 0.00 29.77  ? 190 LEU A H    1 
ATOM   3008 H HA   . LEU A 1 187 ? 19.364 51.245 23.532 0.00 29.03  ? 190 LEU A HA   1 
ATOM   3009 H HB2  . LEU A 1 187 ? 19.821 52.191 25.644 0.00 30.28  ? 190 LEU A HB2  1 
ATOM   3010 H HB3  . LEU A 1 187 ? 21.375 52.085 25.331 0.00 30.28  ? 190 LEU A HB3  1 
ATOM   3011 H HG   . LEU A 1 187 ? 21.057 53.712 23.618 0.00 42.08  ? 190 LEU A HG   1 
ATOM   3012 H HD11 . LEU A 1 187 ? 19.001 54.884 23.626 0.00 49.32  ? 190 LEU A HD11 1 
ATOM   3013 H HD12 . LEU A 1 187 ? 18.766 53.364 23.226 0.00 49.32  ? 190 LEU A HD12 1 
ATOM   3014 H HD13 . LEU A 1 187 ? 18.427 53.860 24.697 0.00 49.32  ? 190 LEU A HD13 1 
ATOM   3015 H HD21 . LEU A 1 187 ? 20.934 55.514 25.156 0.00 44.28  ? 190 LEU A HD21 1 
ATOM   3016 H HD22 . LEU A 1 187 ? 20.440 54.510 26.283 0.00 44.28  ? 190 LEU A HD22 1 
ATOM   3017 H HD23 . LEU A 1 187 ? 21.913 54.389 25.702 0.00 44.28  ? 190 LEU A HD23 1 
ATOM   3018 N N    . ILE A 1 188 ? 22.454 50.370 23.118 1.00 27.86  ? 191 ILE A N    1 
ATOM   3019 C CA   . ILE A 1 188 ? 23.515 50.339 22.089 1.00 30.45  ? 191 ILE A CA   1 
ATOM   3020 C C    . ILE A 1 188 ? 23.454 49.111 21.193 1.00 29.92  ? 191 ILE A C    1 
ATOM   3021 O O    . ILE A 1 188 ? 24.154 49.077 20.163 1.00 33.71  ? 191 ILE A O    1 
ATOM   3022 C CB   . ILE A 1 188 ? 24.904 50.471 22.749 1.00 31.91  ? 191 ILE A CB   1 
ATOM   3023 C CG1  . ILE A 1 188 ? 25.235 49.218 23.557 1.00 39.04  ? 191 ILE A CG1  1 
ATOM   3024 C CG2  . ILE A 1 188 ? 24.898 51.719 23.603 1.00 44.65  ? 191 ILE A CG2  1 
ATOM   3025 C CD1  . ILE A 1 188 ? 26.480 49.381 24.446 1.00 54.24  ? 191 ILE A CD1  1 
ATOM   3026 H H    . ILE A 1 188 ? 22.649 49.971 23.854 0.00 33.41  ? 191 ILE A H    1 
ATOM   3027 H HA   . ILE A 1 188 ? 23.389 51.100 21.501 0.00 36.52  ? 191 ILE A HA   1 
ATOM   3028 H HB   . ILE A 1 188 ? 25.596 50.552 22.074 0.00 38.28  ? 191 ILE A HB   1 
ATOM   3029 H HG12 . ILE A 1 188 ? 24.483 49.008 24.133 0.00 46.83  ? 191 ILE A HG12 1 
ATOM   3030 H HG13 . ILE A 1 188 ? 25.399 48.483 22.945 0.00 46.83  ? 191 ILE A HG13 1 
ATOM   3031 H HG21 . ILE A 1 188 ? 25.813 51.965 23.809 0.00 53.56  ? 191 ILE A HG21 1 
ATOM   3032 H HG22 . ILE A 1 188 ? 24.466 52.435 23.112 0.00 53.56  ? 191 ILE A HG22 1 
ATOM   3033 H HG23 . ILE A 1 188 ? 24.411 51.539 24.422 0.00 53.56  ? 191 ILE A HG23 1 
ATOM   3034 H HD11 . ILE A 1 188 ? 26.763 48.507 24.757 0.00 65.07  ? 191 ILE A HD11 1 
ATOM   3035 H HD12 . ILE A 1 188 ? 27.187 49.792 23.925 0.00 65.07  ? 191 ILE A HD12 1 
ATOM   3036 H HD13 . ILE A 1 188 ? 26.256 49.945 25.202 0.00 65.07  ? 191 ILE A HD13 1 
ATOM   3037 N N    . GLY A 1 189 ? 22.591 48.137 21.509 1.00 28.89  ? 192 GLY A N    1 
ATOM   3038 C CA   . GLY A 1 189 ? 22.510 46.848 20.829 1.00 29.30  ? 192 GLY A CA   1 
ATOM   3039 C C    . GLY A 1 189 ? 21.450 46.851 19.737 1.00 31.31  ? 192 GLY A C    1 
ATOM   3040 O O    . GLY A 1 189 ? 20.966 47.904 19.297 1.00 31.66  ? 192 GLY A O    1 
ATOM   3041 H H    . GLY A 1 189 ? 22.017 48.208 22.145 0.00 34.65  ? 192 GLY A H    1 
ATOM   3042 H HA2  . GLY A 1 189 ? 23.367 46.641 20.426 0.00 35.14  ? 192 GLY A HA2  1 
ATOM   3043 H HA3  . GLY A 1 189 ? 22.287 46.157 21.472 0.00 35.14  ? 192 GLY A HA3  1 
ATOM   3044 N N    A SER A 1 190 ? 21.061 45.654 19.336 0.72 29.95  ? 193 SER A N    1 
ATOM   3045 N N    B SER A 1 190 ? 21.068 45.656 19.303 0.28 30.13  ? 193 SER A N    1 
ATOM   3046 C CA   A SER A 1 190 ? 20.214 45.490 18.153 0.72 32.08  ? 193 SER A CA   1 
ATOM   3047 C CA   B SER A 1 190 ? 20.204 45.543 18.127 0.28 32.10  ? 193 SER A CA   1 
ATOM   3048 C C    A SER A 1 190 ? 18.791 45.992 18.370 0.72 30.75  ? 193 SER A C    1 
ATOM   3049 C C    B SER A 1 190 ? 18.775 46.012 18.376 0.28 30.98  ? 193 SER A C    1 
ATOM   3050 O O    A SER A 1 190 ? 18.135 46.395 17.389 0.72 38.07  ? 193 SER A O    1 
ATOM   3051 O O    B SER A 1 190 ? 18.080 46.358 17.410 0.28 37.91  ? 193 SER A O    1 
ATOM   3052 C CB   A SER A 1 190 ? 20.188 44.007 17.738 0.72 32.63  ? 193 SER A CB   1 
ATOM   3053 C CB   B SER A 1 190 ? 20.182 44.098 17.622 0.28 32.92  ? 193 SER A CB   1 
ATOM   3054 O OG   A SER A 1 190 ? 19.711 43.178 18.762 0.72 40.64  ? 193 SER A OG   1 
ATOM   3055 O OG   B SER A 1 190 ? 21.396 43.799 16.966 0.28 33.10  ? 193 SER A OG   1 
ATOM   3056 H H    A SER A 1 190 ? 21.270 44.917 19.725 0.72 35.92  ? 193 SER A H    1 
ATOM   3057 H H    B SER A 1 190 ? 21.290 44.906 19.662 0.28 36.13  ? 193 SER A H    1 
ATOM   3058 H HA   A SER A 1 190 ? 20.594 46.008 17.425 0.72 38.47  ? 193 SER A HA   1 
ATOM   3059 H HA   B SER A 1 190 ? 20.579 46.108 17.434 0.28 38.50  ? 193 SER A HA   1 
ATOM   3060 H HB2  A SER A 1 190 ? 19.609 43.910 16.966 0.72 39.14  ? 193 SER A HB2  1 
ATOM   3061 H HB2  B SER A 1 190 ? 20.070 43.498 18.376 0.28 39.49  ? 193 SER A HB2  1 
ATOM   3062 H HB3  A SER A 1 190 ? 21.091 43.732 17.511 0.72 39.14  ? 193 SER A HB3  1 
ATOM   3063 H HB3  B SER A 1 190 ? 19.447 43.989 16.999 0.28 39.49  ? 193 SER A HB3  1 
ATOM   3064 H HG   A SER A 1 190 ? 20.162 43.296 19.461 0.72 48.75  ? 193 SER A HG   1 
ATOM   3065 H HG   B SER A 1 190 ? 21.544 44.366 16.365 0.28 39.70  ? 193 SER A HG   1 
ATOM   3066 N N    . GLU A 1 191 ? 18.325 46.056 19.634 1.00 29.72  ? 194 GLU A N    1 
ATOM   3067 C CA   . GLU A 1 191 ? 16.977 46.587 19.931 1.00 30.88  ? 194 GLU A CA   1 
ATOM   3068 C C    . GLU A 1 191 ? 16.936 48.082 19.859 1.00 34.83  ? 194 GLU A C    1 
ATOM   3069 O O    . GLU A 1 191 ? 15.844 48.669 19.698 1.00 31.23  ? 194 GLU A O    1 
ATOM   3070 C CB   . GLU A 1 191 ? 16.542 46.190 21.362 1.00 30.16  ? 194 GLU A CB   1 
ATOM   3071 C CG   . GLU A 1 191 ? 16.244 44.755 21.528 1.00 35.61  ? 194 GLU A CG   1 
ATOM   3072 C CD   . GLU A 1 191 ? 17.492 43.984 21.892 1.00 48.42  ? 194 GLU A CD   1 
ATOM   3073 O OE1  . GLU A 1 191 ? 18.589 44.604 21.998 1.00 37.01  ? 194 GLU A OE1  1 
ATOM   3074 O OE2  . GLU A 1 191 ? 17.374 42.780 22.069 1.00 42.73  ? 194 GLU A OE2  1 
ATOM   3075 H H    . GLU A 1 191 ? 18.764 45.801 20.328 0.00 35.65  ? 194 GLU A H    1 
ATOM   3076 H HA   . GLU A 1 191 ? 16.357 46.205 19.291 0.00 37.04  ? 194 GLU A HA   1 
ATOM   3077 H HB2  . GLU A 1 191 ? 17.257 46.415 21.977 0.00 36.17  ? 194 GLU A HB2  1 
ATOM   3078 H HB3  . GLU A 1 191 ? 15.740 46.685 21.590 0.00 36.17  ? 194 GLU A HB3  1 
ATOM   3079 H HG2  . GLU A 1 191 ? 15.593 44.640 22.239 0.00 42.71  ? 194 GLU A HG2  1 
ATOM   3080 H HG3  . GLU A 1 191 ? 15.893 44.399 20.697 0.00 42.71  ? 194 GLU A HG3  1 
ATOM   3081 N N    . GLY A 1 192 ? 18.101 48.727 20.022 1.00 29.94  ? 195 GLY A N    1 
ATOM   3082 C CA   . GLY A 1 192 ? 18.140 50.205 20.020 1.00 28.87  ? 195 GLY A CA   1 
ATOM   3083 C C    . GLY A 1 192 ? 18.862 50.804 18.841 1.00 35.10  ? 195 GLY A C    1 
ATOM   3084 O O    . GLY A 1 192 ? 18.420 50.714 17.696 1.00 34.83  ? 195 GLY A O    1 
ATOM   3085 H H    . GLY A 1 192 ? 18.864 48.345 20.134 0.00 35.91  ? 195 GLY A H    1 
ATOM   3086 H HA2  . GLY A 1 192 ? 17.231 50.542 20.016 0.00 34.62  ? 195 GLY A HA2  1 
ATOM   3087 H HA3  . GLY A 1 192 ? 18.586 50.507 20.827 0.00 34.62  ? 195 GLY A HA3  1 
ATOM   3088 N N    . ALA A 1 193 ? 19.995 51.473 19.114 1.00 30.42  ? 196 ALA A N    1 
ATOM   3089 C CA   . ALA A 1 193 ? 20.709 52.218 18.098 1.00 34.00  ? 196 ALA A CA   1 
ATOM   3090 C C    . ALA A 1 193 ? 21.560 51.337 17.173 1.00 36.48  ? 196 ALA A C    1 
ATOM   3091 O O    . ALA A 1 193 ? 21.995 51.826 16.124 1.00 41.23  ? 196 ALA A O    1 
ATOM   3092 C CB   . ALA A 1 193 ? 21.596 53.260 18.790 1.00 40.73  ? 196 ALA A CB   1 
ATOM   3093 H H    . ALA A 1 193 ? 20.364 51.503 19.890 0.00 36.48  ? 196 ALA A H    1 
ATOM   3094 H HA   . ALA A 1 193 ? 20.070 52.677 17.531 0.00 40.78  ? 196 ALA A HA   1 
ATOM   3095 H HB1  . ALA A 1 193 ? 22.084 53.758 18.114 0.00 48.86  ? 196 ALA A HB1  1 
ATOM   3096 H HB2  . ALA A 1 193 ? 21.035 53.862 19.303 0.00 48.86  ? 196 ALA A HB2  1 
ATOM   3097 H HB3  . ALA A 1 193 ? 22.219 52.805 19.378 0.00 48.86  ? 196 ALA A HB3  1 
ATOM   3098 N N    . GLY A 1 194 ? 21.784 50.071 17.514 1.00 35.72  ? 197 GLY A N    1 
ATOM   3099 C CA   . GLY A 1 194 ? 22.403 49.163 16.547 1.00 34.59  ? 197 GLY A CA   1 
ATOM   3100 C C    . GLY A 1 194 ? 23.906 49.319 16.402 1.00 39.76  ? 197 GLY A C    1 
ATOM   3101 O O    . GLY A 1 194 ? 24.449 48.984 15.351 1.00 41.51  ? 197 GLY A O    1 
ATOM   3102 H H    . GLY A 1 194 ? 21.593 49.720 18.276 0.00 42.84  ? 197 GLY A H    1 
ATOM   3103 H HA2  . GLY A 1 194 ? 22.225 48.249 16.819 0.00 41.49  ? 197 GLY A HA2  1 
ATOM   3104 H HA3  . GLY A 1 194 ? 22.004 49.317 15.676 0.00 41.49  ? 197 GLY A HA3  1 
ATOM   3105 N N    . ILE A 1 195 ? 24.587 49.791 17.443 1.00 30.88  ? 198 ILE A N    1 
ATOM   3106 C CA   . ILE A 1 195 ? 26.042 50.039 17.361 1.00 37.22  ? 198 ILE A CA   1 
ATOM   3107 C C    . ILE A 1 195 ? 26.841 48.761 17.644 1.00 40.92  ? 198 ILE A C    1 
ATOM   3108 O O    . ILE A 1 195 ? 27.923 48.549 17.089 1.00 42.08  ? 198 ILE A O    1 
ATOM   3109 C CB   . ILE A 1 195 ? 26.422 51.140 18.360 1.00 40.41  ? 198 ILE A CB   1 
ATOM   3110 C CG1  . ILE A 1 195 ? 25.686 52.446 18.006 1.00 54.22  ? 198 ILE A CG1  1 
ATOM   3111 C CG2  . ILE A 1 195 ? 27.932 51.363 18.315 1.00 55.93  ? 198 ILE A CG2  1 
ATOM   3112 C CD1  . ILE A 1 195 ? 25.697 53.435 19.132 1.00 59.42  ? 198 ILE A CD1  1 
ATOM   3113 H H    . ILE A 1 195 ? 24.241 49.978 18.208 0.00 37.03  ? 198 ILE A H    1 
ATOM   3114 H HA   . ILE A 1 195 ? 26.253 50.330 16.460 0.00 44.65  ? 198 ILE A HA   1 
ATOM   3115 H HB   . ILE A 1 195 ? 26.162 50.868 19.254 0.00 48.47  ? 198 ILE A HB   1 
ATOM   3116 H HG12 . ILE A 1 195 ? 26.118 52.855 17.240 0.00 65.05  ? 198 ILE A HG12 1 
ATOM   3117 H HG13 . ILE A 1 195 ? 24.761 52.240 17.795 0.00 65.05  ? 198 ILE A HG13 1 
ATOM   3118 H HG21 . ILE A 1 195 ? 28.151 52.152 18.835 0.00 67.10  ? 198 ILE A HG21 1 
ATOM   3119 H HG22 . ILE A 1 195 ? 28.377 50.586 18.689 0.00 67.10  ? 198 ILE A HG22 1 
ATOM   3120 H HG23 . ILE A 1 195 ? 28.205 51.489 17.393 0.00 67.10  ? 198 ILE A HG23 1 
ATOM   3121 H HD11 . ILE A 1 195 ? 25.141 54.193 18.892 0.00 71.29  ? 198 ILE A HD11 1 
ATOM   3122 H HD12 . ILE A 1 195 ? 25.349 53.009 19.931 0.00 71.29  ? 198 ILE A HD12 1 
ATOM   3123 H HD13 . ILE A 1 195 ? 26.609 53.729 19.285 0.00 71.29  ? 198 ILE A HD13 1 
ATOM   3124 N N    . VAL A 1 196 ? 26.380 47.957 18.586 1.00 31.19  ? 199 VAL A N    1 
ATOM   3125 C CA   . VAL A 1 196 ? 26.994 46.668 18.931 1.00 35.34  ? 199 VAL A CA   1 
ATOM   3126 C C    . VAL A 1 196 ? 26.233 45.554 18.213 1.00 37.65  ? 199 VAL A C    1 
ATOM   3127 O O    . VAL A 1 196 ? 25.000 45.516 18.301 1.00 35.48  ? 199 VAL A O    1 
ATOM   3128 C CB   . VAL A 1 196 ? 26.943 46.463 20.463 1.00 44.77  ? 199 VAL A CB   1 
ATOM   3129 C CG1  . VAL A 1 196 ? 27.501 45.109 20.916 1.00 42.69  ? 199 VAL A CG1  1 
ATOM   3130 C CG2  . VAL A 1 196 ? 27.776 47.611 21.156 1.00 43.48  ? 199 VAL A CG2  1 
ATOM   3131 H H    . VAL A 1 196 ? 25.686 48.136 19.063 0.00 37.41  ? 199 VAL A H    1 
ATOM   3132 H HA   . VAL A 1 196 ? 27.913 46.639 18.625 0.00 42.39  ? 199 VAL A HA   1 
ATOM   3133 H HB   . VAL A 1 196 ? 26.010 46.486 20.727 0.00 53.70  ? 199 VAL A HB   1 
ATOM   3134 H HG11 . VAL A 1 196 ? 27.441 45.051 21.883 0.00 51.21  ? 199 VAL A HG11 1 
ATOM   3135 H HG12 . VAL A 1 196 ? 26.979 44.400 20.509 0.00 51.21  ? 199 VAL A HG12 1 
ATOM   3136 H HG13 . VAL A 1 196 ? 28.427 45.040 20.638 0.00 51.21  ? 199 VAL A HG13 1 
ATOM   3137 H HG21 . VAL A 1 196 ? 27.755 47.479 22.117 0.00 52.16  ? 199 VAL A HG21 1 
ATOM   3138 H HG22 . VAL A 1 196 ? 28.691 47.574 20.837 0.00 52.16  ? 199 VAL A HG22 1 
ATOM   3139 H HG23 . VAL A 1 196 ? 27.381 48.468 20.931 0.00 52.16  ? 199 VAL A HG23 1 
ATOM   3140 N N    . PRO A 1 197 ? 26.911 44.613 17.545 1.00 30.37  ? 200 PRO A N    1 
ATOM   3141 C CA   . PRO A 1 197 ? 26.185 43.546 16.821 1.00 33.66  ? 200 PRO A CA   1 
ATOM   3142 C C    . PRO A 1 197 ? 25.520 42.523 17.754 1.00 28.86  ? 200 PRO A C    1 
ATOM   3143 O O    . PRO A 1 197 ? 25.932 42.313 18.889 1.00 30.57  ? 200 PRO A O    1 
ATOM   3144 C CB   . PRO A 1 197 ? 27.275 42.868 15.990 1.00 38.29  ? 200 PRO A CB   1 
ATOM   3145 C CG   . PRO A 1 197 ? 28.519 43.292 16.521 1.00 45.41  ? 200 PRO A CG   1 
ATOM   3146 C CD   . PRO A 1 197 ? 28.366 44.556 17.309 1.00 37.50  ? 200 PRO A CD   1 
ATOM   3147 H HA   . PRO A 1 197 ? 25.510 43.947 16.251 0.00 40.38  ? 200 PRO A HA   1 
ATOM   3148 H HB2  . PRO A 1 197 ? 27.184 41.905 16.062 0.00 45.93  ? 200 PRO A HB2  1 
ATOM   3149 H HB3  . PRO A 1 197 ? 27.190 43.141 15.063 0.00 45.93  ? 200 PRO A HB3  1 
ATOM   3150 H HG2  . PRO A 1 197 ? 28.859 42.590 17.098 0.00 54.48  ? 200 PRO A HG2  1 
ATOM   3151 H HG3  . PRO A 1 197 ? 29.131 43.441 15.784 0.00 54.48  ? 200 PRO A HG3  1 
ATOM   3152 H HD2  . PRO A 1 197 ? 28.853 44.505 18.146 0.00 44.98  ? 200 PRO A HD2  1 
ATOM   3153 H HD3  . PRO A 1 197 ? 28.666 45.323 16.796 0.00 44.98  ? 200 PRO A HD3  1 
ATOM   3154 N N    . LEU A 1 198 ? 24.545 41.795 17.189 1.00 31.79  ? 201 LEU A N    1 
ATOM   3155 C CA   . LEU A 1 198 ? 23.731 40.876 18.016 1.00 28.07  ? 201 LEU A CA   1 
ATOM   3156 C C    . LEU A 1 198 ? 24.586 39.804 18.699 1.00 30.65  ? 201 LEU A C    1 
ATOM   3157 O O    . LEU A 1 198 ? 24.315 39.434 19.843 1.00 33.44  ? 201 LEU A O    1 
ATOM   3158 C CB   . LEU A 1 198 ? 22.636 40.238 17.144 1.00 28.05  ? 201 LEU A CB   1 
ATOM   3159 C CG   . LEU A 1 198 ? 21.649 39.239 17.813 1.00 27.80  ? 201 LEU A CG   1 
ATOM   3160 C CD1  . LEU A 1 198 ? 20.924 39.825 19.076 1.00 34.06  ? 201 LEU A CD1  1 
ATOM   3161 C CD2  . LEU A 1 198 ? 20.612 38.747 16.781 1.00 36.24  ? 201 LEU A CD2  1 
ATOM   3162 H H    . LEU A 1 198 ? 24.336 41.811 16.355 0.00 38.13  ? 201 LEU A H    1 
ATOM   3163 H HA   . LEU A 1 198 ? 23.304 41.386 18.722 0.00 33.67  ? 201 LEU A HA   1 
ATOM   3164 H HB2  . LEU A 1 198 ? 22.097 40.957 16.778 0.00 33.64  ? 201 LEU A HB2  1 
ATOM   3165 H HB3  . LEU A 1 198 ? 23.076 39.755 16.427 0.00 33.64  ? 201 LEU A HB3  1 
ATOM   3166 H HG   . LEU A 1 198 ? 22.174 38.488 18.132 0.00 33.34  ? 201 LEU A HG   1 
ATOM   3167 H HD11 . LEU A 1 198 ? 20.339 39.147 19.448 0.00 40.86  ? 201 LEU A HD11 1 
ATOM   3168 H HD12 . LEU A 1 198 ? 21.591 40.083 19.732 0.00 40.86  ? 201 LEU A HD12 1 
ATOM   3169 H HD13 . LEU A 1 198 ? 20.405 40.600 18.811 0.00 40.86  ? 201 LEU A HD13 1 
ATOM   3170 H HD21 . LEU A 1 198 ? 20.126 37.995 17.155 0.00 43.47  ? 201 LEU A HD21 1 
ATOM   3171 H HD22 . LEU A 1 198 ? 19.998 39.470 16.580 0.00 43.47  ? 201 LEU A HD22 1 
ATOM   3172 H HD23 . LEU A 1 198 ? 21.075 38.473 15.974 0.00 43.47  ? 201 LEU A HD23 1 
ATOM   3173 N N    A ASN A 1 199 ? 25.640 39.287 18.034 0.74 30.84  ? 202 ASN A N    1 
ATOM   3174 N N    B ASN A 1 199 ? 25.616 39.292 18.012 0.26 30.88  ? 202 ASN A N    1 
ATOM   3175 C CA   A ASN A 1 199 ? 26.429 38.242 18.688 0.74 28.27  ? 202 ASN A CA   1 
ATOM   3176 C CA   B ASN A 1 199 ? 26.486 38.286 18.618 0.26 28.48  ? 202 ASN A CA   1 
ATOM   3177 C C    A ASN A 1 199 ? 27.164 38.748 19.929 0.74 33.76  ? 202 ASN A C    1 
ATOM   3178 C C    B ASN A 1 199 ? 27.100 38.784 19.922 0.26 33.60  ? 202 ASN A C    1 
ATOM   3179 O O    A ASN A 1 199 ? 27.235 38.040 20.953 0.74 33.34  ? 202 ASN A O    1 
ATOM   3180 O O    B ASN A 1 199 ? 27.036 38.104 20.957 0.26 33.07  ? 202 ASN A O    1 
ATOM   3181 C CB   A ASN A 1 199 ? 27.383 37.579 17.678 0.74 33.99  ? 202 ASN A CB   1 
ATOM   3182 C CB   B ASN A 1 199 ? 27.576 37.880 17.623 0.26 34.86  ? 202 ASN A CB   1 
ATOM   3183 C CG   A ASN A 1 199 ? 28.483 38.500 17.217 0.74 34.82  ? 202 ASN A CG   1 
ATOM   3184 C CG   B ASN A 1 199 ? 28.419 36.722 18.121 0.26 28.07  ? 202 ASN A CG   1 
ATOM   3185 O OD1  A ASN A 1 199 ? 28.227 39.552 16.647 0.74 44.05  ? 202 ASN A OD1  1 
ATOM   3186 O OD1  B ASN A 1 199 ? 28.173 36.169 19.180 0.26 34.90  ? 202 ASN A OD1  1 
ATOM   3187 N ND2  A ASN A 1 199 ? 29.732 38.101 17.473 0.74 51.20  ? 202 ASN A ND2  1 
ATOM   3188 N ND2  B ASN A 1 199 ? 29.443 36.366 17.352 0.26 51.59  ? 202 ASN A ND2  1 
ATOM   3189 H H    A ASN A 1 199 ? 25.899 39.516 17.247 0.74 36.99  ? 202 ASN A H    1 
ATOM   3190 H H    B ASN A 1 199 ? 25.826 39.508 17.207 0.26 37.04  ? 202 ASN A H    1 
ATOM   3191 H HA   A ASN A 1 199 ? 25.820 37.555 18.999 0.74 33.90  ? 202 ASN A HA   1 
ATOM   3192 H HA   B ASN A 1 199 ? 25.955 37.502 18.828 0.26 34.16  ? 202 ASN A HA   1 
ATOM   3193 H HB2  A ASN A 1 199 ? 27.796 36.806 18.095 0.74 40.77  ? 202 ASN A HB2  1 
ATOM   3194 H HB2  B ASN A 1 199 ? 27.158 37.611 16.790 0.26 41.82  ? 202 ASN A HB2  1 
ATOM   3195 H HB3  A ASN A 1 199 ? 26.876 37.304 16.898 0.74 40.77  ? 202 ASN A HB3  1 
ATOM   3196 H HB3  B ASN A 1 199 ? 28.164 38.636 17.471 0.26 41.82  ? 202 ASN A HB3  1 
ATOM   3197 H HD21 A ASN A 1 199 ? 29.871 37.356 17.879 0.74 61.43  ? 202 ASN A HD21 1 
ATOM   3198 H HD21 B ASN A 1 199 ? 29.596 36.787 16.617 0.26 61.89  ? 202 ASN A HD21 1 
ATOM   3199 H HD22 A ASN A 1 199 ? 30.398 38.589 17.231 0.74 61.43  ? 202 ASN A HD22 1 
ATOM   3200 H HD22 B ASN A 1 199 ? 29.953 35.716 17.589 0.26 61.89  ? 202 ASN A HD22 1 
ATOM   3201 N N    . ILE A 1 200 ? 27.710 39.972 19.892 1.00 30.11  ? 203 ILE A N    1 
ATOM   3202 C CA   . ILE A 1 200 ? 28.326 40.521 21.092 1.00 26.24  ? 203 ILE A CA   1 
ATOM   3203 C C    . ILE A 1 200 ? 27.253 40.906 22.136 1.00 26.18  ? 203 ILE A C    1 
ATOM   3204 O O    . ILE A 1 200 ? 27.435 40.712 23.335 1.00 29.59  ? 203 ILE A O    1 
ATOM   3205 C CB   . ILE A 1 200 ? 29.193 41.736 20.683 1.00 34.39  ? 203 ILE A CB   1 
ATOM   3206 C CG1  . ILE A 1 200 ? 30.298 41.261 19.702 1.00 36.24  ? 203 ILE A CG1  1 
ATOM   3207 C CG2  . ILE A 1 200 ? 29.762 42.428 21.927 1.00 37.49  ? 203 ILE A CG2  1 
ATOM   3208 C CD1  . ILE A 1 200 ? 31.248 40.165 20.239 1.00 39.38  ? 203 ILE A CD1  1 
ATOM   3209 H H    . ILE A 1 200 ? 27.731 40.483 19.201 0.00 36.12  ? 203 ILE A H    1 
ATOM   3210 H HA   . ILE A 1 200 ? 28.890 39.849 21.504 0.00 31.47  ? 203 ILE A HA   1 
ATOM   3211 H HB   . ILE A 1 200 ? 28.651 42.396 20.224 0.00 41.25  ? 203 ILE A HB   1 
ATOM   3212 H HG12 . ILE A 1 200 ? 29.868 40.905 18.909 0.00 43.47  ? 203 ILE A HG12 1 
ATOM   3213 H HG13 . ILE A 1 200 ? 30.846 42.026 19.467 0.00 43.47  ? 203 ILE A HG13 1 
ATOM   3214 H HG21 . ILE A 1 200 ? 30.428 43.077 21.651 0.00 44.96  ? 203 ILE A HG21 1 
ATOM   3215 H HG22 . ILE A 1 200 ? 29.040 42.874 22.397 0.00 44.96  ? 203 ILE A HG22 1 
ATOM   3216 H HG23 . ILE A 1 200 ? 30.168 41.761 22.501 0.00 44.96  ? 203 ILE A HG23 1 
ATOM   3217 H HD11 . ILE A 1 200 ? 31.955 40.015 19.593 0.00 47.24  ? 203 ILE A HD11 1 
ATOM   3218 H HD12 . ILE A 1 200 ? 31.627 40.461 21.081 0.00 47.24  ? 203 ILE A HD12 1 
ATOM   3219 H HD13 . ILE A 1 200 ? 30.743 39.347 20.373 0.00 47.24  ? 203 ILE A HD13 1 
ATOM   3220 N N    . GLU A 1 201 ? 26.169 41.522 21.709 1.00 28.00  ? 204 GLU A N    1 
ATOM   3221 C CA   . GLU A 1 201 ? 25.062 41.782 22.643 1.00 27.65  ? 204 GLU A CA   1 
ATOM   3222 C C    . GLU A 1 201 ? 24.628 40.510 23.406 1.00 28.18  ? 204 GLU A C    1 
ATOM   3223 O O    . GLU A 1 201 ? 24.330 40.559 24.616 1.00 26.36  ? 204 GLU A O    1 
ATOM   3224 C CB   . GLU A 1 201 ? 23.867 42.317 21.844 1.00 30.71  ? 204 GLU A CB   1 
ATOM   3225 C CG   . GLU A 1 201 ? 22.645 42.648 22.774 1.00 35.69  ? 204 GLU A CG   1 
ATOM   3226 C CD   . GLU A 1 201 ? 21.379 43.038 22.024 1.00 40.72  ? 204 GLU A CD   1 
ATOM   3227 O OE1  . GLU A 1 201 ? 21.465 43.387 20.851 1.00 31.83  ? 204 GLU A OE1  1 
ATOM   3228 O OE2  . GLU A 1 201 ? 20.277 43.000 22.609 1.00 47.04  ? 204 GLU A OE2  1 
ATOM   3229 H H    . GLU A 1 201 ? 26.041 41.799 20.905 0.00 33.58  ? 204 GLU A H    1 
ATOM   3230 H HA   . GLU A 1 201 ? 25.353 42.436 23.297 0.00 33.16  ? 204 GLU A HA   1 
ATOM   3231 H HB2  . GLU A 1 201 ? 24.128 43.130 21.384 0.00 36.84  ? 204 GLU A HB2  1 
ATOM   3232 H HB3  . GLU A 1 201 ? 23.587 41.648 21.200 0.00 36.84  ? 204 GLU A HB3  1 
ATOM   3233 H HG2  . GLU A 1 201 ? 22.440 41.864 23.308 0.00 42.81  ? 204 GLU A HG2  1 
ATOM   3234 H HG3  . GLU A 1 201 ? 22.885 43.389 23.351 0.00 42.81  ? 204 GLU A HG3  1 
ATOM   3235 N N    . THR A 1 202 ? 24.495 39.387 22.685 1.00 22.36  ? 205 THR A N    1 
ATOM   3236 C CA   . THR A 1 202 ? 24.059 38.135 23.339 1.00 25.86  ? 205 THR A CA   1 
ATOM   3237 C C    . THR A 1 202 ? 25.108 37.664 24.359 1.00 26.34  ? 205 THR A C    1 
ATOM   3238 O O    . THR A 1 202 ? 24.756 37.193 25.458 1.00 24.79  ? 205 THR A O    1 
ATOM   3239 C CB   . THR A 1 202 ? 23.826 37.071 22.237 1.00 28.74  ? 205 THR A CB   1 
ATOM   3240 O OG1  . THR A 1 202 ? 22.836 37.532 21.325 1.00 26.31  ? 205 THR A OG1  1 
ATOM   3241 C CG2  . THR A 1 202 ? 23.341 35.679 22.779 1.00 23.34  ? 205 THR A CG2  1 
ATOM   3242 H H    . THR A 1 202 ? 24.646 39.320 21.841 0.00 26.81  ? 205 THR A H    1 
ATOM   3243 H HA   . THR A 1 202 ? 23.228 38.269 23.821 0.00 31.02  ? 205 THR A HA   1 
ATOM   3244 H HB   . THR A 1 202 ? 24.685 36.934 21.808 0.00 34.47  ? 205 THR A HB   1 
ATOM   3245 H HG1  . THR A 1 202 ? 23.103 38.228 20.938 0.00 31.55  ? 205 THR A HG1  1 
ATOM   3246 H HG21 . THR A 1 202 ? 23.209 35.063 22.041 0.00 27.99  ? 205 THR A HG21 1 
ATOM   3247 H HG22 . THR A 1 202 ? 24.003 35.309 23.384 0.00 27.99  ? 205 THR A HG22 1 
ATOM   3248 H HG23 . THR A 1 202 ? 22.502 35.783 23.256 0.00 27.99  ? 205 THR A HG23 1 
ATOM   3249 N N    . LEU A 1 203 ? 26.413 37.763 24.012 1.00 26.11  ? 206 LEU A N    1 
ATOM   3250 C CA   . LEU A 1 203 ? 27.464 37.526 25.019 1.00 25.70  ? 206 LEU A CA   1 
ATOM   3251 C C    . LEU A 1 203 ? 27.291 38.411 26.257 1.00 25.01  ? 206 LEU A C    1 
ATOM   3252 O O    . LEU A 1 203 ? 27.392 37.937 27.393 1.00 25.91  ? 206 LEU A O    1 
ATOM   3253 C CB   . LEU A 1 203 ? 28.845 37.788 24.363 1.00 26.49  ? 206 LEU A CB   1 
ATOM   3254 C CG   . LEU A 1 203 ? 30.048 37.859 25.273 1.00 31.07  ? 206 LEU A CG   1 
ATOM   3255 C CD1  . LEU A 1 203 ? 30.176 36.573 26.132 1.00 33.89  ? 206 LEU A CD1  1 
ATOM   3256 C CD2  . LEU A 1 203 ? 31.304 38.040 24.376 1.00 33.37  ? 206 LEU A CD2  1 
ATOM   3257 H H    . LEU A 1 203 ? 26.703 37.960 23.226 0.00 31.32  ? 206 LEU A H    1 
ATOM   3258 H HA   . LEU A 1 203 ? 27.412 36.603 25.315 0.00 30.82  ? 206 LEU A HA   1 
ATOM   3259 H HB2  . LEU A 1 203 ? 29.014 37.073 23.730 0.00 31.77  ? 206 LEU A HB2  1 
ATOM   3260 H HB3  . LEU A 1 203 ? 28.795 38.638 23.898 0.00 31.77  ? 206 LEU A HB3  1 
ATOM   3261 H HG   . LEU A 1 203 ? 29.964 38.601 25.892 0.00 37.26  ? 206 LEU A HG   1 
ATOM   3262 H HD11 . LEU A 1 203 ? 30.988 36.626 26.660 0.00 40.64  ? 206 LEU A HD11 1 
ATOM   3263 H HD12 . LEU A 1 203 ? 29.405 36.505 26.716 0.00 40.64  ? 206 LEU A HD12 1 
ATOM   3264 H HD13 . LEU A 1 203 ? 30.214 35.803 25.543 0.00 40.64  ? 206 LEU A HD13 1 
ATOM   3265 H HD21 . LEU A 1 203 ? 32.094 38.056 24.939 0.00 40.03  ? 206 LEU A HD21 1 
ATOM   3266 H HD22 . LEU A 1 203 ? 31.356 37.299 23.752 0.00 40.03  ? 206 LEU A HD22 1 
ATOM   3267 H HD23 . LEU A 1 203 ? 31.227 38.877 23.891 0.00 40.03  ? 206 LEU A HD23 1 
ATOM   3268 N N    . LEU A 1 204 ? 27.046 39.713 26.068 1.00 25.28  ? 207 LEU A N    1 
ATOM   3269 C CA   . LEU A 1 204 ? 26.977 40.585 27.240 1.00 25.13  ? 207 LEU A CA   1 
ATOM   3270 C C    . LEU A 1 204 ? 25.785 40.221 28.136 1.00 24.96  ? 207 LEU A C    1 
ATOM   3271 O O    . LEU A 1 204 ? 25.910 40.224 29.367 1.00 26.99  ? 207 LEU A O    1 
ATOM   3272 C CB   . LEU A 1 204 ? 26.867 42.049 26.802 1.00 23.99  ? 207 LEU A CB   1 
ATOM   3273 C CG   . LEU A 1 204 ? 28.093 42.604 26.019 1.00 27.66  ? 207 LEU A CG   1 
ATOM   3274 C CD1  . LEU A 1 204 ? 27.772 44.013 25.591 1.00 30.19  ? 207 LEU A CD1  1 
ATOM   3275 C CD2  . LEU A 1 204 ? 29.317 42.615 26.932 1.00 35.89  ? 207 LEU A CD2  1 
ATOM   3276 H H    . LEU A 1 204 ? 26.922 40.096 25.308 0.00 30.31  ? 207 LEU A H    1 
ATOM   3277 H HA   . LEU A 1 204 ? 27.794 40.476 27.751 0.00 30.13  ? 207 LEU A HA   1 
ATOM   3278 H HB2  . LEU A 1 204 ? 26.091 42.138 26.227 0.00 28.77  ? 207 LEU A HB2  1 
ATOM   3279 H HB3  . LEU A 1 204 ? 26.757 42.597 27.595 0.00 28.77  ? 207 LEU A HB3  1 
ATOM   3280 H HG   . LEU A 1 204 ? 28.288 42.055 25.243 0.00 33.17  ? 207 LEU A HG   1 
ATOM   3281 H HD11 . LEU A 1 204 ? 28.548 44.394 25.151 0.00 36.20  ? 207 LEU A HD11 1 
ATOM   3282 H HD12 . LEU A 1 204 ? 27.021 43.994 24.977 0.00 36.20  ? 207 LEU A HD12 1 
ATOM   3283 H HD13 . LEU A 1 204 ? 27.545 44.538 26.375 0.00 36.20  ? 207 LEU A HD13 1 
ATOM   3284 H HD21 . LEU A 1 204 ? 30.049 43.057 26.474 0.00 43.05  ? 207 LEU A HD21 1 
ATOM   3285 H HD22 . LEU A 1 204 ? 29.099 43.094 27.747 0.00 43.05  ? 207 LEU A HD22 1 
ATOM   3286 H HD23 . LEU A 1 204 ? 29.563 41.700 27.142 0.00 43.05  ? 207 LEU A HD23 1 
ATOM   3287 N N    . PHE A 1 205 ? 24.609 39.948 27.542 1.00 25.02  ? 208 PHE A N    1 
ATOM   3288 C CA   . PHE A 1 205 ? 23.495 39.597 28.404 1.00 23.36  ? 208 PHE A CA   1 
ATOM   3289 C C    . PHE A 1 205 ? 23.705 38.260 29.067 1.00 21.55  ? 208 PHE A C    1 
ATOM   3290 O O    . PHE A 1 205 ? 23.200 38.040 30.181 1.00 25.12  ? 208 PHE A O    1 
ATOM   3291 C CB   . PHE A 1 205 ? 22.142 39.503 27.588 1.00 21.25  ? 208 PHE A CB   1 
ATOM   3292 C CG   . PHE A 1 205 ? 21.456 40.853 27.301 1.00 21.18  ? 208 PHE A CG   1 
ATOM   3293 C CD1  . PHE A 1 205 ? 21.253 41.812 28.269 1.00 26.37  ? 208 PHE A CD1  1 
ATOM   3294 C CD2  . PHE A 1 205 ? 20.958 41.103 26.015 1.00 25.24  ? 208 PHE A CD2  1 
ATOM   3295 C CE1  . PHE A 1 205 ? 20.573 43.024 27.944 1.00 25.88  ? 208 PHE A CE1  1 
ATOM   3296 C CE2  . PHE A 1 205 ? 20.254 42.286 25.671 1.00 27.13  ? 208 PHE A CE2  1 
ATOM   3297 C CZ   . PHE A 1 205 ? 20.089 43.238 26.631 1.00 27.37  ? 208 PHE A CZ   1 
ATOM   3298 H H    . PHE A 1 205 ? 24.452 39.961 26.696 0.00 30.00  ? 208 PHE A H    1 
ATOM   3299 H HA   . PHE A 1 205 ? 23.422 40.301 29.068 0.00 28.02  ? 208 PHE A HA   1 
ATOM   3300 H HB2  . PHE A 1 205 ? 22.329 39.085 26.733 0.00 25.48  ? 208 PHE A HB2  1 
ATOM   3301 H HB3  . PHE A 1 205 ? 21.517 38.961 28.093 0.00 25.48  ? 208 PHE A HB3  1 
ATOM   3302 H HD1  . PHE A 1 205 ? 21.561 41.670 29.135 0.00 31.63  ? 208 PHE A HD1  1 
ATOM   3303 H HD2  . PHE A 1 205 ? 21.097 40.463 25.355 0.00 30.27  ? 208 PHE A HD2  1 
ATOM   3304 H HE1  . PHE A 1 205 ? 20.447 43.674 28.597 0.00 31.04  ? 208 PHE A HE1  1 
ATOM   3305 H HE2  . PHE A 1 205 ? 19.913 42.407 24.814 0.00 32.54  ? 208 PHE A HE2  1 
ATOM   3306 H HZ   . PHE A 1 205 ? 19.656 44.034 26.423 0.00 32.82  ? 208 PHE A HZ   1 
ATOM   3307 N N    . MET A 1 206 ? 24.500 37.344 28.463 1.00 24.86  ? 209 MET A N    1 
ATOM   3308 C CA   . MET A 1 206 ? 24.682 36.050 29.113 1.00 24.15  ? 209 MET A CA   1 
ATOM   3309 C C    . MET A 1 206 ? 25.574 36.222 30.356 1.00 23.24  ? 209 MET A C    1 
ATOM   3310 O O    . MET A 1 206 ? 25.288 35.658 31.400 1.00 25.41  ? 209 MET A O    1 
ATOM   3311 C CB   . MET A 1 206 ? 25.239 35.021 28.115 1.00 27.80  ? 209 MET A CB   1 
ATOM   3312 C CG   . MET A 1 206 ? 25.494 33.654 28.849 1.00 30.04  ? 209 MET A CG   1 
ATOM   3313 S SD   . MET A 1 206 ? 27.101 33.305 29.404 1.00 43.12  ? 209 MET A SD   1 
ATOM   3314 C CE   . MET A 1 206 ? 27.451 32.836 27.743 1.00 25.50  ? 209 MET A CE   1 
ATOM   3315 H H    . MET A 1 206 ? 24.916 37.452 27.718 0.00 29.81  ? 209 MET A H    1 
ATOM   3316 H HA   . MET A 1 206 ? 23.826 35.692 29.396 0.00 28.96  ? 209 MET A HA   1 
ATOM   3317 H HB2  . MET A 1 206 ? 24.599 34.878 27.400 0.00 33.34  ? 209 MET A HB2  1 
ATOM   3318 H HB3  . MET A 1 206 ? 26.078 35.341 27.749 0.00 33.34  ? 209 MET A HB3  1 
ATOM   3319 H HG2  . MET A 1 206 ? 24.920 33.629 29.631 0.00 36.02  ? 209 MET A HG2  1 
ATOM   3320 H HG3  . MET A 1 206 ? 25.252 32.942 28.237 0.00 36.02  ? 209 MET A HG3  1 
ATOM   3321 H HE1  . MET A 1 206 ? 28.390 32.603 27.671 0.00 30.58  ? 209 MET A HE1  1 
ATOM   3322 H HE2  . MET A 1 206 ? 26.902 32.071 27.508 0.00 30.58  ? 209 MET A HE2  1 
ATOM   3323 H HE3  . MET A 1 206 ? 27.249 33.581 27.155 0.00 30.58  ? 209 MET A HE3  1 
ATOM   3324 N N    . VAL A 1 207 ? 26.643 37.053 30.272 1.00 22.01  ? 210 VAL A N    1 
ATOM   3325 C CA   . VAL A 1 207 ? 27.474 37.327 31.434 1.00 24.00  ? 210 VAL A CA   1 
ATOM   3326 C C    . VAL A 1 207 ? 26.662 38.027 32.523 1.00 24.79  ? 210 VAL A C    1 
ATOM   3327 O O    . VAL A 1 207 ? 26.764 37.683 33.715 1.00 25.17  ? 210 VAL A O    1 
ATOM   3328 C CB   . VAL A 1 207 ? 28.698 38.194 31.051 1.00 27.61  ? 210 VAL A CB   1 
ATOM   3329 C CG1  . VAL A 1 207 ? 29.477 38.541 32.315 1.00 35.95  ? 210 VAL A CG1  1 
ATOM   3330 C CG2  . VAL A 1 207 ? 29.592 37.371 30.094 1.00 31.20  ? 210 VAL A CG2  1 
ATOM   3331 H H    . VAL A 1 207 ? 26.893 37.458 29.556 0.00 26.39  ? 210 VAL A H    1 
ATOM   3332 H HA   . VAL A 1 207 ? 27.790 36.473 31.769 0.00 28.78  ? 210 VAL A HA   1 
ATOM   3333 H HB   . VAL A 1 207 ? 28.422 39.016 30.617 0.00 33.12  ? 210 VAL A HB   1 
ATOM   3334 H HG11 . VAL A 1 207 ? 30.372 38.822 32.067 0.00 43.12  ? 210 VAL A HG11 1 
ATOM   3335 H HG12 . VAL A 1 207 ? 29.021 39.260 32.779 0.00 43.12  ? 210 VAL A HG12 1 
ATOM   3336 H HG13 . VAL A 1 207 ? 29.522 37.757 32.884 0.00 43.12  ? 210 VAL A HG13 1 
ATOM   3337 H HG21 . VAL A 1 207 ? 30.339 37.920 29.808 0.00 37.42  ? 210 VAL A HG21 1 
ATOM   3338 H HG22 . VAL A 1 207 ? 29.919 36.587 30.562 0.00 37.42  ? 210 VAL A HG22 1 
ATOM   3339 H HG23 . VAL A 1 207 ? 29.066 37.101 29.324 0.00 37.42  ? 210 VAL A HG23 1 
ATOM   3340 N N    . LEU A 1 208 ? 25.822 38.978 32.132 1.00 23.30  ? 211 LEU A N    1 
ATOM   3341 C CA   . LEU A 1 208 ? 25.031 39.666 33.145 1.00 22.42  ? 211 LEU A CA   1 
ATOM   3342 C C    . LEU A 1 208 ? 24.053 38.702 33.800 1.00 25.35  ? 211 LEU A C    1 
ATOM   3343 O O    . LEU A 1 208 ? 23.888 38.715 35.022 1.00 24.57  ? 211 LEU A O    1 
ATOM   3344 C CB   . LEU A 1 208 ? 24.255 40.861 32.503 1.00 22.29  ? 211 LEU A CB   1 
ATOM   3345 C CG   . LEU A 1 208 ? 25.158 42.053 32.083 1.00 23.86  ? 211 LEU A CG   1 
ATOM   3346 C CD1  . LEU A 1 208 ? 24.284 43.104 31.292 1.00 26.84  ? 211 LEU A CD1  1 
ATOM   3347 C CD2  . LEU A 1 208 ? 25.852 42.782 33.275 1.00 31.45  ? 211 LEU A CD2  1 
ATOM   3348 H H    . LEU A 1 208 ? 25.696 39.235 31.321 0.00 27.94  ? 211 LEU A H    1 
ATOM   3349 H HA   . LEU A 1 208 ? 25.627 40.020 33.823 0.00 26.88  ? 211 LEU A HA   1 
ATOM   3350 H HB2  . LEU A 1 208 ? 23.798 40.542 31.708 0.00 26.73  ? 211 LEU A HB2  1 
ATOM   3351 H HB3  . LEU A 1 208 ? 23.609 41.192 33.146 0.00 26.73  ? 211 LEU A HB3  1 
ATOM   3352 H HG   . LEU A 1 208 ? 25.869 41.688 31.535 0.00 28.61  ? 211 LEU A HG   1 
ATOM   3353 H HD11 . LEU A 1 208 ? 24.848 43.849 31.029 0.00 32.19  ? 211 LEU A HD11 1 
ATOM   3354 H HD12 . LEU A 1 208 ? 23.912 42.677 30.505 0.00 32.19  ? 211 LEU A HD12 1 
ATOM   3355 H HD13 . LEU A 1 208 ? 23.570 43.418 31.868 0.00 32.19  ? 211 LEU A HD13 1 
ATOM   3356 H HD21 . LEU A 1 208 ? 26.397 43.506 32.928 0.00 37.73  ? 211 LEU A HD21 1 
ATOM   3357 H HD22 . LEU A 1 208 ? 25.171 43.136 33.869 0.00 37.73  ? 211 LEU A HD22 1 
ATOM   3358 H HD23 . LEU A 1 208 ? 26.409 42.148 33.752 0.00 37.73  ? 211 LEU A HD23 1 
ATOM   3359 N N    . ASP A 1 209 ? 23.330 37.921 32.981 1.00 21.94  ? 212 ASP A N    1 
ATOM   3360 C CA   . ASP A 1 209 ? 22.278 37.032 33.518 1.00 20.08  ? 212 ASP A CA   1 
ATOM   3361 C C    . ASP A 1 209 ? 22.885 35.991 34.474 1.00 24.56  ? 212 ASP A C    1 
ATOM   3362 O O    . ASP A 1 209 ? 22.327 35.721 35.546 1.00 22.38  ? 212 ASP A O    1 
ATOM   3363 C CB   . ASP A 1 209 ? 21.572 36.251 32.392 1.00 23.81  ? 212 ASP A CB   1 
ATOM   3364 C CG   . ASP A 1 209 ? 20.527 37.069 31.614 1.00 25.92  ? 212 ASP A CG   1 
ATOM   3365 O OD1  . ASP A 1 209 ? 20.062 38.148 32.121 1.00 24.49  ? 212 ASP A OD1  1 
ATOM   3366 O OD2  . ASP A 1 209 ? 20.139 36.581 30.493 1.00 24.13  ? 212 ASP A OD2  1 
ATOM   3367 H H    . ASP A 1 209 ? 23.424 37.886 32.127 0.00 26.31  ? 212 ASP A H    1 
ATOM   3368 H HA   . ASP A 1 209 ? 21.634 37.597 33.973 0.00 24.07  ? 212 ASP A HA   1 
ATOM   3369 H HB2  . ASP A 1 209 ? 22.241 35.950 31.757 0.00 28.56  ? 212 ASP A HB2  1 
ATOM   3370 H HB3  . ASP A 1 209 ? 21.117 35.488 32.782 0.00 28.56  ? 212 ASP A HB3  1 
ATOM   3371 N N    . VAL A 1 210 ? 23.990 35.358 34.072 1.00 24.06  ? 213 VAL A N    1 
ATOM   3372 C CA   . VAL A 1 210 ? 24.566 34.331 34.976 1.00 23.67  ? 213 VAL A CA   1 
ATOM   3373 C C    . VAL A 1 210 ? 25.046 34.984 36.275 1.00 26.26  ? 213 VAL A C    1 
ATOM   3374 O O    . VAL A 1 210 ? 24.885 34.406 37.384 1.00 25.27  ? 213 VAL A O    1 
ATOM   3375 C CB   . VAL A 1 210 ? 25.730 33.599 34.244 1.00 25.91  ? 213 VAL A CB   1 
ATOM   3376 C CG1  . VAL A 1 210 ? 26.460 32.667 35.201 1.00 33.66  ? 213 VAL A CG1  1 
ATOM   3377 C CG2  . VAL A 1 210 ? 25.150 32.780 33.051 1.00 29.32  ? 213 VAL A CG2  1 
ATOM   3378 H H    . VAL A 1 210 ? 24.406 35.489 33.331 0.00 28.85  ? 213 VAL A H    1 
ATOM   3379 H HA   . VAL A 1 210 ? 23.883 33.680 35.202 0.00 28.39  ? 213 VAL A HA   1 
ATOM   3380 H HB   . VAL A 1 210 ? 26.364 34.254 33.913 0.00 31.07  ? 213 VAL A HB   1 
ATOM   3381 H HG11 . VAL A 1 210 ? 27.024 32.067 34.689 0.00 40.38  ? 213 VAL A HG11 1 
ATOM   3382 H HG12 . VAL A 1 210 ? 27.003 33.197 35.805 0.00 40.38  ? 213 VAL A HG12 1 
ATOM   3383 H HG13 . VAL A 1 210 ? 25.806 32.157 35.705 0.00 40.38  ? 213 VAL A HG13 1 
ATOM   3384 H HG21 . VAL A 1 210 ? 25.877 32.329 32.595 0.00 35.16  ? 213 VAL A HG21 1 
ATOM   3385 H HG22 . VAL A 1 210 ? 24.519 32.128 33.394 0.00 35.16  ? 213 VAL A HG22 1 
ATOM   3386 H HG23 . VAL A 1 210 ? 24.701 33.386 32.441 0.00 35.16  ? 213 VAL A HG23 1 
ATOM   3387 N N    . SER A 1 211 ? 25.647 36.177 36.190 1.00 24.16  ? 214 SER A N    1 
ATOM   3388 C CA   . SER A 1 211 ? 26.131 36.846 37.407 1.00 23.68  ? 214 SER A CA   1 
ATOM   3389 C C    . SER A 1 211 ? 24.950 37.249 38.305 1.00 26.43  ? 214 SER A C    1 
ATOM   3390 O O    . SER A 1 211 ? 25.024 37.142 39.531 1.00 25.71  ? 214 SER A O    1 
ATOM   3391 C CB   . SER A 1 211 ? 26.964 38.100 37.053 1.00 26.47  ? 214 SER A CB   1 
ATOM   3392 O OG   . SER A 1 211 ? 28.100 37.696 36.286 1.00 30.89  ? 214 SER A OG   1 
ATOM   3393 H H    . SER A 1 211 ? 25.785 36.610 35.460 0.00 28.97  ? 214 SER A H    1 
ATOM   3394 H HA   . SER A 1 211 ? 26.708 36.230 37.885 0.00 28.39  ? 214 SER A HA   1 
ATOM   3395 H HB2  . SER A 1 211 ? 26.423 38.713 36.532 0.00 31.75  ? 214 SER A HB2  1 
ATOM   3396 H HB3  . SER A 1 211 ? 27.262 38.532 37.869 0.00 31.75  ? 214 SER A HB3  1 
ATOM   3397 H HG   . SER A 1 211 ? 27.849 37.333 35.571 0.00 37.05  ? 214 SER A HG   1 
ATOM   3398 N N    . ALA A 1 212 ? 23.867 37.767 37.693 1.00 23.13  ? 215 ALA A N    1 
ATOM   3399 C CA   . ALA A 1 212 ? 22.762 38.335 38.508 1.00 22.32  ? 215 ALA A CA   1 
ATOM   3400 C C    . ALA A 1 212 ? 21.852 37.280 39.072 1.00 24.84  ? 215 ALA A C    1 
ATOM   3401 O O    . ALA A 1 212 ? 21.038 37.563 39.977 1.00 27.18  ? 215 ALA A O    1 
ATOM   3402 C CB   . ALA A 1 212 ? 21.844 39.352 37.603 1.00 24.31  ? 215 ALA A CB   1 
ATOM   3403 H H    . ALA A 1 212 ? 23.749 37.801 36.842 0.00 27.74  ? 215 ALA A H    1 
ATOM   3404 H HA   . ALA A 1 212 ? 23.177 38.815 39.243 0.00 26.77  ? 215 ALA A HA   1 
ATOM   3405 H HB1  . ALA A 1 212 ? 21.131 39.711 38.156 0.00 29.16  ? 215 ALA A HB1  1 
ATOM   3406 H HB2  . ALA A 1 212 ? 22.402 40.074 37.274 0.00 29.16  ? 215 ALA A HB2  1 
ATOM   3407 H HB3  . ALA A 1 212 ? 21.467 38.858 36.858 0.00 29.16  ? 215 ALA A HB3  1 
ATOM   3408 N N    . LYS A 1 213 ? 21.976 36.040 38.549 1.00 23.15  ? 216 LYS A N    1 
ATOM   3409 C CA   . LYS A 1 213 ? 21.139 34.897 38.998 1.00 21.45  ? 216 LYS A CA   1 
ATOM   3410 C C    . LYS A 1 213 ? 22.003 33.864 39.758 1.00 25.35  ? 216 LYS A C    1 
ATOM   3411 O O    . LYS A 1 213 ? 21.713 33.639 40.965 1.00 26.42  ? 216 LYS A O    1 
ATOM   3412 C CB   . LYS A 1 213 ? 20.442 34.264 37.779 1.00 21.66  ? 216 LYS A CB   1 
ATOM   3413 C CG   . LYS A 1 213 ? 19.424 35.222 37.174 1.00 23.08  ? 216 LYS A CG   1 
ATOM   3414 C CD   . LYS A 1 213 ? 18.625 34.567 36.033 1.00 23.08  ? 216 LYS A CD   1 
ATOM   3415 C CE   . LYS A 1 213 ? 17.388 35.380 35.672 1.00 25.23  ? 216 LYS A CE   1 
ATOM   3416 N NZ   . LYS A 1 213 ? 17.718 36.558 34.879 1.00 23.68  ? 216 LYS A NZ   1 
ATOM   3417 H HA   . LYS A 1 213 ? 20.492 35.259 39.638 1.00 25.72  ? 216 LYS A HA   1 
ATOM   3418 H HB2  . LYS A 1 213 ? 21.115 34.011 37.115 1.00 25.98  ? 216 LYS A HB2  1 
ATOM   3419 H HB3  . LYS A 1 213 ? 20.011 33.427 38.048 1.00 25.98  ? 216 LYS A HB3  1 
ATOM   3420 H HG2  . LYS A 1 213 ? 18.793 35.537 37.853 1.00 27.68  ? 216 LYS A HG2  1 
ATOM   3421 H HG3  . LYS A 1 213 ? 19.862 36.024 36.824 1.00 27.68  ? 216 LYS A HG3  1 
ATOM   3422 H HD2  . LYS A 1 213 ? 19.199 34.468 35.246 1.00 27.68  ? 216 LYS A HD2  1 
ATOM   3423 H HD3  . LYS A 1 213 ? 18.362 33.661 36.295 1.00 27.68  ? 216 LYS A HD3  1 
ATOM   3424 H HE2  . LYS A 1 213 ? 16.777 34.841 35.130 1.00 30.25  ? 216 LYS A HE2  1 
ATOM   3425 H HE3  . LYS A 1 213 ? 16.949 35.705 36.485 1.00 30.25  ? 216 LYS A HE3  1 
ATOM   3426 H HZ2  . LYS A 1 213 ? 17.846 36.452 34.012 1.00 28.40  ? 216 LYS A HZ2  1 
ATOM   3427 N N    . VAL A 1 214 ? 22.941 33.185 39.098 1.00 24.37  ? 217 VAL A N    1 
ATOM   3428 C CA   . VAL A 1 214 ? 23.736 32.181 39.815 1.00 23.37  ? 217 VAL A CA   1 
ATOM   3429 C C    . VAL A 1 214 ? 24.754 32.822 40.748 1.00 25.56  ? 217 VAL A C    1 
ATOM   3430 O O    . VAL A 1 214 ? 24.974 32.330 41.877 1.00 29.45  ? 217 VAL A O    1 
ATOM   3431 C CB   . VAL A 1 214 ? 24.425 31.250 38.751 1.00 25.30  ? 217 VAL A CB   1 
ATOM   3432 C CG1  . VAL A 1 214 ? 25.294 30.177 39.458 1.00 28.02  ? 217 VAL A CG1  1 
ATOM   3433 C CG2  . VAL A 1 214 ? 23.387 30.595 37.848 1.00 29.08  ? 217 VAL A CG2  1 
ATOM   3434 H H    . VAL A 1 214 ? 23.131 33.282 38.265 0.00 29.23  ? 217 VAL A H    1 
ATOM   3435 H HA   . VAL A 1 214 ? 23.162 31.651 40.390 0.00 28.03  ? 217 VAL A HA   1 
ATOM   3436 H HB   . VAL A 1 214 ? 25.004 31.791 38.191 0.00 30.34  ? 217 VAL A HB   1 
ATOM   3437 H HG11 . VAL A 1 214 ? 25.639 29.561 38.793 0.00 33.61  ? 217 VAL A HG11 1 
ATOM   3438 H HG12 . VAL A 1 214 ? 26.029 30.616 39.915 0.00 33.61  ? 217 VAL A HG12 1 
ATOM   3439 H HG13 . VAL A 1 214 ? 24.745 29.698 40.099 0.00 33.61  ? 217 VAL A HG13 1 
ATOM   3440 H HG21 . VAL A 1 214 ? 23.780 29.812 37.432 0.00 34.88  ? 217 VAL A HG21 1 
ATOM   3441 H HG22 . VAL A 1 214 ? 22.621 30.337 38.384 0.00 34.88  ? 217 VAL A HG22 1 
ATOM   3442 H HG23 . VAL A 1 214 ? 23.116 31.230 37.167 0.00 34.88  ? 217 VAL A HG23 1 
ATOM   3443 N N    . GLY A 1 215 ? 25.441 33.909 40.315 1.00 27.11  ? 218 GLY A N    1 
ATOM   3444 C CA   . GLY A 1 215 ? 26.357 34.587 41.259 1.00 29.65  ? 218 GLY A CA   1 
ATOM   3445 C C    . GLY A 1 215 ? 25.636 35.131 42.497 1.00 28.88  ? 218 GLY A C    1 
ATOM   3446 O O    . GLY A 1 215 ? 26.077 34.931 43.645 1.00 28.22  ? 218 GLY A O    1 
ATOM   3447 H H    . GLY A 1 215 ? 25.397 34.251 39.527 0.00 32.51  ? 218 GLY A H    1 
ATOM   3448 H HA2  . GLY A 1 215 ? 27.035 33.960 41.554 0.00 35.56  ? 218 GLY A HA2  1 
ATOM   3449 H HA3  . GLY A 1 215 ? 26.789 35.330 40.808 0.00 35.56  ? 218 GLY A HA3  1 
ATOM   3450 N N    . PHE A 1 216 ? 24.539 35.889 42.272 1.00 27.83  ? 219 PHE A N    1 
ATOM   3451 C CA   . PHE A 1 216 ? 23.702 36.363 43.361 1.00 29.15  ? 219 PHE A CA   1 
ATOM   3452 C C    . PHE A 1 216 ? 23.304 35.222 44.280 1.00 25.55  ? 219 PHE A C    1 
ATOM   3453 O O    . PHE A 1 216 ? 23.419 35.354 45.493 1.00 27.86  ? 219 PHE A O    1 
ATOM   3454 C CB   . PHE A 1 216 ? 22.427 37.036 42.750 1.00 27.27  ? 219 PHE A CB   1 
ATOM   3455 C CG   . PHE A 1 216 ? 21.439 37.581 43.724 1.00 27.98  ? 219 PHE A CG   1 
ATOM   3456 C CD1  . PHE A 1 216 ? 20.461 36.760 44.295 1.00 27.32  ? 219 PHE A CD1  1 
ATOM   3457 C CD2  . PHE A 1 216 ? 21.343 38.955 43.945 1.00 29.97  ? 219 PHE A CD2  1 
ATOM   3458 C CE1  . PHE A 1 216 ? 19.458 37.305 45.179 1.00 31.24  ? 219 PHE A CE1  1 
ATOM   3459 C CE2  . PHE A 1 216 ? 20.334 39.498 44.765 1.00 30.21  ? 219 PHE A CE2  1 
ATOM   3460 C CZ   . PHE A 1 216 ? 19.396 38.680 45.396 1.00 31.59  ? 219 PHE A CZ   1 
ATOM   3461 H H    . PHE A 1 216 ? 24.269 36.135 41.493 0.00 33.37  ? 219 PHE A H    1 
ATOM   3462 H HA   . PHE A 1 216 ? 24.189 37.016 43.888 0.00 34.96  ? 219 PHE A HA   1 
ATOM   3463 H HB2  . PHE A 1 216 ? 22.714 37.775 42.190 0.00 32.71  ? 219 PHE A HB2  1 
ATOM   3464 H HB3  . PHE A 1 216 ? 21.964 36.374 42.213 0.00 32.71  ? 219 PHE A HB3  1 
ATOM   3465 H HD1  . PHE A 1 216 ? 20.457 35.850 44.102 0.00 32.76  ? 219 PHE A HD1  1 
ATOM   3466 H HD2  . PHE A 1 216 ? 21.958 39.525 43.542 0.00 35.95  ? 219 PHE A HD2  1 
ATOM   3467 H HE1  . PHE A 1 216 ? 18.855 36.739 45.603 0.00 37.47  ? 219 PHE A HE1  1 
ATOM   3468 H HE2  . PHE A 1 216 ? 20.293 40.419 44.888 0.00 36.24  ? 219 PHE A HE2  1 
ATOM   3469 H HZ   . PHE A 1 216 ? 18.743 39.045 45.949 0.00 37.89  ? 219 PHE A HZ   1 
ATOM   3470 N N    . GLY A 1 217 ? 22.834 34.078 43.722 1.00 24.28  ? 220 GLY A N    1 
ATOM   3471 C CA   . GLY A 1 217 ? 22.353 33.002 44.601 1.00 29.51  ? 220 GLY A CA   1 
ATOM   3472 C C    . GLY A 1 217 ? 23.454 32.324 45.396 1.00 32.42  ? 220 GLY A C    1 
ATOM   3473 O O    . GLY A 1 217 ? 23.209 31.863 46.516 1.00 29.85  ? 220 GLY A O    1 
ATOM   3474 H H    . GLY A 1 217 ? 22.787 33.916 42.879 0.00 29.11  ? 220 GLY A H    1 
ATOM   3475 H HA2  . GLY A 1 217 ? 21.712 33.370 45.229 0.00 35.40  ? 220 GLY A HA2  1 
ATOM   3476 H HA3  . GLY A 1 217 ? 21.914 32.326 44.061 0.00 35.40  ? 220 GLY A HA3  1 
ATOM   3477 N N    . LEU A 1 218 ? 24.670 32.204 44.827 1.00 26.75  ? 221 LEU A N    1 
ATOM   3478 C CA   . LEU A 1 218 ? 25.772 31.616 45.565 1.00 31.16  ? 221 LEU A CA   1 
ATOM   3479 C C    . LEU A 1 218 ? 26.117 32.454 46.809 1.00 33.63  ? 221 LEU A C    1 
ATOM   3480 O O    . LEU A 1 218 ? 26.401 31.898 47.882 1.00 35.91  ? 221 LEU A O    1 
ATOM   3481 C CB   . LEU A 1 218 ? 27.003 31.501 44.665 1.00 27.93  ? 221 LEU A CB   1 
ATOM   3482 C CG   . LEU A 1 218 ? 26.928 30.356 43.635 1.00 43.13  ? 221 LEU A CG   1 
ATOM   3483 C CD1  . LEU A 1 218 ? 28.055 30.506 42.661 1.00 38.98  ? 221 LEU A CD1  1 
ATOM   3484 C CD2  . LEU A 1 218 ? 26.996 28.988 44.329 1.00 37.21  ? 221 LEU A CD2  1 
ATOM   3485 H H    . LEU A 1 218 ? 24.868 32.454 44.029 0.00 32.08  ? 221 LEU A H    1 
ATOM   3486 H HA   . LEU A 1 218 ? 25.511 30.727 45.852 0.00 37.38  ? 221 LEU A HA   1 
ATOM   3487 H HB2  . LEU A 1 218 ? 27.108 32.332 44.176 0.00 33.49  ? 221 LEU A HB2  1 
ATOM   3488 H HB3  . LEU A 1 218 ? 27.781 31.344 45.224 0.00 33.49  ? 221 LEU A HB3  1 
ATOM   3489 H HG   . LEU A 1 218 ? 26.084 30.397 43.158 0.00 51.74  ? 221 LEU A HG   1 
ATOM   3490 H HD11 . LEU A 1 218 ? 27.988 29.808 41.991 0.00 46.75  ? 221 LEU A HD11 1 
ATOM   3491 H HD12 . LEU A 1 218 ? 27.994 31.377 42.239 0.00 46.75  ? 221 LEU A HD12 1 
ATOM   3492 H HD13 . LEU A 1 218 ? 28.896 30.428 43.138 0.00 46.75  ? 221 LEU A HD13 1 
ATOM   3493 H HD21 . LEU A 1 218 ? 27.086 28.296 43.656 0.00 44.63  ? 221 LEU A HD21 1 
ATOM   3494 H HD22 . LEU A 1 218 ? 27.762 28.973 44.924 0.00 44.63  ? 221 LEU A HD22 1 
ATOM   3495 H HD23 . LEU A 1 218 ? 26.180 28.851 44.837 0.00 44.63  ? 221 LEU A HD23 1 
ATOM   3496 N N    . ILE A 1 219 ? 26.076 33.783 46.683 1.00 28.94  ? 222 ILE A N    1 
ATOM   3497 C CA   . ILE A 1 219 ? 26.325 34.679 47.830 1.00 30.74  ? 222 ILE A CA   1 
ATOM   3498 C C    . ILE A 1 219 ? 25.247 34.495 48.892 1.00 34.25  ? 222 ILE A C    1 
ATOM   3499 O O    . ILE A 1 219 ? 25.544 34.323 50.085 1.00 32.92  ? 222 ILE A O    1 
ATOM   3500 C CB   . ILE A 1 219 ? 26.401 36.148 47.346 1.00 30.72  ? 222 ILE A CB   1 
ATOM   3501 C CG1  . ILE A 1 219 ? 27.613 36.367 46.451 1.00 31.54  ? 222 ILE A CG1  1 
ATOM   3502 C CG2  . ILE A 1 219 ? 26.467 37.116 48.539 1.00 36.45  ? 222 ILE A CG2  1 
ATOM   3503 C CD1  . ILE A 1 219 ? 27.610 37.681 45.639 1.00 38.05  ? 222 ILE A CD1  1 
ATOM   3504 H H    . ILE A 1 219 ? 25.907 34.197 45.948 0.00 34.71  ? 222 ILE A H    1 
ATOM   3505 H HA   . ILE A 1 219 ? 27.177 34.445 48.231 0.00 36.87  ? 222 ILE A HA   1 
ATOM   3506 H HB   . ILE A 1 219 ? 25.596 36.323 46.834 0.00 36.84  ? 222 ILE A HB   1 
ATOM   3507 H HG12 . ILE A 1 219 ? 28.407 36.374 47.009 0.00 37.83  ? 222 ILE A HG12 1 
ATOM   3508 H HG13 . ILE A 1 219 ? 27.661 35.635 45.816 0.00 37.83  ? 222 ILE A HG13 1 
ATOM   3509 H HG21 . ILE A 1 219 ? 26.876 37.947 48.250 0.00 43.73  ? 222 ILE A HG21 1 
ATOM   3510 H HG22 . ILE A 1 219 ? 25.567 37.284 48.860 0.00 43.73  ? 222 ILE A HG22 1 
ATOM   3511 H HG23 . ILE A 1 219 ? 26.999 36.714 49.243 0.00 43.73  ? 222 ILE A HG23 1 
ATOM   3512 H HD11 . ILE A 1 219 ? 28.382 37.691 45.052 0.00 45.64  ? 222 ILE A HD11 1 
ATOM   3513 H HD12 . ILE A 1 219 ? 26.795 37.726 45.114 0.00 45.64  ? 222 ILE A HD12 1 
ATOM   3514 H HD13 . ILE A 1 219 ? 27.650 38.431 46.252 0.00 45.64  ? 222 ILE A HD13 1 
ATOM   3515 N N    . LEU A 1 220 ? 23.981 34.519 48.469 1.00 27.64  ? 223 LEU A N    1 
ATOM   3516 C CA   . LEU A 1 220 ? 22.858 34.466 49.416 1.00 26.60  ? 223 LEU A CA   1 
ATOM   3517 C C    . LEU A 1 220 ? 22.807 33.123 50.127 1.00 33.25  ? 223 LEU A C    1 
ATOM   3518 O O    . LEU A 1 220 ? 22.637 33.061 51.354 1.00 34.12  ? 223 LEU A O    1 
ATOM   3519 C CB   . LEU A 1 220 ? 21.512 34.685 48.652 1.00 25.92  ? 223 LEU A CB   1 
ATOM   3520 C CG   . LEU A 1 220 ? 20.250 34.584 49.552 1.00 29.44  ? 223 LEU A CG   1 
ATOM   3521 C CD1  . LEU A 1 220 ? 20.210 35.683 50.555 1.00 32.20  ? 223 LEU A CD1  1 
ATOM   3522 C CD2  . LEU A 1 220 ? 18.992 34.702 48.675 1.00 28.18  ? 223 LEU A CD2  1 
ATOM   3523 H H    . LEU A 1 220 ? 23.742 34.564 47.644 0.00 33.15  ? 223 LEU A H    1 
ATOM   3524 H HA   . LEU A 1 220 ? 22.976 35.171 50.072 0.00 31.90  ? 223 LEU A HA   1 
ATOM   3525 H HB2  . LEU A 1 220 ? 21.521 35.570 48.255 0.00 31.09  ? 223 LEU A HB2  1 
ATOM   3526 H HB3  . LEU A 1 220 ? 21.435 34.011 47.959 0.00 31.09  ? 223 LEU A HB3  1 
ATOM   3527 H HG   . LEU A 1 220 ? 20.274 33.733 50.017 0.00 35.31  ? 223 LEU A HG   1 
ATOM   3528 H HD11 . LEU A 1 220 ? 19.390 35.611 51.069 0.00 38.62  ? 223 LEU A HD11 1 
ATOM   3529 H HD12 . LEU A 1 220 ? 20.977 35.601 51.144 0.00 38.62  ? 223 LEU A HD12 1 
ATOM   3530 H HD13 . LEU A 1 220 ? 20.237 36.534 50.092 0.00 38.62  ? 223 LEU A HD13 1 
ATOM   3531 H HD21 . LEU A 1 220 ? 18.206 34.631 49.240 0.00 33.80  ? 223 LEU A HD21 1 
ATOM   3532 H HD22 . LEU A 1 220 ? 19.000 35.562 48.226 0.00 33.80  ? 223 LEU A HD22 1 
ATOM   3533 H HD23 . LEU A 1 220 ? 18.995 33.987 48.020 0.00 33.80  ? 223 LEU A HD23 1 
ATOM   3534 N N    . LEU A 1 221 ? 22.928 32.023 49.376 1.00 30.86  ? 224 LEU A N    1 
ATOM   3535 C CA   . LEU A 1 221 ? 22.674 30.703 50.000 1.00 33.18  ? 224 LEU A CA   1 
ATOM   3536 C C    . LEU A 1 221 ? 23.858 30.179 50.806 1.00 40.14  ? 224 LEU A C    1 
ATOM   3537 O O    . LEU A 1 221 ? 23.728 29.135 51.439 1.00 37.79  ? 224 LEU A O    1 
ATOM   3538 C CB   . LEU A 1 221 ? 22.235 29.676 48.926 1.00 32.27  ? 224 LEU A CB   1 
ATOM   3539 C CG   . LEU A 1 221 ? 20.967 30.083 48.124 1.00 33.83  ? 224 LEU A CG   1 
ATOM   3540 C CD1  . LEU A 1 221 ? 20.672 29.078 46.986 1.00 33.99  ? 224 LEU A CD1  1 
ATOM   3541 C CD2  . LEU A 1 221 ? 19.729 30.177 49.050 1.00 33.74  ? 224 LEU A CD2  1 
ATOM   3542 H H    . LEU A 1 221 ? 23.146 32.008 48.544 0.00 37.02  ? 224 LEU A H    1 
ATOM   3543 H HA   . LEU A 1 221 ? 21.934 30.793 50.620 0.00 39.79  ? 224 LEU A HA   1 
ATOM   3544 H HB2  . LEU A 1 221 ? 22.961 29.565 48.292 0.00 38.70  ? 224 LEU A HB2  1 
ATOM   3545 H HB3  . LEU A 1 221 ? 22.047 28.833 49.366 0.00 38.70  ? 224 LEU A HB3  1 
ATOM   3546 H HG   . LEU A 1 221 ? 21.137 30.954 47.732 0.00 40.57  ? 224 LEU A HG   1 
ATOM   3547 H HD11 . LEU A 1 221 ? 19.858 29.345 46.532 0.00 40.76  ? 224 LEU A HD11 1 
ATOM   3548 H HD12 . LEU A 1 221 ? 21.415 29.079 46.363 0.00 40.76  ? 224 LEU A HD12 1 
ATOM   3549 H HD13 . LEU A 1 221 ? 20.562 28.193 47.367 0.00 40.76  ? 224 LEU A HD13 1 
ATOM   3550 H HD21 . LEU A 1 221 ? 18.932 30.266 48.504 0.00 40.47  ? 224 LEU A HD21 1 
ATOM   3551 H HD22 . LEU A 1 221 ? 19.673 29.371 49.586 0.00 40.47  ? 224 LEU A HD22 1 
ATOM   3552 H HD23 . LEU A 1 221 ? 19.823 30.952 49.626 0.00 40.47  ? 224 LEU A HD23 1 
ATOM   3553 N N    A ARG A 1 222 ? 25.009 30.852 50.796 0.32 36.66  ? 225 ARG A N    1 
ATOM   3554 N N    B ARG A 1 222 ? 24.983 30.877 50.803 0.68 36.61  ? 225 ARG A N    1 
ATOM   3555 C CA   A ARG A 1 222 ? 26.085 30.503 51.717 0.32 43.65  ? 225 ARG A CA   1 
ATOM   3556 C CA   B ARG A 1 222 ? 26.100 30.549 51.665 0.68 43.71  ? 225 ARG A CA   1 
ATOM   3557 C C    A ARG A 1 222 ? 26.000 31.271 53.027 0.32 42.57  ? 225 ARG A C    1 
ATOM   3558 C C    B ARG A 1 222 ? 26.106 31.390 52.933 0.68 42.12  ? 225 ARG A C    1 
ATOM   3559 O O    A ARG A 1 222 ? 26.710 30.926 53.984 0.32 43.82  ? 225 ARG A O    1 
ATOM   3560 O O    B ARG A 1 222 ? 26.983 31.199 53.787 0.68 46.29  ? 225 ARG A O    1 
ATOM   3561 C CB   A ARG A 1 222 ? 27.460 30.743 51.074 0.32 43.67  ? 225 ARG A CB   1 
ATOM   3562 C CB   B ARG A 1 222 ? 27.398 30.719 50.880 0.68 43.13  ? 225 ARG A CB   1 
ATOM   3563 C CG   A ARG A 1 222 ? 27.717 32.133 50.519 0.32 46.33  ? 225 ARG A CG   1 
ATOM   3564 C CG   B ARG A 1 222 ? 27.540 29.642 49.790 0.68 56.06  ? 225 ARG A CG   1 
ATOM   3565 C CD   A ARG A 1 222 ? 27.843 33.215 51.572 0.32 48.41  ? 225 ARG A CD   1 
ATOM   3566 C CD   B ARG A 1 222 ? 28.762 29.863 48.899 0.68 59.10  ? 225 ARG A CD   1 
ATOM   3567 N NE   A ARG A 1 222 ? 28.216 34.499 50.994 0.32 43.10  ? 225 ARG A NE   1 
ATOM   3568 N NE   B ARG A 1 222 ? 29.993 29.545 49.609 0.68 72.14  ? 225 ARG A NE   1 
ATOM   3569 C CZ   A ARG A 1 222 ? 28.029 35.670 51.585 0.32 43.86  ? 225 ARG A CZ   1 
ATOM   3570 C CZ   B ARG A 1 222 ? 30.466 28.318 49.787 0.68 78.21  ? 225 ARG A CZ   1 
ATOM   3571 N NH1  A ARG A 1 222 ? 27.370 35.772 52.724 0.32 54.08  ? 225 ARG A NH1  1 
ATOM   3572 N NH1  B ARG A 1 222 ? 29.847 27.257 49.296 0.68 76.91  ? 225 ARG A NH1  1 
ATOM   3573 N NH2  A ARG A 1 222 ? 28.532 36.767 51.028 0.32 58.46  ? 225 ARG A NH2  1 
ATOM   3574 N NH2  B ARG A 1 222 ? 31.588 28.153 50.480 0.68 75.60  ? 225 ARG A NH2  1 
ATOM   3575 H H    A ARG A 1 222 ? 25.187 31.509 50.270 0.32 43.97  ? 225 ARG A H    1 
ATOM   3576 H H    B ARG A 1 222 ? 25.124 31.559 50.299 0.68 43.91  ? 225 ARG A H    1 
ATOM   3577 H HA   A ARG A 1 222 ? 26.026 29.555 51.912 0.32 52.37  ? 225 ARG A HA   1 
ATOM   3578 H HA   B ARG A 1 222 ? 26.054 29.621 51.945 0.68 52.44  ? 225 ARG A HA   1 
ATOM   3579 H HB2  A ARG A 1 222 ? 28.140 30.575 51.745 0.32 52.39  ? 225 ARG A HB2  1 
ATOM   3580 H HB2  B ARG A 1 222 ? 27.402 31.590 50.452 0.68 51.73  ? 225 ARG A HB2  1 
ATOM   3581 H HB3  A ARG A 1 222 ? 27.561 30.120 50.337 0.32 52.39  ? 225 ARG A HB3  1 
ATOM   3582 H HB3  B ARG A 1 222 ? 28.152 30.644 51.485 0.68 51.73  ? 225 ARG A HB3  1 
ATOM   3583 H HG2  A ARG A 1 222 ? 28.545 32.118 50.015 0.32 55.58  ? 225 ARG A HG2  1 
ATOM   3584 H HG2  B ARG A 1 222 ? 27.630 28.774 50.213 0.68 67.25  ? 225 ARG A HG2  1 
ATOM   3585 H HG3  A ARG A 1 222 ? 26.979 32.376 49.938 0.32 55.58  ? 225 ARG A HG3  1 
ATOM   3586 H HG3  B ARG A 1 222 ? 26.751 29.656 49.226 0.68 67.25  ? 225 ARG A HG3  1 
ATOM   3587 H HD2  A ARG A 1 222 ? 26.991 33.322 52.024 0.32 58.08  ? 225 ARG A HD2  1 
ATOM   3588 H HD2  B ARG A 1 222 ? 28.701 29.289 48.119 0.68 70.91  ? 225 ARG A HD2  1 
ATOM   3589 H HD3  A ARG A 1 222 ? 28.527 32.961 52.211 0.32 58.08  ? 225 ARG A HD3  1 
ATOM   3590 H HD3  B ARG A 1 222 ? 28.797 30.793 48.625 0.68 70.91  ? 225 ARG A HD3  1 
ATOM   3591 H HE   A ARG A 1 222 ? 28.583 34.497 50.216 0.32 51.70  ? 225 ARG A HE   1 
ATOM   3592 H HE   B ARG A 1 222 ? 30.445 30.199 49.937 0.68 86.55  ? 225 ARG A HE   1 
ATOM   3593 H HH11 A ARG A 1 222 ? 27.050 35.067 53.100 0.32 64.88  ? 225 ARG A HH11 1 
ATOM   3594 H HH11 B ARG A 1 222 ? 29.118 27.353 48.848 0.68 92.28  ? 225 ARG A HH11 1 
ATOM   3595 H HH12 A ARG A 1 222 ? 27.260 36.542 53.090 0.32 64.88  ? 225 ARG A HH12 1 
ATOM   3596 H HH12 B ARG A 1 222 ? 30.172 26.471 49.424 0.68 92.28  ? 225 ARG A HH12 1 
ATOM   3597 H HH21 A ARG A 1 222 ? 28.974 36.712 50.292 0.32 70.13  ? 225 ARG A HH21 1 
ATOM   3598 H HH21 B ARG A 1 222 ? 31.997 28.835 50.806 0.68 90.70  ? 225 ARG A HH21 1 
ATOM   3599 H HH22 A ARG A 1 222 ? 28.416 37.532 51.404 0.32 70.13  ? 225 ARG A HH22 1 
ATOM   3600 H HH22 B ARG A 1 222 ? 31.905 27.363 50.602 0.68 90.70  ? 225 ARG A HH22 1 
ATOM   3601 N N    . SER A 1 223 ? 25.112 32.254 53.106 1.00 38.63  ? 226 SER A N    1 
ATOM   3602 C CA   . SER A 1 223 ? 25.083 33.174 54.238 1.00 45.54  ? 226 SER A CA   1 
ATOM   3603 C C    . SER A 1 223 ? 24.306 32.564 55.405 1.00 40.49  ? 226 SER A C    1 
ATOM   3604 O O    . SER A 1 223 ? 23.375 31.774 55.217 1.00 47.13  ? 226 SER A O    1 
ATOM   3605 C CB   . SER A 1 223 ? 24.440 34.500 53.781 1.00 46.50  ? 226 SER A CB   1 
ATOM   3606 O OG   . SER A 1 223 ? 23.952 35.249 54.894 1.00 61.41  ? 226 SER A OG   1 
ATOM   3607 H H    . SER A 1 223 ? 24.438 32.325 52.577 0.00 46.34  ? 226 SER A H    1 
ATOM   3608 H HA   . SER A 1 223 ? 25.979 33.357 54.562 0.00 54.63  ? 226 SER A HA   1 
ATOM   3609 H HB2  . SER A 1 223 ? 25.107 35.029 53.316 0.00 55.78  ? 226 SER A HB2  1 
ATOM   3610 H HB3  . SER A 1 223 ? 23.700 34.303 53.187 0.00 55.78  ? 226 SER A HB3  1 
ATOM   3611 H HG   . SER A 1 223 ? 23.446 35.863 54.627 0.00 73.67  ? 226 SER A HG   1 
ATOM   3612 N N    . ARG A 1 224 ? 24.699 32.916 56.636 1.00 43.13  ? 227 ARG A N    1 
ATOM   3613 C CA   . ARG A 1 224 ? 23.891 32.492 57.784 1.00 44.10  ? 227 ARG A CA   1 
ATOM   3614 C C    . ARG A 1 224 ? 22.612 33.320 57.926 1.00 43.53  ? 227 ARG A C    1 
ATOM   3615 O O    . ARG A 1 224 ? 21.755 32.986 58.769 1.00 45.52  ? 227 ARG A O    1 
ATOM   3616 C CB   . ARG A 1 224 ? 24.692 32.586 59.083 1.00 51.45  ? 227 ARG A CB   1 
ATOM   3617 C CG   . ARG A 1 224 ? 25.306 31.212 59.510 1.00 67.30  ? 227 ARG A CG   1 
ATOM   3618 C CD   . ARG A 1 224 ? 24.212 30.220 59.998 1.00 80.66  ? 227 ARG A CD   1 
ATOM   3619 N NE   . ARG A 1 224 ? 24.500 28.829 59.650 1.00 99.04  ? 227 ARG A NE   1 
ATOM   3620 C CZ   . ARG A 1 224 ? 23.825 27.774 60.099 1.00 105.09 ? 227 ARG A CZ   1 
ATOM   3621 N NH1  . ARG A 1 224 ? 22.800 27.905 60.927 1.00 94.95  ? 227 ARG A NH1  1 
ATOM   3622 N NH2  . ARG A 1 224 ? 24.194 26.553 59.712 1.00 120.43 ? 227 ARG A NH2  1 
ATOM   3623 H H    . ARG A 1 224 ? 25.398 33.380 56.823 0.00 51.74  ? 227 ARG A H    1 
ATOM   3624 H HA   . ARG A 1 224 ? 23.651 31.560 57.660 0.00 52.91  ? 227 ARG A HA   1 
ATOM   3625 H HB2  . ARG A 1 224 ? 25.419 33.216 58.962 0.00 61.72  ? 227 ARG A HB2  1 
ATOM   3626 H HB3  . ARG A 1 224 ? 24.106 32.888 59.795 0.00 61.72  ? 227 ARG A HB3  1 
ATOM   3627 H HG2  . ARG A 1 224 ? 25.761 30.815 58.752 0.00 80.74  ? 227 ARG A HG2  1 
ATOM   3628 H HG3  . ARG A 1 224 ? 25.934 31.354 60.236 0.00 80.74  ? 227 ARG A HG3  1 
ATOM   3629 H HD2  . ARG A 1 224 ? 24.143 30.278 60.964 0.00 96.78  ? 227 ARG A HD2  1 
ATOM   3630 H HD3  . ARG A 1 224 ? 23.365 30.460 59.590 0.00 96.78  ? 227 ARG A HD3  1 
ATOM   3631 H HE   . ARG A 1 224 ? 25.156 28.681 59.114 0.00 118.83 ? 227 ARG A HE   1 
ATOM   3632 H HH11 . ARG A 1 224 ? 22.554 28.687 61.187 0.00 113.92 ? 227 ARG A HH11 1 
ATOM   3633 H HH12 . ARG A 1 224 ? 22.379 27.207 61.204 0.00 113.92 ? 227 ARG A HH12 1 
ATOM   3634 H HH21 . ARG A 1 224 ? 24.862 26.455 59.179 0.00 144.49 ? 227 ARG A HH21 1 
ATOM   3635 H HH22 . ARG A 1 224 ? 23.766 25.864 59.997 0.00 144.49 ? 227 ARG A HH22 1 
ATOM   3636 N N    . ALA A 1 225 ? 22.467 34.367 57.113 1.00 46.70  ? 228 ALA A N    1 
ATOM   3637 C CA   . ALA A 1 225 ? 21.336 35.282 57.231 1.00 51.91  ? 228 ALA A CA   1 
ATOM   3638 C C    . ALA A 1 225 ? 20.006 34.611 56.902 1.00 54.23  ? 228 ALA A C    1 
ATOM   3639 O O    . ALA A 1 225 ? 18.960 35.062 57.371 1.00 46.24  ? 228 ALA A O    1 
ATOM   3640 C CB   . ALA A 1 225 ? 21.535 36.473 56.291 1.00 48.12  ? 228 ALA A CB   1 
ATOM   3641 H H    . ALA A 1 225 ? 23.014 34.571 56.482 0.00 56.02  ? 228 ALA A H    1 
ATOM   3642 H HA   . ALA A 1 225 ? 21.301 35.596 58.148 0.00 62.28  ? 228 ALA A HA   1 
ATOM   3643 H HB1  . ALA A 1 225 ? 20.793 37.089 56.400 0.00 57.73  ? 228 ALA A HB1  1 
ATOM   3644 H HB2  . ALA A 1 225 ? 22.368 36.917 56.514 0.00 57.73  ? 228 ALA A HB2  1 
ATOM   3645 H HB3  . ALA A 1 225 ? 21.566 36.152 55.376 0.00 57.73  ? 228 ALA A HB3  1 
ATOM   3646 N N    . ILE A 1 226 ? 20.013 33.558 56.086 1.00 36.56  ? 229 ILE A N    1 
ATOM   3647 C CA   . ILE A 1 226 ? 18.733 32.944 55.676 1.00 33.29  ? 229 ILE A CA   1 
ATOM   3648 C C    . ILE A 1 226 ? 18.134 32.020 56.720 1.00 36.10  ? 229 ILE A C    1 
ATOM   3649 O O    . ILE A 1 226 ? 17.013 31.531 56.520 1.00 40.79  ? 229 ILE A O    1 
ATOM   3650 C CB   . ILE A 1 226 ? 18.959 32.186 54.352 1.00 34.27  ? 229 ILE A CB   1 
ATOM   3651 C CG1  . ILE A 1 226 ? 19.975 31.035 54.548 1.00 41.18  ? 229 ILE A CG1  1 
ATOM   3652 C CG2  . ILE A 1 226 ? 19.481 33.131 53.248 1.00 37.57  ? 229 ILE A CG2  1 
ATOM   3653 C CD1  . ILE A 1 226 ? 20.017 30.072 53.308 1.00 44.09  ? 229 ILE A CD1  1 
ATOM   3654 H H    . ILE A 1 226 ? 20.718 33.187 55.762 0.00 43.85  ? 229 ILE A H    1 
ATOM   3655 H HA   . ILE A 1 226 ? 18.072 33.641 55.544 0.00 39.92  ? 229 ILE A HA   1 
ATOM   3656 H HB   . ILE A 1 226 ? 18.101 31.824 54.081 0.00 41.11  ? 229 ILE A HB   1 
ATOM   3657 H HG12 . ILE A 1 226 ? 20.861 31.409 54.672 0.00 49.40  ? 229 ILE A HG12 1 
ATOM   3658 H HG13 . ILE A 1 226 ? 19.722 30.516 55.327 0.00 49.40  ? 229 ILE A HG13 1 
ATOM   3659 H HG21 . ILE A 1 226 ? 19.532 32.642 52.412 0.00 45.06  ? 229 ILE A HG21 1 
ATOM   3660 H HG22 . ILE A 1 226 ? 18.871 33.879 53.157 0.00 45.06  ? 229 ILE A HG22 1 
ATOM   3661 H HG23 . ILE A 1 226 ? 20.362 33.451 53.497 0.00 45.06  ? 229 ILE A HG23 1 
ATOM   3662 H HD11 . ILE A 1 226 ? 20.622 29.339 53.498 0.00 52.88  ? 229 ILE A HD11 1 
ATOM   3663 H HD12 . ILE A 1 226 ? 19.124 29.731 53.144 0.00 52.88  ? 229 ILE A HD12 1 
ATOM   3664 H HD13 . ILE A 1 226 ? 20.329 30.567 52.535 0.00 52.88  ? 229 ILE A HD13 1 
ATOM   3665 N N    . PHE A 1 227 ? 18.870 31.717 57.803 1.00 40.85  ? 230 PHE A N    1 
ATOM   3666 C CA   . PHE A 1 227 ? 18.373 30.865 58.880 1.00 42.56  ? 230 PHE A CA   1 
ATOM   3667 C C    . PHE A 1 227 ? 17.865 31.716 60.030 1.00 44.96  ? 230 PHE A C    1 
ATOM   3668 O O    . PHE A 1 227 ? 18.444 32.759 60.346 1.00 44.15  ? 230 PHE A O    1 
ATOM   3669 C CB   . PHE A 1 227 ? 19.467 29.939 59.411 1.00 45.23  ? 230 PHE A CB   1 
ATOM   3670 C CG   . PHE A 1 227 ? 19.903 28.909 58.415 1.00 47.83  ? 230 PHE A CG   1 
ATOM   3671 C CD1  . PHE A 1 227 ? 19.251 27.691 58.329 1.00 48.66  ? 230 PHE A CD1  1 
ATOM   3672 C CD2  . PHE A 1 227 ? 20.920 29.190 57.511 1.00 57.45  ? 230 PHE A CD2  1 
ATOM   3673 C CE1  . PHE A 1 227 ? 19.638 26.747 57.395 1.00 58.99  ? 230 PHE A CE1  1 
ATOM   3674 C CE2  . PHE A 1 227 ? 21.311 28.253 56.570 1.00 58.27  ? 230 PHE A CE2  1 
ATOM   3675 C CZ   . PHE A 1 227 ? 20.671 27.027 56.507 1.00 56.91  ? 230 PHE A CZ   1 
ATOM   3676 H H    . PHE A 1 227 ? 19.672 32.001 57.931 0.00 49.01  ? 230 PHE A H    1 
ATOM   3677 H HA   . PHE A 1 227 ? 17.646 30.326 58.532 0.00 51.06  ? 230 PHE A HA   1 
ATOM   3678 H HB2  . PHE A 1 227 ? 20.242 30.472 59.648 0.00 54.26  ? 230 PHE A HB2  1 
ATOM   3679 H HB3  . PHE A 1 227 ? 19.132 29.474 60.194 0.00 54.26  ? 230 PHE A HB3  1 
ATOM   3680 H HD1  . PHE A 1 227 ? 18.545 27.506 58.905 0.00 58.37  ? 230 PHE A HD1  1 
ATOM   3681 H HD2  . PHE A 1 227 ? 21.344 30.017 57.539 0.00 68.92  ? 230 PHE A HD2  1 
ATOM   3682 H HE1  . PHE A 1 227 ? 19.207 25.924 57.361 0.00 70.76  ? 230 PHE A HE1  1 
ATOM   3683 H HE2  . PHE A 1 227 ? 22.003 28.448 55.979 0.00 69.90  ? 230 PHE A HE2  1 
ATOM   3684 H HZ   . PHE A 1 227 ? 20.930 26.396 55.876 0.00 68.27  ? 230 PHE A HZ   1 
ATOM   3685 N N    . GLY A 1 228 ? 16.790 31.260 60.657 1.00 49.13  ? 231 GLY A N    1 
ATOM   3686 C CA   . GLY A 1 228 ? 16.351 31.901 61.873 1.00 55.13  ? 231 GLY A CA   1 
ATOM   3687 C C    . GLY A 1 228 ? 17.411 31.807 62.957 1.00 67.33  ? 231 GLY A C    1 
ATOM   3688 O O    . GLY A 1 228 ? 18.305 30.972 62.919 1.00 50.38  ? 231 GLY A O    1 
ATOM   3689 H H    . GLY A 1 228 ? 16.311 30.594 60.401 0.00 58.94  ? 231 GLY A H    1 
ATOM   3690 H HA2  . GLY A 1 228 ? 16.166 32.837 61.699 0.00 66.14  ? 231 GLY A HA2  1 
ATOM   3691 H HA3  . GLY A 1 228 ? 15.541 31.473 62.192 0.00 66.14  ? 231 GLY A HA3  1 
ATOM   3692 N N    . GLU A 1 229 ? 17.341 32.708 63.919 1.00 61.58  ? 232 GLU A N    1 
ATOM   3693 C CA   . GLU A 1 229 ? 18.273 32.652 65.039 1.00 71.04  ? 232 GLU A CA   1 
ATOM   3694 C C    . GLU A 1 229 ? 17.796 31.565 66.002 1.00 70.30  ? 232 GLU A C    1 
ATOM   3695 O O    . GLU A 1 229 ? 16.686 31.646 66.539 1.00 68.52  ? 232 GLU A O    1 
ATOM   3696 C CB   . GLU A 1 229 ? 18.364 34.023 65.714 1.00 75.59  ? 232 GLU A CB   1 
ATOM   3697 C CG   . GLU A 1 229 ? 19.587 34.221 66.619 1.00 74.01  ? 232 GLU A CG   1 
ATOM   3698 C CD   . GLU A 1 229 ? 19.736 35.672 67.101 1.00 76.60  ? 232 GLU A CD   1 
ATOM   3699 O OE1  . GLU A 1 229 ? 18.715 36.396 67.106 1.00 64.42  ? 232 GLU A OE1  1 
ATOM   3700 O OE2  . GLU A 1 229 ? 20.853 36.068 67.527 1.00 62.55  ? 232 GLU A OE2  1 
ATOM   3701 H H    . GLU A 1 229 ? 16.774 33.354 63.950 0.00 73.87  ? 232 GLU A H    1 
ATOM   3702 H HA   . GLU A 1 229 ? 19.166 32.421 64.740 0.00 85.23  ? 232 GLU A HA   1 
ATOM   3703 H HB2  . GLU A 1 229 ? 18.401 34.703 65.023 0.00 90.69  ? 232 GLU A HB2  1 
ATOM   3704 H HB3  . GLU A 1 229 ? 17.574 34.149 66.262 0.00 90.69  ? 232 GLU A HB3  1 
ATOM   3705 H HG2  . GLU A 1 229 ? 19.499 33.652 67.399 0.00 88.79  ? 232 GLU A HG2  1 
ATOM   3706 H HG3  . GLU A 1 229 ? 20.388 33.985 66.125 0.00 88.79  ? 232 GLU A HG3  1 
ATOM   3707 N N    . ALA A 1 230 ? 18.611 30.533 66.202 1.00 56.14  ? 233 ALA A N    1 
ATOM   3708 C CA   . ALA A 1 230 ? 18.190 29.384 67.000 1.00 64.80  ? 233 ALA A CA   1 
ATOM   3709 C C    . ALA A 1 230 ? 19.365 28.829 67.785 1.00 65.04  ? 233 ALA A C    1 
ATOM   3710 O O    . ALA A 1 230 ? 20.528 29.011 67.420 1.00 69.12  ? 233 ALA A O    1 
ATOM   3711 C CB   . ALA A 1 230 ? 17.584 28.273 66.125 1.00 79.07  ? 233 ALA A CB   1 
ATOM   3712 H H    . ALA A 1 230 ? 19.409 30.474 65.888 0.00 67.34  ? 233 ALA A H    1 
ATOM   3713 H HA   . ALA A 1 230 ? 17.522 29.684 67.636 0.00 77.74  ? 233 ALA A HA   1 
ATOM   3714 H HB1  . ALA A 1 230 ? 17.320 27.533 66.693 0.00 94.87  ? 233 ALA A HB1  1 
ATOM   3715 H HB2  . ALA A 1 230 ? 16.810 28.625 65.659 0.00 94.87  ? 233 ALA A HB2  1 
ATOM   3716 H HB3  . ALA A 1 230 ? 18.250 27.977 65.485 0.00 94.87  ? 233 ALA A HB3  1 
ATOM   3717 N N    . GLU A 1 231 ? 19.044 28.151 68.887 1.00 60.72  ? 234 GLU A N    1 
ATOM   3718 C CA   . GLU A 1 231 ? 20.068 27.582 69.761 1.00 72.72  ? 234 GLU A CA   1 
ATOM   3719 C C    . GLU A 1 231 ? 20.471 26.191 69.269 1.00 81.12  ? 234 GLU A C    1 
ATOM   3720 O O    . GLU A 1 231 ? 19.756 25.210 69.503 1.00 85.74  ? 234 GLU A O    1 
ATOM   3721 C CB   . GLU A 1 231 ? 19.578 27.493 71.206 1.00 64.40  ? 234 GLU A CB   1 
ATOM   3722 C CG   . GLU A 1 231 ? 20.690 27.274 72.192 1.00 67.20  ? 234 GLU A CG   1 
ATOM   3723 C CD   . GLU A 1 231 ? 21.674 28.440 72.188 1.00 65.11  ? 234 GLU A CD   1 
ATOM   3724 O OE1  . GLU A 1 231 ? 21.197 29.579 72.123 1.00 63.60  ? 234 GLU A OE1  1 
ATOM   3725 O OE2  . GLU A 1 231 ? 22.888 28.230 72.251 1.00 65.74  ? 234 GLU A OE2  1 
ATOM   3726 H H    . GLU A 1 231 ? 18.238 28.007 69.150 0.00 72.85  ? 234 GLU A H    1 
ATOM   3727 H HA   . GLU A 1 231 ? 20.845 28.162 69.751 0.00 87.25  ? 234 GLU A HA   1 
ATOM   3728 H HB2  . GLU A 1 231 ? 19.131 28.322 71.438 0.00 77.26  ? 234 GLU A HB2  1 
ATOM   3729 H HB3  . GLU A 1 231 ? 18.960 26.750 71.283 0.00 77.26  ? 234 GLU A HB3  1 
ATOM   3730 H HG2  . GLU A 1 231 ? 20.317 27.192 73.083 0.00 80.62  ? 234 GLU A HG2  1 
ATOM   3731 H HG3  . GLU A 1 231 ? 21.172 26.466 71.958 0.00 80.62  ? 234 GLU A HG3  1 
HETATM 3732 C C52  . LI1 B 2 .   ? 13.331 60.170 25.152 1.00 59.18  ? 301 LI1 A C52  1 
HETATM 3733 C C53  . LI1 B 2 .   ? 13.047 60.049 23.629 1.00 57.12  ? 301 LI1 A C53  1 
HETATM 3734 C C55  . LI1 B 2 .   ? 14.381 60.193 22.861 1.00 58.90  ? 301 LI1 A C55  1 
HETATM 3735 C C56  . LI1 B 2 .   ? 14.085 60.275 21.339 1.00 49.52  ? 301 LI1 A C56  1 
HETATM 3736 C C57  . LI1 B 2 .   ? 15.348 59.994 20.483 1.00 71.79  ? 301 LI1 A C57  1 
HETATM 3737 C C58  . LI1 B 2 .   ? 14.985 60.005 18.970 1.00 54.24  ? 301 LI1 A C58  1 
HETATM 3738 C C46  . LI1 C 2 .   ? 4.976  61.528 20.143 1.00 72.88  ? 302 LI1 A C46  1 
HETATM 3739 C C47  . LI1 C 2 .   ? 4.082  61.582 21.433 1.00 67.25  ? 302 LI1 A C47  1 
HETATM 3740 C C48  . LI1 C 2 .   ? 4.914  61.201 22.683 1.00 61.62  ? 302 LI1 A C48  1 
HETATM 3741 C C49  . LI1 C 2 .   ? 5.366  59.756 22.538 1.00 79.67  ? 302 LI1 A C49  1 
HETATM 3742 C C50  . LI1 C 2 .   ? 4.098  61.371 23.981 1.00 57.75  ? 302 LI1 A C50  1 
HETATM 3743 C C51  . LI1 C 2 .   ? 4.926  61.016 25.257 1.00 61.33  ? 302 LI1 A C51  1 
HETATM 3744 C C52  . LI1 C 2 .   ? 4.038  61.262 26.508 1.00 61.03  ? 302 LI1 A C52  1 
HETATM 3745 C C53  . LI1 C 2 .   ? 4.890  61.562 27.772 1.00 69.78  ? 302 LI1 A C53  1 
HETATM 3746 C C55  . LI1 C 2 .   ? 6.097  60.589 27.832 1.00 78.30  ? 302 LI1 A C55  1 
HETATM 3747 C C56  . LI1 C 2 .   ? 7.120  61.067 28.903 1.00 98.33  ? 302 LI1 A C56  1 
HETATM 3748 C C57  . LI1 C 2 .   ? 8.368  60.138 28.952 1.00 77.73  ? 302 LI1 A C57  1 
HETATM 3749 C C58  . LI1 C 2 .   ? 9.240  60.388 30.224 1.00 81.35  ? 302 LI1 A C58  1 
HETATM 3750 C C59  . LI1 C 2 .   ? 8.781  61.664 30.972 1.00 103.83 ? 302 LI1 A C59  1 
HETATM 3751 C C60  . LI1 C 2 .   ? 9.193  59.191 31.204 1.00 63.63  ? 302 LI1 A C60  1 
HETATM 3752 H H461 . LI1 C 2 .   ? 5.944  61.988 20.339 1.00 87.44  ? 302 LI1 A H461 1 
HETATM 3753 H H462 . LI1 C 2 .   ? 5.118  60.494 19.828 1.00 87.44  ? 302 LI1 A H462 1 
HETATM 3754 H H471 . LI1 C 2 .   ? 3.691  62.589 21.556 1.00 80.69  ? 302 LI1 A H471 1 
HETATM 3755 H H472 . LI1 C 2 .   ? 3.256  60.882 21.325 1.00 80.69  ? 302 LI1 A H472 1 
HETATM 3756 H H48  . LI1 C 2 .   ? 5.775  61.866 22.753 1.00 73.93  ? 302 LI1 A H48  1 
HETATM 3757 C C50  . LI1 D 2 .   ? 23.830 22.175 24.058 1.00 59.86  ? 303 LI1 A C50  1 
HETATM 3758 C C51  . LI1 D 2 .   ? 23.155 22.856 25.293 1.00 62.57  ? 303 LI1 A C51  1 
HETATM 3759 C C52  . LI1 D 2 .   ? 23.793 22.393 26.628 1.00 58.22  ? 303 LI1 A C52  1 
HETATM 3760 C C53  . LI1 D 2 .   ? 22.852 21.388 27.364 1.00 69.65  ? 303 LI1 A C53  1 
HETATM 3761 C C55  . LI1 D 2 .   ? 22.617 21.865 28.822 1.00 66.93  ? 303 LI1 A C55  1 
HETATM 3762 C C56  . LI1 D 2 .   ? 22.780 20.720 29.864 1.00 64.14  ? 303 LI1 A C56  1 
HETATM 3763 C C57  . LI1 D 2 .   ? 24.146 20.854 30.597 1.00 62.27  ? 303 LI1 A C57  1 
HETATM 3764 C C58  . LI1 D 2 .   ? 23.982 20.572 32.123 1.00 60.87  ? 303 LI1 A C58  1 
HETATM 3765 C C45  . LI1 E 2 .   ? -1.266 31.010 19.164 1.00 64.13  ? 304 LI1 A C45  1 
HETATM 3766 C C46  . LI1 E 2 .   ? -2.071 30.909 20.506 1.00 63.01  ? 304 LI1 A C46  1 
HETATM 3767 C C47  . LI1 E 2 .   ? -1.168 30.927 21.784 1.00 49.35  ? 304 LI1 A C47  1 
HETATM 3768 C C48  . LI1 E 2 .   ? -2.025 31.359 22.993 1.00 54.45  ? 304 LI1 A C48  1 
HETATM 3769 C C50  . LI1 E 2 .   ? -1.244 31.221 24.307 1.00 58.39  ? 304 LI1 A C50  1 
HETATM 3770 C C51  . LI1 E 2 .   ? -2.255 31.015 25.468 1.00 57.70  ? 304 LI1 A C51  1 
HETATM 3771 C C52  . LI1 E 2 .   ? -1.609 31.216 26.870 1.00 67.70  ? 304 LI1 A C52  1 
HETATM 3772 C C53  . LI1 E 2 .   ? -2.393 32.293 27.684 1.00 66.76  ? 304 LI1 A C53  1 
HETATM 3773 C C55  . LI1 E 2 .   ? -2.349 31.991 29.213 1.00 50.45  ? 304 LI1 A C55  1 
HETATM 3774 C C56  . LI1 E 2 .   ? -2.226 33.316 30.028 1.00 73.91  ? 304 LI1 A C56  1 
HETATM 3775 C C57  . LI1 E 2 .   ? -3.050 34.463 29.378 1.00 62.71  ? 304 LI1 A C57  1 
HETATM 3776 C C58  . LI1 E 2 .   ? -3.488 35.502 30.448 1.00 64.08  ? 304 LI1 A C58  1 
HETATM 3777 H H451 . LI1 E 2 .   ? -1.193 32.052 18.861 1.00 76.94  ? 304 LI1 A H451 1 
HETATM 3778 H H452 . LI1 E 2 .   ? -0.269 30.595 19.299 1.00 76.94  ? 304 LI1 A H452 1 
HETATM 3779 H H461 . LI1 E 2 .   ? -2.638 29.978 20.498 1.00 75.59  ? 304 LI1 A H461 1 
HETATM 3780 H H462 . LI1 E 2 .   ? -2.759 31.753 20.559 1.00 75.59  ? 304 LI1 A H462 1 
HETATM 3781 C C45  . LI1 F 2 .   ? 26.406 60.025 53.463 1.00 77.65  ? 305 LI1 A C45  1 
HETATM 3782 C C46  . LI1 F 2 .   ? 25.243 60.420 52.486 1.00 73.26  ? 305 LI1 A C46  1 
HETATM 3783 C C47  . LI1 F 2 .   ? 24.503 59.134 51.999 1.00 74.00  ? 305 LI1 A C47  1 
HETATM 3784 C C48  . LI1 F 2 .   ? 23.699 59.434 50.712 1.00 71.00  ? 305 LI1 A C48  1 
HETATM 3785 C C50  . LI1 F 2 .   ? 24.646 59.784 49.555 1.00 73.32  ? 305 LI1 A C50  1 
HETATM 3786 C C51  . LI1 F 2 .   ? 23.823 60.236 48.313 1.00 65.72  ? 305 LI1 A C51  1 
HETATM 3787 C C52  . LI1 F 2 .   ? 23.596 59.008 47.385 1.00 84.37  ? 305 LI1 A C52  1 
HETATM 3788 C C53  . LI1 F 2 .   ? 22.886 59.452 46.079 1.00 84.37  ? 305 LI1 A C53  1 
HETATM 3789 C C55  . LI1 F 2 .   ? 23.871 60.200 45.146 1.00 70.60  ? 305 LI1 A C55  1 
HETATM 3790 C C56  . LI1 F 2 .   ? 23.097 60.652 43.880 1.00 69.41  ? 305 LI1 A C56  1 
HETATM 3791 C C57  . LI1 F 2 .   ? 23.638 59.941 42.617 1.00 71.19  ? 305 LI1 A C57  1 
HETATM 3792 C C58  . LI1 F 2 .   ? 23.089 60.654 41.350 1.00 69.54  ? 305 LI1 A C58  1 
HETATM 3793 C C59  . LI1 F 2 .   ? 22.713 59.603 40.274 1.00 75.43  ? 305 LI1 A C59  1 
HETATM 3794 H H451 . LI1 F 2 .   ? 26.008 59.442 54.291 1.00 93.16  ? 305 LI1 A H451 1 
HETATM 3795 H H452 . LI1 F 2 .   ? 27.152 59.439 52.928 1.00 93.16  ? 305 LI1 A H452 1 
HETATM 3796 H H461 . LI1 F 2 .   ? 24.538 61.068 53.006 1.00 87.89  ? 305 LI1 A H461 1 
HETATM 3797 H H462 . LI1 F 2 .   ? 25.656 60.948 51.626 1.00 87.89  ? 305 LI1 A H462 1 
HETATM 3798 H H471 . LI1 F 2 .   ? 23.823 58.795 52.777 1.00 88.78  ? 305 LI1 A H471 1 
HETATM 3799 H H472 . LI1 F 2 .   ? 25.235 58.355 51.792 1.00 88.78  ? 305 LI1 A H472 1 
HETATM 3800 C C46  . LI1 G 2 .   ? 27.278 51.174 45.295 1.00 70.28  ? 306 LI1 A C46  1 
HETATM 3801 C C47  . LI1 G 2 .   ? 26.839 52.383 44.419 1.00 100.32 ? 306 LI1 A C47  1 
HETATM 3802 C C48  . LI1 G 2 .   ? 26.422 51.891 43.016 1.00 100.53 ? 306 LI1 A C48  1 
HETATM 3803 C C50  . LI1 G 2 .   ? 27.587 52.130 42.045 1.00 101.14 ? 306 LI1 A C50  1 
HETATM 3804 C C51  . LI1 G 2 .   ? 27.045 52.372 40.605 1.00 82.46  ? 306 LI1 A C51  1 
HETATM 3805 C C52  . LI1 G 2 .   ? 28.233 52.233 39.614 1.00 85.96  ? 306 LI1 A C52  1 
HETATM 3806 C C53  . LI1 G 2 .   ? 27.758 52.702 38.219 1.00 87.23  ? 306 LI1 A C53  1 
HETATM 3807 C C55  . LI1 G 2 .   ? 26.506 51.886 37.835 1.00 72.37  ? 306 LI1 A C55  1 
HETATM 3808 C C56  . LI1 G 2 .   ? 26.385 51.859 36.289 1.00 77.21  ? 306 LI1 A C56  1 
HETATM 3809 C C57  . LI1 G 2 .   ? 27.086 50.608 35.719 1.00 66.01  ? 306 LI1 A C57  1 
HETATM 3810 C C58  . LI1 G 2 .   ? 27.284 50.840 34.193 1.00 72.58  ? 306 LI1 A C58  1 
HETATM 3811 C C59  . LI1 G 2 .   ? 26.347 51.986 33.736 1.00 60.27  ? 306 LI1 A C59  1 
HETATM 3812 C C60  . LI1 G 2 .   ? 26.986 49.563 33.376 1.00 64.45  ? 306 LI1 A C60  1 
HETATM 3813 H H461 . LI1 G 2 .   ? 27.717 50.407 44.655 1.00 84.32  ? 306 LI1 A H461 1 
HETATM 3814 H H462 . LI1 G 2 .   ? 28.019 51.501 46.027 1.00 84.32  ? 306 LI1 A H462 1 
HETATM 3815 H H471 . LI1 G 2 .   ? 27.669 53.080 44.325 1.00 120.36 ? 306 LI1 A H471 1 
HETATM 3816 H H472 . LI1 G 2 .   ? 25.997 52.884 44.892 1.00 120.36 ? 306 LI1 A H472 1 
HETATM 3817 C C18  . OLC H 3 .   ? 20.235 19.415 32.756 1.00 70.57  ? 307 OLC A C18  1 
HETATM 3818 C C10  . OLC H 3 .   ? 12.755 20.984 35.812 1.00 53.55  ? 307 OLC A C10  1 
HETATM 3819 C C9   . OLC H 3 .   ? 12.204 21.084 37.033 1.00 57.83  ? 307 OLC A C9   1 
HETATM 3820 C C17  . OLC H 3 .   ? 19.456 19.891 34.007 1.00 72.21  ? 307 OLC A C17  1 
HETATM 3821 C C11  . OLC H 3 .   ? 13.203 22.159 34.913 1.00 62.76  ? 307 OLC A C11  1 
HETATM 3822 C C8   . OLC H 3 .   ? 11.646 21.915 38.223 1.00 60.66  ? 307 OLC A C8   1 
HETATM 3823 C C24  . OLC H 3 .   ? 11.266 23.015 49.250 1.00 71.72  ? 307 OLC A C24  1 
HETATM 3824 C C16  . OLC H 3 .   ? 18.478 21.005 33.582 1.00 65.25  ? 307 OLC A C16  1 
HETATM 3825 C C12  . OLC H 3 .   ? 14.678 22.482 35.264 1.00 65.94  ? 307 OLC A C12  1 
HETATM 3826 C C7   . OLC H 3 .   ? 12.313 21.345 39.491 1.00 65.73  ? 307 OLC A C7   1 
HETATM 3827 C C15  . OLC H 3 .   ? 18.025 21.849 34.792 1.00 62.94  ? 307 OLC A C15  1 
HETATM 3828 C C13  . OLC H 3 .   ? 15.584 21.386 34.644 1.00 64.72  ? 307 OLC A C13  1 
HETATM 3829 C C6   . OLC H 3 .   ? 11.877 22.091 40.781 1.00 67.78  ? 307 OLC A C6   1 
HETATM 3830 C C14  . OLC H 3 .   ? 16.849 21.167 35.511 1.00 63.94  ? 307 OLC A C14  1 
HETATM 3831 C C5   . OLC H 3 .   ? 12.134 23.616 40.719 1.00 55.26  ? 307 OLC A C5   1 
HETATM 3832 C C4   . OLC H 3 .   ? 11.618 24.188 42.070 1.00 47.71  ? 307 OLC A C4   1 
HETATM 3833 C C3   . OLC H 3 .   ? 12.731 24.028 43.133 1.00 51.51  ? 307 OLC A C3   1 
HETATM 3834 C C2   . OLC H 3 .   ? 12.214 24.643 44.455 1.00 44.81  ? 307 OLC A C2   1 
HETATM 3835 C C21  . OLC H 3 .   ? 13.275 23.844 48.031 1.00 52.18  ? 307 OLC A C21  1 
HETATM 3836 C C1   . OLC H 3 .   ? 13.085 24.224 45.674 1.00 49.09  ? 307 OLC A C1   1 
HETATM 3837 C C22  . OLC H 3 .   ? 12.380 24.080 49.255 1.00 62.47  ? 307 OLC A C22  1 
HETATM 3838 O O19  . OLC H 3 .   ? 14.249 24.055 45.602 1.00 52.62  ? 307 OLC A O19  1 
HETATM 3839 O O25  . OLC H 3 .   ? 10.300 23.273 50.246 1.00 63.42  ? 307 OLC A O25  1 
HETATM 3840 O O23  . OLC H 3 .   ? 13.174 23.991 50.403 1.00 80.54  ? 307 OLC A O23  1 
HETATM 3841 O O20  . OLC H 3 .   ? 12.458 24.099 46.916 1.00 50.99  ? 307 OLC A O20  1 
HETATM 3842 H H18  . OLC H 3 .   ? 20.770 20.256 32.320 0.00 84.67  ? 307 OLC A H18  1 
HETATM 3843 H H18A . OLC H 3 .   ? 20.946 18.643 33.044 0.00 84.67  ? 307 OLC A H18A 1 
HETATM 3844 H H18B . OLC H 3 .   ? 19.537 19.011 32.026 0.00 84.67  ? 307 OLC A H18B 1 
HETATM 3845 H H10  . OLC H 3 .   ? 13.808 20.730 35.903 0.00 64.24  ? 307 OLC A H10  1 
HETATM 3846 H H9   . OLC H 3 .   ? 12.544 22.116 37.003 0.00 69.38  ? 307 OLC A H9   1 
HETATM 3847 H H17  . OLC H 3 .   ? 20.154 20.279 34.748 0.00 86.63  ? 307 OLC A H17  1 
HETATM 3848 H H17A . OLC H 3 .   ? 18.901 19.057 34.433 0.00 86.63  ? 307 OLC A H17A 1 
HETATM 3849 H H11  . OLC H 3 .   ? 13.124 21.875 33.862 0.00 75.29  ? 307 OLC A H11  1 
HETATM 3850 H H11A . OLC H 3 .   ? 12.576 23.032 35.101 0.00 75.29  ? 307 OLC A H11A 1 
HETATM 3851 H H8   . OLC H 3 .   ? 10.563 21.809 38.285 0.00 72.77  ? 307 OLC A H8   1 
HETATM 3852 H H8A  . OLC H 3 .   ? 11.902 22.968 38.102 0.00 72.77  ? 307 OLC A H8A  1 
HETATM 3853 H H24  . OLC H 3 .   ? 11.710 22.038 49.432 0.00 86.04  ? 307 OLC A H24  1 
HETATM 3854 H H24A . OLC H 3 .   ? 10.780 23.017 48.275 0.00 86.04  ? 307 OLC A H24A 1 
HETATM 3855 H H16  . OLC H 3 .   ? 18.973 21.655 32.861 0.00 78.28  ? 307 OLC A H16  1 
HETATM 3856 H H16A . OLC H 3 .   ? 17.602 20.549 33.120 0.00 78.28  ? 307 OLC A H16A 1 
HETATM 3857 H H12  . OLC H 3 .   ? 14.947 23.455 34.856 0.00 79.11  ? 307 OLC A H12  1 
HETATM 3858 H H12A . OLC H 3 .   ? 14.804 22.495 36.345 0.00 79.11  ? 307 OLC A H12A 1 
HETATM 3859 H H7   . OLC H 3 .   ? 12.040 20.294 39.587 0.00 78.86  ? 307 OLC A H7   1 
HETATM 3860 H H7A  . OLC H 3 .   ? 13.394 21.432 39.387 0.00 78.86  ? 307 OLC A H7A  1 
HETATM 3861 H H15  . OLC H 3 .   ? 17.712 22.833 34.446 0.00 75.50  ? 307 OLC A H15  1 
HETATM 3862 H H15A . OLC H 3 .   ? 18.857 21.957 35.486 0.00 75.50  ? 307 OLC A H15A 1 
HETATM 3863 H H13  . OLC H 3 .   ? 15.884 21.694 33.644 0.00 77.65  ? 307 OLC A H13  1 
HETATM 3864 H H13A . OLC H 3 .   ? 15.025 20.453 34.584 0.00 77.65  ? 307 OLC A H13A 1 
HETATM 3865 H H6   . OLC H 3 .   ? 10.810 21.925 40.934 0.00 81.32  ? 307 OLC A H6   1 
HETATM 3866 H H6A  . OLC H 3 .   ? 12.432 21.680 41.624 0.00 81.32  ? 307 OLC A H6A  1 
HETATM 3867 H H14  . OLC H 3 .   ? 16.707 21.611 36.496 0.00 76.71  ? 307 OLC A H14  1 
HETATM 3868 H H14A . OLC H 3 .   ? 17.047 20.100 35.618 0.00 76.71  ? 307 OLC A H14A 1 
HETATM 3869 H H5   . OLC H 3 .   ? 11.588 24.059 39.886 0.00 66.29  ? 307 OLC A H5   1 
HETATM 3870 H H5A  . OLC H 3 .   ? 13.199 23.817 40.603 0.00 66.29  ? 307 OLC A H5A  1 
HETATM 3871 H H4   . OLC H 3 .   ? 11.372 25.244 41.952 0.00 57.24  ? 307 OLC A H4   1 
HETATM 3872 H H4A  . OLC H 3 .   ? 10.729 23.642 42.385 0.00 57.24  ? 307 OLC A H4A  1 
HETATM 3873 H H3   . OLC H 3 .   ? 12.956 22.972 43.279 0.00 61.79  ? 307 OLC A H3   1 
HETATM 3874 H H3A  . OLC H 3 .   ? 13.631 24.550 42.809 0.00 61.79  ? 307 OLC A H3A  1 
HETATM 3875 H H2   . OLC H 3 .   ? 12.231 25.728 44.368 0.00 53.76  ? 307 OLC A H2   1 
HETATM 3876 H H2A  . OLC H 3 .   ? 11.192 24.308 44.623 0.00 53.76  ? 307 OLC A H2A  1 
HETATM 3877 H H21  . OLC H 3 .   ? 14.126 24.524 48.044 0.00 62.60  ? 307 OLC A H21  1 
HETATM 3878 H H21A . OLC H 3 .   ? 13.633 22.814 48.013 0.00 62.60  ? 307 OLC A H21A 1 
HETATM 3879 H H22  . OLC H 3 .   ? 11.916 25.066 49.233 0.00 74.94  ? 307 OLC A H22  1 
HETATM 3880 H HO25 . OLC H 3 .   ? 10.017 22.457 50.633 0.00 76.08  ? 307 OLC A HO25 1 
HETATM 3881 H HO23 . OLC H 3 .   ? 12.627 24.090 51.173 0.00 96.63  ? 307 OLC A HO23 1 
HETATM 3882 C C18  . OLC I 3 .   ? 6.294  32.456 41.733 1.00 72.69  ? 308 OLC A C18  1 
HETATM 3883 C C10  . OLC I 3 .   ? 8.054  29.194 32.542 1.00 54.94  ? 308 OLC A C10  1 
HETATM 3884 C C9   . OLC I 3 .   ? 8.072  28.950 31.222 1.00 64.94  ? 308 OLC A C9   1 
HETATM 3885 C C17  . OLC I 3 .   ? 5.805  32.495 40.274 1.00 63.72  ? 308 OLC A C17  1 
HETATM 3886 C C11  . OLC I 3 .   ? 6.855  29.695 33.366 1.00 56.13  ? 308 OLC A C11  1 
HETATM 3887 C C8   . OLC I 3 .   ? 7.432  28.891 29.822 1.00 63.62  ? 308 OLC A C8   1 
HETATM 3888 C C24  . OLC I 3 .   ? 4.840  32.387 19.082 1.00 88.79  ? 308 OLC A C24  1 
HETATM 3889 C C16  . OLC I 3 .   ? 6.501  31.368 39.480 1.00 60.34  ? 308 OLC A C16  1 
HETATM 3890 C C12  . OLC I 3 .   ? 7.317  29.718 34.846 1.00 53.29  ? 308 OLC A C12  1 
HETATM 3891 C C7   . OLC I 3 .   ? 7.019  30.301 29.315 1.00 55.68  ? 308 OLC A C7   1 
HETATM 3892 C C15  . OLC I 3 .   ? 6.120  31.502 37.983 1.00 60.95  ? 308 OLC A C15  1 
HETATM 3893 C C13  . OLC I 3 .   ? 6.282  30.456 35.704 1.00 42.21  ? 308 OLC A C13  1 
HETATM 3894 C C6   . OLC I 3 .   ? 6.100  30.048 28.094 1.00 67.34  ? 308 OLC A C6   1 
HETATM 3895 C C14  . OLC I 3 .   ? 6.662  30.288 37.197 1.00 53.94  ? 308 OLC A C14  1 
HETATM 3896 C C5   . OLC I 3 .   ? 5.667  31.369 27.433 1.00 61.61  ? 308 OLC A C5   1 
HETATM 3897 C C4   . OLC I 3 .   ? 4.598  30.974 26.382 1.00 64.60  ? 308 OLC A C4   1 
HETATM 3898 C C3   . OLC I 3 .   ? 4.532  32.009 25.228 1.00 66.33  ? 308 OLC A C3   1 
HETATM 3899 C C2   . OLC I 3 .   ? 3.870  31.265 24.039 1.00 70.34  ? 308 OLC A C2   1 
HETATM 3900 C C21  . OLC I 3 .   ? 3.052  32.964 20.758 1.00 75.38  ? 308 OLC A C21  1 
HETATM 3901 C C1   . OLC I 3 .   ? 3.304  32.251 22.997 1.00 69.97  ? 308 OLC A C1   1 
HETATM 3902 C C22  . OLC I 3 .   ? 3.330  32.448 19.342 1.00 81.49  ? 308 OLC A C22  1 
HETATM 3903 O O19  . OLC I 3 .   ? 2.406  32.975 23.279 1.00 79.90  ? 308 OLC A O19  1 
HETATM 3904 O O25  . OLC I 3 .   ? 5.373  33.692 19.102 1.00 94.07  ? 308 OLC A O25  1 
HETATM 3905 O O23  . OLC I 3 .   ? 2.791  31.167 19.210 1.00 94.32  ? 308 OLC A O23  1 
HETATM 3906 O O20  . OLC I 3 .   ? 3.844  32.254 21.694 1.00 70.72  ? 308 OLC A O20  1 
HETATM 3907 H H18  . OLC I 3 .   ? 5.913  33.324 42.266 0.00 87.21  ? 308 OLC A H18  1 
HETATM 3908 H H18A . OLC I 3 .   ? 5.933  31.548 42.212 0.00 87.21  ? 308 OLC A H18A 1 
HETATM 3909 H H18B . OLC I 3 .   ? 7.382  32.467 41.751 0.00 87.21  ? 308 OLC A H18B 1 
HETATM 3910 H H10  . OLC I 3 .   ? 7.959  28.258 33.087 0.00 65.91  ? 308 OLC A H10  1 
HETATM 3911 H H9   . OLC I 3 .   ? 6.987  28.927 31.278 0.00 77.91  ? 308 OLC A H9   1 
HETATM 3912 H H17  . OLC I 3 .   ? 4.727  32.348 40.247 0.00 76.44  ? 308 OLC A H17  1 
HETATM 3913 H H17A . OLC I 3 .   ? 6.052  33.459 39.832 0.00 76.44  ? 308 OLC A H17A 1 
HETATM 3914 H H11  . OLC I 3 .   ? 6.569  30.697 33.045 0.00 67.33  ? 308 OLC A H11  1 
HETATM 3915 H H11A . OLC I 3 .   ? 6.007  29.019 33.247 0.00 67.33  ? 308 OLC A H11A 1 
HETATM 3916 H H8   . OLC I 3 .   ? 6.546  28.258 29.866 0.00 76.33  ? 308 OLC A H8   1 
HETATM 3917 H H8A  . OLC I 3 .   ? 8.151  28.461 29.124 0.00 76.33  ? 308 OLC A H8A  1 
HETATM 3918 H H24  . OLC I 3 .   ? 5.022  31.935 18.108 0.00 106.53 ? 308 OLC A H24  1 
HETATM 3919 H H24A . OLC I 3 .   ? 5.318  31.787 19.855 0.00 106.53 ? 308 OLC A H24A 1 
HETATM 3920 H H16  . OLC I 3 .   ? 7.582  31.456 39.592 0.00 72.39  ? 308 OLC A H16  1 
HETATM 3921 H H16A . OLC I 3 .   ? 6.174  30.399 39.857 0.00 72.39  ? 308 OLC A H16A 1 
HETATM 3922 H H12  . OLC I 3 .   ? 7.424  28.697 35.208 0.00 63.93  ? 308 OLC A H12  1 
HETATM 3923 H H12A . OLC I 3 .   ? 8.276  30.230 34.917 0.00 63.93  ? 308 OLC A H12A 1 
HETATM 3924 H H7   . OLC I 3 .   ? 6.480  30.842 30.092 0.00 66.80  ? 308 OLC A H7   1 
HETATM 3925 H H7A  . OLC I 3 .   ? 7.899  30.872 29.019 0.00 66.80  ? 308 OLC A H7A  1 
HETATM 3926 H H15  . OLC I 3 .   ? 6.551  32.416 37.579 0.00 73.12  ? 308 OLC A H15  1 
HETATM 3927 H H15A . OLC I 3 .   ? 5.036  31.539 37.888 0.00 73.12  ? 308 OLC A H15A 1 
HETATM 3928 H H13  . OLC I 3 .   ? 5.293  30.035 35.528 0.00 50.63  ? 308 OLC A H13  1 
HETATM 3929 H H13A . OLC I 3 .   ? 6.278  31.514 35.444 0.00 50.63  ? 308 OLC A H13A 1 
HETATM 3930 H H6   . OLC I 3 .   ? 6.640  29.447 27.362 0.00 80.78  ? 308 OLC A H6   1 
HETATM 3931 H H6A  . OLC I 3 .   ? 5.213  29.509 28.423 0.00 80.78  ? 308 OLC A H6A  1 
HETATM 3932 H H14  . OLC I 3 .   ? 6.221  29.371 37.587 0.00 64.71  ? 308 OLC A H14  1 
HETATM 3933 H H14A . OLC I 3 .   ? 7.747  30.241 37.296 0.00 64.71  ? 308 OLC A H14A 1 
HETATM 3934 H H5   . OLC I 3 .   ? 5.240  32.044 28.175 0.00 73.91  ? 308 OLC A H5   1 
HETATM 3935 H H5A  . OLC I 3 .   ? 6.517  31.851 26.950 0.00 73.91  ? 308 OLC A H5A  1 
HETATM 3936 H H4   . OLC I 3 .   ? 4.850  29.997 25.970 0.00 77.50  ? 308 OLC A H4   1 
HETATM 3937 H H4A  . OLC I 3 .   ? 3.624  30.923 26.869 0.00 77.50  ? 308 OLC A H4A  1 
HETATM 3938 H H3   . OLC I 3 .   ? 3.931  32.869 25.522 0.00 79.58  ? 308 OLC A H3   1 
HETATM 3939 H H3A  . OLC I 3 .   ? 5.535  32.341 24.958 0.00 79.58  ? 308 OLC A H3A  1 
HETATM 3940 H H2   . OLC I 3 .   ? 4.615  30.633 23.558 0.00 84.39  ? 308 OLC A H2   1 
HETATM 3941 H H2A  . OLC I 3 .   ? 3.058  30.646 24.417 0.00 84.39  ? 308 OLC A H2A  1 
HETATM 3942 H H21  . OLC I 3 .   ? 3.295  34.026 20.810 0.00 90.44  ? 308 OLC A H21  1 
HETATM 3943 H H21A . OLC I 3 .   ? 1.997  32.821 20.995 0.00 90.44  ? 308 OLC A H21A 1 
HETATM 3944 H H22  . OLC I 3 .   ? 2.874  33.126 18.621 0.00 97.76  ? 308 OLC A H22  1 
HETATM 3945 H HO25 . OLC I 3 .   ? 5.845  33.851 18.298 0.00 112.87 ? 308 OLC A HO25 1 
HETATM 3946 H HO23 . OLC I 3 .   ? 2.265  30.968 19.975 0.00 113.16 ? 308 OLC A HO23 1 
HETATM 3947 C C18  . OLC J 3 .   ? 35.018 36.021 35.689 1.00 79.30  ? 309 OLC A C18  1 
HETATM 3948 C C10  . OLC J 3 .   ? 32.851 40.034 28.017 1.00 72.99  ? 309 OLC A C10  1 
HETATM 3949 C C9   . OLC J 3 .   ? 33.099 41.172 27.361 1.00 72.99  ? 309 OLC A C9   1 
HETATM 3950 C C17  . OLC J 3 .   ? 35.900 35.338 34.619 1.00 78.92  ? 309 OLC A C17  1 
HETATM 3951 C C11  . OLC J 3 .   ? 32.936 39.775 29.548 1.00 69.75  ? 309 OLC A C11  1 
HETATM 3952 C C8   . OLC J 3 .   ? 33.232 42.045 26.075 1.00 67.38  ? 309 OLC A C8   1 
HETATM 3953 C C24  . OLC J 3 .   ? 36.263 45.728 14.395 1.00 91.08  ? 309 OLC A C24  1 
HETATM 3954 C C16  . OLC J 3 .   ? 35.307 35.580 33.213 1.00 80.15  ? 309 OLC A C16  1 
HETATM 3955 C C12  . OLC J 3 .   ? 34.345 39.179 29.841 1.00 73.26  ? 309 OLC A C12  1 
HETATM 3956 C C7   . OLC J 3 .   ? 34.292 41.437 25.085 1.00 63.48  ? 309 OLC A C7   1 
HETATM 3957 C C15  . OLC J 3 .   ? 35.806 36.934 32.635 1.00 71.31  ? 309 OLC A C15  1 
HETATM 3958 C C13  . OLC J 3 .   ? 34.447 38.678 31.313 1.00 88.26  ? 309 OLC A C13  1 
HETATM 3959 C C6   . OLC J 3 .   ? 33.620 41.308 23.691 1.00 72.80  ? 309 OLC A C6   1 
HETATM 3960 C C14  . OLC J 3 .   ? 35.000 37.219 31.337 1.00 83.82  ? 309 OLC A C14  1 
HETATM 3961 C C5   . OLC J 3 .   ? 34.653 40.733 22.677 1.00 58.41  ? 309 OLC A C5   1 
HETATM 3962 C C4   . OLC J 3 .   ? 35.217 41.872 21.782 1.00 58.72  ? 309 OLC A C4   1 
HETATM 3963 C C3   . OLC J 3 .   ? 34.765 41.738 20.298 1.00 58.65  ? 309 OLC A C3   1 
HETATM 3964 C C2   . OLC J 3 .   ? 34.779 43.144 19.628 1.00 78.64  ? 309 OLC A C2   1 
HETATM 3965 C C21  . OLC J 3 .   ? 35.965 43.962 16.144 1.00 91.59  ? 309 OLC A C21  1 
HETATM 3966 C C1   . OLC J 3 .   ? 35.461 43.068 18.239 1.00 83.49  ? 309 OLC A C1   1 
HETATM 3967 C C22  . OLC J 3 .   ? 35.439 44.501 14.810 1.00 101.85 ? 309 OLC A C22  1 
HETATM 3968 O O19  . OLC J 3 .   ? 36.486 42.474 18.138 1.00 90.68  ? 309 OLC A O19  1 
HETATM 3969 O O25  . OLC J 3 .   ? 35.788 46.868 15.085 1.00 84.28  ? 309 OLC A O25  1 
HETATM 3970 O O23  . OLC J 3 .   ? 35.569 43.506 13.836 1.00 110.19 ? 309 OLC A O23  1 
HETATM 3971 O O20  . OLC J 3 .   ? 34.931 43.700 17.084 1.00 91.54  ? 309 OLC A O20  1 
HETATM 3972 H H18  . OLC J 3 .   ? 35.419 35.811 36.678 0.00 95.14  ? 309 OLC A H18  1 
HETATM 3973 H H18A . OLC J 3 .   ? 35.011 37.096 35.521 0.00 95.14  ? 309 OLC A H18A 1 
HETATM 3974 H H18B . OLC J 3 .   ? 34.002 35.638 35.621 0.00 95.14  ? 309 OLC A H18B 1 
HETATM 3975 H H10  . OLC J 3 .   ? 33.707 39.370 27.930 0.00 87.57  ? 309 OLC A H10  1 
HETATM 3976 H H9   . OLC J 3 .   ? 32.568 40.731 26.521 0.00 87.57  ? 309 OLC A H9   1 
HETATM 3977 H H17  . OLC J 3 .   ? 36.906 35.752 34.662 0.00 94.68  ? 309 OLC A H17  1 
HETATM 3978 H H17A . OLC J 3 .   ? 35.939 34.267 34.814 0.00 94.68  ? 309 OLC A H17A 1 
HETATM 3979 H H11  . OLC J 3 .   ? 32.807 40.712 30.092 0.00 83.68  ? 309 OLC A H11  1 
HETATM 3980 H H11A . OLC J 3 .   ? 32.162 39.069 29.851 0.00 83.68  ? 309 OLC A H11A 1 
HETATM 3981 H H8   . OLC J 3 .   ? 33.545 43.050 26.357 0.00 80.84  ? 309 OLC A H8   1 
HETATM 3982 H H8A  . OLC J 3 .   ? 32.265 42.093 25.575 0.00 80.84  ? 309 OLC A H8A  1 
HETATM 3983 H H24  . OLC J 3 .   ? 36.165 45.886 13.322 0.00 109.28 ? 309 OLC A H24  1 
HETATM 3984 H H24A . OLC J 3 .   ? 37.311 45.563 14.643 0.00 109.28 ? 309 OLC A H24A 1 
HETATM 3985 H H16  . OLC J 3 .   ? 35.616 34.772 32.550 0.00 96.17  ? 309 OLC A H16  1 
HETATM 3986 H H16A . OLC J 3 .   ? 34.220 35.599 33.281 0.00 96.17  ? 309 OLC A H16A 1 
HETATM 3987 H H12  . OLC J 3 .   ? 34.524 38.342 29.167 0.00 87.89  ? 309 OLC A H12  1 
HETATM 3988 H H12A . OLC J 3 .   ? 35.098 39.947 29.674 0.00 87.89  ? 309 OLC A H12A 1 
HETATM 3989 H H7   . OLC J 3 .   ? 35.159 42.094 25.019 0.00 76.16  ? 309 OLC A H7   1 
HETATM 3990 H H7A  . OLC J 3 .   ? 34.608 40.455 25.437 0.00 76.16  ? 309 OLC A H7A  1 
HETATM 3991 H H15  . OLC J 3 .   ? 36.869 36.870 32.406 0.00 85.55  ? 309 OLC A H15  1 
HETATM 3992 H H15A . OLC J 3 .   ? 35.639 37.731 33.359 0.00 85.55  ? 309 OLC A H15A 1 
HETATM 3993 H H13  . OLC J 3 .   ? 33.459 38.698 31.771 0.00 105.89 ? 309 OLC A H13  1 
HETATM 3994 H H13A . OLC J 3 .   ? 35.118 39.329 31.871 0.00 105.89 ? 309 OLC A H13A 1 
HETATM 3995 H H6   . OLC J 3 .   ? 32.764 40.637 23.759 0.00 87.34  ? 309 OLC A H6   1 
HETATM 3996 H H6A  . OLC J 3 .   ? 33.286 42.289 23.355 0.00 87.34  ? 309 OLC A H6A  1 
HETATM 3997 H H14  . OLC J 3 .   ? 34.164 36.522 31.280 0.00 100.56 ? 309 OLC A H14  1 
HETATM 3998 H H14A . OLC J 3 .   ? 35.653 37.073 30.476 0.00 100.56 ? 309 OLC A H14A 1 
HETATM 3999 H H5   . OLC J 3 .   ? 34.164 39.989 22.047 0.00 70.08  ? 309 OLC A H5   1 
HETATM 4000 H H5A  . OLC J 3 .   ? 35.472 40.265 23.223 0.00 70.08  ? 309 OLC A H5A  1 
HETATM 4001 H H4   . OLC J 3 .   ? 34.866 42.828 22.170 0.00 70.44  ? 309 OLC A H4   1 
HETATM 4002 H H4A  . OLC J 3 .   ? 36.306 41.841 21.821 0.00 70.44  ? 309 OLC A H4A  1 
HETATM 4003 H H3   . OLC J 3 .   ? 35.449 41.075 19.768 0.00 70.36  ? 309 OLC A H3   1 
HETATM 4004 H H3A  . OLC J 3 .   ? 33.757 41.325 20.260 0.00 70.36  ? 309 OLC A H3A  1 
HETATM 4005 H H2   . OLC J 3 .   ? 33.755 43.495 19.507 0.00 94.35  ? 309 OLC A H2   1 
HETATM 4006 H H2A  . OLC J 3 .   ? 35.328 43.839 20.261 0.00 94.35  ? 309 OLC A H2A  1 
HETATM 4007 H H21  . OLC J 3 .   ? 36.506 43.035 15.955 0.00 109.89 ? 309 OLC A H21  1 
HETATM 4008 H H21A . OLC J 3 .   ? 36.645 44.699 16.572 0.00 109.89 ? 309 OLC A H21A 1 
HETATM 4009 H H22  . OLC J 3 .   ? 34.391 44.784 14.913 0.00 122.20 ? 309 OLC A H22  1 
HETATM 4010 H HO25 . OLC J 3 .   ? 35.580 46.630 15.976 0.00 101.12 ? 309 OLC A HO25 1 
HETATM 4011 H HO23 . OLC J 3 .   ? 36.486 43.299 13.710 0.00 132.21 ? 309 OLC A HO23 1 
HETATM 4012 C C18  . OLC K 3 .   ? 3.565  38.784 36.605 1.00 64.21  ? 310 OLC A C18  1 
HETATM 4013 C C10  . OLC K 3 .   ? 4.973  37.298 43.777 1.00 90.84  ? 310 OLC A C10  1 
HETATM 4014 C C9   . OLC K 3 .   ? 4.467  38.338 44.479 1.00 84.51  ? 310 OLC A C9   1 
HETATM 4015 C C17  . OLC K 3 .   ? 4.271  39.607 37.703 1.00 70.27  ? 310 OLC A C17  1 
HETATM 4016 C C11  . OLC K 3 .   ? 6.400  37.092 43.239 1.00 71.22  ? 310 OLC A C11  1 
HETATM 4017 C C8   . OLC K 3 .   ? 4.524  39.705 45.189 1.00 84.79  ? 310 OLC A C8   1 
HETATM 4018 C C24  . OLC K 3 .   ? 4.694  36.400 56.354 1.00 105.60 ? 310 OLC A C24  1 
HETATM 4019 C C16  . OLC K 3 .   ? 3.708  39.243 39.101 1.00 67.62  ? 310 OLC A C16  1 
HETATM 4020 C C12  . OLC K 3 .   ? 6.642  37.290 41.722 1.00 63.45  ? 310 OLC A C12  1 
HETATM 4021 C C7   . OLC K 3 .   ? 3.221  39.989 45.985 1.00 75.87  ? 310 OLC A C7   1 
HETATM 4022 C C15  . OLC K 3 .   ? 3.902  37.738 39.449 1.00 89.52  ? 310 OLC A C15  1 
HETATM 4023 C C13  . OLC K 3 .   ? 5.713  36.473 40.775 1.00 68.45  ? 310 OLC A C13  1 
HETATM 4024 C C6   . OLC K 3 .   ? 3.485  40.254 47.497 1.00 68.38  ? 310 OLC A C6   1 
HETATM 4025 C C14  . OLC K 3 .   ? 5.407  37.337 39.504 1.00 68.09  ? 310 OLC A C14  1 
HETATM 4026 C C5   . OLC K 3 .   ? 4.156  39.040 48.211 1.00 83.62  ? 310 OLC A C5   1 
HETATM 4027 C C4   . OLC K 3 .   ? 4.858  39.523 49.522 1.00 74.49  ? 310 OLC A C4   1 
HETATM 4028 C C3   . OLC K 3 .   ? 4.472  38.640 50.746 1.00 91.39  ? 310 OLC A C3   1 
HETATM 4029 C C2   . OLC K 3 .   ? 5.669  38.551 51.739 1.00 103.13 ? 310 OLC A C2   1 
HETATM 4030 C C21  . OLC K 3 .   ? 3.869  37.399 54.210 1.00 118.91 ? 310 OLC A C21  1 
HETATM 4031 C C1   . OLC K 3 .   ? 5.239  38.999 53.157 1.00 103.81 ? 310 OLC A C1   1 
HETATM 4032 C C22  . OLC K 3 .   ? 3.982  36.105 55.024 1.00 120.18 ? 310 OLC A C22  1 
HETATM 4033 O O19  . OLC K 3 .   ? 5.009  40.141 53.379 1.00 102.99 ? 310 OLC A O19  1 
HETATM 4034 O O25  . OLC K 3 .   ? 4.708  35.227 57.134 1.00 99.20  ? 310 OLC A O25  1 
HETATM 4035 O O23  . OLC K 3 .   ? 2.701  35.582 55.247 1.00 120.41 ? 310 OLC A O23  1 
HETATM 4036 O O20  . OLC K 3 .   ? 5.124  38.054 54.200 1.00 115.87 ? 310 OLC A O20  1 
HETATM 4037 H H18  . OLC K 3 .   ? 3.873  37.743 36.679 0.00 77.03  ? 310 OLC A H18  1 
HETATM 4038 H H18A . OLC K 3 .   ? 2.488  38.854 36.736 0.00 77.03  ? 310 OLC A H18A 1 
HETATM 4039 H H18B . OLC K 3 .   ? 3.839  39.174 35.627 0.00 77.03  ? 310 OLC A H18B 1 
HETATM 4040 H H10  . OLC K 3 .   ? 5.197  36.480 44.456 0.00 108.99 ? 310 OLC A H10  1 
HETATM 4041 H H9   . OLC K 3 .   ? 5.306  38.932 44.126 0.00 101.39 ? 310 OLC A H9   1 
HETATM 4042 H H17  . OLC K 3 .   ? 4.108  40.668 37.516 0.00 84.30  ? 310 OLC A H17  1 
HETATM 4043 H H17A . OLC K 3 .   ? 5.339  39.395 37.680 0.00 84.30  ? 310 OLC A H17A 1 
HETATM 4044 H H11  . OLC K 3 .   ? 7.049  37.794 43.765 0.00 85.44  ? 310 OLC A H11  1 
HETATM 4045 H H11A . OLC K 3 .   ? 6.694  36.071 43.484 0.00 85.44  ? 310 OLC A H11A 1 
HETATM 4046 H H8   . OLC K 3 .   ? 4.659  40.487 44.442 0.00 101.73 ? 310 OLC A H8   1 
HETATM 4047 H H8A  . OLC K 3 .   ? 5.368  39.712 45.878 0.00 101.73 ? 310 OLC A H8A  1 
HETATM 4048 H H24  . OLC K 3 .   ? 4.162  37.187 56.887 0.00 126.70 ? 310 OLC A H24  1 
HETATM 4049 H H24A . OLC K 3 .   ? 5.716  36.721 56.159 0.00 126.70 ? 310 OLC A H24A 1 
HETATM 4050 H H16  . OLC K 3 .   ? 4.221  39.844 39.852 0.00 81.13  ? 310 OLC A H16  1 
HETATM 4051 H H16A . OLC K 3 .   ? 2.642  39.471 39.119 0.00 81.13  ? 310 OLC A H16A 1 
HETATM 4052 H H12  . OLC K 3 .   ? 6.503  38.346 41.497 0.00 76.12  ? 310 OLC A H12  1 
HETATM 4053 H H12A . OLC K 3 .   ? 7.671  37.005 41.508 0.00 76.12  ? 310 OLC A H12A 1 
HETATM 4054 H H7   . OLC K 3 .   ? 2.735  40.865 45.557 0.00 91.02  ? 310 OLC A H7   1 
HETATM 4055 H H7A  . OLC K 3 .   ? 2.561  39.126 45.892 0.00 91.02  ? 310 OLC A H7A  1 
HETATM 4056 H H15  . OLC K 3 .   ? 3.406  37.135 38.689 0.00 107.40 ? 310 OLC A H15  1 
HETATM 4057 H H15A . OLC K 3 .   ? 3.451  37.541 40.420 0.00 107.40 ? 310 OLC A H15A 1 
HETATM 4058 H H13  . OLC K 3 .   ? 4.782  36.235 41.289 0.00 82.12  ? 310 OLC A H13  1 
HETATM 4059 H H13A . OLC K 3 .   ? 6.210  35.550 40.480 0.00 82.12  ? 310 OLC A H13A 1 
HETATM 4060 H H6   . OLC K 3 .   ? 4.140  41.120 47.591 0.00 82.03  ? 310 OLC A H6   1 
HETATM 4061 H H6A  . OLC K 3 .   ? 2.533  40.464 47.986 0.00 82.03  ? 310 OLC A H6A  1 
HETATM 4062 H H14  . OLC K 3 .   ? 6.016  38.240 39.533 0.00 81.69  ? 310 OLC A H14  1 
HETATM 4063 H H14A . OLC K 3 .   ? 5.655  36.760 38.613 0.00 81.69  ? 310 OLC A H14A 1 
HETATM 4064 H H5   . OLC K 3 .   ? 3.396  38.299 48.459 0.00 100.33 ? 310 OLC A H5   1 
HETATM 4065 H H5A  . OLC K 3 .   ? 4.896  38.592 47.548 0.00 100.33 ? 310 OLC A H5A  1 
HETATM 4066 H H4   . OLC K 3 .   ? 5.938  39.478 49.380 0.00 89.37  ? 310 OLC A H4   1 
HETATM 4067 H H4A  . OLC K 3 .   ? 4.561  40.552 49.721 0.00 89.37  ? 310 OLC A H4A  1 
HETATM 4068 H H3   . OLC K 3 .   ? 3.615  39.083 51.254 0.00 109.65 ? 310 OLC A H3   1 
HETATM 4069 H H3A  . OLC K 3 .   ? 4.214  37.639 50.402 0.00 109.65 ? 310 OLC A H3A  1 
HETATM 4070 H H2   . OLC K 3 .   ? 6.022  37.521 51.781 0.00 123.73 ? 310 OLC A H2   1 
HETATM 4071 H H2A  . OLC K 3 .   ? 6.473  39.196 51.389 0.00 123.73 ? 310 OLC A H2A  1 
HETATM 4072 H H21  . OLC K 3 .   ? 3.572  37.163 53.188 0.00 142.67 ? 310 OLC A H21  1 
HETATM 4073 H H21A . OLC K 3 .   ? 3.121  38.051 54.664 0.00 142.67 ? 310 OLC A H21A 1 
HETATM 4074 H H22  . OLC K 3 .   ? 4.566  35.367 54.474 0.00 144.19 ? 310 OLC A H22  1 
HETATM 4075 H HO25 . OLC K 3 .   ? 4.111  34.597 56.758 0.00 119.03 ? 310 OLC A HO25 1 
HETATM 4076 H HO23 . OLC K 3 .   ? 2.312  36.006 56.000 0.00 144.48 ? 310 OLC A HO23 1 
HETATM 4077 C C18  . OLC L 3 .   ? 21.807 55.097 37.597 1.00 75.83  ? 311 OLC A C18  1 
HETATM 4078 C C10  . OLC L 3 .   ? 23.161 56.935 29.497 1.00 79.74  ? 311 OLC A C10  1 
HETATM 4079 C C9   . OLC L 3 .   ? 23.374 57.450 28.281 1.00 81.05  ? 311 OLC A C9   1 
HETATM 4080 C C17  . OLC L 3 .   ? 22.413 53.904 36.825 1.00 74.67  ? 311 OLC A C17  1 
HETATM 4081 C C11  . OLC L 3 .   ? 21.813 56.560 30.140 1.00 79.91  ? 311 OLC A C11  1 
HETATM 4082 C C8   . OLC L 3 .   ? 22.943 57.969 26.893 1.00 92.86  ? 311 OLC A C8   1 
HETATM 4083 C C24  . OLC L 3 .   ? 28.466 55.981 15.571 1.00 112.37 ? 311 OLC A C24  1 
HETATM 4084 C C16  . OLC L 3 .   ? 21.567 53.566 35.563 1.00 80.89  ? 311 OLC A C16  1 
HETATM 4085 C C12  . OLC L 3 .   ? 22.132 55.741 31.424 1.00 81.16  ? 311 OLC A C12  1 
HETATM 4086 C C7   . OLC L 3 .   ? 24.148 58.044 25.911 1.00 105.42 ? 311 OLC A C7   1 
HETATM 4087 C C15  . OLC L 3 .   ? 21.698 54.664 34.480 1.00 72.03  ? 311 OLC A C15  1 
HETATM 4088 C C13  . OLC L 3 .   ? 20.839 55.389 32.213 1.00 84.03  ? 311 OLC A C13  1 
HETATM 4089 C C6   . OLC L 3 .   ? 23.587 58.004 24.455 1.00 97.46  ? 311 OLC A C6   1 
HETATM 4090 C C14  . OLC L 3 .   ? 21.113 54.157 33.129 1.00 60.99  ? 311 OLC A C14  1 
HETATM 4091 C C5   . OLC L 3 .   ? 24.708 57.723 23.414 1.00 96.69  ? 311 OLC A C5   1 
HETATM 4092 C C4   . OLC L 3 .   ? 24.045 57.121 22.133 1.00 99.98  ? 311 OLC A C4   1 
HETATM 4093 C C3   . OLC L 3 .   ? 24.543 57.824 20.837 1.00 94.65  ? 311 OLC A C3   1 
HETATM 4094 C C2   . OLC L 3 .   ? 24.641 56.744 19.727 1.00 106.65 ? 311 OLC A C2   1 
HETATM 4095 C C21  . OLC L 3 .   ? 26.273 56.649 16.627 1.00 112.79 ? 311 OLC A C21  1 
HETATM 4096 C C1   . OLC L 3 .   ? 24.724 57.343 18.301 1.00 102.93 ? 311 OLC A C1   1 
HETATM 4097 C C22  . OLC L 3 .   ? 27.590 55.866 16.832 1.00 109.62 ? 311 OLC A C22  1 
HETATM 4098 O O19  . OLC L 3 .   ? 23.751 57.642 17.681 1.00 101.61 ? 311 OLC A O19  1 
HETATM 4099 O O25  . OLC L 3 .   ? 29.456 54.973 15.569 1.00 110.96 ? 311 OLC A O25  1 
HETATM 4100 O O23  . OLC L 3 .   ? 28.297 56.333 17.953 1.00 97.24  ? 311 OLC A O23  1 
HETATM 4101 O O20  . OLC L 3 .   ? 26.010 57.490 17.737 1.00 107.02 ? 311 OLC A O20  1 
HETATM 4102 H H18  . OLC L 3 .   ? 22.356 55.246 38.525 0.00 90.98  ? 311 OLC A H18  1 
HETATM 4103 H H18A . OLC L 3 .   ? 21.875 55.996 36.988 0.00 90.98  ? 311 OLC A H18A 1 
HETATM 4104 H H18B . OLC L 3 .   ? 20.763 54.890 37.823 0.00 90.98  ? 311 OLC A H18B 1 
HETATM 4105 H H10  . OLC L 3 .   ? 23.215 57.725 30.241 0.00 95.67  ? 311 OLC A H10  1 
HETATM 4106 H H9   . OLC L 3 .   ? 22.323 57.729 28.270 0.00 97.24  ? 311 OLC A H9   1 
HETATM 4107 H H17  . OLC L 3 .   ? 22.440 53.034 37.479 0.00 89.58  ? 311 OLC A H17  1 
HETATM 4108 H H17A . OLC L 3 .   ? 23.426 54.158 36.517 0.00 89.58  ? 311 OLC A H17A 1 
HETATM 4109 H H11  . OLC L 3 .   ? 21.223 55.957 29.448 0.00 95.88  ? 311 OLC A H11  1 
HETATM 4110 H H11A . OLC L 3 .   ? 21.259 57.463 30.400 0.00 95.88  ? 311 OLC A H11A 1 
HETATM 4111 H H8   . OLC L 3 .   ? 22.515 58.965 27.005 0.00 111.42 ? 311 OLC A H8   1 
HETATM 4112 H H8A  . OLC L 3 .   ? 22.192 57.295 26.481 0.00 111.42 ? 311 OLC A H8A  1 
HETATM 4113 H H24  . OLC L 3 .   ? 28.947 56.957 15.556 0.00 134.82 ? 311 OLC A H24  1 
HETATM 4114 H H24A . OLC L 3 .   ? 27.840 55.871 14.687 0.00 134.82 ? 311 OLC A H24A 1 
HETATM 4115 H H16  . OLC L 3 .   ? 20.520 53.477 35.853 0.00 97.05  ? 311 OLC A H16  1 
HETATM 4116 H H16A . OLC L 3 .   ? 21.911 52.618 35.150 0.00 97.05  ? 311 OLC A H16A 1 
HETATM 4117 H H12  . OLC L 3 .   ? 22.634 54.817 31.139 0.00 97.37  ? 311 OLC A H12  1 
HETATM 4118 H H12A . OLC L 3 .   ? 22.788 56.328 32.065 0.00 97.37  ? 311 OLC A H12A 1 
HETATM 4119 H H7   . OLC L 3 .   ? 24.697 58.972 26.070 0.00 126.48 ? 311 OLC A H7   1 
HETATM 4120 H H7A  . OLC L 3 .   ? 24.812 57.195 26.075 0.00 126.48 ? 311 OLC A H7A  1 
HETATM 4121 H H15  . OLC L 3 .   ? 22.749 54.915 34.347 0.00 86.42  ? 311 OLC A H15  1 
HETATM 4122 H H15A . OLC L 3 .   ? 21.151 55.551 34.799 0.00 86.42  ? 311 OLC A H15A 1 
HETATM 4123 H H13  . OLC L 3 .   ? 20.039 55.151 31.513 0.00 100.82 ? 311 OLC A H13  1 
HETATM 4124 H H13A . OLC L 3 .   ? 20.544 56.240 32.825 0.00 100.82 ? 311 OLC A H13A 1 
HETATM 4125 H H6   . OLC L 3 .   ? 22.837 57.217 24.387 0.00 116.94 ? 311 OLC A H6   1 
HETATM 4126 H H6A  . OLC L 3 .   ? 23.127 58.965 24.227 0.00 116.94 ? 311 OLC A H6A  1 
HETATM 4127 H H14  . OLC L 3 .   ? 20.183 53.619 33.310 0.00 73.17  ? 311 OLC A H14  1 
HETATM 4128 H H14A . OLC L 3 .   ? 21.829 53.492 32.646 0.00 73.17  ? 311 OLC A H14A 1 
HETATM 4129 H H5   . OLC L 3 .   ? 25.425 57.014 23.826 0.00 116.01 ? 311 OLC A H5   1 
HETATM 4130 H H5A  . OLC L 3 .   ? 25.220 58.652 23.163 0.00 116.01 ? 311 OLC A H5A  1 
HETATM 4131 H H4   . OLC L 3 .   ? 24.290 56.061 22.075 0.00 119.95 ? 311 OLC A H4   1 
HETATM 4132 H H4A  . OLC L 3 .   ? 22.965 57.241 22.206 0.00 119.95 ? 311 OLC A H4A  1 
HETATM 4133 H H3   . OLC L 3 .   ? 23.838 58.600 20.540 0.00 113.56 ? 311 OLC A H3   1 
HETATM 4134 H H3A  . OLC L 3 .   ? 25.523 58.270 21.009 0.00 113.56 ? 311 OLC A H3A  1 
HETATM 4135 H H2   . OLC L 3 .   ? 25.533 56.145 19.903 0.00 127.96 ? 311 OLC A H2   1 
HETATM 4136 H H2A  . OLC L 3 .   ? 23.760 56.107 19.784 0.00 127.96 ? 311 OLC A H2A  1 
HETATM 4137 H H21  . OLC L 3 .   ? 26.356 57.260 15.728 0.00 135.33 ? 311 OLC A H21  1 
HETATM 4138 H H21A . OLC L 3 .   ? 25.451 55.942 16.512 0.00 135.33 ? 311 OLC A H21A 1 
HETATM 4139 H H22  . OLC L 3 .   ? 27.339 54.820 17.009 0.00 131.52 ? 311 OLC A H22  1 
HETATM 4140 H HO25 . OLC L 3 .   ? 29.142 54.222 16.052 0.00 133.14 ? 311 OLC A HO25 1 
HETATM 4141 H HO23 . OLC L 3 .   ? 27.683 56.638 18.609 0.00 116.67 ? 311 OLC A HO23 1 
HETATM 4142 C C45  . LI1 M 2 .   ? 31.195 33.804 46.644 1.00 84.45  ? 312 LI1 A C45  1 
HETATM 4143 C C46  . LI1 M 2 .   ? 30.571 33.587 45.224 1.00 68.53  ? 312 LI1 A C46  1 
HETATM 4144 C C47  . LI1 M 2 .   ? 31.668 33.706 44.119 1.00 85.59  ? 312 LI1 A C47  1 
HETATM 4145 C C48  . LI1 M 2 .   ? 31.647 35.127 43.515 1.00 81.70  ? 312 LI1 A C48  1 
HETATM 4146 C C50  . LI1 M 2 .   ? 31.154 35.099 42.058 1.00 89.04  ? 312 LI1 A C50  1 
HETATM 4147 C C51  . LI1 M 2 .   ? 29.780 35.832 41.937 1.00 80.22  ? 312 LI1 A C51  1 
HETATM 4148 C C52  . LI1 M 2 .   ? 29.939 37.374 42.097 1.00 78.56  ? 312 LI1 A C52  1 
HETATM 4149 C C53  . LI1 M 2 .   ? 28.909 38.123 41.203 1.00 58.38  ? 312 LI1 A C53  1 
HETATM 4150 C C55  . LI1 M 2 .   ? 29.457 38.178 39.756 1.00 77.64  ? 312 LI1 A C55  1 
HETATM 4151 C C56  . LI1 M 2 .   ? 30.037 39.587 39.493 1.00 60.46  ? 312 LI1 A C56  1 
HETATM 4152 H H451 . LI1 M 2 .   ? 30.393 33.941 47.368 1.00 101.32 ? 312 LI1 A H451 1 
HETATM 4153 H H452 . LI1 M 2 .   ? 31.823 34.694 46.629 1.00 101.32 ? 312 LI1 A H452 1 
HETATM 4154 H H461 . LI1 M 2 .   ? 30.122 32.594 45.178 1.00 82.22  ? 312 LI1 A H461 1 
HETATM 4155 H H462 . LI1 M 2 .   ? 29.803 34.341 45.051 1.00 82.22  ? 312 LI1 A H462 1 
HETATM 4156 H H471 . LI1 M 2 .   ? 31.472 32.977 43.336 1.00 102.68 ? 312 LI1 A H471 1 
HETATM 4157 H H472 . LI1 M 2 .   ? 32.645 33.514 44.558 1.00 102.68 ? 312 LI1 A H472 1 
HETATM 4158 C C45  . LI1 N 2 .   ? 31.098 27.905 46.113 1.00 83.26  ? 313 LI1 A C45  1 
HETATM 4159 C C46  . LI1 N 2 .   ? 31.051 26.489 45.436 1.00 79.47  ? 313 LI1 A C46  1 
HETATM 4160 C C47  . LI1 N 2 .   ? 31.220 26.627 43.882 1.00 79.47  ? 313 LI1 A C47  1 
HETATM 4161 C C48  . LI1 N 2 .   ? 29.836 26.669 43.195 1.00 77.88  ? 313 LI1 A C48  1 
HETATM 4162 C C50  . LI1 N 2 .   ? 30.011 26.579 41.673 1.00 80.28  ? 313 LI1 A C50  1 
HETATM 4163 C C51  . LI1 N 2 .   ? 28.667 26.177 40.995 1.00 70.43  ? 313 LI1 A C51  1 
HETATM 4164 C C52  . LI1 N 2 .   ? 28.927 25.881 39.487 1.00 82.46  ? 313 LI1 A C52  1 
HETATM 4165 C C53  . LI1 N 2 .   ? 28.184 26.913 38.592 1.00 82.62  ? 313 LI1 A C53  1 
HETATM 4166 C C55  . LI1 N 2 .   ? 28.335 28.333 39.209 1.00 78.02  ? 313 LI1 A C55  1 
HETATM 4167 C C56  . LI1 N 2 .   ? 28.807 29.396 38.173 1.00 70.75  ? 313 LI1 A C56  1 
HETATM 4168 C C57  . LI1 N 2 .   ? 29.079 30.746 38.909 1.00 67.15  ? 313 LI1 A C57  1 
HETATM 4169 C C58  . LI1 N 2 .   ? 29.549 31.818 37.891 1.00 65.54  ? 313 LI1 A C58  1 
HETATM 4170 C C59  . LI1 N 2 .   ? 29.276 33.232 38.450 1.00 58.58  ? 313 LI1 A C59  1 
HETATM 4171 H H451 . LI1 N 2 .   ? 30.192 28.456 45.865 1.00 99.89  ? 313 LI1 A H451 1 
HETATM 4172 H H452 . LI1 N 2 .   ? 31.965 28.456 45.748 1.00 99.89  ? 313 LI1 A H452 1 
HETATM 4173 H H461 . LI1 N 2 .   ? 30.093 26.017 45.654 1.00 95.35  ? 313 LI1 A H461 1 
HETATM 4174 H H462 . LI1 N 2 .   ? 31.859 25.874 45.833 1.00 95.35  ? 313 LI1 A H462 1 
HETATM 4175 H H471 . LI1 N 2 .   ? 31.783 25.776 43.505 1.00 95.35  ? 313 LI1 A H471 1 
HETATM 4176 H H472 . LI1 N 2 .   ? 31.758 27.546 43.660 1.00 95.35  ? 313 LI1 A H472 1 
HETATM 4177 C C50  . LI1 O 2 .   ? 28.980 25.156 23.219 1.00 64.57  ? 314 LI1 A C50  1 
HETATM 4178 C C51  . LI1 O 2 .   ? 28.777 23.840 24.028 1.00 74.41  ? 314 LI1 A C51  1 
HETATM 4179 C C52  . LI1 O 2 .   ? 28.352 24.185 25.478 1.00 56.45  ? 314 LI1 A C52  1 
HETATM 4180 C C53  . LI1 O 2 .   ? 28.882 23.105 26.459 1.00 61.16  ? 314 LI1 A C53  1 
HETATM 4181 C C55  . LI1 O 2 .   ? 28.949 23.660 27.911 1.00 78.74  ? 314 LI1 A C55  1 
HETATM 4182 C C56  . LI1 O 2 .   ? 30.366 23.470 28.529 1.00 90.16  ? 314 LI1 A C56  1 
HETATM 4183 C C57  . LI1 O 2 .   ? 30.340 23.755 30.056 1.00 84.59  ? 314 LI1 A C57  1 
HETATM 4184 C C58  . LI1 O 2 .   ? 31.293 24.934 30.399 1.00 84.63  ? 314 LI1 A C58  1 
HETATM 4185 C C46  . LI1 P 2 .   ? 30.887 32.867 33.677 1.00 78.85  ? 315 LI1 A C46  1 
HETATM 4186 C C47  . LI1 P 2 .   ? 30.938 33.923 32.523 1.00 71.86  ? 315 LI1 A C47  1 
HETATM 4187 C C48  . LI1 P 2 .   ? 31.685 33.335 31.299 1.00 79.14  ? 315 LI1 A C48  1 
HETATM 4188 C C50  . LI1 P 2 .   ? 31.736 31.800 31.424 1.00 91.75  ? 315 LI1 A C50  1 
HETATM 4189 C C51  . LI1 P 2 .   ? 33.006 31.213 30.728 1.00 100.99 ? 315 LI1 A C51  1 
HETATM 4190 C C52  . LI1 P 2 .   ? 33.051 29.669 30.940 1.00 92.32  ? 315 LI1 A C52  1 
HETATM 4191 C C53  . LI1 P 2 .   ? 34.448 29.100 30.579 1.00 86.87  ? 315 LI1 A C53  1 
HETATM 4192 C C55  . LI1 P 2 .   ? 34.338 27.578 30.326 1.00 77.62  ? 315 LI1 A C55  1 
HETATM 4193 C C56  . LI1 P 2 .   ? 34.197 27.315 28.805 1.00 80.06  ? 315 LI1 A C56  1 
HETATM 4194 C C57  . LI1 P 2 .   ? 33.805 25.831 28.609 1.00 82.43  ? 315 LI1 A C57  1 
HETATM 4195 C C58  . LI1 P 2 .   ? 34.272 25.356 27.210 1.00 84.43  ? 315 LI1 A C58  1 
HETATM 4196 C C59  . LI1 P 2 .   ? 34.430 26.586 26.280 1.00 76.37  ? 315 LI1 A C59  1 
HETATM 4197 C C60  . LI1 P 2 .   ? 33.210 24.396 26.628 1.00 88.56  ? 315 LI1 A C60  1 
HETATM 4198 C C45  . LI1 Q 2 .   ? 9.290  59.530 46.156 1.00 69.03  ? 316 LI1 A C45  1 
HETATM 4199 C C46  . LI1 Q 2 .   ? 9.957  58.435 45.268 1.00 76.90  ? 316 LI1 A C46  1 
HETATM 4200 C C47  . LI1 Q 2 .   ? 11.367 58.948 44.844 1.00 79.75  ? 316 LI1 A C47  1 
HETATM 4201 C C48  . LI1 Q 2 .   ? 11.305 59.622 43.462 1.00 81.11  ? 316 LI1 A C48  1 
HETATM 4202 C C50  . LI1 Q 2 .   ? 12.745 59.862 42.992 1.00 78.21  ? 316 LI1 A C50  1 
HETATM 4203 C C51  . LI1 Q 2 .   ? 13.293 58.601 42.251 1.00 67.99  ? 316 LI1 A C51  1 
HETATM 4204 C C52  . LI1 Q 2 .   ? 14.652 58.969 41.579 1.00 68.68  ? 316 LI1 A C52  1 
HETATM 4205 C C53  . LI1 Q 2 .   ? 15.846 58.313 42.346 1.00 80.81  ? 316 LI1 A C53  1 
HETATM 4206 C C55  . LI1 Q 2 .   ? 17.169 58.410 41.523 1.00 64.96  ? 316 LI1 A C55  1 
HETATM 4207 C C56  . LI1 Q 2 .   ? 17.977 57.076 41.586 1.00 63.10  ? 316 LI1 A C56  1 
HETATM 4208 C C57  . LI1 Q 2 .   ? 18.852 56.994 42.869 1.00 71.32  ? 316 LI1 A C57  1 
HETATM 4209 C C58  . LI1 Q 2 .   ? 19.706 55.689 42.875 1.00 72.61  ? 316 LI1 A C58  1 
HETATM 4210 C C59  . LI1 Q 2 .   ? 20.934 55.846 43.814 1.00 76.51  ? 316 LI1 A C59  1 
HETATM 4211 H H451 . LI1 Q 2 .   ? 9.809  59.581 47.110 1.00 82.81  ? 316 LI1 A H451 1 
HETATM 4212 H H452 . LI1 Q 2 .   ? 9.367  60.491 45.650 1.00 82.81  ? 316 LI1 A H452 1 
HETATM 4213 H H461 . LI1 Q 2 .   ? 9.348  58.256 44.383 1.00 92.27  ? 316 LI1 A H461 1 
HETATM 4214 H H462 . LI1 Q 2 .   ? 10.056 57.509 45.835 1.00 92.27  ? 316 LI1 A H462 1 
HETATM 4215 H H471 . LI1 Q 2 .   ? 12.056 58.107 44.802 1.00 95.68  ? 316 LI1 A H471 1 
HETATM 4216 H H472 . LI1 Q 2 .   ? 11.720 59.670 45.578 1.00 95.68  ? 316 LI1 A H472 1 
HETATM 4217 C C52  . LI1 R 2 .   ? 26.871 18.814 43.286 1.00 81.94  ? 317 LI1 A C52  1 
HETATM 4218 C C53  . LI1 R 2 .   ? 25.921 17.743 42.643 1.00 78.35  ? 317 LI1 A C53  1 
HETATM 4219 C C55  . LI1 R 2 .   ? 25.020 18.403 41.551 1.00 62.04  ? 317 LI1 A C55  1 
HETATM 4220 C C56  . LI1 R 2 .   ? 25.866 19.330 40.654 1.00 69.63  ? 317 LI1 A C56  1 
HETATM 4221 C C57  . LI1 R 2 .   ? 25.366 19.259 39.205 1.00 72.21  ? 317 LI1 A C57  1 
HETATM 4222 C C58  . LI1 R 2 .   ? 24.765 17.851 38.917 1.00 83.31  ? 317 LI1 A C58  1 
HETATM 4223 C C1   . RET S 4 .   ? 15.195 46.724 29.679 1.00 23.11  ? 318 RET A C1   1 
HETATM 4224 C C2   . RET S 4 .   ? 14.890 47.648 28.492 1.00 32.09  ? 318 RET A C2   1 
HETATM 4225 C C3   . RET S 4 .   ? 15.200 49.109 28.572 1.00 38.23  ? 318 RET A C3   1 
HETATM 4226 C C4   . RET S 4 .   ? 15.031 49.738 29.921 1.00 26.18  ? 318 RET A C4   1 
HETATM 4227 C C5   . RET S 4 .   ? 15.360 48.850 31.065 1.00 25.15  ? 318 RET A C5   1 
HETATM 4228 C C6   . RET S 4 .   ? 15.516 47.519 30.977 1.00 23.76  ? 318 RET A C6   1 
HETATM 4229 C C7   . RET S 4 .   ? 15.914 46.728 32.183 1.00 23.00  ? 318 RET A C7   1 
HETATM 4230 C C8   . RET S 4 .   ? 16.150 45.437 32.408 1.00 23.19  ? 318 RET A C8   1 
HETATM 4231 C C9   . RET S 4 .   ? 16.554 44.718 33.615 1.00 23.27  ? 318 RET A C9   1 
HETATM 4232 C C10  . RET S 4 .   ? 16.764 43.383 33.548 1.00 22.95  ? 318 RET A C10  1 
HETATM 4233 C C11  . RET S 4 .   ? 17.269 42.525 34.552 1.00 21.76  ? 318 RET A C11  1 
HETATM 4234 C C12  . RET S 4 .   ? 17.478 41.220 34.318 1.00 25.33  ? 318 RET A C12  1 
HETATM 4235 C C13  . RET S 4 .   ? 17.879 40.203 35.235 1.00 25.06  ? 318 RET A C13  1 
HETATM 4236 C C14  . RET S 4 .   ? 17.868 38.927 34.752 1.00 27.28  ? 318 RET A C14  1 
HETATM 4237 C C15  . RET S 4 .   ? 17.833 37.790 35.414 1.00 25.02  ? 318 RET A C15  1 
HETATM 4238 C C16  . RET S 4 .   ? 16.400 45.932 29.186 1.00 24.73  ? 318 RET A C16  1 
HETATM 4239 C C17  . RET S 4 .   ? 13.994 45.781 29.865 1.00 27.83  ? 318 RET A C17  1 
HETATM 4240 C C18  . RET S 4 .   ? 15.459 49.641 32.357 1.00 26.11  ? 318 RET A C18  1 
HETATM 4241 C C19  . RET S 4 .   ? 16.886 45.539 34.854 1.00 24.24  ? 318 RET A C19  1 
HETATM 4242 C C20  . RET S 4 .   ? 18.236 40.594 36.648 1.00 26.90  ? 318 RET A C20  1 
HETATM 4243 H H21  . RET S 4 .   ? 15.365 47.308 27.706 1.00 38.49  ? 318 RET A H21  1 
HETATM 4244 H H22  . RET S 4 .   ? 13.936 47.580 28.285 1.00 38.49  ? 318 RET A H22  1 
HETATM 4245 H H31  . RET S 4 .   ? 14.630 49.588 27.936 1.00 45.85  ? 318 RET A H31  1 
HETATM 4246 H H32  . RET S 4 .   ? 16.124 49.252 28.280 1.00 45.85  ? 318 RET A H32  1 
HETATM 4247 H H41  . RET S 4 .   ? 14.105 50.038 30.023 1.00 31.39  ? 318 RET A H41  1 
HETATM 4248 H H42  . RET S 4 .   ? 15.597 50.535 29.979 1.00 31.39  ? 318 RET A H42  1 
HETATM 4249 H H7   . RET S 4 .   ? 15.660 47.230 32.984 1.00 27.58  ? 318 RET A H7   1 
HETATM 4250 H H8   . RET S 4 .   ? 16.442 44.964 31.602 1.00 27.81  ? 318 RET A H8   1 
HETATM 4251 H H10  . RET S 4 .   ? 16.542 42.940 32.703 1.00 27.52  ? 318 RET A H10  1 
HETATM 4252 H H11  . RET S 4 .   ? 17.136 42.793 35.484 1.00 26.09  ? 318 RET A H11  1 
HETATM 4253 H H12  . RET S 4 .   ? 17.339 40.918 33.397 1.00 30.37  ? 318 RET A H12  1 
HETATM 4254 H H14  . RET S 4 .   ? 17.888 38.787 33.783 1.00 32.72  ? 318 RET A H14  1 
HETATM 4255 H H15  . RET S 4 .   ? 17.898 37.864 36.388 1.00 30.00  ? 318 RET A H15  1 
HETATM 4256 H H161 . RET S 4 .   ? 16.193 45.417 28.380 1.00 29.66  ? 318 RET A H161 1 
HETATM 4257 H H162 . RET S 4 .   ? 17.155 46.515 28.967 1.00 29.66  ? 318 RET A H162 1 
HETATM 4258 H H163 . RET S 4 .   ? 16.717 45.294 29.858 1.00 29.66  ? 318 RET A H163 1 
HETATM 4259 H H171 . RET S 4 .   ? 14.140 45.173 30.617 1.00 33.37  ? 318 RET A H171 1 
HETATM 4260 H H172 . RET S 4 .   ? 13.847 45.240 29.062 1.00 33.37  ? 318 RET A H172 1 
HETATM 4261 H H173 . RET S 4 .   ? 13.175 46.289 30.041 1.00 33.37  ? 318 RET A H173 1 
HETATM 4262 H H181 . RET S 4 .   ? 15.643 50.594 32.224 1.00 31.31  ? 318 RET A H181 1 
HETATM 4263 H H182 . RET S 4 .   ? 16.168 49.331 32.957 1.00 31.31  ? 318 RET A H182 1 
HETATM 4264 H H183 . RET S 4 .   ? 14.644 49.617 32.899 1.00 31.31  ? 318 RET A H183 1 
HETATM 4265 H H191 . RET S 4 .   ? 17.850 45.524 35.023 1.00 29.07  ? 318 RET A H191 1 
HETATM 4266 H H192 . RET S 4 .   ? 16.604 46.469 34.732 1.00 29.07  ? 318 RET A H192 1 
HETATM 4267 H H193 . RET S 4 .   ? 16.425 45.174 35.637 1.00 29.07  ? 318 RET A H193 1 
HETATM 4268 H H201 . RET S 4 .   ? 17.494 41.057 37.087 1.00 32.26  ? 318 RET A H201 1 
HETATM 4269 H H202 . RET S 4 .   ? 18.457 39.809 37.189 1.00 32.26  ? 318 RET A H202 1 
HETATM 4270 H H203 . RET S 4 .   ? 19.011 41.193 36.666 1.00 32.26  ? 318 RET A H203 1 
HETATM 4271 O O    . HOH T 5 .   ? 20.708 19.885 52.690 1.00 67.36  ? 401 HOH A O    1 
HETATM 4272 O O    . HOH T 5 .   ? 4.317  29.644 18.376 1.00 61.92  ? 402 HOH A O    1 
HETATM 4273 O O    . HOH T 5 .   ? 23.105 35.477 67.434 1.00 50.97  ? 403 HOH A O    1 
HETATM 4274 O O    . HOH T 5 .   ? 23.080 45.473 16.401 1.00 44.81  ? 404 HOH A O    1 
HETATM 4275 O O    . HOH T 5 .   ? 9.699  48.300 54.507 1.00 59.90  ? 405 HOH A O    1 
HETATM 4276 O O    . HOH T 5 .   ? 14.298 34.538 60.336 1.00 81.99  ? 406 HOH A O    1 
HETATM 4277 O O    . HOH T 5 .   ? 22.231 26.509 53.448 1.00 59.04  ? 407 HOH A O    1 
HETATM 4278 O O    . HOH T 5 .   ? 8.030  31.089 18.181 1.00 51.73  ? 408 HOH A O    1 
HETATM 4279 O O    . HOH T 5 .   ? 19.257 29.345 73.843 1.00 43.43  ? 409 HOH A O    1 
HETATM 4280 O O    . HOH T 5 .   ? 18.233 37.033 28.765 1.00 28.37  ? 410 HOH A O    1 
HETATM 4281 O O    . HOH T 5 .   ? 8.052  45.052 58.352 1.00 66.07  ? 411 HOH A O    1 
HETATM 4282 O O    . HOH T 5 .   ? 18.019 35.529 32.375 1.00 25.11  ? 412 HOH A O    1 
HETATM 4283 O O    . HOH T 5 .   ? 8.824  28.210 54.533 1.00 39.73  ? 413 HOH A O    1 
HETATM 4284 O O    . HOH T 5 .   ? 15.588 41.230 23.275 1.00 43.43  ? 414 HOH A O    1 
HETATM 4285 O O    . HOH T 5 .   ? 26.677 34.720 56.877 1.00 64.69  ? 415 HOH A O    1 
HETATM 4286 O O    . HOH T 5 .   ? 16.534 34.673 28.941 1.00 28.59  ? 416 HOH A O    1 
HETATM 4287 O O    . HOH T 5 .   ? 18.944 37.905 69.389 1.00 40.69  ? 417 HOH A O    1 
HETATM 4288 O O    . HOH T 5 .   ? 23.655 37.422 14.519 1.00 47.91  ? 418 HOH A O    1 
HETATM 4289 O O    . HOH T 5 .   ? 16.047 21.305 47.207 1.00 45.95  ? 419 HOH A O    1 
HETATM 4290 O O    . HOH T 5 .   ? 25.874 39.432 15.124 1.00 45.02  ? 420 HOH A O    1 
HETATM 4291 O O    . HOH T 5 .   ? 16.858 23.960 46.698 1.00 37.75  ? 421 HOH A O    1 
HETATM 4292 O O    . HOH T 5 .   ? 23.719 42.275 14.515 1.00 48.60  ? 422 HOH A O    1 
HETATM 4293 O O    . HOH T 5 .   ? 15.037 25.961 14.761 1.00 53.27  ? 423 HOH A O    1 
HETATM 4294 O O    . HOH T 5 .   ? 31.299 37.493 50.980 1.00 82.95  ? 424 HOH A O    1 
HETATM 4295 O O    . HOH T 5 .   ? 10.475 31.578 15.734 1.00 53.98  ? 425 HOH A O    1 
HETATM 4296 O O    . HOH T 5 .   ? 22.623 45.904 61.806 1.00 71.92  ? 426 HOH A O    1 
HETATM 4297 O O    . HOH T 5 .   ? 19.036 48.610 15.758 1.00 52.03  ? 427 HOH A O    1 
HETATM 4298 O O    . HOH T 5 .   ? 8.303  33.572 17.862 1.00 53.27  ? 428 HOH A O    1 
HETATM 4299 O O    . HOH T 5 .   ? 4.534  51.856 20.406 1.00 28.20  ? 429 HOH A O    1 
HETATM 4300 O O    . HOH T 5 .   ? 20.365 40.286 40.794 1.00 29.03  ? 430 HOH A O    1 
HETATM 4301 O O    . HOH T 5 .   ? 22.195 35.986 26.183 1.00 25.82  ? 431 HOH A O    1 
HETATM 4302 O O    . HOH T 5 .   ? 17.582 23.368 58.502 1.00 57.93  ? 432 HOH A O    1 
HETATM 4303 O O    . HOH T 5 .   ? 21.567 31.354 66.011 1.00 70.19  ? 433 HOH A O    1 
HETATM 4304 O O    . HOH T 5 .   ? 18.952 40.151 22.416 1.00 41.40  ? 434 HOH A O    1 
HETATM 4305 O O    . HOH T 5 .   ? 22.292 25.227 11.541 1.00 85.01  ? 435 HOH A O    1 
HETATM 4306 O O    . HOH T 5 .   ? 11.860 38.126 8.332  1.00 73.31  ? 436 HOH A O    1 
HETATM 4307 O O    . HOH T 5 .   ? 19.972 35.720 14.165 1.00 59.45  ? 437 HOH A O    1 
HETATM 4308 O O    . HOH T 5 .   ? 17.313 40.500 20.094 1.00 33.82  ? 438 HOH A O    1 
HETATM 4309 O O    . HOH T 5 .   ? 9.540  38.529 60.145 1.00 86.00  ? 439 HOH A O    1 
HETATM 4310 O O    . HOH T 5 .   ? 21.147 23.331 12.220 1.00 97.30  ? 440 HOH A O    1 
HETATM 4311 O O    . HOH T 5 .   ? 8.515  49.524 10.312 1.00 54.77  ? 441 HOH A O    1 
HETATM 4312 O O    . HOH T 5 .   ? 16.958 42.751 6.913  1.00 80.52  ? 442 HOH A O    1 
HETATM 4313 O O    . HOH T 5 .   ? 10.433 49.437 8.489  1.00 65.16  ? 443 HOH A O    1 
HETATM 4314 O O    . HOH T 5 .   ? 31.451 54.497 18.078 0.62 95.46  ? 444 HOH A O    1 
HETATM 4315 O O    . HOH T 5 .   ? 15.244 58.582 16.249 1.00 71.74  ? 445 HOH A O    1 
HETATM 4316 O O    . HOH T 5 .   ? 28.770 56.038 21.242 1.00 70.18  ? 446 HOH A O    1 
HETATM 4317 O O    . HOH T 5 .   ? 21.388 46.098 14.378 1.00 58.40  ? 447 HOH A O    1 
HETATM 4318 O O    . HOH T 5 .   ? 18.776 19.734 60.768 1.00 87.94  ? 448 HOH A O    1 
HETATM 4319 O O    . HOH T 5 .   ? 0.000  36.344 22.377 0.33 65.06  ? 449 HOH A O    1 
HETATM 4320 O O    . HOH T 5 .   ? 0.000  36.344 25.695 0.33 66.07  ? 450 HOH A O    1 
HETATM 4321 O O    . HOH T 5 .   ? 18.376 35.293 12.523 1.00 56.95  ? 451 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 
6    N N   . THR A 2   ? 1.0638 0.8459 0.6252 -0.0238 0.0957  -0.0867 5   THR A N   
7    C CA  . THR A 2   ? 0.9886 0.7982 0.5867 0.0080  0.1302  -0.0743 5   THR A CA  
8    C C   . THR A 2   ? 0.9385 0.7724 0.5189 0.0039  0.1344  -0.0595 5   THR A C   
9    O O   . THR A 2   ? 1.1208 0.9876 0.7374 0.0231  0.1607  -0.0445 5   THR A O   
10   C CB  . THR A 2   ? 1.2155 0.9703 0.7694 0.0375  0.1708  -0.0884 5   THR A CB  
11   O OG1 . THR A 2   ? 1.1793 0.8549 0.6195 0.0251  0.1761  -0.1092 5   THR A OG1 
12   C CG2 . THR A 2   ? 1.1895 0.9280 0.7752 0.0496  0.1707  -0.0956 5   THR A CG2 
19   N N   . GLY A 3   ? 1.1375 0.9605 0.6640 -0.0224 0.1085  -0.0603 6   GLY A N   
20   C CA  . GLY A 3   ? 0.9363 0.7818 0.4435 -0.0250 0.1105  -0.0424 6   GLY A CA  
21   C C   . GLY A 3   ? 0.9799 0.8875 0.5675 -0.0221 0.1004  -0.0150 6   GLY A C   
22   O O   . GLY A 3   ? 1.0020 0.9243 0.5781 -0.0209 0.1073  0.0035  6   GLY A O   
26   N N   . ARG A 4   ? 0.8066 0.7415 0.4655 -0.0216 0.0853  -0.0118 7   ARG A N   
27   C CA  . ARG A 4   ? 0.7149 0.6904 0.4383 -0.0183 0.0797  0.0110  7   ARG A CA  
28   C C   . ARG A 4   ? 0.6253 0.6170 0.4066 -0.0054 0.1032  0.0130  7   ARG A C   
29   O O   . ARG A 4   ? 0.5853 0.5757 0.3943 0.0005  0.1037  0.0003  7   ARG A O   
30   C CB  . ARG A 4   ? 0.5782 0.5731 0.3347 -0.0267 0.0473  0.0156  7   ARG A CB  
31   C CG  . ARG A 4   ? 0.6086 0.6149 0.3262 -0.0412 0.0177  0.0255  7   ARG A CG  
32   C CD  . ARG A 4   ? 0.6688 0.7017 0.4297 -0.0465 -0.0081 0.0285  7   ARG A CD  
33   N NE  . ARG A 4   ? 0.7699 0.7801 0.5212 -0.0586 -0.0118 0.0039  7   ARG A NE  
34   C CZ  . ARG A 4   ? 0.6861 0.7092 0.4732 -0.0641 -0.0261 0.0008  7   ARG A CZ  
35   N NH1 . ARG A 4   ? 0.4314 0.4824 0.2787 -0.0501 -0.0274 0.0143  7   ARG A NH1 
36   N NH2 . ARG A 4   ? 0.7609 0.7578 0.5156 -0.0844 -0.0355 -0.0178 7   ARG A NH2 
50   N N   . PRO A 5   ? 0.5504 0.5609 0.3530 -0.0039 0.1205  0.0313  8   PRO A N   
51   C CA  . PRO A 5   ? 0.5206 0.5583 0.3780 0.0022  0.1412  0.0355  8   PRO A CA  
52   C C   . PRO A 5   ? 0.5104 0.5637 0.4252 -0.0022 0.1235  0.0338  8   PRO A C   
53   O O   . PRO A 5   ? 0.4736 0.5515 0.4295 0.0040  0.1339  0.0327  8   PRO A O   
54   C CB  . PRO A 5   ? 0.5846 0.6380 0.4471 -0.0059 0.1583  0.0587  8   PRO A CB  
55   C CG  . PRO A 5   ? 0.7473 0.7765 0.5658 -0.0128 0.1419  0.0683  8   PRO A CG  
56   C CD  . PRO A 5   ? 0.5525 0.5613 0.3258 -0.0094 0.1230  0.0512  8   PRO A CD  
64   N N   . GLU A 6   ? 0.4109 0.4536 0.3286 -0.0099 0.0980  0.0354  9   GLU A N   
65   C CA  . GLU A 6   ? 0.3657 0.4154 0.3267 -0.0127 0.0831  0.0322  9   GLU A CA  
66   C C   . GLU A 6   ? 0.3706 0.4160 0.3363 -0.0053 0.0737  0.0142  9   GLU A C   
67   O O   . GLU A 6   ? 0.3165 0.3675 0.3144 -0.0064 0.0622  0.0117  9   GLU A O   
68   C CB  . GLU A 6   ? 0.4219 0.4571 0.3790 -0.0171 0.0657  0.0430  9   GLU A CB  
69   C CG  . GLU A 6   ? 0.4153 0.4462 0.3434 -0.0122 0.0469  0.0416  9   GLU A CG  
70   C CD  . GLU A 6   ? 0.4714 0.4988 0.3560 -0.0122 0.0483  0.0540  9   GLU A CD  
71   O OE1 . GLU A 6   ? 0.4972 0.5196 0.3632 -0.0140 0.0672  0.0595  9   GLU A OE1 
72   O OE2 . GLU A 6   ? 0.4644 0.5002 0.3317 -0.0109 0.0297  0.0611  9   GLU A OE2 
79   N N   . TRP A 7   ? 0.3897 0.4172 0.3169 0.0009  0.0800  0.0014  10  TRP A N   
80   C CA  . TRP A 7   ? 0.3880 0.3975 0.3101 0.0035  0.0702  -0.0149 10  TRP A CA  
81   C C   . TRP A 7   ? 0.3908 0.4161 0.3584 0.0157  0.0788  -0.0158 10  TRP A C   
82   O O   . TRP A 7   ? 0.3679 0.3871 0.3502 0.0158  0.0660  -0.0221 10  TRP A O   
83   C CB  . TRP A 7   ? 0.4666 0.4363 0.3230 0.0050  0.0797  -0.0301 10  TRP A CB  
84   C CG  . TRP A 7   ? 0.5886 0.5480 0.4352 0.0269  0.1130  -0.0341 10  TRP A CG  
85   C CD1 . TRP A 7   ? 0.6266 0.5939 0.4565 0.0364  0.1390  -0.0261 10  TRP A CD1 
86   C CD2 . TRP A 7   ? 0.5556 0.4978 0.4086 0.0471  0.1281  -0.0427 10  TRP A CD2 
87   N NE1 . TRP A 7   ? 0.7347 0.6970 0.5644 0.0634  0.1709  -0.0284 10  TRP A NE1 
88   C CE2 . TRP A 7   ? 0.6390 0.5844 0.4821 0.0723  0.1646  -0.0379 10  TRP A CE2 
89   C CE3 . TRP A 7   ? 0.5733 0.4974 0.4376 0.0489  0.1165  -0.0512 10  TRP A CE3 
90   C CZ2 . TRP A 7   ? 0.8152 0.7476 0.6608 0.1040  0.1905  -0.0398 10  TRP A CZ2 
91   C CZ3 . TRP A 7   ? 0.7474 0.6528 0.6110 0.0771  0.1398  -0.0541 10  TRP A CZ3 
92   C CH2 . TRP A 7   ? 0.7347 0.6452 0.5898 0.1068  0.1769  -0.0476 10  TRP A CH2 
103  N N   . ILE A 8   ? 0.3575 0.4105 0.3500 0.0256  0.1007  -0.0059 11  ILE A N   
104  C CA  . ILE A 8   ? 0.3301 0.4087 0.3664 0.0391  0.1066  -0.0028 11  ILE A CA  
105  C C   . ILE A 8   ? 0.2845 0.3806 0.3606 0.0249  0.0827  0.0014  11  ILE A C   
106  O O   . ILE A 8   ? 0.3036 0.4035 0.3996 0.0326  0.0757  -0.0014 11  ILE A O   
107  C CB  . ILE A 8   ? 0.4034 0.5272 0.4684 0.0508  0.1335  0.0133  11  ILE A CB  
108  C CG1 . ILE A 8   ? 0.4456 0.6173 0.5688 0.0609  0.1331  0.0247  11  ILE A CG1 
109  C CG2 . ILE A 8   ? 0.4068 0.5557 0.4863 0.0273  0.1315  0.0282  11  ILE A CG2 
110  C CD1 . ILE A 8   ? 0.6717 0.8164 0.7841 0.0869  0.1357  0.0146  11  ILE A CD1 
122  N N   . TRP A 9   ? 0.2690 0.3676 0.3492 0.0055  0.0714  0.0088  12  TRP A N   
123  C CA  . TRP A 9   ? 0.2406 0.3409 0.3438 -0.0066 0.0522  0.0105  12  TRP A CA  
124  C C   . TRP A 9   ? 0.2773 0.3494 0.3638 -0.0033 0.0362  0.0001  12  TRP A C   
125  O O   . TRP A 9   ? 0.2550 0.3269 0.3574 -0.0046 0.0248  -0.0018 12  TRP A O   
126  C CB  . TRP A 9   ? 0.2516 0.3452 0.3514 -0.0262 0.0497  0.0215  12  TRP A CB  
127  C CG  . TRP A 9   ? 0.2653 0.3896 0.3796 -0.0354 0.0672  0.0350  12  TRP A CG  
128  C CD1 . TRP A 9   ? 0.2935 0.4085 0.3850 -0.0415 0.0799  0.0443  12  TRP A CD1 
129  C CD2 . TRP A 9   ? 0.2763 0.4531 0.4335 -0.0391 0.0745  0.0448  12  TRP A CD2 
130  N NE1 . TRP A 9   ? 0.3497 0.5070 0.4676 -0.0503 0.0969  0.0582  12  TRP A NE1 
131  C CE2 . TRP A 9   ? 0.3279 0.5285 0.4894 -0.0486 0.0932  0.0597  12  TRP A CE2 
132  C CE3 . TRP A 9   ? 0.2823 0.4945 0.4761 -0.0339 0.0668  0.0458  12  TRP A CE3 
133  C CZ2 . TRP A 9   ? 0.3442 0.6115 0.5523 -0.0549 0.1052  0.0774  12  TRP A CZ2 
134  C CZ3 . TRP A 9   ? 0.2403 0.5218 0.4805 -0.0375 0.0777  0.0649  12  TRP A CZ3 
135  C CH2 . TRP A 9   ? 0.2828 0.5923 0.5312 -0.0483 0.0961  0.0801  12  TRP A CH2 
146  N N   . LEU A 10  ? 0.2731 0.3261 0.3272 -0.0018 0.0344  -0.0042 13  LEU A N   
147  C CA  . LEU A 10  ? 0.2678 0.3073 0.3117 -0.0024 0.0197  -0.0105 13  LEU A CA  
148  C C   . LEU A 10  ? 0.2705 0.2997 0.3154 0.0041  0.0208  -0.0215 13  LEU A C   
149  O O   . LEU A 10  ? 0.2835 0.3086 0.3373 0.0024  0.0097  -0.0232 13  LEU A O   
150  C CB  . LEU A 10  ? 0.2752 0.3075 0.2837 -0.0082 0.0143  -0.0096 13  LEU A CB  
151  C CG  . LEU A 10  ? 0.2939 0.3340 0.2982 -0.0092 0.0126  0.0063  13  LEU A CG  
152  C CD1 . LEU A 10  ? 0.3358 0.3787 0.3038 -0.0150 0.0046  0.0099  13  LEU A CD1 
153  C CD2 . LEU A 10  ? 0.3047 0.3472 0.3295 -0.0050 0.0040  0.0149  13  LEU A CD2 
165  N N   . ALA A 11  ? 0.3164 0.3375 0.3489 0.0149  0.0377  -0.0268 14  ALA A N   
166  C CA  . ALA A 11  ? 0.2902 0.2890 0.3150 0.0278  0.0444  -0.0349 14  ALA A CA  
167  C C   . ALA A 11  ? 0.2945 0.3203 0.3638 0.0366  0.0408  -0.0267 14  ALA A C   
168  O O   . ALA A 11  ? 0.2942 0.3045 0.3642 0.0395  0.0334  -0.0295 14  ALA A O   
169  C CB  . ALA A 11  ? 0.3412 0.3191 0.3347 0.0447  0.0700  -0.0398 14  ALA A CB  
175  N N   A LEU A 12  ? 0.3124 0.3794 0.4162 0.0369  0.0445  -0.0148 15  LEU A N   
176  N N   B LEU A 12  ? 0.3114 0.3786 0.4156 0.0369  0.0444  -0.0147 15  LEU A N   
177  C CA  A LEU A 12  ? 0.2641 0.3635 0.4066 0.0378  0.0358  -0.0053 15  LEU A CA  
178  C CA  B LEU A 12  ? 0.2643 0.3626 0.4065 0.0381  0.0354  -0.0056 15  LEU A CA  
179  C C   A LEU A 12  ? 0.2803 0.3662 0.4213 0.0229  0.0153  -0.0084 15  LEU A C   
180  C C   B LEU A 12  ? 0.2810 0.3660 0.4215 0.0229  0.0149  -0.0087 15  LEU A C   
181  O O   A LEU A 12  ? 0.2620 0.3492 0.4123 0.0277  0.0070  -0.0071 15  LEU A O   
182  O O   B LEU A 12  ? 0.2631 0.3492 0.4128 0.0272  0.0063  -0.0074 15  LEU A O   
183  C CB  A LEU A 12  ? 0.2321 0.3815 0.4082 0.0297  0.0406  0.0094  15  LEU A CB  
184  C CB  B LEU A 12  ? 0.2347 0.3848 0.4126 0.0310  0.0396  0.0095  15  LEU A CB  
185  C CG  A LEU A 12  ? 0.2976 0.4944 0.5148 0.0255  0.0296  0.0230  15  LEU A CG  
186  C CG  B LEU A 12  ? 0.2490 0.4316 0.4429 0.0531  0.0638  0.0199  15  LEU A CG  
187  C CD1 A LEU A 12  ? 0.3213 0.5333 0.5537 0.0555  0.0357  0.0294  15  LEU A CD1 
188  C CD1 B LEU A 12  ? 0.2465 0.4817 0.4720 0.0360  0.0684  0.0361  15  LEU A CD1 
189  C CD2 A LEU A 12  ? 0.2937 0.5452 0.5428 0.0115  0.0365  0.0396  15  LEU A CD2 
190  C CD2 B LEU A 12  ? 0.3187 0.5255 0.5373 0.0788  0.0677  0.0295  15  LEU A CD2 
213  N N   . GLY A 13  ? 0.2419 0.3128 0.3673 0.0091  0.0094  -0.0106 16  GLY A N   
214  C CA  . GLY A 13  ? 0.2457 0.3006 0.3648 0.0024  -0.0035 -0.0117 16  GLY A CA  
215  C C   . GLY A 13  ? 0.2710 0.3094 0.3801 0.0086  -0.0078 -0.0171 16  GLY A C   
216  O O   . GLY A 13  ? 0.2744 0.3085 0.3870 0.0093  -0.0149 -0.0163 16  GLY A O   
220  N N   . THR A 14  ? 0.2527 0.2785 0.3436 0.0095  -0.0033 -0.0225 17  THR A N   
221  C CA  . THR A 14  ? 0.2974 0.3030 0.3742 0.0072  -0.0076 -0.0271 17  THR A CA  
222  C C   . THR A 14  ? 0.2999 0.2962 0.3838 0.0195  -0.0043 -0.0272 17  THR A C   
223  O O   . THR A 14  ? 0.3016 0.2886 0.3851 0.0180  -0.0103 -0.0254 17  THR A O   
224  C CB  . THR A 14  ? 0.2977 0.2813 0.3414 -0.0003 -0.0038 -0.0350 17  THR A CB  
225  O OG1 . THR A 14  ? 0.2977 0.2976 0.3347 -0.0108 -0.0095 -0.0308 17  THR A OG1 
226  C CG2 . THR A 14  ? 0.3613 0.3181 0.3837 -0.0134 -0.0104 -0.0393 17  THR A CG2 
234  N N   . ALA A 15  ? 0.2767 0.2784 0.3667 0.0344  0.0071  -0.0261 18  ALA A N   
235  C CA  . ALA A 15  ? 0.2793 0.2763 0.3763 0.0530  0.0118  -0.0210 18  ALA A CA  
236  C C   . ALA A 15  ? 0.2987 0.3237 0.4215 0.0504  -0.0026 -0.0119 18  ALA A C   
237  O O   . ALA A 15  ? 0.3386 0.3499 0.4567 0.0568  -0.0066 -0.0083 18  ALA A O   
238  C CB  . ALA A 15  ? 0.3162 0.3299 0.4235 0.0757  0.0301  -0.0151 18  ALA A CB  
244  N N   . LEU A 16  ? 0.2448 0.3022 0.3870 0.0390  -0.0100 -0.0079 19  LEU A N   
245  C CA  . LEU A 16  ? 0.2349 0.3101 0.3883 0.0316  -0.0247 -0.0014 19  LEU A CA  
246  C C   . LEU A 16  ? 0.2843 0.3295 0.4153 0.0240  -0.0316 -0.0065 19  LEU A C   
247  O O   . LEU A 16  ? 0.2692 0.3127 0.3958 0.0255  -0.0399 -0.0023 19  LEU A O   
248  C CB  . LEU A 16  ? 0.2475 0.3510 0.4148 0.0138  -0.0307 0.0027  19  LEU A CB  
249  C CG  . LEU A 16  ? 0.2162 0.3701 0.4169 0.0182  -0.0244 0.0148  19  LEU A CG  
250  C CD1 . LEU A 16  ? 0.2610 0.4353 0.4697 -0.0090 -0.0294 0.0186  19  LEU A CD1 
251  C CD2 . LEU A 16  ? 0.3484 0.5400 0.5731 0.0322  -0.0311 0.0293  19  LEU A CD2 
263  N N   . MET A 17  ? 0.2610 0.2884 0.3784 0.0179  -0.0275 -0.0122 20  MET A N   
264  C CA  . MET A 17  ? 0.2630 0.2738 0.3659 0.0155  -0.0296 -0.0118 20  MET A CA  
265  C C   . MET A 17  ? 0.2738 0.2712 0.3711 0.0201  -0.0283 -0.0103 20  MET A C   
266  O O   . MET A 17  ? 0.2940 0.2835 0.3830 0.0210  -0.0302 -0.0061 20  MET A O   
267  C CB  . MET A 17  ? 0.2502 0.2602 0.3475 0.0117  -0.0253 -0.0109 20  MET A CB  
268  C CG  . MET A 17  ? 0.2355 0.2449 0.3299 0.0084  -0.0238 -0.0108 20  MET A CG  
269  S SD  . MET A 17  ? 0.2949 0.2787 0.3664 0.0073  -0.0257 -0.0104 20  MET A SD  
270  C CE  . MET A 17  ? 0.3051 0.2709 0.3622 0.0032  -0.0185 -0.0084 20  MET A CE  
280  N N   . GLY A 18  ? 0.2913 0.2783 0.3854 0.0223  -0.0228 -0.0137 21  GLY A N   
281  C CA  . GLY A 18  ? 0.3469 0.3049 0.4250 0.0235  -0.0196 -0.0128 21  GLY A CA  
282  C C   . GLY A 18  ? 0.3327 0.2880 0.4133 0.0391  -0.0211 -0.0048 21  GLY A C   
283  O O   . GLY A 18  ? 0.3657 0.3033 0.4342 0.0383  -0.0219 0.0007  21  GLY A O   
287  N N   . LEU A 19  ? 0.3544 0.3313 0.4513 0.0536  -0.0208 -0.0009 22  LEU A N   
288  C CA  . LEU A 19  ? 0.3509 0.3411 0.4557 0.0697  -0.0259 0.0121  22  LEU A CA  
289  C C   . LEU A 19  ? 0.3420 0.3448 0.4433 0.0584  -0.0404 0.0155  22  LEU A C   
290  O O   . LEU A 19  ? 0.3527 0.3473 0.4428 0.0659  -0.0448 0.0248  22  LEU A O   
291  C CB  . LEU A 19  ? 0.3505 0.3831 0.4838 0.0841  -0.0244 0.0205  22  LEU A CB  
292  C CG  . LEU A 19  ? 0.5119 0.5263 0.6408 0.1071  -0.0039 0.0211  22  LEU A CG  
293  C CD1 . LEU A 19  ? 0.5340 0.6101 0.7014 0.1194  -0.0013 0.0335  22  LEU A CD1 
294  C CD2 . LEU A 19  ? 0.6765 0.6462 0.7813 0.1316  0.0065  0.0293  22  LEU A CD2 
306  N N   . GLY A 20  ? 0.3034 0.3184 0.4061 0.0418  -0.0462 0.0085  23  GLY A N   
307  C CA  . GLY A 20  ? 0.3305 0.3386 0.4131 0.0319  -0.0549 0.0084  23  GLY A CA  
308  C C   . GLY A 20  ? 0.3576 0.3376 0.4190 0.0341  -0.0477 0.0098  23  GLY A C   
309  O O   . GLY A 20  ? 0.3389 0.3104 0.3806 0.0363  -0.0525 0.0157  23  GLY A O   
313  N N   . THR A 21  ? 0.3164 0.2865 0.3815 0.0315  -0.0369 0.0068  24  THR A N   
314  C CA  . THR A 21  ? 0.3200 0.2758 0.3727 0.0287  -0.0294 0.0123  24  THR A CA  
315  C C   . THR A 21  ? 0.3755 0.3115 0.4163 0.0351  -0.0293 0.0209  24  THR A C   
316  O O   . THR A 21  ? 0.3595 0.2855 0.3830 0.0357  -0.0268 0.0290  24  THR A O   
317  C CB  . THR A 21  ? 0.3220 0.2819 0.3850 0.0175  -0.0231 0.0107  24  THR A CB  
318  O OG1 . THR A 21  ? 0.3021 0.2818 0.3751 0.0161  -0.0224 0.0072  24  THR A OG1 
319  C CG2 . THR A 21  ? 0.3322 0.2917 0.3903 0.0087  -0.0161 0.0212  24  THR A CG2 
327  N N   . LEU A 22  ? 0.3603 0.2852 0.4054 0.0426  -0.0286 0.0208  25  LEU A N   
328  C CA  . LEU A 22  ? 0.4030 0.2981 0.4310 0.0539  -0.0251 0.0316  25  LEU A CA  
329  C C   . LEU A 22  ? 0.4031 0.3134 0.4261 0.0674  -0.0355 0.0432  25  LEU A C   
330  O O   . LEU A 22  ? 0.4288 0.3172 0.4300 0.0725  -0.0336 0.0550  25  LEU A O   
331  C CB  . LEU A 22  ? 0.4328 0.3055 0.4598 0.0672  -0.0172 0.0297  25  LEU A CB  
332  C CG  . LEU A 22  ? 0.6398 0.4800 0.6526 0.0490  -0.0081 0.0179  25  LEU A CG  
333  C CD1 . LEU A 22  ? 0.6748 0.4839 0.6748 0.0669  0.0034  0.0135  25  LEU A CD1 
334  C CD2 . LEU A 22  ? 0.6733 0.4741 0.6598 0.0288  -0.0034 0.0225  25  LEU A CD2 
346  N N   . TYR A 23  ? 0.3386 0.2864 0.3780 0.0699  -0.0478 0.0417  26  TYR A N   
347  C CA  . TYR A 23  ? 0.4026 0.3709 0.4338 0.0760  -0.0634 0.0540  26  TYR A CA  
348  C C   . TYR A 23  ? 0.3796 0.3295 0.3764 0.0642  -0.0650 0.0524  26  TYR A C   
349  O O   . TYR A 23  ? 0.4212 0.3606 0.3939 0.0712  -0.0689 0.0650  26  TYR A O   
350  C CB  . TYR A 23  ? 0.3325 0.3483 0.3876 0.0700  -0.0785 0.0529  26  TYR A CB  
351  C CG  . TYR A 23  ? 0.3914 0.4361 0.4356 0.0662  -0.1008 0.0655  26  TYR A CG  
352  C CD1 . TYR A 23  ? 0.5815 0.6491 0.6338 0.0883  -0.1080 0.0885  26  TYR A CD1 
353  C CD2 . TYR A 23  ? 0.4337 0.4775 0.4516 0.0405  -0.1146 0.0557  26  TYR A CD2 
354  C CE1 . TYR A 23  ? 0.5437 0.6468 0.5846 0.0821  -0.1333 0.1035  26  TYR A CE1 
355  C CE2 . TYR A 23  ? 0.4672 0.5350 0.4634 0.0297  -0.1403 0.0670  26  TYR A CE2 
356  C CZ  . TYR A 23  ? 0.5652 0.6689 0.5770 0.0491  -0.1510 0.0913  26  TYR A CZ  
357  O OH  . TYR A 23  ? 0.6980 0.8326 0.6878 0.0353  -0.1799 0.1045  26  TYR A OH  
367  N N   . PHE A 24  ? 0.3748 0.3185 0.3656 0.0501  -0.0589 0.0387  27  PHE A N   
368  C CA  . PHE A 24  ? 0.4132 0.3361 0.3663 0.0453  -0.0540 0.0380  27  PHE A CA  
369  C C   . PHE A 24  ? 0.4250 0.3281 0.3681 0.0504  -0.0387 0.0490  27  PHE A C   
370  O O   . PHE A 24  ? 0.4797 0.3670 0.3880 0.0529  -0.0353 0.0565  27  PHE A O   
371  C CB  . PHE A 24  ? 0.3806 0.2979 0.3299 0.0380  -0.0443 0.0253  27  PHE A CB  
372  C CG  . PHE A 24  ? 0.3629 0.2853 0.3080 0.0269  -0.0574 0.0145  27  PHE A CG  
373  C CD1 . PHE A 24  ? 0.4082 0.3429 0.3422 0.0178  -0.0793 0.0168  27  PHE A CD1 
374  C CD2 . PHE A 24  ? 0.3732 0.2906 0.3253 0.0233  -0.0484 0.0052  27  PHE A CD2 
375  C CE1 . PHE A 24  ? 0.4790 0.4196 0.4082 -0.0013 -0.0926 0.0086  27  PHE A CE1 
376  C CE2 . PHE A 24  ? 0.4144 0.3267 0.3561 0.0087  -0.0586 -0.0038 27  PHE A CE2 
377  C CZ  . PHE A 24  ? 0.4446 0.3695 0.3766 -0.0069 -0.0812 -0.0026 27  PHE A CZ  
387  N N   . LEU A 25  ? 0.4157 0.3164 0.3833 0.0479  -0.0288 0.0501  28  LEU A N   
388  C CA  . LEU A 25  ? 0.4726 0.3532 0.4300 0.0439  -0.0156 0.0619  28  LEU A CA  
389  C C   . LEU A 25  ? 0.5629 0.4192 0.4970 0.0554  -0.0194 0.0764  28  LEU A C   
390  O O   . LEU A 25  ? 0.5862 0.4262 0.4935 0.0552  -0.0116 0.0891  28  LEU A O   
391  C CB  . LEU A 25  ? 0.5207 0.3978 0.5004 0.0307  -0.0092 0.0581  28  LEU A CB  
392  C CG  . LEU A 25  ? 0.7590 0.6185 0.7293 0.0149  0.0032  0.0707  28  LEU A CG  
393  C CD1 . LEU A 25  ? 0.6466 0.5453 0.6366 0.0022  0.0118  0.0731  28  LEU A CD1 
394  C CD2 . LEU A 25  ? 0.9025 0.7270 0.8691 0.0029  0.0041  0.0680  28  LEU A CD2 
406  N N   . VAL A 26  ? 0.4899 0.3463 0.4327 0.0693  -0.0294 0.0784  29  VAL A N   
407  C CA  . VAL A 26  ? 0.5577 0.3938 0.4782 0.0868  -0.0322 0.0976  29  VAL A CA  
408  C C   . VAL A 26  ? 0.5857 0.4398 0.4810 0.0902  -0.0461 0.1050  29  VAL A C   
409  O O   . VAL A 26  ? 0.6205 0.4529 0.4828 0.0966  -0.0437 0.1216  29  VAL A O   
410  C CB  . VAL A 26  ? 0.5565 0.3957 0.4953 0.1090  -0.0362 0.1031  29  VAL A CB  
411  C CG1 . VAL A 26  ? 0.6400 0.4656 0.5577 0.1345  -0.0394 0.1283  29  VAL A CG1 
412  C CG2 . VAL A 26  ? 0.6987 0.5005 0.6425 0.1042  -0.0196 0.0934  29  VAL A CG2 
422  N N   . LYS A 27  ? 0.5118 0.3997 0.4146 0.0834  -0.0616 0.0935  30  LYS A N   
423  C CA  . LYS A 27  ? 0.5239 0.4195 0.3891 0.0792  -0.0774 0.0970  30  LYS A CA  
424  C C   . LYS A 27  ? 0.5940 0.4566 0.4152 0.0736  -0.0614 0.0970  30  LYS A C   
425  O O   . LYS A 27  ? 0.7064 0.5574 0.4828 0.0766  -0.0680 0.1081  30  LYS A O   
426  C CB  . LYS A 27  ? 0.5684 0.4906 0.4395 0.0633  -0.0938 0.0810  30  LYS A CB  
427  C CG  . LYS A 27  ? 0.8167 0.7646 0.6642 0.0569  -0.1230 0.0901  30  LYS A CG  
428  C CD  . LYS A 27  ? 0.9649 0.9552 0.8403 0.0400  -0.1433 0.0826  30  LYS A CD  
429  C CE  . LYS A 27  ? 1.0807 1.0836 0.9114 0.0155  -0.1736 0.0840  30  LYS A CE  
430  N NZ  . LYS A 27  ? 0.9777 0.9211 0.7418 -0.0053 -0.1661 0.0612  30  LYS A NZ  
444  N N   . GLY A 28  ? 0.5721 0.4246 0.4047 0.0668  -0.0396 0.0876  31  GLY A N   
445  C CA  . GLY A 28  ? 0.6655 0.4977 0.4609 0.0656  -0.0202 0.0911  31  GLY A CA  
446  C C   . GLY A 28  ? 0.7334 0.5483 0.5206 0.0683  -0.0045 0.1113  31  GLY A C   
447  O O   . GLY A 28  ? 0.7044 0.5090 0.4639 0.0682  0.0152  0.1187  31  GLY A O   
451  N N   . MET A 29  ? 0.9023 0.5577 0.5427 0.0895  -0.0627 0.1191  32  MET A N   
452  C CA  . MET A 29  ? 1.0591 0.6478 0.6398 0.0821  -0.0516 0.1356  32  MET A CA  
453  C C   . MET A 29  ? 1.0007 0.5722 0.5356 0.0955  -0.0574 0.1443  32  MET A C   
454  O O   . MET A 29  ? 1.1807 0.7688 0.7188 0.1233  -0.0759 0.1401  32  MET A O   
455  C CB  . MET A 29  ? 1.0800 0.6315 0.6522 0.0952  -0.0549 0.1376  32  MET A CB  
456  C CG  . MET A 29  ? 1.3019 0.8321 0.8823 0.0709  -0.0395 0.1368  32  MET A CG  
457  S SD  . MET A 29  ? 1.2690 0.7671 0.8450 0.0912  -0.0451 0.1337  32  MET A SD  
458  C CE  . MET A 29  ? 1.1847 0.6204 0.6990 0.0823  -0.0331 0.1459  32  MET A CE  
468  N N   . GLY A 30  ? 1.1231 0.6721 0.6240 0.0737  -0.0404 0.1528  33  GLY A N   
469  C CA  . GLY A 30  ? 1.2142 0.7496 0.6751 0.0837  -0.0433 0.1593  33  GLY A CA  
470  C C   . GLY A 30  ? 1.2011 0.7769 0.6646 0.0886  -0.0506 0.1544  33  GLY A C   
471  O O   . GLY A 30  ? 1.2468 0.8124 0.6746 0.0927  -0.0503 0.1596  33  GLY A O   
475  N N   . VAL A 31  ? 0.9875 0.6177 0.5031 0.0860  -0.0556 0.1400  34  VAL A N   
476  C CA  . VAL A 31  ? 0.9101 0.5837 0.4371 0.0835  -0.0572 0.1303  34  VAL A CA  
477  C C   . VAL A 31  ? 0.9752 0.6354 0.4746 0.0562  -0.0329 0.1370  34  VAL A C   
478  O O   . VAL A 31  ? 1.0073 0.6665 0.5237 0.0310  -0.0143 0.1372  34  VAL A O   
479  C CB  . VAL A 31  ? 0.9242 0.6599 0.5219 0.0808  -0.0627 0.1105  34  VAL A CB  
480  C CG1 . VAL A 31  ? 0.9176 0.6917 0.5246 0.0754  -0.0611 0.0996  34  VAL A CG1 
481  C CG2 . VAL A 31  ? 0.8983 0.6506 0.5208 0.1065  -0.0855 0.1033  34  VAL A CG2 
491  N N   . SER A 32  ? 0.9800 0.6314 0.4351 0.0610  -0.0328 0.1420  35  SER A N   
492  C CA  . SER A 32  ? 1.0425 0.6822 0.4671 0.0357  -0.0083 0.1484  35  SER A CA  
493  C C   . SER A 32  ? 1.1220 0.8133 0.5685 0.0294  -0.0035 0.1340  35  SER A C   
494  O O   . SER A 32  ? 1.1358 0.8344 0.5770 0.0056  0.0196  0.1342  35  SER A O   
495  C CB  . SER A 32  ? 1.2064 0.7949 0.5664 0.0409  -0.0054 0.1646  35  SER A CB  
496  O OG  . SER A 32  ? 1.3266 0.9212 0.6740 0.0713  -0.0292 0.1622  35  SER A OG  
502  N N   . ASP A 33  ? 0.9050 0.6329 0.3763 0.0493  -0.0237 0.1202  36  ASP A N   
503  C CA  . ASP A 33  ? 0.8517 0.6226 0.3400 0.0448  -0.0196 0.1051  36  ASP A CA  
504  C C   . ASP A 33  ? 0.7355 0.5434 0.2792 0.0243  -0.0032 0.0938  36  ASP A C   
505  O O   . ASP A 33  ? 0.6861 0.5115 0.2775 0.0260  -0.0104 0.0870  36  ASP A O   
506  C CB  . ASP A 33  ? 0.9335 0.7343 0.4421 0.0674  -0.0452 0.0905  36  ASP A CB  
507  C CG  . ASP A 33  ? 0.9208 0.7601 0.4439 0.0634  -0.0417 0.0731  36  ASP A CG  
508  O OD1 . ASP A 33  ? 0.9659 0.7960 0.4442 0.0629  -0.0354 0.0757  36  ASP A OD1 
509  O OD2 . ASP A 33  ? 0.8275 0.7027 0.4035 0.0604  -0.0436 0.0571  36  ASP A OD2 
514  N N   . PRO A 34  ? 0.8346 0.6591 0.3739 0.0075  0.0176  0.0902  37  PRO A N   
515  C CA  . PRO A 34  ? 0.8415 0.7032 0.4326 -0.0090 0.0323  0.0799  37  PRO A CA  
516  C C   . PRO A 34  ? 0.7517 0.6527 0.3961 0.0021  0.0197  0.0620  37  PRO A C   
517  O O   . PRO A 34  ? 0.6515 0.5731 0.3401 -0.0051 0.0239  0.0566  37  PRO A O   
518  C CB  . PRO A 34  ? 0.8768 0.7522 0.4473 -0.0242 0.0556  0.0781  37  PRO A CB  
519  C CG  . PRO A 34  ? 0.9573 0.8058 0.4671 -0.0142 0.0515  0.0851  37  PRO A CG  
520  C CD  . PRO A 34  ? 0.8427 0.6539 0.3275 0.0044  0.0287  0.0955  37  PRO A CD  
528  N N   . ASP A 35  ? 0.6714 0.5822 0.3108 0.0182  0.0048  0.0521  38  ASP A N   
529  C CA  . ASP A 35  ? 0.6437 0.5852 0.3302 0.0260  -0.0059 0.0350  38  ASP A CA  
530  C C   . ASP A 35  ? 0.5861 0.5231 0.3012 0.0329  -0.0217 0.0366  38  ASP A C   
531  O O   . ASP A 35  ? 0.5474 0.5032 0.3071 0.0297  -0.0210 0.0293  38  ASP A O   
532  C CB  . ASP A 35  ? 0.6718 0.6223 0.3416 0.0384  -0.0172 0.0225  38  ASP A CB  
533  C CG  . ASP A 35  ? 0.9642 0.9292 0.6202 0.0327  -0.0003 0.0145  38  ASP A CG  
534  O OD1 . ASP A 35  ? 1.1133 1.0904 0.7839 0.0203  0.0193  0.0160  38  ASP A OD1 
535  O OD2 . ASP A 35  ? 1.4135 1.3806 1.0446 0.0411  -0.0067 0.0053  38  ASP A OD2 
540  N N   . ALA A 36  ? 0.5784 0.4896 0.2664 0.0434  -0.0351 0.0467  39  ALA A N   
541  C CA  . ALA A 36  ? 0.5583 0.4668 0.2728 0.0512  -0.0487 0.0480  39  ALA A CA  
542  C C   . ALA A 36  ? 0.5345 0.4348 0.2696 0.0378  -0.0360 0.0554  39  ALA A C   
543  O O   . ALA A 36  ? 0.4954 0.4086 0.2694 0.0387  -0.0410 0.0502  39  ALA A O   
544  C CB  . ALA A 36  ? 0.6224 0.5045 0.3002 0.0683  -0.0649 0.0577  39  ALA A CB  
550  N N   . LYS A 37  ? 0.5683 0.4463 0.2751 0.0239  -0.0194 0.0673  40  LYS A N   
551  C CA  . LYS A 37  ? 0.5610 0.4342 0.2873 0.0079  -0.0069 0.0720  40  LYS A CA  
552  C C   . LYS A 37  ? 0.5096 0.4229 0.2880 0.0015  -0.0024 0.0589  40  LYS A C   
553  O O   . LYS A 37  ? 0.5296 0.4470 0.3375 -0.0028 -0.0027 0.0582  40  LYS A O   
554  C CB  . LYS A 37  ? 0.6134 0.4656 0.3034 -0.0113 0.0136  0.0827  40  LYS A CB  
555  C CG  . LYS A 37  ? 0.8139 0.6127 0.4456 -0.0086 0.0131  0.0997  40  LYS A CG  
556  C CD  . LYS A 37  ? 0.9594 0.7287 0.5728 -0.0330 0.0325  0.1105  40  LYS A CD  
557  C CE  . LYS A 37  ? 1.0742 0.8127 0.6308 -0.0450 0.0482  0.1223  40  LYS A CE  
558  N NZ  . LYS A 37  ? 1.2114 0.9378 0.7626 -0.0767 0.0718  0.1273  40  LYS A NZ  
572  N N   . LYS A 38  ? 0.4806 0.4219 0.2686 0.0015  0.0025  0.0484  41  LYS A N   
573  C CA  . LYS A 38  ? 0.4348 0.4097 0.2674 -0.0007 0.0062  0.0365  41  LYS A CA  
574  C C   . LYS A 38  ? 0.4197 0.3999 0.2834 0.0103  -0.0093 0.0302  41  LYS A C   
575  O O   . LYS A 38  ? 0.3834 0.3735 0.2778 0.0069  -0.0081 0.0283  41  LYS A O   
576  C CB  . LYS A 38  ? 0.5053 0.5030 0.3369 0.0030  0.0118  0.0251  41  LYS A CB  
577  C CG  . LYS A 38  ? 0.6208 0.6323 0.4418 -0.0095 0.0317  0.0258  41  LYS A CG  
578  C CD  . LYS A 38  ? 0.6594 0.6851 0.4674 -0.0017 0.0351  0.0149  41  LYS A CD  
579  C CE  . LYS A 38  ? 1.0125 1.0655 0.8566 0.0070  0.0347  -0.0002 41  LYS A CE  
580  N NZ  . LYS A 38  ? 1.3469 1.4118 1.1758 0.0142  0.0410  -0.0120 41  LYS A NZ  
594  N N   . PHE A 39  ? 0.4089 0.3844 0.2644 0.0229  -0.0239 0.0260  42  PHE A N   
595  C CA  . PHE A 39  ? 0.3948 0.3779 0.2800 0.0303  -0.0367 0.0192  42  PHE A CA  
596  C C   . PHE A 39  ? 0.3733 0.3424 0.2659 0.0306  -0.0407 0.0278  42  PHE A C   
597  O O   . PHE A 39  ? 0.3628 0.3415 0.2865 0.0301  -0.0426 0.0237  42  PHE A O   
598  C CB  . PHE A 39  ? 0.4280 0.4139 0.3027 0.0417  -0.0519 0.0114  42  PHE A CB  
599  C CG  . PHE A 39  ? 0.4017 0.4013 0.2743 0.0416  -0.0494 -0.0014 42  PHE A CG  
600  C CD1 . PHE A 39  ? 0.4321 0.4454 0.3353 0.0394  -0.0469 -0.0133 42  PHE A CD1 
601  C CD2 . PHE A 39  ? 0.4569 0.4516 0.2938 0.0442  -0.0485 -0.0015 42  PHE A CD2 
602  C CE1 . PHE A 39  ? 0.4435 0.4633 0.3415 0.0406  -0.0441 -0.0261 42  PHE A CE1 
603  C CE2 . PHE A 39  ? 0.5189 0.5247 0.3518 0.0450  -0.0457 -0.0153 42  PHE A CE2 
604  C CZ  . PHE A 39  ? 0.5494 0.5668 0.4136 0.0435  -0.0436 -0.0280 42  PHE A CZ  
614  N N   . TYR A 40  ? 0.4069 0.3498 0.2682 0.0321  -0.0415 0.0397  43  TYR A N   
615  C CA  . TYR A 40  ? 0.4053 0.3310 0.2721 0.0332  -0.0440 0.0467  43  TYR A CA  
616  C C   . TYR A 40  ? 0.3876 0.3174 0.2739 0.0179  -0.0310 0.0479  43  TYR A C   
617  O O   . TYR A 40  ? 0.3967 0.3270 0.3046 0.0183  -0.0335 0.0469  43  TYR A O   
618  C CB  . TYR A 40  ? 0.4552 0.3430 0.2782 0.0382  -0.0459 0.0600  43  TYR A CB  
619  C CG  . TYR A 40  ? 0.4926 0.3752 0.3042 0.0599  -0.0646 0.0595  43  TYR A CG  
620  C CD1 . TYR A 40  ? 0.4910 0.3706 0.3186 0.0712  -0.0739 0.0590  43  TYR A CD1 
621  C CD2 . TYR A 40  ? 0.5247 0.4110 0.3127 0.0695  -0.0729 0.0578  43  TYR A CD2 
622  C CE1 . TYR A 40  ? 0.5583 0.4412 0.3794 0.0930  -0.0918 0.0568  43  TYR A CE1 
623  C CE2 . TYR A 40  ? 0.5631 0.4520 0.3430 0.0909  -0.0924 0.0556  43  TYR A CE2 
624  C CZ  . TYR A 40  ? 0.5730 0.4627 0.3729 0.1024  -0.1014 0.0547  43  TYR A CZ  
625  O OH  . TYR A 40  ? 0.6454 0.5440 0.4402 0.1257  -0.1211 0.0513  43  TYR A OH  
635  N N   . ALA A 41  ? 0.3961 0.3321 0.2758 0.0042  -0.0169 0.0491  44  ALA A N   
636  C CA  . ALA A 41  ? 0.3996 0.3459 0.2998 -0.0103 -0.0061 0.0487  44  ALA A CA  
637  C C   . ALA A 41  ? 0.4032 0.3783 0.3431 -0.0060 -0.0095 0.0386  44  ALA A C   
638  O O   . ALA A 41  ? 0.3564 0.3332 0.3152 -0.0088 -0.0103 0.0381  44  ALA A O   
639  C CB  . ALA A 41  ? 0.4220 0.3778 0.3101 -0.0259 0.0100  0.0499  44  ALA A CB  
645  N N   . ILE A 42  ? 0.3297 0.3233 0.2787 0.0013  -0.0116 0.0303  45  ILE A N   
646  C CA  . ILE A 42  ? 0.3432 0.3563 0.3233 0.0059  -0.0138 0.0217  45  ILE A CA  
647  C C   . ILE A 42  ? 0.3570 0.3617 0.3499 0.0120  -0.0240 0.0212  45  ILE A C   
648  O O   . ILE A 42  ? 0.3272 0.3375 0.3405 0.0108  -0.0235 0.0200  45  ILE A O   
649  C CB  . ILE A 42  ? 0.3008 0.3264 0.2819 0.0129  -0.0139 0.0121  45  ILE A CB  
650  C CG1 . ILE A 42  ? 0.3456 0.3861 0.3183 0.0083  -0.0016 0.0106  45  ILE A CG1 
651  C CG2 . ILE A 42  ? 0.3376 0.3709 0.3446 0.0190  -0.0175 0.0041  45  ILE A CG2 
652  C CD1 . ILE A 42  ? 0.4307 0.4767 0.3937 0.0161  -0.0013 0.0015  45  ILE A CD1 
664  N N   . THR A 43  ? 0.2899 0.2834 0.2706 0.0194  -0.0336 0.0218  46  THR A N   
665  C CA  . THR A 43  ? 0.3043 0.2994 0.3020 0.0260  -0.0429 0.0180  46  THR A CA  
666  C C   . THR A 43  ? 0.3939 0.3760 0.3933 0.0254  -0.0432 0.0246  46  THR A C   
667  O O   . THR A 43  ? 0.3607 0.3485 0.3798 0.0283  -0.0465 0.0210  46  THR A O   
668  C CB  . THR A 43  ? 0.3308 0.3262 0.3176 0.0355  -0.0544 0.0142  46  THR A CB  
669  O OG1 . THR A 43  ? 0.3434 0.3485 0.3253 0.0347  -0.0534 0.0065  46  THR A OG1 
670  C CG2 . THR A 43  ? 0.4153 0.4224 0.4257 0.0409  -0.0635 0.0068  46  THR A CG2 
678  N N   . THR A 44  ? 0.3172 0.2796 0.2938 0.0211  -0.0389 0.0336  47  THR A N   
679  C CA  . THR A 44  ? 0.3332 0.2778 0.3078 0.0199  -0.0382 0.0387  47  THR A CA  
680  C C   . THR A 44  ? 0.3355 0.2907 0.3287 0.0083  -0.0300 0.0368  47  THR A C   
681  O O   . THR A 44  ? 0.3140 0.2653 0.3177 0.0090  -0.0310 0.0360  47  THR A O   
682  C CB  . THR A 44  ? 0.3668 0.2792 0.3056 0.0171  -0.0353 0.0487  47  THR A CB  
683  O OG1 . THR A 44  ? 0.4165 0.3186 0.3338 0.0313  -0.0449 0.0512  47  THR A OG1 
684  C CG2 . THR A 44  ? 0.3996 0.2844 0.3305 0.0165  -0.0344 0.0531  47  THR A CG2 
692  N N   . LEU A 45  ? 0.3050 0.2762 0.3024 -0.0006 -0.0224 0.0352  48  LEU A N   
693  C CA  . LEU A 45  ? 0.2583 0.2452 0.2740 -0.0087 -0.0168 0.0324  48  LEU A CA  
694  C C   . LEU A 45  ? 0.2787 0.2776 0.3173 -0.0011 -0.0212 0.0272  48  LEU A C   
695  O O   . LEU A 45  ? 0.2685 0.2715 0.3171 -0.0046 -0.0197 0.0265  48  LEU A O   
696  C CB  . LEU A 45  ? 0.2733 0.2828 0.2925 -0.0156 -0.0088 0.0299  48  LEU A CB  
697  C CG  . LEU A 45  ? 0.4042 0.4101 0.4071 -0.0309 0.0006  0.0338  48  LEU A CG  
698  C CD1 . LEU A 45  ? 0.4320 0.4681 0.4412 -0.0342 0.0088  0.0291  48  LEU A CD1 
699  C CD2 . LEU A 45  ? 0.3429 0.3490 0.3541 -0.0425 0.0028  0.0333  48  LEU A CD2 
711  N N   . VAL A 46  ? 0.2492 0.2531 0.2946 0.0077  -0.0259 0.0230  49  VAL A N   
712  C CA  . VAL A 46  ? 0.2535 0.2646 0.3171 0.0119  -0.0276 0.0182  49  VAL A CA  
713  C C   . VAL A 46  ? 0.2895 0.2933 0.3594 0.0128  -0.0297 0.0192  49  VAL A C   
714  O O   . VAL A 46  ? 0.2438 0.2509 0.3218 0.0106  -0.0268 0.0191  49  VAL A O   
715  C CB  . VAL A 46  ? 0.2473 0.2615 0.3134 0.0173  -0.0315 0.0121  49  VAL A CB  
716  C CG1 . VAL A 46  ? 0.2625 0.2780 0.3445 0.0183  -0.0321 0.0075  49  VAL A CG1 
717  C CG2 . VAL A 46  ? 0.2880 0.3103 0.3499 0.0177  -0.0269 0.0093  49  VAL A CG2 
727  N N   . PRO A 47  ? 0.2562 0.2509 0.3211 0.0174  -0.0346 0.0199  50  PRO A N   
728  C CA  . PRO A 47  ? 0.2387 0.2285 0.3101 0.0194  -0.0349 0.0195  50  PRO A CA  
729  C C   . PRO A 47  ? 0.2764 0.2530 0.3372 0.0133  -0.0311 0.0237  50  PRO A C   
730  O O   . PRO A 47  ? 0.2808 0.2551 0.3467 0.0134  -0.0296 0.0222  50  PRO A O   
731  C CB  . PRO A 47  ? 0.2500 0.2375 0.3196 0.0297  -0.0423 0.0176  50  PRO A CB  
732  C CG  . PRO A 47  ? 0.2874 0.2678 0.3378 0.0317  -0.0460 0.0211  50  PRO A CG  
733  C CD  . PRO A 47  ? 0.2614 0.2524 0.3152 0.0240  -0.0413 0.0196  50  PRO A CD  
741  N N   . ALA A 48  ? 0.2414 0.2095 0.2866 0.0063  -0.0285 0.0279  51  ALA A N   
742  C CA  . ALA A 48  ? 0.2669 0.2224 0.3023 -0.0035 -0.0242 0.0298  51  ALA A CA  
743  C C   . ALA A 48  ? 0.2689 0.2446 0.3193 -0.0097 -0.0213 0.0264  51  ALA A C   
744  O O   . ALA A 48  ? 0.2695 0.2409 0.3196 -0.0137 -0.0203 0.0246  51  ALA A O   
745  C CB  . ALA A 48  ? 0.2983 0.2416 0.3137 -0.0133 -0.0201 0.0345  51  ALA A CB  
751  N N   . ILE A 49  ? 0.2458 0.2427 0.3069 -0.0085 -0.0204 0.0249  52  ILE A N   
752  C CA  . ILE A 49  ? 0.2233 0.2389 0.2962 -0.0094 -0.0194 0.0222  52  ILE A CA  
753  C C   . ILE A 49  ? 0.2106 0.2216 0.2897 -0.0023 -0.0212 0.0212  52  ILE A C   
754  O O   . ILE A 49  ? 0.2217 0.2362 0.3017 -0.0039 -0.0210 0.0201  52  ILE A O   
755  C CB  . ILE A 49  ? 0.2257 0.2607 0.3059 -0.0050 -0.0183 0.0207  52  ILE A CB  
756  C CG1 . ILE A 49  ? 0.2387 0.2849 0.3142 -0.0143 -0.0141 0.0206  52  ILE A CG1 
757  C CG2 . ILE A 49  ? 0.2549 0.3049 0.3445 0.0012  -0.0193 0.0188  52  ILE A CG2 
758  C CD1 . ILE A 49  ? 0.2934 0.3575 0.3737 -0.0075 -0.0119 0.0181  52  ILE A CD1 
770  N N   . ALA A 50  ? 0.2129 0.2189 0.2962 0.0046  -0.0225 0.0206  53  ALA A N   
771  C CA  . ALA A 50  ? 0.2305 0.2344 0.3202 0.0082  -0.0215 0.0191  53  ALA A CA  
772  C C   . ALA A 50  ? 0.2332 0.2275 0.3185 0.0072  -0.0210 0.0184  53  ALA A C   
773  O O   . ALA A 50  ? 0.2461 0.2406 0.3322 0.0074  -0.0184 0.0175  53  ALA A O   
774  C CB  . ALA A 50  ? 0.2633 0.2676 0.3607 0.0122  -0.0223 0.0162  53  ALA A CB  
780  N N   . PHE A 51  ? 0.2240 0.2065 0.3011 0.0071  -0.0230 0.0189  54  PHE A N   
781  C CA  . PHE A 51  ? 0.2388 0.2067 0.3079 0.0077  -0.0222 0.0174  54  PHE A CA  
782  C C   . PHE A 51  ? 0.2757 0.2447 0.3396 -0.0006 -0.0200 0.0163  54  PHE A C   
783  O O   . PHE A 51  ? 0.2704 0.2355 0.3323 0.0009  -0.0181 0.0133  54  PHE A O   
784  C CB  . PHE A 51  ? 0.2684 0.2149 0.3217 0.0090  -0.0245 0.0197  54  PHE A CB  
785  C CG  . PHE A 51  ? 0.3207 0.2445 0.3594 0.0074  -0.0227 0.0179  54  PHE A CG  
786  C CD1 . PHE A 51  ? 0.3216 0.2381 0.3612 0.0188  -0.0229 0.0141  54  PHE A CD1 
787  C CD2 . PHE A 51  ? 0.3625 0.2735 0.3869 -0.0062 -0.0203 0.0184  54  PHE A CD2 
788  C CE1 . PHE A 51  ? 0.3742 0.2649 0.3968 0.0187  -0.0208 0.0111  54  PHE A CE1 
789  C CE2 . PHE A 51  ? 0.4680 0.3533 0.4759 -0.0098 -0.0183 0.0151  54  PHE A CE2 
790  C CZ  . PHE A 51  ? 0.4214 0.2941 0.4268 0.0034  -0.0186 0.0116  54  PHE A CZ  
800  N N   . THR A 52  ? 0.2453 0.2218 0.3064 -0.0095 -0.0202 0.0175  55  THR A N   
801  C CA  . THR A 52  ? 0.2307 0.2137 0.2880 -0.0182 -0.0200 0.0143  55  THR A CA  
802  C C   . THR A 52  ? 0.2240 0.2216 0.2877 -0.0121 -0.0207 0.0137  55  THR A C   
803  O O   . THR A 52  ? 0.2524 0.2507 0.3097 -0.0149 -0.0213 0.0104  55  THR A O   
804  C CB  . THR A 52  ? 0.3000 0.2974 0.3575 -0.0299 -0.0197 0.0137  55  THR A CB  
805  O OG1 . THR A 52  ? 0.3307 0.3511 0.4004 -0.0241 -0.0206 0.0153  55  THR A OG1 
806  C CG2 . THR A 52  ? 0.3339 0.3116 0.3799 -0.0365 -0.0171 0.0163  55  THR A CG2 
814  N N   . MET A 53  ? 0.2196 0.2261 0.2920 -0.0042 -0.0206 0.0167  56  MET A N   
815  C CA  . MET A 53  ? 0.2307 0.2441 0.3028 0.0018  -0.0205 0.0178  56  MET A CA  
816  C C   . MET A 53  ? 0.2392 0.2397 0.3083 0.0051  -0.0162 0.0178  56  MET A C   
817  O O   . MET A 53  ? 0.2436 0.2433 0.3038 0.0066  -0.0151 0.0179  56  MET A O   
818  C CB  . MET A 53  ? 0.2236 0.2450 0.3017 0.0085  -0.0209 0.0206  56  MET A CB  
819  C CG  . MET A 53  ? 0.2615 0.3038 0.3436 0.0075  -0.0242 0.0193  56  MET A CG  
820  S SD  . MET A 53  ? 0.3420 0.4049 0.4207 0.0073  -0.0292 0.0165  56  MET A SD  
821  C CE  . MET A 53  ? 0.4603 0.5265 0.5386 -0.0110 -0.0290 0.0110  56  MET A CE  
831  N N   . TYR A 54  ? 0.2100 0.2027 0.2851 0.0061  -0.0137 0.0165  57  TYR A N   
832  C CA  . TYR A 54  ? 0.2482 0.2352 0.3233 0.0083  -0.0085 0.0140  57  TYR A CA  
833  C C   . TYR A 54  ? 0.2549 0.2345 0.3184 0.0065  -0.0082 0.0105  57  TYR A C   
834  O O   . TYR A 54  ? 0.2713 0.2490 0.3281 0.0075  -0.0036 0.0090  57  TYR A O   
835  C CB  . TYR A 54  ? 0.2101 0.1980 0.2972 0.0117  -0.0080 0.0113  57  TYR A CB  
836  C CG  . TYR A 54  ? 0.2111 0.2064 0.3089 0.0111  -0.0043 0.0114  57  TYR A CG  
837  C CD1 . TYR A 54  ? 0.2484 0.2462 0.3504 0.0104  -0.0073 0.0131  57  TYR A CD1 
838  C CD2 . TYR A 54  ? 0.2567 0.2549 0.3585 0.0095  0.0039  0.0087  57  TYR A CD2 
839  C CE1 . TYR A 54  ? 0.2109 0.2098 0.3193 0.0076  -0.0032 0.0118  57  TYR A CE1 
840  C CE2 . TYR A 54  ? 0.2578 0.2595 0.3676 0.0047  0.0093  0.0079  57  TYR A CE2 
841  C CZ  . TYR A 54  ? 0.2357 0.2359 0.3483 0.0035  0.0053  0.0091  57  TYR A CZ  
842  O OH  . TYR A 54  ? 0.2625 0.2602 0.3793 -0.0034 0.0110  0.0074  57  TYR A OH  
852  N N   . LEU A 55  ? 0.2392 0.2117 0.2973 0.0027  -0.0121 0.0088  58  LEU A N   
853  C CA  . LEU A 55  ? 0.2777 0.2383 0.3219 -0.0006 -0.0114 0.0037  58  LEU A CA  
854  C C   . LEU A 55  ? 0.2652 0.2356 0.3014 -0.0047 -0.0129 0.0028  58  LEU A C   
855  O O   . LEU A 55  ? 0.2954 0.2598 0.3197 -0.0045 -0.0106 -0.0015 58  LEU A O   
856  C CB  . LEU A 55  ? 0.2638 0.2090 0.2995 -0.0074 -0.0143 0.0022  58  LEU A CB  
857  C CG  . LEU A 55  ? 0.2981 0.2231 0.3157 -0.0130 -0.0133 -0.0048 58  LEU A CG  
858  C CD1 . LEU A 55  ? 0.3653 0.2753 0.3782 -0.0009 -0.0087 -0.0092 58  LEU A CD1 
859  C CD2 . LEU A 55  ? 0.3510 0.2566 0.3577 -0.0229 -0.0144 -0.0049 58  LEU A CD2 
871  N N   . SER A 56  ? 0.2334 0.2201 0.2743 -0.0067 -0.0173 0.0062  59  SER A N   
872  C CA  . SER A 56  ? 0.2368 0.2363 0.2692 -0.0075 -0.0212 0.0049  59  SER A CA  
873  C C   . SER A 56  ? 0.2951 0.2905 0.3191 0.0010  -0.0171 0.0084  59  SER A C   
874  O O   . SER A 56  ? 0.3032 0.3006 0.3125 0.0019  -0.0188 0.0066  59  SER A O   
875  C CB  . SER A 56  ? 0.3057 0.3280 0.3466 -0.0071 -0.0270 0.0072  59  SER A CB  
876  O OG  . SER A 56  ? 0.3402 0.3639 0.3852 0.0037  -0.0256 0.0140  59  SER A OG  
882  N N   . MET A 57  ? 0.2715 0.2611 0.3032 0.0060  -0.0113 0.0132  60  MET A N   
883  C CA  . MET A 57  ? 0.2704 0.2523 0.2917 0.0103  -0.0044 0.0166  60  MET A CA  
884  C C   . MET A 57  ? 0.2871 0.2612 0.3019 0.0087  0.0024  0.0112  60  MET A C   
885  O O   . MET A 57  ? 0.3104 0.2800 0.3075 0.0101  0.0063  0.0116  60  MET A O   
886  C CB  . MET A 57  ? 0.2711 0.2488 0.3030 0.0120  0.0014  0.0213  60  MET A CB  
887  C CG  . MET A 57  ? 0.2711 0.2518 0.3026 0.0167  -0.0040 0.0266  60  MET A CG  
888  S SD  . MET A 57  ? 0.3386 0.3065 0.3759 0.0172  0.0033  0.0309  60  MET A SD  
889  C CE  . MET A 57  ? 0.3665 0.3454 0.4286 0.0125  0.0009  0.0249  60  MET A CE  
899  N N   . LEU A 58  ? 0.2729 0.2443 0.2992 0.0076  0.0040  0.0060  61  LEU A N   
900  C CA  . LEU A 58  ? 0.2816 0.2463 0.3021 0.0093  0.0107  -0.0009 61  LEU A CA  
901  C C   . LEU A 58  ? 0.3790 0.3373 0.3782 0.0068  0.0079  -0.0058 61  LEU A C   
902  O O   . LEU A 58  ? 0.3669 0.3210 0.3525 0.0087  0.0147  -0.0094 61  LEU A O   
903  C CB  . LEU A 58  ? 0.2741 0.2345 0.3072 0.0125  0.0097  -0.0054 61  LEU A CB  
904  C CG  . LEU A 58  ? 0.3269 0.2794 0.3551 0.0186  0.0156  -0.0140 61  LEU A CG  
905  C CD1 . LEU A 58  ? 0.3720 0.3380 0.4090 0.0219  0.0266  -0.0154 61  LEU A CD1 
906  C CD2 . LEU A 58  ? 0.3913 0.3338 0.4259 0.0251  0.0113  -0.0169 61  LEU A CD2 
918  N N   . LEU A 59  ? 0.3091 0.2679 0.3050 0.0011  -0.0015 -0.0076 62  LEU A N   
919  C CA  . LEU A 59  ? 0.3128 0.2675 0.2896 -0.0042 -0.0052 -0.0151 62  LEU A CA  
920  C C   . LEU A 59  ? 0.3779 0.3454 0.3409 -0.0029 -0.0094 -0.0123 62  LEU A C   
921  O O   . LEU A 59  ? 0.4394 0.4067 0.3844 -0.0066 -0.0132 -0.0196 62  LEU A O   
922  C CB  . LEU A 59  ? 0.3476 0.2995 0.3261 -0.0148 -0.0126 -0.0200 62  LEU A CB  
923  C CG  . LEU A 59  ? 0.3584 0.2901 0.3422 -0.0148 -0.0096 -0.0215 62  LEU A CG  
924  C CD1 . LEU A 59  ? 0.3906 0.3151 0.3706 -0.0287 -0.0146 -0.0251 62  LEU A CD1 
925  C CD2 . LEU A 59  ? 0.4506 0.3607 0.4214 -0.0084 -0.0029 -0.0292 62  LEU A CD2 
937  N N   . GLY A 60  ? 0.3852 0.3708 0.3933 -0.0670 0.0402  -0.0386 63  GLY A N   
938  C CA  . GLY A 60  ? 0.4093 0.3869 0.3737 -0.0611 0.0282  -0.0476 63  GLY A CA  
939  C C   . GLY A 60  ? 0.3991 0.4087 0.3796 -0.0664 0.0040  -0.0436 63  GLY A C   
940  O O   . GLY A 60  ? 0.4189 0.4250 0.3645 -0.0599 -0.0079 -0.0489 63  GLY A O   
944  N N   . TYR A 61  ? 0.3654 0.4096 0.3977 -0.0766 -0.0032 -0.0319 64  TYR A N   
945  C CA  . TYR A 61  ? 0.3533 0.4372 0.4069 -0.0809 -0.0251 -0.0251 64  TYR A CA  
946  C C   . TYR A 61  ? 0.3259 0.4391 0.3740 -0.0656 -0.0205 -0.0153 64  TYR A C   
947  O O   . TYR A 61  ? 0.3570 0.4889 0.3968 -0.0599 -0.0366 -0.0146 64  TYR A O   
948  C CB  . TYR A 61  ? 0.3290 0.4464 0.4440 -0.0964 -0.0310 -0.0108 64  TYR A CB  
949  C CG  . TYR A 61  ? 0.3177 0.4843 0.4612 -0.1020 -0.0529 -0.0006 64  TYR A CG  
950  C CD1 . TYR A 61  ? 0.3514 0.5133 0.4956 -0.1162 -0.0785 -0.0090 64  TYR A CD1 
951  C CD2 . TYR A 61  ? 0.2761 0.4978 0.4445 -0.0915 -0.0481 0.0170  64  TYR A CD2 
952  C CE1 . TYR A 61  ? 0.4251 0.6401 0.5983 -0.1211 -0.0988 0.0031  64  TYR A CE1 
953  C CE2 . TYR A 61  ? 0.2676 0.5417 0.4619 -0.0926 -0.0669 0.0279  64  TYR A CE2 
954  C CZ  . TYR A 61  ? 0.3134 0.5862 0.5128 -0.1079 -0.0911 0.0231  64  TYR A CZ  
955  O OH  . TYR A 61  ? 0.4004 0.7302 0.6297 -0.1106 -0.1103 0.0362  64  TYR A OH  
965  N N   . GLY A 62  ? 0.2997 0.4167 0.3532 -0.0587 -0.0001 -0.0085 65  GLY A N   
966  C CA  . GLY A 62  ? 0.3356 0.4792 0.3905 -0.0454 0.0035  -0.0013 65  GLY A CA  
967  C C   . GLY A 62  ? 0.3509 0.4594 0.3588 -0.0335 0.0091  -0.0077 65  GLY A C   
968  O O   . GLY A 62  ? 0.3135 0.4256 0.3196 -0.0248 0.0186  -0.0045 65  GLY A O   
972  N N   . LEU A 63  ? 0.3534 0.4275 0.3237 -0.0338 0.0034  -0.0164 66  LEU A N   
973  C CA  . LEU A 63  ? 0.3698 0.4108 0.2942 -0.0233 0.0091  -0.0179 66  LEU A CA  
974  C C   . LEU A 63  ? 0.4399 0.4804 0.3383 -0.0161 -0.0112 -0.0202 66  LEU A C   
975  O O   . LEU A 63  ? 0.4527 0.5000 0.3522 -0.0238 -0.0276 -0.0275 66  LEU A O   
976  C CB  . LEU A 63  ? 0.3972 0.4029 0.2965 -0.0276 0.0253  -0.0233 66  LEU A CB  
977  C CG  . LEU A 63  ? 0.4950 0.4685 0.3460 -0.0193 0.0333  -0.0223 66  LEU A CG  
978  C CD1 . LEU A 63  ? 0.5169 0.4883 0.3712 -0.0145 0.0448  -0.0104 66  LEU A CD1 
979  C CD2 . LEU A 63  ? 0.6280 0.5777 0.4596 -0.0220 0.0491  -0.0289 66  LEU A CD2 
991  N N   . THR A 64  ? 0.4169 0.4476 0.2913 -0.0017 -0.0118 -0.0136 67  THR A N   
992  C CA  . THR A 64  ? 0.4517 0.4814 0.2970 0.0082  -0.0295 -0.0122 67  THR A CA  
993  C C   . THR A 64  ? 0.4867 0.4803 0.2891 0.0195  -0.0198 -0.0044 67  THR A C   
994  O O   . THR A 64  ? 0.5195 0.4927 0.3219 0.0188  -0.0012 0.0006  67  THR A O   
995  C CB  . THR A 64  ? 0.4350 0.5049 0.3078 0.0182  -0.0456 -0.0058 67  THR A CB  
996  O OG1 . THR A 64  ? 0.5026 0.5804 0.3523 0.0253  -0.0661 -0.0042 67  THR A OG1 
997  C CG2 . THR A 64  ? 0.4484 0.5142 0.3265 0.0347  -0.0364 0.0020  67  THR A CG2 
1005 N N   . MET A 65  ? 0.5268 0.5144 0.2935 0.0287  -0.0326 -0.0010 68  MET A N   
1006 C CA  . MET A 65  ? 0.5645 0.5201 0.2917 0.0399  -0.0231 0.0121  68  MET A CA  
1007 C C   . MET A 65  ? 0.6536 0.6137 0.3800 0.0585  -0.0345 0.0258  68  MET A C   
1008 O O   . MET A 65  ? 0.6149 0.6032 0.3433 0.0662  -0.0551 0.0257  68  MET A O   
1009 C CB  . MET A 65  ? 0.6287 0.5714 0.3071 0.0402  -0.0251 0.0095  68  MET A CB  
1010 C CG  . MET A 65  ? 0.8670 0.8044 0.5460 0.0256  -0.0159 -0.0081 68  MET A CG  
1011 S SD  . MET A 65  ? 0.8738 0.7835 0.5489 0.0215  0.0183  0.0000  68  MET A SD  
1012 C CE  . MET A 65  ? 0.9485 0.8368 0.5880 0.0343  0.0271  0.0256  68  MET A CE  
1022 N N   . VAL A 66  ? 0.5878 0.5200 0.3131 0.0658  -0.0218 0.0378  69  VAL A N   
1023 C CA  . VAL A 66  ? 0.6044 0.5318 0.3317 0.0863  -0.0306 0.0499  69  VAL A CA  
1024 C C   . VAL A 66  ? 0.6561 0.5450 0.3448 0.0945  -0.0242 0.0702  69  VAL A C   
1025 O O   . VAL A 66  ? 0.6640 0.5219 0.3462 0.0846  -0.0060 0.0765  69  VAL A O   
1026 C CB  . VAL A 66  ? 0.5776 0.5017 0.3403 0.0897  -0.0243 0.0450  69  VAL A CB  
1027 C CG1 . VAL A 66  ? 0.6450 0.5576 0.4057 0.1158  -0.0336 0.0557  69  VAL A CG1 
1028 C CG2 . VAL A 66  ? 0.5306 0.5002 0.3332 0.0821  -0.0285 0.0293  69  VAL A CG2 
1038 N N   . PRO A 67  ? 0.6942 0.5877 0.3581 0.1121  -0.0383 0.0841  70  PRO A N   
1039 C CA  . PRO A 67  ? 0.7467 0.6053 0.3758 0.1210  -0.0314 0.1088  70  PRO A CA  
1040 C C   . PRO A 67  ? 0.8680 0.6896 0.5138 0.1329  -0.0266 0.1216  70  PRO A C   
1041 O O   . PRO A 67  ? 0.8337 0.6647 0.4997 0.1503  -0.0384 0.1185  70  PRO A O   
1042 C CB  . PRO A 67  ? 0.7914 0.6761 0.3913 0.1371  -0.0512 0.1185  70  PRO A CB  
1043 C CG  . PRO A 67  ? 0.7489 0.6733 0.3820 0.1447  -0.0698 0.1053  70  PRO A CG  
1044 C CD  . PRO A 67  ? 0.6928 0.6277 0.3631 0.1252  -0.0616 0.0817  70  PRO A CD  
1052 N N   . PHE A 68  ? 0.8250 0.6048 0.4637 0.1235  -0.0095 0.1353  71  PHE A N   
1053 C CA  . PHE A 68  ? 0.8438 0.5761 0.4908 0.1332  -0.0064 0.1516  71  PHE A CA  
1054 C C   . PHE A 68  ? 0.9856 0.6821 0.6162 0.1180  0.0116  0.1745  71  PHE A C   
1055 O O   . PHE A 68  ? 0.8980 0.6075 0.5233 0.0982  0.0251  0.1703  71  PHE A O   
1056 C CB  . PHE A 68  ? 0.8345 0.5578 0.5208 0.1328  -0.0071 0.1296  71  PHE A CB  
1057 C CG  . PHE A 68  ? 0.7475 0.4762 0.4555 0.1063  0.0063  0.1112  71  PHE A CG  
1058 C CD1 . PHE A 68  ? 0.8899 0.5809 0.6013 0.0878  0.0211  0.1209  71  PHE A CD1 
1059 C CD2 . PHE A 68  ? 0.6918 0.4656 0.4199 0.0997  0.0035  0.0874  71  PHE A CD2 
1060 C CE1 . PHE A 68  ? 0.7386 0.4402 0.4718 0.0648  0.0324  0.1059  71  PHE A CE1 
1061 C CE2 . PHE A 68  ? 0.6778 0.4596 0.4268 0.0775  0.0158  0.0735  71  PHE A CE2 
1062 C CZ  . PHE A 68  ? 0.6964 0.4436 0.4476 0.0606  0.0302  0.0820  71  PHE A CZ  
1072 N N   . GLY A 69  ? 1.1536 0.8070 0.7771 0.1287  0.0119  0.2018  72  GLY A N   
1073 C CA  . GLY A 69  ? 1.1150 0.7395 0.7237 0.1148  0.0283  0.2315  72  GLY A CA  
1074 C C   . GLY A 69  ? 1.1916 0.8491 0.7594 0.1149  0.0343  0.2469  72  GLY A C   
1075 O O   . GLY A 69  ? 1.1559 0.8113 0.7140 0.0984  0.0527  0.2618  72  GLY A O   
1079 N N   . GLY A 70  ? 1.0653 0.7566 0.6082 0.1340  0.0189  0.2436  73  GLY A N   
1080 C CA  . GLY A 70  ? 1.0660 0.7878 0.5640 0.1363  0.0221  0.2552  73  GLY A CA  
1081 C C   . GLY A 70  ? 1.2728 1.0217 0.7644 0.1178  0.0340  0.2316  73  GLY A C   
1082 O O   . GLY A 70  ? 1.2339 0.9978 0.6881 0.1171  0.0447  0.2435  73  GLY A O   
1086 N N   . GLU A 71  ? 1.0017 0.7580 0.5283 0.1048  0.0332  0.1994  74  GLU A N   
1087 C CA  . GLU A 71  ? 0.9527 0.7331 0.4786 0.0895  0.0430  0.1754  74  GLU A CA  
1088 C C   . GLU A 71  ? 0.8941 0.7008 0.4420 0.0892  0.0256  0.1420  74  GLU A C   
1089 O O   . GLU A 71  ? 0.8110 0.6178 0.3824 0.0983  0.0107  0.1381  74  GLU A O   
1090 C CB  . GLU A 71  ? 0.9951 0.7584 0.5505 0.0690  0.0648  0.1761  74  GLU A CB  
1093 N N   . GLN A 72  ? 0.8027 0.6322 0.3440 0.0798  0.0281  0.1193  75  GLN A N   
1094 C CA  . GLN A 72  ? 0.8060 0.6573 0.3800 0.0724  0.0167  0.0899  75  GLN A CA  
1095 C C   . GLN A 72  ? 0.8050 0.6493 0.4159 0.0556  0.0342  0.0807  75  GLN A C   
1096 O O   . GLN A 72  ? 0.8487 0.6904 0.4509 0.0464  0.0523  0.0796  75  GLN A O   
1097 C CB  . GLN A 72  ? 1.1336 1.0097 0.6832 0.0712  0.0051  0.0693  75  GLN A CB  
1098 C CG  . GLN A 72  ? 1.2040 1.0898 0.7051 0.0860  -0.0090 0.0791  75  GLN A CG  
1099 C CD  . GLN A 72  ? 1.3376 1.2498 0.8505 0.0936  -0.0378 0.0728  75  GLN A CD  
1100 O OE1 . GLN A 72  ? 1.4389 1.3726 0.9748 0.0839  -0.0512 0.0496  75  GLN A OE1 
1101 N NE2 . GLN A 72  ? 1.3550 1.2679 0.8547 0.1115  -0.0476 0.0962  75  GLN A NE2 
1110 N N   . ASN A 73  ? 0.6655 0.5111 0.3171 0.0537  0.0289  0.0742  76  ASN A N   
1111 C CA  . ASN A 73  ? 0.6308 0.4712 0.3160 0.0392  0.0438  0.0689  76  ASN A CA  
1112 C C   . ASN A 73  ? 0.6688 0.5391 0.3842 0.0315  0.0387  0.0462  76  ASN A C   
1113 O O   . ASN A 73  ? 0.5669 0.4573 0.2983 0.0384  0.0217  0.0379  76  ASN A O   
1114 C CB  . ASN A 73  ? 0.6349 0.4536 0.3427 0.0428  0.0419  0.0765  76  ASN A CB  
1115 C CG  . ASN A 73  ? 0.7712 0.5539 0.4537 0.0492  0.0463  0.1030  76  ASN A CG  
1116 O OD1 . ASN A 73  ? 0.8183 0.5829 0.4984 0.0369  0.0631  0.1172  76  ASN A OD1 
1117 N ND2 . ASN A 73  ? 0.7177 0.4942 0.3829 0.0685  0.0315  0.1129  76  ASN A ND2 
1124 N N   . PRO A 74  ? 0.5873 0.4637 0.3151 0.0181  0.0536  0.0388  77  PRO A N   
1125 C CA  . PRO A 74  ? 0.5175 0.4209 0.2797 0.0102  0.0500  0.0216  77  PRO A CA  
1126 C C   . PRO A 74  ? 0.5511 0.4670 0.3533 0.0082  0.0482  0.0194  77  PRO A C   
1127 O O   . PRO A 74  ? 0.5549 0.4593 0.3689 0.0022  0.0603  0.0250  77  PRO A O   
1128 C CB  . PRO A 74  ? 0.6183 0.5195 0.3790 0.0002  0.0693  0.0190  77  PRO A CB  
1129 C CG  . PRO A 74  ? 0.7382 0.6180 0.4792 -0.0004 0.0864  0.0367  77  PRO A CG  
1130 C CD  . PRO A 74  ? 0.6463 0.5079 0.3597 0.0108  0.0759  0.0500  77  PRO A CD  
1138 N N   . ILE A 75  ? 0.4577 0.4006 0.2809 0.0136  0.0323  0.0113  78  ILE A N   
1139 C CA  . ILE A 75  ? 0.4269 0.3892 0.2846 0.0158  0.0303  0.0075  78  ILE A CA  
1140 C C   . ILE A 75  ? 0.3882 0.3896 0.2799 0.0073  0.0286  -0.0002 78  ILE A C   
1141 O O   . ILE A 75  ? 0.3823 0.4053 0.2795 0.0082  0.0151  -0.0031 78  ILE A O   
1142 C CB  . ILE A 75  ? 0.4420 0.4079 0.2970 0.0346  0.0147  0.0093  78  ILE A CB  
1143 C CG1 . ILE A 75  ? 0.4890 0.4099 0.3129 0.0436  0.0168  0.0208  78  ILE A CG1 
1144 C CG2 . ILE A 75  ? 0.4281 0.4201 0.3152 0.0403  0.0129  0.0022  78  ILE A CG2 
1145 C CD1 . ILE A 75  ? 0.5124 0.4023 0.3422 0.0352  0.0309  0.0232  78  ILE A CD1 
1157 N N   . TYR A 76  ? 0.3572 0.3694 0.2737 -0.0022 0.0414  -0.0015 79  TYR A N   
1158 C CA  . TYR A 76  ? 0.3207 0.3728 0.2738 -0.0088 0.0407  -0.0041 79  TYR A CA  
1159 C C   . TYR A 76  ? 0.3203 0.4095 0.2973 0.0019  0.0303  -0.0053 79  TYR A C   
1160 O O   . TYR A 76  ? 0.3144 0.4148 0.3040 0.0052  0.0355  -0.0076 79  TYR A O   
1161 C CB  . TYR A 76  ? 0.2977 0.3539 0.2684 -0.0202 0.0581  -0.0020 79  TYR A CB  
1162 C CG  . TYR A 76  ? 0.3119 0.3456 0.2679 -0.0283 0.0694  -0.0005 79  TYR A CG  
1163 C CD1 . TYR A 76  ? 0.3234 0.3658 0.2913 -0.0332 0.0668  -0.0033 79  TYR A CD1 
1164 C CD2 . TYR A 76  ? 0.3486 0.3534 0.2807 -0.0302 0.0825  0.0039  79  TYR A CD2 
1165 C CE1 . TYR A 76  ? 0.3262 0.3452 0.2789 -0.0369 0.0784  -0.0055 79  TYR A CE1 
1166 C CE2 . TYR A 76  ? 0.3812 0.3697 0.2973 -0.0334 0.0957  0.0050  79  TYR A CE2 
1167 C CZ  . TYR A 76  ? 0.3691 0.3639 0.2946 -0.0350 0.0933  -0.0019 79  TYR A CZ  
1168 O OH  . TYR A 76  ? 0.4200 0.3948 0.3254 -0.0337 0.1059  -0.0046 79  TYR A OH  
1178 N N   . TRP A 77  ? 0.3172 0.3521 0.2462 -0.0049 -0.0366 -0.0145 80  TRP A N   
1179 C CA  . TRP A 77  ? 0.2951 0.3312 0.2370 0.0002  -0.0445 -0.0083 80  TRP A CA  
1180 C C   . TRP A 77  ? 0.2620 0.2994 0.2294 -0.0022 -0.0431 -0.0134 80  TRP A C   
1181 O O   . TRP A 77  ? 0.2629 0.3007 0.2424 0.0011  -0.0453 -0.0078 80  TRP A O   
1182 C CB  . TRP A 77  ? 0.3020 0.3534 0.2381 0.0042  -0.0570 -0.0098 80  TRP A CB  
1183 C CG  . TRP A 77  ? 0.3052 0.3692 0.2467 -0.0039 -0.0604 -0.0248 80  TRP A CG  
1184 C CD1 . TRP A 77  ? 0.3793 0.4463 0.3020 -0.0074 -0.0615 -0.0335 80  TRP A CD1 
1185 C CD2 . TRP A 77  ? 0.3268 0.3968 0.2905 -0.0113 -0.0620 -0.0329 80  TRP A CD2 
1186 N NE1 . TRP A 77  ? 0.4447 0.5178 0.3769 -0.0163 -0.0652 -0.0480 80  TRP A NE1 
1187 C CE2 . TRP A 77  ? 0.3639 0.4368 0.3205 -0.0201 -0.0650 -0.0471 80  TRP A CE2 
1188 C CE3 . TRP A 77  ? 0.3463 0.4175 0.3311 -0.0127 -0.0608 -0.0296 80  TRP A CE3 
1189 C CZ2 . TRP A 77  ? 0.4405 0.5127 0.4099 -0.0321 -0.0667 -0.0573 80  TRP A CZ2 
1190 C CZ3 . TRP A 77  ? 0.3698 0.4429 0.3671 -0.0248 -0.0615 -0.0385 80  TRP A CZ3 
1191 C CH2 . TRP A 77  ? 0.3935 0.4648 0.3824 -0.0353 -0.0646 -0.0520 80  TRP A CH2 
1202 N N   . ALA A 78  ? 0.2819 0.3166 0.2544 -0.0066 -0.0390 -0.0240 81  ALA A N   
1203 C CA  . ALA A 78  ? 0.2604 0.2882 0.2505 -0.0079 -0.0383 -0.0265 81  ALA A CA  
1204 C C   . ALA A 78  ? 0.2931 0.3156 0.2932 -0.0039 -0.0340 -0.0190 81  ALA A C   
1205 O O   . ALA A 78  ? 0.2823 0.2998 0.2934 -0.0041 -0.0349 -0.0175 81  ALA A O   
1206 C CB  . ALA A 78  ? 0.3394 0.3564 0.3275 -0.0095 -0.0356 -0.0391 81  ALA A CB  
1212 N N   . ARG A 79  ? 0.2506 0.2733 0.2452 -0.0024 -0.0287 -0.0147 82  ARG A N   
1213 C CA  . ARG A 79  ? 0.2853 0.3047 0.2891 -0.0009 -0.0260 -0.0096 82  ARG A CA  
1214 C C   . ARG A 79  ? 0.2482 0.2643 0.2554 0.0016  -0.0308 -0.0022 82  ARG A C   
1215 O O   . ARG A 79  ? 0.2771 0.2904 0.2941 0.0032  -0.0305 -0.0007 82  ARG A O   
1216 C CB  . ARG A 79  ? 0.3287 0.3489 0.3231 -0.0051 -0.0195 -0.0061 82  ARG A CB  
1217 C CG  . ARG A 79  ? 0.3511 0.3826 0.3444 -0.0076 -0.0124 -0.0143 82  ARG A CG  
1218 C CD  . ARG A 79  ? 0.3184 0.3555 0.3072 -0.0170 -0.0036 -0.0111 82  ARG A CD  
1219 N NE  . ARG A 79  ? 0.3406 0.3958 0.3262 -0.0211 0.0057  -0.0194 82  ARG A NE  
1220 C CZ  . ARG A 79  ? 0.3325 0.4079 0.3365 -0.0152 0.0089  -0.0313 82  ARG A CZ  
1221 N NH1 . ARG A 79  ? 0.3452 0.4211 0.3682 -0.0063 0.0031  -0.0340 82  ARG A NH1 
1222 N NH2 . ARG A 79  ? 0.4019 0.4988 0.4038 -0.0177 0.0185  -0.0402 82  ARG A NH2 
1236 N N   . TYR A 80  ? 0.2630 0.2815 0.2608 0.0040  -0.0356 0.0020  83  TYR A N   
1237 C CA  . TYR A 80  ? 0.2428 0.2620 0.2444 0.0102  -0.0397 0.0074  83  TYR A CA  
1238 C C   . TYR A 80  ? 0.2461 0.2781 0.2634 0.0084  -0.0417 0.0036  83  TYR A C   
1239 O O   . TYR A 80  ? 0.2752 0.3096 0.2998 0.0117  -0.0414 0.0062  83  TYR A O   
1240 C CB  . TYR A 80  ? 0.2419 0.2622 0.2284 0.0185  -0.0462 0.0124  83  TYR A CB  
1241 C CG  . TYR A 80  ? 0.3037 0.3035 0.2678 0.0165  -0.0424 0.0182  83  TYR A CG  
1242 C CD1 . TYR A 80  ? 0.3454 0.3235 0.2997 0.0174  -0.0396 0.0244  83  TYR A CD1 
1243 C CD2 . TYR A 80  ? 0.3396 0.3411 0.2905 0.0106  -0.0403 0.0163  83  TYR A CD2 
1244 C CE1 . TYR A 80  ? 0.3548 0.3122 0.2865 0.0093  -0.0339 0.0297  83  TYR A CE1 
1245 C CE2 . TYR A 80  ? 0.3401 0.3250 0.2689 0.0044  -0.0338 0.0217  83  TYR A CE2 
1246 C CZ  . TYR A 80  ? 0.3538 0.3166 0.2735 0.0022  -0.0303 0.0288  83  TYR A CZ  
1247 O OH  . TYR A 80  ? 0.4044 0.3494 0.3012 -0.0086 -0.0226 0.0345  83  TYR A OH  
1257 N N   . ALA A 81  ? 0.2398 0.2781 0.2599 0.0013  -0.0429 -0.0032 84  ALA A N   
1258 C CA  . ALA A 81  ? 0.2290 0.2744 0.2605 -0.0060 -0.0433 -0.0065 84  ALA A CA  
1259 C C   . ALA A 81  ? 0.2939 0.3224 0.3285 -0.0073 -0.0383 -0.0045 84  ALA A C   
1260 O O   . ALA A 81  ? 0.2840 0.3155 0.3244 -0.0103 -0.0367 -0.0019 84  ALA A O   
1261 C CB  . ALA A 81  ? 0.2438 0.2925 0.2727 -0.0159 -0.0460 -0.0155 84  ALA A CB  
1267 N N   . ASP A 82  ? 0.2268 0.2410 0.2568 -0.0041 -0.0358 -0.0059 85  ASP A N   
1268 C CA  . ASP A 82  ? 0.2347 0.2359 0.2665 -0.0010 -0.0335 -0.0040 85  ASP A CA  
1269 C C   . ASP A 82  ? 0.2435 0.2492 0.2783 0.0032  -0.0330 0.0023  85  ASP A C   
1270 O O   . ASP A 82  ? 0.2581 0.2614 0.2939 0.0024  -0.0323 0.0057  85  ASP A O   
1271 C CB  . ASP A 82  ? 0.2096 0.2073 0.2395 0.0042  -0.0318 -0.0092 85  ASP A CB  
1272 C CG  . ASP A 82  ? 0.2711 0.2639 0.3047 0.0115  -0.0315 -0.0089 85  ASP A CG  
1273 O OD1 . ASP A 82  ? 0.2742 0.2653 0.3093 0.0126  -0.0326 -0.0034 85  ASP A OD1 
1274 O OD2 . ASP A 82  ? 0.2733 0.2681 0.3083 0.0174  -0.0305 -0.0156 85  ASP A OD2 
1279 N N   . TRP A 83  ? 0.2337 0.2433 0.2659 0.0065  -0.0328 0.0040  86  TRP A N   
1280 C CA  . TRP A 83  ? 0.2383 0.2453 0.2696 0.0102  -0.0324 0.0078  86  TRP A CA  
1281 C C   . TRP A 83  ? 0.2434 0.2571 0.2762 0.0134  -0.0333 0.0103  86  TRP A C   
1282 O O   . TRP A 83  ? 0.2496 0.2608 0.2818 0.0163  -0.0323 0.0117  86  TRP A O   
1283 C CB  . TRP A 83  ? 0.2468 0.2485 0.2695 0.0101  -0.0315 0.0091  86  TRP A CB  
1284 C CG  . TRP A 83  ? 0.2449 0.2486 0.2684 0.0050  -0.0281 0.0053  86  TRP A CG  
1285 C CD1 . TRP A 83  ? 0.2550 0.2654 0.2878 0.0058  -0.0273 0.0000  86  TRP A CD1 
1286 C CD2 . TRP A 83  ? 0.2336 0.2341 0.2468 -0.0007 -0.0245 0.0063  86  TRP A CD2 
1287 N NE1 . TRP A 83  ? 0.2467 0.2664 0.2803 0.0016  -0.0229 -0.0045 86  TRP A NE1 
1288 C CE2 . TRP A 83  ? 0.2595 0.2728 0.2804 -0.0049 -0.0202 -0.0001 86  TRP A CE2 
1289 C CE3 . TRP A 83  ? 0.2764 0.2626 0.2718 -0.0020 -0.0245 0.0124  86  TRP A CE3 
1290 C CZ2 . TRP A 83  ? 0.2662 0.2843 0.2798 -0.0140 -0.0136 -0.0011 86  TRP A CZ2 
1291 C CZ3 . TRP A 83  ? 0.3244 0.3057 0.3065 -0.0119 -0.0187 0.0137  86  TRP A CZ3 
1292 C CH2 . TRP A 83  ? 0.3478 0.3483 0.3408 -0.0197 -0.0122 0.0065  86  TRP A CH2 
1303 N N   . LEU A 84  ? 0.2203 0.2468 0.2557 0.0132  -0.0352 0.0096  87  LEU A N   
1304 C CA  . LEU A 84  ? 0.2264 0.2701 0.2678 0.0169  -0.0354 0.0097  87  LEU A CA  
1305 C C   . LEU A 84  ? 0.2663 0.3117 0.3117 0.0107  -0.0309 0.0104  87  LEU A C   
1306 O O   . LEU A 84  ? 0.2720 0.3271 0.3188 0.0152  -0.0283 0.0109  87  LEU A O   
1307 C CB  . LEU A 84  ? 0.2200 0.2866 0.2680 0.0149  -0.0391 0.0065  87  LEU A CB  
1308 C CG  . LEU A 84  ? 0.3761 0.4733 0.4354 0.0194  -0.0394 0.0043  87  LEU A CG  
1309 C CD1 . LEU A 84  ? 0.4517 0.5457 0.5039 0.0392  -0.0424 0.0061  87  LEU A CD1 
1310 C CD2 . LEU A 84  ? 0.4291 0.5565 0.4987 0.0131  -0.0441 -0.0014 87  LEU A CD2 
1322 N N   . PHE A 85  ? 0.2432 0.2776 0.2873 0.0011  -0.0296 0.0103  88  PHE A N   
1323 C CA  . PHE A 85  ? 0.2614 0.2894 0.3018 -0.0055 -0.0254 0.0133  88  PHE A CA  
1324 C C   . PHE A 85  ? 0.3309 0.3386 0.3621 0.0003  -0.0261 0.0163  88  PHE A C   
1325 O O   . PHE A 85  ? 0.3016 0.3066 0.3260 0.0002  -0.0235 0.0199  88  PHE A O   
1326 C CB  . PHE A 85  ? 0.2869 0.3064 0.3251 -0.0194 -0.0243 0.0121  88  PHE A CB  
1327 C CG  . PHE A 85  ? 0.2995 0.3461 0.3486 -0.0286 -0.0240 0.0076  88  PHE A CG  
1328 C CD1 . PHE A 85  ? 0.4250 0.4980 0.4819 -0.0346 -0.0191 0.0079  88  PHE A CD1 
1329 C CD2 . PHE A 85  ? 0.3039 0.3541 0.3555 -0.0303 -0.0288 0.0020  88  PHE A CD2 
1330 C CE1 . PHE A 85  ? 0.4206 0.5292 0.4921 -0.0427 -0.0199 0.0016  88  PHE A CE1 
1331 C CE2 . PHE A 85  ? 0.4481 0.5299 0.5110 -0.0375 -0.0311 -0.0037 88  PHE A CE2 
1332 C CZ  . PHE A 85  ? 0.3886 0.5017 0.4632 -0.0432 -0.0271 -0.0042 88  PHE A CZ  
1342 N N   . THR A 86  ? 0.2698 0.2675 0.3005 0.0053  -0.0296 0.0141  89  THR A N   
1343 C CA  . THR A 86  ? 0.2460 0.2323 0.2709 0.0111  -0.0318 0.0153  89  THR A CA  
1344 C C   . THR A 86  ? 0.2980 0.2910 0.3226 0.0162  -0.0326 0.0148  89  THR A C   
1345 O O   . THR A 86  ? 0.2897 0.2783 0.3077 0.0197  -0.0346 0.0160  89  THR A O   
1346 C CB  . THR A 86  ? 0.2931 0.2743 0.3205 0.0156  -0.0349 0.0108  89  THR A CB  
1347 O OG1 . THR A 86  ? 0.2523 0.2451 0.2867 0.0147  -0.0339 0.0069  89  THR A OG1 
1348 C CG2 . THR A 86  ? 0.2719 0.2370 0.2937 0.0127  -0.0349 0.0100  89  THR A CG2 
1356 N N   . THR A 87  ? 0.2481 0.2473 0.2759 0.0169  -0.0320 0.0127  90  THR A N   
1357 C CA  . THR A 87  ? 0.2420 0.2385 0.2650 0.0201  -0.0329 0.0109  90  THR A CA  
1358 C C   . THR A 87  ? 0.3128 0.3115 0.3294 0.0237  -0.0309 0.0118  90  THR A C   
1359 O O   . THR A 87  ? 0.2876 0.2822 0.2971 0.0256  -0.0326 0.0099  90  THR A O   
1360 C CB  . THR A 87  ? 0.2487 0.2399 0.2692 0.0198  -0.0329 0.0093  90  THR A CB  
1361 O OG1 . THR A 87  ? 0.2629 0.2572 0.2828 0.0238  -0.0323 0.0112  90  THR A OG1 
1362 C CG2 . THR A 87  ? 0.2876 0.2803 0.3127 0.0138  -0.0329 0.0076  90  THR A CG2 
1370 N N   . PRO A 88  ? 0.2871 0.2963 0.3062 0.0238  -0.0272 0.0135  91  PRO A N   
1371 C CA  . PRO A 88  ? 0.2567 0.2727 0.2692 0.0266  -0.0233 0.0135  91  PRO A CA  
1372 C C   . PRO A 88  ? 0.2911 0.3005 0.2940 0.0221  -0.0226 0.0177  91  PRO A C   
1373 O O   . PRO A 88  ? 0.3302 0.3395 0.3214 0.0251  -0.0211 0.0172  91  PRO A O   
1374 C CB  . PRO A 88  ? 0.3687 0.4071 0.3905 0.0260  -0.0185 0.0130  91  PRO A CB  
1375 C CG  . PRO A 88  ? 0.4813 0.5215 0.5124 0.0202  -0.0211 0.0140  91  PRO A CG  
1376 C CD  . PRO A 88  ? 0.2915 0.3127 0.3196 0.0218  -0.0263 0.0137  91  PRO A CD  
1384 N N   . LEU A 89  ? 0.2883 0.2891 0.2916 0.0159  -0.0238 0.0221  92  LEU A N   
1385 C CA  . LEU A 89  ? 0.2757 0.2616 0.2634 0.0149  -0.0250 0.0278  92  LEU A CA  
1386 C C   . LEU A 89  ? 0.3284 0.3095 0.3101 0.0236  -0.0324 0.0253  92  LEU A C   
1387 O O   . LEU A 89  ? 0.3579 0.3335 0.3231 0.0264  -0.0339 0.0283  92  LEU A O   
1388 C CB  . LEU A 89  ? 0.3102 0.2794 0.2965 0.0098  -0.0264 0.0314  92  LEU A CB  
1389 C CG  . LEU A 89  ? 0.3569 0.3286 0.3438 -0.0043 -0.0189 0.0341  92  LEU A CG  
1390 C CD1 . LEU A 89  ? 0.3372 0.2852 0.3200 -0.0095 -0.0214 0.0350  92  LEU A CD1 
1391 C CD2 . LEU A 89  ? 0.4122 0.3813 0.3813 -0.0128 -0.0113 0.0413  92  LEU A CD2 
1403 N N   . LEU A 90  ? 0.2863 0.2715 0.2802 0.0265  -0.0372 0.0192  93  LEU A N   
1404 C CA  . LEU A 90  ? 0.2824 0.2704 0.2738 0.0316  -0.0444 0.0147  93  LEU A CA  
1405 C C   . LEU A 90  ? 0.2777 0.2684 0.2599 0.0320  -0.0436 0.0106  93  LEU A C   
1406 O O   . LEU A 90  ? 0.3170 0.3088 0.2883 0.0354  -0.0492 0.0086  93  LEU A O   
1407 C CB  . LEU A 90  ? 0.2841 0.2802 0.2915 0.0299  -0.0469 0.0084  93  LEU A CB  
1408 C CG  . LEU A 90  ? 0.3169 0.3129 0.3317 0.0334  -0.0490 0.0091  93  LEU A CG  
1409 C CD1 . LEU A 90  ? 0.3089 0.3174 0.3392 0.0283  -0.0471 0.0025  93  LEU A CD1 
1410 C CD2 . LEU A 90  ? 0.3349 0.3323 0.3439 0.0440  -0.0577 0.0089  93  LEU A CD2 
1422 N N   . LEU A 91  ? 0.3030 0.2944 0.2874 0.0306  -0.0378 0.0083  94  LEU A N   
1423 C CA  . LEU A 91  ? 0.2928 0.2828 0.2655 0.0339  -0.0363 0.0027  94  LEU A CA  
1424 C C   . LEU A 91  ? 0.3149 0.3087 0.2723 0.0362  -0.0324 0.0066  94  LEU A C   
1425 O O   . LEU A 91  ? 0.3520 0.3444 0.2939 0.0394  -0.0342 0.0018  94  LEU A O   
1426 C CB  . LEU A 91  ? 0.3024 0.2904 0.2790 0.0372  -0.0315 -0.0005 94  LEU A CB  
1427 C CG  . LEU A 91  ? 0.3335 0.3101 0.3155 0.0338  -0.0348 -0.0035 94  LEU A CG  
1428 C CD1 . LEU A 91  ? 0.3767 0.3461 0.3573 0.0410  -0.0318 -0.0043 94  LEU A CD1 
1429 C CD2 . LEU A 91  ? 0.3911 0.3574 0.3654 0.0286  -0.0399 -0.0109 94  LEU A CD2 
1441 N N   A LEU A 92  ? 0.3127 0.3102 0.2710 0.0324  -0.0266 0.0148  95  LEU A N   
1442 N N   B LEU A 92  ? 0.3137 0.3112 0.2720 0.0324  -0.0266 0.0148  95  LEU A N   
1443 C CA  A LEU A 92  ? 0.3477 0.3466 0.2873 0.0304  -0.0210 0.0205  95  LEU A CA  
1444 C CA  B LEU A 92  ? 0.3482 0.3468 0.2874 0.0306  -0.0212 0.0204  95  LEU A CA  
1445 C C   A LEU A 92  ? 0.3997 0.3855 0.3198 0.0332  -0.0291 0.0248  95  LEU A C   
1446 C C   B LEU A 92  ? 0.3987 0.3848 0.3190 0.0337  -0.0296 0.0242  95  LEU A C   
1447 O O   A LEU A 92  ? 0.4091 0.3946 0.3068 0.0349  -0.0274 0.0261  95  LEU A O   
1448 O O   B LEU A 92  ? 0.4117 0.3979 0.3102 0.0359  -0.0285 0.0244  95  LEU A O   
1449 C CB  A LEU A 92  ? 0.3327 0.3363 0.2770 0.0206  -0.0124 0.0281  95  LEU A CB  
1450 C CB  B LEU A 92  ? 0.3413 0.3427 0.2832 0.0207  -0.0131 0.0287  95  LEU A CB  
1451 C CG  A LEU A 92  ? 0.3704 0.3769 0.2948 0.0128  -0.0026 0.0350  95  LEU A CG  
1452 C CG  B LEU A 92  ? 0.3792 0.4033 0.3384 0.0175  -0.0045 0.0249  95  LEU A CG  
1453 C CD1 A LEU A 92  ? 0.4542 0.4846 0.3773 0.0172  0.0058  0.0272  95  LEU A CD1 
1454 C CD1 B LEU A 92  ? 0.3894 0.4145 0.3497 0.0026  0.0020  0.0327  95  LEU A CD1 
1455 C CD2 A LEU A 92  ? 0.3520 0.3573 0.2807 -0.0022 0.0043  0.0424  95  LEU A CD2 
1456 C CD2 B LEU A 92  ? 0.4238 0.4676 0.3774 0.0231  0.0033  0.0187  95  LEU A CD2 
1479 N N   . ASP A 93  ? 0.3519 0.3292 0.2784 0.0356  -0.0383 0.0267  96  ASP A N   
1480 C CA  . ASP A 93  ? 0.3593 0.3293 0.2688 0.0432  -0.0490 0.0291  96  ASP A CA  
1481 C C   . ASP A 93  ? 0.4063 0.3874 0.3099 0.0469  -0.0546 0.0186  96  ASP A C   
1482 O O   . ASP A 93  ? 0.4468 0.4258 0.3265 0.0514  -0.0591 0.0203  96  ASP A O   
1483 C CB  . ASP A 93  ? 0.3787 0.3476 0.3033 0.0487  -0.0583 0.0279  96  ASP A CB  
1484 C CG  . ASP A 93  ? 0.3887 0.3353 0.3016 0.0522  -0.0598 0.0387  96  ASP A CG  
1485 O OD1 . ASP A 93  ? 0.4096 0.3362 0.2959 0.0504  -0.0564 0.0495  96  ASP A OD1 
1486 O OD2 . ASP A 93  ? 0.4214 0.3685 0.3492 0.0582  -0.0654 0.0356  96  ASP A OD2 
1491 N N   . LEU A 94  ? 0.3642 0.3540 0.2862 0.0439  -0.0550 0.0077  97  LEU A N   
1492 C CA  . LEU A 94  ? 0.3717 0.3665 0.2861 0.0442  -0.0604 -0.0042 97  LEU A CA  
1493 C C   . LEU A 94  ? 0.4099 0.4014 0.3029 0.0460  -0.0530 -0.0062 97  LEU A C   
1494 O O   . LEU A 94  ? 0.4167 0.4096 0.2897 0.0487  -0.0583 -0.0118 97  LEU A O   
1495 C CB  . LEU A 94  ? 0.3872 0.3822 0.3198 0.0376  -0.0603 -0.0143 97  LEU A CB  
1496 C CG  . LEU A 94  ? 0.3725 0.3778 0.3255 0.0339  -0.0668 -0.0156 97  LEU A CG  
1497 C CD1 . LEU A 94  ? 0.4611 0.4619 0.4278 0.0240  -0.0630 -0.0219 97  LEU A CD1 
1498 C CD2 . LEU A 94  ? 0.4583 0.4805 0.4077 0.0364  -0.0801 -0.0220 97  LEU A CD2 
1510 N N   . ALA A 95  ? 0.3915 0.3829 0.2891 0.0453  -0.0409 -0.0037 98  ALA A N   
1511 C CA  . ALA A 95  ? 0.4130 0.4083 0.2931 0.0490  -0.0320 -0.0080 98  ALA A CA  
1512 C C   . ALA A 95  ? 0.4830 0.4805 0.3374 0.0487  -0.0290 0.0007  98  ALA A C   
1513 O O   . ALA A 95  ? 0.4778 0.4785 0.3092 0.0522  -0.0259 -0.0051 98  ALA A O   
1514 C CB  . ALA A 95  ? 0.4139 0.4182 0.3098 0.0498  -0.0201 -0.0073 98  ALA A CB  
1520 N N   . LEU A 96  ? 0.4093 0.4014 0.2625 0.0442  -0.0287 0.0147  99  LEU A N   
1521 C CA  . LEU A 96  ? 0.4656 0.4510 0.2865 0.0427  -0.0258 0.0256  99  LEU A CA  
1522 C C   . LEU A 96  ? 0.4904 0.4695 0.2888 0.0507  -0.0405 0.0235  99  LEU A C   
1523 O O   . LEU A 96  ? 0.5470 0.5233 0.3121 0.0523  -0.0392 0.0273  99  LEU A O   
1524 C CB  . LEU A 96  ? 0.5280 0.4984 0.3478 0.0355  -0.0231 0.0416  99  LEU A CB  
1525 C CG  . LEU A 96  ? 0.5859 0.5674 0.4255 0.0242  -0.0084 0.0433  99  LEU A CG  
1526 C CD1 . LEU A 96  ? 0.6316 0.5918 0.4646 0.0140  -0.0064 0.0577  99  LEU A CD1 
1527 C CD2 . LEU A 96  ? 0.7715 0.7751 0.6017 0.0195  0.0075  0.0399  99  LEU A CD2 
1539 N N   . LEU A 97  ? 0.4905 0.4709 0.3064 0.0551  -0.0546 0.0174  100 LEU A N   
1540 C CA  . LEU A 97  ? 0.5314 0.5146 0.3309 0.0628  -0.0707 0.0134  100 LEU A CA  
1541 C C   . LEU A 97  ? 0.5376 0.5287 0.3191 0.0631  -0.0707 -0.0003 100 LEU A C   
1542 O O   . LEU A 97  ? 0.5952 0.5867 0.3462 0.0685  -0.0786 0.0001  100 LEU A O   
1543 C CB  . LEU A 97  ? 0.5371 0.5305 0.3666 0.0646  -0.0831 0.0061  100 LEU A CB  
1544 C CG  . LEU A 97  ? 0.7048 0.7107 0.5301 0.0737  -0.1021 0.0020  100 LEU A CG  
1545 C CD1 . LEU A 97  ? 0.6183 0.6077 0.4188 0.0856  -0.1075 0.0192  100 LEU A CD1 
1546 C CD2 . LEU A 97  ? 0.5680 0.5918 0.4311 0.0705  -0.1080 -0.0078 100 LEU A CD2 
1558 N N   . VAL A 98  ? 0.5182 0.5124 0.3141 0.0589  -0.0624 -0.0128 101 VAL A N   
1559 C CA  . VAL A 98  ? 0.5369 0.5326 0.3141 0.0603  -0.0620 -0.0287 101 VAL A CA  
1560 C C   . VAL A 98  ? 0.6237 0.6210 0.3818 0.0626  -0.0450 -0.0277 101 VAL A C   
1561 O O   . VAL A 98  ? 0.6043 0.6017 0.3472 0.0662  -0.0419 -0.0425 101 VAL A O   
1562 C CB  . VAL A 98  ? 0.5740 0.5651 0.3716 0.0560  -0.0649 -0.0454 101 VAL A CB  
1563 C CG1 . VAL A 98  ? 0.6285 0.6261 0.4476 0.0501  -0.0794 -0.0476 101 VAL A CG1 
1564 C CG2 . VAL A 98  ? 0.5650 0.5500 0.3822 0.0561  -0.0517 -0.0443 101 VAL A CG2 
1574 N N   . ASP A 99  ? 0.5666 0.5664 0.3245 0.0598  -0.0333 -0.0121 102 ASP A N   
1575 C CA  . ASP A 99  ? 0.5138 0.5245 0.2566 0.0594  -0.0151 -0.0116 102 ASP A CA  
1576 C C   . ASP A 99  ? 0.4835 0.5032 0.2441 0.0654  -0.0065 -0.0280 102 ASP A C   
1577 O O   . ASP A 99  ? 0.5602 0.5888 0.3027 0.0719  0.0022  -0.0392 102 ASP A O   
1578 C CB  . ASP A 99  ? 0.6056 0.6170 0.3046 0.0619  -0.0148 -0.0122 102 ASP A CB  
1579 C CG  . ASP A 99  ? 0.8618 0.8870 0.5425 0.0570  0.0060  -0.0050 102 ASP A CG  
1580 O OD1 . ASP A 99  ? 0.8974 0.9284 0.5961 0.0479  0.0170  0.0066  102 ASP A OD1 
1581 O OD2 . ASP A 99  ? 1.0358 1.0685 0.6842 0.0605  0.0121  -0.0120 102 ASP A OD2 
1586 N N   . ALA A 100 ? 0.4943 0.5108 0.2879 0.0649  -0.0087 -0.0287 103 ALA A N   
1587 C CA  . ALA A 100 ? 0.5377 0.5559 0.3458 0.0738  -0.0033 -0.0424 103 ALA A CA  
1588 C C   . ALA A 100 ? 0.5530 0.5982 0.3630 0.0785  0.0145  -0.0429 103 ALA A C   
1589 O O   . ALA A 100 ? 0.5363 0.5988 0.3501 0.0688  0.0236  -0.0296 103 ALA A O   
1590 C CB  . ALA A 100 ? 0.4731 0.4819 0.3119 0.0716  -0.0092 -0.0396 103 ALA A CB  
1596 N N   . ASP A 101 ? 0.4843 0.5335 0.2918 0.0932  0.0196  -0.0594 104 ASP A N   
1597 C CA  A ASP A 101 ? 0.5548 0.6385 0.3694 0.1013  0.0363  -0.0638 104 ASP A CA  
1598 C CA  B ASP A 101 ? 0.5558 0.6394 0.3704 0.1014  0.0362  -0.0639 104 ASP A CA  
1599 C C   . ASP A 101 ? 0.5341 0.6347 0.3848 0.1009  0.0388  -0.0574 104 ASP A C   
1600 O O   . ASP A 101 ? 0.4888 0.5682 0.3557 0.1002  0.0277  -0.0541 104 ASP A O   
1601 C CB  A ASP A 101 ? 0.6429 0.7232 0.4435 0.1227  0.0392  -0.0857 104 ASP A CB  
1602 C CB  B ASP A 101 ? 0.6406 0.7204 0.4418 0.1228  0.0389  -0.0857 104 ASP A CB  
1603 C CG  A ASP A 101 ? 0.6045 0.6563 0.4181 0.1360  0.0291  -0.0946 104 ASP A CG  
1604 C CG  B ASP A 101 ? 0.5572 0.6275 0.3203 0.1235  0.0388  -0.0948 104 ASP A CG  
1605 O OD1 A ASP A 101 ? 0.7272 0.7397 0.5299 0.1316  0.0157  -0.0977 104 ASP A OD1 
1606 O OD1 B ASP A 101 ? 0.8106 0.9058 0.5572 0.1163  0.0501  -0.0890 104 ASP A OD1 
1607 O OD2 A ASP A 101 ? 0.7415 0.8106 0.5753 0.1503  0.0342  -0.0983 104 ASP A OD2 
1608 O OD2 B ASP A 101 ? 0.6622 0.6986 0.4093 0.1293  0.0273  -0.1078 104 ASP A OD2 
1615 N N   . GLN A 102 ? 0.5149 0.4926 0.3305 0.0048  -0.0046 0.0169  105 GLN A N   
1616 C CA  . GLN A 102 ? 0.5336 0.5019 0.3768 0.0068  -0.0029 0.0283  105 GLN A CA  
1617 C C   . GLN A 102 ? 0.5130 0.4854 0.3856 0.0019  0.0060  0.0193  105 GLN A C   
1618 O O   . GLN A 102 ? 0.4779 0.4510 0.3731 0.0041  -0.0002 0.0228  105 GLN A O   
1619 C CB  . GLN A 102 ? 0.7515 0.7035 0.5900 0.0056  0.0095  0.0443  105 GLN A CB  
1620 C CG  . GLN A 102 ? 0.9808 0.9224 0.8116 0.0119  -0.0006 0.0602  105 GLN A CG  
1621 C CD  . GLN A 102 ? 1.3088 1.2345 1.1315 0.0095  0.0130  0.0750  105 GLN A CD  
1622 O OE1 . GLN A 102 ? 1.4862 1.4087 1.2883 0.0071  0.0248  0.0743  105 GLN A OE1 
1623 N NE2 . GLN A 102 ? 1.3587 1.2740 1.1971 0.0088  0.0123  0.0876  105 GLN A NE2 
1632 N N   . GLY A 103 ? 0.4742 0.4471 0.3454 -0.0046 0.0221  0.0083  106 GLY A N   
1633 C CA  . GLY A 103 ? 0.5080 0.4824 0.4071 -0.0076 0.0331  0.0017  106 GLY A CA  
1634 C C   . GLY A 103 ? 0.4979 0.4841 0.4091 -0.0068 0.0213  -0.0104 106 GLY A C   
1635 O O   . GLY A 103 ? 0.4490 0.4359 0.3853 -0.0054 0.0223  -0.0085 106 GLY A O   
1639 N N   . THR A 104 ? 0.4066 0.4040 0.3004 -0.0077 0.0098  -0.0223 107 THR A N   
1640 C CA  . THR A 104 ? 0.4512 0.4623 0.3581 -0.0071 -0.0009 -0.0339 107 THR A CA  
1641 C C   . THR A 104 ? 0.4381 0.4497 0.3574 0.0017  -0.0163 -0.0224 107 THR A C   
1642 O O   . THR A 104 ? 0.3931 0.4082 0.3329 0.0028  -0.0185 -0.0264 107 THR A O   
1643 C CB  . THR A 104 ? 0.4679 0.4957 0.3540 -0.0108 -0.0105 -0.0482 107 THR A CB  
1644 O OG1 . THR A 104 ? 0.5100 0.5340 0.3825 -0.0216 0.0064  -0.0617 107 THR A OG1 
1645 C CG2 . THR A 104 ? 0.5177 0.5632 0.4203 -0.0106 -0.0212 -0.0601 107 THR A CG2 
1653 N N   . ILE A 105 ? 0.3761 0.3816 0.2819 0.0077  -0.0252 -0.0081 108 ILE A N   
1654 C CA  . ILE A 105 ? 0.4035 0.4041 0.3192 0.0151  -0.0369 0.0025  108 ILE A CA  
1655 C C   . ILE A 105 ? 0.4416 0.4324 0.3794 0.0126  -0.0295 0.0084  108 ILE A C   
1656 O O   . ILE A 105 ? 0.3777 0.3690 0.3301 0.0150  -0.0355 0.0072  108 ILE A O   
1657 C CB  . ILE A 105 ? 0.3989 0.3896 0.2945 0.0212  -0.0437 0.0175  108 ILE A CB  
1658 C CG1 . ILE A 105 ? 0.4289 0.4332 0.3035 0.0267  -0.0553 0.0141  108 ILE A CG1 
1659 C CG2 . ILE A 105 ? 0.5016 0.4803 0.4068 0.0265  -0.0509 0.0282  108 ILE A CG2 
1660 C CD1 . ILE A 105 ? 0.5262 0.5182 0.3778 0.0350  -0.0607 0.0320  108 ILE A CD1 
1672 N N   . LEU A 106 ? 0.4092 0.3924 0.3498 0.0080  -0.0163 0.0155  109 LEU A N   
1673 C CA  A LEU A 106 ? 0.3867 0.3664 0.3497 0.0058  -0.0105 0.0224  109 LEU A CA  
1674 C CA  B LEU A 106 ? 0.3878 0.3675 0.3508 0.0056  -0.0097 0.0224  109 LEU A CA  
1675 C C   . LEU A 106 ? 0.3946 0.3815 0.3748 0.0048  -0.0055 0.0119  109 LEU A C   
1676 O O   . LEU A 106 ? 0.3790 0.3659 0.3743 0.0057  -0.0094 0.0151  109 LEU A O   
1677 C CB  A LEU A 106 ? 0.4202 0.3949 0.3863 0.0019  0.0039  0.0328  109 LEU A CB  
1678 C CB  B LEU A 106 ? 0.4181 0.3937 0.3839 0.0016  0.0060  0.0309  109 LEU A CB  
1679 C CG  A LEU A 106 ? 0.4546 0.4316 0.4461 0.0000  0.0082  0.0421  109 LEU A CG  
1680 C CG  B LEU A 106 ? 0.4558 0.4224 0.4113 0.0011  0.0051  0.0448  109 LEU A CG  
1681 C CD1 A LEU A 106 ? 0.5464 0.5197 0.5410 -0.0004 -0.0060 0.0496  109 LEU A CD1 
1682 C CD1 B LEU A 106 ? 0.4235 0.3872 0.3741 -0.0020 0.0230  0.0484  109 LEU A CD1 
1683 C CD2 A LEU A 106 ? 0.5339 0.5104 0.5328 -0.0028 0.0235  0.0525  109 LEU A CD2 
1684 C CD2 B LEU A 106 ? 0.5029 0.4677 0.4764 -0.0010 0.0003  0.0560  109 LEU A CD2 
1707 N N   . ALA A 107 ? 0.3448 0.3365 0.3220 0.0021  0.0038  -0.0009 110 ALA A N   
1708 C CA  . ALA A 107 ? 0.3439 0.3400 0.3370 0.0007  0.0108  -0.0116 110 ALA A CA  
1709 C C   . ALA A 107 ? 0.3743 0.3760 0.3726 0.0042  -0.0033 -0.0169 110 ALA A C   
1710 O O   . ALA A 107 ? 0.3687 0.3700 0.3826 0.0050  -0.0006 -0.0175 110 ALA A O   
1711 C CB  . ALA A 107 ? 0.4403 0.4390 0.4253 -0.0049 0.0223  -0.0276 110 ALA A CB  
1717 N N   . LEU A 108 ? 0.3362 0.3440 0.3213 0.0069  -0.0171 -0.0208 111 LEU A N   
1718 C CA  . LEU A 108 ? 0.3642 0.3789 0.3551 0.0113  -0.0290 -0.0263 111 LEU A CA  
1719 C C   . LEU A 108 ? 0.3981 0.4021 0.3948 0.0156  -0.0352 -0.0149 111 LEU A C   
1720 O O   . LEU A 108 ? 0.3661 0.3702 0.3743 0.0172  -0.0364 -0.0185 111 LEU A O   
1721 C CB  . LEU A 108 ? 0.3674 0.3933 0.3435 0.0155  -0.0425 -0.0297 111 LEU A CB  
1722 C CG  . LEU A 108 ? 0.4471 0.4910 0.4183 0.0105  -0.0422 -0.0456 111 LEU A CG  
1723 C CD1 . LEU A 108 ? 0.5287 0.5859 0.4828 0.0164  -0.0580 -0.0433 111 LEU A CD1 
1724 C CD2 . LEU A 108 ? 0.5253 0.5807 0.5165 0.0077  -0.0399 -0.0603 111 LEU A CD2 
1736 N N   . VAL A 109 ? 0.3428 0.3368 0.3294 0.0168  -0.0396 -0.0018 112 VAL A N   
1737 C CA  . VAL A 109 ? 0.3403 0.3226 0.3302 0.0181  -0.0452 0.0074  112 VAL A CA  
1738 C C   . VAL A 109 ? 0.3548 0.3364 0.3597 0.0134  -0.0378 0.0100  112 VAL A C   
1739 O O   . VAL A 109 ? 0.3202 0.2974 0.3300 0.0137  -0.0419 0.0106  112 VAL A O   
1740 C CB  . VAL A 109 ? 0.3840 0.3548 0.3609 0.0180  -0.0486 0.0200  112 VAL A CB  
1741 C CG1 . VAL A 109 ? 0.4342 0.3920 0.4154 0.0148  -0.0519 0.0282  112 VAL A CG1 
1742 C CG2 . VAL A 109 ? 0.4489 0.4192 0.4105 0.0256  -0.0574 0.0199  112 VAL A CG2 
1752 N N   . GLY A 110 ? 0.2970 0.2829 0.3087 0.0097  -0.0260 0.0125  113 GLY A N   
1753 C CA  . GLY A 110 ? 0.3232 0.3111 0.3505 0.0075  -0.0191 0.0183  113 GLY A CA  
1754 C C   . GLY A 110 ? 0.3364 0.3276 0.3726 0.0095  -0.0152 0.0089  113 GLY A C   
1755 O O   . GLY A 110 ? 0.2881 0.2787 0.3312 0.0097  -0.0167 0.0129  113 GLY A O   
1759 N N   . ALA A 111 ? 0.2756 0.2709 0.3108 0.0100  -0.0098 -0.0043 114 ALA A N   
1760 C CA  . ALA A 111 ? 0.2504 0.2481 0.2952 0.0110  -0.0045 -0.0141 114 ALA A CA  
1761 C C   . ALA A 111 ? 0.2547 0.2502 0.2971 0.0143  -0.0166 -0.0163 114 ALA A C   
1762 O O   . ALA A 111 ? 0.2651 0.2590 0.3144 0.0154  -0.0134 -0.0188 114 ALA A O   
1763 C CB  . ALA A 111 ? 0.3212 0.3253 0.3652 0.0082  0.0025  -0.0298 114 ALA A CB  
1769 N N   . ASP A 112 ? 0.2571 0.2513 0.2885 0.0167  -0.0291 -0.0159 115 ASP A N   
1770 C CA  . ASP A 112 ? 0.2604 0.2496 0.2894 0.0209  -0.0383 -0.0177 115 ASP A CA  
1771 C C   . ASP A 112 ? 0.2886 0.2667 0.3158 0.0189  -0.0403 -0.0086 115 ASP A C   
1772 O O   . ASP A 112 ? 0.2829 0.2560 0.3111 0.0204  -0.0409 -0.0121 115 ASP A O   
1773 C CB  . ASP A 112 ? 0.2536 0.2420 0.2713 0.0255  -0.0490 -0.0163 115 ASP A CB  
1774 C CG  . ASP A 112 ? 0.3432 0.3264 0.3602 0.0322  -0.0560 -0.0192 115 ASP A CG  
1775 O OD1 . ASP A 112 ? 0.3732 0.3410 0.3843 0.0320  -0.0587 -0.0131 115 ASP A OD1 
1776 O OD2 . ASP A 112 ? 0.4298 0.4254 0.4534 0.0367  -0.0574 -0.0281 115 ASP A OD2 
1781 N N   . GLY A 113 ? 0.2850 0.2597 0.3088 0.0147  -0.0417 0.0026  116 GLY A N   
1782 C CA  . GLY A 113 ? 0.2881 0.2571 0.3112 0.0102  -0.0447 0.0109  116 GLY A CA  
1783 C C   . GLY A 113 ? 0.2905 0.2654 0.3230 0.0102  -0.0374 0.0109  116 GLY A C   
1784 O O   . GLY A 113 ? 0.3002 0.2706 0.3287 0.0085  -0.0409 0.0123  116 GLY A O   
1788 N N   . ILE A 114 ? 0.2472 0.2309 0.2908 0.0116  -0.0259 0.0104  117 ILE A N   
1789 C CA  . ILE A 114 ? 0.2322 0.2193 0.2847 0.0132  -0.0166 0.0124  117 ILE A CA  
1790 C C   . ILE A 114 ? 0.2509 0.2324 0.3005 0.0161  -0.0159 0.0010  117 ILE A C   
1791 O O   . ILE A 114 ? 0.2695 0.2485 0.3179 0.0168  -0.0141 0.0041  117 ILE A O   
1792 C CB  . ILE A 114 ? 0.2646 0.2573 0.3292 0.0146  -0.0010 0.0132  117 ILE A CB  
1793 C CG1 . ILE A 114 ? 0.3125 0.3113 0.3824 0.0128  -0.0002 0.0275  117 ILE A CG1 
1794 C CG2 . ILE A 114 ? 0.3213 0.3137 0.3949 0.0181  0.0120  0.0138  117 ILE A CG2 
1795 C CD1 . ILE A 114 ? 0.3790 0.3800 0.4590 0.0145  0.0172  0.0284  117 ILE A CD1 
1807 N N   . MET A 115 ? 0.2469 0.2287 0.2963 0.0179  -0.0164 -0.0112 118 MET A N   
1808 C CA  . MET A 115 ? 0.2367 0.2165 0.2881 0.0208  -0.0139 -0.0225 118 MET A CA  
1809 C C   . MET A 115 ? 0.2834 0.2524 0.3234 0.0216  -0.0223 -0.0200 118 MET A C   
1810 O O   . MET A 115 ? 0.2737 0.2377 0.3127 0.0228  -0.0173 -0.0223 118 MET A O   
1811 C CB  . MET A 115 ? 0.2432 0.2304 0.2972 0.0225  -0.0174 -0.0341 118 MET A CB  
1812 C CG  . MET A 115 ? 0.2873 0.2756 0.3467 0.0262  -0.0165 -0.0448 118 MET A CG  
1813 S SD  . MET A 115 ? 0.2869 0.2937 0.3539 0.0281  -0.0222 -0.0568 118 MET A SD  
1814 C CE  . MET A 115 ? 0.2938 0.2931 0.3467 0.0344  -0.0378 -0.0480 118 MET A CE  
1824 N N   . ILE A 116 ? 0.2586 0.2214 0.2881 0.0205  -0.0337 -0.0159 119 ILE A N   
1825 C CA  . ILE A 116 ? 0.2977 0.2461 0.3144 0.0203  -0.0396 -0.0164 119 ILE A CA  
1826 C C   . ILE A 116 ? 0.2908 0.2363 0.3003 0.0143  -0.0406 -0.0079 119 ILE A C   
1827 O O   . ILE A 116 ? 0.2918 0.2280 0.2914 0.0135  -0.0402 -0.0105 119 ILE A O   
1828 C CB  . ILE A 116 ? 0.3079 0.2464 0.3149 0.0207  -0.0489 -0.0148 119 ILE A CB  
1829 C CG1 . ILE A 116 ? 0.2990 0.2436 0.3121 0.0286  -0.0498 -0.0212 119 ILE A CG1 
1830 C CG2 . ILE A 116 ? 0.3578 0.2766 0.3496 0.0188  -0.0519 -0.0165 119 ILE A CG2 
1831 C CD1 . ILE A 116 ? 0.3022 0.2504 0.3240 0.0347  -0.0441 -0.0321 119 ILE A CD1 
1843 N N   . GLY A 117 ? 0.2519 0.2065 0.2656 0.0098  -0.0424 0.0026  120 GLY A N   
1844 C CA  . GLY A 117 ? 0.2751 0.2330 0.2840 0.0040  -0.0460 0.0124  120 GLY A CA  
1845 C C   . GLY A 117 ? 0.3097 0.2719 0.3213 0.0077  -0.0372 0.0137  120 GLY A C   
1846 O O   . GLY A 117 ? 0.3015 0.2608 0.3008 0.0045  -0.0408 0.0166  120 GLY A O   
1850 N N   . THR A 118 ? 0.2723 0.2400 0.2979 0.0138  -0.0248 0.0112  121 THR A N   
1851 C CA  . THR A 118 ? 0.2513 0.2196 0.2792 0.0178  -0.0139 0.0133  121 THR A CA  
1852 C C   . THR A 118 ? 0.3121 0.2676 0.3299 0.0197  -0.0112 0.0016  121 THR A C   
1853 O O   . THR A 118 ? 0.2984 0.2502 0.3089 0.0213  -0.0057 0.0046  121 THR A O   
1854 C CB  . THR A 118 ? 0.2748 0.2492 0.3208 0.0225  0.0021  0.0136  121 THR A CB  
1855 O OG1 . THR A 118 ? 0.2797 0.2522 0.3320 0.0227  0.0052  -0.0008 121 THR A OG1 
1856 C CG2 . THR A 118 ? 0.2990 0.2847 0.3552 0.0223  0.0032  0.0271  121 THR A CG2 
1864 N N   . GLY A 119 ? 0.2871 0.2368 0.3055 0.0207  -0.0135 -0.0105 122 GLY A N   
1865 C CA  . GLY A 119 ? 0.3235 0.2610 0.3331 0.0229  -0.0116 -0.0204 122 GLY A CA  
1866 C C   . GLY A 119 ? 0.3570 0.2822 0.3441 0.0185  -0.0190 -0.0172 122 GLY A C   
1867 O O   . GLY A 119 ? 0.3293 0.2455 0.3059 0.0196  -0.0129 -0.0203 122 GLY A O   
1871 N N   . LEU A 120 ? 0.3081 0.2323 0.2865 0.0121  -0.0314 -0.0117 123 LEU A N   
1872 C CA  . LEU A 120 ? 0.2993 0.2120 0.2547 0.0046  -0.0391 -0.0104 123 LEU A CA  
1873 C C   . LEU A 120 ? 0.3006 0.2222 0.2486 0.0020  -0.0384 -0.0007 123 LEU A C   
1874 O O   . LEU A 120 ? 0.3500 0.2611 0.2767 -0.0012 -0.0386 -0.0032 123 LEU A O   
1875 C CB  . LEU A 120 ? 0.2996 0.2124 0.2518 -0.0035 -0.0513 -0.0060 123 LEU A CB  
1876 C CG  . LEU A 120 ? 0.3971 0.3001 0.3262 -0.0156 -0.0606 -0.0054 123 LEU A CG  
1877 C CD1 . LEU A 120 ? 0.3998 0.2765 0.3080 -0.0161 -0.0569 -0.0180 123 LEU A CD1 
1878 C CD2 . LEU A 120 ? 0.4662 0.3716 0.3989 -0.0238 -0.0700 -0.0008 123 LEU A CD2 
1890 N N   . VAL A 121 ? 0.2758 0.2169 0.2395 0.0036  -0.0377 0.0116  124 VAL A N   
1891 C CA  . VAL A 121 ? 0.2944 0.2463 0.2534 0.0041  -0.0364 0.0237  124 VAL A CA  
1892 C C   . VAL A 121 ? 0.3052 0.2470 0.2581 0.0114  -0.0223 0.0194  124 VAL A C   
1893 O O   . VAL A 121 ? 0.3392 0.2782 0.2728 0.0100  -0.0229 0.0234  124 VAL A O   
1894 C CB  . VAL A 121 ? 0.2997 0.2725 0.2808 0.0080  -0.0336 0.0383  124 VAL A CB  
1895 C CG1 . VAL A 121 ? 0.3373 0.3214 0.3160 0.0127  -0.0292 0.0531  124 VAL A CG1 
1896 C CG2 . VAL A 121 ? 0.3687 0.3537 0.3550 -0.0005 -0.0477 0.0447  124 VAL A CG2 
1906 N N   . GLY A 122 ? 0.3206 0.2574 0.2895 0.0182  -0.0092 0.0106  125 GLY A N   
1907 C CA  . GLY A 122 ? 0.3362 0.2632 0.3016 0.0239  0.0059  0.0059  125 GLY A CA  
1908 C C   . GLY A 122 ? 0.3405 0.2498 0.2825 0.0211  0.0041  -0.0040 125 GLY A C   
1909 O O   . GLY A 122 ? 0.3765 0.2776 0.3036 0.0231  0.0124  -0.0027 125 GLY A O   
1913 N N   . ALA A 123 ? 0.3278 0.2286 0.2656 0.0173  -0.0046 -0.0138 126 ALA A N   
1914 C CA  . ALA A 123 ? 0.3650 0.2454 0.2809 0.0151  -0.0039 -0.0241 126 ALA A CA  
1915 C C   . ALA A 123 ? 0.4235 0.2978 0.3080 0.0069  -0.0115 -0.0188 126 ALA A C   
1916 O O   . ALA A 123 ? 0.3957 0.2523 0.2571 0.0059  -0.0053 -0.0255 126 ALA A O   
1917 C CB  . ALA A 123 ? 0.3912 0.2629 0.3099 0.0137  -0.0110 -0.0329 126 ALA A CB  
1923 N N   . LEU A 124 ? 0.3436 0.2336 0.2260 0.0002  -0.0247 -0.0071 127 LEU A N   
1924 C CA  . LEU A 124 ? 0.3710 0.2612 0.2245 -0.0101 -0.0355 -0.0023 127 LEU A CA  
1925 C C   . LEU A 124 ? 0.3778 0.2857 0.2276 -0.0066 -0.0343 0.0137  127 LEU A C   
1926 O O   . LEU A 124 ? 0.4054 0.3186 0.2301 -0.0147 -0.0446 0.0194  127 LEU A O   
1927 C CB  . LEU A 124 ? 0.4089 0.3084 0.2637 -0.0217 -0.0527 0.0007  127 LEU A CB  
1928 C CG  . LEU A 124 ? 0.4120 0.2913 0.2660 -0.0258 -0.0545 -0.0127 127 LEU A CG  
1929 C CD1 . LEU A 124 ? 0.4773 0.3665 0.3341 -0.0380 -0.0695 -0.0079 127 LEU A CD1 
1930 C CD2 . LEU A 124 ? 0.4743 0.3252 0.2969 -0.0308 -0.0502 -0.0261 127 LEU A CD2 
1942 N N   . THR A 125 ? 0.3660 0.2808 0.2370 0.0053  -0.0206 0.0204  128 THR A N   
1943 C CA  . THR A 125 ? 0.3659 0.2956 0.2359 0.0115  -0.0164 0.0382  128 THR A CA  
1944 C C   . THR A 125 ? 0.4366 0.3515 0.2782 0.0141  -0.0068 0.0373  128 THR A C   
1945 O O   . THR A 125 ? 0.4654 0.3593 0.3040 0.0177  0.0078  0.0243  128 THR A O   
1946 C CB  . THR A 125 ? 0.3707 0.3080 0.2747 0.0227  -0.0018 0.0440  128 THR A CB  
1947 O OG1 . THR A 125 ? 0.3997 0.3557 0.3248 0.0208  -0.0113 0.0517  128 THR A OG1 
1948 C CG2 . THR A 125 ? 0.4076 0.3491 0.3119 0.0333  0.0126  0.0599  128 THR A CG2 
1956 N N   . LYS A 126 ? 0.4174 0.3448 0.2374 0.0123  -0.0150 0.0521  129 LYS A N   
1957 C CA  . LYS A 126 ? 0.4520 0.3641 0.2377 0.0132  -0.0074 0.0512  129 LYS A CA  
1958 C C   . LYS A 126 ? 0.5607 0.4712 0.3527 0.0277  0.0127  0.0639  129 LYS A C   
1959 O O   . LYS A 126 ? 0.5839 0.4778 0.3493 0.0299  0.0235  0.0622  129 LYS A O   
1960 C CB  . LYS A 126 ? 0.5144 0.4408 0.2666 0.0030  -0.0269 0.0603  129 LYS A CB  
1961 C CG  . LYS A 126 ? 0.6138 0.5348 0.3523 -0.0146 -0.0443 0.0445  129 LYS A CG  
1962 C CD  . LYS A 126 ? 0.7195 0.6602 0.4275 -0.0279 -0.0657 0.0529  129 LYS A CD  
1963 C CE  . LYS A 126 ? 0.9794 0.9280 0.6910 -0.0452 -0.0848 0.0444  129 LYS A CE  
1964 N NZ  . LYS A 126 ? 1.3531 1.3437 1.0804 -0.0486 -0.1032 0.0642  129 LYS A NZ  
1978 N N   . VAL A 127 ? 0.4429 0.3688 0.2664 0.0372  0.0190  0.0777  130 VAL A N   
1979 C CA  . VAL A 127 ? 0.4595 0.3795 0.2912 0.0508  0.0416  0.0892  130 VAL A CA  
1980 C C   . VAL A 127 ? 0.4771 0.3779 0.3328 0.0536  0.0617  0.0715  130 VAL A C   
1981 O O   . VAL A 127 ? 0.4372 0.3446 0.3229 0.0529  0.0613  0.0658  130 VAL A O   
1982 C CB  . VAL A 127 ? 0.5066 0.4500 0.3610 0.0602  0.0417  0.1129  130 VAL A CB  
1983 C CG1 . VAL A 127 ? 0.5086 0.4389 0.3726 0.0744  0.0698  0.1230  130 VAL A CG1 
1984 C CG2 . VAL A 127 ? 0.5897 0.5591 0.4227 0.0579  0.0201  0.1325  130 VAL A CG2 
1994 N N   . TYR A 128 ? 0.3456 0.4484 0.2599 0.0177  0.0096  0.0590  131 TYR A N   
1995 C CA  . TYR A 128 ? 0.3560 0.4578 0.2877 0.0149  0.0232  0.0545  131 TYR A CA  
1996 C C   . TYR A 128 ? 0.3688 0.4535 0.3262 0.0096  0.0237  0.0641  131 TYR A C   
1997 O O   . TYR A 128 ? 0.3045 0.3851 0.2826 0.0074  0.0251  0.0540  131 TYR A O   
1998 C CB  . TYR A 128 ? 0.4331 0.5541 0.3481 0.0131  0.0379  0.0642  131 TYR A CB  
1999 C CG  . TYR A 128 ? 0.4034 0.5417 0.3387 0.0101  0.0523  0.0619  131 TYR A CG  
2000 C CD1 . TYR A 128 ? 0.4767 0.6229 0.4177 0.0206  0.0557  0.0419  131 TYR A CD1 
2001 C CD2 . TYR A 128 ? 0.5144 0.6617 0.4617 -0.0043 0.0614  0.0819  131 TYR A CD2 
2002 C CE1 . TYR A 128 ? 0.4414 0.6155 0.4050 0.0213  0.0685  0.0430  131 TYR A CE1 
2003 C CE2 . TYR A 128 ? 0.4509 0.6275 0.4208 -0.0105 0.0728  0.0829  131 TYR A CE2 
2004 C CZ  . TYR A 128 ? 0.5477 0.7428 0.5280 0.0045  0.0764  0.0638  131 TYR A CZ  
2005 O OH  . TYR A 128 ? 0.5550 0.7900 0.5610 0.0019  0.0872  0.0676  131 TYR A OH  
2015 N N   A SER A 129 ? 0.3588 0.4283 0.3098 0.0085  0.0222  0.0838  132 SER A N   
2016 N N   B SER A 129 ? 0.3579 0.4274 0.3089 0.0085  0.0223  0.0839  132 SER A N   
2017 C CA  A SER A 129 ? 0.3894 0.4298 0.3536 0.0034  0.0233  0.0910  132 SER A CA  
2018 C CA  B SER A 129 ? 0.3892 0.4294 0.3534 0.0035  0.0232  0.0910  132 SER A CA  
2019 C C   A SER A 129 ? 0.3801 0.4093 0.3617 0.0110  0.0157  0.0785  132 SER A C   
2020 C C   B SER A 129 ? 0.3808 0.4101 0.3625 0.0110  0.0157  0.0784  132 SER A C   
2021 O O   A SER A 129 ? 0.3701 0.3799 0.3633 0.0054  0.0174  0.0746  132 SER A O   
2022 O O   B SER A 129 ? 0.3700 0.3803 0.3635 0.0052  0.0174  0.0742  132 SER A O   
2023 C CB  A SER A 129 ? 0.4568 0.4700 0.4017 0.0053  0.0228  0.1142  132 SER A CB  
2024 C CB  B SER A 129 ? 0.4569 0.4701 0.4018 0.0062  0.0223  0.1140  132 SER A CB  
2025 O OG  A SER A 129 ? 0.3796 0.3921 0.3193 0.0236  0.0129  0.1185  132 SER A OG  
2026 O OG  B SER A 129 ? 0.5868 0.6078 0.5150 -0.0054 0.0308  0.1289  132 SER A OG  
2037 N N   . TYR A 130 ? 0.3305 0.3749 0.3127 0.0210  0.0067  0.0728  133 TYR A N   
2038 C CA  . TYR A 130 ? 0.2896 0.3309 0.2892 0.0267  0.0011  0.0642  133 TYR A CA  
2039 C C   . TYR A 130 ? 0.2923 0.3372 0.3053 0.0191  0.0022  0.0463  133 TYR A C   
2040 O O   . TYR A 130 ? 0.2919 0.3296 0.3181 0.0208  0.0004  0.0406  133 TYR A O   
2041 C CB  . TYR A 130 ? 0.3097 0.3766 0.3105 0.0343  -0.0099 0.0657  133 TYR A CB  
2042 C CG  . TYR A 130 ? 0.4214 0.4946 0.4132 0.0480  -0.0140 0.0854  133 TYR A CG  
2043 C CD1 . TYR A 130 ? 0.4277 0.4695 0.4088 0.0569  -0.0075 0.1004  133 TYR A CD1 
2044 C CD2 . TYR A 130 ? 0.3547 0.4644 0.3464 0.0511  -0.0262 0.0898  133 TYR A CD2 
2045 C CE1 . TYR A 130 ? 0.4777 0.5217 0.4468 0.0745  -0.0117 0.1212  133 TYR A CE1 
2046 C CE2 . TYR A 130 ? 0.4540 0.5783 0.4393 0.0665  -0.0316 0.1100  133 TYR A CE2 
2047 C CZ  . TYR A 130 ? 0.4975 0.5878 0.4713 0.0813  -0.0237 0.1263  133 TYR A CZ  
2048 O OH  . TYR A 130 ? 0.6058 0.7084 0.5707 0.1018  -0.0297 0.1490  133 TYR A OH  
2058 N N   . ARG A 131 ? 0.2878 0.3436 0.2952 0.0140  0.0058  0.0380  134 ARG A N   
2059 C CA  . ARG A 131 ? 0.2746 0.3303 0.2933 0.0118  0.0073  0.0234  134 ARG A CA  
2060 C C   . ARG A 131 ? 0.3006 0.3456 0.3356 0.0068  0.0110  0.0253  134 ARG A C   
2061 O O   . ARG A 131 ? 0.2877 0.3287 0.3338 0.0067  0.0082  0.0165  134 ARG A O   
2062 C CB  . ARG A 131 ? 0.2999 0.3687 0.3076 0.0139  0.0143  0.0167  134 ARG A CB  
2063 C CG  . ARG A 131 ? 0.3111 0.3812 0.2920 0.0173  0.0084  0.0094  134 ARG A CG  
2064 C CD  . ARG A 131 ? 0.3220 0.4009 0.2815 0.0251  0.0187  0.0013  134 ARG A CD  
2065 N NE  . ARG A 131 ? 0.3421 0.4134 0.3062 0.0339  0.0223  -0.0129 134 ARG A NE  
2066 C CZ  . ARG A 131 ? 0.3842 0.4294 0.3300 0.0370  0.0143  -0.0286 134 ARG A CZ  
2067 N NH1 . ARG A 131 ? 0.3770 0.4077 0.3008 0.0276  0.0014  -0.0329 134 ARG A NH1 
2068 N NH2 . ARG A 131 ? 0.3963 0.4291 0.3426 0.0490  0.0182  -0.0389 134 ARG A NH2 
2082 N N   . PHE A 132 ? 0.2800 0.3173 0.3124 0.0000  0.0159  0.0373  135 PHE A N   
2083 C CA  . PHE A 132 ? 0.2807 0.3050 0.3225 -0.0108 0.0170  0.0380  135 PHE A CA  
2084 C C   . PHE A 132 ? 0.3102 0.3025 0.3479 -0.0067 0.0125  0.0371  135 PHE A C   
2085 O O   . PHE A 132 ? 0.3089 0.2880 0.3505 -0.0139 0.0108  0.0318  135 PHE A O   
2086 C CB  . PHE A 132 ? 0.2777 0.3024 0.3134 -0.0259 0.0232  0.0524  135 PHE A CB  
2087 C CG  . PHE A 132 ? 0.2917 0.3583 0.3326 -0.0267 0.0313  0.0538  135 PHE A CG  
2088 C CD1 . PHE A 132 ? 0.3102 0.4076 0.3709 -0.0287 0.0339  0.0471  135 PHE A CD1 
2089 C CD2 . PHE A 132 ? 0.2973 0.3745 0.3216 -0.0218 0.0364  0.0615  135 PHE A CD2 
2090 C CE1 . PHE A 132 ? 0.3926 0.5314 0.4572 -0.0223 0.0438  0.0479  135 PHE A CE1 
2091 C CE2 . PHE A 132 ? 0.4189 0.5342 0.4432 -0.0183 0.0461  0.0605  135 PHE A CE2 
2092 C CZ  . PHE A 132 ? 0.3906 0.5368 0.4358 -0.0167 0.0508  0.0535  135 PHE A CZ  
2102 N N   . VAL A 133 ? 0.2789 0.2629 0.3079 0.0065  0.0106  0.0424  136 VAL A N   
2103 C CA  . VAL A 133 ? 0.2680 0.2310 0.2941 0.0184  0.0090  0.0410  136 VAL A CA  
2104 C C   . VAL A 133 ? 0.2872 0.2668 0.3278 0.0193  0.0061  0.0285  136 VAL A C   
2105 O O   . VAL A 133 ? 0.2891 0.2521 0.3283 0.0200  0.0066  0.0227  136 VAL A O   
2106 C CB  . VAL A 133 ? 0.3406 0.3085 0.3602 0.0366  0.0076  0.0522  136 VAL A CB  
2107 C CG1 . VAL A 133 ? 0.3736 0.3346 0.3949 0.0551  0.0084  0.0507  136 VAL A CG1 
2108 C CG2 . VAL A 133 ? 0.4428 0.3827 0.4414 0.0373  0.0104  0.0680  136 VAL A CG2 
2118 N N   . TRP A 134 ? 0.2499 0.2581 0.2994 0.0181  0.0025  0.0241  137 TRP A N   
2119 C CA  . TRP A 134 ? 0.2127 0.2298 0.2720 0.0165  -0.0009 0.0147  137 TRP A CA  
2120 C C   . TRP A 134 ? 0.2691 0.2789 0.3325 0.0086  0.0000  0.0074  137 TRP A C   
2121 O O   . TRP A 134 ? 0.2515 0.2572 0.3181 0.0082  -0.0017 0.0026  137 TRP A O   
2122 C CB  . TRP A 134 ? 0.2125 0.2484 0.2719 0.0134  -0.0067 0.0111  137 TRP A CB  
2123 C CG  . TRP A 134 ? 0.2121 0.2667 0.2710 0.0181  -0.0111 0.0199  137 TRP A CG  
2124 C CD1 . TRP A 134 ? 0.2526 0.3187 0.3017 0.0186  -0.0146 0.0254  137 TRP A CD1 
2125 C CD2 . TRP A 134 ? 0.2490 0.3202 0.3181 0.0238  -0.0127 0.0257  137 TRP A CD2 
2126 N NE1 . TRP A 134 ? 0.2269 0.3179 0.2818 0.0244  -0.0201 0.0358  137 TRP A NE1 
2127 C CE2 . TRP A 134 ? 0.2601 0.3585 0.3296 0.0280  -0.0183 0.0362  137 TRP A CE2 
2128 C CE3 . TRP A 134 ? 0.2183 0.2903 0.2959 0.0265  -0.0094 0.0242  137 TRP A CE3 
2129 C CZ2 . TRP A 134 ? 0.2520 0.3854 0.3357 0.0363  -0.0205 0.0468  137 TRP A CZ2 
2130 C CZ3 . TRP A 134 ? 0.2337 0.3388 0.3230 0.0353  -0.0093 0.0341  137 TRP A CZ3 
2131 C CH2 . TRP A 134 ? 0.2453 0.3841 0.3402 0.0400  -0.0150 0.0457  137 TRP A CH2 
2142 N N   . TRP A 135 ? 0.2480 0.2630 0.3120 0.0028  0.0026  0.0083  138 TRP A N   
2143 C CA  . TRP A 135 ? 0.2206 0.2407 0.2930 -0.0043 0.0023  0.0047  138 TRP A CA  
2144 C C   . TRP A 135 ? 0.2743 0.2730 0.3419 -0.0120 0.0004  0.0047  138 TRP A C   
2145 O O   . TRP A 135 ? 0.2732 0.2734 0.3444 -0.0155 -0.0036 -0.0005 138 TRP A O   
2146 C CB  . TRP A 135 ? 0.2483 0.2893 0.3254 -0.0097 0.0074  0.0097  138 TRP A CB  
2147 C CG  . TRP A 135 ? 0.2383 0.3002 0.3300 -0.0179 0.0063  0.0100  138 TRP A CG  
2148 C CD1 . TRP A 135 ? 0.2403 0.3276 0.3438 -0.0084 0.0063  0.0061  138 TRP A CD1 
2149 C CD2 . TRP A 135 ? 0.2197 0.2793 0.3139 -0.0370 0.0036  0.0155  138 TRP A CD2 
2150 N NE1 . TRP A 135 ? 0.2485 0.3622 0.3679 -0.0195 0.0036  0.0111  138 TRP A NE1 
2151 C CE2 . TRP A 135 ? 0.2579 0.3540 0.3708 -0.0408 0.0009  0.0161  138 TRP A CE2 
2152 C CE3 . TRP A 135 ? 0.3462 0.3725 0.4247 -0.0519 0.0024  0.0205  138 TRP A CE3 
2153 C CZ2 . TRP A 135 ? 0.3442 0.4525 0.4637 -0.0640 -0.0048 0.0219  138 TRP A CZ2 
2154 C CZ3 . TRP A 135 ? 0.3964 0.4215 0.4749 -0.0760 -0.0029 0.0242  138 TRP A CZ3 
2155 C CH2 . TRP A 135 ? 0.3854 0.4545 0.4855 -0.0845 -0.0073 0.0250  138 TRP A CH2 
2166 N N   . ALA A 136 ? 0.2684 0.2418 0.3222 -0.0132 0.0027  0.0103  139 ALA A N   
2167 C CA  . ALA A 136 ? 0.3114 0.2504 0.3492 -0.0208 0.0008  0.0076  139 ALA A CA  
2168 C C   . ALA A 136 ? 0.3502 0.2788 0.3815 -0.0079 0.0006  0.0000  139 ALA A C   
2169 O O   . ALA A 136 ? 0.3407 0.2542 0.3617 -0.0145 -0.0026 -0.0071 139 ALA A O   
2170 C CB  . ALA A 136 ? 0.3633 0.2647 0.3798 -0.0226 0.0038  0.0160  139 ALA A CB  
2176 N N   . ILE A 137 ? 0.2912 0.2324 0.3273 0.0089  0.0038  0.0024  140 ILE A N   
2177 C CA  . ILE A 137 ? 0.2965 0.2414 0.3308 0.0202  0.0056  -0.0017 140 ILE A CA  
2178 C C   . ILE A 137 ? 0.3011 0.2636 0.3451 0.0114  0.0009  -0.0072 140 ILE A C   
2179 O O   . ILE A 137 ? 0.3175 0.2727 0.3520 0.0121  0.0010  -0.0121 140 ILE A O   
2180 C CB  . ILE A 137 ? 0.3046 0.2746 0.3487 0.0349  0.0083  0.0058  140 ILE A CB  
2181 C CG1 . ILE A 137 ? 0.3339 0.2840 0.3644 0.0515  0.0134  0.0133  140 ILE A CG1 
2182 C CG2 . ILE A 137 ? 0.3254 0.3150 0.3742 0.0413  0.0107  0.0046  140 ILE A CG2 
2183 C CD1 . ILE A 137 ? 0.3624 0.3510 0.4077 0.0637  0.0127  0.0248  140 ILE A CD1 
2195 N N   . SER A 138 ? 0.2559 0.2390 0.3146 0.0053  -0.0030 -0.0062 141 SER A N   
2196 C CA  . SER A 138 ? 0.2724 0.2660 0.3370 0.0013  -0.0078 -0.0094 141 SER A CA  
2197 C C   . SER A 138 ? 0.2771 0.2654 0.3379 -0.0071 -0.0119 -0.0126 141 SER A C   
2198 O O   . SER A 138 ? 0.2777 0.2665 0.3339 -0.0081 -0.0157 -0.0147 141 SER A O   
2199 C CB  . SER A 138 ? 0.2626 0.2691 0.3361 0.0017  -0.0098 -0.0089 141 SER A CB  
2200 O OG  . SER A 138 ? 0.2787 0.2873 0.3538 0.0026  -0.0143 -0.0108 141 SER A OG  
2206 N N   . THR A 139 ? 0.2450 0.2310 0.3065 -0.0157 -0.0123 -0.0114 142 THR A N   
2207 C CA  . THR A 139 ? 0.2406 0.2276 0.2992 -0.0302 -0.0191 -0.0131 142 THR A CA  
2208 C C   . THR A 139 ? 0.3203 0.2747 0.3528 -0.0337 -0.0208 -0.0198 142 THR A C   
2209 O O   . THR A 139 ? 0.3470 0.3036 0.3718 -0.0418 -0.0285 -0.0235 142 THR A O   
2210 C CB  . THR A 139 ? 0.2647 0.2591 0.3296 -0.0447 -0.0189 -0.0074 142 THR A CB  
2211 O OG1 . THR A 139 ? 0.2922 0.3219 0.3784 -0.0372 -0.0156 -0.0026 142 THR A OG1 
2212 C CG2 . THR A 139 ? 0.3299 0.3336 0.3943 -0.0669 -0.0288 -0.0070 142 THR A CG2 
2220 N N   . ALA A 140 ? 0.3175 0.2419 0.3326 -0.0242 -0.0135 -0.0215 143 ALA A N   
2221 C CA  . ALA A 140 ? 0.3338 0.2243 0.3179 -0.0206 -0.0123 -0.0300 143 ALA A CA  
2222 C C   . ALA A 140 ? 0.3393 0.2487 0.3239 -0.0116 -0.0116 -0.0321 143 ALA A C   
2223 O O   . ALA A 140 ? 0.3931 0.2885 0.3547 -0.0164 -0.0154 -0.0392 143 ALA A O   
2224 C CB  . ALA A 140 ? 0.3837 0.2419 0.3494 -0.0025 -0.0020 -0.0297 143 ALA A CB  
2230 N N   . ALA A 141 ? 0.3103 0.2490 0.3167 -0.0021 -0.0080 -0.0254 144 ALA A N   
2231 C CA  . ALA A 141 ? 0.3237 0.2791 0.3301 0.0011  -0.0080 -0.0236 144 ALA A CA  
2232 C C   . ALA A 141 ? 0.3303 0.2941 0.3376 -0.0102 -0.0191 -0.0238 144 ALA A C   
2233 O O   . ALA A 141 ? 0.3194 0.2827 0.3109 -0.0108 -0.0213 -0.0248 144 ALA A O   
2234 C CB  . ALA A 141 ? 0.2660 0.2458 0.2934 0.0059  -0.0051 -0.0152 144 ALA A CB  
2240 N N   . MET A 142 ? 0.3068 0.2841 0.3330 -0.0168 -0.0256 -0.0210 145 MET A N   
2241 C CA  . MET A 142 ? 0.2914 0.2863 0.3225 -0.0235 -0.0366 -0.0186 145 MET A CA  
2242 C C   . MET A 142 ? 0.3516 0.3352 0.3607 -0.0374 -0.0443 -0.0249 145 MET A C   
2243 O O   . MET A 142 ? 0.3399 0.3330 0.3398 -0.0404 -0.0530 -0.0238 145 MET A O   
2244 C CB  . MET A 142 ? 0.2816 0.3013 0.3380 -0.0244 -0.0395 -0.0137 145 MET A CB  
2245 C CG  . MET A 142 ? 0.3201 0.3686 0.3857 -0.0259 -0.0506 -0.0084 145 MET A CG  
2246 S SD  . MET A 142 ? 0.3351 0.4264 0.4327 -0.0217 -0.0509 -0.0010 145 MET A SD  
2247 C CE  . MET A 142 ? 0.3797 0.4802 0.4747 -0.0497 -0.0585 -0.0022 145 MET A CE  
2257 N N   . LEU A 143 ? 0.3354 0.2937 0.3305 -0.0473 -0.0428 -0.0314 146 LEU A N   
2258 C CA  . LEU A 143 ? 0.3755 0.3126 0.3410 -0.0650 -0.0524 -0.0396 146 LEU A CA  
2259 C C   . LEU A 143 ? 0.4074 0.3206 0.3374 -0.0562 -0.0493 -0.0479 146 LEU A C   
2260 O O   . LEU A 143 ? 0.4443 0.3525 0.3494 -0.0690 -0.0606 -0.0535 146 LEU A O   
2261 C CB  . LEU A 143 ? 0.4045 0.3035 0.3526 -0.0792 -0.0516 -0.0449 146 LEU A CB  
2262 C CG  . LEU A 143 ? 0.5078 0.4359 0.4870 -0.0952 -0.0558 -0.0349 146 LEU A CG  
2263 C CD1 . LEU A 143 ? 0.6725 0.5532 0.6297 -0.1080 -0.0527 -0.0371 146 LEU A CD1 
2264 C CD2 . LEU A 143 ? 0.5219 0.4914 0.5144 -0.1171 -0.0721 -0.0304 146 LEU A CD2 
2276 N N   . TYR A 144 ? 0.3791 0.2826 0.3053 -0.0354 -0.0344 -0.0480 147 TYR A N   
2277 C CA  . TYR A 144 ? 0.4354 0.3290 0.3314 -0.0244 -0.0282 -0.0529 147 TYR A CA  
2278 C C   . TYR A 144 ? 0.4107 0.3355 0.3128 -0.0281 -0.0366 -0.0450 147 TYR A C   
2279 O O   . TYR A 144 ? 0.4347 0.3515 0.3047 -0.0320 -0.0413 -0.0502 147 TYR A O   
2280 C CB  . TYR A 144 ? 0.4331 0.3302 0.3350 -0.0014 -0.0101 -0.0493 147 TYR A CB  
2281 C CG  . TYR A 144 ? 0.4526 0.3529 0.3286 0.0112  -0.0003 -0.0509 147 TYR A CG  
2282 C CD1 . TYR A 144 ? 0.5699 0.4322 0.3989 0.0208  0.0065  -0.0652 147 TYR A CD1 
2283 C CD2 . TYR A 144 ? 0.4941 0.4305 0.3860 0.0123  0.0018  -0.0383 147 TYR A CD2 
2284 C CE1 . TYR A 144 ? 0.6085 0.4779 0.4098 0.0345  0.0177  -0.0669 147 TYR A CE1 
2285 C CE2 . TYR A 144 ? 0.5439 0.4889 0.4110 0.0212  0.0117  -0.0371 147 TYR A CE2 
2286 C CZ  . TYR A 144 ? 0.5176 0.4332 0.3404 0.0338  0.0207  -0.0517 147 TYR A CZ  
2287 O OH  . TYR A 144 ? 0.6405 0.5685 0.4346 0.0451  0.0330  -0.0508 147 TYR A OH  
2297 N N   . ILE A 145 ? 0.3484 0.3041 0.2870 -0.0258 -0.0390 -0.0321 148 ILE A N   
2298 C CA  . ILE A 145 ? 0.3373 0.3145 0.2787 -0.0260 -0.0473 -0.0220 148 ILE A CA  
2299 C C   . ILE A 145 ? 0.3725 0.3596 0.3050 -0.0395 -0.0647 -0.0235 148 ILE A C   
2300 O O   . ILE A 145 ? 0.3792 0.3699 0.2878 -0.0418 -0.0719 -0.0215 148 ILE A O   
2301 C CB  . ILE A 145 ? 0.3274 0.3215 0.3024 -0.0191 -0.0467 -0.0102 148 ILE A CB  
2302 C CG1 . ILE A 145 ? 0.3249 0.3144 0.3023 -0.0119 -0.0332 -0.0064 148 ILE A CG1 
2303 C CG2 . ILE A 145 ? 0.3407 0.3494 0.3167 -0.0168 -0.0583 0.0016  148 ILE A CG2 
2304 C CD1 . ILE A 145 ? 0.3540 0.3477 0.3585 -0.0086 -0.0325 -0.0001 148 ILE A CD1 
2316 N N   . LEU A 146 ? 0.3580 0.3529 0.3070 -0.0512 -0.0723 -0.0262 149 LEU A N   
2317 C CA  . LEU A 146 ? 0.4021 0.4200 0.3486 -0.0677 -0.0912 -0.0245 149 LEU A CA  
2318 C C   . LEU A 146 ? 0.4955 0.4835 0.3936 -0.0831 -0.0979 -0.0381 149 LEU A C   
2319 O O   . LEU A 146 ? 0.4836 0.4887 0.3659 -0.0936 -0.1139 -0.0362 149 LEU A O   
2320 C CB  . LEU A 146 ? 0.3871 0.4279 0.3632 -0.0816 -0.0973 -0.0222 149 LEU A CB  
2321 C CG  . LEU A 146 ? 0.4856 0.5559 0.5043 -0.0658 -0.0901 -0.0112 149 LEU A CG  
2322 C CD1 . LEU A 146 ? 0.5703 0.6764 0.6159 -0.0821 -0.0966 -0.0065 149 LEU A CD1 
2323 C CD2 . LEU A 146 ? 0.5034 0.5974 0.5338 -0.0462 -0.0936 0.0007  149 LEU A CD2 
2335 N N   . TYR A 147 ? 0.4258 0.3668 0.2959 -0.0822 -0.0860 -0.0522 150 TYR A N   
2336 C CA  . TYR A 147 ? 0.4998 0.3991 0.3127 -0.0919 -0.0897 -0.0686 150 TYR A CA  
2337 C C   . TYR A 147 ? 0.5144 0.4226 0.3019 -0.0802 -0.0882 -0.0664 150 TYR A C   
2338 O O   . TYR A 147 ? 0.5845 0.4914 0.3374 -0.0938 -0.1028 -0.0714 150 TYR A O   
2339 C CB  . TYR A 147 ? 0.5128 0.3578 0.3007 -0.0805 -0.0723 -0.0817 150 TYR A CB  
2340 C CG  . TYR A 147 ? 0.7064 0.4975 0.4263 -0.0824 -0.0720 -0.1012 150 TYR A CG  
2341 C CD1 . TYR A 147 ? 0.9777 0.7334 0.6597 -0.1119 -0.0899 -0.1141 150 TYR A CD1 
2342 C CD2 . TYR A 147 ? 0.8385 0.6172 0.5303 -0.0554 -0.0537 -0.1060 150 TYR A CD2 
2343 C CE1 . TYR A 147 ? 1.0348 0.7301 0.6439 -0.1132 -0.0900 -0.1353 150 TYR A CE1 
2344 C CE2 . TYR A 147 ? 1.0268 0.7537 0.6495 -0.0518 -0.0507 -0.1258 150 TYR A CE2 
2345 C CZ  . TYR A 147 ? 1.0678 0.7480 0.6463 -0.0802 -0.0694 -0.1418 150 TYR A CZ  
2346 O OH  . TYR A 147 ? 1.2303 0.8528 0.7360 -0.0757 -0.0664 -0.1630 150 TYR A OH  
2356 N N   . VAL A 148 ? 0.4797 0.4007 0.2838 -0.0575 -0.0716 -0.0567 151 VAL A N   
2357 C CA  . VAL A 148 ? 0.5197 0.4495 0.2976 -0.0485 -0.0679 -0.0515 151 VAL A CA  
2358 C C   . VAL A 148 ? 0.4952 0.4595 0.2808 -0.0579 -0.0881 -0.0377 151 VAL A C   
2359 O O   . VAL A 148 ? 0.5728 0.5380 0.3202 -0.0623 -0.0960 -0.0384 151 VAL A O   
2360 C CB  . VAL A 148 ? 0.5434 0.4857 0.3434 -0.0290 -0.0476 -0.0400 151 VAL A CB  
2361 C CG1 . VAL A 148 ? 0.5419 0.5011 0.3221 -0.0240 -0.0443 -0.0279 151 VAL A CG1 
2362 C CG2 . VAL A 148 ? 0.5550 0.4712 0.3434 -0.0150 -0.0279 -0.0522 151 VAL A CG2 
2372 N N   . LEU A 149 ? 0.4911 0.4852 0.3237 -0.0580 -0.0962 -0.0244 152 LEU A N   
2373 C CA  . LEU A 149 ? 0.4605 0.4903 0.3029 -0.0598 -0.1148 -0.0087 152 LEU A CA  
2374 C C   . LEU A 149 ? 0.5790 0.6191 0.3965 -0.0818 -0.1366 -0.0163 152 LEU A C   
2375 O O   . LEU A 149 ? 0.5806 0.6457 0.3846 -0.0836 -0.1524 -0.0057 152 LEU A O   
2376 C CB  . LEU A 149 ? 0.4566 0.5145 0.3516 -0.0505 -0.1172 0.0047  152 LEU A CB  
2377 C CG  . LEU A 149 ? 0.4569 0.5030 0.3714 -0.0324 -0.1011 0.0134  152 LEU A CG  
2378 C CD1 . LEU A 149 ? 0.5676 0.6362 0.5246 -0.0211 -0.1048 0.0233  152 LEU A CD1 
2379 C CD2 . LEU A 149 ? 0.5250 0.5620 0.4167 -0.0240 -0.0975 0.0264  152 LEU A CD2 
2391 N N   . PHE A 150 ? 0.5633 0.5809 0.3686 -0.1011 -0.1394 -0.0339 153 PHE A N   
2392 C CA  . PHE A 150 ? 0.5917 0.6134 0.3668 -0.1300 -0.1630 -0.0426 153 PHE A CA  
2393 C C   . PHE A 150 ? 0.7624 0.7333 0.4660 -0.1378 -0.1619 -0.0630 153 PHE A C   
2394 O O   . PHE A 150 ? 0.9581 0.9380 0.6262 -0.1555 -0.1824 -0.0659 153 PHE A O   
2395 C CB  . PHE A 150 ? 0.7494 0.7720 0.5455 -0.1543 -0.1707 -0.0487 153 PHE A CB  
2396 C CG  . PHE A 150 ? 0.6921 0.7838 0.5470 -0.1571 -0.1829 -0.0289 153 PHE A CG  
2397 C CD1 . PHE A 150 ? 0.6415 0.7847 0.5023 -0.1718 -0.2065 -0.0187 153 PHE A CD1 
2398 C CD2 . PHE A 150 ? 0.6933 0.8008 0.5974 -0.1414 -0.1686 -0.0201 153 PHE A CD2 
2399 C CE1 . PHE A 150 ? 0.7871 0.9984 0.7055 -0.1651 -0.2122 0.0009  153 PHE A CE1 
2400 C CE2 . PHE A 150 ? 0.8767 1.0504 0.8319 -0.1388 -0.1773 -0.0023 153 PHE A CE2 
2401 C CZ  . PHE A 150 ? 0.6550 0.8858 0.6177 -0.1513 -0.2011 0.0091  153 PHE A CZ  
2411 N N   . PHE A 151 ? 0.8671 0.7860 0.5454 -0.1241 -0.1391 -0.0778 154 PHE A N   
2412 C CA  . PHE A 151 ? 0.9210 0.7856 0.5252 -0.1271 -0.1358 -0.1001 154 PHE A CA  
2413 C C   . PHE A 151 ? 1.2026 1.0639 0.7829 -0.0980 -0.1140 -0.0976 154 PHE A C   
2414 O O   . PHE A 151 ? 1.3129 1.1313 0.8295 -0.0922 -0.1053 -0.1161 154 PHE A O   
2415 C CB  . PHE A 151 ? 0.8710 0.6711 0.4511 -0.1326 -0.1273 -0.1210 154 PHE A CB  
2416 C CG  . PHE A 151 ? 0.9428 0.7479 0.5492 -0.1646 -0.1461 -0.1201 154 PHE A CG  
2417 C CD1 . PHE A 151 ? 0.9629 0.8028 0.6311 -0.1671 -0.1459 -0.1053 154 PHE A CD1 
2418 C CD2 . PHE A 151 ? 1.1549 0.9398 0.7354 -0.1880 -0.1591 -0.1297 154 PHE A CD2 
2419 C CE1 . PHE A 151 ? 0.8852 0.7399 0.5816 -0.1948 -0.1590 -0.1006 154 PHE A CE1 
2420 C CE2 . PHE A 151 ? 1.1501 0.9488 0.7614 -0.2168 -0.1725 -0.1236 154 PHE A CE2 
2421 C CZ  . PHE A 151 ? 1.0513 0.8881 0.7216 -0.2194 -0.1714 -0.1081 154 PHE A CZ  
2431 N N   . GLY A 152 ? 0.9558 0.6566 0.4475 0.1345  -0.0176 -0.0991 155 GLY A N   
2432 C CA  . GLY A 152 ? 1.1347 0.8859 0.6271 0.1532  -0.0045 -0.0889 155 GLY A CA  
2433 C C   . GLY A 152 ? 0.8611 0.6466 0.3720 0.1306  -0.0151 -0.0799 155 GLY A C   
2434 O O   . GLY A 152 ? 0.9329 0.7208 0.4124 0.1339  -0.0181 -0.0821 155 GLY A O   
2438 N N   . PHE A 153 ? 0.9256 0.7410 0.4959 0.1060  -0.0215 -0.0674 156 PHE A N   
2439 C CA  . PHE A 153 ? 0.8927 0.7505 0.4925 0.0890  -0.0287 -0.0532 156 PHE A CA  
2440 C C   . PHE A 153 ? 1.0908 0.9223 0.6653 0.0697  -0.0489 -0.0627 156 PHE A C   
2441 O O   . PHE A 153 ? 1.0751 0.9279 0.6401 0.0675  -0.0529 -0.0564 156 PHE A O   
2442 C CB  . PHE A 153 ? 0.8091 0.6999 0.4730 0.0718  -0.0307 -0.0388 156 PHE A CB  
2443 C CG  . PHE A 153 ? 0.8089 0.7419 0.5020 0.0846  -0.0142 -0.0231 156 PHE A CG  
2444 C CD1 . PHE A 153 ? 0.7916 0.7323 0.4594 0.1116  0.0029  -0.0233 156 PHE A CD1 
2445 C CD2 . PHE A 153 ? 0.7247 0.6912 0.4686 0.0697  -0.0168 -0.0073 156 PHE A CD2 
2446 C CE1 . PHE A 153 ? 0.7704 0.7579 0.4679 0.1202  0.0167  -0.0064 156 PHE A CE1 
2447 C CE2 . PHE A 153 ? 0.7127 0.7168 0.4816 0.0767  -0.0046 0.0081  156 PHE A CE2 
2448 C CZ  . PHE A 153 ? 0.8021 0.8206 0.5500 0.1004  0.0120  0.0097  156 PHE A CZ  
2458 N N   . THR A 154 ? 0.9752 0.7636 0.5397 0.0534  -0.0627 -0.0757 157 THR A N   
2459 C CA  . THR A 154 ? 1.1091 0.8760 0.6503 0.0317  -0.0840 -0.0836 157 THR A CA  
2460 C C   . THR A 154 ? 1.1216 0.8640 0.5979 0.0463  -0.0846 -0.0944 157 THR A C   
2461 O O   . THR A 154 ? 1.1068 0.8625 0.5732 0.0356  -0.0963 -0.0916 157 THR A O   
2462 C CB  . THR A 154 ? 1.1064 0.8289 0.6405 0.0114  -0.0980 -0.0952 157 THR A CB  
2463 O OG1 . THR A 154 ? 0.9038 0.6575 0.5002 -0.0027 -0.0979 -0.0838 157 THR A OG1 
2464 C CG2 . THR A 154 ? 1.2929 0.9924 0.7972 -0.0130 -0.1216 -0.1033 157 THR A CG2 
2472 N N   . SER A 155 ? 1.0963 0.8099 0.5385 0.0715  -0.0704 -0.1042 158 SER A N   
2473 C CA  . SER A 155 ? 1.3709 1.0705 0.7714 0.0859  -0.0668 -0.1116 158 SER A CA  
2474 C C   . SER A 155 ? 1.4517 1.2042 0.8554 0.0956  -0.0589 -0.0985 158 SER A C   
2475 O O   . SER A 155 ? 1.3272 1.0786 0.7055 0.0916  -0.0659 -0.1015 158 SER A O   
2476 C CB  . SER A 155 ? 1.1556 0.8250 0.5315 0.1154  -0.0508 -0.1198 158 SER A CB  
2479 N N   . LYS A 156 ? 1.2501 1.0512 0.6857 0.1066  -0.0448 -0.0820 159 LYS A N   
2480 C CA  . LYS A 156 ? 1.3220 1.1755 0.7628 0.1139  -0.0366 -0.0657 159 LYS A CA  
2481 C C   . LYS A 156 ? 1.2539 1.1296 0.7156 0.0879  -0.0548 -0.0541 159 LYS A C   
2482 O O   . LYS A 156 ? 1.1249 1.0185 0.5692 0.0864  -0.0583 -0.0483 159 LYS A O   
2483 C CB  . LYS A 156 ? 1.2348 1.1380 0.7070 0.1320  -0.0150 -0.0483 159 LYS A CB  
2484 C CG  . LYS A 156 ? 1.4271 1.3747 0.8937 0.1473  0.0001  -0.0357 159 LYS A CG  
2485 C CD  . LYS A 156 ? 1.1749 1.1760 0.6781 0.1614  0.0203  -0.0168 159 LYS A CD  
2486 C CE  . LYS A 156 ? 1.1024 1.1637 0.6224 0.1586  0.0279  0.0066  159 LYS A CE  
2487 N NZ  . LYS A 156 ? 1.1369 1.2043 0.6582 0.1342  0.0113  0.0160  159 LYS A NZ  
2501 N N   . ALA A 157 ? 1.0996 0.9798 0.6127 0.0653  -0.0651 -0.0488 160 ALA A N   
2502 C CA  . ALA A 157 ? 1.0118 0.9160 0.5573 0.0417  -0.0819 -0.0366 160 ALA A CA  
2503 C C   . ALA A 157 ? 1.1741 1.0569 0.6759 0.0319  -0.0998 -0.0464 160 ALA A C   
2504 O O   . ALA A 157 ? 1.1440 1.0541 0.6513 0.0241  -0.1083 -0.0341 160 ALA A O   
2505 C CB  . ALA A 157 ? 0.8830 0.7852 0.4778 0.0227  -0.0913 -0.0355 160 ALA A CB  
2511 N N   . GLU A 158 ? 1.0448 0.8757 0.4996 0.0316  -0.1070 -0.0682 161 GLU A N   
2512 C CA  . GLU A 158 ? 1.2727 1.0859 0.7035 0.0151  -0.1245 -0.0774 161 GLU A CA  
2513 C C   . GLU A 158 ? 1.2322 1.0600 0.6302 0.0278  -0.1184 -0.0754 161 GLU A C   
2514 O O   . GLU A 158 ? 1.3165 1.1401 0.6979 0.0143  -0.1333 -0.0794 161 GLU A O   
2515 C CB  . GLU A 158 ? 1.3534 1.1122 0.7607 0.0096  -0.1288 -0.0974 161 GLU A CB  
2516 C CG  . GLU A 158 ? 1.4802 1.2291 0.9228 -0.0124 -0.1399 -0.0976 161 GLU A CG  
2517 C CD  . GLU A 158 ? 1.6701 1.3782 1.0970 -0.0329 -0.1546 -0.1102 161 GLU A CD  
2518 O OE1 . GLU A 158 ? 1.8488 1.5166 1.2301 -0.0231 -0.1520 -0.1233 161 GLU A OE1 
2519 O OE2 . GLU A 158 ? 1.5388 1.2564 1.0001 -0.0583 -0.1683 -0.1055 161 GLU A OE2 
2526 N N   . SER A 159 ? 1.3224 1.1719 0.7132 0.0525  -0.0967 -0.0680 162 SER A N   
2527 C CA  . SER A 159 ? 1.3563 1.2269 0.7198 0.0644  -0.0884 -0.0633 162 SER A CA  
2528 C C   . SER A 159 ? 1.3178 1.2434 0.7087 0.0612  -0.0861 -0.0371 162 SER A C   
2529 O O   . SER A 159 ? 1.2087 1.1589 0.5831 0.0706  -0.0760 -0.0283 162 SER A O   
2530 C CB  . SER A 159 ? 1.4274 1.2880 0.7657 0.0941  -0.0651 -0.0714 162 SER A CB  
2531 O OG  . SER A 159 ? 1.3725 1.2626 0.7435 0.1081  -0.0473 -0.0587 162 SER A OG  
2537 N N   . MET A 160 ? 1.0770 1.0196 0.5089 0.0473  -0.0966 -0.0237 163 MET A N   
2538 C CA  . MET A 160 ? 1.0255 1.0146 0.4883 0.0435  -0.0963 0.0030  163 MET A CA  
2539 C C   . MET A 160 ? 0.9728 0.9679 0.4483 0.0219  -0.1202 0.0104  163 MET A C   
2540 O O   . MET A 160 ? 0.9667 0.9372 0.4252 0.0103  -0.1367 -0.0045 163 MET A O   
2541 C CB  . MET A 160 ? 0.9156 0.9231 0.4370 0.0417  -0.0862 0.0145  163 MET A CB  
2542 C CG  . MET A 160 ? 1.2133 1.2098 0.7245 0.0615  -0.0663 0.0038  163 MET A CG  
2543 S SD  . MET A 160 ? 1.1222 1.1611 0.6864 0.0668  -0.0472 0.0251  163 MET A SD  
2544 C CE  . MET A 160 ? 0.9447 1.0354 0.5181 0.0608  -0.0452 0.0559  163 MET A CE  
2554 N N   . ARG A 161 ? 0.8821 0.9132 0.3922 0.0159  -0.1215 0.0353  164 ARG A N   
2555 C CA  . ARG A 161 ? 0.9635 1.0038 0.4902 -0.0005 -0.1435 0.0456  164 ARG A CA  
2556 C C   . ARG A 161 ? 0.6949 0.7166 0.2478 -0.0141 -0.1590 0.0327  164 ARG A C   
2557 O O   . ARG A 161 ? 0.6816 0.6938 0.2622 -0.0132 -0.1510 0.0261  164 ARG A O   
2558 C CB  . ARG A 161 ? 0.9450 1.0155 0.5131 -0.0040 -0.1421 0.0734  164 ARG A CB  
2559 C CG  . ARG A 161 ? 0.9658 1.0549 0.5205 0.0046  -0.1270 0.0900  164 ARG A CG  
2560 C CD  . ARG A 161 ? 1.0719 1.1811 0.6692 0.0009  -0.1187 0.1126  164 ARG A CD  
2561 N NE  . ARG A 161 ? 1.0001 1.1060 0.6340 -0.0098 -0.1354 0.1238  164 ARG A NE  
2562 C CZ  . ARG A 161 ? 0.9112 1.0211 0.5814 -0.0150 -0.1339 0.1397  164 ARG A CZ  
2563 N NH1 . ARG A 161 ? 0.7564 0.8788 0.4360 -0.0142 -0.1177 0.1482  164 ARG A NH1 
2564 N NH2 . ARG A 161 ? 0.9195 1.0200 0.6163 -0.0201 -0.1492 0.1466  164 ARG A NH2 
2578 N N   . PRO A 162 ? 0.7220 0.7439 0.2740 -0.0252 -0.1783 0.0291  165 PRO A N   
2579 C CA  . PRO A 162 ? 0.6978 0.7112 0.2776 -0.0394 -0.1917 0.0188  165 PRO A CA  
2580 C C   . PRO A 162 ? 0.7533 0.7835 0.3872 -0.0427 -0.1933 0.0315  165 PRO A C   
2581 O O   . PRO A 162 ? 0.7011 0.7223 0.3574 -0.0492 -0.1945 0.0217  165 PRO A O   
2582 C CB  . PRO A 162 ? 0.7176 0.7423 0.2947 -0.0480 -0.2087 0.0182  165 PRO A CB  
2583 C CG  . PRO A 162 ? 0.8330 0.8559 0.3639 -0.0380 -0.2036 0.0181  165 PRO A CG  
2584 C CD  . PRO A 162 ? 0.8185 0.8489 0.3439 -0.0236 -0.1854 0.0307  165 PRO A CD  
2592 N N   . GLU A 163 ? 0.6871 0.7400 0.3455 -0.0369 -0.1914 0.0525  166 GLU A N   
2593 C CA  . GLU A 163 ? 0.6925 0.7558 0.4022 -0.0362 -0.1911 0.0621  166 GLU A CA  
2594 C C   . GLU A 163 ? 0.5757 0.6276 0.2999 -0.0296 -0.1709 0.0568  166 GLU A C   
2595 O O   . GLU A 163 ? 0.6281 0.6807 0.3892 -0.0303 -0.1698 0.0557  166 GLU A O   
2596 C CB  . GLU A 163 ? 0.8004 0.8798 0.5287 -0.0306 -0.1945 0.0844  166 GLU A CB  
2597 C CG  . GLU A 163 ? 0.8427 0.9231 0.5543 -0.0251 -0.1811 0.0983  166 GLU A CG  
2598 C CD  . GLU A 163 ? 0.9604 1.0446 0.6338 -0.0229 -0.1809 0.1003  166 GLU A CD  
2599 O OE1 . GLU A 163 ? 0.8824 0.9612 0.5310 -0.0256 -0.1883 0.0852  166 GLU A OE1 
2600 O OE2 . GLU A 163 ? 1.0502 1.1414 0.7178 -0.0195 -0.1737 0.1170  166 GLU A OE2 
2607 N N   . VAL A 164 ? 0.6130 0.6583 0.3085 -0.0216 -0.1547 0.0546  167 VAL A N   
2608 C CA  . VAL A 164 ? 0.5397 0.5777 0.2477 -0.0144 -0.1361 0.0496  167 VAL A CA  
2609 C C   . VAL A 164 ? 0.5504 0.5643 0.2535 -0.0172 -0.1363 0.0277  167 VAL A C   
2610 O O   . VAL A 164 ? 0.5926 0.6021 0.3255 -0.0175 -0.1306 0.0242  167 VAL A O   
2611 C CB  . VAL A 164 ? 0.6796 0.7249 0.3570 -0.0027 -0.1188 0.0545  167 VAL A CB  
2612 C CG1 . VAL A 164 ? 0.7136 0.7523 0.3972 0.0073  -0.0999 0.0463  167 VAL A CG1 
2613 C CG2 . VAL A 164 ? 0.6601 0.7310 0.3475 -0.0043 -0.1183 0.0802  167 VAL A CG2 
2623 N N   . ALA A 165 ? 0.6871 0.6822 0.3497 -0.0212 -0.1448 0.0133  168 ALA A N   
2624 C CA  . ALA A 165 ? 0.6586 0.6230 0.3086 -0.0270 -0.1471 -0.0067 168 ALA A CA  
2625 C C   . ALA A 165 ? 0.6629 0.6358 0.3558 -0.0422 -0.1595 -0.0061 168 ALA A C   
2626 O O   . ALA A 165 ? 0.6921 0.6519 0.4008 -0.0443 -0.1538 -0.0139 168 ALA A O   
2627 C CB  . ALA A 165 ? 0.7907 0.7280 0.3828 -0.0313 -0.1577 -0.0215 168 ALA A CB  
2633 N N   . SER A 166 ? 0.6594 0.6578 0.3718 -0.0513 -0.1761 0.0044  169 SER A N   
2634 C CA  . SER A 166 ? 0.5955 0.6105 0.3478 -0.0632 -0.1875 0.0060  169 SER A CA  
2635 C C   . SER A 166 ? 0.5517 0.5805 0.3506 -0.0541 -0.1762 0.0145  169 SER A C   
2636 O O   . SER A 166 ? 0.5366 0.5676 0.3615 -0.0598 -0.1758 0.0098  169 SER A O   
2637 C CB  . SER A 166 ? 0.7732 0.8171 0.5337 -0.0713 -0.2082 0.0161  169 SER A CB  
2638 O OG  . SER A 166 ? 0.9142 0.9721 0.6754 -0.0593 -0.2066 0.0316  169 SER A OG  
2644 N N   . THR A 167 ? 0.5159 0.5528 0.3236 -0.0415 -0.1674 0.0275  170 THR A N   
2645 C CA  . THR A 167 ? 0.4304 0.4728 0.2757 -0.0340 -0.1577 0.0340  170 THR A CA  
2646 C C   . THR A 167 ? 0.4749 0.4986 0.3184 -0.0310 -0.1410 0.0234  170 THR A C   
2647 O O   . THR A 167 ? 0.4834 0.5091 0.3566 -0.0306 -0.1369 0.0217  170 THR A O   
2648 C CB  . THR A 167 ? 0.5121 0.5621 0.3635 -0.0253 -0.1550 0.0517  170 THR A CB  
2649 O OG1 . THR A 167 ? 0.5699 0.6338 0.4188 -0.0265 -0.1711 0.0621  170 THR A OG1 
2650 C CG2 . THR A 167 ? 0.5218 0.5725 0.4089 -0.0195 -0.1492 0.0577  170 THR A CG2 
2658 N N   . PHE A 168 ? 0.5123 0.5195 0.3202 -0.0263 -0.1310 0.0169  171 PHE A N   
2659 C CA  . PHE A 168 ? 0.5315 0.5207 0.3352 -0.0205 -0.1159 0.0070  171 PHE A CA  
2660 C C   . PHE A 168 ? 0.4991 0.4714 0.3061 -0.0313 -0.1220 -0.0068 171 PHE A C   
2661 O O   . PHE A 168 ? 0.5039 0.4737 0.3347 -0.0307 -0.1149 -0.0089 171 PHE A O   
2662 C CB  . PHE A 168 ? 0.5360 0.5115 0.2959 -0.0094 -0.1048 0.0017  171 PHE A CB  
2663 C CG  . PHE A 168 ? 0.6264 0.5797 0.3758 -0.0002 -0.0907 -0.0100 171 PHE A CG  
2664 C CD1 . PHE A 168 ? 0.5509 0.5170 0.3265 0.0083  -0.0765 -0.0026 171 PHE A CD1 
2665 C CD2 . PHE A 168 ? 0.6968 0.6140 0.4093 -0.0015 -0.0939 -0.0277 171 PHE A CD2 
2666 C CE1 . PHE A 168 ? 0.6680 0.6153 0.4342 0.0181  -0.0646 -0.0123 171 PHE A CE1 
2667 C CE2 . PHE A 168 ? 0.6716 0.5638 0.3720 0.0086  -0.0823 -0.0375 171 PHE A CE2 
2668 C CZ  . PHE A 168 ? 0.6386 0.5480 0.3671 0.0193  -0.0674 -0.0296 171 PHE A CZ  
2678 N N   . LYS A 169 ? 0.5496 0.5111 0.3320 -0.0436 -0.1366 -0.0150 172 LYS A N   
2679 C CA  . LYS A 169 ? 0.5894 0.5339 0.3710 -0.0589 -0.1443 -0.0261 172 LYS A CA  
2680 C C   . LYS A 169 ? 0.5832 0.5550 0.4164 -0.0648 -0.1461 -0.0188 172 LYS A C   
2681 O O   . LYS A 169 ? 0.5579 0.5187 0.4015 -0.0692 -0.1410 -0.0242 172 LYS A O   
2682 C CB  . LYS A 169 ? 0.5724 0.5093 0.3244 -0.0762 -0.1643 -0.0318 172 LYS A CB  
2685 N N   . VAL A 170 ? 0.5181 0.5247 0.3813 -0.0628 -0.1532 -0.0063 173 VAL A N   
2686 C CA  . VAL A 170 ? 0.4757 0.5101 0.3846 -0.0630 -0.1543 0.0004  173 VAL A CA  
2687 C C   . VAL A 170 ? 0.4560 0.4837 0.3834 -0.0502 -0.1374 0.0015  173 VAL A C   
2688 O O   . VAL A 170 ? 0.4117 0.4443 0.3615 -0.0530 -0.1335 -0.0009 173 VAL A O   
2689 C CB  . VAL A 170 ? 0.5533 0.6208 0.4835 -0.0576 -0.1654 0.0134  173 VAL A CB  
2690 C CG1 . VAL A 170 ? 0.4755 0.5697 0.4490 -0.0511 -0.1644 0.0194  173 VAL A CG1 
2691 C CG2 . VAL A 170 ? 0.5730 0.6529 0.4873 -0.0718 -0.1837 0.0133  173 VAL A CG2 
2701 N N   . LEU A 171 ? 0.4218 0.4424 0.3414 -0.0374 -0.1279 0.0068  174 LEU A N   
2702 C CA  . LEU A 171 ? 0.3763 0.3930 0.3135 -0.0278 -0.1139 0.0091  174 LEU A CA  
2703 C C   . LEU A 171 ? 0.4123 0.4071 0.3370 -0.0286 -0.1027 -0.0018 174 LEU A C   
2704 O O   . LEU A 171 ? 0.4126 0.4080 0.3579 -0.0258 -0.0950 -0.0023 174 LEU A O   
2705 C CB  . LEU A 171 ? 0.3905 0.4077 0.3207 -0.0184 -0.1077 0.0197  174 LEU A CB  
2706 C CG  . LEU A 171 ? 0.4586 0.4901 0.4020 -0.0159 -0.1186 0.0330  174 LEU A CG  
2707 C CD1 . LEU A 171 ? 0.4945 0.5242 0.4252 -0.0120 -0.1138 0.0450  174 LEU A CD1 
2708 C CD2 . LEU A 171 ? 0.4143 0.4525 0.3910 -0.0109 -0.1206 0.0363  174 LEU A CD2 
2720 N N   A ARG A 172 ? 0.4448 0.4174 0.3323 -0.0311 -0.1026 -0.0107 175 ARG A N   
2721 N N   B ARG A 172 ? 0.4455 0.4180 0.3332 -0.0312 -0.1026 -0.0108 175 ARG A N   
2722 C CA  A ARG A 172 ? 0.4688 0.4127 0.3367 -0.0299 -0.0940 -0.0217 175 ARG A CA  
2723 C CA  B ARG A 172 ? 0.4687 0.4130 0.3380 -0.0296 -0.0935 -0.0215 175 ARG A CA  
2724 C C   A ARG A 172 ? 0.4385 0.3804 0.3243 -0.0438 -0.0997 -0.0259 175 ARG A C   
2725 C C   B ARG A 172 ? 0.4432 0.3836 0.3274 -0.0440 -0.0997 -0.0264 175 ARG A C   
2726 O O   A ARG A 172 ? 0.4665 0.3991 0.3614 -0.0411 -0.0905 -0.0283 175 ARG A O   
2727 O O   B ARG A 172 ? 0.4687 0.3969 0.3587 -0.0418 -0.0908 -0.0296 175 ARG A O   
2728 C CB  A ARG A 172 ? 0.5715 0.4858 0.3885 -0.0296 -0.0971 -0.0319 175 ARG A CB  
2729 C CB  B ARG A 172 ? 0.5764 0.4914 0.3953 -0.0268 -0.0942 -0.0312 175 ARG A CB  
2730 C CG  A ARG A 172 ? 0.6307 0.5026 0.4159 -0.0286 -0.0926 -0.0454 175 ARG A CG  
2731 C CG  B ARG A 172 ? 0.6173 0.4949 0.4074 -0.0194 -0.0847 -0.0426 175 ARG A CG  
2732 C CD  A ARG A 172 ? 0.6541 0.4893 0.3865 -0.0352 -0.1036 -0.0577 175 ARG A CD  
2733 C CD  B ARG A 172 ? 0.6969 0.5376 0.4547 -0.0356 -0.0981 -0.0551 175 ARG A CD  
2734 N NE  A ARG A 172 ? 0.7179 0.5537 0.4546 -0.0613 -0.1233 -0.0593 175 ARG A NE  
2735 N NE  B ARG A 172 ? 0.6397 0.4614 0.3521 -0.0354 -0.1062 -0.0621 175 ARG A NE  
2736 C CZ  A ARG A 172 ? 0.8179 0.6256 0.5119 -0.0735 -0.1379 -0.0685 175 ARG A CZ  
2737 C CZ  B ARG A 172 ? 0.8063 0.6291 0.5099 -0.0550 -0.1248 -0.0636 175 ARG A CZ  
2738 N NH1 A ARG A 172 ? 0.8570 0.6282 0.4974 -0.0594 -0.1341 -0.0790 175 ARG A NH1 
2739 N NH1 B ARG A 172 ? 0.7305 0.5794 0.4709 -0.0753 -0.1366 -0.0571 175 ARG A NH1 
2740 N NH2 A ARG A 172 ? 0.7990 0.6170 0.5026 -0.1000 -0.1570 -0.0668 175 ARG A NH2 
2741 N NH2 B ARG A 172 ? 0.8171 0.6181 0.4732 -0.0533 -0.1317 -0.0713 175 ARG A NH2 
2768 N N   . ASN A 173 ? 0.4996 0.4534 0.3899 -0.0598 -0.1152 -0.0257 176 ASN A N   
2769 C CA  . ASN A 173 ? 0.4579 0.4174 0.3649 -0.0765 -0.1216 -0.0271 176 ASN A CA  
2770 C C   . ASN A 173 ? 0.4701 0.4604 0.4221 -0.0701 -0.1148 -0.0194 176 ASN A C   
2771 O O   . ASN A 173 ? 0.4701 0.4581 0.4331 -0.0767 -0.1109 -0.0210 176 ASN A O   
2772 C CB  . ASN A 173 ? 0.4670 0.4450 0.3730 -0.0956 -0.1410 -0.0251 176 ASN A CB  
2773 C CG  . ASN A 173 ? 0.6300 0.5693 0.4850 -0.1071 -0.1507 -0.0353 176 ASN A CG  
2774 O OD1 . ASN A 173 ? 0.7197 0.6162 0.5389 -0.0988 -0.1422 -0.0448 176 ASN A OD1 
2775 N ND2 . ASN A 173 ? 0.6933 0.6476 0.5419 -0.1240 -0.1691 -0.0334 176 ASN A ND2 
2782 N N   . VAL A 174 ? 0.3754 0.3925 0.3506 -0.0579 -0.1147 -0.0107 177 VAL A N   
2783 C CA  . VAL A 174 ? 0.3194 0.3576 0.3298 -0.0477 -0.1081 -0.0051 177 VAL A CA  
2784 C C   . VAL A 174 ? 0.3961 0.4132 0.4036 -0.0401 -0.0933 -0.0086 177 VAL A C   
2785 O O   . VAL A 174 ? 0.3662 0.3901 0.3924 -0.0403 -0.0879 -0.0089 177 VAL A O   
2786 C CB  . VAL A 174 ? 0.3219 0.3771 0.3459 -0.0342 -0.1117 0.0039  177 VAL A CB  
2787 C CG1 . VAL A 174 ? 0.4120 0.4733 0.4604 -0.0211 -0.1040 0.0073  177 VAL A CG1 
2788 C CG2 . VAL A 174 ? 0.3706 0.4546 0.4040 -0.0399 -0.1268 0.0085  177 VAL A CG2 
2798 N N   . THR A 175 ? 0.3601 0.3557 0.3441 -0.0327 -0.0863 -0.0101 178 THR A N   
2799 C CA  . THR A 175 ? 0.4006 0.3833 0.3835 -0.0233 -0.0725 -0.0110 178 THR A CA  
2800 C C   . THR A 175 ? 0.3996 0.3617 0.3719 -0.0292 -0.0681 -0.0188 178 THR A C   
2801 O O   . THR A 175 ? 0.4053 0.3686 0.3925 -0.0256 -0.0602 -0.0181 178 THR A O   
2802 C CB  . THR A 175 ? 0.4069 0.3808 0.3673 -0.0135 -0.0662 -0.0085 178 THR A CB  
2803 O OG1 . THR A 175 ? 0.4099 0.4018 0.3824 -0.0102 -0.0705 0.0019  178 THR A OG1 
2804 C CG2 . THR A 175 ? 0.4081 0.3746 0.3665 -0.0034 -0.0521 -0.0083 178 THR A CG2 
2812 N N   . VAL A 176 ? 0.4193 0.3592 0.3632 -0.0393 -0.0746 -0.0260 179 VAL A N   
2813 C CA  . VAL A 176 ? 0.4072 0.3166 0.3328 -0.0452 -0.0717 -0.0329 179 VAL A CA  
2814 C C   . VAL A 176 ? 0.4166 0.3431 0.3701 -0.0584 -0.0745 -0.0296 179 VAL A C   
2815 O O   . VAL A 176 ? 0.4546 0.3691 0.4100 -0.0575 -0.0670 -0.0303 179 VAL A O   
2816 C CB  . VAL A 176 ? 0.5915 0.4647 0.4733 -0.0545 -0.0808 -0.0419 179 VAL A CB  
2817 C CG1 . VAL A 176 ? 0.7242 0.5611 0.5866 -0.0663 -0.0825 -0.0475 179 VAL A CG1 
2818 C CG2 . VAL A 176 ? 0.5968 0.4519 0.4464 -0.0358 -0.0736 -0.0459 179 VAL A CG2 
2828 N N   . VAL A 177 ? 0.4163 0.3749 0.3917 -0.0699 -0.0852 -0.0249 180 VAL A N   
2829 C CA  . VAL A 177 ? 0.3792 0.3659 0.3841 -0.0806 -0.0869 -0.0198 180 VAL A CA  
2830 C C   . VAL A 177 ? 0.3740 0.3798 0.4069 -0.0647 -0.0753 -0.0160 180 VAL A C   
2831 O O   . VAL A 177 ? 0.3644 0.3717 0.4065 -0.0681 -0.0693 -0.0150 180 VAL A O   
2832 C CB  . VAL A 177 ? 0.4056 0.4314 0.4289 -0.0916 -0.1005 -0.0142 180 VAL A CB  
2833 C CG1 . VAL A 177 ? 0.4746 0.5429 0.5336 -0.0974 -0.0997 -0.0067 180 VAL A CG1 
2834 C CG2 . VAL A 177 ? 0.5056 0.5111 0.4994 -0.1128 -0.1140 -0.0179 180 VAL A CG2 
2844 N N   . LEU A 178 ? 0.2838 0.3037 0.3292 -0.0488 -0.0734 -0.0131 181 LEU A N   
2845 C CA  . LEU A 178 ? 0.2889 0.3221 0.3565 -0.0352 -0.0651 -0.0102 181 LEU A CA  
2846 C C   . LEU A 178 ? 0.3282 0.3364 0.3847 -0.0288 -0.0535 -0.0127 181 LEU A C   
2847 O O   . LEU A 178 ? 0.2895 0.3039 0.3592 -0.0257 -0.0470 -0.0120 181 LEU A O   
2848 C CB  . LEU A 178 ? 0.2785 0.3222 0.3549 -0.0217 -0.0685 -0.0059 181 LEU A CB  
2849 C CG  . LEU A 178 ? 0.3766 0.4499 0.4683 -0.0215 -0.0794 -0.0018 181 LEU A CG  
2850 C CD1 . LEU A 178 ? 0.3571 0.4286 0.4497 -0.0073 -0.0835 0.0030  181 LEU A CD1 
2851 C CD2 . LEU A 178 ? 0.3260 0.4304 0.4423 -0.0201 -0.0785 0.0000  181 LEU A CD2 
2863 N N   . TRP A 179 ? 0.2818 0.2658 0.3142 -0.0245 -0.0503 -0.0150 182 TRP A N   
2864 C CA  . TRP A 179 ? 0.3172 0.2864 0.3427 -0.0151 -0.0390 -0.0152 182 TRP A CA  
2865 C C   . TRP A 179 ? 0.3506 0.3029 0.3680 -0.0216 -0.0353 -0.0187 182 TRP A C   
2866 O O   . TRP A 179 ? 0.3265 0.2785 0.3510 -0.0159 -0.0275 -0.0170 182 TRP A O   
2867 C CB  . TRP A 179 ? 0.3215 0.2759 0.3230 -0.0064 -0.0350 -0.0156 182 TRP A CB  
2868 C CG  . TRP A 179 ? 0.2981 0.2700 0.3083 -0.0004 -0.0365 -0.0085 182 TRP A CG  
2869 C CD1 . TRP A 179 ? 0.3068 0.2942 0.3319 -0.0035 -0.0453 -0.0045 182 TRP A CD1 
2870 C CD2 . TRP A 179 ? 0.3118 0.2871 0.3137 0.0092  -0.0294 -0.0027 182 TRP A CD2 
2871 N NE1 . TRP A 179 ? 0.3234 0.3172 0.3475 0.0017  -0.0452 0.0036  182 TRP A NE1 
2872 C CE2 . TRP A 179 ? 0.3044 0.2944 0.3159 0.0077  -0.0353 0.0053  182 TRP A CE2 
2873 C CE3 . TRP A 179 ? 0.3560 0.3257 0.3435 0.0194  -0.0189 -0.0024 182 TRP A CE3 
2874 C CZ2 . TRP A 179 ? 0.3420 0.3435 0.3495 0.0119  -0.0313 0.0153  182 TRP A CZ2 
2875 C CZ3 . TRP A 179 ? 0.3584 0.3466 0.3451 0.0265  -0.0137 0.0073  182 TRP A CZ3 
2876 C CH2 . TRP A 179 ? 0.2816 0.2859 0.2785 0.0205  -0.0202 0.0164  182 TRP A CH2 
2887 N N   . SER A 180 ? 0.3639 0.3014 0.3655 -0.0358 -0.0426 -0.0223 183 SER A N   
2888 C CA  . SER A 180 ? 0.3440 0.2580 0.3324 -0.0448 -0.0409 -0.0239 183 SER A CA  
2889 C C   . SER A 180 ? 0.3623 0.3020 0.3786 -0.0508 -0.0384 -0.0187 183 SER A C   
2890 O O   . SER A 180 ? 0.3743 0.2972 0.3827 -0.0551 -0.0344 -0.0177 183 SER A O   
2891 C CB  . SER A 180 ? 0.4054 0.2965 0.3695 -0.0643 -0.0526 -0.0276 183 SER A CB  
2892 O OG  . SER A 180 ? 0.5006 0.3602 0.4302 -0.0565 -0.0541 -0.0344 183 SER A OG  
2898 N N   . ALA A 181 ? 0.3081 0.2871 0.3540 -0.0501 -0.0410 -0.0150 184 ALA A N   
2899 C CA  . ALA A 181 ? 0.3147 0.3226 0.3855 -0.0515 -0.0374 -0.0105 184 ALA A CA  
2900 C C   . ALA A 181 ? 0.2856 0.2913 0.3623 -0.0362 -0.0271 -0.0103 184 ALA A C   
2901 O O   . ALA A 181 ? 0.2976 0.3127 0.3826 -0.0384 -0.0222 -0.0077 184 ALA A O   
2902 C CB  . ALA A 181 ? 0.3028 0.3528 0.3997 -0.0494 -0.0430 -0.0073 184 ALA A CB  
2908 N N   . TYR A 182 ? 0.2513 0.2465 0.3227 -0.0227 -0.0243 -0.0119 185 TYR A N   
2909 C CA  . TYR A 182 ? 0.2422 0.2393 0.3202 -0.0112 -0.0170 -0.0106 185 TYR A CA  
2910 C C   . TYR A 182 ? 0.2616 0.2422 0.3288 -0.0123 -0.0099 -0.0097 185 TYR A C   
2911 O O   . TYR A 182 ? 0.2832 0.2752 0.3610 -0.0092 -0.0056 -0.0078 185 TYR A O   
2912 C CB  . TYR A 182 ? 0.2791 0.2701 0.3517 -0.0011 -0.0167 -0.0096 185 TYR A CB  
2913 C CG  . TYR A 182 ? 0.2427 0.2476 0.3267 0.0023  -0.0235 -0.0083 185 TYR A CG  
2914 C CD1 . TYR A 182 ? 0.2555 0.2635 0.3371 -0.0015 -0.0309 -0.0086 185 TYR A CD1 
2915 C CD2 . TYR A 182 ? 0.2396 0.2502 0.3332 0.0094  -0.0241 -0.0066 185 TYR A CD2 
2916 C CE1 . TYR A 182 ? 0.2828 0.3005 0.3729 0.0033  -0.0378 -0.0063 185 TYR A CE1 
2917 C CE2 . TYR A 182 ? 0.2391 0.2532 0.3376 0.0136  -0.0318 -0.0052 185 TYR A CE2 
2918 C CZ  . TYR A 182 ? 0.2352 0.2529 0.3323 0.0113  -0.0383 -0.0044 185 TYR A CZ  
2919 O OH  . TYR A 182 ? 0.2390 0.2571 0.3386 0.0170  -0.0467 -0.0019 185 TYR A OH  
2929 N N   . PRO A 183 ? 0.2917 0.2432 0.3350 -0.0138 -0.0087 -0.0111 186 PRO A N   
2930 C CA  . PRO A 183 ? 0.3068 0.2384 0.3371 -0.0126 -0.0027 -0.0092 186 PRO A CA  
2931 C C   . PRO A 183 ? 0.3451 0.2823 0.3814 -0.0272 -0.0040 -0.0061 186 PRO A C   
2932 O O   . PRO A 183 ? 0.3206 0.2543 0.3557 -0.0256 0.0014  -0.0025 186 PRO A O   
2933 C CB  . PRO A 183 ? 0.3786 0.2719 0.3761 -0.0103 -0.0037 -0.0127 186 PRO A CB  
2934 C CG  . PRO A 183 ? 0.3909 0.2849 0.3838 -0.0156 -0.0111 -0.0169 186 PRO A CG  
2935 C CD  . PRO A 183 ? 0.2793 0.2107 0.3013 -0.0118 -0.0118 -0.0146 186 PRO A CD  
2943 N N   . VAL A 184 ? 0.3103 0.2609 0.3539 -0.0426 -0.0112 -0.0059 187 VAL A N   
2944 C CA  . VAL A 184 ? 0.3122 0.2789 0.3650 -0.0587 -0.0119 0.0002  187 VAL A CA  
2945 C C   . VAL A 184 ? 0.3163 0.3226 0.3957 -0.0495 -0.0057 0.0027  187 VAL A C   
2946 O O   . VAL A 184 ? 0.2978 0.3118 0.3799 -0.0534 -0.0006 0.0079  187 VAL A O   
2947 C CB  . VAL A 184 ? 0.3519 0.3309 0.4075 -0.0789 -0.0222 0.0019  187 VAL A CB  
2948 C CG1 . VAL A 184 ? 0.3658 0.3710 0.4336 -0.0985 -0.0228 0.0115  187 VAL A CG1 
2949 C CG2 . VAL A 184 ? 0.3714 0.3037 0.3933 -0.0882 -0.0302 -0.0026 187 VAL A CG2 
2959 N N   . VAL A 185 ? 0.2627 0.2921 0.3586 -0.0374 -0.0067 -0.0006 188 VAL A N   
2960 C CA  . VAL A 185 ? 0.2405 0.2997 0.3547 -0.0254 -0.0020 -0.0004 188 VAL A CA  
2961 C C   . VAL A 185 ? 0.2735 0.3180 0.3800 -0.0162 0.0048  -0.0006 188 VAL A C   
2962 O O   . VAL A 185 ? 0.2925 0.3536 0.4049 -0.0133 0.0100  0.0015  188 VAL A O   
2963 C CB  . VAL A 185 ? 0.2617 0.3334 0.3863 -0.0125 -0.0066 -0.0047 188 VAL A CB  
2964 C CG1 . VAL A 185 ? 0.2926 0.3821 0.4268 0.0037  -0.0030 -0.0069 188 VAL A CG1 
2965 C CG2 . VAL A 185 ? 0.2686 0.3646 0.4043 -0.0201 -0.0137 -0.0028 188 VAL A CG2 
2975 N N   . TRP A 186 ? 0.2542 0.2711 0.3468 -0.0111 0.0051  -0.0023 189 TRP A N   
2976 C CA  . TRP A 186 ? 0.2561 0.2639 0.3426 -0.0021 0.0105  -0.0008 189 TRP A CA  
2977 C C   . TRP A 186 ? 0.2828 0.2816 0.3599 -0.0090 0.0152  0.0044  189 TRP A C   
2978 O O   . TRP A 186 ? 0.3166 0.3243 0.3958 -0.0048 0.0197  0.0069  189 TRP A O   
2979 C CB  . TRP A 186 ? 0.2702 0.2580 0.3448 0.0046  0.0099  -0.0013 189 TRP A CB  
2980 C CG  . TRP A 186 ? 0.2973 0.2847 0.3694 0.0151  0.0135  0.0017  189 TRP A CG  
2981 C CD1 . TRP A 186 ? 0.3523 0.3499 0.4311 0.0205  0.0106  0.0021  189 TRP A CD1 
2982 C CD2 . TRP A 186 ? 0.2670 0.2439 0.3280 0.0198  0.0189  0.0064  189 TRP A CD2 
2983 N NE1 . TRP A 186 ? 0.2912 0.2907 0.3662 0.0265  0.0136  0.0072  189 TRP A NE1 
2984 C CE2 . TRP A 186 ? 0.3171 0.3053 0.3818 0.0284  0.0191  0.0097  189 TRP A CE2 
2985 C CE3 . TRP A 186 ? 0.2978 0.2561 0.3448 0.0171  0.0223  0.0094  189 TRP A CE3 
2986 C CZ2 . TRP A 186 ? 0.3720 0.3594 0.4297 0.0361  0.0231  0.0157  189 TRP A CZ2 
2987 C CZ3 . TRP A 186 ? 0.3712 0.3216 0.4080 0.0266  0.0266  0.0149  189 TRP A CZ3 
2988 C CH2 . TRP A 186 ? 0.3854 0.3539 0.4294 0.0370  0.0273  0.0179  189 TRP A CH2 
2999 N N   . LEU A 187 ? 0.3003 0.2789 0.3641 -0.0209 0.0130  0.0064  190 LEU A N   
3000 C CA  . LEU A 187 ? 0.3037 0.2635 0.3525 -0.0294 0.0155  0.0127  190 LEU A CA  
3001 C C   . LEU A 187 ? 0.3808 0.3718 0.4440 -0.0396 0.0180  0.0185  190 LEU A C   
3002 O O   . LEU A 187 ? 0.3832 0.3723 0.4408 -0.0392 0.0229  0.0243  190 LEU A O   
3003 C CB  . LEU A 187 ? 0.3369 0.2599 0.3625 -0.0418 0.0095  0.0126  190 LEU A CB  
3004 C CG  . LEU A 187 ? 0.4812 0.3695 0.4823 -0.0517 0.0092  0.0193  190 LEU A CG  
3005 C CD1 . LEU A 187 ? 0.5707 0.4354 0.5561 -0.0307 0.0153  0.0199  190 LEU A CD1 
3006 C CD2 . LEU A 187 ? 0.5265 0.3749 0.5013 -0.0677 -0.0004 0.0174  190 LEU A CD2 
3018 N N   . ILE A 188 ? 0.3171 0.3422 0.3994 -0.0464 0.0153  0.0180  191 ILE A N   
3019 C CA  . ILE A 188 ? 0.3322 0.3959 0.4288 -0.0544 0.0191  0.0251  191 ILE A CA  
3020 C C   . ILE A 188 ? 0.3105 0.4053 0.4213 -0.0355 0.0250  0.0210  191 ILE A C   
3021 O O   . ILE A 188 ? 0.3449 0.4721 0.4637 -0.0368 0.0305  0.0265  191 ILE A O   
3022 C CB  . ILE A 188 ? 0.3377 0.4283 0.4466 -0.0720 0.0132  0.0294  191 ILE A CB  
3023 C CG1 . ILE A 188 ? 0.4147 0.5282 0.5404 -0.0589 0.0099  0.0217  191 ILE A CG1 
3024 C CG2 . ILE A 188 ? 0.5197 0.5697 0.6070 -0.0924 0.0051  0.0322  191 ILE A CG2 
3025 C CD1 . ILE A 188 ? 0.5953 0.7337 0.7320 -0.0757 0.0018  0.0261  191 ILE A CD1 
3037 N N   . GLY A 189 ? 0.3916 0.3259 0.3802 -0.0389 0.0148  0.0626  192 GLY A N   
3038 C CA  . GLY A 189 ? 0.3800 0.3502 0.3831 -0.0354 0.0154  0.0590  192 GLY A CA  
3039 C C   . GLY A 189 ? 0.4077 0.3837 0.3982 -0.0229 0.0170  0.0655  192 GLY A C   
3040 O O   . GLY A 189 ? 0.4257 0.3804 0.3968 -0.0171 0.0192  0.0749  192 GLY A O   
3044 N N   A SER A 190 ? 0.3782 0.3818 0.3781 -0.0182 0.0151  0.0602  193 SER A N   
3045 N N   B SER A 190 ? 0.3803 0.3842 0.3801 -0.0183 0.0152  0.0604  193 SER A N   
3046 C CA  A SER A 190 ? 0.4044 0.4206 0.3938 -0.0094 0.0158  0.0651  193 SER A CA  
3047 C CA  B SER A 190 ? 0.4052 0.4206 0.3939 -0.0092 0.0160  0.0656  193 SER A CA  
3048 C C   A SER A 190 ? 0.3936 0.4034 0.3713 0.0050  0.0119  0.0700  193 SER A C   
3049 C C   B SER A 190 ? 0.3966 0.4062 0.3741 0.0052  0.0119  0.0701  193 SER A C   
3050 O O   A SER A 190 ? 0.4900 0.5030 0.4537 0.0134  0.0131  0.0782  193 SER A O   
3051 O O   B SER A 190 ? 0.4874 0.5014 0.4515 0.0138  0.0128  0.0779  193 SER A O   
3052 C CB  A SER A 190 ? 0.3983 0.4426 0.3989 -0.0102 0.0135  0.0563  193 SER A CB  
3053 C CB  B SER A 190 ? 0.4028 0.4465 0.4017 -0.0099 0.0140  0.0574  193 SER A CB  
3054 O OG  A SER A 190 ? 0.4941 0.5443 0.5058 -0.0086 0.0073  0.0481  193 SER A OG  
3055 O OG  B SER A 190 ? 0.4005 0.4529 0.4041 -0.0183 0.0198  0.0559  193 SER A OG  
3066 N N   . GLU A 191 ? 0.3818 0.3837 0.3637 0.0094  0.0078  0.0661  194 GLU A N   
3067 C CA  . GLU A 191 ? 0.4010 0.4002 0.3721 0.0256  0.0051  0.0712  194 GLU A CA  
3068 C C   . GLU A 191 ? 0.4696 0.4348 0.4190 0.0331  0.0087  0.0806  194 GLU A C   
3069 O O   . GLU A 191 ? 0.4293 0.3923 0.3648 0.0503  0.0081  0.0878  194 GLU A O   
3070 C CB  . GLU A 191 ? 0.3876 0.3896 0.3686 0.0286  0.0006  0.0642  194 GLU A CB  
3071 C CG  . GLU A 191 ? 0.4408 0.4730 0.4391 0.0239  -0.0038 0.0568  194 GLU A CG  
3072 C CD  . GLU A 191 ? 0.5989 0.6300 0.6110 0.0096  -0.0036 0.0482  194 GLU A CD  
3073 O OE1 . GLU A 191 ? 0.4612 0.4734 0.4717 0.0025  -0.0001 0.0483  194 GLU A OE1 
3074 O OE2 . GLU A 191 ? 0.5170 0.5660 0.5407 0.0055  -0.0069 0.0420  194 GLU A OE2 
3081 N N   . GLY A 192 ? 0.4182 0.3560 0.3635 0.0206  0.0123  0.0810  195 GLY A N   
3082 C CA  . GLY A 192 ? 0.4269 0.3226 0.3474 0.0251  0.0155  0.0897  195 GLY A CA  
3083 C C   . GLY A 192 ? 0.5138 0.3971 0.4228 0.0160  0.0215  0.0995  195 GLY A C   
3084 O O   . GLY A 192 ? 0.5073 0.4060 0.4100 0.0230  0.0235  0.1069  195 GLY A O   
3088 N N   . ALA A 193 ? 0.4652 0.3206 0.3700 -0.0009 0.0243  0.1003  196 ALA A N   
3089 C CA  . ALA A 193 ? 0.5206 0.3594 0.4119 -0.0117 0.0307  0.1115  196 ALA A CA  
3090 C C   . ALA A 193 ? 0.5332 0.4101 0.4430 -0.0247 0.0348  0.1110  196 ALA A C   
3091 O O   . ALA A 193 ? 0.5986 0.4708 0.4972 -0.0310 0.0411  0.1219  196 ALA A O   
3092 C CB  . ALA A 193 ? 0.6240 0.4197 0.5039 -0.0280 0.0315  0.1126  196 ALA A CB  
3098 N N   . GLY A 194 ? 0.5032 0.4158 0.4382 -0.0275 0.0318  0.0993  197 GLY A N   
3099 C CA  . GLY A 194 ? 0.4727 0.4208 0.4209 -0.0338 0.0358  0.0981  197 GLY A CA  
3100 C C   . GLY A 194 ? 0.5334 0.4863 0.4912 -0.0540 0.0415  0.0998  197 GLY A C   
3101 O O   . GLY A 194 ? 0.5472 0.5227 0.5075 -0.0581 0.0477  0.1036  197 GLY A O   
3105 N N   . ILE A 195 ? 0.4248 0.3602 0.3882 -0.0668 0.0394  0.0968  198 ILE A N   
3106 C CA  . ILE A 195 ? 0.4989 0.4425 0.4730 -0.0887 0.0442  0.0996  198 ILE A CA  
3107 C C   . ILE A 195 ? 0.5219 0.5080 0.5247 -0.0921 0.0435  0.0888  198 ILE A C   
3108 O O   . ILE A 195 ? 0.5239 0.5363 0.5385 -0.1034 0.0496  0.0916  198 ILE A O   
3109 C CB  . ILE A 195 ? 0.5548 0.4603 0.5203 -0.1027 0.0409  0.1007  198 ILE A CB  
3110 C CG1 . ILE A 195 ? 0.7570 0.6141 0.6892 -0.0975 0.0425  0.1123  198 ILE A CG1 
3111 C CG2 . ILE A 195 ? 0.7419 0.6621 0.7211 -0.1283 0.0447  0.1038  198 ILE A CG2 
3112 C CD1 . ILE A 195 ? 0.8433 0.6539 0.7605 -0.1046 0.0372  0.1100  198 ILE A CD1 
3124 N N   . VAL A 196 ? 0.3931 0.3853 0.4067 -0.0827 0.0362  0.0771  199 VAL A N   
3125 C CA  . VAL A 196 ? 0.4261 0.4531 0.4635 -0.0819 0.0346  0.0667  199 VAL A CA  
3126 C C   . VAL A 196 ? 0.4496 0.4949 0.4861 -0.0659 0.0348  0.0623  199 VAL A C   
3127 O O   . VAL A 196 ? 0.4300 0.4622 0.4557 -0.0543 0.0304  0.0614  199 VAL A O   
3128 C CB  . VAL A 196 ? 0.5451 0.5640 0.5918 -0.0822 0.0261  0.0574  199 VAL A CB  
3129 C CG1 . VAL A 196 ? 0.5010 0.5516 0.5696 -0.0789 0.0237  0.0474  199 VAL A CG1 
3130 C CG2 . VAL A 196 ? 0.5359 0.5352 0.5809 -0.1010 0.0249  0.0608  199 VAL A CG2 
3140 N N   . PRO A 197 ? 0.3437 0.4195 0.3908 -0.0646 0.0392  0.0588  200 PRO A N   
3141 C CA  . PRO A 197 ? 0.3830 0.4711 0.4250 -0.0509 0.0385  0.0533  200 PRO A CA  
3142 C C   . PRO A 197 ? 0.3203 0.4072 0.3693 -0.0427 0.0300  0.0422  200 PRO A C   
3143 O O   . PRO A 197 ? 0.3378 0.4239 0.3998 -0.0458 0.0261  0.0372  200 PRO A O   
3144 C CB  . PRO A 197 ? 0.4292 0.5467 0.4789 -0.0516 0.0461  0.0517  200 PRO A CB  
3145 C CG  . PRO A 197 ? 0.5108 0.6388 0.5759 -0.0640 0.0491  0.0543  200 PRO A CG  
3146 C CD  . PRO A 197 ? 0.4208 0.5216 0.4823 -0.0755 0.0456  0.0607  200 PRO A CD  
3154 N N   . LEU A 198 ? 0.3595 0.4490 0.3993 -0.0331 0.0273  0.0385  201 LEU A N   
3155 C CA  . LEU A 198 ? 0.3122 0.3986 0.3560 -0.0274 0.0192  0.0300  201 LEU A CA  
3156 C C   . LEU A 198 ? 0.3368 0.4325 0.3953 -0.0275 0.0179  0.0208  201 LEU A C   
3157 O O   . LEU A 198 ? 0.3719 0.4610 0.4375 -0.0269 0.0119  0.0166  201 LEU A O   
3158 C CB  . LEU A 198 ? 0.3146 0.4054 0.3456 -0.0206 0.0163  0.0278  201 LEU A CB  
3159 C CG  . LEU A 198 ? 0.3114 0.4007 0.3443 -0.0177 0.0078  0.0204  201 LEU A CG  
3160 C CD1 . LEU A 198 ? 0.3925 0.4713 0.4303 -0.0174 0.0029  0.0235  201 LEU A CD1 
3161 C CD2 . LEU A 198 ? 0.4204 0.5171 0.4395 -0.0145 0.0046  0.0191  201 LEU A CD2 
3173 N N   A ASN A 199 ? 0.3324 0.4446 0.3947 -0.0266 0.0239  0.0183  202 ASN A N   
3174 N N   B ASN A 199 ? 0.3331 0.4451 0.3951 -0.0265 0.0239  0.0184  202 ASN A N   
3175 C CA  A ASN A 199 ? 0.2928 0.4137 0.3675 -0.0230 0.0226  0.0101  202 ASN A CA  
3176 C CA  B ASN A 199 ? 0.2952 0.4171 0.3698 -0.0232 0.0232  0.0105  202 ASN A CA  
3177 C C   A ASN A 199 ? 0.3565 0.4790 0.4473 -0.0296 0.0206  0.0119  202 ASN A C   
3178 C C   B ASN A 199 ? 0.3550 0.4765 0.4452 -0.0297 0.0205  0.0121  202 ASN A C   
3179 O O   A ASN A 199 ? 0.3494 0.4696 0.4480 -0.0263 0.0152  0.0062  202 ASN A O   
3180 O O   B ASN A 199 ? 0.3475 0.4648 0.4443 -0.0265 0.0146  0.0065  202 ASN A O   
3181 C CB  A ASN A 199 ? 0.3592 0.4995 0.4330 -0.0171 0.0301  0.0070  202 ASN A CB  
3182 C CB  B ASN A 199 ? 0.3686 0.5119 0.4441 -0.0192 0.0317  0.0094  202 ASN A CB  
3183 C CG  A ASN A 199 ? 0.3607 0.5201 0.4422 -0.0241 0.0388  0.0153  202 ASN A CG  
3184 C CG  B ASN A 199 ? 0.2758 0.4296 0.3613 -0.0109 0.0314  0.0011  202 ASN A CG  
3185 O OD1 A ASN A 199 ? 0.4816 0.6366 0.5555 -0.0312 0.0420  0.0242  202 ASN A OD1 
3186 O OD1 B ASN A 199 ? 0.3641 0.5072 0.4546 -0.0088 0.0244  -0.0036 202 ASN A OD1 
3187 N ND2 A ASN A 199 ? 0.5557 0.7376 0.6522 -0.0221 0.0426  0.0133  202 ASN A ND2 
3188 N ND2 B ASN A 199 ? 0.5656 0.7415 0.6530 -0.0047 0.0395  0.0000  202 ASN A ND2 
3201 N N   . ILE A 200 ? 0.3085 0.4330 0.4027 -0.0399 0.0243  0.0199  203 ILE A N   
3202 C CA  . ILE A 200 ? 0.2556 0.3791 0.3623 -0.0485 0.0207  0.0207  203 ILE A CA  
3203 C C   . ILE A 200 ? 0.2656 0.3634 0.3658 -0.0483 0.0129  0.0197  203 ILE A C   
3204 O O   . ILE A 200 ? 0.3068 0.4025 0.4149 -0.0490 0.0073  0.0157  203 ILE A O   
3205 C CB  . ILE A 200 ? 0.3558 0.4857 0.4651 -0.0626 0.0265  0.0296  203 ILE A CB  
3206 C CG1 . ILE A 200 ? 0.3654 0.5283 0.4832 -0.0615 0.0352  0.0310  203 ILE A CG1 
3207 C CG2 . ILE A 200 ? 0.3935 0.5185 0.5123 -0.0747 0.0213  0.0299  203 ILE A CG2 
3208 C CD1 . ILE A 200 ? 0.3903 0.5801 0.5259 -0.0543 0.0343  0.0238  203 ILE A CD1 
3220 N N   . GLU A 201 ? 0.2997 0.3797 0.3846 -0.0464 0.0129  0.0241  204 GLU A N   
3221 C CA  . GLU A 201 ? 0.3040 0.3644 0.3823 -0.0425 0.0065  0.0232  204 GLU A CA  
3222 C C   . GLU A 201 ? 0.3069 0.3723 0.3913 -0.0354 0.0009  0.0155  204 GLU A C   
3223 O O   . GLU A 201 ? 0.2861 0.3430 0.3726 -0.0347 -0.0043 0.0133  204 GLU A O   
3224 C CB  . GLU A 201 ? 0.3520 0.4013 0.4137 -0.0369 0.0077  0.0289  204 GLU A CB  
3225 C CG  . GLU A 201 ? 0.4227 0.4563 0.4772 -0.0303 0.0022  0.0291  204 GLU A CG  
3226 C CD  . GLU A 201 ? 0.4925 0.5224 0.5325 -0.0217 0.0026  0.0350  204 GLU A CD  
3227 O OE1 . GLU A 201 ? 0.3818 0.4138 0.4139 -0.0220 0.0070  0.0404  204 GLU A OE1 
3228 O OE2 . GLU A 201 ? 0.5743 0.6021 0.6109 -0.0140 -0.0015 0.0349  204 GLU A OE2 
3235 N N   . THR A 202 ? 0.2297 0.3059 0.3139 -0.0300 0.0018  0.0116  205 THR A N   
3236 C CA  . THR A 202 ? 0.2734 0.3492 0.3601 -0.0248 -0.0035 0.0052  205 THR A CA  
3237 C C   . THR A 202 ? 0.2733 0.3546 0.3729 -0.0250 -0.0055 0.0013  205 THR A C   
3238 O O   . THR A 202 ? 0.2550 0.3301 0.3567 -0.0230 -0.0109 -0.0011 205 THR A O   
3239 C CB  . THR A 202 ? 0.3105 0.3914 0.3900 -0.0204 -0.0021 0.0010  205 THR A CB  
3240 O OG1 . THR A 202 ? 0.2842 0.3635 0.3518 -0.0205 -0.0015 0.0050  205 THR A OG1 
3241 C CG2 . THR A 202 ? 0.2447 0.3193 0.3227 -0.0171 -0.0078 -0.0054 205 THR A CG2 
3249 N N   . LEU A 203 ? 0.2625 0.3588 0.3710 -0.0270 -0.0010 0.0013  206 LEU A N   
3250 C CA  . LEU A 203 ? 0.2491 0.3560 0.3714 -0.0274 -0.0035 -0.0010 206 LEU A CA  
3251 C C   . LEU A 203 ? 0.2432 0.3398 0.3672 -0.0342 -0.0088 0.0007  206 LEU A C   
3252 O O   . LEU A 203 ? 0.2533 0.3493 0.3819 -0.0314 -0.0143 -0.0023 206 LEU A O   
3253 C CB  . LEU A 203 ? 0.2475 0.3786 0.3805 -0.0307 0.0028  0.0010  206 LEU A CB  
3254 C CG  . LEU A 203 ? 0.2936 0.4437 0.4431 -0.0341 0.0004  0.0006  206 LEU A CG  
3255 C CD1 . LEU A 203 ? 0.3275 0.4793 0.4808 -0.0219 -0.0047 -0.0050 206 LEU A CD1 
3256 C CD2 . LEU A 203 ? 0.3090 0.4897 0.4693 -0.0371 0.0081  0.0038  206 LEU A CD2 
3268 N N   . LEU A 204 ? 0.2523 0.3382 0.3699 -0.0423 -0.0073 0.0055  207 LEU A N   
3269 C CA  . LEU A 204 ? 0.2557 0.3279 0.3711 -0.0481 -0.0123 0.0056  207 LEU A CA  
3270 C C   . LEU A 204 ? 0.2609 0.3190 0.3686 -0.0401 -0.0174 0.0034  207 LEU A C   
3271 O O   . LEU A 204 ? 0.2871 0.3420 0.3965 -0.0404 -0.0227 0.0006  207 LEU A O   
3272 C CB  . LEU A 204 ? 0.2503 0.3060 0.3551 -0.0570 -0.0095 0.0112  207 LEU A CB  
3273 C CG  . LEU A 204 ? 0.2897 0.3594 0.4018 -0.0692 -0.0043 0.0154  207 LEU A CG  
3274 C CD1 . LEU A 204 ? 0.3354 0.3800 0.4316 -0.0774 -0.0017 0.0220  207 LEU A CD1 
3275 C CD2 . LEU A 204 ? 0.3837 0.4696 0.5105 -0.0786 -0.0085 0.0125  207 LEU A CD2 
3287 N N   . PHE A 205 ? 0.2666 0.3187 0.3653 -0.0337 -0.0159 0.0051  208 PHE A N   
3288 C CA  . PHE A 205 ? 0.2499 0.2946 0.3432 -0.0275 -0.0201 0.0043  208 PHE A CA  
3289 C C   . PHE A 205 ? 0.2218 0.2745 0.3226 -0.0242 -0.0236 0.0003  208 PHE A C   
3290 O O   . PHE A 205 ? 0.2691 0.3173 0.3680 -0.0215 -0.0276 -0.0002 208 PHE A O   
3291 C CB  . PHE A 205 ? 0.2266 0.2700 0.3107 -0.0225 -0.0184 0.0077  208 PHE A CB  
3292 C CG  . PHE A 205 ? 0.2339 0.2650 0.3058 -0.0205 -0.0163 0.0131  208 PHE A CG  
3293 C CD1 . PHE A 205 ? 0.3073 0.3230 0.3718 -0.0186 -0.0179 0.0137  208 PHE A CD1 
3294 C CD2 . PHE A 205 ? 0.2867 0.3205 0.3519 -0.0186 -0.0128 0.0174  208 PHE A CD2 
3295 C CE1 . PHE A 205 ? 0.3112 0.3113 0.3607 -0.0135 -0.0156 0.0189  208 PHE A CE1 
3296 C CE2 . PHE A 205 ? 0.3191 0.3409 0.3709 -0.0137 -0.0108 0.0237  208 PHE A CE2 
3297 C CZ  . PHE A 205 ? 0.3308 0.3345 0.3746 -0.0107 -0.0119 0.0244  208 PHE A CZ  
3307 N N   . MET A 206 ? 0.2578 0.3211 0.3655 -0.0231 -0.0219 -0.0023 209 MET A N   
3308 C CA  . MET A 206 ? 0.2470 0.3122 0.3582 -0.0180 -0.0253 -0.0054 209 MET A CA  
3309 C C   . MET A 206 ? 0.2313 0.3015 0.3503 -0.0184 -0.0292 -0.0065 209 MET A C   
3310 O O   . MET A 206 ? 0.2608 0.3266 0.3782 -0.0150 -0.0336 -0.0069 209 MET A O   
3311 C CB  . MET A 206 ? 0.2910 0.3620 0.4032 -0.0136 -0.0222 -0.0085 209 MET A CB  
3312 C CG  . MET A 206 ? 0.3208 0.3873 0.4331 -0.0065 -0.0259 -0.0113 209 MET A CG  
3313 S SD  . MET A 206 ? 0.4773 0.5595 0.6017 0.0002  -0.0265 -0.0131 209 MET A SD  
3314 C CE  . MET A 206 ? 0.2539 0.3406 0.3744 0.0049  -0.0195 -0.0161 209 MET A CE  
3324 N N   . VAL A 207 ? 0.2095 0.2902 0.3364 -0.0241 -0.0281 -0.0065 210 VAL A N   
3325 C CA  . VAL A 207 ? 0.2299 0.3181 0.3638 -0.0267 -0.0332 -0.0079 210 VAL A CA  
3326 C C   . VAL A 207 ? 0.2488 0.3205 0.3726 -0.0287 -0.0375 -0.0078 210 VAL A C   
3327 O O   . VAL A 207 ? 0.2534 0.3259 0.3770 -0.0256 -0.0429 -0.0093 210 VAL A O   
3328 C CB  . VAL A 207 ? 0.2671 0.3711 0.4110 -0.0365 -0.0314 -0.0072 210 VAL A CB  
3329 C CG1 . VAL A 207 ? 0.3679 0.4804 0.5177 -0.0416 -0.0385 -0.0092 210 VAL A CG1 
3330 C CG2 . VAL A 207 ? 0.3013 0.4279 0.4562 -0.0313 -0.0265 -0.0072 210 VAL A CG2 
3340 N N   . LEU A 208 ? 0.2384 0.2951 0.3517 -0.0315 -0.0350 -0.0059 211 LEU A N   
3341 C CA  . LEU A 208 ? 0.2366 0.2774 0.3378 -0.0302 -0.0381 -0.0062 211 LEU A CA  
3342 C C   . LEU A 208 ? 0.2750 0.3156 0.3727 -0.0215 -0.0398 -0.0053 211 LEU A C   
3343 O O   . LEU A 208 ? 0.2678 0.3051 0.3606 -0.0188 -0.0438 -0.0065 211 LEU A O   
3344 C CB  . LEU A 208 ? 0.2450 0.2685 0.3334 -0.0313 -0.0343 -0.0034 211 LEU A CB  
3345 C CG  . LEU A 208 ? 0.2680 0.2837 0.3548 -0.0426 -0.0332 -0.0032 211 LEU A CG  
3346 C CD1 . LEU A 208 ? 0.3180 0.3129 0.3890 -0.0406 -0.0286 0.0013  211 LEU A CD1 
3347 C CD2 . LEU A 208 ? 0.3686 0.3754 0.4511 -0.0501 -0.0393 -0.0077 211 LEU A CD2 
3359 N N   . ASP A 209 ? 0.2307 0.2741 0.3288 -0.0182 -0.0367 -0.0029 212 ASP A N   
3360 C CA  . ASP A 209 ? 0.2086 0.2517 0.3025 -0.0134 -0.0381 -0.0007 212 ASP A CA  
3361 C C   . ASP A 209 ? 0.2628 0.3094 0.3609 -0.0111 -0.0422 -0.0018 212 ASP A C   
3362 O O   . ASP A 209 ? 0.2375 0.2822 0.3304 -0.0083 -0.0446 0.0001  212 ASP A O   
3363 C CB  . ASP A 209 ? 0.2551 0.3009 0.3488 -0.0138 -0.0354 0.0012  212 ASP A CB  
3364 C CG  . ASP A 209 ? 0.2839 0.3297 0.3714 -0.0135 -0.0323 0.0045  212 ASP A CG  
3365 O OD1 . ASP A 209 ? 0.2696 0.3105 0.3505 -0.0103 -0.0319 0.0062  212 ASP A OD1 
3366 O OD2 . ASP A 209 ? 0.2600 0.3099 0.3471 -0.0152 -0.0307 0.0052  212 ASP A OD2 
3371 N N   . VAL A 210 ? 0.2517 0.3043 0.3581 -0.0108 -0.0424 -0.0041 213 VAL A N   
3372 C CA  . VAL A 210 ? 0.2453 0.3003 0.3538 -0.0057 -0.0465 -0.0042 213 VAL A CA  
3373 C C   . VAL A 210 ? 0.2768 0.3358 0.3852 -0.0058 -0.0513 -0.0052 213 VAL A C   
3374 O O   . VAL A 210 ? 0.2664 0.3237 0.3701 -0.0014 -0.0550 -0.0032 213 VAL A O   
3375 C CB  . VAL A 210 ? 0.2681 0.3312 0.3850 -0.0018 -0.0452 -0.0065 213 VAL A CB  
3376 C CG1 . VAL A 210 ? 0.3648 0.4311 0.4832 0.0063  -0.0497 -0.0059 213 VAL A CG1 
3377 C CG2 . VAL A 210 ? 0.3162 0.3701 0.4277 -0.0008 -0.0413 -0.0068 213 VAL A CG2 
3387 N N   . SER A 211 ? 0.2477 0.3108 0.3593 -0.0117 -0.0517 -0.0080 214 SER A N   
3388 C CA  . SER A 211 ? 0.2420 0.3069 0.3507 -0.0137 -0.0575 -0.0105 214 SER A CA  
3389 C C   . SER A 211 ? 0.2864 0.3377 0.3800 -0.0108 -0.0582 -0.0096 214 SER A C   
3390 O O   . SER A 211 ? 0.2790 0.3312 0.3668 -0.0077 -0.0629 -0.0102 214 SER A O   
3391 C CB  . SER A 211 ? 0.2752 0.3429 0.3877 -0.0242 -0.0581 -0.0138 214 SER A CB  
3392 O OG  . SER A 211 ? 0.3195 0.4067 0.4476 -0.0263 -0.0568 -0.0137 214 SER A OG  
3398 N N   . ALA A 212 ? 0.2504 0.2916 0.3371 -0.0106 -0.0532 -0.0078 215 ALA A N   
3399 C CA  . ALA A 212 ? 0.2482 0.2799 0.3202 -0.0057 -0.0528 -0.0069 215 ALA A CA  
3400 C C   . ALA A 212 ? 0.2790 0.3163 0.3486 0.0001  -0.0521 -0.0017 215 ALA A C   
3401 O O   . ALA A 212 ? 0.3129 0.3484 0.3713 0.0055  -0.0518 -0.0001 215 ALA A O   
3402 C CB  . ALA A 212 ? 0.2794 0.3006 0.3438 -0.0048 -0.0473 -0.0055 215 ALA A CB  
3408 N N   . LYS A 213 ? 0.2528 0.2957 0.3312 -0.0010 -0.0516 0.0013  216 LYS A N   
3409 C CA  . LYS A 213 ? 0.2316 0.2765 0.3069 0.0011  -0.0511 0.0074  216 LYS A CA  
3410 C C   . LYS A 213 ? 0.2805 0.3255 0.3573 0.0036  -0.0555 0.0083  216 LYS A C   
3411 O O   . LYS A 213 ? 0.2963 0.3422 0.3652 0.0071  -0.0576 0.0117  216 LYS A O   
3412 C CB  . LYS A 213 ? 0.2331 0.2780 0.3120 -0.0030 -0.0475 0.0103  216 LYS A CB  
3413 C CG  . LYS A 213 ? 0.2507 0.2993 0.3269 -0.0032 -0.0436 0.0114  216 LYS A CG  
3414 C CD  . LYS A 213 ? 0.2485 0.3011 0.3274 -0.0083 -0.0414 0.0144  216 LYS A CD  
3415 C CE  . LYS A 213 ? 0.2734 0.3359 0.3491 -0.0062 -0.0382 0.0179  216 LYS A CE  
3416 N NZ  . LYS A 213 ? 0.2557 0.3135 0.3306 -0.0035 -0.0362 0.0146  216 LYS A NZ  
3427 N N   . VAL A 214 ? 0.2656 0.3102 0.3503 0.0038  -0.0565 0.0065  217 VAL A N   
3428 C CA  . VAL A 214 ? 0.2531 0.2975 0.3375 0.0096  -0.0606 0.0084  217 VAL A CA  
3429 C C   . VAL A 214 ? 0.2764 0.3316 0.3630 0.0124  -0.0659 0.0050  217 VAL A C   
3430 O O   . VAL A 214 ? 0.3272 0.3839 0.4080 0.0178  -0.0702 0.0080  217 VAL A O   
3431 C CB  . VAL A 214 ? 0.2768 0.3174 0.3671 0.0121  -0.0592 0.0070  217 VAL A CB  
3432 C CG1 . VAL A 214 ? 0.3125 0.3513 0.4008 0.0218  -0.0633 0.0095  217 VAL A CG1 
3433 C CG2 . VAL A 214 ? 0.3308 0.3584 0.4158 0.0073  -0.0553 0.0092  217 VAL A CG2 
3443 N N   . GLY A 215 ? 0.2909 0.3541 0.3850 0.0077  -0.0665 -0.0010 218 GLY A N   
3444 C CA  . GLY A 215 ? 0.3194 0.3931 0.4141 0.0069  -0.0730 -0.0048 218 GLY A CA  
3445 C C   . GLY A 215 ? 0.3169 0.3839 0.3964 0.0080  -0.0755 -0.0049 218 GLY A C   
3446 O O   . GLY A 215 ? 0.3083 0.3815 0.3826 0.0120  -0.0815 -0.0047 218 GLY A O   
3450 N N   . PHE A 216 ? 0.3103 0.3659 0.3811 0.0058  -0.0708 -0.0053 219 PHE A N   
3451 C CA  . PHE A 216 ? 0.3344 0.3842 0.3890 0.0098  -0.0712 -0.0051 219 PHE A CA  
3452 C C   . PHE A 216 ? 0.2894 0.3432 0.3384 0.0163  -0.0720 0.0021  219 PHE A C   
3453 O O   . PHE A 216 ? 0.3215 0.3775 0.3595 0.0204  -0.0761 0.0015  219 PHE A O   
3454 C CB  . PHE A 216 ? 0.3156 0.3566 0.3640 0.0102  -0.0642 -0.0039 219 PHE A CB  
3455 C CG  . PHE A 216 ? 0.3316 0.3687 0.3627 0.0172  -0.0626 -0.0034 219 PHE A CG  
3456 C CD1 . PHE A 216 ? 0.3220 0.3671 0.3489 0.0223  -0.0594 0.0046  219 PHE A CD1 
3457 C CD2 . PHE A 216 ? 0.3658 0.3898 0.3832 0.0188  -0.0628 -0.0101 219 PHE A CD2 
3458 C CE1 . PHE A 216 ? 0.3766 0.4229 0.3873 0.0307  -0.0562 0.0059  219 PHE A CE1 
3459 C CE2 . PHE A 216 ? 0.3764 0.3962 0.3754 0.0287  -0.0599 -0.0100 219 PHE A CE2 
3460 C CZ  . PHE A 216 ? 0.3900 0.4239 0.3864 0.0354  -0.0563 -0.0019 219 PHE A CZ  
3470 N N   . GLY A 217 ? 0.2718 0.3246 0.3261 0.0165  -0.0682 0.0091  220 GLY A N   
3471 C CA  . GLY A 217 ? 0.3409 0.3933 0.3872 0.0207  -0.0684 0.0176  220 GLY A CA  
3472 C C   . GLY A 217 ? 0.3769 0.4327 0.4224 0.0263  -0.0750 0.0187  220 GLY A C   
3473 O O   . GLY A 217 ? 0.3479 0.4043 0.3820 0.0311  -0.0767 0.0245  220 GLY A O   
3477 N N   . LEU A 218 ? 0.2995 0.3601 0.3569 0.0269  -0.0784 0.0144  221 LEU A N   
3478 C CA  . LEU A 218 ? 0.3524 0.4215 0.4102 0.0344  -0.0852 0.0158  221 LEU A CA  
3479 C C   . LEU A 218 ? 0.3830 0.4624 0.4324 0.0353  -0.0918 0.0119  221 LEU A C   
3480 O O   . LEU A 218 ? 0.4133 0.4973 0.4540 0.0427  -0.0966 0.0164  221 LEU A O   
3481 C CB  . LEU A 218 ? 0.3026 0.3819 0.3766 0.0354  -0.0869 0.0116  221 LEU A CB  
3482 C CG  . LEU A 218 ? 0.4978 0.5653 0.5756 0.0392  -0.0821 0.0154  221 LEU A CG  
3483 C CD1 . LEU A 218 ? 0.4353 0.5168 0.5289 0.0404  -0.0820 0.0101  221 LEU A CD1 
3484 C CD2 . LEU A 218 ? 0.4300 0.4866 0.4970 0.0499  -0.0842 0.0239  221 LEU A CD2 
3496 N N   . ILE A 219 ? 0.3234 0.4039 0.3724 0.0281  -0.0922 0.0034  222 ILE A N   
3497 C CA  . ILE A 219 ? 0.3490 0.4337 0.3855 0.0275  -0.0988 -0.0024 222 ILE A CA  
3498 C C   . ILE A 219 ? 0.4021 0.4801 0.4190 0.0341  -0.0964 0.0027  222 ILE A C   
3499 O O   . ILE A 219 ? 0.3871 0.4716 0.3923 0.0396  -0.1023 0.0038  222 ILE A O   
3500 C CB  . ILE A 219 ? 0.3509 0.4292 0.3871 0.0176  -0.0989 -0.0125 222 ILE A CB  
3501 C CG1 . ILE A 219 ? 0.3509 0.4412 0.4062 0.0095  -0.1019 -0.0165 222 ILE A CG1 
3502 C CG2 . ILE A 219 ? 0.4312 0.5058 0.4481 0.0168  -0.1054 -0.0199 222 ILE A CG2 
3503 C CD1 . ILE A 219 ? 0.4367 0.5161 0.4930 -0.0023 -0.0997 -0.0236 222 ILE A CD1 
3515 N N   . LEU A 220 ? 0.3228 0.3911 0.3362 0.0337  -0.0877 0.0066  223 LEU A N   
3516 C CA  . LEU A 220 ? 0.3159 0.3828 0.3118 0.0395  -0.0838 0.0119  223 LEU A CA  
3517 C C   . LEU A 220 ? 0.4003 0.4710 0.3919 0.0446  -0.0844 0.0235  223 LEU A C   
3518 O O   . LEU A 220 ? 0.4153 0.4904 0.3906 0.0507  -0.0864 0.0265  223 LEU A O   
3519 C CB  . LEU A 220 ? 0.3084 0.3709 0.3057 0.0376  -0.0740 0.0152  223 LEU A CB  
3520 C CG  . LEU A 220 ? 0.3563 0.4243 0.3381 0.0437  -0.0682 0.0226  223 LEU A CG  
3521 C CD1 . LEU A 220 ? 0.3981 0.4648 0.3605 0.0510  -0.0703 0.0148  223 LEU A CD1 
3522 C CD2 . LEU A 220 ? 0.3373 0.4083 0.3251 0.0413  -0.0593 0.0270  223 LEU A CD2 
3534 N N   . LEU A 221 ? 0.3678 0.4341 0.3708 0.0426  -0.0825 0.0303  224 LEU A N   
3535 C CA  . LEU A 221 ? 0.4011 0.4635 0.3960 0.0466  -0.0819 0.0430  224 LEU A CA  
3536 C C   . LEU A 221 ? 0.4893 0.5560 0.4800 0.0551  -0.0904 0.0446  224 LEU A C   
3537 O O   . LEU A 221 ? 0.4648 0.5258 0.4453 0.0600  -0.0905 0.0558  224 LEU A O   
3538 C CB  . LEU A 221 ? 0.3912 0.4405 0.3943 0.0408  -0.0768 0.0496  224 LEU A CB  
3539 C CG  . LEU A 221 ? 0.4094 0.4589 0.4169 0.0320  -0.0689 0.0498  224 LEU A CG  
3540 C CD1 . LEU A 221 ? 0.4136 0.4495 0.4282 0.0245  -0.0659 0.0542  224 LEU A CD1 
3541 C CD2 . LEU A 221 ? 0.4098 0.4679 0.4044 0.0318  -0.0639 0.0579  224 LEU A CD2 
3553 N N   A ARG A 222 ? 0.4190 0.5177 0.4562 0.0270  -0.0945 0.1109  225 ARG A N   
3554 N N   B ARG A 222 ? 0.4188 0.5172 0.4551 0.0266  -0.0946 0.1106  225 ARG A N   
3555 C CA  A ARG A 222 ? 0.5055 0.6061 0.5470 0.0500  -0.1220 0.1243  225 ARG A CA  
3556 C CA  B ARG A 222 ? 0.5046 0.6075 0.5488 0.0490  -0.1220 0.1237  225 ARG A CA  
3557 C C   A ARG A 222 ? 0.5069 0.6004 0.5101 0.0510  -0.1549 0.1227  225 ARG A C   
3558 C C   B ARG A 222 ? 0.4960 0.5967 0.5079 0.0493  -0.1566 0.1215  225 ARG A C   
3559 O O   A ARG A 222 ? 0.5264 0.6234 0.5154 0.0758  -0.1808 0.1322  225 ARG A O   
3560 O O   B ARG A 222 ? 0.5439 0.6597 0.5551 0.0714  -0.1860 0.1284  225 ARG A O   
3561 C CB  A ARG A 222 ? 0.4629 0.6175 0.5790 0.0541  -0.1352 0.1249  225 ARG A CB  
3562 C CB  B ARG A 222 ? 0.4549 0.6096 0.5742 0.0520  -0.1302 0.1242  225 ARG A CB  
3563 C CG  A ARG A 222 ? 0.4701 0.6614 0.6288 0.0308  -0.1419 0.1115  225 ARG A CG  
3564 C CG  B ARG A 222 ? 0.6109 0.7626 0.7564 0.0576  -0.0959 0.1284  225 ARG A CG  
3565 C CD  A ARG A 222 ? 0.4970 0.6974 0.6451 0.0220  -0.1729 0.1011  225 ARG A CD  
3566 C CD  B ARG A 222 ? 0.6079 0.8084 0.8293 0.0581  -0.0982 0.1278  225 ARG A CD  
3567 N NE  A ARG A 222 ? 0.4048 0.6319 0.6009 -0.0007 -0.1677 0.0874  225 ARG A NE  
3568 N NE  B ARG A 222 ? 0.7545 0.9806 1.0060 0.0831  -0.1263 0.1370  225 ARG A NE  
3569 C CZ  A ARG A 222 ? 0.4181 0.6427 0.6057 -0.0185 -0.1770 0.0736  225 ARG A CZ  
3570 C CZ  B ARG A 222 ? 0.8361 1.0489 1.0868 0.1128  -0.1182 0.1530  225 ARG A CZ  
3571 N NH1 A ARG A 222 ? 0.5754 0.7746 0.7047 -0.0177 -0.1947 0.0712  225 ARG A NH1 
3572 N NH1 B ARG A 222 ? 0.8433 1.0102 1.0688 0.1153  -0.0774 0.1588  225 ARG A NH1 
3573 N NH2 A ARG A 222 ? 0.5801 0.8227 0.8183 -0.0380 -0.1629 0.0610  225 ARG A NH2 
3574 N NH2 B ARG A 222 ? 0.7820 1.0312 1.0593 0.1419  -0.1494 0.1611  225 ARG A NH2 
3601 N N   . SER A 223 ? 0.4673 0.5517 0.4487 0.0284  -0.1531 0.1109  226 SER A N   
3602 C CA  . SER A 223 ? 0.5652 0.6470 0.5183 0.0232  -0.1818 0.1040  226 SER A CA  
3603 C C   . SER A 223 ? 0.5459 0.5730 0.4197 0.0365  -0.1809 0.1118  226 SER A C   
3604 O O   . SER A 223 ? 0.6551 0.6395 0.4960 0.0371  -0.1484 0.1157  226 SER A O   
3605 C CB  . SER A 223 ? 0.5726 0.6592 0.5351 -0.0042 -0.1717 0.0907  226 SER A CB  
3606 O OG  . SER A 223 ? 0.7837 0.8479 0.7016 -0.0127 -0.1866 0.0827  226 SER A OG  
3612 N N   . ARG A 224 ? 0.5892 0.6184 0.4313 0.0471  -0.2140 0.1106  227 ARG A N   
3613 C CA  . ARG A 224 ? 0.6497 0.6195 0.4066 0.0598  -0.2097 0.1187  227 ARG A CA  
3614 C C   . ARG A 224 ? 0.6634 0.6015 0.3891 0.0311  -0.1938 0.1052  227 ARG A C   
3615 O O   . ARG A 224 ? 0.7302 0.6123 0.3870 0.0362  -0.1810 0.1094  227 ARG A O   
3616 C CB  . ARG A 224 ? 0.7482 0.7354 0.4712 0.0857  -0.2517 0.1212  227 ARG A CB  
3617 C CG  . ARG A 224 ? 0.9647 0.9362 0.6561 0.1350  -0.2524 0.1486  227 ARG A CG  
3618 C CD  . ARG A 224 ? 1.1939 1.0701 0.8009 0.1500  -0.2099 0.1684  227 ARG A CD  
3619 N NE  . ARG A 224 ? 1.4386 1.2822 1.0422 0.1819  -0.1782 0.1931  227 ARG A NE  
3620 C CZ  . ARG A 224 ? 1.5672 1.3240 1.1020 0.2026  -0.1338 0.2126  227 ARG A CZ  
3621 N NH1 . ARG A 224 ? 1.4787 1.1787 0.9501 0.1919  -0.1149 0.2078  227 ARG A NH1 
3622 N NH2 . ARG A 224 ? 1.7697 1.4963 1.3096 0.2307  -0.0998 0.2337  227 ARG A NH2 
3636 N N   . ALA A 225 ? 0.6773 0.6464 0.4506 0.0045  -0.1898 0.0910  228 ALA A N   
3637 C CA  . ALA A 225 ? 0.7594 0.7052 0.5078 -0.0174 -0.1758 0.0798  228 ALA A CA  
3638 C C   . ALA A 225 ? 0.8110 0.7201 0.5293 -0.0200 -0.1390 0.0804  228 ALA A C   
3639 O O   . ALA A 225 ? 0.7323 0.6119 0.4128 -0.0310 -0.1276 0.0726  228 ALA A O   
3640 C CB  . ALA A 225 ? 0.6801 0.6632 0.4852 -0.0364 -0.1711 0.0704  228 ALA A CB  
3646 N N   . ILE A 226 ? 0.5783 0.4927 0.3180 -0.0126 -0.1176 0.0845  229 ILE A N   
3647 C CA  . ILE A 226 ? 0.5491 0.4424 0.2732 -0.0212 -0.0792 0.0734  229 ILE A CA  
3648 C C   . ILE A 226 ? 0.6277 0.4541 0.2897 -0.0143 -0.0590 0.0760  229 ILE A C   
3649 O O   . ILE A 226 ? 0.6974 0.5039 0.3487 -0.0263 -0.0225 0.0597  229 ILE A O   
3650 C CB  . ILE A 226 ? 0.5336 0.4614 0.3072 -0.0204 -0.0590 0.0692  229 ILE A CB  
3651 C CG1 . ILE A 226 ? 0.6263 0.5355 0.4030 -0.0004 -0.0589 0.0855  229 ILE A CG1 
3652 C CG2 . ILE A 226 ? 0.5373 0.5248 0.3652 -0.0245 -0.0717 0.0686  229 ILE A CG2 
3653 C CD1 . ILE A 226 ? 0.6423 0.5719 0.4609 -0.0028 -0.0274 0.0769  229 ILE A CD1 
3665 N N   . PHE A 227 ? 0.6880 0.5195 0.3449 0.0457  -0.0722 -0.0058 230 PHE A N   
3666 C CA  . PHE A 227 ? 0.7550 0.5008 0.3614 0.0247  -0.0922 0.0083  230 PHE A CA  
3667 C C   . PHE A 227 ? 0.8047 0.5227 0.3807 -0.0225 -0.0526 0.0243  230 PHE A C   
3668 O O   . PHE A 227 ? 0.7827 0.5358 0.3588 -0.0354 -0.0302 0.0190  230 PHE A O   
3669 C CB  . PHE A 227 ? 0.8057 0.5353 0.3777 0.0450  -0.1445 0.0012  230 PHE A CB  
3670 C CG  . PHE A 227 ? 0.8281 0.5717 0.4174 0.0973  -0.1925 -0.0162 230 PHE A CG  
3671 C CD1 . PHE A 227 ? 0.8659 0.5408 0.4421 0.1081  -0.2318 -0.0118 230 PHE A CD1 
3672 C CD2 . PHE A 227 ? 0.9108 0.7402 0.5318 0.1377  -0.1999 -0.0355 230 PHE A CD2 
3673 C CE1 . PHE A 227 ? 0.9904 0.6722 0.5786 0.1617  -0.2816 -0.0321 230 PHE A CE1 
3674 C CE2 . PHE A 227 ? 0.9111 0.7591 0.5438 0.1939  -0.2449 -0.0544 230 PHE A CE2 
3675 C CZ  . PHE A 227 ? 0.9261 0.6961 0.5401 0.2079  -0.2873 -0.0558 230 PHE A CZ  
3685 N N   . GLY A 228 ? 0.8868 0.5434 0.4365 -0.0466 -0.0473 0.0451  231 GLY A N   
3686 C CA  . GLY A 228 ? 0.9845 0.6156 0.4947 -0.0841 -0.0160 0.0604  231 GLY A CA  
3687 C C   . GLY A 228 ? 1.1577 0.7778 0.6229 -0.0887 -0.0387 0.0567  231 GLY A C   
3688 O O   . GLY A 228 ? 0.9465 0.5634 0.4044 -0.0668 -0.0831 0.0488  231 GLY A O   
3692 N N   . GLU A 229 ? 1.0970 0.7123 0.5303 -0.1145 -0.0094 0.0603  232 GLU A N   
3693 C CA  . GLU A 229 ? 1.2372 0.8381 0.6238 -0.1208 -0.0300 0.0575  232 GLU A CA  
3694 C C   . GLU A 229 ? 1.2618 0.8065 0.6028 -0.1322 -0.0515 0.0816  232 GLU A C   
3695 O O   . GLU A 229 ? 1.2534 0.7750 0.5748 -0.1534 -0.0258 0.1037  232 GLU A O   
3696 C CB  . GLU A 229 ? 1.2975 0.9099 0.6645 -0.1410 0.0040  0.0503  232 GLU A CB  
3697 C CG  . GLU A 229 ? 1.2898 0.9012 0.6209 -0.1433 -0.0190 0.0401  232 GLU A CG  
3698 C CD  . GLU A 229 ? 1.3230 0.9448 0.6424 -0.1599 0.0076  0.0287  232 GLU A CD  
3699 O OE1 . GLU A 229 ? 1.1713 0.7861 0.4902 -0.1717 0.0452  0.0317  232 GLU A OE1 
3700 O OE2 . GLU A 229 ? 1.1452 0.7784 0.4531 -0.1608 -0.0120 0.0172  232 GLU A OE2 
3707 N N   . ALA A 230 ? 1.0935 0.6201 0.4193 -0.1174 -0.0998 0.0803  233 ALA A N   
3708 C CA  . ALA A 230 ? 1.2329 0.7060 0.5231 -0.1278 -0.1281 0.1068  233 ALA A CA  
3709 C C   . ALA A 230 ? 1.2533 0.7118 0.5059 -0.1207 -0.1684 0.1009  233 ALA A C   
3710 O O   . ALA A 230 ? 1.2909 0.7807 0.5547 -0.0994 -0.1854 0.0759  233 ALA A O   
3711 C CB  . ALA A 230 ? 1.4115 0.8597 0.7332 -0.1142 -0.1584 0.1177  233 ALA A CB  
3717 N N   . GLU A 231 ? 1.2275 0.6433 0.4364 -0.1390 -0.1833 0.1275  234 GLU A N   
3718 C CA  . GLU A 231 ? 1.3992 0.7963 0.5677 -0.1352 -0.2209 0.1257  234 GLU A CA  
3719 C C   . GLU A 231 ? 1.5118 0.8789 0.6917 -0.1118 -0.2812 0.1261  234 GLU A C   
3720 O O   . GLU A 231 ? 1.5807 0.9102 0.7669 -0.1213 -0.3019 0.1518  234 GLU A O   
3721 C CB  . GLU A 231 ? 1.3129 0.6913 0.4428 -0.1619 -0.2075 0.1520  234 GLU A CB  
3722 C CG  . GLU A 231 ? 1.3582 0.7351 0.4599 -0.1582 -0.2302 0.1423  234 GLU A CG  
3723 C CD  . GLU A 231 ? 1.3217 0.7342 0.4179 -0.1511 -0.2131 0.1105  234 GLU A CD  
3724 O OE1 . GLU A 231 ? 1.2963 0.7280 0.3921 -0.1616 -0.1715 0.1047  234 GLU A OE1 
3725 O OE2 . GLU A 231 ? 1.3241 0.7491 0.4247 -0.1351 -0.2404 0.0923  234 GLU A OE2 
4223 C C1  . RET S .   ? 0.3142 0.2726 0.2914 0.0583  -0.0111 0.0366  318 RET A C1  
4224 C C2  . RET S .   ? 0.4373 0.3821 0.3999 0.0663  -0.0077 0.0445  318 RET A C2  
4225 C C3  . RET S .   ? 0.5392 0.4378 0.4754 0.0725  -0.0054 0.0457  318 RET A C3  
4226 C C4  . RET S .   ? 0.4004 0.2742 0.3200 0.0826  -0.0062 0.0401  318 RET A C4  
4227 C C5  . RET S .   ? 0.3767 0.2673 0.3116 0.0741  -0.0098 0.0318  318 RET A C5  
4228 C C6  . RET S .   ? 0.3382 0.2654 0.2991 0.0627  -0.0119 0.0306  318 RET A C6  
4229 C C7  . RET S .   ? 0.3215 0.2590 0.2934 0.0554  -0.0156 0.0233  318 RET A C7  
4230 C C8  . RET S .   ? 0.3079 0.2727 0.3007 0.0453  -0.0181 0.0212  318 RET A C8  
4231 C C9  . RET S .   ? 0.3041 0.2759 0.3044 0.0400  -0.0217 0.0155  318 RET A C9  
4232 C C10 . RET S .   ? 0.2854 0.2817 0.3050 0.0305  -0.0237 0.0154  318 RET A C10 
4233 C C11 . RET S .   ? 0.2651 0.2686 0.2930 0.0245  -0.0273 0.0114  318 RET A C11 
4234 C C12 . RET S .   ? 0.2989 0.3208 0.3426 0.0163  -0.0289 0.0120  318 RET A C12 
4235 C C13 . RET S .   ? 0.2905 0.3200 0.3416 0.0119  -0.0323 0.0100  318 RET A C13 
4236 C C14 . RET S .   ? 0.3102 0.3533 0.3731 0.0055  -0.0331 0.0118  318 RET A C14 
4237 C C15 . RET S .   ? 0.2773 0.3281 0.3451 0.0028  -0.0354 0.0129  318 RET A C15 
4238 C C16 . RET S .   ? 0.3271 0.2915 0.3211 0.0379  -0.0128 0.0328  318 RET A C16 
4239 C C17 . RET S .   ? 0.3564 0.3548 0.3460 0.0659  -0.0118 0.0397  318 RET A C17 
4240 C C18 . RET S .   ? 0.4068 0.2648 0.3203 0.0814  -0.0110 0.0249  318 RET A C18 
4241 C C19 . RET S .   ? 0.3309 0.2765 0.3137 0.0442  -0.0235 0.0092  318 RET A C19 
4242 C C20 . RET S .   ? 0.3200 0.3398 0.3623 0.0154  -0.0350 0.0059  318 RET A C20 
# 
